data_6YZ7
# 
_entry.id   6YZ7 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.325 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   6YZ7         
WWPDB D_1292108594 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        6YZ7 
_pdbx_database_status.recvd_initial_deposition_date   2020-05-06 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Naismith, J.H.' 1 0000-0001-6744-5061 
'Ren, J.'        2 0000-0003-4015-1404 
'Zhou, D.'       3 0000-0002-7188-5243 
'Zhao, Y.'       4 0000-0001-8916-8552 
'Stuart, D.I.'   5 0000-0002-3426-4210 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Structural characterisation of a nanobody derived from a naive library that neutralises SARS-CoV-2' 
_citation.year                      2020 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.unpublished_flag          ? 
# 
_citation_author.citation_id        primary 
_citation_author.name               'Naismith, J.H.' 
_citation_author.ordinal            1 
_citation_author.identifier_ORCID   0000-0001-6744-5061 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     6YZ7 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     154.598 
_cell.length_a_esd                 ? 
_cell.length_b                     154.598 
_cell.length_b_esd                 ? 
_cell.length_c                     229.312 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_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             ? 
# 
_symmetry.entry_id                         6YZ7 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                91 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 41 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Spike glycoprotein'   23716.580 2 ? ? ? ?         
2 polymer     man 'Antibody Cr3022'      24455.520 2 ? ? ? ?         
3 polymer     man 'Antibody light chain' 24289.885 2 ? ? ? ?         
4 polymer     man Nanobody               15010.732 2 ? ? ? 'His tag' 
5 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208   2 ? ? ? ?         
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'S glycoprotein,E2,Peplomer protein' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;PNITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSFVIRGDEVRQ
IAPGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCY
FPLQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTNKHHHHHH
;
;PNITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSFVIRGDEVRQ
IAPGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCY
FPLQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTNKHHHHHH
;
AAA,EEE ? 
2 'polypeptide(L)' no no 
;TQMQLVQSGTEVKKPGESLKISCKGSGYGFITYWIGWVRQMPGKGLEWMGIIYPGDSETRYSPSFQGQVTISADKSINTA
YLQWSSLKASDTAIYYCAGGSGISTPMDVWGQGTTVTVASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWN
SGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKHHHHHH
;
;TQMQLVQSGTEVKKPGESLKISCKGSGYGFITYWIGWVRQMPGKGLEWMGIIYPGDSETRYSPSFQGQVTISADKSINTA
YLQWSSLKASDTAIYYCAGGSGISTPMDVWGQGTTVTVASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWN
SGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKHHHHHH
;
BBB,HHH ? 
3 'polypeptide(L)' no no 
;DIQLTQSPDSLAVSLGERATINCKSSQSVLYSSINKNYLAWYQQKPGQPPKLLIYWASTRESGVPDRFSGSGSGTDFTLT
ISSLQAEDVAVYYCQQYYSTPYTFGQGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNAL
QSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
;
;DIQLTQSPDSLAVSLGERATINCKSSQSVLYSSINKNYLAWYQQKPGQPPKLLIYWASTRESGVPDRFSGSGSGTDFTLT
ISSLQAEDVAVYYCQQYYSTPYTFGQGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNAL
QSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
;
CCC,LLL ? 
4 'polypeptide(L)' no no 
;QVQLVESGGGLMQAGGSLRLSCAVSGRTFSTAAMGWFRQAPGKEREFVAAIRWSGGSAYYADSVKGRFTISRDKAKNTVY
LQMNSLKYEDTAVYYCARTENVRSLLSDYATWPYDYWGQGTQVTVSSKHHHHHH
;
;QVQLVESGGGLMQAGGSLRLSCAVSGRTFSTAAMGWFRQAPGKEREFVAAIRWSGGSAYYADSVKGRFTISRDKAKNTVY
LQMNSLKYEDTAVYYCARTENVRSLLSDYATWPYDYWGQGTQVTVSSKHHHHHH
;
DDD,FFF ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   PRO n 
1 2   ASN n 
1 3   ILE n 
1 4   THR n 
1 5   ASN n 
1 6   LEU n 
1 7   CYS n 
1 8   PRO n 
1 9   PHE n 
1 10  GLY n 
1 11  GLU n 
1 12  VAL n 
1 13  PHE n 
1 14  ASN n 
1 15  ALA n 
1 16  THR n 
1 17  ARG n 
1 18  PHE n 
1 19  ALA n 
1 20  SER n 
1 21  VAL n 
1 22  TYR n 
1 23  ALA n 
1 24  TRP n 
1 25  ASN n 
1 26  ARG n 
1 27  LYS n 
1 28  ARG n 
1 29  ILE n 
1 30  SER n 
1 31  ASN n 
1 32  CYS n 
1 33  VAL n 
1 34  ALA n 
1 35  ASP n 
1 36  TYR n 
1 37  SER n 
1 38  VAL n 
1 39  LEU n 
1 40  TYR n 
1 41  ASN n 
1 42  SER n 
1 43  ALA n 
1 44  SER n 
1 45  PHE n 
1 46  SER n 
1 47  THR n 
1 48  PHE n 
1 49  LYS n 
1 50  CYS n 
1 51  TYR n 
1 52  GLY n 
1 53  VAL n 
1 54  SER n 
1 55  PRO n 
1 56  THR n 
1 57  LYS n 
1 58  LEU n 
1 59  ASN n 
1 60  ASP n 
1 61  LEU n 
1 62  CYS n 
1 63  PHE n 
1 64  THR n 
1 65  ASN n 
1 66  VAL n 
1 67  TYR n 
1 68  ALA n 
1 69  ASP n 
1 70  SER n 
1 71  PHE n 
1 72  VAL n 
1 73  ILE n 
1 74  ARG n 
1 75  GLY n 
1 76  ASP n 
1 77  GLU n 
1 78  VAL n 
1 79  ARG n 
1 80  GLN n 
1 81  ILE n 
1 82  ALA n 
1 83  PRO n 
1 84  GLY n 
1 85  GLN n 
1 86  THR n 
1 87  GLY n 
1 88  LYS n 
1 89  ILE n 
1 90  ALA n 
1 91  ASP n 
1 92  TYR n 
1 93  ASN n 
1 94  TYR n 
1 95  LYS n 
1 96  LEU n 
1 97  PRO n 
1 98  ASP n 
1 99  ASP n 
1 100 PHE n 
1 101 THR n 
1 102 GLY n 
1 103 CYS n 
1 104 VAL n 
1 105 ILE n 
1 106 ALA n 
1 107 TRP n 
1 108 ASN n 
1 109 SER n 
1 110 ASN n 
1 111 ASN n 
1 112 LEU n 
1 113 ASP n 
1 114 SER n 
1 115 LYS n 
1 116 VAL n 
1 117 GLY n 
1 118 GLY n 
1 119 ASN n 
1 120 TYR n 
1 121 ASN n 
1 122 TYR n 
1 123 LEU n 
1 124 TYR n 
1 125 ARG n 
1 126 LEU n 
1 127 PHE n 
1 128 ARG n 
1 129 LYS n 
1 130 SER n 
1 131 ASN n 
1 132 LEU n 
1 133 LYS n 
1 134 PRO n 
1 135 PHE n 
1 136 GLU n 
1 137 ARG n 
1 138 ASP n 
1 139 ILE n 
1 140 SER n 
1 141 THR n 
1 142 GLU n 
1 143 ILE n 
1 144 TYR n 
1 145 GLN n 
1 146 ALA n 
1 147 GLY n 
1 148 SER n 
1 149 THR n 
1 150 PRO n 
1 151 CYS n 
1 152 ASN n 
1 153 GLY n 
1 154 VAL n 
1 155 GLU n 
1 156 GLY n 
1 157 PHE n 
1 158 ASN n 
1 159 CYS n 
1 160 TYR n 
1 161 PHE n 
1 162 PRO n 
1 163 LEU n 
1 164 GLN n 
1 165 SER n 
1 166 TYR n 
1 167 GLY n 
1 168 PHE n 
1 169 GLN n 
1 170 PRO n 
1 171 THR n 
1 172 ASN n 
1 173 GLY n 
1 174 VAL n 
1 175 GLY n 
1 176 TYR n 
1 177 GLN n 
1 178 PRO n 
1 179 TYR n 
1 180 ARG n 
1 181 VAL n 
1 182 VAL n 
1 183 VAL n 
1 184 LEU n 
1 185 SER n 
1 186 PHE n 
1 187 GLU n 
1 188 LEU n 
1 189 LEU n 
1 190 HIS n 
1 191 ALA n 
1 192 PRO n 
1 193 ALA n 
1 194 THR n 
1 195 VAL n 
1 196 CYS n 
1 197 GLY n 
1 198 PRO n 
1 199 LYS n 
1 200 LYS n 
1 201 SER n 
1 202 THR n 
1 203 ASN n 
1 204 LYS n 
1 205 HIS n 
1 206 HIS n 
1 207 HIS n 
1 208 HIS n 
1 209 HIS n 
1 210 HIS n 
2 1   THR n 
2 2   GLN n 
2 3   MET n 
2 4   GLN n 
2 5   LEU n 
2 6   VAL n 
2 7   GLN n 
2 8   SER n 
2 9   GLY n 
2 10  THR n 
2 11  GLU n 
2 12  VAL n 
2 13  LYS n 
2 14  LYS n 
2 15  PRO n 
2 16  GLY n 
2 17  GLU n 
2 18  SER n 
2 19  LEU n 
2 20  LYS n 
2 21  ILE n 
2 22  SER n 
2 23  CYS n 
2 24  LYS n 
2 25  GLY n 
2 26  SER n 
2 27  GLY n 
2 28  TYR n 
2 29  GLY n 
2 30  PHE n 
2 31  ILE n 
2 32  THR n 
2 33  TYR n 
2 34  TRP n 
2 35  ILE n 
2 36  GLY n 
2 37  TRP n 
2 38  VAL n 
2 39  ARG n 
2 40  GLN n 
2 41  MET n 
2 42  PRO n 
2 43  GLY n 
2 44  LYS n 
2 45  GLY n 
2 46  LEU n 
2 47  GLU n 
2 48  TRP n 
2 49  MET n 
2 50  GLY n 
2 51  ILE n 
2 52  ILE n 
2 53  TYR n 
2 54  PRO n 
2 55  GLY n 
2 56  ASP n 
2 57  SER n 
2 58  GLU n 
2 59  THR n 
2 60  ARG n 
2 61  TYR n 
2 62  SER n 
2 63  PRO n 
2 64  SER n 
2 65  PHE n 
2 66  GLN n 
2 67  GLY n 
2 68  GLN n 
2 69  VAL n 
2 70  THR n 
2 71  ILE n 
2 72  SER n 
2 73  ALA n 
2 74  ASP n 
2 75  LYS n 
2 76  SER n 
2 77  ILE n 
2 78  ASN n 
2 79  THR n 
2 80  ALA n 
2 81  TYR n 
2 82  LEU n 
2 83  GLN n 
2 84  TRP n 
2 85  SER n 
2 86  SER n 
2 87  LEU n 
2 88  LYS n 
2 89  ALA n 
2 90  SER n 
2 91  ASP n 
2 92  THR n 
2 93  ALA n 
2 94  ILE n 
2 95  TYR n 
2 96  TYR n 
2 97  CYS n 
2 98  ALA n 
2 99  GLY n 
2 100 GLY n 
2 101 SER n 
2 102 GLY n 
2 103 ILE n 
2 104 SER n 
2 105 THR n 
2 106 PRO n 
2 107 MET n 
2 108 ASP n 
2 109 VAL n 
2 110 TRP n 
2 111 GLY n 
2 112 GLN n 
2 113 GLY n 
2 114 THR n 
2 115 THR n 
2 116 VAL n 
2 117 THR n 
2 118 VAL n 
2 119 ALA n 
2 120 SER n 
2 121 THR n 
2 122 LYS n 
2 123 GLY n 
2 124 PRO n 
2 125 SER n 
2 126 VAL n 
2 127 PHE n 
2 128 PRO n 
2 129 LEU n 
2 130 ALA n 
2 131 PRO n 
2 132 SER n 
2 133 SER n 
2 134 LYS n 
2 135 SER n 
2 136 THR n 
2 137 SER n 
2 138 GLY n 
2 139 GLY n 
2 140 THR n 
2 141 ALA n 
2 142 ALA n 
2 143 LEU n 
2 144 GLY n 
2 145 CYS n 
2 146 LEU n 
2 147 VAL n 
2 148 LYS n 
2 149 ASP n 
2 150 TYR n 
2 151 PHE n 
2 152 PRO n 
2 153 GLU n 
2 154 PRO n 
2 155 VAL n 
2 156 THR n 
2 157 VAL n 
2 158 SER n 
2 159 TRP n 
2 160 ASN n 
2 161 SER n 
2 162 GLY n 
2 163 ALA n 
2 164 LEU n 
2 165 THR n 
2 166 SER n 
2 167 GLY n 
2 168 VAL n 
2 169 HIS n 
2 170 THR n 
2 171 PHE n 
2 172 PRO n 
2 173 ALA n 
2 174 VAL n 
2 175 LEU n 
2 176 GLN n 
2 177 SER n 
2 178 SER n 
2 179 GLY n 
2 180 LEU n 
2 181 TYR n 
2 182 SER n 
2 183 LEU n 
2 184 SER n 
2 185 SER n 
2 186 VAL n 
2 187 VAL n 
2 188 THR n 
2 189 VAL n 
2 190 PRO n 
2 191 SER n 
2 192 SER n 
2 193 SER n 
2 194 LEU n 
2 195 GLY n 
2 196 THR n 
2 197 GLN n 
2 198 THR n 
2 199 TYR n 
2 200 ILE n 
2 201 CYS n 
2 202 ASN n 
2 203 VAL n 
2 204 ASN n 
2 205 HIS n 
2 206 LYS n 
2 207 PRO n 
2 208 SER n 
2 209 ASN n 
2 210 THR n 
2 211 LYS n 
2 212 VAL n 
2 213 ASP n 
2 214 LYS n 
2 215 LYS n 
2 216 VAL n 
2 217 GLU n 
2 218 PRO n 
2 219 LYS n 
2 220 SER n 
2 221 CYS n 
2 222 ASP n 
2 223 LYS n 
2 224 HIS n 
2 225 HIS n 
2 226 HIS n 
2 227 HIS n 
2 228 HIS n 
2 229 HIS n 
3 1   ASP n 
3 2   ILE n 
3 3   GLN n 
3 4   LEU n 
3 5   THR n 
3 6   GLN n 
3 7   SER n 
3 8   PRO n 
3 9   ASP n 
3 10  SER n 
3 11  LEU n 
3 12  ALA n 
3 13  VAL n 
3 14  SER n 
3 15  LEU n 
3 16  GLY n 
3 17  GLU n 
3 18  ARG n 
3 19  ALA n 
3 20  THR n 
3 21  ILE n 
3 22  ASN n 
3 23  CYS n 
3 24  LYS n 
3 25  SER n 
3 26  SER n 
3 27  GLN n 
3 28  SER n 
3 29  VAL n 
3 30  LEU n 
3 31  TYR n 
3 32  SER n 
3 33  SER n 
3 34  ILE n 
3 35  ASN n 
3 36  LYS n 
3 37  ASN n 
3 38  TYR n 
3 39  LEU n 
3 40  ALA n 
3 41  TRP n 
3 42  TYR n 
3 43  GLN n 
3 44  GLN n 
3 45  LYS n 
3 46  PRO n 
3 47  GLY n 
3 48  GLN n 
3 49  PRO n 
3 50  PRO n 
3 51  LYS n 
3 52  LEU n 
3 53  LEU n 
3 54  ILE n 
3 55  TYR n 
3 56  TRP n 
3 57  ALA n 
3 58  SER n 
3 59  THR n 
3 60  ARG n 
3 61  GLU n 
3 62  SER n 
3 63  GLY n 
3 64  VAL n 
3 65  PRO n 
3 66  ASP n 
3 67  ARG n 
3 68  PHE n 
3 69  SER n 
3 70  GLY n 
3 71  SER n 
3 72  GLY n 
3 73  SER n 
3 74  GLY n 
3 75  THR n 
3 76  ASP n 
3 77  PHE n 
3 78  THR n 
3 79  LEU n 
3 80  THR n 
3 81  ILE n 
3 82  SER n 
3 83  SER n 
3 84  LEU n 
3 85  GLN n 
3 86  ALA n 
3 87  GLU n 
3 88  ASP n 
3 89  VAL n 
3 90  ALA n 
3 91  VAL n 
3 92  TYR n 
3 93  TYR n 
3 94  CYS n 
3 95  GLN n 
3 96  GLN n 
3 97  TYR n 
3 98  TYR n 
3 99  SER n 
3 100 THR n 
3 101 PRO n 
3 102 TYR n 
3 103 THR n 
3 104 PHE n 
3 105 GLY n 
3 106 GLN n 
3 107 GLY n 
3 108 THR n 
3 109 LYS n 
3 110 VAL n 
3 111 GLU n 
3 112 ILE n 
3 113 LYS n 
3 114 ARG n 
3 115 THR n 
3 116 VAL n 
3 117 ALA n 
3 118 ALA n 
3 119 PRO n 
3 120 SER n 
3 121 VAL n 
3 122 PHE n 
3 123 ILE n 
3 124 PHE n 
3 125 PRO n 
3 126 PRO n 
3 127 SER n 
3 128 ASP n 
3 129 GLU n 
3 130 GLN n 
3 131 LEU n 
3 132 LYS n 
3 133 SER n 
3 134 GLY n 
3 135 THR n 
3 136 ALA n 
3 137 SER n 
3 138 VAL n 
3 139 VAL n 
3 140 CYS n 
3 141 LEU n 
3 142 LEU n 
3 143 ASN n 
3 144 ASN n 
3 145 PHE n 
3 146 TYR n 
3 147 PRO n 
3 148 ARG n 
3 149 GLU n 
3 150 ALA n 
3 151 LYS n 
3 152 VAL n 
3 153 GLN n 
3 154 TRP n 
3 155 LYS n 
3 156 VAL n 
3 157 ASP n 
3 158 ASN n 
3 159 ALA n 
3 160 LEU n 
3 161 GLN n 
3 162 SER n 
3 163 GLY n 
3 164 ASN n 
3 165 SER n 
3 166 GLN n 
3 167 GLU n 
3 168 SER n 
3 169 VAL n 
3 170 THR n 
3 171 GLU n 
3 172 GLN n 
3 173 ASP n 
3 174 SER n 
3 175 LYS n 
3 176 ASP n 
3 177 SER n 
3 178 THR n 
3 179 TYR n 
3 180 SER n 
3 181 LEU n 
3 182 SER n 
3 183 SER n 
3 184 THR n 
3 185 LEU n 
3 186 THR n 
3 187 LEU n 
3 188 SER n 
3 189 LYS n 
3 190 ALA n 
3 191 ASP n 
3 192 TYR n 
3 193 GLU n 
3 194 LYS n 
3 195 HIS n 
3 196 LYS n 
3 197 VAL n 
3 198 TYR n 
3 199 ALA n 
3 200 CYS n 
3 201 GLU n 
3 202 VAL n 
3 203 THR n 
3 204 HIS n 
3 205 GLN n 
3 206 GLY n 
3 207 LEU n 
3 208 SER n 
3 209 SER n 
3 210 PRO n 
3 211 VAL n 
3 212 THR n 
3 213 LYS n 
3 214 SER n 
3 215 PHE n 
3 216 ASN n 
3 217 ARG n 
3 218 GLY n 
3 219 GLU n 
3 220 CYS n 
4 1   GLN n 
4 2   VAL n 
4 3   GLN n 
4 4   LEU n 
4 5   VAL n 
4 6   GLU n 
4 7   SER n 
4 8   GLY n 
4 9   GLY n 
4 10  GLY n 
4 11  LEU n 
4 12  MET n 
4 13  GLN n 
4 14  ALA n 
4 15  GLY n 
4 16  GLY n 
4 17  SER n 
4 18  LEU n 
4 19  ARG n 
4 20  LEU n 
4 21  SER n 
4 22  CYS n 
4 23  ALA n 
4 24  VAL n 
4 25  SER n 
4 26  GLY n 
4 27  ARG n 
4 28  THR n 
4 29  PHE n 
4 30  SER n 
4 31  THR n 
4 32  ALA n 
4 33  ALA n 
4 34  MET n 
4 35  GLY n 
4 36  TRP n 
4 37  PHE n 
4 38  ARG n 
4 39  GLN n 
4 40  ALA n 
4 41  PRO n 
4 42  GLY n 
4 43  LYS n 
4 44  GLU n 
4 45  ARG n 
4 46  GLU n 
4 47  PHE n 
4 48  VAL n 
4 49  ALA n 
4 50  ALA n 
4 51  ILE n 
4 52  ARG n 
4 53  TRP n 
4 54  SER n 
4 55  GLY n 
4 56  GLY n 
4 57  SER n 
4 58  ALA n 
4 59  TYR n 
4 60  TYR n 
4 61  ALA n 
4 62  ASP n 
4 63  SER n 
4 64  VAL n 
4 65  LYS n 
4 66  GLY n 
4 67  ARG n 
4 68  PHE n 
4 69  THR n 
4 70  ILE n 
4 71  SER n 
4 72  ARG n 
4 73  ASP n 
4 74  LYS n 
4 75  ALA n 
4 76  LYS n 
4 77  ASN n 
4 78  THR n 
4 79  VAL n 
4 80  TYR n 
4 81  LEU n 
4 82  GLN n 
4 83  MET n 
4 84  ASN n 
4 85  SER n 
4 86  LEU n 
4 87  LYS n 
4 88  TYR n 
4 89  GLU n 
4 90  ASP n 
4 91  THR n 
4 92  ALA n 
4 93  VAL n 
4 94  TYR n 
4 95  TYR n 
4 96  CYS n 
4 97  ALA n 
4 98  ARG n 
4 99  THR n 
4 100 GLU n 
4 101 ASN n 
4 102 VAL n 
4 103 ARG n 
4 104 SER n 
4 105 LEU n 
4 106 LEU n 
4 107 SER n 
4 108 ASP n 
4 109 TYR n 
4 110 ALA n 
4 111 THR n 
4 112 TRP n 
4 113 PRO n 
4 114 TYR n 
4 115 ASP n 
4 116 TYR n 
4 117 TRP n 
4 118 GLY n 
4 119 GLN n 
4 120 GLY n 
4 121 THR n 
4 122 GLN n 
4 123 VAL n 
4 124 THR n 
4 125 VAL n 
4 126 SER n 
4 127 SER n 
4 128 LYS n 
4 129 HIS n 
4 130 HIS n 
4 131 HIS n 
4 132 HIS n 
4 133 HIS n 
4 134 HIS n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 210 2019-nCoV ? 'S, 2' ? ? ? ? ? ? 'Severe acute respiratory syndrome coronavirus 2' 2697049 ? 
? ? ? ? ? ? human 'Homo sapiens'     9606 ? ? ? ? ? ? ? ? 'HEK293S GnTI-' CRL-3022 ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 229 human     ? ?      ? ? ? ? ? ? 'Homo sapiens'                                    9606    ? 
? ? ? ? ? ? human 'Homo sapiens'     9606 ? ? ? ? ? ? ? ? HEK293T         ?        ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 220 human     ? ?      ? ? ? ? ? ? 'Homo sapiens'                                    9606    ? 
? ? ? ? ? ? human 'Homo sapiens'     9606 ? ? ? ? ? ? ? ? ?               ?        ? ? ? ? ? ? ? ? ? ? ? 
4 1 sample 'Biological sequence' 1 134 llama     ? ?      ? ? ? ? ? ? 'Lama glama'                                      9844    ? 
? ? ? ? ? ? ?     'Escherichia coli' 562  ? ? ? ? ? ? ? ? ?               ?        ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP SPIKE_SARS2 P0DTC2 ? 1 
;PNITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSFVIRGDEVRQ
IAPGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCY
FPLQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTN
;
330 
2 PDB 6YZ7        6YZ7   ? 2 ? 1   
3 PDB 6YZ7        6YZ7   ? 3 ? 1   
4 PDB 6YZ7        6YZ7   ? 4 ? 1   
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 6YZ7 AAA 1 ? 203 ? P0DTC2 330 ? 532 ? 330 532 
2 2 6YZ7 BBB 1 ? 229 ? 6YZ7   0   ? 228 ? 0   228 
3 3 6YZ7 CCC 1 ? 220 ? 6YZ7   1   ? 220 ? 1   220 
4 4 6YZ7 DDD 1 ? 134 ? 6YZ7   1   ? 134 ? 1   134 
5 1 6YZ7 EEE 1 ? 203 ? P0DTC2 330 ? 532 ? 330 532 
6 4 6YZ7 FFF 1 ? 134 ? 6YZ7   1   ? 134 ? 1   134 
7 2 6YZ7 HHH 1 ? 229 ? 6YZ7   0   ? 228 ? 0   228 
8 3 6YZ7 LLL 1 ? 220 ? 6YZ7   1   ? 220 ? 1   220 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 6YZ7 LYS AAA 204 ? UNP P0DTC2 ? ? 'expression tag' 533 1  
1 6YZ7 HIS AAA 205 ? UNP P0DTC2 ? ? 'expression tag' 534 2  
1 6YZ7 HIS AAA 206 ? UNP P0DTC2 ? ? 'expression tag' 535 3  
1 6YZ7 HIS AAA 207 ? UNP P0DTC2 ? ? 'expression tag' 536 4  
1 6YZ7 HIS AAA 208 ? UNP P0DTC2 ? ? 'expression tag' 537 5  
1 6YZ7 HIS AAA 209 ? UNP P0DTC2 ? ? 'expression tag' 538 6  
1 6YZ7 HIS AAA 210 ? UNP P0DTC2 ? ? 'expression tag' 539 7  
5 6YZ7 LYS EEE 204 ? UNP P0DTC2 ? ? 'expression tag' 533 8  
5 6YZ7 HIS EEE 205 ? UNP P0DTC2 ? ? 'expression tag' 534 9  
5 6YZ7 HIS EEE 206 ? UNP P0DTC2 ? ? 'expression tag' 535 10 
5 6YZ7 HIS EEE 207 ? UNP P0DTC2 ? ? 'expression tag' 536 11 
5 6YZ7 HIS EEE 208 ? UNP P0DTC2 ? ? 'expression tag' 537 12 
5 6YZ7 HIS EEE 209 ? UNP P0DTC2 ? ? 'expression tag' 538 13 
5 6YZ7 HIS EEE 210 ? UNP P0DTC2 ? ? 'expression tag' 539 14 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking'          y ALANINE                ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking'          y ARGININE               ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking'          y ASPARAGINE             ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking'          y 'ASPARTIC ACID'        ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking'          y CYSTEINE               ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking'          y GLUTAMINE              ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking'          y 'GLUTAMIC ACID'        ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'            y GLYCINE                ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking'          y HISTIDINE              ? 'C6 H10 N3 O2 1' 156.162 
ILE 'L-peptide linking'          y ISOLEUCINE             ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking'          y LEUCINE                ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking'          y LYSINE                 ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking'          y METHIONINE             ? 'C5 H11 N O2 S'  149.211 
NAG 'D-saccharide, beta linking' . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6'    221.208 
PHE 'L-peptide linking'          y PHENYLALANINE          ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking'          y PROLINE                ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking'          y SERINE                 ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking'          y THREONINE              ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking'          y TRYPTOPHAN             ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking'          y TYROSINE               ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking'          y VALINE                 ? 'C5 H11 N O2'    117.146 
# 
_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                   6YZ7 
_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            3.92 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         68.59 
_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_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION' 
_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            298 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;The best crystals were grown in condition containing 0.1 M sodium citrate tribasic dihydrate, pH 5.0, 10% (w/v) Polyethylene glycol 6000.
;
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             'liquid nitrogen' 
_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 PILATUS 6M-F' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-04-20 
_diffrn_detector.pdbx_frequency               ? 
# 
_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   0.978 
_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                        'DIAMOND BEAMLINE I03' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.978 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I03 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         6YZ7 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                3.29 
_reflns.d_resolution_low                 128.187 
_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                       40954 
_reflns.observed_criterion               ? 
_reflns.observed_criterion_F_max         ? 
_reflns.observed_criterion_F_min         ? 
_reflns.observed_criterion_I_max         ? 
_reflns.observed_criterion_I_min         ? 
_reflns.observed_criterion_sigma_F       ? 
_reflns.observed_criterion_sigma_I       ? 
_reflns.percent_possible_obs             98 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  78 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  ? 
_reflns.pdbx_netI_over_av_sigmaI         ? 
_reflns.pdbx_netI_over_sigmaI            4.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  ? 
_reflns.pdbx_Rpim_I_all                  0.094 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         ? 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     0.994 
_reflns.pdbx_CC_star                     ? 
_reflns.pdbx_R_split                     ? 
# 
_reflns_shell.d_res_high                  3.29 
_reflns_shell.d_res_low                   3.35 
_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           1538 
_reflns_shell.percent_possible_all        ? 
_reflns_shell.percent_possible_obs        ? 
_reflns_shell.Rmerge_F_all                ? 
_reflns_shell.Rmerge_F_obs                ? 
_reflns_shell.Rmerge_I_all                ? 
_reflns_shell.Rmerge_I_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_Rsym_value             ? 
_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             4.094 
_reflns_shell.pdbx_rejects                ? 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_CC_half                0.369 
_reflns_shell.pdbx_CC_star                ? 
_reflns_shell.pdbx_R_split                ? 
# 
_refine.aniso_B[1][1]                            -1.970 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.000 
_refine.aniso_B[2][2]                            -1.970 
_refine.aniso_B[2][3]                            0.000 
_refine.aniso_B[3][3]                            3.940 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               144.159 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.935 
_refine.correlation_coeff_Fo_to_Fc_free          0.930 
_refine.details                                  'Hydrogens have been added in their riding positions' 
_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                                 6YZ7 
_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                            3.300 
_refine.ls_d_res_low                             128.187 
_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                     40954 
_refine.ls_number_reflns_R_free                  1939 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.292 
_refine.ls_percent_reflns_R_free                 4.735 
_refine.ls_R_factor_all                          0.239 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.2688 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2377 
_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                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      6YLA 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  0.500 
_refine.pdbx_solvent_vdw_probe_radii             1.100 
_refine.pdbx_solvent_ion_probe_radii             1.000 
_refine.pdbx_solvent_shrinkage_radii             1.000 
_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                 ? 
_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                             94.993 
_refine.overall_SU_ML                            0.571 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        11686 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         28 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               11714 
_refine_hist.d_res_high                       3.300 
_refine_hist.d_res_low                        128.187 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.004  0.013   12028 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.017   10650 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.390  1.649   16366 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.126  1.574   24822 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.668  5.000   1504  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 33.684 22.796  558   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 17.533 15.000  1886  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 14.960 15.000  52    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.049  0.200   1560  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.004  0.020   13512 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020   2568  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? 0.206  0.200   1894  ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? 0.179  0.200   10037 ? r_symmetry_nbd_other         ? ? 
'X-RAY DIFFRACTION' ? 0.169  0.200   5567  ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? 0.073  0.200   5591  ? r_symmetry_nbtor_other       ? ? 
'X-RAY DIFFRACTION' ? 0.164  0.200   237   ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? 0.320  0.200   4     ? r_symmetry_xyhbond_nbd_other ? ? 
'X-RAY DIFFRACTION' ? 0.236  0.200   19    ? r_symmetry_nbd_refined       ? ? 
'X-RAY DIFFRACTION' ? 0.237  0.200   62    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? 1.678  9.809   6045  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.679  9.808   6044  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.879  14.712  7540  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.879  14.713  7541  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 1.600  9.993   5982  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.600  9.994   5983  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.857  14.928  8826  ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.857  14.929  8827  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.952  109.116 12487 ? r_lrange_it                  ? ? 
'X-RAY DIFFRACTION' ? 4.951  109.116 12488 ? r_lrange_other               ? ? 
'X-RAY DIFFRACTION' ? 0.046  0.050   6051  ? r_ncsr_local_group_1         ? ? 
'X-RAY DIFFRACTION' ? 0.063  0.050   6154  ? r_ncsr_local_group_2         ? ? 
'X-RAY DIFFRACTION' ? 0.042  0.050   6556  ? r_ncsr_local_group_3         ? ? 
'X-RAY DIFFRACTION' ? 0.014  0.050   3842  ? r_ncsr_local_group_4         ? ? 
# 
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 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
'X-RAY DIFFRACTION' 3.300  3.386   3094 . 66  1472 49.7091  . 0.413 . 0.379 . 0.415 . . . . . 0.413 . 20 . 0.550 0.582 
'X-RAY DIFFRACTION' 3.386  3.478   2979 . 141 2818 99.3286  . 0.438 . 0.467 . 0.436 . . . . . 0.432 . 20 . 0.536 0.494 
'X-RAY DIFFRACTION' 3.478  3.579   2946 . 151 2795 100.0000 . 0.385 . 0.422 . 0.383 . . . . . 0.387 . 20 . 0.469 0.466 
'X-RAY DIFFRACTION' 3.579  3.689   2855 . 152 2703 100.0000 . 0.396 . 0.419 . 0.394 . . . . . 0.394 . 20 . 0.506 0.499 
'X-RAY DIFFRACTION' 3.689  3.810   2755 . 117 2638 100.0000 . 0.335 . 0.301 . 0.337 . . . . . 0.338 . 20 . 0.633 0.623 
'X-RAY DIFFRACTION' 3.810  3.944   2687 . 131 2556 100.0000 . 0.349 . 0.415 . 0.346 . . . . . 0.337 . 20 . 0.717 0.674 
'X-RAY DIFFRACTION' 3.944  4.092   2578 . 116 2462 100.0000 . 0.281 . 0.298 . 0.280 . . . . . 0.265 . 20 . 0.834 0.855 
'X-RAY DIFFRACTION' 4.092  4.259   2495 . 120 2375 100.0000 . 0.238 . 0.240 . 0.238 . . . . . 0.217 . 20 . 0.901 0.903 
'X-RAY DIFFRACTION' 4.259  4.449   2405 . 101 2304 100.0000 . 0.213 . 0.250 . 0.212 . . . . . 0.183 . 20 . 0.929 0.900 
'X-RAY DIFFRACTION' 4.449  4.665   2308 . 110 2198 100.0000 . 0.188 . 0.207 . 0.187 . . . . . 0.158 . 20 . 0.940 0.945 
'X-RAY DIFFRACTION' 4.665  4.917   2168 . 106 2062 100.0000 . 0.169 . 0.214 . 0.167 . . . . . 0.138 . 20 . 0.956 0.938 
'X-RAY DIFFRACTION' 4.917  5.215   2106 . 105 2001 100.0000 . 0.203 . 0.257 . 0.200 . . . . . 0.163 . 20 . 0.936 0.921 
'X-RAY DIFFRACTION' 5.215  5.575   1954 . 92  1862 100.0000 . 0.202 . 0.239 . 0.200 . . . . . 0.166 . 20 . 0.938 0.913 
'X-RAY DIFFRACTION' 5.575  6.020   1840 . 100 1740 100.0000 . 0.216 . 0.266 . 0.214 . . . . . 0.178 . 20 . 0.939 0.921 
'X-RAY DIFFRACTION' 6.020  6.593   1707 . 77  1630 100.0000 . 0.236 . 0.264 . 0.235 . . . . . 0.201 . 20 . 0.931 0.929 
'X-RAY DIFFRACTION' 6.593  7.369   1561 . 66  1495 100.0000 . 0.219 . 0.285 . 0.216 . . . . . 0.183 . 20 . 0.934 0.909 
'X-RAY DIFFRACTION' 7.369  8.505   1368 . 67  1301 100.0000 . 0.169 . 0.199 . 0.168 . . . . . 0.142 . 20 . 0.958 0.950 
'X-RAY DIFFRACTION' 8.505  10.405  1197 . 49  1148 100.0000 . 0.149 . 0.167 . 0.148 . . . . . 0.136 . 20 . 0.975 0.974 
'X-RAY DIFFRACTION' 10.405 14.666  941  . 46  895  100.0000 . 0.179 . 0.222 . 0.177 . . . . . 0.167 . 20 . 0.974 0.970 
'X-RAY DIFFRACTION' 14.666 128.187 586  . 26  560  100.0000 . 0.411 . 0.356 . 0.414 . . . . . 0.397 . 20 . 0.906 0.944 
# 
loop_
_struct_ncs_dom.id 
_struct_ncs_dom.details 
_struct_ncs_dom.pdbx_ens_id 
1 'Chains AAA EEE' 1 
2 'Chains BBB HHH' 2 
3 'Chains CCC LLL' 3 
4 'Chains DDD FFF' 4 
# 
loop_
_struct_ncs_ens.details 
_struct_ncs_ens.id 
_struct_ncs_ens.point_group 
? 1 ? 
? 2 ? 
? 3 ? 
? 4 ? 
# 
_struct.entry_id                     6YZ7 
_struct.title                        'H11-D4, SARS-CoV-2 RBD, CR3022 ternary complex' 
_struct.pdbx_descriptor              'Spike glycoprotein, Antibody Cr3022, Antibody light chain, Nanobody' 
_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        6YZ7 
_struct_keywords.text            'Antibody, nanobody complex, rbd, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 1 ? 
F N N 4 ? 
G N N 2 ? 
H N N 3 ? 
I N N 5 ? 
J N N 5 ? 
# 
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 PHE A 9   ? ASN A 14  ? PHE AAA 338 ASN AAA 343 1 ? 6 
HELX_P HELX_P2  AA2 SER A 20  ? TRP A 24  ? SER AAA 349 TRP AAA 353 5 ? 5 
HELX_P HELX_P3  AA3 TYR A 36  ? ASN A 41  ? TYR AAA 365 ASN AAA 370 1 ? 6 
HELX_P HELX_P4  AA4 LYS A 57  ? LEU A 61  ? LYS AAA 386 LEU AAA 390 5 ? 5 
HELX_P HELX_P5  AA5 ASP A 76  ? ILE A 81  ? ASP AAA 405 ILE AAA 410 5 ? 6 
HELX_P HELX_P6  AA6 GLY A 87  ? ASN A 93  ? GLY AAA 416 ASN AAA 422 1 ? 7 
HELX_P HELX_P7  AA7 SER A 109 ? SER A 114 ? SER AAA 438 SER AAA 443 1 ? 6 
HELX_P HELX_P8  AA8 GLY A 173 ? TYR A 176 ? GLY AAA 502 TYR AAA 505 5 ? 4 
HELX_P HELX_P9  AA9 GLY B 29  ? ILE B 31  ? GLY BBB 28  ILE BBB 30  5 ? 3 
HELX_P HELX_P10 AB1 LYS B 75  ? ILE B 77  ? LYS BBB 74  ILE BBB 76  5 ? 3 
HELX_P HELX_P11 AB2 SER B 161 ? ALA B 163 ? SER BBB 160 ALA BBB 162 5 ? 3 
HELX_P HELX_P12 AB3 SER B 192 ? LEU B 194 ? SER BBB 191 LEU BBB 193 5 ? 3 
HELX_P HELX_P13 AB4 GLN C 85  ? VAL C 89  ? GLN CCC 85  VAL CCC 89  5 ? 5 
HELX_P HELX_P14 AB5 SER C 127 ? GLY C 134 ? SER CCC 127 GLY CCC 134 1 ? 8 
HELX_P HELX_P15 AB6 LYS C 189 ? GLU C 193 ? LYS CCC 189 GLU CCC 193 1 ? 5 
HELX_P HELX_P16 AB7 ARG D 27  ? THR D 31  ? ARG DDD 27  THR DDD 31  5 ? 5 
HELX_P HELX_P17 AB8 LYS D 87  ? THR D 91  ? LYS DDD 87  THR DDD 91  5 ? 5 
HELX_P HELX_P18 AB9 LEU D 105 ? ALA D 110 ? LEU DDD 105 ALA DDD 110 5 ? 6 
HELX_P HELX_P19 AC1 PHE E 9   ? ASN E 14  ? PHE EEE 338 ASN EEE 343 1 ? 6 
HELX_P HELX_P20 AC2 SER E 20  ? TRP E 24  ? SER EEE 349 TRP EEE 353 5 ? 5 
HELX_P HELX_P21 AC3 TYR E 36  ? ASN E 41  ? TYR EEE 365 ASN EEE 370 1 ? 6 
HELX_P HELX_P22 AC4 LYS E 57  ? LEU E 61  ? LYS EEE 386 LEU EEE 390 5 ? 5 
HELX_P HELX_P23 AC5 ASP E 76  ? ILE E 81  ? ASP EEE 405 ILE EEE 410 5 ? 6 
HELX_P HELX_P24 AC6 GLY E 87  ? ASN E 93  ? GLY EEE 416 ASN EEE 422 1 ? 7 
HELX_P HELX_P25 AC7 SER E 109 ? SER E 114 ? SER EEE 438 SER EEE 443 1 ? 6 
HELX_P HELX_P26 AC8 GLY E 173 ? TYR E 176 ? GLY EEE 502 TYR EEE 505 5 ? 4 
HELX_P HELX_P27 AC9 ARG F 27  ? THR F 31  ? ARG FFF 27  THR FFF 31  5 ? 5 
HELX_P HELX_P28 AD1 LYS F 87  ? THR F 91  ? LYS FFF 87  THR FFF 91  5 ? 5 
HELX_P HELX_P29 AD2 SER F 107 ? TRP F 112 ? SER FFF 107 TRP FFF 112 1 ? 6 
HELX_P HELX_P30 AD3 GLY G 29  ? ILE G 31  ? GLY HHH 28  ILE HHH 30  5 ? 3 
HELX_P HELX_P31 AD4 LYS G 75  ? ILE G 77  ? LYS HHH 74  ILE HHH 76  5 ? 3 
HELX_P HELX_P32 AD5 SER G 161 ? ALA G 163 ? SER HHH 160 ALA HHH 162 5 ? 3 
HELX_P HELX_P33 AD6 SER G 192 ? LEU G 194 ? SER HHH 191 LEU HHH 193 5 ? 3 
HELX_P HELX_P34 AD7 GLN H 85  ? VAL H 89  ? GLN LLL 85  VAL LLL 89  5 ? 5 
HELX_P HELX_P35 AD8 SER H 127 ? GLY H 134 ? SER LLL 127 GLY LLL 134 1 ? 8 
HELX_P HELX_P36 AD9 LYS H 189 ? GLU H 193 ? LYS LLL 189 GLU LLL 193 1 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ?   ? A CYS 7   SG  ? ? ? 1_555 A CYS 32  SG ? ? AAA CYS 336 AAA CYS 361 1_555 ? ? ? ? ? ? ? 2.050 ? 
disulf2  disulf ?   ? A CYS 50  SG  ? ? ? 1_555 A CYS 103 SG ? ? AAA CYS 379 AAA CYS 432 1_555 ? ? ? ? ? ? ? 2.035 ? 
disulf3  disulf ?   ? A CYS 62  SG  ? ? ? 1_555 A CYS 196 SG ? ? AAA CYS 391 AAA CYS 525 1_555 ? ? ? ? ? ? ? 2.040 ? 
disulf4  disulf ?   ? A CYS 151 SG  ? ? ? 1_555 A CYS 159 SG ? ? AAA CYS 480 AAA CYS 488 1_555 ? ? ? ? ? ? ? 2.038 ? 
disulf5  disulf ?   ? B CYS 23  SG  ? ? ? 1_555 B CYS 97  SG ? ? BBB CYS 22  BBB CYS 96  1_555 ? ? ? ? ? ? ? 2.046 ? 
disulf6  disulf ?   ? B CYS 145 SG  ? ? ? 1_555 B CYS 201 SG ? ? BBB CYS 144 BBB CYS 200 1_555 ? ? ? ? ? ? ? 2.038 ? 
disulf7  disulf ?   ? C CYS 23  SG  ? ? ? 1_555 C CYS 94  SG ? ? CCC CYS 23  CCC CYS 94  1_555 ? ? ? ? ? ? ? 2.060 ? 
disulf8  disulf ?   ? C CYS 140 SG  ? ? ? 1_555 C CYS 200 SG ? ? CCC CYS 140 CCC CYS 200 1_555 ? ? ? ? ? ? ? 2.027 ? 
disulf9  disulf ?   ? D CYS 22  SG  ? ? ? 1_555 D CYS 96  SG ? ? DDD CYS 22  DDD CYS 96  1_555 ? ? ? ? ? ? ? 2.037 ? 
disulf10 disulf ?   ? E CYS 7   SG  ? ? ? 1_555 E CYS 32  SG ? ? EEE CYS 336 EEE CYS 361 1_555 ? ? ? ? ? ? ? 2.053 ? 
disulf11 disulf ?   ? E CYS 50  SG  ? ? ? 1_555 E CYS 103 SG ? ? EEE CYS 379 EEE CYS 432 1_555 ? ? ? ? ? ? ? 2.043 ? 
disulf12 disulf ?   ? E CYS 62  SG  ? ? ? 1_555 E CYS 196 SG ? ? EEE CYS 391 EEE CYS 525 1_555 ? ? ? ? ? ? ? 2.029 ? 
disulf13 disulf ?   ? E CYS 151 SG  ? ? ? 1_555 E CYS 159 SG ? ? EEE CYS 480 EEE CYS 488 1_555 ? ? ? ? ? ? ? 1.987 ? 
disulf14 disulf ?   ? F CYS 22  SG  ? ? ? 1_555 F CYS 96  SG ? ? FFF CYS 22  FFF CYS 96  1_555 ? ? ? ? ? ? ? 2.035 ? 
disulf15 disulf ?   ? G CYS 23  SG  ? ? ? 1_555 G CYS 97  SG ? ? HHH CYS 22  HHH CYS 96  1_555 ? ? ? ? ? ? ? 2.056 ? 
disulf16 disulf ?   ? G CYS 145 SG  ? ? ? 1_555 G CYS 201 SG ? ? HHH CYS 144 HHH CYS 200 1_555 ? ? ? ? ? ? ? 2.046 ? 
disulf17 disulf ?   ? H CYS 23  SG  ? ? ? 1_555 H CYS 94  SG ? ? LLL CYS 23  LLL CYS 94  1_555 ? ? ? ? ? ? ? 2.053 ? 
disulf18 disulf ?   ? H CYS 140 SG  ? ? ? 1_555 H CYS 200 SG ? ? LLL CYS 140 LLL CYS 200 1_555 ? ? ? ? ? ? ? 2.027 ? 
covale1  covale one ? A ASN 14  ND2 ? ? ? 1_555 I NAG .   C1 ? ? AAA ASN 343 AAA NAG 601 1_555 ? ? ? ? ? ? ? 1.435 ? 
covale2  covale one ? E ASN 14  ND2 ? ? ? 1_555 J NAG .   C1 ? ? EEE ASN 343 EEE NAG 601 1_555 ? ? ? ? ? ? ? 1.430 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
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  PHE 151 B . ? PHE 150 BBB PRO 152 B ? PRO 151 BBB 1 -12.47 
2  GLU 153 B . ? GLU 152 BBB PRO 154 B ? PRO 153 BBB 1 -4.66  
3  SER 7   C . ? SER 7   CCC PRO 8   C ? PRO 8   CCC 1 1.17   
4  THR 100 C . ? THR 100 CCC PRO 101 C ? PRO 101 CCC 1 -1.20  
5  TYR 146 C . ? TYR 146 CCC PRO 147 C ? PRO 147 CCC 1 6.87   
6  PHE 151 G . ? PHE 150 HHH PRO 152 G ? PRO 151 HHH 1 -11.55 
7  GLU 153 G . ? GLU 152 HHH PRO 154 G ? PRO 153 HHH 1 5.15   
8  SER 7   H . ? SER 7   LLL PRO 8   H ? PRO 8   LLL 1 1.56   
9  THR 100 H . ? THR 100 LLL PRO 101 H ? PRO 101 LLL 1 1.33   
10 TYR 146 H . ? TYR 146 LLL PRO 147 H ? PRO 147 LLL 1 6.65   
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 4 ? 
AA5 ? 6 ? 
AA6 ? 4 ? 
AA7 ? 4 ? 
AA8 ? 4 ? 
AA9 ? 3 ? 
AB1 ? 4 ? 
AB2 ? 6 ? 
AB3 ? 4 ? 
AB4 ? 2 ? 
AB5 ? 4 ? 
AB6 ? 4 ? 
AB7 ? 4 ? 
AB8 ? 5 ? 
AB9 ? 4 ? 
AC1 ? 5 ? 
AC2 ? 2 ? 
AC3 ? 2 ? 
AC4 ? 4 ? 
AC5 ? 5 ? 
AC6 ? 4 ? 
AC7 ? 4 ? 
AC8 ? 6 ? 
AC9 ? 4 ? 
AD1 ? 4 ? 
AD2 ? 4 ? 
AD3 ? 3 ? 
AD4 ? 4 ? 
AD5 ? 6 ? 
AD6 ? 4 ? 
AD7 ? 2 ? 
AD8 ? 4 ? 
AD9 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB2 1 2 ? parallel      
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB2 4 5 ? anti-parallel 
AB2 5 6 ? anti-parallel 
AB3 1 2 ? parallel      
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB6 2 3 ? anti-parallel 
AB6 3 4 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB7 3 4 ? anti-parallel 
AB8 1 2 ? parallel      
AB8 2 3 ? anti-parallel 
AB8 3 4 ? anti-parallel 
AB8 4 5 ? anti-parallel 
AB9 1 2 ? parallel      
AB9 2 3 ? anti-parallel 
AB9 3 4 ? anti-parallel 
AC1 1 2 ? anti-parallel 
AC1 2 3 ? anti-parallel 
AC1 3 4 ? anti-parallel 
AC1 4 5 ? anti-parallel 
AC2 1 2 ? anti-parallel 
AC3 1 2 ? anti-parallel 
AC4 1 2 ? anti-parallel 
AC4 2 3 ? anti-parallel 
AC4 3 4 ? anti-parallel 
AC5 1 2 ? parallel      
AC5 2 3 ? anti-parallel 
AC5 3 4 ? anti-parallel 
AC5 4 5 ? anti-parallel 
AC6 1 2 ? parallel      
AC6 2 3 ? anti-parallel 
AC6 3 4 ? anti-parallel 
AC7 1 2 ? anti-parallel 
AC7 2 3 ? anti-parallel 
AC7 3 4 ? anti-parallel 
AC8 1 2 ? parallel      
AC8 2 3 ? anti-parallel 
AC8 3 4 ? anti-parallel 
AC8 4 5 ? anti-parallel 
AC8 5 6 ? anti-parallel 
AC9 1 2 ? parallel      
AC9 2 3 ? anti-parallel 
AC9 3 4 ? anti-parallel 
AD1 1 2 ? anti-parallel 
AD1 2 3 ? anti-parallel 
AD1 3 4 ? anti-parallel 
AD2 1 2 ? anti-parallel 
AD2 2 3 ? anti-parallel 
AD2 3 4 ? anti-parallel 
AD3 1 2 ? anti-parallel 
AD3 2 3 ? anti-parallel 
AD4 1 2 ? anti-parallel 
AD4 2 3 ? anti-parallel 
AD4 3 4 ? anti-parallel 
AD5 1 2 ? parallel      
AD5 2 3 ? anti-parallel 
AD5 3 4 ? anti-parallel 
AD5 4 5 ? anti-parallel 
AD5 5 6 ? anti-parallel 
AD6 1 2 ? parallel      
AD6 2 3 ? anti-parallel 
AD6 3 4 ? anti-parallel 
AD7 1 2 ? anti-parallel 
AD8 1 2 ? anti-parallel 
AD8 2 3 ? anti-parallel 
AD8 3 4 ? anti-parallel 
AD9 1 2 ? anti-parallel 
AD9 2 3 ? anti-parallel 
AD9 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ASN A 25  ? ILE A 29  ? ASN AAA 354 ILE AAA 358 
AA1 2 ASN A 65  ? ARG A 74  ? ASN AAA 394 ARG AAA 403 
AA1 3 PRO A 178 ? GLU A 187 ? PRO AAA 507 GLU AAA 516 
AA1 4 GLY A 102 ? ASN A 108 ? GLY AAA 431 ASN AAA 437 
AA1 5 THR A 47  ? TYR A 51  ? THR AAA 376 TYR AAA 380 
AA2 1 LEU A 123 ? ARG A 125 ? LEU AAA 452 ARG AAA 454 
AA2 2 LEU A 163 ? SER A 165 ? LEU AAA 492 SER AAA 494 
AA3 1 TYR A 144 ? GLN A 145 ? TYR AAA 473 GLN AAA 474 
AA3 2 CYS A 159 ? TYR A 160 ? CYS AAA 488 TYR AAA 489 
AA4 1 MET B 3   ? GLN B 7   ? MET BBB 2   GLN BBB 6   
AA4 2 LEU B 19  ? GLY B 27  ? LEU BBB 18  GLY BBB 26  
AA4 3 THR B 79  ? TRP B 84  ? THR BBB 78  TRP BBB 83  
AA4 4 VAL B 69  ? ASP B 74  ? VAL BBB 68  ASP BBB 73  
AA5 1 GLU B 11  ? LYS B 13  ? GLU BBB 10  LYS BBB 12  
AA5 2 THR B 114 ? VAL B 118 ? THR BBB 113 VAL BBB 117 
AA5 3 ALA B 93  ? SER B 101 ? ALA BBB 92  SER BBB 100 
AA5 4 TYR B 33  ? GLN B 40  ? TYR BBB 32  GLN BBB 39  
AA5 5 LEU B 46  ? TYR B 53  ? LEU BBB 45  TYR BBB 52  
AA5 6 GLU B 58  ? TYR B 61  ? GLU BBB 57  TYR BBB 60  
AA6 1 GLU B 11  ? LYS B 13  ? GLU BBB 10  LYS BBB 12  
AA6 2 THR B 114 ? VAL B 118 ? THR BBB 113 VAL BBB 117 
AA6 3 ALA B 93  ? SER B 101 ? ALA BBB 92  SER BBB 100 
AA6 4 VAL B 109 ? TRP B 110 ? VAL BBB 108 TRP BBB 109 
AA7 1 SER B 125 ? LEU B 129 ? SER BBB 124 LEU BBB 128 
AA7 2 THR B 140 ? TYR B 150 ? THR BBB 139 TYR BBB 149 
AA7 3 TYR B 181 ? PRO B 190 ? TYR BBB 180 PRO BBB 189 
AA7 4 VAL B 168 ? THR B 170 ? VAL BBB 167 THR BBB 169 
AA8 1 SER B 125 ? LEU B 129 ? SER BBB 124 LEU BBB 128 
AA8 2 THR B 140 ? TYR B 150 ? THR BBB 139 TYR BBB 149 
AA8 3 TYR B 181 ? PRO B 190 ? TYR BBB 180 PRO BBB 189 
AA8 4 VAL B 174 ? LEU B 175 ? VAL BBB 173 LEU BBB 174 
AA9 1 VAL B 155 ? TRP B 159 ? VAL BBB 154 TRP BBB 158 
AA9 2 TYR B 199 ? HIS B 205 ? TYR BBB 198 HIS BBB 204 
AA9 3 THR B 210 ? VAL B 216 ? THR BBB 209 VAL BBB 215 
AB1 1 LEU C 4   ? SER C 7   ? LEU CCC 4   SER CCC 7   
AB1 2 THR C 20  ? SER C 25  ? THR CCC 20  SER CCC 25  
AB1 3 ASP C 76  ? ILE C 81  ? ASP CCC 76  ILE CCC 81  
AB1 4 PHE C 68  ? SER C 73  ? PHE CCC 68  SER CCC 73  
AB2 1 SER C 10  ? SER C 14  ? SER CCC 10  SER CCC 14  
AB2 2 THR C 108 ? LYS C 113 ? THR CCC 108 LYS CCC 113 
AB2 3 ALA C 90  ? GLN C 96  ? ALA CCC 90  GLN CCC 96  
AB2 4 LEU C 39  ? GLN C 44  ? LEU CCC 39  GLN CCC 44  
AB2 5 LYS C 51  ? TYR C 55  ? LYS CCC 51  TYR CCC 55  
AB2 6 THR C 59  ? ARG C 60  ? THR CCC 59  ARG CCC 60  
AB3 1 SER C 10  ? SER C 14  ? SER CCC 10  SER CCC 14  
AB3 2 THR C 108 ? LYS C 113 ? THR CCC 108 LYS CCC 113 
AB3 3 ALA C 90  ? GLN C 96  ? ALA CCC 90  GLN CCC 96  
AB3 4 THR C 103 ? PHE C 104 ? THR CCC 103 PHE CCC 104 
AB4 1 LEU C 30  ? TYR C 31  ? LEU CCC 30  TYR CCC 31  
AB4 2 LYS C 36  ? ASN C 37  ? LYS CCC 36  ASN CCC 37  
AB5 1 SER C 120 ? PHE C 124 ? SER CCC 120 PHE CCC 124 
AB5 2 THR C 135 ? PHE C 145 ? THR CCC 135 PHE CCC 145 
AB5 3 TYR C 179 ? SER C 188 ? TYR CCC 179 SER CCC 188 
AB5 4 SER C 165 ? VAL C 169 ? SER CCC 165 VAL CCC 169 
AB6 1 LEU C 160 ? GLN C 161 ? LEU CCC 160 GLN CCC 161 
AB6 2 ALA C 150 ? VAL C 156 ? ALA CCC 150 VAL CCC 156 
AB6 3 VAL C 197 ? HIS C 204 ? VAL CCC 197 HIS CCC 204 
AB6 4 VAL C 211 ? ASN C 216 ? VAL CCC 211 ASN CCC 216 
AB7 1 GLN D 3   ? VAL D 5   ? GLN DDD 3   VAL DDD 5   
AB7 2 SER D 17  ? SER D 25  ? SER DDD 17  SER DDD 25  
AB7 3 THR D 78  ? ASN D 84  ? THR DDD 78  ASN DDD 84  
AB7 4 PHE D 68  ? ASP D 73  ? PHE DDD 68  ASP DDD 73  
AB8 1 LEU D 11  ? GLN D 13  ? LEU DDD 11  GLN DDD 13  
AB8 2 THR D 121 ? SER D 126 ? THR DDD 121 SER DDD 126 
AB8 3 ALA D 92  ? THR D 99  ? ALA DDD 92  THR DDD 99  
AB8 4 ALA D 33  ? GLN D 39  ? ALA DDD 33  GLN DDD 39  
AB8 5 GLU D 46  ? ARG D 52  ? GLU DDD 46  ARG DDD 52  
AB9 1 LEU D 11  ? GLN D 13  ? LEU DDD 11  GLN DDD 13  
AB9 2 THR D 121 ? SER D 126 ? THR DDD 121 SER DDD 126 
AB9 3 ALA D 92  ? THR D 99  ? ALA DDD 92  THR DDD 99  
AB9 4 TYR D 116 ? TRP D 117 ? TYR DDD 116 TRP DDD 117 
AC1 1 ASN E 25  ? ILE E 29  ? ASN EEE 354 ILE EEE 358 
AC1 2 ASN E 65  ? ARG E 74  ? ASN EEE 394 ARG EEE 403 
AC1 3 PRO E 178 ? GLU E 187 ? PRO EEE 507 GLU EEE 516 
AC1 4 GLY E 102 ? ASN E 108 ? GLY EEE 431 ASN EEE 437 
AC1 5 THR E 47  ? TYR E 51  ? THR EEE 376 TYR EEE 380 
AC2 1 LEU E 123 ? ARG E 125 ? LEU EEE 452 ARG EEE 454 
AC2 2 LEU E 163 ? SER E 165 ? LEU EEE 492 SER EEE 494 
AC3 1 TYR E 144 ? GLN E 145 ? TYR EEE 473 GLN EEE 474 
AC3 2 CYS E 159 ? TYR E 160 ? CYS EEE 488 TYR EEE 489 
AC4 1 GLN F 3   ? VAL F 5   ? GLN FFF 3   VAL FFF 5   
AC4 2 SER F 17  ? SER F 25  ? SER FFF 17  SER FFF 25  
AC4 3 THR F 78  ? ASN F 84  ? THR FFF 78  ASN FFF 84  
AC4 4 PHE F 68  ? ASP F 73  ? PHE FFF 68  ASP FFF 73  
AC5 1 LEU F 11  ? GLN F 13  ? LEU FFF 11  GLN FFF 13  
AC5 2 THR F 121 ? SER F 126 ? THR FFF 121 SER FFF 126 
AC5 3 ALA F 92  ? THR F 99  ? ALA FFF 92  THR FFF 99  
AC5 4 ALA F 33  ? GLN F 39  ? ALA FFF 33  GLN FFF 39  
AC5 5 GLU F 46  ? ARG F 52  ? GLU FFF 46  ARG FFF 52  
AC6 1 LEU F 11  ? GLN F 13  ? LEU FFF 11  GLN FFF 13  
AC6 2 THR F 121 ? SER F 126 ? THR FFF 121 SER FFF 126 
AC6 3 ALA F 92  ? THR F 99  ? ALA FFF 92  THR FFF 99  
AC6 4 TYR F 116 ? TRP F 117 ? TYR FFF 116 TRP FFF 117 
AC7 1 MET G 3   ? GLN G 7   ? MET HHH 2   GLN HHH 6   
AC7 2 LEU G 19  ? GLY G 27  ? LEU HHH 18  GLY HHH 26  
AC7 3 THR G 79  ? TRP G 84  ? THR HHH 78  TRP HHH 83  
AC7 4 VAL G 69  ? ASP G 74  ? VAL HHH 68  ASP HHH 73  
AC8 1 GLU G 11  ? LYS G 13  ? GLU HHH 10  LYS HHH 12  
AC8 2 THR G 114 ? VAL G 118 ? THR HHH 113 VAL HHH 117 
AC8 3 ALA G 93  ? SER G 101 ? ALA HHH 92  SER HHH 100 
AC8 4 TYR G 33  ? GLN G 40  ? TYR HHH 32  GLN HHH 39  
AC8 5 LEU G 46  ? TYR G 53  ? LEU HHH 45  TYR HHH 52  
AC8 6 GLU G 58  ? TYR G 61  ? GLU HHH 57  TYR HHH 60  
AC9 1 GLU G 11  ? LYS G 13  ? GLU HHH 10  LYS HHH 12  
AC9 2 THR G 114 ? VAL G 118 ? THR HHH 113 VAL HHH 117 
AC9 3 ALA G 93  ? SER G 101 ? ALA HHH 92  SER HHH 100 
AC9 4 VAL G 109 ? TRP G 110 ? VAL HHH 108 TRP HHH 109 
AD1 1 SER G 125 ? LEU G 129 ? SER HHH 124 LEU HHH 128 
AD1 2 THR G 140 ? TYR G 150 ? THR HHH 139 TYR HHH 149 
AD1 3 TYR G 181 ? PRO G 190 ? TYR HHH 180 PRO HHH 189 
AD1 4 VAL G 168 ? THR G 170 ? VAL HHH 167 THR HHH 169 
AD2 1 SER G 125 ? LEU G 129 ? SER HHH 124 LEU HHH 128 
AD2 2 THR G 140 ? TYR G 150 ? THR HHH 139 TYR HHH 149 
AD2 3 TYR G 181 ? PRO G 190 ? TYR HHH 180 PRO HHH 189 
AD2 4 VAL G 174 ? LEU G 175 ? VAL HHH 173 LEU HHH 174 
AD3 1 VAL G 155 ? TRP G 159 ? VAL HHH 154 TRP HHH 158 
AD3 2 TYR G 199 ? HIS G 205 ? TYR HHH 198 HIS HHH 204 
AD3 3 THR G 210 ? VAL G 216 ? THR HHH 209 VAL HHH 215 
AD4 1 LEU H 4   ? SER H 7   ? LEU LLL 4   SER LLL 7   
AD4 2 THR H 20  ? SER H 25  ? THR LLL 20  SER LLL 25  
AD4 3 ASP H 76  ? ILE H 81  ? ASP LLL 76  ILE LLL 81  
AD4 4 PHE H 68  ? SER H 73  ? PHE LLL 68  SER LLL 73  
AD5 1 SER H 10  ? SER H 14  ? SER LLL 10  SER LLL 14  
AD5 2 THR H 108 ? LYS H 113 ? THR LLL 108 LYS LLL 113 
AD5 3 ALA H 90  ? GLN H 96  ? ALA LLL 90  GLN LLL 96  
AD5 4 LEU H 39  ? GLN H 44  ? LEU LLL 39  GLN LLL 44  
AD5 5 LYS H 51  ? TYR H 55  ? LYS LLL 51  TYR LLL 55  
AD5 6 THR H 59  ? ARG H 60  ? THR LLL 59  ARG LLL 60  
AD6 1 SER H 10  ? SER H 14  ? SER LLL 10  SER LLL 14  
AD6 2 THR H 108 ? LYS H 113 ? THR LLL 108 LYS LLL 113 
AD6 3 ALA H 90  ? GLN H 96  ? ALA LLL 90  GLN LLL 96  
AD6 4 THR H 103 ? PHE H 104 ? THR LLL 103 PHE LLL 104 
AD7 1 LEU H 30  ? TYR H 31  ? LEU LLL 30  TYR LLL 31  
AD7 2 LYS H 36  ? ASN H 37  ? LYS LLL 36  ASN LLL 37  
AD8 1 SER H 120 ? PHE H 124 ? SER LLL 120 PHE LLL 124 
AD8 2 THR H 135 ? PHE H 145 ? THR LLL 135 PHE LLL 145 
AD8 3 TYR H 179 ? SER H 188 ? TYR LLL 179 SER LLL 188 
AD8 4 SER H 165 ? VAL H 169 ? SER LLL 165 VAL LLL 169 
AD9 1 LEU H 160 ? GLN H 161 ? LEU LLL 160 GLN LLL 161 
AD9 2 ALA H 150 ? VAL H 156 ? ALA LLL 150 VAL LLL 156 
AD9 3 VAL H 197 ? HIS H 204 ? VAL LLL 197 HIS LLL 204 
AD9 4 VAL H 211 ? ASN H 216 ? VAL LLL 211 ASN LLL 216 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ILE A 29  ? N ILE AAA 358 O VAL A 66  ? O VAL AAA 395 
AA1 2 3 N PHE A 71  ? N PHE AAA 400 O VAL A 181 ? O VAL AAA 510 
AA1 3 4 O VAL A 182 ? O VAL AAA 511 N ILE A 105 ? N ILE AAA 434 
AA1 4 5 O GLY A 102 ? O GLY AAA 431 N TYR A 51  ? N TYR AAA 380 
AA2 1 2 N TYR A 124 ? N TYR AAA 453 O GLN A 164 ? O GLN AAA 493 
AA3 1 2 N TYR A 144 ? N TYR AAA 473 O TYR A 160 ? O TYR AAA 489 
AA4 1 2 N VAL B 6   ? N VAL BBB 5   O LYS B 24  ? O LYS BBB 23  
AA4 2 3 N CYS B 23  ? N CYS BBB 22  O ALA B 80  ? O ALA BBB 79  
AA4 3 4 O TYR B 81  ? O TYR BBB 80  N SER B 72  ? N SER BBB 71  
AA5 1 2 N GLU B 11  ? N GLU BBB 10  O THR B 117 ? O THR BBB 116 
AA5 2 3 O THR B 114 ? O THR BBB 113 N TYR B 95  ? N TYR BBB 94  
AA5 3 4 O GLY B 100 ? O GLY BBB 99  N TRP B 34  ? N TRP BBB 33  
AA5 4 5 N ARG B 39  ? N ARG BBB 38  O GLU B 47  ? O GLU BBB 46  
AA5 5 6 N ILE B 51  ? N ILE BBB 50  O ARG B 60  ? O ARG BBB 59  
AA6 1 2 N GLU B 11  ? N GLU BBB 10  O THR B 117 ? O THR BBB 116 
AA6 2 3 O THR B 114 ? O THR BBB 113 N TYR B 95  ? N TYR BBB 94  
AA6 3 4 N GLY B 99  ? N GLY BBB 98  O VAL B 109 ? O VAL BBB 108 
AA7 1 2 N PHE B 127 ? N PHE BBB 126 O LEU B 146 ? O LEU BBB 145 
AA7 2 3 N CYS B 145 ? N CYS BBB 144 O SER B 185 ? O SER BBB 184 
AA7 3 4 O VAL B 186 ? O VAL BBB 185 N HIS B 169 ? N HIS BBB 168 
AA8 1 2 N PHE B 127 ? N PHE BBB 126 O LEU B 146 ? O LEU BBB 145 
AA8 2 3 N CYS B 145 ? N CYS BBB 144 O SER B 185 ? O SER BBB 184 
AA8 3 4 O SER B 182 ? O SER BBB 181 N VAL B 174 ? N VAL BBB 173 
AA9 1 2 N SER B 158 ? N SER BBB 157 O ASN B 202 ? O ASN BBB 201 
AA9 2 3 N VAL B 203 ? N VAL BBB 202 O VAL B 212 ? O VAL BBB 211 
AB1 1 2 N THR C 5   ? N THR CCC 5   O LYS C 24  ? O LYS CCC 24  
AB1 2 3 N CYS C 23  ? N CYS CCC 23  O PHE C 77  ? O PHE CCC 77  
AB1 3 4 O THR C 80  ? O THR CCC 80  N SER C 69  ? N SER CCC 69  
AB2 1 2 N LEU C 11  ? N LEU CCC 11  O GLU C 111 ? O GLU CCC 111 
AB2 2 3 O VAL C 110 ? O VAL CCC 110 N ALA C 90  ? N ALA CCC 90  
AB2 3 4 O TYR C 93  ? O TYR CCC 93  N TYR C 42  ? N TYR CCC 42  
AB2 4 5 N GLN C 43  ? N GLN CCC 43  O LYS C 51  ? O LYS CCC 51  
AB2 5 6 N TYR C 55  ? N TYR CCC 55  O THR C 59  ? O THR CCC 59  
AB3 1 2 N LEU C 11  ? N LEU CCC 11  O GLU C 111 ? O GLU CCC 111 
AB3 2 3 O VAL C 110 ? O VAL CCC 110 N ALA C 90  ? N ALA CCC 90  
AB3 3 4 N GLN C 96  ? N GLN CCC 96  O THR C 103 ? O THR CCC 103 
AB4 1 2 N TYR C 31  ? N TYR CCC 31  O LYS C 36  ? O LYS CCC 36  
AB5 1 2 N PHE C 122 ? N PHE CCC 122 O LEU C 141 ? O LEU CCC 141 
AB5 2 3 N VAL C 138 ? N VAL CCC 138 O LEU C 185 ? O LEU CCC 185 
AB5 3 4 O SER C 182 ? O SER CCC 182 N SER C 168 ? N SER CCC 168 
AB6 1 2 O GLN C 161 ? O GLN CCC 161 N TRP C 154 ? N TRP CCC 154 
AB6 2 3 N GLN C 153 ? N GLN CCC 153 O GLU C 201 ? O GLU CCC 201 
AB6 3 4 N VAL C 202 ? N VAL CCC 202 O VAL C 211 ? O VAL CCC 211 
AB7 1 2 N VAL D 5   ? N VAL DDD 5   O ALA D 23  ? O ALA DDD 23  
AB7 2 3 N CYS D 22  ? N CYS DDD 22  O VAL D 79  ? O VAL DDD 79  
AB7 3 4 O TYR D 80  ? O TYR DDD 80  N SER D 71  ? N SER DDD 71  
AB8 1 2 N MET D 12  ? N MET DDD 12  O SER D 126 ? O SER DDD 126 
AB8 2 3 O THR D 121 ? O THR DDD 121 N TYR D 94  ? N TYR DDD 94  
AB8 3 4 O TYR D 95  ? O TYR DDD 95  N PHE D 37  ? N PHE DDD 37  
AB8 4 5 N TRP D 36  ? N TRP DDD 36  O ALA D 49  ? O ALA DDD 49  
AB9 1 2 N MET D 12  ? N MET DDD 12  O SER D 126 ? O SER DDD 126 
AB9 2 3 O THR D 121 ? O THR DDD 121 N TYR D 94  ? N TYR DDD 94  
AB9 3 4 N ARG D 98  ? N ARG DDD 98  O TYR D 116 ? O TYR DDD 116 
AC1 1 2 N ILE E 29  ? N ILE EEE 358 O VAL E 66  ? O VAL EEE 395 
AC1 2 3 N ILE E 73  ? N ILE EEE 402 O TYR E 179 ? O TYR EEE 508 
AC1 3 4 O VAL E 182 ? O VAL EEE 511 N ILE E 105 ? N ILE EEE 434 
AC1 4 5 O GLY E 102 ? O GLY EEE 431 N TYR E 51  ? N TYR EEE 380 
AC2 1 2 N TYR E 124 ? N TYR EEE 453 O GLN E 164 ? O GLN EEE 493 
AC3 1 2 N TYR E 144 ? N TYR EEE 473 O TYR E 160 ? O TYR EEE 489 
AC4 1 2 N VAL F 5   ? N VAL FFF 5   O ALA F 23  ? O ALA FFF 23  
AC4 2 3 N CYS F 22  ? N CYS FFF 22  O VAL F 79  ? O VAL FFF 79  
AC4 3 4 O TYR F 80  ? O TYR FFF 80  N SER F 71  ? N SER FFF 71  
AC5 1 2 N MET F 12  ? N MET FFF 12  O THR F 124 ? O THR FFF 124 
AC5 2 3 O THR F 121 ? O THR FFF 121 N TYR F 94  ? N TYR FFF 94  
AC5 3 4 O TYR F 95  ? O TYR FFF 95  N PHE F 37  ? N PHE FFF 37  
AC5 4 5 N TRP F 36  ? N TRP FFF 36  O ALA F 49  ? O ALA FFF 49  
AC6 1 2 N MET F 12  ? N MET FFF 12  O THR F 124 ? O THR FFF 124 
AC6 2 3 O THR F 121 ? O THR FFF 121 N TYR F 94  ? N TYR FFF 94  
AC6 3 4 N ARG F 98  ? N ARG FFF 98  O TYR F 116 ? O TYR FFF 116 
AC7 1 2 N VAL G 6   ? N VAL HHH 5   O LYS G 24  ? O LYS HHH 23  
AC7 2 3 N CYS G 23  ? N CYS HHH 22  O ALA G 80  ? O ALA HHH 79  
AC7 3 4 O TYR G 81  ? O TYR HHH 80  N SER G 72  ? N SER HHH 71  
AC8 1 2 N GLU G 11  ? N GLU HHH 10  O THR G 117 ? O THR HHH 116 
AC8 2 3 O THR G 114 ? O THR HHH 113 N TYR G 95  ? N TYR HHH 94  
AC8 3 4 O GLY G 100 ? O GLY HHH 99  N TRP G 34  ? N TRP HHH 33  
AC8 4 5 N ARG G 39  ? N ARG HHH 38  O GLU G 47  ? O GLU HHH 46  
AC8 5 6 N ILE G 51  ? N ILE HHH 50  O ARG G 60  ? O ARG HHH 59  
AC9 1 2 N GLU G 11  ? N GLU HHH 10  O THR G 117 ? O THR HHH 116 
AC9 2 3 O THR G 114 ? O THR HHH 113 N TYR G 95  ? N TYR HHH 94  
AC9 3 4 N GLY G 99  ? N GLY HHH 98  O VAL G 109 ? O VAL HHH 108 
AD1 1 2 N PHE G 127 ? N PHE HHH 126 O LEU G 146 ? O LEU HHH 145 
AD1 2 3 N CYS G 145 ? N CYS HHH 144 O SER G 185 ? O SER HHH 184 
AD1 3 4 O VAL G 186 ? O VAL HHH 185 N HIS G 169 ? N HIS HHH 168 
AD2 1 2 N PHE G 127 ? N PHE HHH 126 O LEU G 146 ? O LEU HHH 145 
AD2 2 3 N CYS G 145 ? N CYS HHH 144 O SER G 185 ? O SER HHH 184 
AD2 3 4 O SER G 182 ? O SER HHH 181 N VAL G 174 ? N VAL HHH 173 
AD3 1 2 N SER G 158 ? N SER HHH 157 O ASN G 202 ? O ASN HHH 201 
AD3 2 3 N CYS G 201 ? N CYS HHH 200 O LYS G 214 ? O LYS HHH 213 
AD4 1 2 N THR H 5   ? N THR LLL 5   O LYS H 24  ? O LYS LLL 24  
AD4 2 3 N CYS H 23  ? N CYS LLL 23  O PHE H 77  ? O PHE LLL 77  
AD4 3 4 O THR H 80  ? O THR LLL 80  N SER H 69  ? N SER LLL 69  
AD5 1 2 N LEU H 11  ? N LEU LLL 11  O GLU H 111 ? O GLU LLL 111 
AD5 2 3 O VAL H 110 ? O VAL LLL 110 N ALA H 90  ? N ALA LLL 90  
AD5 3 4 O TYR H 93  ? O TYR LLL 93  N TYR H 42  ? N TYR LLL 42  
AD5 4 5 N GLN H 43  ? N GLN LLL 43  O LYS H 51  ? O LYS LLL 51  
AD5 5 6 N TYR H 55  ? N TYR LLL 55  O THR H 59  ? O THR LLL 59  
AD6 1 2 N LEU H 11  ? N LEU LLL 11  O GLU H 111 ? O GLU LLL 111 
AD6 2 3 O VAL H 110 ? O VAL LLL 110 N ALA H 90  ? N ALA LLL 90  
AD6 3 4 N GLN H 96  ? N GLN LLL 96  O THR H 103 ? O THR LLL 103 
AD7 1 2 N TYR H 31  ? N TYR LLL 31  O LYS H 36  ? O LYS LLL 36  
AD8 1 2 N PHE H 122 ? N PHE LLL 122 O LEU H 141 ? O LEU LLL 141 
AD8 2 3 N VAL H 138 ? N VAL LLL 138 O LEU H 185 ? O LEU LLL 185 
AD8 3 4 O SER H 182 ? O SER LLL 182 N SER H 168 ? N SER LLL 168 
AD9 1 2 O GLN H 161 ? O GLN LLL 161 N TRP H 154 ? N TRP LLL 154 
AD9 2 3 N GLN H 153 ? N GLN LLL 153 O GLU H 201 ? O GLU LLL 201 
AD9 3 4 N VAL H 202 ? N VAL LLL 202 O VAL H 211 ? O VAL LLL 211 
# 
_atom_sites.entry_id                    6YZ7 
_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.fract_transf_matrix[1][1]   0.006468 
_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]   0.006468 
_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]   0.004361 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
C 2.310  20.844 1.020 10.208 1.589 0.569  0.865 51.651 0.216   
H 0.493  10.511 0.323 26.126 0.140 3.142  0.041 57.800 0.003   
N 12.222 0.006  3.135 9.893  2.014 28.997 1.167 0.583  -11.538 
O 3.049  13.277 2.287 5.701  1.546 0.324  0.867 32.909 0.251   
S 6.905  1.468  5.203 22.215 1.438 0.254  1.586 56.172 1.049   
# 
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   . ASN A 1 5   ? -58.474 -15.530 35.835  1.000 219.337 ? 334 ASN AAA N   1 
ATOM   2     C CA  . ASN A 1 5   ? -59.164 -16.825 36.153  1.000 211.676 ? 334 ASN AAA CA  1 
ATOM   3     C C   . ASN A 1 5   ? -58.170 -17.982 35.952  1.000 206.182 ? 334 ASN AAA C   1 
ATOM   4     O O   . ASN A 1 5   ? -58.339 -18.750 34.992  1.000 205.134 ? 334 ASN AAA O   1 
ATOM   5     C CB  . ASN A 1 5   ? -60.478 -16.987 35.372  1.000 213.405 ? 334 ASN AAA CB  1 
ATOM   6     C CG  . ASN A 1 5   ? -60.525 -16.209 34.070  1.000 221.033 ? 334 ASN AAA CG  1 
ATOM   7     O OD1 . ASN A 1 5   ? -59.562 -16.212 33.305  1.000 222.564 ? 334 ASN AAA OD1 1 
ATOM   8     N ND2 . ASN A 1 5   ? -61.635 -15.531 33.812  1.000 225.488 ? 334 ASN AAA ND2 1 
ATOM   9     N N   . LEU A 1 6   ? -57.174 -18.084 36.845  1.000 203.438 ? 335 LEU AAA N   1 
ATOM   10    C CA  . LEU A 1 6   ? -56.146 -19.164 36.907  1.000 199.560 ? 335 LEU AAA CA  1 
ATOM   11    C C   . LEU A 1 6   ? -56.426 -20.054 38.128  1.000 194.931 ? 335 LEU AAA C   1 
ATOM   12    O O   . LEU A 1 6   ? -56.468 -19.506 39.247  1.000 196.595 ? 335 LEU AAA O   1 
ATOM   13    C CB  . LEU A 1 6   ? -54.760 -18.511 36.988  1.000 202.732 ? 335 LEU AAA CB  1 
ATOM   14    C CG  . LEU A 1 6   ? -53.617 -19.375 37.536  1.000 198.559 ? 335 LEU AAA CG  1 
ATOM   15    C CD1 . LEU A 1 6   ? -53.425 -20.644 36.717  1.000 194.752 ? 335 LEU AAA CD1 1 
ATOM   16    C CD2 . LEU A 1 6   ? -52.318 -18.581 37.588  1.000 202.724 ? 335 LEU AAA CD2 1 
ATOM   17    N N   . CYS A 1 7   ? -56.580 -21.371 37.926  1.000 191.594 ? 336 CYS AAA N   1 
ATOM   18    C CA  . CYS A 1 7   ? -57.036 -22.351 38.957  1.000 186.297 ? 336 CYS AAA CA  1 
ATOM   19    C C   . CYS A 1 7   ? -56.173 -22.229 40.211  1.000 183.018 ? 336 CYS AAA C   1 
ATOM   20    O O   . CYS A 1 7   ? -54.976 -22.516 40.181  1.000 182.076 ? 336 CYS AAA O   1 
ATOM   21    C CB  . CYS A 1 7   ? -56.990 -23.795 38.467  1.000 183.759 ? 336 CYS AAA CB  1 
ATOM   22    S SG  . CYS A 1 7   ? -58.166 -24.207 37.146  1.000 187.634 ? 336 CYS AAA SG  1 
ATOM   23    N N   . PRO A 1 8   ? -56.759 -21.792 41.347  1.000 181.502 ? 337 PRO AAA N   1 
ATOM   24    C CA  . PRO A 1 8   ? -56.002 -21.573 42.574  1.000 181.220 ? 337 PRO AAA CA  1 
ATOM   25    C C   . PRO A 1 8   ? -55.814 -22.885 43.339  1.000 175.454 ? 337 PRO AAA C   1 
ATOM   26    O O   . PRO A 1 8   ? -56.538 -23.130 44.275  1.000 173.837 ? 337 PRO AAA O   1 
ATOM   27    C CB  . PRO A 1 8   ? -56.885 -20.579 43.338  1.000 184.261 ? 337 PRO AAA CB  1 
ATOM   28    C CG  . PRO A 1 8   ? -58.292 -20.980 42.949  1.000 182.504 ? 337 PRO AAA CG  1 
ATOM   29    C CD  . PRO A 1 8   ? -58.186 -21.478 41.519  1.000 182.047 ? 337 PRO AAA CD  1 
ATOM   30    N N   . PHE A 1 9   ? -54.862 -23.701 42.896  1.000 174.224 ? 338 PHE AAA N   1 
ATOM   31    C CA  . PHE A 1 9   ? -54.293 -24.819 43.686  1.000 172.485 ? 338 PHE AAA CA  1 
ATOM   32    C C   . PHE A 1 9   ? -53.387 -24.220 44.769  1.000 175.522 ? 338 PHE AAA C   1 
ATOM   33    O O   . PHE A 1 9   ? -53.145 -24.887 45.793  1.000 173.044 ? 338 PHE AAA O   1 
ATOM   34    C CB  . PHE A 1 9   ? -53.561 -25.798 42.767  1.000 172.048 ? 338 PHE AAA CB  1 
ATOM   35    C CG  . PHE A 1 9   ? -54.446 -26.481 41.755  1.000 170.841 ? 338 PHE AAA CG  1 
ATOM   36    C CD1 . PHE A 1 9   ? -55.587 -27.157 42.157  1.000 167.349 ? 338 PHE AAA CD1 1 
ATOM   37    C CD2 . PHE A 1 9   ? -54.132 -26.462 40.404  1.000 173.341 ? 338 PHE AAA CD2 1 
ATOM   38    C CE1 . PHE A 1 9   ? -56.398 -27.794 41.232  1.000 166.310 ? 338 PHE AAA CE1 1 
ATOM   39    C CE2 . PHE A 1 9   ? -54.948 -27.096 39.480  1.000 172.423 ? 338 PHE AAA CE2 1 
ATOM   40    C CZ  . PHE A 1 9   ? -56.080 -27.761 39.895  1.000 169.054 ? 338 PHE AAA CZ  1 
ATOM   41    N N   . GLY A 1 10  ? -52.916 -22.988 44.541  1.000 181.834 ? 339 GLY AAA N   1 
ATOM   42    C CA  . GLY A 1 10  ? -52.120 -22.187 45.491  1.000 186.657 ? 339 GLY AAA CA  1 
ATOM   43    C C   . GLY A 1 10  ? -52.692 -22.218 46.900  1.000 186.142 ? 339 GLY AAA C   1 
ATOM   44    O O   . GLY A 1 10  ? -51.905 -22.419 47.835  1.000 188.017 ? 339 GLY AAA O   1 
ATOM   45    N N   . GLU A 1 11  ? -54.013 -22.050 47.048  1.000 184.332 ? 340 GLU AAA N   1 
ATOM   46    C CA  . GLU A 1 11  ? -54.708 -21.979 48.365  1.000 183.714 ? 340 GLU AAA CA  1 
ATOM   47    C C   . GLU A 1 11  ? -55.257 -23.364 48.754  1.000 176.939 ? 340 GLU AAA C   1 
ATOM   48    O O   . GLU A 1 11  ? -56.231 -23.420 49.533  1.000 176.213 ? 340 GLU AAA O   1 
ATOM   49    C CB  . GLU A 1 11  ? -55.788 -20.889 48.335  1.000 187.567 ? 340 GLU AAA CB  1 
ATOM   50    C CG  . GLU A 1 11  ? -56.965 -21.175 47.413  1.000 185.894 ? 340 GLU AAA CG  1 
ATOM   51    C CD  . GLU A 1 11  ? -58.026 -20.083 47.365  1.000 189.890 ? 340 GLU AAA CD  1 
ATOM   52    O OE1 . GLU A 1 11  ? -59.155 -20.320 47.856  1.000 188.858 ? 340 GLU AAA OE1 1 
ATOM   53    O OE2 . GLU A 1 11  ? -57.729 -18.998 46.824  1.000 194.366 ? 340 GLU AAA OE2 1 
ATOM   54    N N   . VAL A 1 12  ? -54.642 -24.442 48.255  1.000 171.765 ? 341 VAL AAA N   1 
ATOM   55    C CA  . VAL A 1 12  ? -54.958 -25.854 48.627  1.000 166.536 ? 341 VAL AAA CA  1 
ATOM   56    C C   . VAL A 1 12  ? -53.672 -26.516 49.124  1.000 166.805 ? 341 VAL AAA C   1 
ATOM   57    O O   . VAL A 1 12  ? -53.651 -26.947 50.279  1.000 166.920 ? 341 VAL AAA O   1 
ATOM   58    C CB  . VAL A 1 12  ? -55.572 -26.636 47.449  1.000 161.277 ? 341 VAL AAA CB  1 
ATOM   59    C CG1 . VAL A 1 12  ? -55.812 -28.100 47.790  1.000 156.160 ? 341 VAL AAA CG1 1 
ATOM   60    C CG2 . VAL A 1 12  ? -56.858 -25.990 46.959  1.000 162.178 ? 341 VAL AAA CG2 1 
ATOM   61    N N   . PHE A 1 13  ? -52.649 -26.580 48.270  1.000 168.736 ? 342 PHE AAA N   1 
ATOM   62    C CA  . PHE A 1 13  ? -51.342 -27.226 48.551  1.000 171.787 ? 342 PHE AAA CA  1 
ATOM   63    C C   . PHE A 1 13  ? -50.573 -26.397 49.583  1.000 180.261 ? 342 PHE AAA C   1 
ATOM   64    O O   . PHE A 1 13  ? -50.221 -26.924 50.655  1.000 181.082 ? 342 PHE AAA O   1 
ATOM   65    C CB  . PHE A 1 13  ? -50.530 -27.380 47.263  1.000 170.628 ? 342 PHE AAA CB  1 
ATOM   66    C CG  . PHE A 1 13  ? -51.094 -28.396 46.306  1.000 164.958 ? 342 PHE AAA CG  1 
ATOM   67    C CD1 . PHE A 1 13  ? -52.154 -28.077 45.472  1.000 163.684 ? 342 PHE AAA CD1 1 
ATOM   68    C CD2 . PHE A 1 13  ? -50.574 -29.677 46.249  1.000 162.065 ? 342 PHE AAA CD2 1 
ATOM   69    C CE1 . PHE A 1 13  ? -52.680 -29.019 44.602  1.000 160.341 ? 342 PHE AAA CE1 1 
ATOM   70    C CE2 . PHE A 1 13  ? -51.093 -30.616 45.372  1.000 158.690 ? 342 PHE AAA CE2 1 
ATOM   71    C CZ  . PHE A 1 13  ? -52.145 -30.285 44.549  1.000 157.943 ? 342 PHE AAA CZ  1 
ATOM   72    N N   . ASN A 1 14  ? -50.342 -25.125 49.255  1.000 188.562 ? 343 ASN AAA N   1 
ATOM   73    C CA  . ASN A 1 14  ? -49.589 -24.155 50.093  1.000 196.410 ? 343 ASN AAA CA  1 
ATOM   74    C C   . ASN A 1 14  ? -50.472 -23.650 51.244  1.000 194.152 ? 343 ASN AAA C   1 
ATOM   75    O O   . ASN A 1 14  ? -49.959 -22.866 52.065  1.000 198.836 ? 343 ASN AAA O   1 
ATOM   76    C CB  . ASN A 1 14  ? -49.054 -22.996 49.247  1.000 205.594 ? 343 ASN AAA CB  1 
ATOM   77    C CG  . ASN A 1 14  ? -47.777 -23.345 48.517  1.000 211.976 ? 343 ASN AAA CG  1 
ATOM   78    O OD1 . ASN A 1 14  ? -46.749 -23.571 49.147  1.000 211.911 ? 343 ASN AAA OD1 1 
ATOM   79    N ND2 . ASN A 1 14  ? -47.827 -23.388 47.198  1.000 225.508 ? 343 ASN AAA ND2 1 
ATOM   80    N N   . ALA A 1 15  ? -51.744 -24.063 51.305  1.000 185.915 ? 344 ALA AAA N   1 
ATOM   81    C CA  . ALA A 1 15  ? -52.703 -23.675 52.368  1.000 184.704 ? 344 ALA AAA CA  1 
ATOM   82    C C   . ALA A 1 15  ? -52.041 -23.861 53.741  1.000 185.847 ? 344 ALA AAA C   1 
ATOM   83    O O   . ALA A 1 15  ? -51.466 -24.942 53.965  1.000 182.734 ? 344 ALA AAA O   1 
ATOM   84    C CB  . ALA A 1 15  ? -53.971 -24.486 52.240  1.000 180.310 ? 344 ALA AAA CB  1 
ATOM   85    N N   . THR A 1 16  ? -52.121 -22.843 54.609  1.000 189.847 ? 345 THR AAA N   1 
ATOM   86    C CA  . THR A 1 16  ? -51.405 -22.746 55.914  1.000 193.732 ? 345 THR AAA CA  1 
ATOM   87    C C   . THR A 1 16  ? -51.743 -23.951 56.803  1.000 191.182 ? 345 THR AAA C   1 
ATOM   88    O O   . THR A 1 16  ? -50.813 -24.659 57.190  1.000 188.909 ? 345 THR AAA O   1 
ATOM   89    C CB  . THR A 1 16  ? -51.710 -21.413 56.616  1.000 199.286 ? 345 THR AAA CB  1 
ATOM   90    O OG1 . THR A 1 16  ? -53.077 -21.066 56.385  1.000 196.673 ? 345 THR AAA OG1 1 
ATOM   91    C CG2 . THR A 1 16  ? -50.826 -20.282 56.137  1.000 203.928 ? 345 THR AAA CG2 1 
ATOM   92    N N   . ARG A 1 17  ? -53.023 -24.167 57.114  1.000 191.919 ? 346 ARG AAA N   1 
ATOM   93    C CA  . ARG A 1 17  ? -53.503 -25.325 57.919  1.000 193.080 ? 346 ARG AAA CA  1 
ATOM   94    C C   . ARG A 1 17  ? -54.241 -26.312 57.001  1.000 188.959 ? 346 ARG AAA C   1 
ATOM   95    O O   . ARG A 1 17  ? -54.844 -25.859 56.012  1.000 188.842 ? 346 ARG AAA O   1 
ATOM   96    C CB  . ARG A 1 17  ? -54.409 -24.839 59.058  1.000 197.023 ? 346 ARG AAA CB  1 
ATOM   97    C CG  . ARG A 1 17  ? -54.563 -25.851 60.184  1.000 198.939 ? 346 ARG AAA CG  1 
ATOM   98    C CD  . ARG A 1 17  ? -55.596 -25.443 61.216  1.000 202.691 ? 346 ARG AAA CD  1 
ATOM   99    N NE  . ARG A 1 17  ? -55.215 -24.247 61.963  1.000 209.572 ? 346 ARG AAA NE  1 
ATOM   100   C CZ  . ARG A 1 17  ? -55.813 -23.054 61.894  1.000 211.649 ? 346 ARG AAA CZ  1 
ATOM   101   N NH1 . ARG A 1 17  ? -56.853 -22.852 61.099  1.000 208.029 ? 346 ARG AAA NH1 1 
ATOM   102   N NH2 . ARG A 1 17  ? -55.369 -22.055 62.639  1.000 217.724 ? 346 ARG AAA NH2 1 
ATOM   103   N N   . PHE A 1 18  ? -54.208 -27.609 57.325  1.000 187.093 ? 347 PHE AAA N   1 
ATOM   104   C CA  . PHE A 1 18  ? -54.939 -28.696 56.618  1.000 181.632 ? 347 PHE AAA CA  1 
ATOM   105   C C   . PHE A 1 18  ? -56.032 -29.257 57.527  1.000 180.307 ? 347 PHE AAA C   1 
ATOM   106   O O   . PHE A 1 18  ? -56.047 -28.906 58.722  1.000 186.435 ? 347 PHE AAA O   1 
ATOM   107   C CB  . PHE A 1 18  ? -53.982 -29.816 56.214  1.000 182.510 ? 347 PHE AAA CB  1 
ATOM   108   C CG  . PHE A 1 18  ? -53.530 -29.765 54.780  1.000 182.207 ? 347 PHE AAA CG  1 
ATOM   109   C CD1 . PHE A 1 18  ? -52.778 -28.697 54.314  1.000 186.312 ? 347 PHE AAA CD1 1 
ATOM   110   C CD2 . PHE A 1 18  ? -53.856 -30.786 53.900  1.000 178.851 ? 347 PHE AAA CD2 1 
ATOM   111   C CE1 . PHE A 1 18  ? -52.355 -28.658 52.995  1.000 185.105 ? 347 PHE AAA CE1 1 
ATOM   112   C CE2 . PHE A 1 18  ? -53.431 -30.746 52.582  1.000 177.150 ? 347 PHE AAA CE2 1 
ATOM   113   C CZ  . PHE A 1 18  ? -52.687 -29.680 52.131  1.000 180.445 ? 347 PHE AAA CZ  1 
ATOM   114   N N   . ALA A 1 19  ? -56.894 -30.115 56.973  1.000 174.405 ? 348 ALA AAA N   1 
ATOM   115   C CA  . ALA A 1 19  ? -58.045 -30.738 57.669  1.000 173.141 ? 348 ALA AAA CA  1 
ATOM   116   C C   . ALA A 1 19  ? -57.625 -32.084 58.275  1.000 171.602 ? 348 ALA AAA C   1 
ATOM   117   O O   . ALA A 1 19  ? -56.578 -32.634 57.860  1.000 168.982 ? 348 ALA AAA O   1 
ATOM   118   C CB  . ALA A 1 19  ? -59.199 -30.901 56.707  1.000 170.084 ? 348 ALA AAA CB  1 
ATOM   119   N N   . SER A 1 20  ? -58.405 -32.574 59.246  1.000 171.526 ? 349 SER AAA N   1 
ATOM   120   C CA  . SER A 1 20  ? -58.282 -33.935 59.833  1.000 170.866 ? 349 SER AAA CA  1 
ATOM   121   C C   . SER A 1 20  ? -58.910 -34.928 58.854  1.000 162.738 ? 349 SER AAA C   1 
ATOM   122   O O   . SER A 1 20  ? -59.939 -34.577 58.236  1.000 158.787 ? 349 SER AAA O   1 
ATOM   123   C CB  . SER A 1 20  ? -58.923 -34.033 61.201  1.000 177.198 ? 349 SER AAA CB  1 
ATOM   124   O OG  . SER A 1 20  ? -58.258 -33.210 62.153  1.000 183.423 ? 349 SER AAA OG  1 
ATOM   125   N N   . VAL A 1 21  ? -58.316 -36.116 58.730  1.000 158.520 ? 350 VAL AAA N   1 
ATOM   126   C CA  . VAL A 1 21  ? -58.626 -37.089 57.642  1.000 152.514 ? 350 VAL AAA CA  1 
ATOM   127   C C   . VAL A 1 21  ? -60.141 -37.300 57.521  1.000 149.056 ? 350 VAL AAA C   1 
ATOM   128   O O   . VAL A 1 21  ? -60.645 -37.114 56.419  1.000 146.160 ? 350 VAL AAA O   1 
ATOM   129   C CB  . VAL A 1 21  ? -57.875 -38.419 57.822  1.000 153.915 ? 350 VAL AAA CB  1 
ATOM   130   C CG1 . VAL A 1 21  ? -58.235 -39.120 59.115  1.000 158.673 ? 350 VAL AAA CG1 1 
ATOM   131   C CG2 . VAL A 1 21  ? -58.104 -39.342 56.640  1.000 151.018 ? 350 VAL AAA CG2 1 
ATOM   132   N N   . TYR A 1 22  ? -60.837 -37.670 58.598  1.000 150.322 ? 351 TYR AAA N   1 
ATOM   133   C CA  . TYR A 1 22  ? -62.288 -38.024 58.599  1.000 149.638 ? 351 TYR AAA CA  1 
ATOM   134   C C   . TYR A 1 22  ? -63.149 -36.828 58.177  1.000 147.574 ? 351 TYR AAA C   1 
ATOM   135   O O   . TYR A 1 22  ? -64.292 -37.086 57.744  1.000 145.154 ? 351 TYR AAA O   1 
ATOM   136   C CB  . TYR A 1 22  ? -62.766 -38.459 59.988  1.000 153.806 ? 351 TYR AAA CB  1 
ATOM   137   C CG  . TYR A 1 22  ? -62.903 -37.319 60.970  1.000 155.321 ? 351 TYR AAA CG  1 
ATOM   138   C CD1 . TYR A 1 22  ? -61.778 -36.719 61.517  1.000 156.750 ? 351 TYR AAA CD1 1 
ATOM   139   C CD2 . TYR A 1 22  ? -64.143 -36.819 61.335  1.000 155.178 ? 351 TYR AAA CD2 1 
ATOM   140   C CE1 . TYR A 1 22  ? -61.874 -35.659 62.403  1.000 158.654 ? 351 TYR AAA CE1 1 
ATOM   141   C CE2 . TYR A 1 22  ? -64.260 -35.758 62.219  1.000 157.344 ? 351 TYR AAA CE2 1 
ATOM   142   C CZ  . TYR A 1 22  ? -63.120 -35.178 62.753  1.000 158.813 ? 351 TYR AAA CZ  1 
ATOM   143   O OH  . TYR A 1 22  ? -63.188 -34.134 63.625  1.000 161.617 ? 351 TYR AAA OH  1 
ATOM   144   N N   . ALA A 1 23  ? -62.633 -35.601 58.359  1.000 148.184 ? 352 ALA AAA N   1 
ATOM   145   C CA  . ALA A 1 23  ? -63.293 -34.301 58.073  1.000 148.969 ? 352 ALA AAA CA  1 
ATOM   146   C C   . ALA A 1 23  ? -62.641 -33.632 56.860  1.000 147.187 ? 352 ALA AAA C   1 
ATOM   147   O O   . ALA A 1 23  ? -62.529 -32.383 56.856  1.000 147.669 ? 352 ALA AAA O   1 
ATOM   148   C CB  . ALA A 1 23  ? -63.193 -33.397 59.273  1.000 152.332 ? 352 ALA AAA CB  1 
ATOM   149   N N   . TRP A 1 24  ? -62.255 -34.441 55.867  1.000 145.563 ? 353 TRP AAA N   1 
ATOM   150   C CA  . TRP A 1 24  ? -61.471 -34.033 54.673  1.000 143.439 ? 353 TRP AAA CA  1 
ATOM   151   C C   . TRP A 1 24  ? -62.166 -32.885 53.945  1.000 143.034 ? 353 TRP AAA C   1 
ATOM   152   O O   . TRP A 1 24  ? -63.408 -32.846 53.926  1.000 142.899 ? 353 TRP AAA O   1 
ATOM   153   C CB  . TRP A 1 24  ? -61.212 -35.223 53.743  1.000 142.024 ? 353 TRP AAA CB  1 
ATOM   154   C CG  . TRP A 1 24  ? -62.413 -36.046 53.389  1.000 141.115 ? 353 TRP AAA CG  1 
ATOM   155   C CD1 . TRP A 1 24  ? -62.949 -37.078 54.100  1.000 142.943 ? 353 TRP AAA CD1 1 
ATOM   156   C CD2 . TRP A 1 24  ? -63.197 -35.939 52.195  1.000 139.449 ? 353 TRP AAA CD2 1 
ATOM   157   N NE1 . TRP A 1 24  ? -64.024 -37.606 53.440  1.000 142.862 ? 353 TRP AAA NE1 1 
ATOM   158   C CE2 . TRP A 1 24  ? -64.197 -36.931 52.265  1.000 140.829 ? 353 TRP AAA CE2 1 
ATOM   159   C CE3 . TRP A 1 24  ? -63.149 -35.101 51.081  1.000 139.068 ? 353 TRP AAA CE3 1 
ATOM   160   C CZ2 . TRP A 1 24  ? -65.145 -37.105 51.261  1.000 141.812 ? 353 TRP AAA CZ2 1 
ATOM   161   C CZ3 . TRP A 1 24  ? -64.088 -35.273 50.090  1.000 140.914 ? 353 TRP AAA CZ3 1 
ATOM   162   C CH2 . TRP A 1 24  ? -65.076 -36.254 50.184  1.000 141.649 ? 353 TRP AAA CH2 1 
ATOM   163   N N   . ASN A 1 25  ? -61.360 -31.999 53.360  1.000 143.677 ? 354 ASN AAA N   1 
ATOM   164   C CA  . ASN A 1 25  ? -61.793 -30.694 52.807  1.000 145.490 ? 354 ASN AAA CA  1 
ATOM   165   C C   . ASN A 1 25  ? -61.804 -30.792 51.278  1.000 144.111 ? 354 ASN AAA C   1 
ATOM   166   O O   . ASN A 1 25  ? -60.733 -31.031 50.687  1.000 142.318 ? 354 ASN AAA O   1 
ATOM   167   C CB  . ASN A 1 25  ? -60.888 -29.576 53.324  1.000 148.061 ? 354 ASN AAA CB  1 
ATOM   168   C CG  . ASN A 1 25  ? -61.665 -28.418 53.906  1.000 151.661 ? 354 ASN AAA CG  1 
ATOM   169   O OD1 . ASN A 1 25  ? -62.788 -28.139 53.482  1.000 151.815 ? 354 ASN AAA OD1 1 
ATOM   170   N ND2 . ASN A 1 25  ? -61.074 -27.753 54.884  1.000 155.154 ? 354 ASN AAA ND2 1 
ATOM   171   N N   . ARG A 1 26  ? -62.983 -30.641 50.669  1.000 145.225 ? 355 ARG AAA N   1 
ATOM   172   C CA  . ARG A 1 26  ? -63.163 -30.663 49.195  1.000 144.620 ? 355 ARG AAA CA  1 
ATOM   173   C C   . ARG A 1 26  ? -63.176 -29.222 48.688  1.000 146.905 ? 355 ARG AAA C   1 
ATOM   174   O O   . ARG A 1 26  ? -63.881 -28.385 49.295  1.000 148.686 ? 355 ARG AAA O   1 
ATOM   175   C CB  . ARG A 1 26  ? -64.463 -31.363 48.789  1.000 145.016 ? 355 ARG AAA CB  1 
ATOM   176   C CG  . ARG A 1 26  ? -64.773 -31.271 47.301  1.000 144.706 ? 355 ARG AAA CG  1 
ATOM   177   C CD  . ARG A 1 26  ? -65.647 -32.407 46.789  1.000 144.204 ? 355 ARG AAA CD  1 
ATOM   178   N NE  . ARG A 1 26  ? -64.927 -33.676 46.742  1.000 141.686 ? 355 ARG AAA NE  1 
ATOM   179   C CZ  . ARG A 1 26  ? -65.310 -34.771 46.078  1.000 141.730 ? 355 ARG AAA CZ  1 
ATOM   180   N NH1 . ARG A 1 26  ? -66.430 -34.784 45.371  1.000 144.098 ? 355 ARG AAA NH1 1 
ATOM   181   N NH2 . ARG A 1 26  ? -64.557 -35.859 46.123  1.000 139.895 ? 355 ARG AAA NH2 1 
ATOM   182   N N   . LYS A 1 27  ? -62.431 -28.965 47.611  1.000 146.982 ? 356 LYS AAA N   1 
ATOM   183   C CA  . LYS A 1 27  ? -62.445 -27.684 46.866  1.000 150.373 ? 356 LYS AAA CA  1 
ATOM   184   C C   . LYS A 1 27  ? -62.905 -27.966 45.438  1.000 150.849 ? 356 LYS AAA C   1 
ATOM   185   O O   . LYS A 1 27  ? -62.257 -28.783 44.758  1.000 146.611 ? 356 LYS AAA O   1 
ATOM   186   C CB  . LYS A 1 27  ? -61.065 -27.026 46.858  1.000 151.960 ? 356 LYS AAA CB  1 
ATOM   187   C CG  . LYS A 1 27  ? -61.085 -25.538 46.541  1.000 156.264 ? 356 LYS AAA CG  1 
ATOM   188   C CD  . LYS A 1 27  ? -61.268 -24.677 47.774  1.000 159.479 ? 356 LYS AAA CD  1 
ATOM   189   C CE  . LYS A 1 27  ? -61.391 -23.202 47.462  1.000 163.858 ? 356 LYS AAA CE  1 
ATOM   190   N NZ  . LYS A 1 27  ? -62.737 -22.859 46.947  1.000 165.322 ? 356 LYS AAA NZ  1 
ATOM   191   N N   . ARG A 1 28  ? -63.997 -27.322 45.027  1.000 155.926 ? 357 ARG AAA N   1 
ATOM   192   C CA  . ARG A 1 28  ? -64.585 -27.467 43.675  1.000 159.983 ? 357 ARG AAA CA  1 
ATOM   193   C C   . ARG A 1 28  ? -63.886 -26.487 42.734  1.000 163.559 ? 357 ARG AAA C   1 
ATOM   194   O O   . ARG A 1 28  ? -64.261 -25.298 42.741  1.000 167.538 ? 357 ARG AAA O   1 
ATOM   195   C CB  . ARG A 1 28  ? -66.092 -27.205 43.718  1.000 163.979 ? 357 ARG AAA CB  1 
ATOM   196   C CG  . ARG A 1 28  ? -66.811 -27.508 42.412  1.000 167.402 ? 357 ARG AAA CG  1 
ATOM   197   C CD  . ARG A 1 28  ? -68.252 -27.906 42.674  1.000 170.964 ? 357 ARG AAA CD  1 
ATOM   198   N NE  . ARG A 1 28  ? -68.896 -28.609 41.573  1.000 173.983 ? 357 ARG AAA NE  1 
ATOM   199   C CZ  . ARG A 1 28  ? -69.366 -28.030 40.470  1.000 180.797 ? 357 ARG AAA CZ  1 
ATOM   200   N NH1 . ARG A 1 28  ? -69.242 -26.724 40.287  1.000 184.872 ? 357 ARG AAA NH1 1 
ATOM   201   N NH2 . ARG A 1 28  ? -69.952 -28.767 39.542  1.000 183.567 ? 357 ARG AAA NH2 1 
ATOM   202   N N   . ILE A 1 29  ? -62.911 -26.972 41.964  1.000 163.058 ? 358 ILE AAA N   1 
ATOM   203   C CA  . ILE A 1 29  ? -62.192 -26.169 40.936  1.000 165.502 ? 358 ILE AAA CA  1 
ATOM   204   C C   . ILE A 1 29  ? -63.066 -26.148 39.680  1.000 168.101 ? 358 ILE AAA C   1 
ATOM   205   O O   . ILE A 1 29  ? -63.428 -27.244 39.188  1.000 165.591 ? 358 ILE AAA O   1 
ATOM   206   C CB  . ILE A 1 29  ? -60.786 -26.733 40.652  1.000 164.298 ? 358 ILE AAA CB  1 
ATOM   207   C CG1 . ILE A 1 29  ? -59.971 -26.946 41.929  1.000 162.859 ? 358 ILE AAA CG1 1 
ATOM   208   C CG2 . ILE A 1 29  ? -60.043 -25.841 39.675  1.000 168.199 ? 358 ILE AAA CG2 1 
ATOM   209   C CD1 . ILE A 1 29  ? -59.509 -25.668 42.590  1.000 166.450 ? 358 ILE AAA CD1 1 
ATOM   210   N N   . SER A 1 30  ? -63.407 -24.945 39.209  1.000 173.208 ? 359 SER AAA N   1 
ATOM   211   C CA  . SER A 1 30  ? -64.275 -24.693 38.029  1.000 178.740 ? 359 SER AAA CA  1 
ATOM   212   C C   . SER A 1 30  ? -63.950 -23.319 37.431  1.000 183.576 ? 359 SER AAA C   1 
ATOM   213   O O   . SER A 1 30  ? -63.395 -22.471 38.155  1.000 183.771 ? 359 SER AAA O   1 
ATOM   214   C CB  . SER A 1 30  ? -65.737 -24.798 38.395  1.000 181.056 ? 359 SER AAA CB  1 
ATOM   215   O OG  . SER A 1 30  ? -66.036 -26.066 38.970  1.000 177.745 ? 359 SER AAA OG  1 
ATOM   216   N N   . ASN A 1 31  ? -64.288 -23.133 36.152  1.000 187.612 ? 360 ASN AAA N   1 
ATOM   217   C CA  . ASN A 1 31  ? -64.100 -21.885 35.360  1.000 194.028 ? 360 ASN AAA CA  1 
ATOM   218   C C   . ASN A 1 31  ? -62.731 -21.267 35.665  1.000 194.566 ? 360 ASN AAA C   1 
ATOM   219   O O   . ASN A 1 31  ? -62.674 -20.140 36.204  1.000 195.646 ? 360 ASN AAA O   1 
ATOM   220   C CB  . ASN A 1 31  ? -65.261 -20.915 35.573  1.000 197.863 ? 360 ASN AAA CB  1 
ATOM   221   C CG  . ASN A 1 31  ? -66.568 -21.510 35.101  1.000 199.210 ? 360 ASN AAA CG  1 
ATOM   222   O OD1 . ASN A 1 31  ? -66.904 -22.631 35.477  1.000 194.704 ? 360 ASN AAA OD1 1 
ATOM   223   N ND2 . ASN A 1 31  ? -67.292 -20.784 34.262  1.000 205.364 ? 360 ASN AAA ND2 1 
ATOM   224   N N   . CYS A 1 32  ? -61.673 -21.993 35.302  1.000 194.030 ? 361 CYS AAA N   1 
ATOM   225   C CA  . CYS A 1 32  ? -60.255 -21.561 35.395  1.000 195.748 ? 361 CYS AAA CA  1 
ATOM   226   C C   . CYS A 1 32  ? -59.389 -22.477 34.521  1.000 193.573 ? 361 CYS AAA C   1 
ATOM   227   O O   . CYS A 1 32  ? -59.804 -23.641 34.274  1.000 190.608 ? 361 CYS AAA O   1 
ATOM   228   C CB  . CYS A 1 32  ? -59.770 -21.611 36.838  1.000 193.829 ? 361 CYS AAA CB  1 
ATOM   229   S SG  . CYS A 1 32  ? -59.927 -23.255 37.589  1.000 189.042 ? 361 CYS AAA SG  1 
ATOM   230   N N   . VAL A 1 33  ? -58.232 -21.979 34.080  1.000 194.778 ? 362 VAL AAA N   1 
ATOM   231   C CA  . VAL A 1 33  ? -57.187 -22.788 33.386  1.000 191.773 ? 362 VAL AAA CA  1 
ATOM   232   C C   . VAL A 1 33  ? -56.100 -23.123 34.405  1.000 185.848 ? 362 VAL AAA C   1 
ATOM   233   O O   . VAL A 1 33  ? -55.711 -22.226 35.166  1.000 186.426 ? 362 VAL AAA O   1 
ATOM   234   C CB  . VAL A 1 33  ? -56.599 -22.048 32.173  1.000 199.202 ? 362 VAL AAA CB  1 
ATOM   235   C CG1 . VAL A 1 33  ? -55.408 -22.783 31.579  1.000 198.523 ? 362 VAL AAA CG1 1 
ATOM   236   C CG2 . VAL A 1 33  ? -57.653 -21.792 31.111  1.000 204.792 ? 362 VAL AAA CG2 1 
ATOM   237   N N   . ALA A 1 34  ? -55.643 -24.373 34.410  1.000 180.475 ? 363 ALA AAA N   1 
ATOM   238   C CA  . ALA A 1 34  ? -54.559 -24.875 35.280  1.000 176.965 ? 363 ALA AAA CA  1 
ATOM   239   C C   . ALA A 1 34  ? -53.436 -25.411 34.397  1.000 176.626 ? 363 ALA AAA C   1 
ATOM   240   O O   . ALA A 1 34  ? -53.706 -26.350 33.625  1.000 175.786 ? 363 ALA AAA O   1 
ATOM   241   C CB  . ALA A 1 34  ? -55.085 -25.960 36.187  1.000 172.060 ? 363 ALA AAA CB  1 
ATOM   242   N N   . ASP A 1 35  ? -52.237 -24.835 34.491  1.000 178.527 ? 364 ASP AAA N   1 
ATOM   243   C CA  . ASP A 1 35  ? -51.008 -25.540 34.054  1.000 178.249 ? 364 ASP AAA CA  1 
ATOM   244   C C   . ASP A 1 35  ? -50.704 -26.552 35.155  1.000 170.817 ? 364 ASP AAA C   1 
ATOM   245   O O   . ASP A 1 35  ? -50.196 -26.140 36.209  1.000 171.124 ? 364 ASP AAA O   1 
ATOM   246   C CB  . ASP A 1 35  ? -49.830 -24.603 33.764  1.000 185.240 ? 364 ASP AAA CB  1 
ATOM   247   C CG  . ASP A 1 35  ? -48.786 -25.227 32.844  1.000 187.423 ? 364 ASP AAA CG  1 
ATOM   248   O OD1 . ASP A 1 35  ? -48.723 -26.483 32.786  1.000 183.742 ? 364 ASP AAA OD1 1 
ATOM   249   O OD2 . ASP A 1 35  ? -48.053 -24.459 32.173  1.000 193.289 ? 364 ASP AAA OD2 1 
ATOM   250   N N   . TYR A 1 36  ? -51.096 -27.808 34.944  1.000 164.952 ? 365 TYR AAA N   1 
ATOM   251   C CA  . TYR A 1 36  ? -50.890 -28.902 35.924  1.000 158.807 ? 365 TYR AAA CA  1 
ATOM   252   C C   . TYR A 1 36  ? -49.385 -29.190 35.988  1.000 158.056 ? 365 TYR AAA C   1 
ATOM   253   O O   . TYR A 1 36  ? -48.923 -29.679 37.032  1.000 154.674 ? 365 TYR AAA O   1 
ATOM   254   C CB  . TYR A 1 36  ? -51.732 -30.132 35.577  1.000 155.489 ? 365 TYR AAA CB  1 
ATOM   255   C CG  . TYR A 1 36  ? -53.229 -29.926 35.526  1.000 156.541 ? 365 TYR AAA CG  1 
ATOM   256   C CD1 . TYR A 1 36  ? -53.849 -29.539 34.346  1.000 161.938 ? 365 TYR AAA CD1 1 
ATOM   257   C CD2 . TYR A 1 36  ? -54.041 -30.176 36.625  1.000 153.090 ? 365 TYR AAA CD2 1 
ATOM   258   C CE1 . TYR A 1 36  ? -55.225 -29.379 34.262  1.000 162.911 ? 365 TYR AAA CE1 1 
ATOM   259   C CE2 . TYR A 1 36  ? -55.418 -30.013 36.562  1.000 154.683 ? 365 TYR AAA CE2 1 
ATOM   260   C CZ  . TYR A 1 36  ? -56.015 -29.613 35.374  1.000 159.391 ? 365 TYR AAA CZ  1 
ATOM   261   O OH  . TYR A 1 36  ? -57.366 -29.443 35.267  1.000 159.516 ? 365 TYR AAA OH  1 
ATOM   262   N N   . SER A 1 37  ? -48.636 -28.843 34.932  1.000 161.541 ? 366 SER AAA N   1 
ATOM   263   C CA  . SER A 1 37  ? -47.148 -28.909 34.905  1.000 163.788 ? 366 SER AAA CA  1 
ATOM   264   C C   . SER A 1 37  ? -46.583 -28.279 36.187  1.000 165.482 ? 366 SER AAA C   1 
ATOM   265   O O   . SER A 1 37  ? -45.610 -28.834 36.732  1.000 166.325 ? 366 SER AAA O   1 
ATOM   266   C CB  . SER A 1 37  ? -46.558 -28.298 33.643  1.000 168.322 ? 366 SER AAA CB  1 
ATOM   267   O OG  . SER A 1 37  ? -46.309 -26.909 33.790  1.000 172.632 ? 366 SER AAA OG  1 
ATOM   268   N N   . VAL A 1 38  ? -47.202 -27.196 36.672  1.000 167.069 ? 367 VAL AAA N   1 
ATOM   269   C CA  . VAL A 1 38  ? -46.869 -26.518 37.964  1.000 167.274 ? 367 VAL AAA CA  1 
ATOM   270   C C   . VAL A 1 38  ? -46.614 -27.567 39.050  1.000 161.242 ? 367 VAL AAA C   1 
ATOM   271   O O   . VAL A 1 38  ? -45.644 -27.390 39.810  1.000 162.394 ? 367 VAL AAA O   1 
ATOM   272   C CB  . VAL A 1 38  ? -47.989 -25.556 38.407  1.000 169.711 ? 367 VAL AAA CB  1 
ATOM   273   C CG1 . VAL A 1 38  ? -47.812 -25.102 39.850  1.000 170.517 ? 367 VAL AAA CG1 1 
ATOM   274   C CG2 . VAL A 1 38  ? -48.095 -24.352 37.481  1.000 176.082 ? 367 VAL AAA CG2 1 
ATOM   275   N N   . LEU A 1 39  ? -47.469 -28.593 39.132  1.000 155.016 ? 368 LEU AAA N   1 
ATOM   276   C CA  . LEU A 1 39  ? -47.477 -29.593 40.233  1.000 151.179 ? 368 LEU AAA CA  1 
ATOM   277   C C   . LEU A 1 39  ? -46.423 -30.675 39.976  1.000 151.128 ? 368 LEU AAA C   1 
ATOM   278   O O   . LEU A 1 39  ? -45.551 -30.848 40.856  1.000 153.195 ? 368 LEU AAA O   1 
ATOM   279   C CB  . LEU A 1 39  ? -48.869 -30.218 40.364  1.000 146.850 ? 368 LEU AAA CB  1 
ATOM   280   C CG  . LEU A 1 39  ? -49.916 -29.371 41.084  1.000 148.282 ? 368 LEU AAA CG  1 
ATOM   281   C CD1 . LEU A 1 39  ? -50.099 -28.009 40.429  1.000 152.623 ? 368 LEU AAA CD1 1 
ATOM   282   C CD2 . LEU A 1 39  ? -51.241 -30.108 41.127  1.000 145.523 ? 368 LEU AAA CD2 1 
ATOM   283   N N   . TYR A 1 40  ? -46.493 -31.376 38.835  1.000 149.403 ? 369 TYR AAA N   1 
ATOM   284   C CA  . TYR A 1 40  ? -45.675 -32.594 38.569  1.000 146.830 ? 369 TYR AAA CA  1 
ATOM   285   C C   . TYR A 1 40  ? -44.210 -32.212 38.326  1.000 149.591 ? 369 TYR AAA C   1 
ATOM   286   O O   . TYR A 1 40  ? -43.333 -32.972 38.758  1.000 147.596 ? 369 TYR AAA O   1 
ATOM   287   C CB  . TYR A 1 40  ? -46.275 -33.500 37.479  1.000 144.618 ? 369 TYR AAA CB  1 
ATOM   288   C CG  . TYR A 1 40  ? -46.574 -32.922 36.114  1.000 147.168 ? 369 TYR AAA CG  1 
ATOM   289   C CD1 . TYR A 1 40  ? -45.609 -32.870 35.120  1.000 150.162 ? 369 TYR AAA CD1 1 
ATOM   290   C CD2 . TYR A 1 40  ? -47.859 -32.531 35.771  1.000 147.247 ? 369 TYR AAA CD2 1 
ATOM   291   C CE1 . TYR A 1 40  ? -45.895 -32.374 33.856  1.000 152.591 ? 369 TYR AAA CE1 1 
ATOM   292   C CE2 . TYR A 1 40  ? -48.162 -32.039 34.511  1.000 149.366 ? 369 TYR AAA CE2 1 
ATOM   293   C CZ  . TYR A 1 40  ? -47.177 -31.957 33.549  1.000 152.079 ? 369 TYR AAA CZ  1 
ATOM   294   O OH  . TYR A 1 40  ? -47.491 -31.461 32.318  1.000 155.443 ? 369 TYR AAA OH  1 
ATOM   295   N N   . ASN A 1 41  ? -43.940 -31.057 37.715  1.000 154.733 ? 370 ASN AAA N   1 
ATOM   296   C CA  . ASN A 1 41  ? -42.549 -30.619 37.416  1.000 160.746 ? 370 ASN AAA CA  1 
ATOM   297   C C   . ASN A 1 41  ? -41.862 -30.151 38.713  1.000 165.111 ? 370 ASN AAA C   1 
ATOM   298   O O   . ASN A 1 41  ? -40.636 -29.917 38.657  1.000 168.617 ? 370 ASN AAA O   1 
ATOM   299   C CB  . ASN A 1 41  ? -42.501 -29.588 36.277  1.000 164.547 ? 370 ASN AAA CB  1 
ATOM   300   C CG  . ASN A 1 41  ? -42.611 -30.194 34.886  1.000 163.156 ? 370 ASN AAA CG  1 
ATOM   301   O OD1 . ASN A 1 41  ? -42.077 -31.271 34.614  1.000 159.790 ? 370 ASN AAA OD1 1 
ATOM   302   N ND2 . ASN A 1 41  ? -43.281 -29.498 33.980  1.000 165.246 ? 370 ASN AAA ND2 1 
ATOM   303   N N   . SER A 1 42  ? -42.588 -30.057 39.842  1.000 166.244 ? 371 SER AAA N   1 
ATOM   304   C CA  . SER A 1 42  ? -42.027 -29.769 41.198  1.000 170.320 ? 371 SER AAA CA  1 
ATOM   305   C C   . SER A 1 42  ? -41.604 -31.066 41.898  1.000 170.742 ? 371 SER AAA C   1 
ATOM   306   O O   . SER A 1 42  ? -42.475 -31.944 42.091  1.000 165.796 ? 371 SER AAA O   1 
ATOM   307   C CB  . SER A 1 42  ? -42.989 -29.023 42.076  1.000 169.336 ? 371 SER AAA CB  1 
ATOM   308   O OG  . SER A 1 42  ? -42.588 -29.141 43.437  1.000 169.470 ? 371 SER AAA OG  1 
ATOM   309   N N   . ALA A 1 43  ? -40.339 -31.139 42.332  1.000 176.554 ? 372 ALA AAA N   1 
ATOM   310   C CA  . ALA A 1 43  ? -39.666 -32.371 42.816  1.000 176.772 ? 372 ALA AAA CA  1 
ATOM   311   C C   . ALA A 1 43  ? -40.186 -32.767 44.205  1.000 174.743 ? 372 ALA AAA C   1 
ATOM   312   O O   . ALA A 1 43  ? -40.040 -33.951 44.576  1.000 173.775 ? 372 ALA AAA O   1 
ATOM   313   C CB  . ALA A 1 43  ? -38.168 -32.168 42.838  1.000 182.785 ? 372 ALA AAA CB  1 
ATOM   314   N N   . SER A 1 44  ? -40.791 -31.820 44.930  1.000 173.918 ? 373 SER AAA N   1 
ATOM   315   C CA  . SER A 1 44  ? -41.097 -31.908 46.381  1.000 173.502 ? 373 SER AAA CA  1 
ATOM   316   C C   . SER A 1 44  ? -42.509 -32.468 46.625  1.000 167.452 ? 373 SER AAA C   1 
ATOM   317   O O   . SER A 1 44  ? -43.335 -31.754 47.207  1.000 167.011 ? 373 SER AAA O   1 
ATOM   318   C CB  . SER A 1 44  ? -40.889 -30.551 47.006  1.000 178.165 ? 373 SER AAA CB  1 
ATOM   319   O OG  . SER A 1 44  ? -41.072 -29.524 46.041  1.000 178.468 ? 373 SER AAA OG  1 
ATOM   320   N N   . PHE A 1 45  ? -42.760 -33.713 46.204  1.000 163.448 ? 374 PHE AAA N   1 
ATOM   321   C CA  . PHE A 1 45  ? -43.930 -34.554 46.584  1.000 159.597 ? 374 PHE AAA CA  1 
ATOM   322   C C   . PHE A 1 45  ? -43.469 -36.010 46.715  1.000 157.199 ? 374 PHE AAA C   1 
ATOM   323   O O   . PHE A 1 45  ? -42.827 -36.502 45.777  1.000 157.382 ? 374 PHE AAA O   1 
ATOM   324   C CB  . PHE A 1 45  ? -45.047 -34.502 45.536  1.000 157.480 ? 374 PHE AAA CB  1 
ATOM   325   C CG  . PHE A 1 45  ? -45.768 -33.185 45.389  1.000 159.966 ? 374 PHE AAA CG  1 
ATOM   326   C CD1 . PHE A 1 45  ? -46.353 -32.560 46.477  1.000 162.950 ? 374 PHE AAA CD1 1 
ATOM   327   C CD2 . PHE A 1 45  ? -45.903 -32.588 44.148  1.000 160.579 ? 374 PHE AAA CD2 1 
ATOM   328   C CE1 . PHE A 1 45  ? -47.022 -31.352 46.335  1.000 164.269 ? 374 PHE AAA CE1 1 
ATOM   329   C CE2 . PHE A 1 45  ? -46.582 -31.388 44.008  1.000 162.976 ? 374 PHE AAA CE2 1 
ATOM   330   C CZ  . PHE A 1 45  ? -47.137 -30.771 45.100  1.000 164.470 ? 374 PHE AAA CZ  1 
ATOM   331   N N   . SER A 1 46  ? -43.784 -36.678 47.827  1.000 155.954 ? 375 SER AAA N   1 
ATOM   332   C CA  . SER A 1 46  ? -43.381 -38.083 48.106  1.000 155.829 ? 375 SER AAA CA  1 
ATOM   333   C C   . SER A 1 46  ? -44.063 -39.026 47.113  1.000 151.506 ? 375 SER AAA C   1 
ATOM   334   O O   . SER A 1 46  ? -43.379 -39.885 46.534  1.000 151.080 ? 375 SER AAA O   1 
ATOM   335   C CB  . SER A 1 46  ? -43.699 -38.484 49.523  1.000 157.590 ? 375 SER AAA CB  1 
ATOM   336   O OG  . SER A 1 46  ? -42.664 -38.087 50.406  1.000 163.083 ? 375 SER AAA OG  1 
ATOM   337   N N   . THR A 1 47  ? -45.371 -38.852 46.947  1.000 149.453 ? 376 THR AAA N   1 
ATOM   338   C CA  . THR A 1 47  ? -46.298 -39.808 46.292  1.000 147.398 ? 376 THR AAA CA  1 
ATOM   339   C C   . THR A 1 47  ? -47.167 -39.016 45.308  1.000 145.446 ? 376 THR AAA C   1 
ATOM   340   O O   . THR A 1 47  ? -48.003 -38.229 45.772  1.000 146.310 ? 376 THR AAA O   1 
ATOM   341   C CB  . THR A 1 47  ? -47.121 -40.549 47.361  1.000 148.472 ? 376 THR AAA CB  1 
ATOM   342   O OG1 . THR A 1 47  ? -46.237 -41.126 48.325  1.000 150.834 ? 376 THR AAA OG1 1 
ATOM   343   C CG2 . THR A 1 47  ? -48.014 -41.631 46.799  1.000 146.255 ? 376 THR AAA CG2 1 
ATOM   344   N N   . PHE A 1 48  ? -46.943 -39.182 44.004  1.000 143.736 ? 377 PHE AAA N   1 
ATOM   345   C CA  . PHE A 1 48  ? -47.796 -38.629 42.918  1.000 140.848 ? 377 PHE AAA CA  1 
ATOM   346   C C   . PHE A 1 48  ? -48.328 -39.812 42.102  1.000 141.593 ? 377 PHE AAA C   1 
ATOM   347   O O   . PHE A 1 48  ? -47.957 -39.982 40.918  1.000 141.480 ? 377 PHE AAA O   1 
ATOM   348   C CB  . PHE A 1 48  ? -47.012 -37.613 42.083  1.000 139.181 ? 377 PHE AAA CB  1 
ATOM   349   C CG  . PHE A 1 48  ? -47.836 -36.512 41.463  1.000 136.216 ? 377 PHE AAA CG  1 
ATOM   350   C CD1 . PHE A 1 48  ? -48.843 -36.792 40.555  1.000 132.538 ? 377 PHE AAA CD1 1 
ATOM   351   C CD2 . PHE A 1 48  ? -47.579 -35.182 41.757  1.000 137.885 ? 377 PHE AAA CD2 1 
ATOM   352   C CE1 . PHE A 1 48  ? -49.579 -35.771 39.973  1.000 131.699 ? 377 PHE AAA CE1 1 
ATOM   353   C CE2 . PHE A 1 48  ? -48.318 -34.159 41.176  1.000 137.244 ? 377 PHE AAA CE2 1 
ATOM   354   C CZ  . PHE A 1 48  ? -49.321 -34.458 40.288  1.000 133.935 ? 377 PHE AAA CZ  1 
ATOM   355   N N   . LYS A 1 49  ? -49.144 -40.645 42.751  1.000 143.737 ? 378 LYS AAA N   1 
ATOM   356   C CA  . LYS A 1 49  ? -49.824 -41.801 42.112  1.000 144.879 ? 378 LYS AAA CA  1 
ATOM   357   C C   . LYS A 1 49  ? -51.066 -41.275 41.393  1.000 143.262 ? 378 LYS AAA C   1 
ATOM   358   O O   . LYS A 1 49  ? -51.943 -40.688 42.066  1.000 141.686 ? 378 LYS AAA O   1 
ATOM   359   C CB  . LYS A 1 49  ? -50.216 -42.876 43.131  1.000 148.120 ? 378 LYS AAA CB  1 
ATOM   360   C CG  . LYS A 1 49  ? -49.088 -43.786 43.601  1.000 151.712 ? 378 LYS AAA CG  1 
ATOM   361   C CD  . LYS A 1 49  ? -49.504 -44.786 44.664  1.000 155.200 ? 378 LYS AAA CD  1 
ATOM   362   C CE  . LYS A 1 49  ? -50.299 -44.141 45.787  1.000 158.790 ? 378 LYS AAA CE  1 
ATOM   363   N NZ  . LYS A 1 49  ? -50.006 -44.740 47.111  1.000 163.611 ? 378 LYS AAA NZ  1 
ATOM   364   N N   . CYS A 1 50  ? -51.109 -41.459 40.074  1.000 142.778 ? 379 CYS AAA N   1 
ATOM   365   C CA  . CYS A 1 50  ? -52.258 -41.101 39.209  1.000 142.257 ? 379 CYS AAA CA  1 
ATOM   366   C C   . CYS A 1 50  ? -52.985 -42.381 38.804  1.000 139.057 ? 379 CYS AAA C   1 
ATOM   367   O O   . CYS A 1 50  ? -52.307 -43.339 38.400  1.000 142.603 ? 379 CYS AAA O   1 
ATOM   368   C CB  . CYS A 1 50  ? -51.788 -40.316 37.992  1.000 145.760 ? 379 CYS AAA CB  1 
ATOM   369   S SG  . CYS A 1 50  ? -51.461 -38.577 38.379  1.000 148.963 ? 379 CYS AAA SG  1 
ATOM   370   N N   . TYR A 1 51  ? -54.310 -42.394 38.935  1.000 133.719 ? 380 TYR AAA N   1 
ATOM   371   C CA  . TYR A 1 51  ? -55.172 -43.559 38.625  1.000 132.030 ? 380 TYR AAA CA  1 
ATOM   372   C C   . TYR A 1 51  ? -56.131 -43.159 37.497  1.000 132.497 ? 380 TYR AAA C   1 
ATOM   373   O O   . TYR A 1 51  ? -56.986 -42.280 37.727  1.000 133.938 ? 380 TYR AAA O   1 
ATOM   374   C CB  . TYR A 1 51  ? -55.900 -44.017 39.894  1.000 132.552 ? 380 TYR AAA CB  1 
ATOM   375   C CG  . TYR A 1 51  ? -55.015 -44.517 41.010  1.000 131.529 ? 380 TYR AAA CG  1 
ATOM   376   C CD1 . TYR A 1 51  ? -54.481 -43.654 41.954  1.000 131.879 ? 380 TYR AAA CD1 1 
ATOM   377   C CD2 . TYR A 1 51  ? -54.721 -45.863 41.136  1.000 132.589 ? 380 TYR AAA CD2 1 
ATOM   378   C CE1 . TYR A 1 51  ? -53.666 -44.113 42.979  1.000 134.222 ? 380 TYR AAA CE1 1 
ATOM   379   C CE2 . TYR A 1 51  ? -53.901 -46.339 42.150  1.000 134.496 ? 380 TYR AAA CE2 1 
ATOM   380   C CZ  . TYR A 1 51  ? -53.369 -45.463 43.080  1.000 135.496 ? 380 TYR AAA CZ  1 
ATOM   381   O OH  . TYR A 1 51  ? -52.556 -45.943 44.073  1.000 137.282 ? 380 TYR AAA OH  1 
ATOM   382   N N   . GLY A 1 52  ? -55.948 -43.749 36.309  1.000 132.225 ? 381 GLY AAA N   1 
ATOM   383   C CA  . GLY A 1 52  ? -56.875 -43.660 35.161  1.000 133.279 ? 381 GLY AAA CA  1 
ATOM   384   C C   . GLY A 1 52  ? -56.883 -42.295 34.487  1.000 132.387 ? 381 GLY AAA C   1 
ATOM   385   O O   . GLY A 1 52  ? -57.940 -41.929 33.919  1.000 133.279 ? 381 GLY AAA O   1 
ATOM   386   N N   . VAL A 1 53  ? -55.769 -41.556 34.535  1.000 129.750 ? 382 VAL AAA N   1 
ATOM   387   C CA  . VAL A 1 53  ? -55.598 -40.309 33.729  1.000 131.031 ? 382 VAL AAA CA  1 
ATOM   388   C C   . VAL A 1 53  ? -54.124 -39.878 33.716  1.000 128.748 ? 382 VAL AAA C   1 
ATOM   389   O O   . VAL A 1 53  ? -53.524 -39.782 34.784  1.000 123.347 ? 382 VAL AAA O   1 
ATOM   390   C CB  . VAL A 1 53  ? -56.526 -39.175 34.212  1.000 131.872 ? 382 VAL AAA CB  1 
ATOM   391   C CG1 . VAL A 1 53  ? -56.182 -38.685 35.607  1.000 129.760 ? 382 VAL AAA CG1 1 
ATOM   392   C CG2 . VAL A 1 53  ? -56.539 -38.013 33.234  1.000 136.147 ? 382 VAL AAA CG2 1 
ATOM   393   N N   . SER A 1 54  ? -53.578 -39.635 32.522  1.000 132.711 ? 383 SER AAA N   1 
ATOM   394   C CA  . SER A 1 54  ? -52.226 -39.062 32.301  1.000 134.378 ? 383 SER AAA CA  1 
ATOM   395   C C   . SER A 1 54  ? -52.282 -37.590 32.683  1.000 135.353 ? 383 SER AAA C   1 
ATOM   396   O O   . SER A 1 54  ? -52.947 -36.832 31.988  1.000 140.712 ? 383 SER AAA O   1 
ATOM   397   C CB  . SER A 1 54  ? -51.760 -39.229 30.862  1.000 138.263 ? 383 SER AAA CB  1 
ATOM   398   O OG  . SER A 1 54  ? -50.918 -40.366 30.676  1.000 137.794 ? 383 SER AAA OG  1 
ATOM   399   N N   . PRO A 1 55  ? -51.617 -37.151 33.778  1.000 133.385 ? 384 PRO AAA N   1 
ATOM   400   C CA  . PRO A 1 55  ? -51.558 -35.733 34.146  1.000 135.482 ? 384 PRO AAA CA  1 
ATOM   401   C C   . PRO A 1 55  ? -50.668 -34.905 33.207  1.000 140.741 ? 384 PRO AAA C   1 
ATOM   402   O O   . PRO A 1 55  ? -50.894 -33.714 33.043  1.000 143.202 ? 384 PRO AAA O   1 
ATOM   403   C CB  . PRO A 1 55  ? -50.943 -35.771 35.548  1.000 131.652 ? 384 PRO AAA CB  1 
ATOM   404   C CG  . PRO A 1 55  ? -50.044 -36.968 35.487  1.000 130.364 ? 384 PRO AAA CG  1 
ATOM   405   C CD  . PRO A 1 55  ? -50.855 -37.985 34.715  1.000 130.243 ? 384 PRO AAA CD  1 
ATOM   406   N N   . THR A 1 56  ? -49.675 -35.556 32.602  1.000 142.765 ? 385 THR AAA N   1 
ATOM   407   C CA  . THR A 1 56  ? -48.784 -34.951 31.583  1.000 148.429 ? 385 THR AAA CA  1 
ATOM   408   C C   . THR A 1 56  ? -49.619 -34.490 30.385  1.000 152.597 ? 385 THR AAA C   1 
ATOM   409   O O   . THR A 1 56  ? -49.157 -33.590 29.658  1.000 158.738 ? 385 THR AAA O   1 
ATOM   410   C CB  . THR A 1 56  ? -47.699 -35.941 31.144  1.000 149.410 ? 385 THR AAA CB  1 
ATOM   411   O OG1 . THR A 1 56  ? -48.346 -37.098 30.614  1.000 148.857 ? 385 THR AAA OG1 1 
ATOM   412   C CG2 . THR A 1 56  ? -46.770 -36.330 32.274  1.000 147.843 ? 385 THR AAA CG2 1 
ATOM   413   N N   . LYS A 1 57  ? -50.790 -35.099 30.178  1.000 151.932 ? 386 LYS AAA N   1 
ATOM   414   C CA  . LYS A 1 57  ? -51.581 -34.972 28.925  1.000 156.656 ? 386 LYS AAA CA  1 
ATOM   415   C C   . LYS A 1 57  ? -52.842 -34.121 29.157  1.000 159.729 ? 386 LYS AAA C   1 
ATOM   416   O O   . LYS A 1 57  ? -53.333 -33.547 28.172  1.000 163.884 ? 386 LYS AAA O   1 
ATOM   417   C CB  . LYS A 1 57  ? -51.856 -36.373 28.357  1.000 154.688 ? 386 LYS AAA CB  1 
ATOM   418   C CG  . LYS A 1 57  ? -50.620 -37.071 27.786  1.000 153.270 ? 386 LYS AAA CG  1 
ATOM   419   C CD  . LYS A 1 57  ? -50.766 -38.547 27.466  1.000 150.282 ? 386 LYS AAA CD  1 
ATOM   420   C CE  . LYS A 1 57  ? -51.702 -38.819 26.314  1.000 153.341 ? 386 LYS AAA CE  1 
ATOM   421   N NZ  . LYS A 1 57  ? -51.174 -38.232 25.065  1.000 158.845 ? 386 LYS AAA NZ  1 
ATOM   422   N N   . LEU A 1 58  ? -53.340 -33.987 30.391  1.000 160.238 ? 387 LEU AAA N   1 
ATOM   423   C CA  . LEU A 1 58  ? -54.602 -33.231 30.661  1.000 166.213 ? 387 LEU AAA CA  1 
ATOM   424   C C   . LEU A 1 58  ? -54.343 -31.715 30.695  1.000 172.732 ? 387 LEU AAA C   1 
ATOM   425   O O   . LEU A 1 58  ? -55.290 -30.965 31.034  1.000 174.039 ? 387 LEU AAA O   1 
ATOM   426   C CB  . LEU A 1 58  ? -55.299 -33.720 31.942  1.000 163.019 ? 387 LEU AAA CB  1 
ATOM   427   C CG  . LEU A 1 58  ? -54.496 -33.753 33.246  1.000 158.392 ? 387 LEU AAA CG  1 
ATOM   428   C CD1 . LEU A 1 58  ? -53.677 -32.498 33.463  1.000 159.760 ? 387 LEU AAA CD1 1 
ATOM   429   C CD2 . LEU A 1 58  ? -55.423 -33.980 34.431  1.000 155.179 ? 387 LEU AAA CD2 1 
ATOM   430   N N   . ASN A 1 59  ? -53.129 -31.270 30.352  1.000 179.281 ? 388 ASN AAA N   1 
ATOM   431   C CA  . ASN A 1 59  ? -52.853 -29.841 30.034  1.000 188.856 ? 388 ASN AAA CA  1 
ATOM   432   C C   . ASN A 1 59  ? -53.160 -29.598 28.545  1.000 196.371 ? 388 ASN AAA C   1 
ATOM   433   O O   . ASN A 1 59  ? -52.675 -28.591 28.012  1.000 203.215 ? 388 ASN AAA O   1 
ATOM   434   C CB  . ASN A 1 59  ? -51.451 -29.381 30.475  1.000 191.195 ? 388 ASN AAA CB  1 
ATOM   435   C CG  . ASN A 1 59  ? -50.284 -30.078 29.799  1.000 194.053 ? 388 ASN AAA CG  1 
ATOM   436   O OD1 . ASN A 1 59  ? -50.019 -29.890 28.609  1.000 198.117 ? 388 ASN AAA OD1 1 
ATOM   437   N ND2 . ASN A 1 59  ? -49.539 -30.850 30.575  1.000 192.746 ? 388 ASN AAA ND2 1 
ATOM   438   N N   . ASP A 1 60  ? -53.944 -30.471 27.895  1.000 196.864 ? 389 ASP AAA N   1 
ATOM   439   C CA  . ASP A 1 60  ? -54.558 -30.210 26.561  1.000 202.536 ? 389 ASP AAA CA  1 
ATOM   440   C C   . ASP A 1 60  ? -55.872 -30.999 26.424  1.000 201.347 ? 389 ASP AAA C   1 
ATOM   441   O O   . ASP A 1 60  ? -56.148 -31.490 25.314  1.000 206.185 ? 389 ASP AAA O   1 
ATOM   442   C CB  . ASP A 1 60  ? -53.556 -30.449 25.416  1.000 206.553 ? 389 ASP AAA CB  1 
ATOM   443   C CG  . ASP A 1 60  ? -52.793 -31.768 25.433  1.000 202.329 ? 389 ASP AAA CG  1 
ATOM   444   O OD1 . ASP A 1 60  ? -53.451 -32.826 25.445  1.000 200.403 ? 389 ASP AAA OD1 1 
ATOM   445   O OD2 . ASP A 1 60  ? -51.537 -31.725 25.402  1.000 201.686 ? 389 ASP AAA OD2 1 
ATOM   446   N N   . LEU A 1 61  ? -56.664 -31.086 27.501  1.000 196.635 ? 390 LEU AAA N   1 
ATOM   447   C CA  . LEU A 1 61  ? -58.000 -31.750 27.528  1.000 195.966 ? 390 LEU AAA CA  1 
ATOM   448   C C   . LEU A 1 61  ? -58.856 -31.136 28.642  1.000 195.021 ? 390 LEU AAA C   1 
ATOM   449   O O   . LEU A 1 61  ? -58.322 -30.941 29.750  1.000 190.681 ? 390 LEU AAA O   1 
ATOM   450   C CB  . LEU A 1 61  ? -57.820 -33.257 27.741  1.000 190.751 ? 390 LEU AAA CB  1 
ATOM   451   C CG  . LEU A 1 61  ? -59.052 -34.117 27.458  1.000 191.421 ? 390 LEU AAA CG  1 
ATOM   452   C CD1 . LEU A 1 61  ? -58.693 -35.323 26.597  1.000 191.337 ? 390 LEU AAA CD1 1 
ATOM   453   C CD2 . LEU A 1 61  ? -59.726 -34.560 28.753  1.000 186.424 ? 390 LEU AAA CD2 1 
ATOM   454   N N   . CYS A 1 62  ? -60.137 -30.877 28.357  1.000 200.918 ? 391 CYS AAA N   1 
ATOM   455   C CA  . CYS A 1 62  ? -61.057 -30.045 29.184  1.000 203.014 ? 391 CYS AAA CA  1 
ATOM   456   C C   . CYS A 1 62  ? -62.027 -30.913 29.995  1.000 200.133 ? 391 CYS AAA C   1 
ATOM   457   O O   . CYS A 1 62  ? -62.866 -31.591 29.370  1.000 205.669 ? 391 CYS AAA O   1 
ATOM   458   C CB  . CYS A 1 62  ? -61.846 -29.090 28.296  1.000 211.358 ? 391 CYS AAA CB  1 
ATOM   459   S SG  . CYS A 1 62  ? -60.817 -27.769 27.605  1.000 218.027 ? 391 CYS AAA SG  1 
ATOM   460   N N   . PHE A 1 63  ? -61.930 -30.861 31.331  1.000 193.574 ? 392 PHE AAA N   1 
ATOM   461   C CA  . PHE A 1 63  ? -62.822 -31.555 32.300  1.000 188.768 ? 392 PHE AAA CA  1 
ATOM   462   C C   . PHE A 1 63  ? -63.847 -30.571 32.871  1.000 188.619 ? 392 PHE AAA C   1 
ATOM   463   O O   . PHE A 1 63  ? -63.490 -29.397 33.077  1.000 191.709 ? 392 PHE AAA O   1 
ATOM   464   C CB  . PHE A 1 63  ? -62.018 -32.156 33.452  1.000 183.883 ? 392 PHE AAA CB  1 
ATOM   465   C CG  . PHE A 1 63  ? -61.209 -33.366 33.071  1.000 183.346 ? 392 PHE AAA CG  1 
ATOM   466   C CD1 . PHE A 1 63  ? -61.806 -34.615 32.961  1.000 183.314 ? 392 PHE AAA CD1 1 
ATOM   467   C CD2 . PHE A 1 63  ? -59.850 -33.253 32.822  1.000 182.985 ? 392 PHE AAA CD2 1 
ATOM   468   C CE1 . PHE A 1 63  ? -61.055 -35.730 32.619  1.000 181.596 ? 392 PHE AAA CE1 1 
ATOM   469   C CE2 . PHE A 1 63  ? -59.100 -34.369 32.480  1.000 181.614 ? 392 PHE AAA CE2 1 
ATOM   470   C CZ  . PHE A 1 63  ? -59.707 -35.602 32.370  1.000 181.157 ? 392 PHE AAA CZ  1 
ATOM   471   N N   . THR A 1 64  ? -65.064 -31.054 33.146  1.000 184.857 ? 393 THR AAA N   1 
ATOM   472   C CA  . THR A 1 64  ? -66.203 -30.258 33.681  1.000 183.428 ? 393 THR AAA CA  1 
ATOM   473   C C   . THR A 1 64  ? -65.853 -29.742 35.079  1.000 176.256 ? 393 THR AAA C   1 
ATOM   474   O O   . THR A 1 64  ? -66.092 -28.549 35.340  1.000 176.293 ? 393 THR AAA O   1 
ATOM   475   C CB  . THR A 1 64  ? -67.502 -31.074 33.695  1.000 184.839 ? 393 THR AAA CB  1 
ATOM   476   O OG1 . THR A 1 64  ? -67.174 -32.437 33.962  1.000 181.109 ? 393 THR AAA OG1 1 
ATOM   477   C CG2 . THR A 1 64  ? -68.257 -30.996 32.389  1.000 191.592 ? 393 THR AAA CG2 1 
ATOM   478   N N   . ASN A 1 65  ? -65.307 -30.612 35.933  1.000 169.028 ? 394 ASN AAA N   1 
ATOM   479   C CA  . ASN A 1 65  ? -64.965 -30.281 37.340  1.000 163.742 ? 394 ASN AAA CA  1 
ATOM   480   C C   . ASN A 1 65  ? -63.731 -31.054 37.793  1.000 157.139 ? 394 ASN AAA C   1 
ATOM   481   O O   . ASN A 1 65  ? -63.629 -32.273 37.523  1.000 154.400 ? 394 ASN AAA O   1 
ATOM   482   C CB  . ASN A 1 65  ? -66.116 -30.574 38.298  1.000 163.869 ? 394 ASN AAA CB  1 
ATOM   483   C CG  . ASN A 1 65  ? -67.253 -29.597 38.126  1.000 170.028 ? 394 ASN AAA CG  1 
ATOM   484   O OD1 . ASN A 1 65  ? -67.108 -28.422 38.450  1.000 172.645 ? 394 ASN AAA OD1 1 
ATOM   485   N ND2 . ASN A 1 65  ? -68.370 -30.066 37.591  1.000 174.463 ? 394 ASN AAA ND2 1 
ATOM   486   N N   . VAL A 1 66  ? -62.845 -30.340 38.480  1.000 154.148 ? 395 VAL AAA N   1 
ATOM   487   C CA  . VAL A 1 66  ? -61.727 -30.921 39.266  1.000 149.208 ? 395 VAL AAA CA  1 
ATOM   488   C C   . VAL A 1 66  ? -62.065 -30.715 40.736  1.000 146.147 ? 395 VAL AAA C   1 
ATOM   489   O O   . VAL A 1 66  ? -62.234 -29.558 41.156  1.000 147.214 ? 395 VAL AAA O   1 
ATOM   490   C CB  . VAL A 1 66  ? -60.384 -30.276 38.899  1.000 150.610 ? 395 VAL AAA CB  1 
ATOM   491   C CG1 . VAL A 1 66  ? -59.239 -30.860 39.712  1.000 147.345 ? 395 VAL AAA CG1 1 
ATOM   492   C CG2 . VAL A 1 66  ? -60.124 -30.390 37.406  1.000 153.775 ? 395 VAL AAA CG2 1 
ATOM   493   N N   . TYR A 1 67  ? -62.207 -31.817 41.461  1.000 142.511 ? 396 TYR AAA N   1 
ATOM   494   C CA  . TYR A 1 67  ? -62.383 -31.840 42.926  1.000 140.782 ? 396 TYR AAA CA  1 
ATOM   495   C C   . TYR A 1 67  ? -61.002 -32.067 43.547  1.000 139.544 ? 396 TYR AAA C   1 
ATOM   496   O O   . TYR A 1 67  ? -60.269 -32.964 43.084  1.000 135.628 ? 396 TYR AAA O   1 
ATOM   497   C CB  . TYR A 1 67  ? -63.427 -32.897 43.285  1.000 139.696 ? 396 TYR AAA CB  1 
ATOM   498   C CG  . TYR A 1 67  ? -64.808 -32.635 42.736  1.000 142.065 ? 396 TYR AAA CG  1 
ATOM   499   C CD1 . TYR A 1 67  ? -65.351 -31.359 42.743  1.000 144.950 ? 396 TYR AAA CD1 1 
ATOM   500   C CD2 . TYR A 1 67  ? -65.595 -33.668 42.251  1.000 142.980 ? 396 TYR AAA CD2 1 
ATOM   501   C CE1 . TYR A 1 67  ? -66.630 -31.112 42.267  1.000 148.458 ? 396 TYR AAA CE1 1 
ATOM   502   C CE2 . TYR A 1 67  ? -66.874 -33.435 41.765  1.000 147.190 ? 396 TYR AAA CE2 1 
ATOM   503   C CZ  . TYR A 1 67  ? -67.399 -32.151 41.773  1.000 149.328 ? 396 TYR AAA CZ  1 
ATOM   504   O OH  . TYR A 1 67  ? -68.656 -31.886 41.303  1.000 151.187 ? 396 TYR AAA OH  1 
ATOM   505   N N   . ALA A 1 68  ? -60.650 -31.239 44.534  1.000 143.132 ? 397 ALA AAA N   1 
ATOM   506   C CA  . ALA A 1 68  ? -59.378 -31.297 45.290  1.000 145.282 ? 397 ALA AAA CA  1 
ATOM   507   C C   . ALA A 1 68  ? -59.677 -31.535 46.778  1.000 147.786 ? 397 ALA AAA C   1 
ATOM   508   O O   . ALA A 1 68  ? -60.039 -30.567 47.490  1.000 152.127 ? 397 ALA AAA O   1 
ATOM   509   C CB  . ALA A 1 68  ? -58.599 -30.026 45.072  1.000 148.053 ? 397 ALA AAA CB  1 
ATOM   510   N N   . ASP A 1 69  ? -59.543 -32.789 47.218  1.000 146.118 ? 398 ASP AAA N   1 
ATOM   511   C CA  . ASP A 1 69  ? -59.761 -33.224 48.621  1.000 144.846 ? 398 ASP AAA CA  1 
ATOM   512   C C   . ASP A 1 69  ? -58.406 -33.167 49.329  1.000 144.971 ? 398 ASP AAA C   1 
ATOM   513   O O   . ASP A 1 69  ? -57.473 -33.827 48.845  1.000 141.853 ? 398 ASP AAA O   1 
ATOM   514   C CB  . ASP A 1 69  ? -60.402 -34.617 48.654  1.000 143.769 ? 398 ASP AAA CB  1 
ATOM   515   C CG  . ASP A 1 69  ? -61.605 -34.755 47.729  1.000 143.647 ? 398 ASP AAA CG  1 
ATOM   516   O OD1 . ASP A 1 69  ? -62.329 -33.747 47.569  1.000 145.184 ? 398 ASP AAA OD1 1 
ATOM   517   O OD2 . ASP A 1 69  ? -61.806 -35.861 47.160  1.000 140.118 ? 398 ASP AAA OD2 1 
ATOM   518   N N   . SER A 1 70  ? -58.295 -32.377 50.397  1.000 136.143 ? 399 SER AAA N   1 
ATOM   519   C CA  . SER A 1 70  ? -57.041 -32.176 51.170  1.000 140.804 ? 399 SER AAA CA  1 
ATOM   520   C C   . SER A 1 70  ? -57.238 -32.633 52.623  1.000 142.367 ? 399 SER AAA C   1 
ATOM   521   O O   . SER A 1 70  ? -58.308 -32.345 53.197  1.000 145.266 ? 399 SER AAA O   1 
ATOM   522   C CB  . SER A 1 70  ? -56.579 -30.736 51.095  1.000 143.707 ? 399 SER AAA CB  1 
ATOM   523   O OG  . SER A 1 70  ? -57.637 -29.836 51.401  1.000 146.552 ? 399 SER AAA OG  1 
ATOM   524   N N   . PHE A 1 71  ? -56.236 -33.304 53.201  1.000 140.614 ? 400 PHE AAA N   1 
ATOM   525   C CA  . PHE A 1 71  ? -56.233 -33.753 54.618  1.000 140.801 ? 400 PHE AAA CA  1 
ATOM   526   C C   . PHE A 1 71  ? -54.857 -34.299 55.017  1.000 143.280 ? 400 PHE AAA C   1 
ATOM   527   O O   . PHE A 1 71  ? -53.980 -34.425 54.146  1.000 146.806 ? 400 PHE AAA O   1 
ATOM   528   C CB  . PHE A 1 71  ? -57.293 -34.831 54.821  1.000 138.366 ? 400 PHE AAA CB  1 
ATOM   529   C CG  . PHE A 1 71  ? -57.120 -36.028 53.926  1.000 134.770 ? 400 PHE AAA CG  1 
ATOM   530   C CD1 . PHE A 1 71  ? -56.216 -37.028 54.248  1.000 135.372 ? 400 PHE AAA CD1 1 
ATOM   531   C CD2 . PHE A 1 71  ? -57.852 -36.148 52.759  1.000 131.928 ? 400 PHE AAA CD2 1 
ATOM   532   C CE1 . PHE A 1 71  ? -56.055 -38.131 53.425  1.000 134.159 ? 400 PHE AAA CE1 1 
ATOM   533   C CE2 . PHE A 1 71  ? -57.700 -37.259 51.944  1.000 131.219 ? 400 PHE AAA CE2 1 
ATOM   534   C CZ  . PHE A 1 71  ? -56.799 -38.247 52.275  1.000 132.131 ? 400 PHE AAA CZ  1 
ATOM   535   N N   . VAL A 1 72  ? -54.698 -34.642 56.301  1.000 144.642 ? 401 VAL AAA N   1 
ATOM   536   C CA  . VAL A 1 72  ? -53.427 -35.144 56.903  1.000 145.660 ? 401 VAL AAA CA  1 
ATOM   537   C C   . VAL A 1 72  ? -53.652 -36.540 57.485  1.000 145.020 ? 401 VAL AAA C   1 
ATOM   538   O O   . VAL A 1 72  ? -54.651 -36.730 58.210  1.000 144.478 ? 401 VAL AAA O   1 
ATOM   539   C CB  . VAL A 1 72  ? -52.908 -34.192 57.995  1.000 150.150 ? 401 VAL AAA CB  1 
ATOM   540   C CG1 . VAL A 1 72  ? -51.883 -34.867 58.892  1.000 153.309 ? 401 VAL AAA CG1 1 
ATOM   541   C CG2 . VAL A 1 72  ? -52.332 -32.915 57.407  1.000 150.674 ? 401 VAL AAA CG2 1 
ATOM   542   N N   . ILE A 1 73  ? -52.715 -37.446 57.206  1.000 145.174 ? 402 ILE AAA N   1 
ATOM   543   C CA  . ILE A 1 73  ? -52.608 -38.803 57.817  1.000 147.939 ? 402 ILE AAA CA  1 
ATOM   544   C C   . ILE A 1 73  ? -51.126 -39.082 58.072  1.000 149.526 ? 402 ILE AAA C   1 
ATOM   545   O O   . ILE A 1 73  ? -50.292 -38.326 57.540  1.000 147.644 ? 402 ILE AAA O   1 
ATOM   546   C CB  . ILE A 1 73  ? -53.245 -39.873 56.909  1.000 147.058 ? 402 ILE AAA CB  1 
ATOM   547   C CG1 . ILE A 1 73  ? -52.798 -39.719 55.453  1.000 145.914 ? 402 ILE AAA CG1 1 
ATOM   548   C CG2 . ILE A 1 73  ? -54.762 -39.850 57.030  1.000 145.810 ? 402 ILE AAA CG2 1 
ATOM   549   C CD1 . ILE A 1 73  ? -52.983 -40.968 54.608  1.000 144.921 ? 402 ILE AAA CD1 1 
ATOM   550   N N   . ARG A 1 74  ? -50.805 -40.121 58.844  1.000 154.343 ? 403 ARG AAA N   1 
ATOM   551   C CA  . ARG A 1 74  ? -49.394 -40.534 59.063  1.000 161.993 ? 403 ARG AAA CA  1 
ATOM   552   C C   . ARG A 1 74  ? -48.929 -41.280 57.807  1.000 160.440 ? 403 ARG AAA C   1 
ATOM   553   O O   . ARG A 1 74  ? -49.739 -42.014 57.225  1.000 158.532 ? 403 ARG AAA O   1 
ATOM   554   C CB  . ARG A 1 74  ? -49.228 -41.309 60.378  1.000 169.792 ? 403 ARG AAA CB  1 
ATOM   555   C CG  . ARG A 1 74  ? -49.789 -42.725 60.409  1.000 172.736 ? 403 ARG AAA CG  1 
ATOM   556   C CD  . ARG A 1 74  ? -49.822 -43.253 61.837  1.000 179.054 ? 403 ARG AAA CD  1 
ATOM   557   N NE  . ARG A 1 74  ? -50.277 -44.635 61.946  1.000 182.089 ? 403 ARG AAA NE  1 
ATOM   558   C CZ  . ARG A 1 74  ? -49.530 -45.712 61.701  1.000 185.514 ? 403 ARG AAA CZ  1 
ATOM   559   N NH1 . ARG A 1 74  ? -48.270 -45.583 61.316  1.000 187.189 ? 403 ARG AAA NH1 1 
ATOM   560   N NH2 . ARG A 1 74  ? -50.048 -46.922 61.840  1.000 186.924 ? 403 ARG AAA NH2 1 
ATOM   561   N N   . GLY A 1 75  ? -47.677 -41.060 57.398  1.000 162.776 ? 404 GLY AAA N   1 
ATOM   562   C CA  . GLY A 1 75  ? -47.084 -41.561 56.141  1.000 162.802 ? 404 GLY AAA CA  1 
ATOM   563   C C   . GLY A 1 75  ? -47.385 -43.025 55.853  1.000 164.590 ? 404 GLY AAA C   1 
ATOM   564   O O   . GLY A 1 75  ? -47.532 -43.358 54.668  1.000 164.015 ? 404 GLY AAA O   1 
ATOM   565   N N   . ASP A 1 76  ? -47.453 -43.880 56.879  1.000 167.461 ? 405 ASP AAA N   1 
ATOM   566   C CA  . ASP A 1 76  ? -47.716 -45.339 56.735  1.000 167.441 ? 405 ASP AAA CA  1 
ATOM   567   C C   . ASP A 1 76  ? -48.985 -45.582 55.918  1.000 163.703 ? 405 ASP AAA C   1 
ATOM   568   O O   . ASP A 1 76  ? -49.011 -46.552 55.145  1.000 161.951 ? 405 ASP AAA O   1 
ATOM   569   C CB  . ASP A 1 76  ? -47.871 -46.014 58.096  1.000 170.538 ? 405 ASP AAA CB  1 
ATOM   570   C CG  . ASP A 1 76  ? -46.547 -46.412 58.711  1.000 175.434 ? 405 ASP AAA CG  1 
ATOM   571   O OD1 . ASP A 1 76  ? -45.516 -46.244 58.031  1.000 176.126 ? 405 ASP AAA OD1 1 
ATOM   572   O OD2 . ASP A 1 76  ? -46.562 -46.887 59.861  1.000 180.344 ? 405 ASP AAA OD2 1 
ATOM   573   N N   . GLU A 1 77  ? -49.994 -44.733 56.108  1.000 163.393 ? 406 GLU AAA N   1 
ATOM   574   C CA  . GLU A 1 77  ? -51.373 -44.938 55.604  1.000 163.947 ? 406 GLU AAA CA  1 
ATOM   575   C C   . GLU A 1 77  ? -51.523 -44.334 54.196  1.000 160.507 ? 406 GLU AAA C   1 
ATOM   576   O O   . GLU A 1 77  ? -52.572 -44.576 53.577  1.000 162.649 ? 406 GLU AAA O   1 
ATOM   577   C CB  . GLU A 1 77  ? -52.370 -44.335 56.602  1.000 167.477 ? 406 GLU AAA CB  1 
ATOM   578   C CG  . GLU A 1 77  ? -52.282 -44.917 58.017  1.000 172.939 ? 406 GLU AAA CG  1 
ATOM   579   C CD  . GLU A 1 77  ? -52.877 -44.078 59.149  1.000 175.266 ? 406 GLU AAA CD  1 
ATOM   580   O OE1 . GLU A 1 77  ? -52.970 -42.836 58.993  1.000 174.911 ? 406 GLU AAA OE1 1 
ATOM   581   O OE2 . GLU A 1 77  ? -53.238 -44.665 60.202  1.000 178.310 ? 406 GLU AAA OE2 1 
ATOM   582   N N   . VAL A 1 78  ? -50.526 -43.597 53.688  1.000 156.686 ? 407 VAL AAA N   1 
ATOM   583   C CA  . VAL A 1 78  ? -50.540 -43.010 52.313  1.000 151.981 ? 407 VAL AAA CA  1 
ATOM   584   C C   . VAL A 1 78  ? -50.976 -44.081 51.313  1.000 148.170 ? 407 VAL AAA C   1 
ATOM   585   O O   . VAL A 1 78  ? -51.883 -43.798 50.526  1.000 141.074 ? 407 VAL AAA O   1 
ATOM   586   C CB  . VAL A 1 78  ? -49.169 -42.425 51.927  1.000 154.924 ? 407 VAL AAA CB  1 
ATOM   587   C CG1 . VAL A 1 78  ? -48.853 -42.568 50.440  1.000 154.734 ? 407 VAL AAA CG1 1 
ATOM   588   C CG2 . VAL A 1 78  ? -49.065 -40.973 52.358  1.000 155.574 ? 407 VAL AAA CG2 1 
ATOM   589   N N   . ARG A 1 79  ? -50.342 -45.254 51.347  1.000 151.432 ? 408 ARG AAA N   1 
ATOM   590   C CA  . ARG A 1 79  ? -50.634 -46.368 50.413  1.000 154.439 ? 408 ARG AAA CA  1 
ATOM   591   C C   . ARG A 1 79  ? -52.142 -46.635 50.364  1.000 153.145 ? 408 ARG AAA C   1 
ATOM   592   O O   . ARG A 1 79  ? -52.609 -46.990 49.274  1.000 154.545 ? 408 ARG AAA O   1 
ATOM   593   C CB  . ARG A 1 79  ? -49.897 -47.640 50.827  1.000 160.882 ? 408 ARG AAA CB  1 
ATOM   594   C CG  . ARG A 1 79  ? -50.583 -48.435 51.928  1.000 166.524 ? 408 ARG AAA CG  1 
ATOM   595   C CD  . ARG A 1 79  ? -49.830 -49.717 52.220  1.000 173.199 ? 408 ARG AAA CD  1 
ATOM   596   N NE  . ARG A 1 79  ? -48.495 -49.475 52.769  1.000 178.844 ? 408 ARG AAA NE  1 
ATOM   597   C CZ  . ARG A 1 79  ? -47.355 -49.348 52.073  1.000 181.721 ? 408 ARG AAA CZ  1 
ATOM   598   N NH1 . ARG A 1 79  ? -47.344 -49.404 50.747  1.000 179.740 ? 408 ARG AAA NH1 1 
ATOM   599   N NH2 . ARG A 1 79  ? -46.220 -49.139 52.723  1.000 185.550 ? 408 ARG AAA NH2 1 
ATOM   600   N N   . GLN A 1 80  ? -52.855 -46.493 51.491  1.000 153.098 ? 409 GLN AAA N   1 
ATOM   601   C CA  . GLN A 1 80  ? -54.297 -46.851 51.629  1.000 153.379 ? 409 GLN AAA CA  1 
ATOM   602   C C   . GLN A 1 80  ? -55.186 -45.871 50.842  1.000 148.570 ? 409 GLN AAA C   1 
ATOM   603   O O   . GLN A 1 80  ? -56.373 -46.200 50.653  1.000 145.911 ? 409 GLN AAA O   1 
ATOM   604   C CB  . GLN A 1 80  ? -54.753 -46.870 53.094  1.000 158.411 ? 409 GLN AAA CB  1 
ATOM   605   C CG  . GLN A 1 80  ? -54.279 -48.078 53.899  1.000 163.795 ? 409 GLN AAA CG  1 
ATOM   606   C CD  . GLN A 1 80  ? -55.254 -48.503 54.978  1.000 166.719 ? 409 GLN AAA CD  1 
ATOM   607   O OE1 . GLN A 1 80  ? -56.016 -47.708 55.531  1.000 164.076 ? 409 GLN AAA OE1 1 
ATOM   608   N NE2 . GLN A 1 80  ? -55.253 -49.792 55.283  1.000 171.079 ? 409 GLN AAA NE2 1 
ATOM   609   N N   . ILE A 1 81  ? -54.654 -44.720 50.410  1.000 146.533 ? 410 ILE AAA N   1 
ATOM   610   C CA  . ILE A 1 81  ? -55.373 -43.742 49.530  1.000 142.739 ? 410 ILE AAA CA  1 
ATOM   611   C C   . ILE A 1 81  ? -55.190 -44.178 48.067  1.000 138.675 ? 410 ILE AAA C   1 
ATOM   612   O O   . ILE A 1 81  ? -54.279 -43.671 47.360  1.000 136.859 ? 410 ILE AAA O   1 
ATOM   613   C CB  . ILE A 1 81  ? -54.914 -42.288 49.780  1.000 142.428 ? 410 ILE AAA CB  1 
ATOM   614   C CG1 . ILE A 1 81  ? -54.788 -41.964 51.273  1.000 143.778 ? 410 ILE AAA CG1 1 
ATOM   615   C CG2 . ILE A 1 81  ? -55.836 -41.307 49.074  1.000 140.356 ? 410 ILE AAA CG2 1 
ATOM   616   C CD1 . ILE A 1 81  ? -56.011 -42.308 52.097  1.000 143.707 ? 410 ILE AAA CD1 1 
ATOM   617   N N   . ALA A 1 82  ? -56.034 -45.117 47.649  1.000 134.907 ? 411 ALA AAA N   1 
ATOM   618   C CA  . ALA A 1 82  ? -55.999 -45.802 46.341  1.000 133.048 ? 411 ALA AAA CA  1 
ATOM   619   C C   . ALA A 1 82  ? -57.209 -46.717 46.264  1.000 133.115 ? 411 ALA AAA C   1 
ATOM   620   O O   . ALA A 1 82  ? -57.622 -47.274 47.275  1.000 136.473 ? 411 ALA AAA O   1 
ATOM   621   C CB  . ALA A 1 82  ? -54.716 -46.579 46.187  1.000 133.646 ? 411 ALA AAA CB  1 
ATOM   622   N N   . PRO A 1 83  ? -57.828 -46.880 45.080  1.000 131.914 ? 412 PRO AAA N   1 
ATOM   623   C CA  . PRO A 1 83  ? -58.998 -47.746 44.942  1.000 135.060 ? 412 PRO AAA CA  1 
ATOM   624   C C   . PRO A 1 83  ? -58.696 -49.194 45.359  1.000 138.561 ? 412 PRO AAA C   1 
ATOM   625   O O   . PRO A 1 83  ? -57.590 -49.643 45.106  1.000 138.163 ? 412 PRO AAA O   1 
ATOM   626   C CB  . PRO A 1 83  ? -59.306 -47.673 43.441  1.000 135.083 ? 412 PRO AAA CB  1 
ATOM   627   C CG  . PRO A 1 83  ? -57.987 -47.255 42.823  1.000 133.233 ? 412 PRO AAA CG  1 
ATOM   628   C CD  . PRO A 1 83  ? -57.423 -46.264 43.812  1.000 130.581 ? 412 PRO AAA CD  1 
ATOM   629   N N   . GLY A 1 84  ? -59.665 -49.858 46.003  1.000 141.896 ? 413 GLY AAA N   1 
ATOM   630   C CA  . GLY A 1 84  ? -59.615 -51.294 46.350  1.000 146.355 ? 413 GLY AAA CA  1 
ATOM   631   C C   . GLY A 1 84  ? -58.888 -51.582 47.657  1.000 148.288 ? 413 GLY AAA C   1 
ATOM   632   O O   . GLY A 1 84  ? -58.983 -52.732 48.135  1.000 151.512 ? 413 GLY AAA O   1 
ATOM   633   N N   . GLN A 1 85  ? -58.173 -50.601 48.211  1.000 147.674 ? 414 GLN AAA N   1 
ATOM   634   C CA  . GLN A 1 85  ? -57.508 -50.695 49.539  1.000 149.752 ? 414 GLN AAA CA  1 
ATOM   635   C C   . GLN A 1 85  ? -58.574 -50.742 50.637  1.000 150.941 ? 414 GLN AAA C   1 
ATOM   636   O O   . GLN A 1 85  ? -59.667 -50.183 50.414  1.000 149.434 ? 414 GLN AAA O   1 
ATOM   637   C CB  . GLN A 1 85  ? -56.610 -49.484 49.771  1.000 149.848 ? 414 GLN AAA CB  1 
ATOM   638   C CG  . GLN A 1 85  ? -55.383 -49.438 48.876  1.000 151.697 ? 414 GLN AAA CG  1 
ATOM   639   C CD  . GLN A 1 85  ? -54.270 -50.346 49.346  1.000 155.836 ? 414 GLN AAA CD  1 
ATOM   640   O OE1 . GLN A 1 85  ? -54.131 -50.645 50.533  1.000 158.348 ? 414 GLN AAA OE1 1 
ATOM   641   N NE2 . GLN A 1 85  ? -53.433 -50.770 48.409  1.000 156.547 ? 414 GLN AAA NE2 1 
ATOM   642   N N   . THR A 1 86  ? -58.256 -51.385 51.767  1.000 153.903 ? 415 THR AAA N   1 
ATOM   643   C CA  . THR A 1 86  ? -59.140 -51.547 52.959  1.000 155.309 ? 415 THR AAA CA  1 
ATOM   644   C C   . THR A 1 86  ? -58.307 -51.464 54.246  1.000 154.306 ? 415 THR AAA C   1 
ATOM   645   O O   . THR A 1 86  ? -57.104 -51.777 54.200  1.000 153.223 ? 415 THR AAA O   1 
ATOM   646   C CB  . THR A 1 86  ? -59.914 -52.872 52.914  1.000 159.415 ? 415 THR AAA CB  1 
ATOM   647   O OG1 . THR A 1 86  ? -58.967 -53.906 52.639  1.000 163.094 ? 415 THR AAA OG1 1 
ATOM   648   C CG2 . THR A 1 86  ? -61.029 -52.882 51.888  1.000 158.430 ? 415 THR AAA CG2 1 
ATOM   649   N N   . GLY A 1 87  ? -58.952 -51.090 55.352  1.000 154.458 ? 416 GLY AAA N   1 
ATOM   650   C CA  . GLY A 1 87  ? -58.326 -50.886 56.671  1.000 157.066 ? 416 GLY AAA CA  1 
ATOM   651   C C   . GLY A 1 87  ? -59.026 -49.774 57.417  1.000 156.822 ? 416 GLY AAA C   1 
ATOM   652   O O   . GLY A 1 87  ? -60.216 -49.571 57.155  1.000 153.414 ? 416 GLY AAA O   1 
ATOM   653   N N   . LYS A 1 88  ? -58.311 -49.066 58.294  1.000 160.784 ? 417 LYS AAA N   1 
ATOM   654   C CA  . LYS A 1 88  ? -58.888 -48.002 59.160  1.000 163.063 ? 417 LYS AAA CA  1 
ATOM   655   C C   . LYS A 1 88  ? -59.215 -46.794 58.284  1.000 158.982 ? 417 LYS AAA C   1 
ATOM   656   O O   . LYS A 1 88  ? -60.390 -46.406 58.223  1.000 157.665 ? 417 LYS AAA O   1 
ATOM   657   C CB  . LYS A 1 88  ? -57.936 -47.620 60.304  1.000 166.825 ? 417 LYS AAA CB  1 
ATOM   658   C CG  . LYS A 1 88  ? -57.462 -48.780 61.175  1.000 173.145 ? 417 LYS AAA CG  1 
ATOM   659   C CD  . LYS A 1 88  ? -58.589 -49.675 61.693  1.000 177.340 ? 417 LYS AAA CD  1 
ATOM   660   C CE  . LYS A 1 88  ? -58.462 -51.135 61.289  1.000 180.314 ? 417 LYS AAA CE  1 
ATOM   661   N NZ  . LYS A 1 88  ? -59.770 -51.724 60.900  1.000 179.756 ? 417 LYS AAA NZ  1 
ATOM   662   N N   . ILE A 1 89  ? -58.209 -46.257 57.601  1.000 157.996 ? 418 ILE AAA N   1 
ATOM   663   C CA  . ILE A 1 89  ? -58.329 -45.009 56.796  1.000 157.127 ? 418 ILE AAA CA  1 
ATOM   664   C C   . ILE A 1 89  ? -59.227 -45.307 55.598  1.000 157.682 ? 418 ILE AAA C   1 
ATOM   665   O O   . ILE A 1 89  ? -60.181 -44.544 55.364  1.000 157.396 ? 418 ILE AAA O   1 
ATOM   666   C CB  . ILE A 1 89  ? -56.943 -44.497 56.358  1.000 156.651 ? 418 ILE AAA CB  1 
ATOM   667   C CG1 . ILE A 1 89  ? -55.989 -44.339 57.545  1.000 160.296 ? 418 ILE AAA CG1 1 
ATOM   668   C CG2 . ILE A 1 89  ? -57.063 -43.206 55.565  1.000 154.136 ? 418 ILE AAA CG2 1 
ATOM   669   C CD1 . ILE A 1 89  ? -56.549 -43.551 58.702  1.000 161.680 ? 418 ILE AAA CD1 1 
ATOM   670   N N   . ALA A 1 90  ? -58.923 -46.390 54.883  1.000 160.488 ? 419 ALA AAA N   1 
ATOM   671   C CA  . ALA A 1 90  ? -59.644 -46.817 53.664  1.000 160.872 ? 419 ALA AAA CA  1 
ATOM   672   C C   . ALA A 1 90  ? -61.148 -46.825 53.943  1.000 160.133 ? 419 ALA AAA C   1 
ATOM   673   O O   . ALA A 1 90  ? -61.871 -46.115 53.243  1.000 158.896 ? 419 ALA AAA O   1 
ATOM   674   C CB  . ALA A 1 90  ? -59.162 -48.172 53.212  1.000 164.140 ? 419 ALA AAA CB  1 
ATOM   675   N N   . ASP A 1 91  ? -61.579 -47.572 54.960  1.000 161.420 ? 420 ASP AAA N   1 
ATOM   676   C CA  . ASP A 1 91  ? -62.991 -48.002 55.120  1.000 162.150 ? 420 ASP AAA CA  1 
ATOM   677   C C   . ASP A 1 91  ? -63.755 -47.114 56.112  1.000 161.658 ? 420 ASP AAA C   1 
ATOM   678   O O   . ASP A 1 91  ? -64.986 -47.144 56.028  1.000 163.733 ? 420 ASP AAA O   1 
ATOM   679   C CB  . ASP A 1 91  ? -63.059 -49.478 55.514  1.000 165.774 ? 420 ASP AAA CB  1 
ATOM   680   C CG  . ASP A 1 91  ? -62.787 -50.437 54.363  1.000 166.160 ? 420 ASP AAA CG  1 
ATOM   681   O OD1 . ASP A 1 91  ? -63.203 -50.134 53.224  1.000 163.575 ? 420 ASP AAA OD1 1 
ATOM   682   O OD2 . ASP A 1 91  ? -62.163 -51.483 54.614  1.000 168.530 ? 420 ASP AAA OD2 1 
ATOM   683   N N   . TYR A 1 92  ? -63.100 -46.347 56.995  1.000 159.549 ? 421 TYR AAA N   1 
ATOM   684   C CA  . TYR A 1 92  ? -63.794 -45.566 58.064  1.000 158.282 ? 421 TYR AAA CA  1 
ATOM   685   C C   . TYR A 1 92  ? -63.559 -44.047 57.954  1.000 154.749 ? 421 TYR AAA C   1 
ATOM   686   O O   . TYR A 1 92  ? -64.216 -43.310 58.731  1.000 154.026 ? 421 TYR AAA O   1 
ATOM   687   C CB  . TYR A 1 92  ? -63.391 -46.060 59.459  1.000 160.988 ? 421 TYR AAA CB  1 
ATOM   688   C CG  . TYR A 1 92  ? -63.752 -47.489 59.784  1.000 164.441 ? 421 TYR AAA CG  1 
ATOM   689   C CD1 . TYR A 1 92  ? -65.022 -47.987 59.542  1.000 165.647 ? 421 TYR AAA CD1 1 
ATOM   690   C CD2 . TYR A 1 92  ? -62.833 -48.337 60.384  1.000 167.599 ? 421 TYR AAA CD2 1 
ATOM   691   C CE1 . TYR A 1 92  ? -65.357 -49.297 59.844  1.000 168.802 ? 421 TYR AAA CE1 1 
ATOM   692   C CE2 . TYR A 1 92  ? -63.157 -49.648 60.706  1.000 170.518 ? 421 TYR AAA CE2 1 
ATOM   693   C CZ  . TYR A 1 92  ? -64.427 -50.128 60.442  1.000 171.022 ? 421 TYR AAA CZ  1 
ATOM   694   O OH  . TYR A 1 92  ? -64.764 -51.413 60.755  1.000 173.497 ? 421 TYR AAA OH  1 
ATOM   695   N N   . ASN A 1 93  ? -62.710 -43.565 57.032  1.000 151.240 ? 422 ASN AAA N   1 
ATOM   696   C CA  . ASN A 1 93  ? -62.282 -42.136 57.005  1.000 148.561 ? 422 ASN AAA CA  1 
ATOM   697   C C   . ASN A 1 93  ? -62.456 -41.506 55.619  1.000 145.686 ? 422 ASN AAA C   1 
ATOM   698   O O   . ASN A 1 93  ? -63.258 -40.544 55.536  1.000 146.987 ? 422 ASN AAA O   1 
ATOM   699   C CB  . ASN A 1 93  ? -60.851 -41.981 57.506  1.000 147.473 ? 422 ASN AAA CB  1 
ATOM   700   C CG  . ASN A 1 93  ? -60.746 -42.391 58.955  1.000 150.403 ? 422 ASN AAA CG  1 
ATOM   701   O OD1 . ASN A 1 93  ? -60.781 -41.540 59.842  1.000 151.201 ? 422 ASN AAA OD1 1 
ATOM   702   N ND2 . ASN A 1 93  ? -60.682 -43.691 59.201  1.000 152.862 ? 422 ASN AAA ND2 1 
ATOM   703   N N   . TYR A 1 94  ? -61.723 -41.998 54.605  1.000 142.126 ? 423 TYR AAA N   1 
ATOM   704   C CA  . TYR A 1 94  ? -61.729 -41.497 53.200  1.000 138.202 ? 423 TYR AAA CA  1 
ATOM   705   C C   . TYR A 1 94  ? -61.632 -42.671 52.212  1.000 137.064 ? 423 TYR AAA C   1 
ATOM   706   O O   . TYR A 1 94  ? -60.518 -43.178 51.981  1.000 133.228 ? 423 TYR AAA O   1 
ATOM   707   C CB  . TYR A 1 94  ? -60.581 -40.503 52.996  1.000 135.660 ? 423 TYR AAA CB  1 
ATOM   708   C CG  . TYR A 1 94  ? -60.579 -39.809 51.659  1.000 133.202 ? 423 TYR AAA CG  1 
ATOM   709   C CD1 . TYR A 1 94  ? -61.550 -38.876 51.337  1.000 133.351 ? 423 TYR AAA CD1 1 
ATOM   710   C CD2 . TYR A 1 94  ? -59.603 -40.077 50.715  1.000 132.262 ? 423 TYR AAA CD2 1 
ATOM   711   C CE1 . TYR A 1 94  ? -61.556 -38.235 50.108  1.000 132.831 ? 423 TYR AAA CE1 1 
ATOM   712   C CE2 . TYR A 1 94  ? -59.596 -39.449 49.479  1.000 131.454 ? 423 TYR AAA CE2 1 
ATOM   713   C CZ  . TYR A 1 94  ? -60.576 -38.522 49.172  1.000 131.417 ? 423 TYR AAA CZ  1 
ATOM   714   O OH  . TYR A 1 94  ? -60.564 -37.896 47.959  1.000 129.940 ? 423 TYR AAA OH  1 
ATOM   715   N N   . LYS A 1 95  ? -62.766 -43.101 51.648  1.000 139.006 ? 424 LYS AAA N   1 
ATOM   716   C CA  . LYS A 1 95  ? -62.823 -44.211 50.658  1.000 140.892 ? 424 LYS AAA CA  1 
ATOM   717   C C   . LYS A 1 95  ? -62.675 -43.609 49.265  1.000 140.228 ? 424 LYS AAA C   1 
ATOM   718   O O   . LYS A 1 95  ? -63.174 -42.479 49.069  1.000 139.927 ? 424 LYS AAA O   1 
ATOM   719   C CB  . LYS A 1 95  ? -64.144 -44.988 50.735  1.000 143.343 ? 424 LYS AAA CB  1 
ATOM   720   C CG  . LYS A 1 95  ? -64.170 -46.335 50.013  1.000 144.363 ? 424 LYS AAA CG  1 
ATOM   721   C CD  . LYS A 1 95  ? -64.015 -47.538 50.939  1.000 146.807 ? 424 LYS AAA CD  1 
ATOM   722   C CE  . LYS A 1 95  ? -63.934 -48.873 50.228  1.000 147.607 ? 424 LYS AAA CE  1 
ATOM   723   N NZ  . LYS A 1 95  ? -62.547 -49.189 49.813  1.000 146.829 ? 424 LYS AAA NZ  1 
ATOM   724   N N   . LEU A 1 96  ? -62.005 -44.332 48.362  1.000 140.399 ? 425 LEU AAA N   1 
ATOM   725   C CA  . LEU A 1 96  ? -61.960 -44.013 46.911  1.000 140.185 ? 425 LEU AAA CA  1 
ATOM   726   C C   . LEU A 1 96  ? -62.653 -45.130 46.137  1.000 140.500 ? 425 LEU AAA C   1 
ATOM   727   O O   . LEU A 1 96  ? -62.507 -46.305 46.468  1.000 140.913 ? 425 LEU AAA O   1 
ATOM   728   C CB  . LEU A 1 96  ? -60.510 -43.845 46.441  1.000 139.899 ? 425 LEU AAA CB  1 
ATOM   729   C CG  . LEU A 1 96  ? -59.844 -42.494 46.722  1.000 139.301 ? 425 LEU AAA CG  1 
ATOM   730   C CD1 . LEU A 1 96  ? -58.441 -42.491 46.128  1.000 138.872 ? 425 LEU AAA CD1 1 
ATOM   731   C CD2 . LEU A 1 96  ? -60.647 -41.314 46.168  1.000 139.469 ? 425 LEU AAA CD2 1 
ATOM   732   N N   . PRO A 1 97  ? -63.419 -44.781 45.079  1.000 140.048 ? 426 PRO AAA N   1 
ATOM   733   C CA  . PRO A 1 97  ? -64.105 -45.770 44.255  1.000 142.502 ? 426 PRO AAA CA  1 
ATOM   734   C C   . PRO A 1 97  ? -63.149 -46.481 43.289  1.000 144.410 ? 426 PRO AAA C   1 
ATOM   735   O O   . PRO A 1 97  ? -62.125 -45.924 42.959  1.000 143.378 ? 426 PRO AAA O   1 
ATOM   736   C CB  . PRO A 1 97  ? -65.099 -44.924 43.454  1.000 142.414 ? 426 PRO AAA CB  1 
ATOM   737   C CG  . PRO A 1 97  ? -64.388 -43.600 43.300  1.000 140.360 ? 426 PRO AAA CG  1 
ATOM   738   C CD  . PRO A 1 97  ? -63.647 -43.408 44.604  1.000 138.814 ? 426 PRO AAA CD  1 
ATOM   739   N N   . ASP A 1 98  ? -63.554 -47.665 42.831  1.000 150.263 ? 427 ASP AAA N   1 
ATOM   740   C CA  . ASP A 1 98  ? -62.780 -48.557 41.928  1.000 154.015 ? 427 ASP AAA CA  1 
ATOM   741   C C   . ASP A 1 98  ? -62.538 -47.839 40.587  1.000 153.980 ? 427 ASP AAA C   1 
ATOM   742   O O   . ASP A 1 98  ? -61.411 -47.979 40.037  1.000 152.681 ? 427 ASP AAA O   1 
ATOM   743   C CB  . ASP A 1 98  ? -63.505 -49.901 41.774  1.000 158.868 ? 427 ASP AAA CB  1 
ATOM   744   C CG  . ASP A 1 98  ? -64.081 -50.443 43.076  1.000 161.632 ? 427 ASP AAA CG  1 
ATOM   745   O OD1 . ASP A 1 98  ? -63.352 -50.410 44.093  1.000 162.432 ? 427 ASP AAA OD1 1 
ATOM   746   O OD2 . ASP A 1 98  ? -65.264 -50.868 43.072  1.000 163.491 ? 427 ASP AAA OD2 1 
ATOM   747   N N   . ASP A 1 99  ? -63.535 -47.084 40.092  1.000 154.133 ? 428 ASP AAA N   1 
ATOM   748   C CA  . ASP A 1 99  ? -63.458 -46.324 38.813  1.000 152.075 ? 428 ASP AAA CA  1 
ATOM   749   C C   . ASP A 1 99  ? -62.964 -44.906 39.113  1.000 146.850 ? 428 ASP AAA C   1 
ATOM   750   O O   . ASP A 1 99  ? -63.548 -43.939 38.574  1.000 145.334 ? 428 ASP AAA O   1 
ATOM   751   C CB  . ASP A 1 99  ? -64.799 -46.323 38.068  1.000 155.741 ? 428 ASP AAA CB  1 
ATOM   752   C CG  . ASP A 1 99  ? -65.973 -45.730 38.836  1.000 157.697 ? 428 ASP AAA CG  1 
ATOM   753   O OD1 . ASP A 1 99  ? -65.739 -44.938 39.774  1.000 155.394 ? 428 ASP AAA OD1 1 
ATOM   754   O OD2 . ASP A 1 99  ? -67.120 -46.061 38.485  1.000 161.978 ? 428 ASP AAA OD2 1 
ATOM   755   N N   . PHE A 1 100 ? -61.934 -44.788 39.950  1.000 142.342 ? 429 PHE AAA N   1 
ATOM   756   C CA  . PHE A 1 100 ? -61.324 -43.490 40.308  1.000 138.807 ? 429 PHE AAA CA  1 
ATOM   757   C C   . PHE A 1 100 ? -60.503 -43.000 39.116  1.000 138.955 ? 429 PHE AAA C   1 
ATOM   758   O O   . PHE A 1 100 ? -59.741 -43.805 38.549  1.000 139.814 ? 429 PHE AAA O   1 
ATOM   759   C CB  . PHE A 1 100 ? -60.463 -43.623 41.561  1.000 136.086 ? 429 PHE AAA CB  1 
ATOM   760   C CG  . PHE A 1 100 ? -59.760 -42.351 41.939  1.000 134.013 ? 429 PHE AAA CG  1 
ATOM   761   C CD1 . PHE A 1 100 ? -60.468 -41.167 42.068  1.000 134.248 ? 429 PHE AAA CD1 1 
ATOM   762   C CD2 . PHE A 1 100 ? -58.396 -42.341 42.173  1.000 134.078 ? 429 PHE AAA CD2 1 
ATOM   763   C CE1 . PHE A 1 100 ? -59.821 -39.994 42.419  1.000 135.210 ? 429 PHE AAA CE1 1 
ATOM   764   C CE2 . PHE A 1 100 ? -57.749 -41.167 42.524  1.000 134.554 ? 429 PHE AAA CE2 1 
ATOM   765   C CZ  . PHE A 1 100 ? -58.463 -39.996 42.646  1.000 135.102 ? 429 PHE AAA CZ  1 
ATOM   766   N N   . THR A 1 101 ? -60.683 -41.732 38.744  1.000 139.305 ? 430 THR AAA N   1 
ATOM   767   C CA  . THR A 1 101 ? -59.970 -41.067 37.622  1.000 139.698 ? 430 THR AAA CA  1 
ATOM   768   C C   . THR A 1 101 ? -59.378 -39.763 38.147  1.000 135.697 ? 430 THR AAA C   1 
ATOM   769   O O   . THR A 1 101 ? -59.913 -38.681 37.840  1.000 136.902 ? 430 THR AAA O   1 
ATOM   770   C CB  . THR A 1 101 ? -60.885 -40.850 36.415  1.000 144.819 ? 430 THR AAA CB  1 
ATOM   771   O OG1 . THR A 1 101 ? -61.949 -39.991 36.827  1.000 150.356 ? 430 THR AAA OG1 1 
ATOM   772   C CG2 . THR A 1 101 ? -61.427 -42.152 35.870  1.000 147.797 ? 430 THR AAA CG2 1 
ATOM   773   N N   . GLY A 1 102 ? -58.320 -39.888 38.940  1.000 132.086 ? 431 GLY AAA N   1 
ATOM   774   C CA  . GLY A 1 102 ? -57.643 -38.751 39.577  1.000 131.513 ? 431 GLY AAA CA  1 
ATOM   775   C C   . GLY A 1 102 ? -56.263 -39.142 40.049  1.000 131.678 ? 431 GLY AAA C   1 
ATOM   776   O O   . GLY A 1 102 ? -55.772 -40.209 39.623  1.000 130.407 ? 431 GLY AAA O   1 
ATOM   777   N N   . CYS A 1 103 ? -55.651 -38.305 40.887  1.000 133.401 ? 432 CYS AAA N   1 
ATOM   778   C CA  . CYS A 1 103 ? -54.306 -38.554 41.458  1.000 135.201 ? 432 CYS AAA CA  1 
ATOM   779   C C   . CYS A 1 103 ? -54.304 -38.276 42.958  1.000 134.644 ? 432 CYS AAA C   1 
ATOM   780   O O   . CYS A 1 103 ? -55.064 -37.403 43.423  1.000 137.365 ? 432 CYS AAA O   1 
ATOM   781   C CB  . CYS A 1 103 ? -53.241 -37.715 40.767  1.000 137.468 ? 432 CYS AAA CB  1 
ATOM   782   S SG  . CYS A 1 103 ? -53.285 -37.892 38.966  1.000 141.160 ? 432 CYS AAA SG  1 
ATOM   783   N N   . VAL A 1 104 ? -53.456 -39.020 43.657  1.000 131.396 ? 433 VAL AAA N   1 
ATOM   784   C CA  . VAL A 1 104 ? -53.174 -38.890 45.106  1.000 129.523 ? 433 VAL AAA CA  1 
ATOM   785   C C   . VAL A 1 104 ? -51.807 -38.225 45.204  1.000 130.502 ? 433 VAL AAA C   1 
ATOM   786   O O   . VAL A 1 104 ? -50.849 -38.789 44.651  1.000 128.345 ? 433 VAL AAA O   1 
ATOM   787   C CB  . VAL A 1 104 ? -53.210 -40.286 45.747  1.000 129.022 ? 433 VAL AAA CB  1 
ATOM   788   C CG1 . VAL A 1 104 ? -52.630 -40.295 47.147  1.000 131.467 ? 433 VAL AAA CG1 1 
ATOM   789   C CG2 . VAL A 1 104 ? -54.618 -40.851 45.734  1.000 127.519 ? 433 VAL AAA CG2 1 
ATOM   790   N N   . ILE A 1 105 ? -51.741 -37.043 45.814  1.000 134.466 ? 434 ILE AAA N   1 
ATOM   791   C CA  . ILE A 1 105 ? -50.486 -36.246 45.952  1.000 139.742 ? 434 ILE AAA CA  1 
ATOM   792   C C   . ILE A 1 105 ? -50.216 -36.045 47.446  1.000 141.659 ? 434 ILE AAA C   1 
ATOM   793   O O   . ILE A 1 105 ? -51.058 -35.437 48.125  1.000 140.994 ? 434 ILE AAA O   1 
ATOM   794   C CB  . ILE A 1 105 ? -50.581 -34.912 45.182  1.000 140.951 ? 434 ILE AAA CB  1 
ATOM   795   C CG1 . ILE A 1 105 ? -51.139 -35.123 43.771  1.000 140.403 ? 434 ILE AAA CG1 1 
ATOM   796   C CG2 . ILE A 1 105 ? -49.236 -34.182 45.157  1.000 141.339 ? 434 ILE AAA CG2 1 
ATOM   797   C CD1 . ILE A 1 105 ? -51.815 -33.899 43.199  1.000 141.104 ? 434 ILE AAA CD1 1 
ATOM   798   N N   . ALA A 1 106 ? -49.075 -36.545 47.921  1.000 143.432 ? 435 ALA AAA N   1 
ATOM   799   C CA  . ALA A 1 106 ? -48.706 -36.598 49.350  1.000 146.262 ? 435 ALA AAA CA  1 
ATOM   800   C C   . ALA A 1 106 ? -47.248 -36.176 49.531  1.000 148.000 ? 435 ALA AAA C   1 
ATOM   801   O O   . ALA A 1 106 ? -46.379 -36.716 48.832  1.000 147.439 ? 435 ALA AAA O   1 
ATOM   802   C CB  . ALA A 1 106 ? -48.937 -37.991 49.870  1.000 148.047 ? 435 ALA AAA CB  1 
ATOM   803   N N   . TRP A 1 107 ? -47.000 -35.256 50.462  1.000 150.386 ? 436 TRP AAA N   1 
ATOM   804   C CA  . TRP A 1 107 ? -45.633 -34.864 50.888  1.000 154.120 ? 436 TRP AAA CA  1 
ATOM   805   C C   . TRP A 1 107 ? -45.510 -34.971 52.405  1.000 156.594 ? 436 TRP AAA C   1 
ATOM   806   O O   . TRP A 1 107 ? -46.517 -34.738 53.097  1.000 155.023 ? 436 TRP AAA O   1 
ATOM   807   C CB  . TRP A 1 107 ? -45.288 -33.461 50.387  1.000 154.427 ? 436 TRP AAA CB  1 
ATOM   808   C CG  . TRP A 1 107 ? -46.148 -32.363 50.929  1.000 153.680 ? 436 TRP AAA CG  1 
ATOM   809   C CD1 . TRP A 1 107 ? -45.886 -31.580 52.013  1.000 156.759 ? 436 TRP AAA CD1 1 
ATOM   810   C CD2 . TRP A 1 107 ? -47.386 -31.885 50.383  1.000 149.659 ? 436 TRP AAA CD2 1 
ATOM   811   N NE1 . TRP A 1 107 ? -46.879 -30.653 52.181  1.000 155.812 ? 436 TRP AAA NE1 1 
ATOM   812   C CE2 . TRP A 1 107 ? -47.811 -30.815 51.194  1.000 151.235 ? 436 TRP AAA CE2 1 
ATOM   813   C CE3 . TRP A 1 107 ? -48.176 -32.260 49.296  1.000 147.162 ? 436 TRP AAA CE3 1 
ATOM   814   C CZ2 . TRP A 1 107 ? -48.990 -30.120 50.953  1.000 149.969 ? 436 TRP AAA CZ2 1 
ATOM   815   C CZ3 . TRP A 1 107 ? -49.342 -31.573 49.055  1.000 147.424 ? 436 TRP AAA CZ3 1 
ATOM   816   C CH2 . TRP A 1 107 ? -49.742 -30.520 49.876  1.000 148.804 ? 436 TRP AAA CH2 1 
ATOM   817   N N   . ASN A 1 108 ? -44.311 -35.317 52.879  1.000 159.152 ? 437 ASN AAA N   1 
ATOM   818   C CA  . ASN A 1 108 ? -43.964 -35.357 54.321  1.000 162.551 ? 437 ASN AAA CA  1 
ATOM   819   C C   . ASN A 1 108 ? -44.064 -33.927 54.856  1.000 163.041 ? 437 ASN AAA C   1 
ATOM   820   O O   . ASN A 1 108 ? -43.590 -33.007 54.170  1.000 161.665 ? 437 ASN AAA O   1 
ATOM   821   C CB  . ASN A 1 108 ? -42.581 -35.960 54.570  1.000 166.510 ? 437 ASN AAA CB  1 
ATOM   822   C CG  . ASN A 1 108 ? -42.303 -36.202 56.039  1.000 171.213 ? 437 ASN AAA CG  1 
ATOM   823   O OD1 . ASN A 1 108 ? -42.290 -35.267 56.836  1.000 172.577 ? 437 ASN AAA OD1 1 
ATOM   824   N ND2 . ASN A 1 108 ? -42.065 -37.451 56.407  1.000 174.268 ? 437 ASN AAA ND2 1 
ATOM   825   N N   . SER A 1 109 ? -44.682 -33.762 56.026  1.000 165.119 ? 438 SER AAA N   1 
ATOM   826   C CA  . SER A 1 109 ? -44.974 -32.453 56.661  1.000 166.136 ? 438 SER AAA CA  1 
ATOM   827   C C   . SER A 1 109 ? -44.732 -32.542 58.176  1.000 170.020 ? 438 SER AAA C   1 
ATOM   828   O O   . SER A 1 109 ? -45.525 -31.946 58.937  1.000 173.330 ? 438 SER AAA O   1 
ATOM   829   C CB  . SER A 1 109 ? -46.381 -32.006 56.332  1.000 162.883 ? 438 SER AAA CB  1 
ATOM   830   O OG  . SER A 1 109 ? -47.326 -32.993 56.723  1.000 161.377 ? 438 SER AAA OG  1 
ATOM   831   N N   . ASN A 1 110 ? -43.676 -33.253 58.597  1.000 169.723 ? 439 ASN AAA N   1 
ATOM   832   C CA  . ASN A 1 110 ? -43.145 -33.222 59.988  1.000 171.373 ? 439 ASN AAA CA  1 
ATOM   833   C C   . ASN A 1 110 ? -42.876 -31.748 60.319  1.000 172.587 ? 439 ASN AAA C   1 
ATOM   834   O O   . ASN A 1 110 ? -43.410 -31.262 61.329  1.000 172.232 ? 439 ASN AAA O   1 
ATOM   835   C CB  . ASN A 1 110 ? -41.900 -34.111 60.144  1.000 172.856 ? 439 ASN AAA CB  1 
ATOM   836   C CG  . ASN A 1 110 ? -41.711 -34.700 61.529  1.000 176.172 ? 439 ASN AAA CG  1 
ATOM   837   O OD1 . ASN A 1 110 ? -42.666 -34.904 62.274  1.000 176.146 ? 439 ASN AAA OD1 1 
ATOM   838   N ND2 . ASN A 1 110 ? -40.474 -35.013 61.877  1.000 178.632 ? 439 ASN AAA ND2 1 
ATOM   839   N N   . ASN A 1 111 ? -42.164 -31.059 59.417  1.000 173.062 ? 440 ASN AAA N   1 
ATOM   840   C CA  . ASN A 1 111 ? -41.713 -29.642 59.519  1.000 175.878 ? 440 ASN AAA CA  1 
ATOM   841   C C   . ASN A 1 111 ? -42.867 -28.694 59.896  1.000 174.408 ? 440 ASN AAA C   1 
ATOM   842   O O   . ASN A 1 111 ? -42.558 -27.601 60.400  1.000 176.994 ? 440 ASN AAA O   1 
ATOM   843   C CB  . ASN A 1 111 ? -40.995 -29.175 58.237  1.000 175.479 ? 440 ASN AAA CB  1 
ATOM   844   C CG  . ASN A 1 111 ? -41.809 -29.258 56.954  1.000 170.878 ? 440 ASN AAA CG  1 
ATOM   845   O OD1 . ASN A 1 111 ? -42.198 -30.335 56.518  1.000 167.588 ? 440 ASN AAA OD1 1 
ATOM   846   N ND2 . ASN A 1 111 ? -42.021 -28.131 56.291  1.000 169.687 ? 440 ASN AAA ND2 1 
ATOM   847   N N   . LEU A 1 112 ? -44.131 -29.074 59.672  1.000 171.053 ? 441 LEU AAA N   1 
ATOM   848   C CA  . LEU A 1 112 ? -45.304 -28.161 59.792  1.000 170.362 ? 441 LEU AAA CA  1 
ATOM   849   C C   . LEU A 1 112 ? -46.308 -28.651 60.846  1.000 171.018 ? 441 LEU AAA C   1 
ATOM   850   O O   . LEU A 1 112 ? -46.927 -27.783 61.484  1.000 172.369 ? 441 LEU AAA O   1 
ATOM   851   C CB  . LEU A 1 112 ? -45.980 -28.045 58.421  1.000 166.464 ? 441 LEU AAA CB  1 
ATOM   852   C CG  . LEU A 1 112 ? -45.123 -27.423 57.317  1.000 165.648 ? 441 LEU AAA CG  1 
ATOM   853   C CD1 . LEU A 1 112 ? -45.724 -27.693 55.943  1.000 161.582 ? 441 LEU AAA CD1 1 
ATOM   854   C CD2 . LEU A 1 112 ? -44.932 -25.928 57.547  1.000 166.756 ? 441 LEU AAA CD2 1 
ATOM   855   N N   . ASP A 1 113 ? -46.478 -29.967 61.020  1.000 171.005 ? 442 ASP AAA N   1 
ATOM   856   C CA  . ASP A 1 113 ? -47.645 -30.556 61.736  1.000 172.257 ? 442 ASP AAA CA  1 
ATOM   857   C C   . ASP A 1 113 ? -47.202 -31.368 62.966  1.000 176.896 ? 442 ASP AAA C   1 
ATOM   858   O O   . ASP A 1 113 ? -48.018 -32.198 63.427  1.000 175.779 ? 442 ASP AAA O   1 
ATOM   859   C CB  . ASP A 1 113 ? -48.472 -31.423 60.778  1.000 169.085 ? 442 ASP AAA CB  1 
ATOM   860   C CG  . ASP A 1 113 ? -49.036 -30.676 59.580  1.000 165.733 ? 442 ASP AAA CG  1 
ATOM   861   O OD1 . ASP A 1 113 ? -49.711 -29.653 59.803  1.000 166.710 ? 442 ASP AAA OD1 1 
ATOM   862   O OD2 . ASP A 1 113 ? -48.816 -31.133 58.436  1.000 162.043 ? 442 ASP AAA OD2 1 
ATOM   863   N N   . SER A 1 114 ? -45.996 -31.127 63.503  1.000 183.062 ? 443 SER AAA N   1 
ATOM   864   C CA  . SER A 1 114 ? -45.400 -31.883 64.643  1.000 189.182 ? 443 SER AAA CA  1 
ATOM   865   C C   . SER A 1 114 ? -44.840 -30.931 65.708  1.000 193.246 ? 443 SER AAA C   1 
ATOM   866   O O   . SER A 1 114 ? -43.900 -30.163 65.393  1.000 195.109 ? 443 SER AAA O   1 
ATOM   867   C CB  . SER A 1 114 ? -44.318 -32.825 64.175  1.000 191.758 ? 443 SER AAA CB  1 
ATOM   868   O OG  . SER A 1 114 ? -44.813 -33.738 63.209  1.000 189.895 ? 443 SER AAA OG  1 
ATOM   869   N N   . LYS A 1 115 ? -45.359 -31.022 66.935  1.000 194.810 ? 444 LYS AAA N   1 
ATOM   870   C CA  . LYS A 1 115 ? -44.880 -30.234 68.100  1.000 200.209 ? 444 LYS AAA CA  1 
ATOM   871   C C   . LYS A 1 115 ? -44.023 -31.123 69.005  1.000 202.807 ? 444 LYS AAA C   1 
ATOM   872   O O   . LYS A 1 115 ? -44.219 -32.358 68.992  1.000 201.131 ? 444 LYS AAA O   1 
ATOM   873   C CB  . LYS A 1 115 ? -46.068 -29.677 68.888  1.000 202.933 ? 444 LYS AAA CB  1 
ATOM   874   C CG  . LYS A 1 115 ? -47.058 -28.853 68.079  1.000 200.351 ? 444 LYS AAA CG  1 
ATOM   875   C CD  . LYS A 1 115 ? -48.326 -28.542 68.852  1.000 202.383 ? 444 LYS AAA CD  1 
ATOM   876   C CE  . LYS A 1 115 ? -49.419 -27.930 68.000  1.000 199.118 ? 444 LYS AAA CE  1 
ATOM   877   N NZ  . LYS A 1 115 ? -50.762 -28.195 68.571  1.000 199.172 ? 444 LYS AAA NZ  1 
ATOM   878   N N   . VAL A 1 116 ? -43.128 -30.501 69.776  1.000 205.928 ? 445 VAL AAA N   1 
ATOM   879   C CA  . VAL A 1 116 ? -42.313 -31.174 70.831  1.000 210.653 ? 445 VAL AAA CA  1 
ATOM   880   C C   . VAL A 1 116 ? -43.274 -31.894 71.793  1.000 211.845 ? 445 VAL AAA C   1 
ATOM   881   O O   . VAL A 1 116 ? -43.041 -33.083 72.064  1.000 213.031 ? 445 VAL AAA O   1 
ATOM   882   C CB  . VAL A 1 116 ? -41.361 -30.191 71.548  1.000 215.188 ? 445 VAL AAA CB  1 
ATOM   883   C CG1 . VAL A 1 116 ? -40.308 -29.634 70.600  1.000 213.691 ? 445 VAL AAA CG1 1 
ATOM   884   C CG2 . VAL A 1 116 ? -42.093 -29.056 72.251  1.000 216.733 ? 445 VAL AAA CG2 1 
ATOM   885   N N   . GLY A 1 117 ? -44.351 -31.228 72.230  1.000 211.732 ? 446 GLY AAA N   1 
ATOM   886   C CA  . GLY A 1 117 ? -45.373 -31.790 73.142  1.000 212.989 ? 446 GLY AAA CA  1 
ATOM   887   C C   . GLY A 1 117 ? -46.255 -32.830 72.465  1.000 208.623 ? 446 GLY AAA C   1 
ATOM   888   O O   . GLY A 1 117 ? -46.981 -33.545 73.192  1.000 207.279 ? 446 GLY AAA O   1 
ATOM   889   N N   . GLY A 1 118 ? -46.202 -32.895 71.126  1.000 206.021 ? 447 GLY AAA N   1 
ATOM   890   C CA  . GLY A 1 118 ? -46.982 -33.802 70.255  1.000 202.747 ? 447 GLY AAA CA  1 
ATOM   891   C C   . GLY A 1 118 ? -48.243 -33.132 69.728  1.000 199.629 ? 447 GLY AAA C   1 
ATOM   892   O O   . GLY A 1 118 ? -49.098 -32.791 70.566  1.000 202.303 ? 447 GLY AAA O   1 
ATOM   893   N N   . ASN A 1 119 ? -48.372 -32.951 68.403  1.000 195.037 ? 448 ASN AAA N   1 
ATOM   894   C CA  . ASN A 1 119 ? -49.550 -32.288 67.770  1.000 191.204 ? 448 ASN AAA CA  1 
ATOM   895   C C   . ASN A 1 119 ? -50.711 -33.287 67.715  1.000 189.532 ? 448 ASN AAA C   1 
ATOM   896   O O   . ASN A 1 119 ? -50.812 -34.049 66.733  1.000 185.561 ? 448 ASN AAA O   1 
ATOM   897   C CB  . ASN A 1 119 ? -49.244 -31.710 66.382  1.000 187.623 ? 448 ASN AAA CB  1 
ATOM   898   C CG  . ASN A 1 119 ? -50.330 -30.787 65.854  1.000 184.157 ? 448 ASN AAA CG  1 
ATOM   899   O OD1 . ASN A 1 119 ? -51.465 -30.808 66.328  1.000 182.594 ? 448 ASN AAA OD1 1 
ATOM   900   N ND2 . ASN A 1 119 ? -49.993 -29.964 64.872  1.000 181.118 ? 448 ASN AAA ND2 1 
ATOM   901   N N   . TYR A 1 120 ? -51.575 -33.255 68.731  1.000 193.875 ? 449 TYR AAA N   1 
ATOM   902   C CA  . TYR A 1 120 ? -52.717 -34.188 68.909  1.000 195.607 ? 449 TYR AAA CA  1 
ATOM   903   C C   . TYR A 1 120 ? -53.957 -33.653 68.152  1.000 191.899 ? 449 TYR AAA C   1 
ATOM   904   O O   . TYR A 1 120 ? -55.004 -34.340 68.166  1.000 191.486 ? 449 TYR AAA O   1 
ATOM   905   C CB  . TYR A 1 120 ? -52.980 -34.424 70.406  1.000 201.800 ? 449 TYR AAA CB  1 
ATOM   906   C CG  . TYR A 1 120 ? -51.860 -35.044 71.223  1.000 206.125 ? 449 TYR AAA CG  1 
ATOM   907   C CD1 . TYR A 1 120 ? -51.470 -36.363 71.034  1.000 205.021 ? 449 TYR AAA CD1 1 
ATOM   908   C CD2 . TYR A 1 120 ? -51.224 -34.333 72.234  1.000 211.222 ? 449 TYR AAA CD2 1 
ATOM   909   C CE1 . TYR A 1 120 ? -50.458 -36.942 71.787  1.000 208.667 ? 449 TYR AAA CE1 1 
ATOM   910   C CE2 . TYR A 1 120 ? -50.208 -34.894 72.994  1.000 215.062 ? 449 TYR AAA CE2 1 
ATOM   911   C CZ  . TYR A 1 120 ? -49.824 -36.204 72.771  1.000 214.225 ? 449 TYR AAA CZ  1 
ATOM   912   O OH  . TYR A 1 120 ? -48.830 -36.763 73.519  1.000 219.166 ? 449 TYR AAA OH  1 
ATOM   913   N N   . ASN A 1 121 ? -53.854 -32.491 67.484  1.000 188.686 ? 450 ASN AAA N   1 
ATOM   914   C CA  . ASN A 1 121 ? -55.004 -31.742 66.891  1.000 183.739 ? 450 ASN AAA CA  1 
ATOM   915   C C   . ASN A 1 121 ? -55.425 -32.332 65.535  1.000 175.251 ? 450 ASN AAA C   1 
ATOM   916   O O   . ASN A 1 121 ? -56.459 -31.881 64.995  1.000 167.569 ? 450 ASN AAA O   1 
ATOM   917   C CB  . ASN A 1 121 ? -54.701 -30.249 66.723  1.000 186.031 ? 450 ASN AAA CB  1 
ATOM   918   C CG  . ASN A 1 121 ? -54.493 -29.518 68.034  1.000 191.789 ? 450 ASN AAA CG  1 
ATOM   919   O OD1 . ASN A 1 121 ? -53.357 -29.285 68.445  1.000 195.728 ? 450 ASN AAA OD1 1 
ATOM   920   N ND2 . ASN A 1 121 ? -55.579 -29.139 68.693  1.000 192.029 ? 450 ASN AAA ND2 1 
ATOM   921   N N   . TYR A 1 122 ? -54.646 -33.266 64.984  1.000 173.670 ? 451 TYR AAA N   1 
ATOM   922   C CA  . TYR A 1 122 ? -55.008 -34.061 63.780  1.000 169.875 ? 451 TYR AAA CA  1 
ATOM   923   C C   . TYR A 1 122 ? -55.560 -35.406 64.244  1.000 168.921 ? 451 TYR AAA C   1 
ATOM   924   O O   . TYR A 1 122 ? -54.899 -36.059 65.080  1.000 171.418 ? 451 TYR AAA O   1 
ATOM   925   C CB  . TYR A 1 122 ? -53.815 -34.243 62.841  1.000 169.762 ? 451 TYR AAA CB  1 
ATOM   926   C CG  . TYR A 1 122 ? -53.513 -33.019 62.018  1.000 169.776 ? 451 TYR AAA CG  1 
ATOM   927   C CD1 . TYR A 1 122 ? -54.256 -32.719 60.887  1.000 166.469 ? 451 TYR AAA CD1 1 
ATOM   928   C CD2 . TYR A 1 122 ? -52.507 -32.141 62.391  1.000 173.191 ? 451 TYR AAA CD2 1 
ATOM   929   C CE1 . TYR A 1 122 ? -53.993 -31.586 60.135  1.000 165.607 ? 451 TYR AAA CE1 1 
ATOM   930   C CE2 . TYR A 1 122 ? -52.237 -30.999 61.655  1.000 171.880 ? 451 TYR AAA CE2 1 
ATOM   931   C CZ  . TYR A 1 122 ? -52.981 -30.723 60.521  1.000 168.013 ? 451 TYR AAA CZ  1 
ATOM   932   O OH  . TYR A 1 122 ? -52.717 -29.602 59.794  1.000 166.903 ? 451 TYR AAA OH  1 
ATOM   933   N N   . LEU A 1 123 ? -56.720 -35.791 63.703  1.000 163.997 ? 452 LEU AAA N   1 
ATOM   934   C CA  . LEU A 1 123 ? -57.562 -36.899 64.226  1.000 162.604 ? 452 LEU AAA CA  1 
ATOM   935   C C   . LEU A 1 123 ? -57.857 -37.902 63.118  1.000 157.303 ? 452 LEU AAA C   1 
ATOM   936   O O   . LEU A 1 123 ? -57.516 -37.608 61.953  1.000 155.894 ? 452 LEU AAA O   1 
ATOM   937   C CB  . LEU A 1 123 ? -58.871 -36.319 64.761  1.000 163.417 ? 452 LEU AAA CB  1 
ATOM   938   C CG  . LEU A 1 123 ? -58.719 -35.096 65.660  1.000 165.654 ? 452 LEU AAA CG  1 
ATOM   939   C CD1 . LEU A 1 123 ? -60.087 -34.501 65.958  1.000 165.582 ? 452 LEU AAA CD1 1 
ATOM   940   C CD2 . LEU A 1 123 ? -57.973 -35.451 66.940  1.000 168.968 ? 452 LEU AAA CD2 1 
ATOM   941   N N   . TYR A 1 124 ? -58.493 -39.016 63.496  1.000 155.212 ? 453 TYR AAA N   1 
ATOM   942   C CA  . TYR A 1 124 ? -58.874 -40.140 62.603  1.000 153.869 ? 453 TYR AAA CA  1 
ATOM   943   C C   . TYR A 1 124 ? -59.923 -41.013 63.294  1.000 154.890 ? 453 TYR AAA C   1 
ATOM   944   O O   . TYR A 1 124 ? -59.791 -41.252 64.493  1.000 156.568 ? 453 TYR AAA O   1 
ATOM   945   C CB  . TYR A 1 124 ? -57.632 -40.939 62.191  1.000 154.963 ? 453 TYR AAA CB  1 
ATOM   946   C CG  . TYR A 1 124 ? -57.083 -41.908 63.210  1.000 158.834 ? 453 TYR AAA CG  1 
ATOM   947   C CD1 . TYR A 1 124 ? -56.325 -41.461 64.280  1.000 162.548 ? 453 TYR AAA CD1 1 
ATOM   948   C CD2 . TYR A 1 124 ? -57.283 -43.276 63.083  1.000 159.849 ? 453 TYR AAA CD2 1 
ATOM   949   C CE1 . TYR A 1 124 ? -55.804 -42.341 65.215  1.000 166.595 ? 453 TYR AAA CE1 1 
ATOM   950   C CE2 . TYR A 1 124 ? -56.763 -44.171 64.005  1.000 164.273 ? 453 TYR AAA CE2 1 
ATOM   951   C CZ  . TYR A 1 124 ? -56.022 -43.700 65.079  1.000 167.604 ? 453 TYR AAA CZ  1 
ATOM   952   O OH  . TYR A 1 124 ? -55.498 -44.551 66.012  1.000 170.442 ? 453 TYR AAA OH  1 
ATOM   953   N N   . ARG A 1 125 ? -60.933 -41.462 62.544  1.000 156.575 ? 454 ARG AAA N   1 
ATOM   954   C CA  . ARG A 1 125 ? -62.009 -42.373 63.020  1.000 162.029 ? 454 ARG AAA CA  1 
ATOM   955   C C   . ARG A 1 125 ? -61.444 -43.794 63.124  1.000 165.229 ? 454 ARG AAA C   1 
ATOM   956   O O   . ARG A 1 125 ? -60.480 -44.114 62.397  1.000 163.779 ? 454 ARG AAA O   1 
ATOM   957   C CB  . ARG A 1 125 ? -63.224 -42.331 62.084  1.000 162.641 ? 454 ARG AAA CB  1 
ATOM   958   C CG  . ARG A 1 125 ? -64.439 -43.098 62.590  1.000 165.580 ? 454 ARG AAA CG  1 
ATOM   959   C CD  . ARG A 1 125 ? -65.652 -42.925 61.695  1.000 165.042 ? 454 ARG AAA CD  1 
ATOM   960   N NE  . ARG A 1 125 ? -66.118 -41.545 61.673  1.000 163.742 ? 454 ARG AAA NE  1 
ATOM   961   C CZ  . ARG A 1 125 ? -66.930 -41.000 62.579  1.000 164.107 ? 454 ARG AAA CZ  1 
ATOM   962   N NH1 . ARG A 1 125 ? -67.388 -41.717 63.594  1.000 165.272 ? 454 ARG AAA NH1 1 
ATOM   963   N NH2 . ARG A 1 125 ? -67.294 -39.732 62.457  1.000 163.894 ? 454 ARG AAA NH2 1 
ATOM   964   N N   . LEU A 1 126 ? -62.040 -44.607 63.999  1.000 170.491 ? 455 LEU AAA N   1 
ATOM   965   C CA  . LEU A 1 126 ? -61.496 -45.924 64.421  1.000 174.405 ? 455 LEU AAA CA  1 
ATOM   966   C C   . LEU A 1 126 ? -62.539 -47.038 64.254  1.000 175.766 ? 455 LEU AAA C   1 
ATOM   967   O O   . LEU A 1 126 ? -62.125 -48.175 63.938  1.000 176.863 ? 455 LEU AAA O   1 
ATOM   968   C CB  . LEU A 1 126 ? -61.063 -45.796 65.883  1.000 178.066 ? 455 LEU AAA CB  1 
ATOM   969   C CG  . LEU A 1 126 ? -59.982 -46.774 66.331  1.000 180.196 ? 455 LEU AAA CG  1 
ATOM   970   C CD1 . LEU A 1 126 ? -58.785 -46.727 65.391  1.000 177.822 ? 455 LEU AAA CD1 1 
ATOM   971   C CD2 . LEU A 1 126 ? -59.561 -46.476 67.760  1.000 183.404 ? 455 LEU AAA CD2 1 
ATOM   972   N N   . PHE A 1 127 ? -63.821 -46.733 64.498  1.000 175.460 ? 456 PHE AAA N   1 
ATOM   973   C CA  . PHE A 1 127 ? -64.971 -47.670 64.378  1.000 176.020 ? 456 PHE AAA CA  1 
ATOM   974   C C   . PHE A 1 127 ? -66.086 -47.046 63.542  1.000 172.618 ? 456 PHE AAA C   1 
ATOM   975   O O   . PHE A 1 127 ? -66.127 -45.814 63.338  1.000 169.448 ? 456 PHE AAA O   1 
ATOM   976   C CB  . PHE A 1 127 ? -65.563 -48.037 65.741  1.000 180.046 ? 456 PHE AAA CB  1 
ATOM   977   C CG  . PHE A 1 127 ? -64.525 -48.294 66.800  1.000 182.959 ? 456 PHE AAA CG  1 
ATOM   978   C CD1 . PHE A 1 127 ? -63.654 -49.366 66.689  1.000 183.541 ? 456 PHE AAA CD1 1 
ATOM   979   C CD2 . PHE A 1 127 ? -64.401 -47.445 67.890  1.000 185.176 ? 456 PHE AAA CD2 1 
ATOM   980   C CE1 . PHE A 1 127 ? -62.687 -49.592 67.654  1.000 186.270 ? 456 PHE AAA CE1 1 
ATOM   981   C CE2 . PHE A 1 127 ? -63.434 -47.674 68.857  1.000 188.168 ? 456 PHE AAA CE2 1 
ATOM   982   C CZ  . PHE A 1 127 ? -62.581 -48.747 68.735  1.000 188.956 ? 456 PHE AAA CZ  1 
ATOM   983   N N   . ARG A 1 128 ? -66.992 -47.914 63.106  1.000 172.241 ? 457 ARG AAA N   1 
ATOM   984   C CA  . ARG A 1 128 ? -68.185 -47.535 62.322  1.000 170.597 ? 457 ARG AAA CA  1 
ATOM   985   C C   . ARG A 1 128 ? -69.005 -48.798 62.074  1.000 172.887 ? 457 ARG AAA C   1 
ATOM   986   O O   . ARG A 1 128 ? -68.390 -49.856 61.804  1.000 173.137 ? 457 ARG AAA O   1 
ATOM   987   C CB  . ARG A 1 128 ? -67.742 -46.887 61.013  1.000 168.086 ? 457 ARG AAA CB  1 
ATOM   988   C CG  . ARG A 1 128 ? -68.651 -45.765 60.545  1.000 168.142 ? 457 ARG AAA CG  1 
ATOM   989   C CD  . ARG A 1 128 ? -68.005 -44.964 59.429  1.000 165.455 ? 457 ARG AAA CD  1 
ATOM   990   N NE  . ARG A 1 128 ? -69.005 -44.163 58.739  1.000 164.858 ? 457 ARG AAA NE  1 
ATOM   991   C CZ  . ARG A 1 128 ? -69.856 -44.623 57.824  1.000 165.978 ? 457 ARG AAA CZ  1 
ATOM   992   N NH1 . ARG A 1 128 ? -69.825 -45.896 57.445  1.000 167.033 ? 457 ARG AAA NH1 1 
ATOM   993   N NH2 . ARG A 1 128 ? -70.728 -43.793 57.275  1.000 166.331 ? 457 ARG AAA NH2 1 
ATOM   994   N N   . LYS A 1 129 ? -70.332 -48.683 62.161  1.000 174.963 ? 458 LYS AAA N   1 
ATOM   995   C CA  . LYS A 1 129 ? -71.266 -49.832 62.005  1.000 178.208 ? 458 LYS AAA CA  1 
ATOM   996   C C   . LYS A 1 129 ? -70.992 -50.484 60.642  1.000 177.237 ? 458 LYS AAA C   1 
ATOM   997   O O   . LYS A 1 129 ? -70.996 -51.725 60.594  1.000 180.800 ? 458 LYS AAA O   1 
ATOM   998   C CB  . LYS A 1 129 ? -72.724 -49.408 62.239  1.000 179.491 ? 458 LYS AAA CB  1 
ATOM   999   C CG  . LYS A 1 129 ? -73.021 -48.907 63.651  1.000 181.706 ? 458 LYS AAA CG  1 
ATOM   1000  C CD  . LYS A 1 129 ? -74.322 -49.397 64.279  1.000 184.606 ? 458 LYS AAA CD  1 
ATOM   1001  C CE  . LYS A 1 129 ? -74.457 -48.966 65.728  1.000 186.150 ? 458 LYS AAA CE  1 
ATOM   1002  N NZ  . LYS A 1 129 ? -75.504 -49.718 66.464  1.000 189.343 ? 458 LYS AAA NZ  1 
ATOM   1003  N N   . SER A 1 130 ? -70.690 -49.695 59.601  1.000 173.744 ? 459 SER AAA N   1 
ATOM   1004  C CA  . SER A 1 130 ? -70.354 -50.185 58.237  1.000 171.118 ? 459 SER AAA CA  1 
ATOM   1005  C C   . SER A 1 130 ? -69.180 -49.394 57.648  1.000 165.433 ? 459 SER AAA C   1 
ATOM   1006  O O   . SER A 1 130 ? -68.718 -48.446 58.300  1.000 164.015 ? 459 SER AAA O   1 
ATOM   1007  C CB  . SER A 1 130 ? -71.558 -50.113 57.332  1.000 172.842 ? 459 SER AAA CB  1 
ATOM   1008  O OG  . SER A 1 130 ? -71.702 -48.811 56.780  1.000 171.610 ? 459 SER AAA OG  1 
ATOM   1009  N N   . ASN A 1 131 ? -68.743 -49.776 56.445  1.000 161.737 ? 460 ASN AAA N   1 
ATOM   1010  C CA  . ASN A 1 131 ? -67.670 -49.094 55.676  1.000 156.057 ? 460 ASN AAA CA  1 
ATOM   1011  C C   . ASN A 1 131 ? -68.266 -47.854 54.996  1.000 152.514 ? 460 ASN AAA C   1 
ATOM   1012  O O   . ASN A 1 131 ? -69.472 -47.864 54.699  1.000 152.956 ? 460 ASN AAA O   1 
ATOM   1013  C CB  . ASN A 1 131 ? -67.015 -50.049 54.674  1.000 154.792 ? 460 ASN AAA CB  1 
ATOM   1014  C CG  . ASN A 1 131 ? -66.460 -51.297 55.327  1.000 155.840 ? 460 ASN AAA CG  1 
ATOM   1015  O OD1 . ASN A 1 131 ? -65.635 -51.219 56.238  1.000 154.496 ? 460 ASN AAA OD1 1 
ATOM   1016  N ND2 . ASN A 1 131 ? -66.895 -52.453 54.858  1.000 156.375 ? 460 ASN AAA ND2 1 
ATOM   1017  N N   . LEU A 1 132 ? -67.447 -46.821 54.784  1.000 149.381 ? 461 LEU AAA N   1 
ATOM   1018  C CA  . LEU A 1 132 ? -67.825 -45.582 54.057  1.000 148.362 ? 461 LEU AAA CA  1 
ATOM   1019  C C   . LEU A 1 132 ? -68.139 -45.933 52.603  1.000 149.342 ? 461 LEU AAA C   1 
ATOM   1020  O O   . LEU A 1 132 ? -67.418 -46.775 52.031  1.000 148.956 ? 461 LEU AAA O   1 
ATOM   1021  C CB  . LEU A 1 132 ? -66.672 -44.575 54.096  1.000 146.910 ? 461 LEU AAA CB  1 
ATOM   1022  C CG  . LEU A 1 132 ? -66.463 -43.810 55.402  1.000 148.308 ? 461 LEU AAA CG  1 
ATOM   1023  C CD1 . LEU A 1 132 ? -65.257 -42.899 55.295  1.000 146.372 ? 461 LEU AAA CD1 1 
ATOM   1024  C CD2 . LEU A 1 132 ? -67.678 -42.980 55.771  1.000 150.323 ? 461 LEU AAA CD2 1 
ATOM   1025  N N   . LYS A 1 133 ? -69.157 -45.286 52.030  1.000 151.888 ? 462 LYS AAA N   1 
ATOM   1026  C CA  . LYS A 1 133 ? -69.363 -45.222 50.561  1.000 153.872 ? 462 LYS AAA CA  1 
ATOM   1027  C C   . LYS A 1 133 ? -68.232 -44.383 49.966  1.000 151.211 ? 462 LYS AAA C   1 
ATOM   1028  O O   . LYS A 1 133 ? -67.656 -43.545 50.659  1.000 150.877 ? 462 LYS AAA O   1 
ATOM   1029  C CB  . LYS A 1 133 ? -70.744 -44.640 50.216  1.000 157.876 ? 462 LYS AAA CB  1 
ATOM   1030  C CG  . LYS A 1 133 ? -71.838 -45.646 49.857  1.000 161.712 ? 462 LYS AAA CG  1 
ATOM   1031  C CD  . LYS A 1 133 ? -72.753 -45.171 48.720  1.000 163.585 ? 462 LYS AAA CD  1 
ATOM   1032  C CE  . LYS A 1 133 ? -73.610 -46.263 48.117  1.000 167.426 ? 462 LYS AAA CE  1 
ATOM   1033  N NZ  . LYS A 1 133 ? -74.817 -46.516 48.940  1.000 171.994 ? 462 LYS AAA NZ  1 
ATOM   1034  N N   . PRO A 1 134 ? -67.871 -44.581 48.677  1.000 149.696 ? 463 PRO AAA N   1 
ATOM   1035  C CA  . PRO A 1 134 ? -66.843 -43.765 48.031  1.000 146.289 ? 463 PRO AAA CA  1 
ATOM   1036  C C   . PRO A 1 134 ? -67.108 -42.262 48.190  1.000 144.121 ? 463 PRO AAA C   1 
ATOM   1037  O O   . PRO A 1 134 ? -68.233 -41.849 47.998  1.000 141.245 ? 463 PRO AAA O   1 
ATOM   1038  C CB  . PRO A 1 134 ? -66.918 -44.172 46.552  1.000 146.727 ? 463 PRO AAA CB  1 
ATOM   1039  C CG  . PRO A 1 134 ? -67.501 -45.570 46.573  1.000 148.923 ? 463 PRO AAA CG  1 
ATOM   1040  C CD  . PRO A 1 134 ? -68.430 -45.595 47.769  1.000 150.951 ? 463 PRO AAA CD  1 
ATOM   1041  N N   . PHE A 1 135 ? -66.074 -41.498 48.553  1.000 143.965 ? 464 PHE AAA N   1 
ATOM   1042  C CA  . PHE A 1 135 ? -66.132 -40.026 48.740  1.000 145.389 ? 464 PHE AAA CA  1 
ATOM   1043  C C   . PHE A 1 135 ? -67.181 -39.666 49.797  1.000 146.516 ? 464 PHE AAA C   1 
ATOM   1044  O O   . PHE A 1 135 ? -67.846 -38.625 49.646  1.000 145.676 ? 464 PHE AAA O   1 
ATOM   1045  C CB  . PHE A 1 135 ? -66.488 -39.321 47.427  1.000 147.729 ? 464 PHE AAA CB  1 
ATOM   1046  C CG  . PHE A 1 135 ? -65.471 -39.427 46.319  1.000 148.309 ? 464 PHE AAA CG  1 
ATOM   1047  C CD1 . PHE A 1 135 ? -64.138 -39.108 46.540  1.000 147.535 ? 464 PHE AAA CD1 1 
ATOM   1048  C CD2 . PHE A 1 135 ? -65.858 -39.792 45.040  1.000 149.836 ? 464 PHE AAA CD2 1 
ATOM   1049  C CE1 . PHE A 1 135 ? -63.206 -39.182 45.516  1.000 146.407 ? 464 PHE AAA CE1 1 
ATOM   1050  C CE2 . PHE A 1 135 ? -64.925 -39.864 44.016  1.000 150.168 ? 464 PHE AAA CE2 1 
ATOM   1051  C CZ  . PHE A 1 135 ? -63.601 -39.567 44.256  1.000 148.055 ? 464 PHE AAA CZ  1 
ATOM   1052  N N   . GLU A 1 136 ? -67.354 -40.495 50.826  1.000 148.586 ? 465 GLU AAA N   1 
ATOM   1053  C CA  . GLU A 1 136 ? -68.247 -40.151 51.964  1.000 151.676 ? 465 GLU AAA CA  1 
ATOM   1054  C C   . GLU A 1 136 ? -67.405 -39.418 53.011  1.000 151.789 ? 465 GLU AAA C   1 
ATOM   1055  O O   . GLU A 1 136 ? -66.195 -39.702 53.087  1.000 150.321 ? 465 GLU AAA O   1 
ATOM   1056  C CB  . GLU A 1 136 ? -68.950 -41.379 52.547  1.000 154.533 ? 465 GLU AAA CB  1 
ATOM   1057  C CG  . GLU A 1 136 ? -69.962 -41.019 53.631  1.000 157.293 ? 465 GLU AAA CG  1 
ATOM   1058  C CD  . GLU A 1 136 ? -70.958 -42.100 54.038  1.000 159.732 ? 465 GLU AAA CD  1 
ATOM   1059  O OE1 . GLU A 1 136 ? -70.832 -43.246 53.557  1.000 160.280 ? 465 GLU AAA OE1 1 
ATOM   1060  O OE2 . GLU A 1 136 ? -71.872 -41.791 54.839  1.000 159.610 ? 465 GLU AAA OE2 1 
ATOM   1061  N N   . ARG A 1 137 ? -68.036 -38.505 53.753  1.000 154.697 ? 466 ARG AAA N   1 
ATOM   1062  C CA  . ARG A 1 137 ? -67.389 -37.579 54.721  1.000 157.818 ? 466 ARG AAA CA  1 
ATOM   1063  C C   . ARG A 1 137 ? -68.173 -37.623 56.034  1.000 161.262 ? 466 ARG AAA C   1 
ATOM   1064  O O   . ARG A 1 137 ? -69.049 -36.748 56.234  1.000 161.411 ? 466 ARG AAA O   1 
ATOM   1065  C CB  . ARG A 1 137 ? -67.336 -36.166 54.130  1.000 160.014 ? 466 ARG AAA CB  1 
ATOM   1066  C CG  . ARG A 1 137 ? -66.543 -35.161 54.954  1.000 163.534 ? 466 ARG AAA CG  1 
ATOM   1067  C CD  . ARG A 1 137 ? -66.486 -33.791 54.298  1.000 166.505 ? 466 ARG AAA CD  1 
ATOM   1068  N NE  . ARG A 1 137 ? -65.845 -32.791 55.149  1.000 170.625 ? 466 ARG AAA NE  1 
ATOM   1069  C CZ  . ARG A 1 137 ? -66.392 -32.224 56.227  1.000 174.768 ? 466 ARG AAA CZ  1 
ATOM   1070  N NH1 . ARG A 1 137 ? -67.617 -32.545 56.614  1.000 177.635 ? 466 ARG AAA NH1 1 
ATOM   1071  N NH2 . ARG A 1 137 ? -65.707 -31.324 56.915  1.000 175.312 ? 466 ARG AAA NH2 1 
ATOM   1072  N N   . ASP A 1 138 ? -67.876 -38.619 56.878  1.000 163.222 ? 467 ASP AAA N   1 
ATOM   1073  C CA  . ASP A 1 138 ? -68.588 -38.857 58.163  1.000 163.851 ? 467 ASP AAA CA  1 
ATOM   1074  C C   . ASP A 1 138 ? -67.863 -38.115 59.285  1.000 161.790 ? 467 ASP AAA C   1 
ATOM   1075  O O   . ASP A 1 138 ? -66.644 -38.358 59.444  1.000 160.595 ? 467 ASP AAA O   1 
ATOM   1076  C CB  . ASP A 1 138 ? -68.696 -40.342 58.512  1.000 165.190 ? 467 ASP AAA CB  1 
ATOM   1077  C CG  . ASP A 1 138 ? -69.685 -40.615 59.635  1.000 168.401 ? 467 ASP AAA CG  1 
ATOM   1078  O OD1 . ASP A 1 138 ? -70.139 -39.638 60.282  1.000 171.117 ? 467 ASP AAA OD1 1 
ATOM   1079  O OD2 . ASP A 1 138 ? -70.006 -41.800 59.847  1.000 170.126 ? 467 ASP AAA OD2 1 
ATOM   1080  N N   . ILE A 1 139 ? -68.605 -37.277 60.023  1.000 160.153 ? 468 ILE AAA N   1 
ATOM   1081  C CA  . ILE A 1 139 ? -68.099 -36.419 61.137  1.000 159.921 ? 468 ILE AAA CA  1 
ATOM   1082  C C   . ILE A 1 139 ? -68.957 -36.606 62.401  1.000 162.969 ? 468 ILE AAA C   1 
ATOM   1083  O O   . ILE A 1 139 ? -68.744 -35.833 63.356  1.000 164.727 ? 468 ILE AAA O   1 
ATOM   1084  C CB  . ILE A 1 139 ? -68.046 -34.939 60.695  1.000 158.121 ? 468 ILE AAA CB  1 
ATOM   1085  C CG1 . ILE A 1 139 ? -69.432 -34.297 60.588  1.000 159.997 ? 468 ILE AAA CG1 1 
ATOM   1086  C CG2 . ILE A 1 139 ? -67.291 -34.797 59.387  1.000 155.325 ? 468 ILE AAA CG2 1 
ATOM   1087  C CD1 . ILE A 1 139 ? -69.391 -32.804 60.347  1.000 160.063 ? 468 ILE AAA CD1 1 
ATOM   1088  N N   . SER A 1 140 ? -69.882 -37.575 62.440  1.000 164.448 ? 469 SER AAA N   1 
ATOM   1089  C CA  . SER A 1 140 ? -70.731 -37.853 63.635  1.000 168.285 ? 469 SER AAA CA  1 
ATOM   1090  C C   . SER A 1 140 ? -69.847 -38.403 64.762  1.000 169.955 ? 469 SER AAA C   1 
ATOM   1091  O O   . SER A 1 140 ? -68.886 -39.133 64.435  1.000 169.548 ? 469 SER AAA O   1 
ATOM   1092  C CB  . SER A 1 140 ? -71.875 -38.794 63.315  1.000 169.441 ? 469 SER AAA CB  1 
ATOM   1093  O OG  . SER A 1 140 ? -71.423 -40.134 63.169  1.000 168.772 ? 469 SER AAA OG  1 
ATOM   1094  N N   . THR A 1 141 ? -70.141 -38.057 66.024  1.000 172.097 ? 470 THR AAA N   1 
ATOM   1095  C CA  . THR A 1 141 ? -69.412 -38.554 67.227  1.000 173.559 ? 470 THR AAA CA  1 
ATOM   1096  C C   . THR A 1 141 ? -70.353 -39.445 68.047  1.000 178.728 ? 470 THR AAA C   1 
ATOM   1097  O O   . THR A 1 141 ? -70.419 -39.269 69.285  1.000 183.493 ? 470 THR AAA O   1 
ATOM   1098  C CB  . THR A 1 141 ? -68.830 -37.402 68.056  1.000 172.857 ? 470 THR AAA CB  1 
ATOM   1099  O OG1 . THR A 1 141 ? -69.870 -36.775 68.803  1.000 174.038 ? 470 THR AAA OG1 1 
ATOM   1100  C CG2 . THR A 1 141 ? -68.126 -36.369 67.207  1.000 169.527 ? 470 THR AAA CG2 1 
ATOM   1101  N N   . GLU A 1 142 ? -71.052 -40.359 67.367  1.000 179.353 ? 471 GLU AAA N   1 
ATOM   1102  C CA  . GLU A 1 142 ? -71.962 -41.363 67.979  1.000 183.045 ? 471 GLU AAA CA  1 
ATOM   1103  C C   . GLU A 1 142 ? -71.127 -42.308 68.847  1.000 183.787 ? 471 GLU AAA C   1 
ATOM   1104  O O   . GLU A 1 142 ? -70.156 -42.875 68.324  1.000 180.235 ? 471 GLU AAA O   1 
ATOM   1105  C CB  . GLU A 1 142 ? -72.718 -42.142 66.897  1.000 183.831 ? 471 GLU AAA CB  1 
ATOM   1106  C CG  . GLU A 1 142 ? -73.955 -41.433 66.371  1.000 186.281 ? 471 GLU AAA CG  1 
ATOM   1107  C CD  . GLU A 1 142 ? -75.184 -41.573 67.260  1.000 192.308 ? 471 GLU AAA CD  1 
ATOM   1108  O OE1 . GLU A 1 142 ? -75.029 -41.481 68.494  1.000 196.634 ? 471 GLU AAA OE1 1 
ATOM   1109  O OE2 . GLU A 1 142 ? -76.297 -41.784 66.720  1.000 195.034 ? 471 GLU AAA OE2 1 
ATOM   1110  N N   . ILE A 1 143 ? -71.493 -42.468 70.119  1.000 187.815 ? 472 ILE AAA N   1 
ATOM   1111  C CA  . ILE A 1 143 ? -70.800 -43.394 71.063  1.000 191.070 ? 472 ILE AAA CA  1 
ATOM   1112  C C   . ILE A 1 143 ? -71.004 -44.817 70.525  1.000 191.527 ? 472 ILE AAA C   1 
ATOM   1113  O O   . ILE A 1 143 ? -72.146 -45.310 70.584  1.000 193.930 ? 472 ILE AAA O   1 
ATOM   1114  C CB  . ILE A 1 143 ? -71.320 -43.214 72.505  1.000 195.540 ? 472 ILE AAA CB  1 
ATOM   1115  C CG1 . ILE A 1 143 ? -71.375 -41.739 72.914  1.000 195.042 ? 472 ILE AAA CG1 1 
ATOM   1116  C CG2 . ILE A 1 143 ? -70.498 -44.045 73.481  1.000 199.081 ? 472 ILE AAA CG2 1 
ATOM   1117  C CD1 . ILE A 1 143 ? -70.155 -40.937 72.540  1.000 192.061 ? 472 ILE AAA CD1 1 
ATOM   1118  N N   . TYR A 1 144 ? -69.939 -45.432 69.997  1.000 189.553 ? 473 TYR AAA N   1 
ATOM   1119  C CA  . TYR A 1 144 ? -69.994 -46.646 69.136  1.000 187.866 ? 473 TYR AAA CA  1 
ATOM   1120  C C   . TYR A 1 144 ? -70.272 -47.906 69.967  1.000 191.299 ? 473 TYR AAA C   1 
ATOM   1121  O O   . TYR A 1 144 ? -69.409 -48.319 70.770  1.000 191.629 ? 473 TYR AAA O   1 
ATOM   1122  C CB  . TYR A 1 144 ? -68.702 -46.838 68.338  1.000 184.694 ? 473 TYR AAA CB  1 
ATOM   1123  C CG  . TYR A 1 144 ? -68.667 -48.154 67.605  1.000 184.188 ? 473 TYR AAA CG  1 
ATOM   1124  C CD1 . TYR A 1 144 ? -69.601 -48.436 66.622  1.000 181.854 ? 473 TYR AAA CD1 1 
ATOM   1125  C CD2 . TYR A 1 144 ? -67.753 -49.144 67.933  1.000 186.342 ? 473 TYR AAA CD2 1 
ATOM   1126  C CE1 . TYR A 1 144 ? -69.605 -49.649 65.951  1.000 181.639 ? 473 TYR AAA CE1 1 
ATOM   1127  C CE2 . TYR A 1 144 ? -67.749 -50.368 67.281  1.000 185.527 ? 473 TYR AAA CE2 1 
ATOM   1128  C CZ  . TYR A 1 144 ? -68.676 -50.619 66.284  1.000 182.766 ? 473 TYR AAA CZ  1 
ATOM   1129  O OH  . TYR A 1 144 ? -68.677 -51.816 65.630  1.000 181.718 ? 473 TYR AAA OH  1 
ATOM   1130  N N   . GLN A 1 145 ? -71.427 -48.528 69.712  1.000 191.951 ? 474 GLN AAA N   1 
ATOM   1131  C CA  . GLN A 1 145 ? -71.878 -49.804 70.328  1.000 195.234 ? 474 GLN AAA CA  1 
ATOM   1132  C C   . GLN A 1 145 ? -71.165 -50.976 69.644  1.000 194.195 ? 474 GLN AAA C   1 
ATOM   1133  O O   . GLN A 1 145 ? -71.567 -51.338 68.519  1.000 192.696 ? 474 GLN AAA O   1 
ATOM   1134  C CB  . GLN A 1 145 ? -73.397 -49.937 70.200  1.000 196.624 ? 474 GLN AAA CB  1 
ATOM   1135  C CG  . GLN A 1 145 ? -73.958 -51.216 70.802  1.000 200.684 ? 474 GLN AAA CG  1 
ATOM   1136  C CD  . GLN A 1 145 ? -75.461 -51.292 70.677  1.000 201.865 ? 474 GLN AAA CD  1 
ATOM   1137  O OE1 . GLN A 1 145 ? -76.094 -50.488 69.993  1.000 197.986 ? 474 GLN AAA OE1 1 
ATOM   1138  N NE2 . GLN A 1 145 ? -76.052 -52.272 71.340  1.000 206.212 ? 474 GLN AAA NE2 1 
ATOM   1139  N N   . ALA A 1 146 ? -70.146 -51.533 70.306  1.000 195.119 ? 475 ALA AAA N   1 
ATOM   1140  C CA  . ALA A 1 146 ? -69.397 -52.733 69.868  1.000 195.030 ? 475 ALA AAA CA  1 
ATOM   1141  C C   . ALA A 1 146 ? -70.186 -53.995 70.249  1.000 199.023 ? 475 ALA AAA C   1 
ATOM   1142  O O   . ALA A 1 146 ? -70.718 -54.660 69.338  1.000 199.448 ? 475 ALA AAA O   1 
ATOM   1143  C CB  . ALA A 1 146 ? -68.017 -52.721 70.477  1.000 195.654 ? 475 ALA AAA CB  1 
ATOM   1144  N N   . GLY A 1 147 ? -70.289 -54.291 71.548  1.000 201.912 ? 476 GLY AAA N   1 
ATOM   1145  C CA  . GLY A 1 147 ? -70.912 -55.521 72.074  1.000 204.990 ? 476 GLY AAA CA  1 
ATOM   1146  C C   . GLY A 1 147 ? -72.427 -55.438 72.050  1.000 205.272 ? 476 GLY AAA C   1 
ATOM   1147  O O   . GLY A 1 147 ? -72.955 -54.677 71.225  1.000 200.347 ? 476 GLY AAA O   1 
ATOM   1148  N N   . SER A 1 148 ? -73.094 -56.200 72.924  1.000 211.059 ? 477 SER AAA N   1 
ATOM   1149  C CA  . SER A 1 148 ? -74.574 -56.365 72.989  1.000 213.592 ? 477 SER AAA CA  1 
ATOM   1150  C C   . SER A 1 148 ? -75.239 -55.069 73.465  1.000 213.218 ? 477 SER AAA C   1 
ATOM   1151  O O   . SER A 1 148 ? -75.976 -54.455 72.668  1.000 209.712 ? 477 SER AAA O   1 
ATOM   1152  C CB  . SER A 1 148 ? -74.962 -57.514 73.890  1.000 219.567 ? 477 SER AAA CB  1 
ATOM   1153  O OG  . SER A 1 148 ? -74.077 -58.606 73.722  1.000 221.489 ? 477 SER AAA OG  1 
ATOM   1154  N N   . THR A 1 149 ? -74.971 -54.685 74.719  1.000 217.017 ? 478 THR AAA N   1 
ATOM   1155  C CA  . THR A 1 149 ? -75.671 -53.611 75.479  1.000 217.886 ? 478 THR AAA CA  1 
ATOM   1156  C C   . THR A 1 149 ? -75.750 -52.342 74.627  1.000 212.911 ? 478 THR AAA C   1 
ATOM   1157  O O   . THR A 1 149 ? -74.754 -51.916 74.044  1.000 208.196 ? 478 THR AAA O   1 
ATOM   1158  C CB  . THR A 1 149 ? -75.006 -53.389 76.846  1.000 220.710 ? 478 THR AAA CB  1 
ATOM   1159  O OG1 . THR A 1 149 ? -73.594 -53.571 76.729  1.000 219.716 ? 478 THR AAA OG1 1 
ATOM   1160  C CG2 . THR A 1 149 ? -75.531 -54.331 77.909  1.000 225.794 ? 478 THR AAA CG2 1 
ATOM   1161  N N   . PRO A 1 150 ? -76.942 -51.711 74.509  1.000 213.235 ? 479 PRO AAA N   1 
ATOM   1162  C CA  . PRO A 1 150 ? -77.081 -50.465 73.762  1.000 209.006 ? 479 PRO AAA CA  1 
ATOM   1163  C C   . PRO A 1 150 ? -76.632 -49.282 74.629  1.000 209.719 ? 479 PRO AAA C   1 
ATOM   1164  O O   . PRO A 1 150 ? -77.056 -49.178 75.760  1.000 212.640 ? 479 PRO AAA O   1 
ATOM   1165  C CB  . PRO A 1 150 ? -78.575 -50.381 73.410  1.000 210.070 ? 479 PRO AAA CB  1 
ATOM   1166  C CG  . PRO A 1 150 ? -79.278 -51.387 74.315  1.000 215.916 ? 479 PRO AAA CG  1 
ATOM   1167  C CD  . PRO A 1 150 ? -78.218 -52.144 75.092  1.000 218.043 ? 479 PRO AAA CD  1 
ATOM   1168  N N   . CYS A 1 151 ? -75.779 -48.425 74.069  1.000 208.085 ? 480 CYS AAA N   1 
ATOM   1169  C CA  . CYS A 1 151 ? -75.251 -47.200 74.722  1.000 209.481 ? 480 CYS AAA CA  1 
ATOM   1170  C C   . CYS A 1 151 ? -76.164 -46.016 74.386  1.000 205.762 ? 480 CYS AAA C   1 
ATOM   1171  O O   . CYS A 1 151 ? -76.504 -45.834 73.196  1.000 202.815 ? 480 CYS AAA O   1 
ATOM   1172  C CB  . CYS A 1 151 ? -73.826 -46.876 74.277  1.000 210.395 ? 480 CYS AAA CB  1 
ATOM   1173  S SG  . CYS A 1 151 ? -72.924 -48.224 73.460  1.000 214.222 ? 480 CYS AAA SG  1 
ATOM   1174  N N   . ASN A 1 152 ? -76.520 -45.241 75.405  1.000 206.098 ? 481 ASN AAA N   1 
ATOM   1175  C CA  . ASN A 1 152 ? -77.423 -44.066 75.305  1.000 205.467 ? 481 ASN AAA CA  1 
ATOM   1176  C C   . ASN A 1 152 ? -76.552 -42.807 75.406  1.000 202.382 ? 481 ASN AAA C   1 
ATOM   1177  O O   . ASN A 1 152 ? -76.873 -41.924 76.220  1.000 205.223 ? 481 ASN AAA O   1 
ATOM   1178  C CB  . ASN A 1 152 ? -78.542 -44.153 76.351  1.000 211.421 ? 481 ASN AAA CB  1 
ATOM   1179  C CG  . ASN A 1 152 ? -78.123 -44.879 77.615  1.000 216.691 ? 481 ASN AAA CG  1 
ATOM   1180  O OD1 . ASN A 1 152 ? -77.225 -45.723 77.579  1.000 216.820 ? 481 ASN AAA OD1 1 
ATOM   1181  N ND2 . ASN A 1 152 ? -78.770 -44.573 78.732  1.000 220.807 ? 481 ASN AAA ND2 1 
ATOM   1182  N N   . GLY A 1 153 ? -75.476 -42.743 74.612  1.000 196.863 ? 482 GLY AAA N   1 
ATOM   1183  C CA  . GLY A 1 153 ? -74.461 -41.671 74.673  1.000 193.975 ? 482 GLY AAA CA  1 
ATOM   1184  C C   . GLY A 1 153 ? -73.563 -41.806 75.895  1.000 196.691 ? 482 GLY AAA C   1 
ATOM   1185  O O   . GLY A 1 153 ? -72.734 -40.911 76.133  1.000 195.188 ? 482 GLY AAA O   1 
ATOM   1186  N N   . VAL A 1 154 ? -73.711 -42.900 76.640  1.000 200.349 ? 483 VAL AAA N   1 
ATOM   1187  C CA  . VAL A 1 154 ? -72.891 -43.240 77.836  1.000 204.343 ? 483 VAL AAA CA  1 
ATOM   1188  C C   . VAL A 1 154 ? -71.719 -44.079 77.336  1.000 201.870 ? 483 VAL AAA C   1 
ATOM   1189  O O   . VAL A 1 154 ? -71.967 -45.006 76.556  1.000 198.976 ? 483 VAL AAA O   1 
ATOM   1190  C CB  . VAL A 1 154 ? -73.730 -44.008 78.876  1.000 210.374 ? 483 VAL AAA CB  1 
ATOM   1191  C CG1 . VAL A 1 154 ? -72.908 -44.413 80.091  1.000 214.555 ? 483 VAL AAA CG1 1 
ATOM   1192  C CG2 . VAL A 1 154 ? -74.964 -43.222 79.295  1.000 212.347 ? 483 VAL AAA CG2 1 
ATOM   1193  N N   . GLU A 1 155 ? -70.499 -43.763 77.761  1.000 202.868 ? 484 GLU AAA N   1 
ATOM   1194  C CA  . GLU A 1 155 ? -69.285 -44.509 77.343  1.000 203.235 ? 484 GLU AAA CA  1 
ATOM   1195  C C   . GLU A 1 155 ? -69.008 -45.633 78.347  1.000 207.833 ? 484 GLU AAA C   1 
ATOM   1196  O O   . GLU A 1 155 ? -69.597 -45.592 79.448  1.000 210.801 ? 484 GLU AAA O   1 
ATOM   1197  C CB  . GLU A 1 155 ? -68.102 -43.551 77.243  1.000 203.434 ? 484 GLU AAA CB  1 
ATOM   1198  C CG  . GLU A 1 155 ? -67.446 -43.529 75.879  1.000 200.475 ? 484 GLU AAA CG  1 
ATOM   1199  C CD  . GLU A 1 155 ? -66.668 -42.253 75.609  1.000 199.842 ? 484 GLU AAA CD  1 
ATOM   1200  O OE1 . GLU A 1 155 ? -67.213 -41.147 75.859  1.000 200.558 ? 484 GLU AAA OE1 1 
ATOM   1201  O OE2 . GLU A 1 155 ? -65.518 -42.365 75.148  1.000 199.481 ? 484 GLU AAA OE2 1 
ATOM   1202  N N   . GLY A 1 156 ? -68.170 -46.603 77.959  1.000 207.846 ? 485 GLY AAA N   1 
ATOM   1203  C CA  . GLY A 1 156 ? -67.606 -47.623 78.869  1.000 213.486 ? 485 GLY AAA CA  1 
ATOM   1204  C C   . GLY A 1 156 ? -67.558 -49.021 78.268  1.000 214.124 ? 485 GLY AAA C   1 
ATOM   1205  O O   . GLY A 1 156 ? -66.981 -49.183 77.184  1.000 208.528 ? 485 GLY AAA O   1 
ATOM   1206  N N   . PHE A 1 157 ? -68.117 -49.996 78.993  1.000 221.118 ? 486 PHE AAA N   1 
ATOM   1207  C CA  . PHE A 1 157 ? -68.135 -51.449 78.678  1.000 223.810 ? 486 PHE AAA CA  1 
ATOM   1208  C C   . PHE A 1 157 ? -68.790 -51.658 77.307  1.000 220.341 ? 486 PHE AAA C   1 
ATOM   1209  O O   . PHE A 1 157 ? -70.014 -51.435 77.192  1.000 220.496 ? 486 PHE AAA O   1 
ATOM   1210  C CB  . PHE A 1 157 ? -68.885 -52.192 79.789  1.000 229.757 ? 486 PHE AAA CB  1 
ATOM   1211  C CG  . PHE A 1 157 ? -68.816 -53.698 79.748  1.000 232.323 ? 486 PHE AAA CG  1 
ATOM   1212  C CD1 . PHE A 1 157 ? -69.677 -54.430 78.943  1.000 230.415 ? 486 PHE AAA CD1 1 
ATOM   1213  C CD2 . PHE A 1 157 ? -67.925 -54.389 80.556  1.000 236.883 ? 486 PHE AAA CD2 1 
ATOM   1214  C CE1 . PHE A 1 157 ? -69.620 -55.815 78.917  1.000 233.065 ? 486 PHE AAA CE1 1 
ATOM   1215  C CE2 . PHE A 1 157 ? -67.876 -55.776 80.537  1.000 239.336 ? 486 PHE AAA CE2 1 
ATOM   1216  C CZ  . PHE A 1 157 ? -68.721 -56.486 79.715  1.000 237.508 ? 486 PHE AAA CZ  1 
ATOM   1217  N N   . ASN A 1 158 ? -67.993 -52.046 76.303  1.000 218.332 ? 487 ASN AAA N   1 
ATOM   1218  C CA  . ASN A 1 158 ? -68.438 -52.320 74.907  1.000 214.627 ? 487 ASN AAA CA  1 
ATOM   1219  C C   . ASN A 1 158 ? -68.970 -51.041 74.240  1.000 211.421 ? 487 ASN AAA C   1 
ATOM   1220  O O   . ASN A 1 158 ? -69.688 -51.189 73.242  1.000 208.339 ? 487 ASN AAA O   1 
ATOM   1221  C CB  . ASN A 1 158 ? -69.547 -53.379 74.837  1.000 216.692 ? 487 ASN AAA CB  1 
ATOM   1222  C CG  . ASN A 1 158 ? -69.308 -54.608 75.685  1.000 222.562 ? 487 ASN AAA CG  1 
ATOM   1223  O OD1 . ASN A 1 158 ? -68.197 -54.844 76.149  1.000 225.865 ? 487 ASN AAA OD1 1 
ATOM   1224  N ND2 . ASN A 1 158 ? -70.354 -55.387 75.900  1.000 225.094 ? 487 ASN AAA ND2 1 
ATOM   1225  N N   . CYS A 1 159 ? -68.625 -49.847 74.750  1.000 212.861 ? 488 CYS AAA N   1 
ATOM   1226  C CA  . CYS A 1 159 ? -69.046 -48.531 74.186  1.000 209.931 ? 488 CYS AAA CA  1 
ATOM   1227  C C   . CYS A 1 159 ? -67.901 -47.512 74.251  1.000 207.483 ? 488 CYS AAA C   1 
ATOM   1228  O O   . CYS A 1 159 ? -67.448 -47.171 75.367  1.000 208.973 ? 488 CYS AAA O   1 
ATOM   1229  C CB  . CYS A 1 159 ? -70.251 -47.961 74.918  1.000 213.801 ? 488 CYS AAA CB  1 
ATOM   1230  S SG  . CYS A 1 159 ? -71.719 -49.023 74.896  1.000 219.660 ? 488 CYS AAA SG  1 
ATOM   1231  N N   . TYR A 1 160 ? -67.504 -47.008 73.078  1.000 203.118 ? 489 TYR AAA N   1 
ATOM   1232  C CA  . TYR A 1 160 ? -66.256 -46.240 72.828  1.000 201.713 ? 489 TYR AAA CA  1 
ATOM   1233  C C   . TYR A 1 160 ? -66.585 -45.012 71.976  1.000 196.708 ? 489 TYR AAA C   1 
ATOM   1234  O O   . TYR A 1 160 ? -67.537 -45.085 71.182  1.000 193.675 ? 489 TYR AAA O   1 
ATOM   1235  C CB  . TYR A 1 160 ? -65.223 -47.146 72.146  1.000 201.668 ? 489 TYR AAA CB  1 
ATOM   1236  C CG  . TYR A 1 160 ? -65.165 -48.534 72.736  1.000 207.329 ? 489 TYR AAA CG  1 
ATOM   1237  C CD1 . TYR A 1 160 ? -64.714 -48.732 74.034  1.000 212.663 ? 489 TYR AAA CD1 1 
ATOM   1238  C CD2 . TYR A 1 160 ? -65.596 -49.645 72.025  1.000 206.646 ? 489 TYR AAA CD2 1 
ATOM   1239  C CE1 . TYR A 1 160 ? -64.679 -49.994 74.605  1.000 216.304 ? 489 TYR AAA CE1 1 
ATOM   1240  C CE2 . TYR A 1 160 ? -65.561 -50.915 72.582  1.000 210.868 ? 489 TYR AAA CE2 1 
ATOM   1241  C CZ  . TYR A 1 160 ? -65.116 -51.089 73.883  1.000 215.504 ? 489 TYR AAA CZ  1 
ATOM   1242  O OH  . TYR A 1 160 ? -65.086 -52.328 74.452  1.000 218.973 ? 489 TYR AAA OH  1 
ATOM   1243  N N   . PHE A 1 161 ? -65.840 -43.921 72.168  1.000 196.225 ? 490 PHE AAA N   1 
ATOM   1244  C CA  . PHE A 1 161 ? -65.857 -42.706 71.308  1.000 193.949 ? 490 PHE AAA CA  1 
ATOM   1245  C C   . PHE A 1 161 ? -65.137 -43.050 70.007  1.000 192.373 ? 490 PHE AAA C   1 
ATOM   1246  O O   . PHE A 1 161 ? -64.035 -43.587 70.058  1.000 194.220 ? 490 PHE AAA O   1 
ATOM   1247  C CB  . PHE A 1 161 ? -65.197 -41.535 72.042  1.000 195.441 ? 490 PHE AAA CB  1 
ATOM   1248  C CG  . PHE A 1 161 ? -65.322 -40.185 71.379  1.000 193.711 ? 490 PHE AAA CG  1 
ATOM   1249  C CD1 . PHE A 1 161 ? -66.516 -39.478 71.420  1.000 195.204 ? 490 PHE AAA CD1 1 
ATOM   1250  C CD2 . PHE A 1 161 ? -64.237 -39.593 70.749  1.000 191.299 ? 490 PHE AAA CD2 1 
ATOM   1251  C CE1 . PHE A 1 161 ? -66.631 -38.229 70.823  1.000 192.984 ? 490 PHE AAA CE1 1 
ATOM   1252  C CE2 . PHE A 1 161 ? -64.351 -38.341 70.158  1.000 188.596 ? 490 PHE AAA CE2 1 
ATOM   1253  C CZ  . PHE A 1 161 ? -65.547 -37.660 70.194  1.000 189.417 ? 490 PHE AAA CZ  1 
ATOM   1254  N N   . PRO A 1 162 ? -65.717 -42.773 68.813  1.000 190.141 ? 491 PRO AAA N   1 
ATOM   1255  C CA  . PRO A 1 162 ? -65.225 -43.356 67.561  1.000 186.638 ? 491 PRO AAA CA  1 
ATOM   1256  C C   . PRO A 1 162 ? -63.970 -42.715 66.939  1.000 183.890 ? 491 PRO AAA C   1 
ATOM   1257  O O   . PRO A 1 162 ? -63.430 -43.312 66.024  1.000 182.778 ? 491 PRO AAA O   1 
ATOM   1258  C CB  . PRO A 1 162 ? -66.424 -43.175 66.615  1.000 184.928 ? 491 PRO AAA CB  1 
ATOM   1259  C CG  . PRO A 1 162 ? -67.103 -41.907 67.104  1.000 185.510 ? 491 PRO AAA CG  1 
ATOM   1260  C CD  . PRO A 1 162 ? -66.867 -41.880 68.600  1.000 189.359 ? 491 PRO AAA CD  1 
ATOM   1261  N N   . LEU A 1 163 ? -63.533 -41.547 67.430  1.000 182.930 ? 492 LEU AAA N   1 
ATOM   1262  C CA  . LEU A 1 163 ? -62.333 -40.816 66.922  1.000 179.726 ? 492 LEU AAA CA  1 
ATOM   1263  C C   . LEU A 1 163 ? -61.155 -40.979 67.890  1.000 182.855 ? 492 LEU AAA C   1 
ATOM   1264  O O   . LEU A 1 163 ? -61.387 -41.284 69.067  1.000 187.939 ? 492 LEU AAA O   1 
ATOM   1265  C CB  . LEU A 1 163 ? -62.656 -39.329 66.752  1.000 177.031 ? 492 LEU AAA CB  1 
ATOM   1266  C CG  . LEU A 1 163 ? -63.804 -38.987 65.804  1.000 174.236 ? 492 LEU AAA CG  1 
ATOM   1267  C CD1 . LEU A 1 163 ? -63.772 -37.508 65.450  1.000 172.900 ? 492 LEU AAA CD1 1 
ATOM   1268  C CD2 . LEU A 1 163 ? -63.771 -39.839 64.540  1.000 171.400 ? 492 LEU AAA CD2 1 
ATOM   1269  N N   . GLN A 1 164 ? -59.936 -40.741 67.399  1.000 181.714 ? 493 GLN AAA N   1 
ATOM   1270  C CA  . GLN A 1 164 ? -58.672 -40.737 68.186  1.000 184.159 ? 493 GLN AAA CA  1 
ATOM   1271  C C   . GLN A 1 164 ? -57.735 -39.677 67.589  1.000 183.397 ? 493 GLN AAA C   1 
ATOM   1272  O O   . GLN A 1 164 ? -58.025 -39.192 66.471  1.000 183.410 ? 493 GLN AAA O   1 
ATOM   1273  C CB  . GLN A 1 164 ? -58.032 -42.130 68.186  1.000 184.587 ? 493 GLN AAA CB  1 
ATOM   1274  C CG  . GLN A 1 164 ? -57.081 -42.351 69.352  1.000 188.808 ? 493 GLN AAA CG  1 
ATOM   1275  C CD  . GLN A 1 164 ? -56.661 -43.798 69.575  1.000 191.484 ? 493 GLN AAA CD  1 
ATOM   1276  O OE1 . GLN A 1 164 ? -56.790 -44.269 70.794  1.000 196.230 ? 493 GLN AAA OE1 1 
ATOM   1277  N NE2 . GLN A 1 164 ? -56.504 -44.502 68.397  1.000 187.698 ? 493 GLN AAA NE2 1 
ATOM   1278  N N   . SER A 1 165 ? -56.673 -39.315 68.313  1.000 183.129 ? 494 SER AAA N   1 
ATOM   1279  C CA  . SER A 1 165 ? -55.625 -38.368 67.854  1.000 177.595 ? 494 SER AAA CA  1 
ATOM   1280  C C   . SER A 1 165 ? -54.450 -39.135 67.237  1.000 170.926 ? 494 SER AAA C   1 
ATOM   1281  O O   . SER A 1 165 ? -54.405 -40.375 67.359  1.000 169.880 ? 494 SER AAA O   1 
ATOM   1282  C CB  . SER A 1 165 ? -55.152 -37.485 68.965  1.000 181.452 ? 494 SER AAA CB  1 
ATOM   1283  O OG  . SER A 1 165 ? -54.060 -36.709 68.509  1.000 180.027 ? 494 SER AAA OG  1 
ATOM   1284  N N   . TYR A 1 166 ? -53.525 -38.402 66.618  1.000 165.587 ? 495 TYR AAA N   1 
ATOM   1285  C CA  . TYR A 1 166 ? -52.369 -38.967 65.884  1.000 163.127 ? 495 TYR AAA CA  1 
ATOM   1286  C C   . TYR A 1 166 ? -51.090 -38.854 66.718  1.000 163.831 ? 495 TYR AAA C   1 
ATOM   1287  O O   . TYR A 1 166 ? -50.294 -39.819 66.731  1.000 161.912 ? 495 TYR AAA O   1 
ATOM   1288  C CB  . TYR A 1 166 ? -52.229 -38.284 64.524  1.000 161.108 ? 495 TYR AAA CB  1 
ATOM   1289  C CG  . TYR A 1 166 ? -52.874 -39.047 63.395  1.000 160.237 ? 495 TYR AAA CG  1 
ATOM   1290  C CD1 . TYR A 1 166 ? -52.562 -40.379 63.179  1.000 159.927 ? 495 TYR AAA CD1 1 
ATOM   1291  C CD2 . TYR A 1 166 ? -53.788 -38.445 62.543  1.000 159.311 ? 495 TYR AAA CD2 1 
ATOM   1292  C CE1 . TYR A 1 166 ? -53.152 -41.102 62.160  1.000 157.927 ? 495 TYR AAA CE1 1 
ATOM   1293  C CE2 . TYR A 1 166 ? -54.380 -39.152 61.512  1.000 157.040 ? 495 TYR AAA CE2 1 
ATOM   1294  C CZ  . TYR A 1 166 ? -54.062 -40.485 61.325  1.000 157.318 ? 495 TYR AAA CZ  1 
ATOM   1295  O OH  . TYR A 1 166 ? -54.627 -41.205 60.316  1.000 159.065 ? 495 TYR AAA OH  1 
ATOM   1296  N N   . GLY A 1 167 ? -50.887 -37.710 67.375  1.000 165.914 ? 496 GLY AAA N   1 
ATOM   1297  C CA  . GLY A 1 167 ? -49.701 -37.462 68.216  1.000 167.821 ? 496 GLY AAA CA  1 
ATOM   1298  C C   . GLY A 1 167 ? -48.435 -37.484 67.385  1.000 164.263 ? 496 GLY AAA C   1 
ATOM   1299  O O   . GLY A 1 167 ? -47.625 -38.413 67.542  1.000 162.435 ? 496 GLY AAA O   1 
ATOM   1300  N N   . PHE A 1 168 ? -48.299 -36.505 66.498  1.000 164.022 ? 497 PHE AAA N   1 
ATOM   1301  C CA  . PHE A 1 168 ? -47.116 -36.324 65.629  1.000 165.195 ? 497 PHE AAA CA  1 
ATOM   1302  C C   . PHE A 1 168 ? -46.044 -35.600 66.439  1.000 169.821 ? 497 PHE AAA C   1 
ATOM   1303  O O   . PHE A 1 168 ? -46.293 -34.455 66.875  1.000 170.836 ? 497 PHE AAA O   1 
ATOM   1304  C CB  . PHE A 1 168 ? -47.490 -35.556 64.361  1.000 164.765 ? 497 PHE AAA CB  1 
ATOM   1305  C CG  . PHE A 1 168 ? -48.505 -36.252 63.486  1.000 163.092 ? 497 PHE AAA CG  1 
ATOM   1306  C CD1 . PHE A 1 168 ? -48.201 -37.456 62.866  1.000 160.656 ? 497 PHE AAA CD1 1 
ATOM   1307  C CD2 . PHE A 1 168 ? -49.760 -35.701 63.271  1.000 163.297 ? 497 PHE AAA CD2 1 
ATOM   1308  C CE1 . PHE A 1 168 ? -49.127 -38.095 62.056  1.000 157.918 ? 497 PHE AAA CE1 1 
ATOM   1309  C CE2 . PHE A 1 168 ? -50.685 -36.343 62.460  1.000 160.771 ? 497 PHE AAA CE2 1 
ATOM   1310  C CZ  . PHE A 1 168 ? -50.367 -37.538 61.852  1.000 158.017 ? 497 PHE AAA CZ  1 
ATOM   1311  N N   . GLN A 1 169 ? -44.910 -36.271 66.655  1.000 173.874 ? 498 GLN AAA N   1 
ATOM   1312  C CA  . GLN A 1 169 ? -43.704 -35.697 67.304  1.000 178.270 ? 498 GLN AAA CA  1 
ATOM   1313  C C   . GLN A 1 169 ? -42.611 -35.600 66.241  1.000 176.137 ? 498 GLN AAA C   1 
ATOM   1314  O O   . GLN A 1 169 ? -42.537 -36.450 65.352  1.000 172.912 ? 498 GLN AAA O   1 
ATOM   1315  C CB  . GLN A 1 169 ? -43.320 -36.543 68.522  1.000 182.194 ? 498 GLN AAA CB  1 
ATOM   1316  C CG  . GLN A 1 169 ? -44.507 -36.877 69.422  1.000 184.524 ? 498 GLN AAA CG  1 
ATOM   1317  C CD  . GLN A 1 169 ? -44.215 -36.669 70.892  1.000 191.939 ? 498 GLN AAA CD  1 
ATOM   1318  O OE1 . GLN A 1 169 ? -43.162 -37.049 71.398  1.000 197.779 ? 498 GLN AAA OE1 1 
ATOM   1319  N NE2 . GLN A 1 169 ? -45.159 -36.068 71.602  1.000 194.681 ? 498 GLN AAA NE2 1 
ATOM   1320  N N   . PRO A 1 170 ? -41.777 -34.531 66.254  1.000 177.092 ? 499 PRO AAA N   1 
ATOM   1321  C CA  . PRO A 1 170 ? -40.646 -34.418 65.331  1.000 176.224 ? 499 PRO AAA CA  1 
ATOM   1322  C C   . PRO A 1 170 ? -39.690 -35.621 65.381  1.000 176.270 ? 499 PRO AAA C   1 
ATOM   1323  O O   . PRO A 1 170 ? -39.027 -35.872 64.391  1.000 175.206 ? 499 PRO AAA O   1 
ATOM   1324  C CB  . PRO A 1 170 ? -39.905 -33.155 65.801  1.000 180.559 ? 499 PRO AAA CB  1 
ATOM   1325  C CG  . PRO A 1 170 ? -40.961 -32.335 66.515  1.000 181.523 ? 499 PRO AAA CG  1 
ATOM   1326  C CD  . PRO A 1 170 ? -41.913 -33.347 67.120  1.000 180.183 ? 499 PRO AAA CD  1 
ATOM   1327  N N   . THR A 1 171 ? -39.636 -36.309 66.529  1.000 176.845 ? 500 THR AAA N   1 
ATOM   1328  C CA  . THR A 1 171 ? -38.736 -37.459 66.817  1.000 177.747 ? 500 THR AAA CA  1 
ATOM   1329  C C   . THR A 1 171 ? -39.395 -38.783 66.403  1.000 173.504 ? 500 THR AAA C   1 
ATOM   1330  O O   . THR A 1 171 ? -38.685 -39.799 66.393  1.000 174.063 ? 500 THR AAA O   1 
ATOM   1331  C CB  . THR A 1 171 ? -38.351 -37.495 68.302  1.000 182.458 ? 500 THR AAA CB  1 
ATOM   1332  O OG1 . THR A 1 171 ? -39.560 -37.395 69.053  1.000 182.050 ? 500 THR AAA OG1 1 
ATOM   1333  C CG2 . THR A 1 171 ? -37.398 -36.390 68.705  1.000 186.544 ? 500 THR AAA CG2 1 
ATOM   1334  N N   . ASN A 1 172 ? -40.694 -38.783 66.087  1.000 170.227 ? 501 ASN AAA N   1 
ATOM   1335  C CA  . ASN A 1 172 ? -41.418 -39.970 65.551  1.000 169.551 ? 501 ASN AAA CA  1 
ATOM   1336  C C   . ASN A 1 172 ? -40.684 -40.522 64.322  1.000 170.877 ? 501 ASN AAA C   1 
ATOM   1337  O O   . ASN A 1 172 ? -40.087 -39.713 63.580  1.000 171.047 ? 501 ASN AAA O   1 
ATOM   1338  C CB  . ASN A 1 172 ? -42.862 -39.650 65.149  1.000 165.612 ? 501 ASN AAA CB  1 
ATOM   1339  C CG  . ASN A 1 172 ? -43.884 -40.110 66.166  1.000 165.533 ? 501 ASN AAA CG  1 
ATOM   1340  O OD1 . ASN A 1 172 ? -44.684 -39.312 66.649  1.000 163.908 ? 501 ASN AAA OD1 1 
ATOM   1341  N ND2 . ASN A 1 172 ? -43.867 -41.393 66.492  1.000 166.281 ? 501 ASN AAA ND2 1 
ATOM   1342  N N   . GLY A 1 173 ? -40.758 -41.843 64.105  1.000 172.918 ? 502 GLY AAA N   1 
ATOM   1343  C CA  . GLY A 1 173 ? -40.251 -42.530 62.897  1.000 173.242 ? 502 GLY AAA CA  1 
ATOM   1344  C C   . GLY A 1 173 ? -40.963 -42.043 61.644  1.000 170.471 ? 502 GLY AAA C   1 
ATOM   1345  O O   . GLY A 1 173 ? -42.142 -41.655 61.760  1.000 168.938 ? 502 GLY AAA O   1 
ATOM   1346  N N   . VAL A 1 174 ? -40.291 -42.082 60.485  1.000 171.488 ? 503 VAL AAA N   1 
ATOM   1347  C CA  . VAL A 1 174 ? -40.738 -41.401 59.227  1.000 167.312 ? 503 VAL AAA CA  1 
ATOM   1348  C C   . VAL A 1 174 ? -42.172 -41.836 58.907  1.000 163.268 ? 503 VAL AAA C   1 
ATOM   1349  O O   . VAL A 1 174 ? -42.914 -41.013 58.344  1.000 159.668 ? 503 VAL AAA O   1 
ATOM   1350  C CB  . VAL A 1 174 ? -39.795 -41.657 58.032  1.000 168.926 ? 503 VAL AAA CB  1 
ATOM   1351  C CG1 . VAL A 1 174 ? -40.238 -40.883 56.796  1.000 165.705 ? 503 VAL AAA CG1 1 
ATOM   1352  C CG2 . VAL A 1 174 ? -38.339 -41.338 58.357  1.000 173.529 ? 503 VAL AAA CG2 1 
ATOM   1353  N N   . GLY A 1 175 ? -42.537 -43.075 59.257  1.000 164.198 ? 504 GLY AAA N   1 
ATOM   1354  C CA  . GLY A 1 175 ? -43.883 -43.643 59.043  1.000 163.598 ? 504 GLY AAA CA  1 
ATOM   1355  C C   . GLY A 1 175 ? -44.951 -42.970 59.894  1.000 163.305 ? 504 GLY AAA C   1 
ATOM   1356  O O   . GLY A 1 175 ? -46.071 -42.761 59.381  1.000 161.012 ? 504 GLY AAA O   1 
ATOM   1357  N N   . TYR A 1 176 ? -44.634 -42.657 61.154  1.000 166.369 ? 505 TYR AAA N   1 
ATOM   1358  C CA  . TYR A 1 176 ? -45.560 -42.029 62.135  1.000 166.085 ? 505 TYR AAA CA  1 
ATOM   1359  C C   . TYR A 1 176 ? -45.347 -40.511 62.130  1.000 164.210 ? 505 TYR AAA C   1 
ATOM   1360  O O   . TYR A 1 176 ? -45.770 -39.852 63.102  1.000 167.416 ? 505 TYR AAA O   1 
ATOM   1361  C CB  . TYR A 1 176 ? -45.370 -42.647 63.526  1.000 171.500 ? 505 TYR AAA CB  1 
ATOM   1362  C CG  . TYR A 1 176 ? -45.605 -44.136 63.574  1.000 175.803 ? 505 TYR AAA CG  1 
ATOM   1363  C CD1 . TYR A 1 176 ? -44.588 -45.031 63.270  1.000 179.446 ? 505 TYR AAA CD1 1 
ATOM   1364  C CD2 . TYR A 1 176 ? -46.848 -44.656 63.906  1.000 178.212 ? 505 TYR AAA CD2 1 
ATOM   1365  C CE1 . TYR A 1 176 ? -44.799 -46.401 63.286  1.000 183.528 ? 505 TYR AAA CE1 1 
ATOM   1366  C CE2 . TYR A 1 176 ? -47.072 -46.025 63.939  1.000 182.444 ? 505 TYR AAA CE2 1 
ATOM   1367  C CZ  . TYR A 1 176 ? -46.047 -46.903 63.623  1.000 184.851 ? 505 TYR AAA CZ  1 
ATOM   1368  O OH  . TYR A 1 176 ? -46.264 -48.254 63.652  1.000 187.312 ? 505 TYR AAA OH  1 
ATOM   1369  N N   . GLN A 1 177 ? -44.687 -39.990 61.085  1.000 161.522 ? 506 GLN AAA N   1 
ATOM   1370  C CA  . GLN A 1 177 ? -44.648 -38.544 60.741  1.000 161.102 ? 506 GLN AAA CA  1 
ATOM   1371  C C   . GLN A 1 177 ? -45.878 -38.224 59.894  1.000 157.711 ? 506 GLN AAA C   1 
ATOM   1372  O O   . GLN A 1 177 ? -46.385 -39.093 59.188  1.000 156.779 ? 506 GLN AAA O   1 
ATOM   1373  C CB  . GLN A 1 177 ? -43.356 -38.174 60.003  1.000 161.665 ? 506 GLN AAA CB  1 
ATOM   1374  C CG  . GLN A 1 177 ? -42.116 -38.159 60.889  1.000 164.585 ? 506 GLN AAA CG  1 
ATOM   1375  C CD  . GLN A 1 177 ? -40.878 -37.698 60.157  1.000 166.031 ? 506 GLN AAA CD  1 
ATOM   1376  O OE1 . GLN A 1 177 ? -40.947 -37.055 59.112  1.000 163.667 ? 506 GLN AAA OE1 1 
ATOM   1377  N NE2 . GLN A 1 177 ? -39.724 -38.021 60.715  1.000 170.934 ? 506 GLN AAA NE2 1 
ATOM   1378  N N   . PRO A 1 178 ? -46.405 -36.978 59.946  1.000 156.827 ? 507 PRO AAA N   1 
ATOM   1379  C CA  . PRO A 1 178 ? -47.618 -36.620 59.211  1.000 154.244 ? 507 PRO AAA CA  1 
ATOM   1380  C C   . PRO A 1 178 ? -47.354 -36.240 57.747  1.000 151.962 ? 507 PRO AAA C   1 
ATOM   1381  O O   . PRO A 1 178 ? -46.536 -35.369 57.516  1.000 154.746 ? 507 PRO AAA O   1 
ATOM   1382  C CB  . PRO A 1 178 ? -48.132 -35.396 59.983  1.000 155.115 ? 507 PRO AAA CB  1 
ATOM   1383  C CG  . PRO A 1 178 ? -46.878 -34.733 60.517  1.000 157.519 ? 507 PRO AAA CG  1 
ATOM   1384  C CD  . PRO A 1 178 ? -45.869 -35.846 60.720  1.000 158.821 ? 507 PRO AAA CD  1 
ATOM   1385  N N   . TYR A 1 179 ? -48.051 -36.884 56.806  1.000 147.318 ? 508 TYR AAA N   1 
ATOM   1386  C CA  . TYR A 1 179 ? -48.040 -36.508 55.370  1.000 144.336 ? 508 TYR AAA CA  1 
ATOM   1387  C C   . TYR A 1 179 ? -49.336 -35.768 55.035  1.000 144.203 ? 508 TYR AAA C   1 
ATOM   1388  O O   . TYR A 1 179 ? -50.428 -36.186 55.472  1.000 142.992 ? 508 TYR AAA O   1 
ATOM   1389  C CB  . TYR A 1 179 ? -47.853 -37.731 54.475  1.000 141.682 ? 508 TYR AAA CB  1 
ATOM   1390  C CG  . TYR A 1 179 ? -46.445 -38.265 54.416  1.000 143.659 ? 508 TYR AAA CG  1 
ATOM   1391  C CD1 . TYR A 1 179 ? -45.805 -38.716 55.560  1.000 145.557 ? 508 TYR AAA CD1 1 
ATOM   1392  C CD2 . TYR A 1 179 ? -45.749 -38.340 53.218  1.000 144.643 ? 508 TYR AAA CD2 1 
ATOM   1393  C CE1 . TYR A 1 179 ? -44.515 -39.227 55.518  1.000 147.799 ? 508 TYR AAA CE1 1 
ATOM   1394  C CE2 . TYR A 1 179 ? -44.461 -38.853 53.159  1.000 147.060 ? 508 TYR AAA CE2 1 
ATOM   1395  C CZ  . TYR A 1 179 ? -43.839 -39.302 54.313  1.000 147.859 ? 508 TYR AAA CZ  1 
ATOM   1396  O OH  . TYR A 1 179 ? -42.574 -39.816 54.286  1.000 148.774 ? 508 TYR AAA OH  1 
ATOM   1397  N N   . ARG A 1 180 ? -49.202 -34.673 54.288  1.000 146.894 ? 509 ARG AAA N   1 
ATOM   1398  C CA  . ARG A 1 180 ? -50.338 -33.886 53.753  1.000 147.899 ? 509 ARG AAA CA  1 
ATOM   1399  C C   . ARG A 1 180 ? -50.686 -34.435 52.373  1.000 145.400 ? 509 ARG AAA C   1 
ATOM   1400  O O   . ARG A 1 180 ? -49.780 -34.536 51.529  1.000 147.517 ? 509 ARG AAA O   1 
ATOM   1401  C CB  . ARG A 1 180 ? -49.991 -32.400 53.686  1.000 152.458 ? 509 ARG AAA CB  1 
ATOM   1402  C CG  . ARG A 1 180 ? -49.876 -31.753 55.055  1.000 156.596 ? 509 ARG AAA CG  1 
ATOM   1403  C CD  . ARG A 1 180 ? -49.560 -30.282 54.985  1.000 160.623 ? 509 ARG AAA CD  1 
ATOM   1404  N NE  . ARG A 1 180 ? -49.818 -29.653 56.268  1.000 162.504 ? 509 ARG AAA NE  1 
ATOM   1405  C CZ  . ARG A 1 180 ? -49.958 -28.346 56.451  1.000 165.947 ? 509 ARG AAA CZ  1 
ATOM   1406  N NH1 . ARG A 1 180 ? -49.857 -27.509 55.434  1.000 168.363 ? 509 ARG AAA NH1 1 
ATOM   1407  N NH2 . ARG A 1 180 ? -50.187 -27.875 57.661  1.000 168.445 ? 509 ARG AAA NH2 1 
ATOM   1408  N N   . VAL A 1 181 ? -51.961 -34.754 52.174  1.000 142.632 ? 510 VAL AAA N   1 
ATOM   1409  C CA  . VAL A 1 181 ? -52.491 -35.477 50.987  1.000 139.888 ? 510 VAL AAA CA  1 
ATOM   1410  C C   . VAL A 1 181 ? -53.531 -34.584 50.298  1.000 139.610 ? 510 VAL AAA C   1 
ATOM   1411  O O   . VAL A 1 181 ? -54.513 -34.198 50.964  1.000 140.508 ? 510 VAL AAA O   1 
ATOM   1412  C CB  . VAL A 1 181 ? -53.085 -36.829 51.425  1.000 138.973 ? 510 VAL AAA CB  1 
ATOM   1413  C CG1 . VAL A 1 181 ? -53.650 -37.617 50.253  1.000 139.018 ? 510 VAL AAA CG1 1 
ATOM   1414  C CG2 . VAL A 1 181 ? -52.067 -37.656 52.192  1.000 138.322 ? 510 VAL AAA CG2 1 
ATOM   1415  N N   . VAL A 1 182 ? -53.303 -34.256 49.022  1.000 137.736 ? 511 VAL AAA N   1 
ATOM   1416  C CA  . VAL A 1 182 ? -54.326 -33.695 48.092  1.000 135.396 ? 511 VAL AAA CA  1 
ATOM   1417  C C   . VAL A 1 182 ? -54.760 -34.808 47.135  1.000 132.315 ? 511 VAL AAA C   1 
ATOM   1418  O O   . VAL A 1 182 ? -53.886 -35.566 46.662  1.000 131.660 ? 511 VAL AAA O   1 
ATOM   1419  C CB  . VAL A 1 182 ? -53.783 -32.485 47.316  1.000 137.994 ? 511 VAL AAA CB  1 
ATOM   1420  C CG1 . VAL A 1 182 ? -54.825 -31.938 46.353  1.000 139.871 ? 511 VAL AAA CG1 1 
ATOM   1421  C CG2 . VAL A 1 182 ? -53.278 -31.397 48.253  1.000 140.168 ? 511 VAL AAA CG2 1 
ATOM   1422  N N   . VAL A 1 183 ? -56.057 -34.902 46.852  1.000 130.842 ? 512 VAL AAA N   1 
ATOM   1423  C CA  . VAL A 1 183 ? -56.608 -35.893 45.885  1.000 131.556 ? 512 VAL AAA CA  1 
ATOM   1424  C C   . VAL A 1 183 ? -57.398 -35.145 44.814  1.000 133.664 ? 512 VAL AAA C   1 
ATOM   1425  O O   . VAL A 1 183 ? -58.516 -34.678 45.103  1.000 135.612 ? 512 VAL AAA O   1 
ATOM   1426  C CB  . VAL A 1 183 ? -57.456 -36.966 46.583  1.000 131.435 ? 512 VAL AAA CB  1 
ATOM   1427  C CG1 . VAL A 1 183 ? -58.241 -37.813 45.587  1.000 131.375 ? 512 VAL AAA CG1 1 
ATOM   1428  C CG2 . VAL A 1 183 ? -56.572 -37.842 47.456  1.000 132.065 ? 512 VAL AAA CG2 1 
ATOM   1429  N N   . LEU A 1 184 ? -56.809 -35.045 43.624  1.000 134.090 ? 513 LEU AAA N   1 
ATOM   1430  C CA  . LEU A 1 184 ? -57.417 -34.388 42.447  1.000 134.996 ? 513 LEU AAA CA  1 
ATOM   1431  C C   . LEU A 1 184 ? -58.256 -35.429 41.707  1.000 135.724 ? 513 LEU AAA C   1 
ATOM   1432  O O   . LEU A 1 184 ? -57.661 -36.207 40.948  1.000 137.299 ? 513 LEU AAA O   1 
ATOM   1433  C CB  . LEU A 1 184 ? -56.296 -33.823 41.568  1.000 136.247 ? 513 LEU AAA CB  1 
ATOM   1434  C CG  . LEU A 1 184 ? -55.415 -32.763 42.227  1.000 136.525 ? 513 LEU AAA CG  1 
ATOM   1435  C CD1 . LEU A 1 184 ? -54.395 -32.229 41.236  1.000 138.387 ? 513 LEU AAA CD1 1 
ATOM   1436  C CD2 . LEU A 1 184 ? -56.252 -31.623 42.796  1.000 137.015 ? 513 LEU AAA CD2 1 
ATOM   1437  N N   . SER A 1 185 ? -59.567 -35.466 41.975  1.000 136.403 ? 514 SER AAA N   1 
ATOM   1438  C CA  . SER A 1 185 ? -60.583 -36.208 41.180  1.000 138.656 ? 514 SER AAA CA  1 
ATOM   1439  C C   . SER A 1 185 ? -61.020 -35.328 40.002  1.000 142.203 ? 514 SER AAA C   1 
ATOM   1440  O O   . SER A 1 185 ? -61.180 -34.105 40.205  1.000 145.083 ? 514 SER AAA O   1 
ATOM   1441  C CB  . SER A 1 185 ? -61.763 -36.644 42.024  1.000 138.377 ? 514 SER AAA CB  1 
ATOM   1442  O OG  . SER A 1 185 ? -61.812 -35.928 43.251  1.000 136.791 ? 514 SER AAA OG  1 
ATOM   1443  N N   . PHE A 1 186 ? -61.160 -35.925 38.816  1.000 144.816 ? 515 PHE AAA N   1 
ATOM   1444  C CA  . PHE A 1 186 ? -61.645 -35.271 37.574  1.000 148.616 ? 515 PHE AAA CA  1 
ATOM   1445  C C   . PHE A 1 186 ? -62.954 -35.930 37.151  1.000 155.056 ? 515 PHE AAA C   1 
ATOM   1446  O O   . PHE A 1 186 ? -62.977 -37.169 37.037  1.000 158.275 ? 515 PHE AAA O   1 
ATOM   1447  C CB  . PHE A 1 186 ? -60.640 -35.437 36.433  1.000 148.218 ? 515 PHE AAA CB  1 
ATOM   1448  C CG  . PHE A 1 186 ? -59.294 -34.823 36.712  1.000 145.250 ? 515 PHE AAA CG  1 
ATOM   1449  C CD1 . PHE A 1 186 ? -59.100 -33.464 36.544  1.000 145.388 ? 515 PHE AAA CD1 1 
ATOM   1450  C CD2 . PHE A 1 186 ? -58.227 -35.593 37.145  1.000 142.488 ? 515 PHE AAA CD2 1 
ATOM   1451  C CE1 . PHE A 1 186 ? -57.867 -32.881 36.793  1.000 144.077 ? 515 PHE AAA CE1 1 
ATOM   1452  C CE2 . PHE A 1 186 ? -56.995 -35.010 37.401  1.000 140.758 ? 515 PHE AAA CE2 1 
ATOM   1453  C CZ  . PHE A 1 186 ? -56.818 -33.656 37.230  1.000 141.700 ? 515 PHE AAA CZ  1 
ATOM   1454  N N   . GLU A 1 187 ? -63.998 -35.138 36.911  1.000 160.939 ? 516 GLU AAA N   1 
ATOM   1455  C CA  . GLU A 1 187 ? -65.255 -35.653 36.310  1.000 166.426 ? 516 GLU AAA CA  1 
ATOM   1456  C C   . GLU A 1 187 ? -65.450 -34.985 34.948  1.000 171.142 ? 516 GLU AAA C   1 
ATOM   1457  O O   . GLU A 1 187 ? -64.985 -33.840 34.767  1.000 171.467 ? 516 GLU AAA O   1 
ATOM   1458  C CB  . GLU A 1 187 ? -66.446 -35.463 37.251  1.000 167.898 ? 516 GLU AAA CB  1 
ATOM   1459  C CG  . GLU A 1 187 ? -66.683 -34.030 37.688  1.000 168.953 ? 516 GLU AAA CG  1 
ATOM   1460  C CD  . GLU A 1 187 ? -68.011 -33.812 38.399  1.000 173.282 ? 516 GLU AAA CD  1 
ATOM   1461  O OE1 . GLU A 1 187 ? -68.424 -34.699 39.175  1.000 174.400 ? 516 GLU AAA OE1 1 
ATOM   1462  O OE2 . GLU A 1 187 ? -68.644 -32.762 38.165  1.000 177.864 ? 516 GLU AAA OE2 1 
ATOM   1463  N N   . LEU A 1 188 ? -66.078 -35.715 34.026  1.000 175.682 ? 517 LEU AAA N   1 
ATOM   1464  C CA  . LEU A 1 188 ? -66.424 -35.268 32.653  1.000 180.993 ? 517 LEU AAA CA  1 
ATOM   1465  C C   . LEU A 1 188 ? -67.896 -35.623 32.425  1.000 186.914 ? 517 LEU AAA C   1 
ATOM   1466  O O   . LEU A 1 188 ? -68.181 -36.798 32.121  1.000 189.249 ? 517 LEU AAA O   1 
ATOM   1467  C CB  . LEU A 1 188 ? -65.496 -35.972 31.656  1.000 181.495 ? 517 LEU AAA CB  1 
ATOM   1468  C CG  . LEU A 1 188 ? -65.288 -35.284 30.307  1.000 184.260 ? 517 LEU AAA CG  1 
ATOM   1469  C CD1 . LEU A 1 188 ? -64.018 -35.792 29.638  1.000 183.769 ? 517 LEU AAA CD1 1 
ATOM   1470  C CD2 . LEU A 1 188 ? -66.486 -35.484 29.390  1.000 188.024 ? 517 LEU AAA CD2 1 
ATOM   1471  N N   . LEU A 1 189 ? -68.798 -34.653 32.619  1.000 191.685 ? 518 LEU AAA N   1 
ATOM   1472  C CA  . LEU A 1 189 ? -70.273 -34.831 32.483  1.000 196.772 ? 518 LEU AAA CA  1 
ATOM   1473  C C   . LEU A 1 189 ? -70.645 -34.726 30.991  1.000 201.078 ? 518 LEU AAA C   1 
ATOM   1474  O O   . LEU A 1 189 ? -69.796 -35.093 30.143  1.000 199.887 ? 518 LEU AAA O   1 
ATOM   1475  C CB  . LEU A 1 189 ? -71.001 -33.780 33.339  1.000 197.626 ? 518 LEU AAA CB  1 
ATOM   1476  C CG  . LEU A 1 189 ? -70.556 -33.641 34.799  1.000 192.665 ? 518 LEU AAA CG  1 
ATOM   1477  C CD1 . LEU A 1 189 ? -71.455 -32.659 35.544  1.000 194.484 ? 518 LEU AAA CD1 1 
ATOM   1478  C CD2 . LEU A 1 189 ? -70.542 -34.986 35.514  1.000 190.004 ? 518 LEU AAA CD2 1 
ATOM   1479  N N   . HIS A 1 190 ? -71.874 -34.297 30.675  1.000 204.582 ? 519 HIS AAA N   1 
ATOM   1480  C CA  . HIS A 1 190 ? -72.297 -33.861 29.314  1.000 208.832 ? 519 HIS AAA CA  1 
ATOM   1481  C C   . HIS A 1 190 ? -72.680 -32.372 29.363  1.000 208.800 ? 519 HIS AAA C   1 
ATOM   1482  O O   . HIS A 1 190 ? -73.440 -31.928 28.475  1.000 213.777 ? 519 HIS AAA O   1 
ATOM   1483  C CB  . HIS A 1 190 ? -73.408 -34.773 28.752  1.000 215.176 ? 519 HIS AAA CB  1 
ATOM   1484  C CG  . HIS A 1 190 ? -72.946 -35.763 27.727  1.000 217.755 ? 519 HIS AAA CG  1 
ATOM   1485  N ND1 . HIS A 1 190 ? -73.112 -35.571 26.360  1.000 221.937 ? 519 HIS AAA ND1 1 
ATOM   1486  C CD2 . HIS A 1 190 ? -72.325 -36.956 27.866  1.000 215.971 ? 519 HIS AAA CD2 1 
ATOM   1487  C CE1 . HIS A 1 190 ? -72.610 -36.602 25.710  1.000 222.459 ? 519 HIS AAA CE1 1 
ATOM   1488  N NE2 . HIS A 1 190 ? -72.122 -37.467 26.611  1.000 219.223 ? 519 HIS AAA NE2 1 
ATOM   1489  N N   . ALA A 1 191 ? -72.141 -31.627 30.341  1.000 202.907 ? 520 ALA AAA N   1 
ATOM   1490  C CA  . ALA A 1 191 ? -72.247 -30.149 30.468  1.000 203.348 ? 520 ALA AAA CA  1 
ATOM   1491  C C   . ALA A 1 191 ? -70.950 -29.507 29.973  1.000 200.877 ? 520 ALA AAA C   1 
ATOM   1492  O O   . ALA A 1 191 ? -69.898 -30.126 30.080  1.000 196.306 ? 520 ALA AAA O   1 
ATOM   1493  C CB  . ALA A 1 191 ? -72.538 -29.774 31.900  1.000 201.142 ? 520 ALA AAA CB  1 
ATOM   1494  N N   . PRO A 1 192 ? -70.977 -28.289 29.375  1.000 204.520 ? 521 PRO AAA N   1 
ATOM   1495  C CA  . PRO A 1 192 ? -69.763 -27.664 28.837  1.000 204.691 ? 521 PRO AAA CA  1 
ATOM   1496  C C   . PRO A 1 192 ? -68.624 -27.544 29.866  1.000 201.120 ? 521 PRO AAA C   1 
ATOM   1497  O O   . PRO A 1 192 ? -68.832 -26.889 30.872  1.000 199.477 ? 521 PRO AAA O   1 
ATOM   1498  C CB  . PRO A 1 192 ? -70.237 -26.277 28.370  1.000 209.143 ? 521 PRO AAA CB  1 
ATOM   1499  C CG  . PRO A 1 192 ? -71.708 -26.470 28.080  1.000 213.080 ? 521 PRO AAA CG  1 
ATOM   1500  C CD  . PRO A 1 192 ? -72.177 -27.478 29.111  1.000 209.954 ? 521 PRO AAA CD  1 
ATOM   1501  N N   . ALA A 1 193 ? -67.470 -28.168 29.573  1.000 200.788 ? 522 ALA AAA N   1 
ATOM   1502  C CA  . ALA A 1 193 ? -66.276 -28.306 30.452  1.000 196.891 ? 522 ALA AAA CA  1 
ATOM   1503  C C   . ALA A 1 193 ? -65.712 -26.923 30.803  1.000 199.888 ? 522 ALA AAA C   1 
ATOM   1504  O O   . ALA A 1 193 ? -66.003 -25.965 30.058  1.000 205.898 ? 522 ALA AAA O   1 
ATOM   1505  C CB  . ALA A 1 193 ? -65.219 -29.169 29.788  1.000 195.049 ? 522 ALA AAA CB  1 
ATOM   1506  N N   . THR A 1 194 ? -64.945 -26.816 31.899  1.000 198.254 ? 523 THR AAA N   1 
ATOM   1507  C CA  . THR A 1 194 ? -64.453 -25.516 32.442  1.000 200.954 ? 523 THR AAA CA  1 
ATOM   1508  C C   . THR A 1 194 ? -63.151 -25.648 33.258  1.000 198.594 ? 523 THR AAA C   1 
ATOM   1509  O O   . THR A 1 194 ? -62.905 -24.742 34.086  1.000 199.682 ? 523 THR AAA O   1 
ATOM   1510  C CB  . THR A 1 194 ? -65.519 -24.848 33.326  1.000 202.159 ? 523 THR AAA CB  1 
ATOM   1511  O OG1 . THR A 1 194 ? -65.648 -25.612 34.527  1.000 197.666 ? 523 THR AAA OG1 1 
ATOM   1512  C CG2 . THR A 1 194 ? -66.868 -24.703 32.654  1.000 205.791 ? 523 THR AAA CG2 1 
ATOM   1513  N N   . VAL A 1 195 ? -62.325 -26.685 33.055  1.000 195.731 ? 524 VAL AAA N   1 
ATOM   1514  C CA  . VAL A 1 195 ? -60.998 -26.796 33.743  1.000 191.764 ? 524 VAL AAA CA  1 
ATOM   1515  C C   . VAL A 1 195 ? -59.978 -27.465 32.813  1.000 194.113 ? 524 VAL AAA C   1 
ATOM   1516  O O   . VAL A 1 195 ? -59.726 -28.690 32.967  1.000 192.057 ? 524 VAL AAA O   1 
ATOM   1517  C CB  . VAL A 1 195 ? -61.082 -27.529 35.095  1.000 184.533 ? 524 VAL AAA CB  1 
ATOM   1518  C CG1 . VAL A 1 195 ? -59.810 -27.307 35.893  1.000 181.706 ? 524 VAL AAA CG1 1 
ATOM   1519  C CG2 . VAL A 1 195 ? -62.300 -27.121 35.909  1.000 184.507 ? 524 VAL AAA CG2 1 
ATOM   1520  N N   . CYS A 1 196 ? -59.380 -26.663 31.924  1.000 197.566 ? 525 CYS AAA N   1 
ATOM   1521  C CA  . CYS A 1 196 ? -58.378 -27.081 30.909  1.000 198.242 ? 525 CYS AAA CA  1 
ATOM   1522  C C   . CYS A 1 196 ? -56.991 -26.568 31.316  1.000 199.395 ? 525 CYS AAA C   1 
ATOM   1523  O O   . CYS A 1 196 ? -56.909 -25.827 32.312  1.000 194.744 ? 525 CYS AAA O   1 
ATOM   1524  C CB  . CYS A 1 196 ? -58.756 -26.559 29.526  1.000 202.263 ? 525 CYS AAA CB  1 
ATOM   1525  S SG  . CYS A 1 196 ? -60.543 -26.546 29.215  1.000 199.415 ? 525 CYS AAA SG  1 
ATOM   1526  N N   . GLY A 1 197 ? -55.952 -26.968 30.577  1.000 204.997 ? 526 GLY AAA N   1 
ATOM   1527  C CA  . GLY A 1 197 ? -54.571 -26.462 30.717  1.000 209.703 ? 526 GLY AAA CA  1 
ATOM   1528  C C   . GLY A 1 197 ? -54.116 -25.703 29.470  1.000 219.177 ? 526 GLY AAA C   1 
ATOM   1529  O O   . GLY A 1 197 ? -54.933 -25.412 28.596  1.000 220.796 ? 526 GLY AAA O   1 
ATOM   1530  N N   . PRO A 1 198 ? -52.807 -25.351 29.361  1.000 225.404 ? 527 PRO AAA N   1 
ATOM   1531  C CA  . PRO A 1 198 ? -52.286 -24.607 28.205  1.000 233.725 ? 527 PRO AAA CA  1 
ATOM   1532  C C   . PRO A 1 198 ? -52.335 -25.334 26.840  1.000 238.433 ? 527 PRO AAA C   1 
ATOM   1533  O O   . PRO A 1 198 ? -53.273 -25.067 26.099  1.000 240.941 ? 527 PRO AAA O   1 
ATOM   1534  C CB  . PRO A 1 198 ? -50.836 -24.267 28.618  1.000 235.881 ? 527 PRO AAA CB  1 
ATOM   1535  C CG  . PRO A 1 198 ? -50.472 -25.285 29.682  1.000 229.179 ? 527 PRO AAA CG  1 
ATOM   1536  C CD  . PRO A 1 198 ? -51.776 -25.589 30.388  1.000 223.087 ? 527 PRO AAA CD  1 
ATOM   1537  N N   . LYS A 1 199 ? -51.354 -26.207 26.535  1.000 240.039 ? 528 LYS AAA N   1 
ATOM   1538  C CA  . LYS A 1 199 ? -51.112 -26.856 25.205  1.000 242.912 ? 528 LYS AAA CA  1 
ATOM   1539  C C   . LYS A 1 199 ? -52.432 -27.028 24.438  1.000 242.656 ? 528 LYS AAA C   1 
ATOM   1540  O O   . LYS A 1 199 ? -52.510 -27.694 23.396  1.000 243.768 ? 528 LYS AAA O   1 
ATOM   1541  C CB  . LYS A 1 199 ? -50.420 -28.217 25.377  1.000 238.643 ? 528 LYS AAA CB  1 
ATOM   1542  C CG  . LYS A 1 199 ? -48.903 -28.188 25.515  1.000 239.653 ? 528 LYS AAA CG  1 
ATOM   1543  C CD  . LYS A 1 199 ? -48.186 -28.061 24.192  1.000 246.819 ? 528 LYS AAA CD  1 
ATOM   1544  C CE  . LYS A 1 199 ? -46.740 -28.500 24.256  1.000 249.342 ? 528 LYS AAA CE  1 
ATOM   1545  N NZ  . LYS A 1 199 ? -46.105 -28.452 22.919  1.000 258.538 ? 528 LYS AAA NZ  1 
ATOM   1546  N N   . THR B 2 1   ? -38.416 -32.408 25.457  1.000 150.721 ? 0   THR BBB N   1 
ATOM   1547  C CA  . THR B 2 1   ? -39.598 -33.230 25.861  1.000 148.764 ? 0   THR BBB CA  1 
ATOM   1548  C C   . THR B 2 1   ? -39.647 -33.344 27.384  1.000 142.770 ? 0   THR BBB C   1 
ATOM   1549  O O   . THR B 2 1   ? -38.685 -32.911 28.035  1.000 138.656 ? 0   THR BBB O   1 
ATOM   1550  C CB  . THR B 2 1   ? -39.580 -34.639 25.250  1.000 149.731 ? 0   THR BBB CB  1 
ATOM   1551  O OG1 . THR B 2 1   ? -40.701 -35.355 25.778  1.000 151.186 ? 0   THR BBB OG1 1 
ATOM   1552  C CG2 . THR B 2 1   ? -38.304 -35.404 25.536  1.000 147.330 ? 0   THR BBB CG2 1 
ATOM   1553  N N   . GLN B 2 2   ? -40.727 -33.937 27.897  1.000 140.673 ? 1   GLN BBB N   1 
ATOM   1554  C CA  . GLN B 2 2   ? -40.998 -34.100 29.347  1.000 141.003 ? 1   GLN BBB CA  1 
ATOM   1555  C C   . GLN B 2 2   ? -40.046 -35.146 29.924  1.000 137.075 ? 1   GLN BBB C   1 
ATOM   1556  O O   . GLN B 2 2   ? -39.320 -34.821 30.897  1.000 137.233 ? 1   GLN BBB O   1 
ATOM   1557  C CB  . GLN B 2 2   ? -42.451 -34.527 29.581  1.000 142.287 ? 1   GLN BBB CB  1 
ATOM   1558  C CG  . GLN B 2 2   ? -42.828 -34.688 31.053  1.000 142.644 ? 1   GLN BBB CG  1 
ATOM   1559  C CD  . GLN B 2 2   ? -43.103 -33.376 31.755  1.000 145.418 ? 1   GLN BBB CD  1 
ATOM   1560  O OE1 . GLN B 2 2   ? -43.818 -32.505 31.249  1.000 146.984 ? 1   GLN BBB OE1 1 
ATOM   1561  N NE2 . GLN B 2 2   ? -42.546 -33.230 32.949  1.000 143.027 ? 1   GLN BBB NE2 1 
ATOM   1562  N N   . MET B 2 3   ? -40.078 -36.347 29.340  1.000 132.620 ? 2   MET BBB N   1 
ATOM   1563  C CA  . MET B 2 3   ? -39.465 -37.580 29.898  1.000 129.902 ? 2   MET BBB CA  1 
ATOM   1564  C C   . MET B 2 3   ? -38.894 -38.419 28.758  1.000 125.580 ? 2   MET BBB C   1 
ATOM   1565  O O   . MET B 2 3   ? -39.604 -38.591 27.760  1.000 127.357 ? 2   MET BBB O   1 
ATOM   1566  C CB  . MET B 2 3   ? -40.515 -38.412 30.643  1.000 131.135 ? 2   MET BBB CB  1 
ATOM   1567  C CG  . MET B 2 3   ? -39.940 -39.565 31.460  1.000 130.729 ? 2   MET BBB CG  1 
ATOM   1568  S SD  . MET B 2 3   ? -38.597 -39.102 32.596  1.000 132.001 ? 2   MET BBB SD  1 
ATOM   1569  C CE  . MET B 2 3   ? -39.257 -37.623 33.357  1.000 133.551 ? 2   MET BBB CE  1 
ATOM   1570  N N   . GLN B 2 4   ? -37.668 -38.919 28.926  1.000 120.497 ? 3   GLN BBB N   1 
ATOM   1571  C CA  . GLN B 2 4   ? -36.973 -39.842 27.991  1.000 116.317 ? 3   GLN BBB CA  1 
ATOM   1572  C C   . GLN B 2 4   ? -36.436 -41.005 28.823  1.000 114.106 ? 3   GLN BBB C   1 
ATOM   1573  O O   . GLN B 2 4   ? -35.967 -40.757 29.942  1.000 115.143 ? 3   GLN BBB O   1 
ATOM   1574  C CB  . GLN B 2 4   ? -35.844 -39.095 27.285  1.000 115.627 ? 3   GLN BBB CB  1 
ATOM   1575  C CG  . GLN B 2 4   ? -35.143 -39.878 26.191  1.000 113.001 ? 3   GLN BBB CG  1 
ATOM   1576  C CD  . GLN B 2 4   ? -33.951 -39.098 25.689  1.000 113.799 ? 3   GLN BBB CD  1 
ATOM   1577  O OE1 . GLN B 2 4   ? -33.819 -37.896 25.930  1.000 114.841 ? 3   GLN BBB OE1 1 
ATOM   1578  N NE2 . GLN B 2 4   ? -33.061 -39.780 24.990  1.000 113.299 ? 3   GLN BBB NE2 1 
ATOM   1579  N N   . LEU B 2 5   ? -36.521 -42.231 28.321  1.000 112.019 ? 4   LEU BBB N   1 
ATOM   1580  C CA  . LEU B 2 5   ? -36.069 -43.422 29.080  1.000 110.896 ? 4   LEU BBB CA  1 
ATOM   1581  C C   . LEU B 2 5   ? -34.822 -43.993 28.415  1.000 112.427 ? 4   LEU BBB C   1 
ATOM   1582  O O   . LEU B 2 5   ? -34.877 -44.311 27.207  1.000 115.814 ? 4   LEU BBB O   1 
ATOM   1583  C CB  . LEU B 2 5   ? -37.201 -44.443 29.133  1.000 110.047 ? 4   LEU BBB CB  1 
ATOM   1584  C CG  . LEU B 2 5   ? -38.471 -43.937 29.805  1.000 112.413 ? 4   LEU BBB CG  1 
ATOM   1585  C CD1 . LEU B 2 5   ? -39.505 -45.051 29.903  1.000 113.442 ? 4   LEU BBB CD1 1 
ATOM   1586  C CD2 . LEU B 2 5   ? -38.166 -43.349 31.178  1.000 114.029 ? 4   LEU BBB CD2 1 
ATOM   1587  N N   . VAL B 2 6   ? -33.737 -44.071 29.181  1.000 111.763 ? 5   VAL BBB N   1 
ATOM   1588  C CA  . VAL B 2 6   ? -32.447 -44.669 28.744  1.000 112.178 ? 5   VAL BBB CA  1 
ATOM   1589  C C   . VAL B 2 6   ? -32.397 -46.071 29.339  1.000 113.015 ? 5   VAL BBB C   1 
ATOM   1590  O O   . VAL B 2 6   ? -32.911 -46.254 30.455  1.000 113.142 ? 5   VAL BBB O   1 
ATOM   1591  C CB  . VAL B 2 6   ? -31.243 -43.815 29.178  1.000 113.420 ? 5   VAL BBB CB  1 
ATOM   1592  C CG1 . VAL B 2 6   ? -31.599 -42.334 29.194  1.000 113.385 ? 5   VAL BBB CG1 1 
ATOM   1593  C CG2 . VAL B 2 6   ? -30.673 -44.256 30.522  1.000 115.753 ? 5   VAL BBB CG2 1 
ATOM   1594  N N   . GLN B 2 7   ? -31.823 -47.020 28.609  1.000 114.959 ? 6   GLN BBB N   1 
ATOM   1595  C CA  . GLN B 2 7   ? -31.788 -48.442 29.024  1.000 116.919 ? 6   GLN BBB CA  1 
ATOM   1596  C C   . GLN B 2 7   ? -30.343 -48.926 29.015  1.000 120.180 ? 6   GLN BBB C   1 
ATOM   1597  O O   . GLN B 2 7   ? -29.553 -48.403 28.206  1.000 119.697 ? 6   GLN BBB O   1 
ATOM   1598  C CB  . GLN B 2 7   ? -32.663 -49.290 28.104  1.000 114.411 ? 6   GLN BBB CB  1 
ATOM   1599  C CG  . GLN B 2 7   ? -34.135 -48.913 28.168  1.000 112.193 ? 6   GLN BBB CG  1 
ATOM   1600  C CD  . GLN B 2 7   ? -35.024 -50.095 27.882  1.000 111.532 ? 6   GLN BBB CD  1 
ATOM   1601  O OE1 . GLN B 2 7   ? -35.994 -49.994 27.128  1.000 109.761 ? 6   GLN BBB OE1 1 
ATOM   1602  N NE2 . GLN B 2 7   ? -34.697 -51.223 28.500  1.000 112.088 ? 6   GLN BBB NE2 1 
ATOM   1603  N N   . SER B 2 8   ? -30.031 -49.882 29.893  1.000 124.406 ? 7   SER BBB N   1 
ATOM   1604  C CA  . SER B 2 8   ? -28.718 -50.570 29.955  1.000 126.968 ? 7   SER BBB CA  1 
ATOM   1605  C C   . SER B 2 8   ? -28.372 -51.085 28.555  1.000 129.557 ? 7   SER BBB C   1 
ATOM   1606  O O   . SER B 2 8   ? -29.305 -51.294 27.737  1.000 127.268 ? 7   SER BBB O   1 
ATOM   1607  C CB  . SER B 2 8   ? -28.715 -51.683 30.969  1.000 127.077 ? 7   SER BBB CB  1 
ATOM   1608  O OG  . SER B 2 8   ? -29.660 -52.687 30.628  1.000 126.959 ? 7   SER BBB OG  1 
ATOM   1609  N N   . GLY B 2 9   ? -27.074 -51.257 28.295  1.000 133.594 ? 8   GLY BBB N   1 
ATOM   1610  C CA  . GLY B 2 9   ? -26.541 -51.753 27.014  1.000 133.791 ? 8   GLY BBB CA  1 
ATOM   1611  C C   . GLY B 2 9   ? -26.971 -53.182 26.729  1.000 133.198 ? 8   GLY BBB C   1 
ATOM   1612  O O   . GLY B 2 9   ? -27.807 -53.733 27.481  1.000 131.807 ? 8   GLY BBB O   1 
ATOM   1613  N N   . THR B 2 10  ? -26.405 -53.763 25.672  1.000 132.883 ? 9   THR BBB N   1 
ATOM   1614  C CA  . THR B 2 10  ? -26.701 -55.137 25.199  1.000 132.451 ? 9   THR BBB CA  1 
ATOM   1615  C C   . THR B 2 10  ? -25.982 -56.147 26.093  1.000 135.264 ? 9   THR BBB C   1 
ATOM   1616  O O   . THR B 2 10  ? -24.797 -55.907 26.403  1.000 135.717 ? 9   THR BBB O   1 
ATOM   1617  C CB  . THR B 2 10  ? -26.287 -55.305 23.737  1.000 130.206 ? 9   THR BBB CB  1 
ATOM   1618  O OG1 . THR B 2 10  ? -26.777 -54.157 23.044  1.000 125.894 ? 9   THR BBB OG1 1 
ATOM   1619  C CG2 . THR B 2 10  ? -26.817 -56.586 23.129  1.000 131.999 ? 9   THR BBB CG2 1 
ATOM   1620  N N   . GLU B 2 11  ? -26.677 -57.231 26.456  1.000 136.404 ? 10  GLU BBB N   1 
ATOM   1621  C CA  . GLU B 2 11  ? -26.206 -58.272 27.409  1.000 138.166 ? 10  GLU BBB CA  1 
ATOM   1622  C C   . GLU B 2 11  ? -26.114 -59.624 26.689  1.000 138.626 ? 10  GLU BBB C   1 
ATOM   1623  O O   . GLU B 2 11  ? -27.182 -60.151 26.283  1.000 138.191 ? 10  GLU BBB O   1 
ATOM   1624  C CB  . GLU B 2 11  ? -27.155 -58.342 28.608  1.000 138.690 ? 10  GLU BBB CB  1 
ATOM   1625  C CG  . GLU B 2 11  ? -27.310 -57.022 29.355  1.000 138.379 ? 10  GLU BBB CG  1 
ATOM   1626  C CD  . GLU B 2 11  ? -26.206 -56.665 30.341  1.000 140.369 ? 10  GLU BBB CD  1 
ATOM   1627  O OE1 . GLU B 2 11  ? -25.127 -57.291 30.296  1.000 141.426 ? 10  GLU BBB OE1 1 
ATOM   1628  O OE2 . GLU B 2 11  ? -26.428 -55.753 31.159  1.000 140.525 ? 10  GLU BBB OE2 1 
ATOM   1629  N N   . VAL B 2 12  ? -24.887 -60.134 26.514  1.000 140.541 ? 11  VAL BBB N   1 
ATOM   1630  C CA  . VAL B 2 12  ? -24.584 -61.520 26.040  1.000 143.534 ? 11  VAL BBB CA  1 
ATOM   1631  C C   . VAL B 2 12  ? -24.295 -62.372 27.279  1.000 145.432 ? 11  VAL BBB C   1 
ATOM   1632  O O   . VAL B 2 12  ? -23.234 -62.156 27.911  1.000 147.623 ? 11  VAL BBB O   1 
ATOM   1633  C CB  . VAL B 2 12  ? -23.392 -61.567 25.060  1.000 146.056 ? 11  VAL BBB CB  1 
ATOM   1634  C CG1 . VAL B 2 12  ? -23.280 -62.927 24.385  1.000 148.311 ? 11  VAL BBB CG1 1 
ATOM   1635  C CG2 . VAL B 2 12  ? -23.446 -60.463 24.014  1.000 143.951 ? 11  VAL BBB CG2 1 
ATOM   1636  N N   . LYS B 2 13  ? -25.202 -63.283 27.628  1.000 145.200 ? 12  LYS BBB N   1 
ATOM   1637  C CA  . LYS B 2 13  ? -25.125 -64.061 28.892  1.000 148.491 ? 12  LYS BBB CA  1 
ATOM   1638  C C   . LYS B 2 13  ? -25.210 -65.556 28.580  1.000 151.723 ? 12  LYS BBB C   1 
ATOM   1639  O O   . LYS B 2 13  ? -25.722 -65.918 27.493  1.000 151.049 ? 12  LYS BBB O   1 
ATOM   1640  C CB  . LYS B 2 13  ? -26.226 -63.617 29.863  1.000 147.124 ? 12  LYS BBB CB  1 
ATOM   1641  C CG  . LYS B 2 13  ? -26.151 -62.157 30.293  1.000 145.332 ? 12  LYS BBB CG  1 
ATOM   1642  C CD  . LYS B 2 13  ? -24.999 -61.844 31.227  1.000 147.872 ? 12  LYS BBB CD  1 
ATOM   1643  C CE  . LYS B 2 13  ? -25.301 -62.181 32.674  1.000 151.347 ? 12  LYS BBB CE  1 
ATOM   1644  N NZ  . LYS B 2 13  ? -24.067 -62.348 33.485  1.000 154.639 ? 12  LYS BBB NZ  1 
ATOM   1645  N N   . LYS B 2 14  ? -24.709 -66.368 29.513  1.000 156.211 ? 13  LYS BBB N   1 
ATOM   1646  C CA  . LYS B 2 14  ? -24.772 -67.847 29.485  1.000 159.979 ? 13  LYS BBB CA  1 
ATOM   1647  C C   . LYS B 2 14  ? -26.021 -68.297 30.234  1.000 158.359 ? 13  LYS BBB C   1 
ATOM   1648  O O   . LYS B 2 14  ? -26.399 -67.708 31.248  1.000 157.081 ? 13  LYS BBB O   1 
ATOM   1649  C CB  . LYS B 2 14  ? -23.505 -68.444 30.108  1.000 166.993 ? 13  LYS BBB CB  1 
ATOM   1650  C CG  . LYS B 2 14  ? -22.243 -68.283 29.275  1.000 170.251 ? 13  LYS BBB CG  1 
ATOM   1651  C CD  . LYS B 2 14  ? -22.163 -69.261 28.112  1.000 174.008 ? 13  LYS BBB CD  1 
ATOM   1652  C CE  . LYS B 2 14  ? -20.843 -69.235 27.365  1.000 176.372 ? 13  LYS BBB CE  1 
ATOM   1653  N NZ  . LYS B 2 14  ? -20.697 -68.025 26.516  1.000 173.578 ? 13  LYS BBB NZ  1 
ATOM   1654  N N   . PRO B 2 15  ? -26.701 -69.357 29.749  1.000 157.432 ? 14  PRO BBB N   1 
ATOM   1655  C CA  . PRO B 2 15  ? -27.829 -69.941 30.469  1.000 157.424 ? 14  PRO BBB CA  1 
ATOM   1656  C C   . PRO B 2 15  ? -27.474 -70.258 31.931  1.000 157.709 ? 14  PRO BBB C   1 
ATOM   1657  O O   . PRO B 2 15  ? -26.499 -70.942 32.173  1.000 158.725 ? 14  PRO BBB O   1 
ATOM   1658  C CB  . PRO B 2 15  ? -28.135 -71.229 29.690  1.000 161.220 ? 14  PRO BBB CB  1 
ATOM   1659  C CG  . PRO B 2 15  ? -27.599 -70.976 28.295  1.000 159.523 ? 14  PRO BBB CG  1 
ATOM   1660  C CD  . PRO B 2 15  ? -26.418 -70.048 28.482  1.000 158.141 ? 14  PRO BBB CD  1 
ATOM   1661  N N   . GLY B 2 16  ? -28.275 -69.744 32.862  1.000 155.800 ? 15  GLY BBB N   1 
ATOM   1662  C CA  . GLY B 2 16  ? -28.128 -69.994 34.305  1.000 160.284 ? 15  GLY BBB CA  1 
ATOM   1663  C C   . GLY B 2 16  ? -27.699 -68.741 35.043  1.000 159.574 ? 15  GLY BBB C   1 
ATOM   1664  O O   . GLY B 2 16  ? -28.171 -68.537 36.184  1.000 163.024 ? 15  GLY BBB O   1 
ATOM   1665  N N   . GLU B 2 17  ? -26.839 -67.927 34.423  1.000 156.867 ? 16  GLU BBB N   1 
ATOM   1666  C CA  . GLU B 2 17  ? -26.336 -66.660 35.019  1.000 155.057 ? 16  GLU BBB CA  1 
ATOM   1667  C C   . GLU B 2 17  ? -27.537 -65.776 35.367  1.000 149.893 ? 16  GLU BBB C   1 
ATOM   1668  O O   . GLU B 2 17  ? -28.621 -66.003 34.808  1.000 148.607 ? 16  GLU BBB O   1 
ATOM   1669  C CB  . GLU B 2 17  ? -25.364 -65.950 34.073  1.000 154.876 ? 16  GLU BBB CB  1 
ATOM   1670  C CG  . GLU B 2 17  ? -23.959 -66.533 34.101  1.000 160.178 ? 16  GLU BBB CG  1 
ATOM   1671  C CD  . GLU B 2 17  ? -22.987 -66.010 33.052  1.000 159.714 ? 16  GLU BBB CD  1 
ATOM   1672  O OE1 . GLU B 2 17  ? -23.431 -65.313 32.124  1.000 156.304 ? 16  GLU BBB OE1 1 
ATOM   1673  O OE2 . GLU B 2 17  ? -21.780 -66.318 33.155  1.000 164.329 ? 16  GLU BBB OE2 1 
ATOM   1674  N N   . SER B 2 18  ? -27.339 -64.824 36.275  1.000 146.919 ? 17  SER BBB N   1 
ATOM   1675  C CA  . SER B 2 18  ? -28.346 -63.826 36.714  1.000 142.984 ? 17  SER BBB CA  1 
ATOM   1676  C C   . SER B 2 18  ? -28.014 -62.477 36.076  1.000 137.134 ? 17  SER BBB C   1 
ATOM   1677  O O   . SER B 2 18  ? -26.840 -62.268 35.742  1.000 135.586 ? 17  SER BBB O   1 
ATOM   1678  C CB  . SER B 2 18  ? -28.358 -63.742 38.202  1.000 146.614 ? 17  SER BBB CB  1 
ATOM   1679  O OG  . SER B 2 18  ? -27.044 -63.924 38.699  1.000 151.698 ? 17  SER BBB OG  1 
ATOM   1680  N N   . LEU B 2 19  ? -29.004 -61.597 35.931  1.000 134.070 ? 18  LEU BBB N   1 
ATOM   1681  C CA  . LEU B 2 19  ? -28.880 -60.354 35.125  1.000 132.575 ? 18  LEU BBB CA  1 
ATOM   1682  C C   . LEU B 2 19  ? -29.887 -59.305 35.600  1.000 131.325 ? 18  LEU BBB C   1 
ATOM   1683  O O   . LEU B 2 19  ? -31.073 -59.646 35.693  1.000 131.873 ? 18  LEU BBB O   1 
ATOM   1684  C CB  . LEU B 2 19  ? -29.154 -60.717 33.665  1.000 132.553 ? 18  LEU BBB CB  1 
ATOM   1685  C CG  . LEU B 2 19  ? -29.288 -59.533 32.709  1.000 130.609 ? 18  LEU BBB CG  1 
ATOM   1686  C CD1 . LEU B 2 19  ? -27.924 -58.910 32.440  1.000 131.528 ? 18  LEU BBB CD1 1 
ATOM   1687  C CD2 . LEU B 2 19  ? -29.966 -59.962 31.417  1.000 129.542 ? 18  LEU BBB CD2 1 
ATOM   1688  N N   . LYS B 2 20  ? -29.432 -58.068 35.826  1.000 131.910 ? 19  LYS BBB N   1 
ATOM   1689  C CA  . LYS B 2 20  ? -30.284 -56.908 36.202  1.000 132.175 ? 19  LYS BBB CA  1 
ATOM   1690  C C   . LYS B 2 20  ? -30.098 -55.786 35.178  1.000 129.922 ? 19  LYS BBB C   1 
ATOM   1691  O O   . LYS B 2 20  ? -29.065 -55.076 35.258  1.000 131.629 ? 19  LYS BBB O   1 
ATOM   1692  C CB  . LYS B 2 20  ? -29.930 -56.407 37.607  1.000 136.526 ? 19  LYS BBB CB  1 
ATOM   1693  C CG  . LYS B 2 20  ? -30.716 -55.191 38.082  1.000 136.624 ? 19  LYS BBB CG  1 
ATOM   1694  C CD  . LYS B 2 20  ? -30.749 -55.028 39.601  1.000 140.249 ? 19  LYS BBB CD  1 
ATOM   1695  C CE  . LYS B 2 20  ? -29.507 -54.381 40.179  1.000 142.727 ? 19  LYS BBB CE  1 
ATOM   1696  N NZ  . LYS B 2 20  ? -29.602 -54.259 41.653  1.000 146.012 ? 19  LYS BBB NZ  1 
ATOM   1697  N N   . ILE B 2 21  ? -31.062 -55.624 34.267  1.000 127.150 ? 20  ILE BBB N   1 
ATOM   1698  C CA  . ILE B 2 21  ? -31.052 -54.519 33.262  1.000 123.754 ? 20  ILE BBB CA  1 
ATOM   1699  C C   . ILE B 2 21  ? -31.722 -53.283 33.870  1.000 121.621 ? 20  ILE BBB C   1 
ATOM   1700  O O   . ILE B 2 21  ? -32.695 -53.426 34.640  1.000 120.821 ? 20  ILE BBB O   1 
ATOM   1701  C CB  . ILE B 2 21  ? -31.674 -54.936 31.915  1.000 122.506 ? 20  ILE BBB CB  1 
ATOM   1702  C CG1 . ILE B 2 21  ? -33.166 -55.263 32.008  1.000 122.757 ? 20  ILE BBB CG1 1 
ATOM   1703  C CG2 . ILE B 2 21  ? -30.880 -56.087 31.323  1.000 123.843 ? 20  ILE BBB CG2 1 
ATOM   1704  C CD1 . ILE B 2 21  ? -33.849 -55.308 30.664  1.000 121.909 ? 20  ILE BBB CD1 1 
ATOM   1705  N N   . SER B 2 22  ? -31.170 -52.114 33.550  1.000 120.425 ? 21  SER BBB N   1 
ATOM   1706  C CA  . SER B 2 22  ? -31.569 -50.798 34.098  1.000 119.087 ? 21  SER BBB CA  1 
ATOM   1707  C C   . SER B 2 22  ? -32.525 -50.126 33.117  1.000 115.621 ? 21  SER BBB C   1 
ATOM   1708  O O   . SER B 2 22  ? -32.654 -50.599 31.957  1.000 113.508 ? 21  SER BBB O   1 
ATOM   1709  C CB  . SER B 2 22  ? -30.364 -49.926 34.389  1.000 121.171 ? 21  SER BBB CB  1 
ATOM   1710  O OG  . SER B 2 22  ? -30.144 -48.971 33.355  1.000 121.922 ? 21  SER BBB OG  1 
ATOM   1711  N N   . CYS B 2 23  ? -33.174 -49.076 33.604  1.000 112.969 ? 22  CYS BBB N   1 
ATOM   1712  C CA  . CYS B 2 23  ? -34.013 -48.138 32.831  1.000 110.282 ? 22  CYS BBB CA  1 
ATOM   1713  C C   . CYS B 2 23  ? -34.113 -46.862 33.658  1.000 108.573 ? 22  CYS BBB C   1 
ATOM   1714  O O   . CYS B 2 23  ? -34.761 -46.908 34.709  1.000 107.480 ? 22  CYS BBB O   1 
ATOM   1715  C CB  . CYS B 2 23  ? -35.386 -48.730 32.557  1.000 111.323 ? 22  CYS BBB CB  1 
ATOM   1716  S SG  . CYS B 2 23  ? -36.597 -47.502 32.008  1.000 114.633 ? 22  CYS BBB SG  1 
ATOM   1717  N N   . LYS B 2 24  ? -33.430 -45.804 33.225  1.000 108.544 ? 23  LYS BBB N   1 
ATOM   1718  C CA  . LYS B 2 24  ? -33.321 -44.523 33.964  1.000 110.318 ? 23  LYS BBB CA  1 
ATOM   1719  C C   . LYS B 2 24  ? -34.228 -43.476 33.318  1.000 108.056 ? 23  LYS BBB C   1 
ATOM   1720  O O   . LYS B 2 24  ? -34.345 -43.474 32.087  1.000 109.482 ? 23  LYS BBB O   1 
ATOM   1721  C CB  . LYS B 2 24  ? -31.870 -44.042 33.982  1.000 114.940 ? 23  LYS BBB CB  1 
ATOM   1722  C CG  . LYS B 2 24  ? -31.613 -42.924 34.976  1.000 119.889 ? 23  LYS BBB CG  1 
ATOM   1723  C CD  . LYS B 2 24  ? -30.159 -42.559 35.186  1.000 124.522 ? 23  LYS BBB CD  1 
ATOM   1724  C CE  . LYS B 2 24  ? -29.994 -41.692 36.421  1.000 127.753 ? 23  LYS BBB CE  1 
ATOM   1725  N NZ  . LYS B 2 24  ? -28.716 -40.946 36.435  1.000 130.829 ? 23  LYS BBB NZ  1 
ATOM   1726  N N   . GLY B 2 25  ? -34.822 -42.602 34.129  1.000 108.824 ? 24  GLY BBB N   1 
ATOM   1727  C CA  . GLY B 2 25  ? -35.727 -41.533 33.667  1.000 112.019 ? 24  GLY BBB CA  1 
ATOM   1728  C C   . GLY B 2 25  ? -35.031 -40.182 33.576  1.000 116.479 ? 24  GLY BBB C   1 
ATOM   1729  O O   . GLY B 2 25  ? -34.886 -39.505 34.625  1.000 119.940 ? 24  GLY BBB O   1 
ATOM   1730  N N   . SER B 2 26  ? -34.610 -39.796 32.367  1.000 118.320 ? 25  SER BBB N   1 
ATOM   1731  C CA  . SER B 2 26  ? -34.057 -38.455 32.038  1.000 120.570 ? 25  SER BBB CA  1 
ATOM   1732  C C   . SER B 2 26  ? -35.167 -37.405 32.097  1.000 121.839 ? 25  SER BBB C   1 
ATOM   1733  O O   . SER B 2 26  ? -36.062 -37.443 31.223  1.000 119.846 ? 25  SER BBB O   1 
ATOM   1734  C CB  . SER B 2 26  ? -33.391 -38.444 30.682  1.000 122.727 ? 25  SER BBB CB  1 
ATOM   1735  O OG  . SER B 2 26  ? -33.549 -37.184 30.037  1.000 126.485 ? 25  SER BBB OG  1 
ATOM   1736  N N   . GLY B 2 27  ? -35.101 -36.499 33.075  1.000 125.655 ? 26  GLY BBB N   1 
ATOM   1737  C CA  . GLY B 2 27  ? -35.941 -35.288 33.101  1.000 129.498 ? 26  GLY BBB CA  1 
ATOM   1738  C C   . GLY B 2 27  ? -36.719 -35.124 34.390  1.000 129.538 ? 26  GLY BBB C   1 
ATOM   1739  O O   . GLY B 2 27  ? -36.414 -35.820 35.379  1.000 127.587 ? 26  GLY BBB O   1 
ATOM   1740  N N   . TYR B 2 28  ? -37.702 -34.227 34.362  1.000 131.894 ? 27  TYR BBB N   1 
ATOM   1741  C CA  . TYR B 2 28  ? -38.420 -33.742 35.564  1.000 135.773 ? 27  TYR BBB CA  1 
ATOM   1742  C C   . TYR B 2 28  ? -39.813 -34.352 35.608  1.000 135.025 ? 27  TYR BBB C   1 
ATOM   1743  O O   . TYR B 2 28  ? -40.339 -34.704 34.531  1.000 137.206 ? 27  TYR BBB O   1 
ATOM   1744  C CB  . TYR B 2 28  ? -38.512 -32.220 35.550  1.000 140.585 ? 27  TYR BBB CB  1 
ATOM   1745  C CG  . TYR B 2 28  ? -37.191 -31.555 35.809  1.000 142.852 ? 27  TYR BBB CG  1 
ATOM   1746  C CD1 . TYR B 2 28  ? -36.261 -31.410 34.795  1.000 142.834 ? 27  TYR BBB CD1 1 
ATOM   1747  C CD2 . TYR B 2 28  ? -36.860 -31.106 37.075  1.000 144.120 ? 27  TYR BBB CD2 1 
ATOM   1748  C CE1 . TYR B 2 28  ? -35.033 -30.818 35.029  1.000 144.026 ? 27  TYR BBB CE1 1 
ATOM   1749  C CE2 . TYR B 2 28  ? -35.638 -30.509 37.326  1.000 145.497 ? 27  TYR BBB CE2 1 
ATOM   1750  C CZ  . TYR B 2 28  ? -34.723 -30.369 36.299  1.000 145.774 ? 27  TYR BBB CZ  1 
ATOM   1751  O OH  . TYR B 2 28  ? -33.516 -29.788 36.541  1.000 150.877 ? 27  TYR BBB OH  1 
ATOM   1752  N N   . GLY B 2 29  ? -40.371 -34.449 36.816  1.000 133.072 ? 28  GLY BBB N   1 
ATOM   1753  C CA  . GLY B 2 29  ? -41.724 -34.975 37.067  1.000 132.025 ? 28  GLY BBB CA  1 
ATOM   1754  C C   . GLY B 2 29  ? -41.770 -36.482 36.918  1.000 128.043 ? 28  GLY BBB C   1 
ATOM   1755  O O   . GLY B 2 29  ? -42.877 -37.039 36.740  1.000 128.462 ? 28  GLY BBB O   1 
ATOM   1756  N N   . PHE B 2 30  ? -40.614 -37.135 37.021  1.000 124.733 ? 29  PHE BBB N   1 
ATOM   1757  C CA  . PHE B 2 30  ? -40.510 -38.614 36.999  1.000 122.859 ? 29  PHE BBB CA  1 
ATOM   1758  C C   . PHE B 2 30  ? -41.457 -39.196 38.057  1.000 122.285 ? 29  PHE BBB C   1 
ATOM   1759  O O   . PHE B 2 30  ? -41.891 -40.362 37.945  1.000 121.538 ? 29  PHE BBB O   1 
ATOM   1760  C CB  . PHE B 2 30  ? -39.064 -39.048 37.238  1.000 122.432 ? 29  PHE BBB CB  1 
ATOM   1761  C CG  . PHE B 2 30  ? -38.870 -40.542 37.219  1.000 121.901 ? 29  PHE BBB CG  1 
ATOM   1762  C CD1 . PHE B 2 30  ? -38.649 -41.210 36.025  1.000 120.507 ? 29  PHE BBB CD1 1 
ATOM   1763  C CD2 . PHE B 2 30  ? -38.934 -41.283 38.390  1.000 122.009 ? 29  PHE BBB CD2 1 
ATOM   1764  C CE1 . PHE B 2 30  ? -38.473 -42.584 36.006  1.000 118.432 ? 29  PHE BBB CE1 1 
ATOM   1765  C CE2 . PHE B 2 30  ? -38.758 -42.656 38.368  1.000 120.830 ? 29  PHE BBB CE2 1 
ATOM   1766  C CZ  . PHE B 2 30  ? -38.521 -43.302 37.177  1.000 119.337 ? 29  PHE BBB CZ  1 
ATOM   1767  N N   . ILE B 2 31  ? -41.765 -38.391 39.074  1.000 122.275 ? 30  ILE BBB N   1 
ATOM   1768  C CA  . ILE B 2 31  ? -42.489 -38.838 40.293  1.000 123.530 ? 30  ILE BBB CA  1 
ATOM   1769  C C   . ILE B 2 31  ? -43.847 -39.421 39.905  1.000 122.610 ? 30  ILE BBB C   1 
ATOM   1770  O O   . ILE B 2 31  ? -44.271 -40.360 40.595  1.000 124.078 ? 30  ILE BBB O   1 
ATOM   1771  C CB  . ILE B 2 31  ? -42.615 -37.692 41.316  1.000 127.221 ? 30  ILE BBB CB  1 
ATOM   1772  C CG1 . ILE B 2 31  ? -43.153 -38.208 42.653  1.000 129.714 ? 30  ILE BBB CG1 1 
ATOM   1773  C CG2 . ILE B 2 31  ? -43.443 -36.533 40.777  1.000 127.678 ? 30  ILE BBB CG2 1 
ATOM   1774  C CD1 . ILE B 2 31  ? -42.286 -39.271 43.295  1.000 129.967 ? 30  ILE BBB CD1 1 
ATOM   1775  N N   . THR B 2 32  ? -44.484 -38.894 38.853  1.000 122.409 ? 31  THR BBB N   1 
ATOM   1776  C CA  . THR B 2 32  ? -45.856 -39.286 38.429  1.000 123.524 ? 31  THR BBB CA  1 
ATOM   1777  C C   . THR B 2 32  ? -45.819 -40.561 37.593  1.000 121.819 ? 31  THR BBB C   1 
ATOM   1778  O O   . THR B 2 32  ? -46.909 -41.153 37.424  1.000 123.378 ? 31  THR BBB O   1 
ATOM   1779  C CB  . THR B 2 32  ? -46.552 -38.244 37.549  1.000 125.367 ? 31  THR BBB CB  1 
ATOM   1780  O OG1 . THR B 2 32  ? -45.996 -38.314 36.235  1.000 124.255 ? 31  THR BBB OG1 1 
ATOM   1781  C CG2 . THR B 2 32  ? -46.430 -36.840 38.094  1.000 128.628 ? 31  THR BBB CG2 1 
ATOM   1782  N N   . TYR B 2 33  ? -44.631 -40.923 37.083  1.000 119.161 ? 32  TYR BBB N   1 
ATOM   1783  C CA  . TYR B 2 33  ? -44.422 -41.951 36.027  1.000 117.403 ? 32  TYR BBB CA  1 
ATOM   1784  C C   . TYR B 2 33  ? -44.385 -43.344 36.649  1.000 114.197 ? 32  TYR BBB C   1 
ATOM   1785  O O   . TYR B 2 33  ? -43.745 -43.518 37.703  1.000 113.055 ? 32  TYR BBB O   1 
ATOM   1786  C CB  . TYR B 2 33  ? -43.147 -41.691 35.217  1.000 118.189 ? 32  TYR BBB CB  1 
ATOM   1787  C CG  . TYR B 2 33  ? -43.339 -40.732 34.070  1.000 119.093 ? 32  TYR BBB CG  1 
ATOM   1788  C CD1 . TYR B 2 33  ? -43.851 -41.165 32.857  1.000 119.858 ? 32  TYR BBB CD1 1 
ATOM   1789  C CD2 . TYR B 2 33  ? -43.048 -39.385 34.212  1.000 119.608 ? 32  TYR BBB CD2 1 
ATOM   1790  C CE1 . TYR B 2 33  ? -44.054 -40.288 31.804  1.000 121.130 ? 32  TYR BBB CE1 1 
ATOM   1791  C CE2 . TYR B 2 33  ? -43.252 -38.493 33.173  1.000 121.829 ? 32  TYR BBB CE2 1 
ATOM   1792  C CZ  . TYR B 2 33  ? -43.752 -38.948 31.963  1.000 122.745 ? 32  TYR BBB CZ  1 
ATOM   1793  O OH  . TYR B 2 33  ? -43.956 -38.091 30.920  1.000 124.984 ? 32  TYR BBB OH  1 
ATOM   1794  N N   . TRP B 2 34  ? -45.057 -44.290 35.988  1.000 113.577 ? 33  TRP BBB N   1 
ATOM   1795  C CA  . TRP B 2 34  ? -45.042 -45.743 36.291  1.000 115.841 ? 33  TRP BBB CA  1 
ATOM   1796  C C   . TRP B 2 34  ? -44.318 -46.453 35.147  1.000 114.480 ? 33  TRP BBB C   1 
ATOM   1797  O O   . TRP B 2 34  ? -44.848 -46.430 34.014  1.000 115.127 ? 33  TRP BBB O   1 
ATOM   1798  C CB  . TRP B 2 34  ? -46.464 -46.297 36.444  1.000 119.395 ? 33  TRP BBB CB  1 
ATOM   1799  C CG  . TRP B 2 34  ? -47.298 -45.746 37.564  1.000 121.999 ? 33  TRP BBB CG  1 
ATOM   1800  C CD1 . TRP B 2 34  ? -47.593 -44.441 37.845  1.000 122.924 ? 33  TRP BBB CD1 1 
ATOM   1801  C CD2 . TRP B 2 34  ? -48.039 -46.526 38.513  1.000 121.863 ? 33  TRP BBB CD2 1 
ATOM   1802  N NE1 . TRP B 2 34  ? -48.437 -44.357 38.922  1.000 121.965 ? 33  TRP BBB NE1 1 
ATOM   1803  C CE2 . TRP B 2 34  ? -48.724 -45.624 39.352  1.000 122.211 ? 33  TRP BBB CE2 1 
ATOM   1804  C CE3 . TRP B 2 34  ? -48.160 -47.898 38.747  1.000 122.526 ? 33  TRP BBB CE3 1 
ATOM   1805  C CZ2 . TRP B 2 34  ? -49.521 -46.060 40.405  1.000 125.119 ? 33  TRP BBB CZ2 1 
ATOM   1806  C CZ3 . TRP B 2 34  ? -48.957 -48.327 39.781  1.000 124.857 ? 33  TRP BBB CZ3 1 
ATOM   1807  C CH2 . TRP B 2 34  ? -49.624 -47.418 40.601  1.000 126.148 ? 33  TRP BBB CH2 1 
ATOM   1808  N N   . ILE B 2 35  ? -43.168 -47.066 35.427  1.000 114.607 ? 34  ILE BBB N   1 
ATOM   1809  C CA  . ILE B 2 35  ? -42.339 -47.725 34.382  1.000 115.799 ? 34  ILE BBB CA  1 
ATOM   1810  C C   . ILE B 2 35  ? -42.749 -49.190 34.296  1.000 116.586 ? 34  ILE BBB C   1 
ATOM   1811  O O   . ILE B 2 35  ? -42.555 -49.917 35.299  1.000 115.849 ? 34  ILE BBB O   1 
ATOM   1812  C CB  . ILE B 2 35  ? -40.833 -47.580 34.651  1.000 118.150 ? 34  ILE BBB CB  1 
ATOM   1813  C CG1 . ILE B 2 35  ? -40.358 -46.148 34.408  1.000 120.264 ? 34  ILE BBB CG1 1 
ATOM   1814  C CG2 . ILE B 2 35  ? -40.049 -48.564 33.799  1.000 119.495 ? 34  ILE BBB CG2 1 
ATOM   1815  C CD1 . ILE B 2 35  ? -40.617 -45.217 35.557  1.000 123.746 ? 34  ILE BBB CD1 1 
ATOM   1816  N N   . GLY B 2 36  ? -43.275 -49.575 33.128  1.000 117.246 ? 35  GLY BBB N   1 
ATOM   1817  C CA  . GLY B 2 36  ? -43.555 -50.966 32.729  1.000 118.387 ? 35  GLY BBB CA  1 
ATOM   1818  C C   . GLY B 2 36  ? -42.385 -51.578 31.975  1.000 117.298 ? 35  GLY BBB C   1 
ATOM   1819  O O   . GLY B 2 36  ? -41.493 -50.830 31.525  1.000 116.025 ? 35  GLY BBB O   1 
ATOM   1820  N N   . TRP B 2 37  ? -42.385 -52.904 31.862  1.000 118.221 ? 36  TRP BBB N   1 
ATOM   1821  C CA  . TRP B 2 37  ? -41.420 -53.692 31.056  1.000 117.629 ? 36  TRP BBB CA  1 
ATOM   1822  C C   . TRP B 2 37  ? -42.189 -54.545 30.047  1.000 118.822 ? 36  TRP BBB C   1 
ATOM   1823  O O   . TRP B 2 37  ? -43.201 -55.161 30.418  1.000 120.172 ? 36  TRP BBB O   1 
ATOM   1824  C CB  . TRP B 2 37  ? -40.539 -54.558 31.957  1.000 117.998 ? 36  TRP BBB CB  1 
ATOM   1825  C CG  . TRP B 2 37  ? -39.573 -53.778 32.785  1.000 116.394 ? 36  TRP BBB CG  1 
ATOM   1826  C CD1 . TRP B 2 37  ? -39.753 -53.363 34.067  1.000 117.374 ? 36  TRP BBB CD1 1 
ATOM   1827  C CD2 . TRP B 2 37  ? -38.267 -53.326 32.391  1.000 116.516 ? 36  TRP BBB CD2 1 
ATOM   1828  N NE1 . TRP B 2 37  ? -38.646 -52.689 34.502  1.000 118.227 ? 36  TRP BBB NE1 1 
ATOM   1829  C CE2 . TRP B 2 37  ? -37.721 -52.645 33.496  1.000 117.318 ? 36  TRP BBB CE2 1 
ATOM   1830  C CE3 . TRP B 2 37  ? -37.511 -53.425 31.219  1.000 118.020 ? 36  TRP BBB CE3 1 
ATOM   1831  C CZ2 . TRP B 2 37  ? -36.450 -52.074 33.464  1.000 119.156 ? 36  TRP BBB CZ2 1 
ATOM   1832  C CZ3 . TRP B 2 37  ? -36.252 -52.863 31.184  1.000 118.961 ? 36  TRP BBB CZ3 1 
ATOM   1833  C CH2 . TRP B 2 37  ? -35.732 -52.195 32.293  1.000 120.165 ? 36  TRP BBB CH2 1 
ATOM   1834  N N   . VAL B 2 38  ? -41.701 -54.590 28.814  1.000 120.376 ? 37  VAL BBB N   1 
ATOM   1835  C CA  . VAL B 2 38  ? -42.327 -55.358 27.707  1.000 123.015 ? 37  VAL BBB CA  1 
ATOM   1836  C C   . VAL B 2 38  ? -41.253 -56.249 27.081  1.000 123.871 ? 37  VAL BBB C   1 
ATOM   1837  O O   . VAL B 2 38  ? -40.133 -55.755 26.835  1.000 124.011 ? 37  VAL BBB O   1 
ATOM   1838  C CB  . VAL B 2 38  ? -42.959 -54.402 26.681  1.000 123.371 ? 37  VAL BBB CB  1 
ATOM   1839  C CG1 . VAL B 2 38  ? -43.584 -55.161 25.525  1.000 125.535 ? 37  VAL BBB CG1 1 
ATOM   1840  C CG2 . VAL B 2 38  ? -43.972 -53.475 27.338  1.000 123.714 ? 37  VAL BBB CG2 1 
ATOM   1841  N N   . ARG B 2 39  ? -41.591 -57.515 26.851  1.000 125.526 ? 38  ARG BBB N   1 
ATOM   1842  C CA  . ARG B 2 39  ? -40.732 -58.482 26.129  1.000 126.021 ? 38  ARG BBB CA  1 
ATOM   1843  C C   . ARG B 2 39  ? -41.252 -58.626 24.696  1.000 124.910 ? 38  ARG BBB C   1 
ATOM   1844  O O   . ARG B 2 39  ? -42.435 -58.970 24.501  1.000 125.569 ? 38  ARG BBB O   1 
ATOM   1845  C CB  . ARG B 2 39  ? -40.721 -59.831 26.850  1.000 130.687 ? 38  ARG BBB CB  1 
ATOM   1846  C CG  . ARG B 2 39  ? -39.831 -60.872 26.190  1.000 133.840 ? 38  ARG BBB CG  1 
ATOM   1847  C CD  . ARG B 2 39  ? -39.732 -62.151 26.997  1.000 137.934 ? 38  ARG BBB CD  1 
ATOM   1848  N NE  . ARG B 2 39  ? -40.927 -62.981 26.912  1.000 141.220 ? 38  ARG BBB NE  1 
ATOM   1849  C CZ  . ARG B 2 39  ? -41.026 -64.204 27.427  1.000 147.550 ? 38  ARG BBB CZ  1 
ATOM   1850  N NH1 . ARG B 2 39  ? -40.002 -64.748 28.073  1.000 149.414 ? 38  ARG BBB NH1 1 
ATOM   1851  N NH2 . ARG B 2 39  ? -42.150 -64.886 27.293  1.000 151.499 ? 38  ARG BBB NH2 1 
ATOM   1852  N N   . GLN B 2 40  ? -40.390 -58.352 23.726  1.000 122.271 ? 39  GLN BBB N   1 
ATOM   1853  C CA  . GLN B 2 40  ? -40.599 -58.745 22.317  1.000 123.484 ? 39  GLN BBB CA  1 
ATOM   1854  C C   . GLN B 2 40  ? -39.590 -59.855 22.031  1.000 123.498 ? 39  GLN BBB C   1 
ATOM   1855  O O   . GLN B 2 40  ? -38.379 -59.563 22.025  1.000 120.600 ? 39  GLN BBB O   1 
ATOM   1856  C CB  . GLN B 2 40  ? -40.441 -57.524 21.410  1.000 123.326 ? 39  GLN BBB CB  1 
ATOM   1857  C CG  . GLN B 2 40  ? -40.590 -57.844 19.931  1.000 125.133 ? 39  GLN BBB CG  1 
ATOM   1858  C CD  . GLN B 2 40  ? -41.022 -56.640 19.130  1.000 124.989 ? 39  GLN BBB CD  1 
ATOM   1859  O OE1 . GLN B 2 40  ? -40.244 -55.721 18.871  1.000 123.802 ? 39  GLN BBB OE1 1 
ATOM   1860  N NE2 . GLN B 2 40  ? -42.281 -56.644 18.724  1.000 127.189 ? 39  GLN BBB NE2 1 
ATOM   1861  N N   . MET B 2 41  ? -40.062 -61.089 21.865  1.000 125.460 ? 40  MET BBB N   1 
ATOM   1862  C CA  . MET B 2 41  ? -39.173 -62.230 21.535  1.000 129.200 ? 40  MET BBB CA  1 
ATOM   1863  C C   . MET B 2 41  ? -38.771 -62.153 20.060  1.000 133.179 ? 40  MET BBB C   1 
ATOM   1864  O O   . MET B 2 41  ? -39.419 -61.467 19.274  1.000 139.695 ? 40  MET BBB O   1 
ATOM   1865  C CB  . MET B 2 41  ? -39.861 -63.557 21.849  1.000 130.747 ? 40  MET BBB CB  1 
ATOM   1866  C CG  . MET B 2 41  ? -39.509 -64.067 23.218  1.000 131.135 ? 40  MET BBB CG  1 
ATOM   1867  S SD  . MET B 2 41  ? -40.633 -65.366 23.704  1.000 137.371 ? 40  MET BBB SD  1 
ATOM   1868  C CE  . MET B 2 41  ? -39.504 -66.486 24.526  1.000 140.135 ? 40  MET BBB CE  1 
ATOM   1869  N N   . PRO B 2 42  ? -37.680 -62.833 19.634  1.000 133.917 ? 41  PRO BBB N   1 
ATOM   1870  C CA  . PRO B 2 42  ? -37.234 -62.792 18.240  1.000 131.922 ? 41  PRO BBB CA  1 
ATOM   1871  C C   . PRO B 2 42  ? -38.381 -62.966 17.234  1.000 133.102 ? 41  PRO BBB C   1 
ATOM   1872  O O   . PRO B 2 42  ? -38.889 -64.068 17.107  1.000 134.760 ? 41  PRO BBB O   1 
ATOM   1873  C CB  . PRO B 2 42  ? -36.277 -63.985 18.147  1.000 134.356 ? 41  PRO BBB CB  1 
ATOM   1874  C CG  . PRO B 2 42  ? -35.709 -64.109 19.539  1.000 135.415 ? 41  PRO BBB CG  1 
ATOM   1875  C CD  . PRO B 2 42  ? -36.830 -63.695 20.469  1.000 135.947 ? 41  PRO BBB CD  1 
ATOM   1876  N N   . GLY B 2 43  ? -38.767 -61.869 16.575  1.000 132.421 ? 42  GLY BBB N   1 
ATOM   1877  C CA  . GLY B 2 43  ? -39.762 -61.844 15.484  1.000 133.820 ? 42  GLY BBB CA  1 
ATOM   1878  C C   . GLY B 2 43  ? -41.147 -62.210 15.974  1.000 135.076 ? 42  GLY BBB C   1 
ATOM   1879  O O   . GLY B 2 43  ? -41.862 -62.928 15.252  1.000 136.529 ? 42  GLY BBB O   1 
ATOM   1880  N N   . LYS B 2 44  ? -41.507 -61.726 17.160  1.000 135.663 ? 43  LYS BBB N   1 
ATOM   1881  C CA  . LYS B 2 44  ? -42.789 -62.032 17.842  1.000 139.933 ? 43  LYS BBB CA  1 
ATOM   1882  C C   . LYS B 2 44  ? -43.455 -60.725 18.264  1.000 140.069 ? 43  LYS BBB C   1 
ATOM   1883  O O   . LYS B 2 44  ? -42.829 -59.653 18.094  1.000 139.083 ? 43  LYS BBB O   1 
ATOM   1884  C CB  . LYS B 2 44  ? -42.554 -62.875 19.097  1.000 142.082 ? 43  LYS BBB CB  1 
ATOM   1885  C CG  . LYS B 2 44  ? -41.655 -64.086 18.914  1.000 143.324 ? 43  LYS BBB CG  1 
ATOM   1886  C CD  . LYS B 2 44  ? -42.351 -65.237 18.260  1.000 146.586 ? 43  LYS BBB CD  1 
ATOM   1887  C CE  . LYS B 2 44  ? -41.667 -66.547 18.551  1.000 149.050 ? 43  LYS BBB CE  1 
ATOM   1888  N NZ  . LYS B 2 44  ? -42.435 -67.661 17.957  1.000 154.523 ? 43  LYS BBB NZ  1 
ATOM   1889  N N   . GLY B 2 45  ? -44.656 -60.838 18.838  1.000 141.650 ? 44  GLY BBB N   1 
ATOM   1890  C CA  . GLY B 2 45  ? -45.450 -59.705 19.345  1.000 140.015 ? 44  GLY BBB CA  1 
ATOM   1891  C C   . GLY B 2 45  ? -44.940 -59.195 20.679  1.000 136.510 ? 44  GLY BBB C   1 
ATOM   1892  O O   . GLY B 2 45  ? -43.948 -59.752 21.211  1.000 136.968 ? 44  GLY BBB O   1 
ATOM   1893  N N   . LEU B 2 46  ? -45.610 -58.166 21.197  1.000 134.021 ? 45  LEU BBB N   1 
ATOM   1894  C CA  . LEU B 2 46  ? -45.246 -57.466 22.454  1.000 131.801 ? 45  LEU BBB CA  1 
ATOM   1895  C C   . LEU B 2 46  ? -45.982 -58.124 23.620  1.000 133.999 ? 45  LEU BBB C   1 
ATOM   1896  O O   . LEU B 2 46  ? -47.215 -58.161 23.576  1.000 136.597 ? 45  LEU BBB O   1 
ATOM   1897  C CB  . LEU B 2 46  ? -45.650 -55.996 22.330  1.000 129.738 ? 45  LEU BBB CB  1 
ATOM   1898  C CG  . LEU B 2 46  ? -45.056 -55.241 21.143  1.000 128.120 ? 45  LEU BBB CG  1 
ATOM   1899  C CD1 . LEU B 2 46  ? -45.656 -53.851 21.046  1.000 127.534 ? 45  LEU BBB CD1 1 
ATOM   1900  C CD2 . LEU B 2 46  ? -43.542 -55.159 21.247  1.000 125.915 ? 45  LEU BBB CD2 1 
ATOM   1901  N N   . GLU B 2 47  ? -45.251 -58.619 24.617  1.000 136.288 ? 46  GLU BBB N   1 
ATOM   1902  C CA  . GLU B 2 47  ? -45.825 -59.187 25.864  1.000 141.241 ? 46  GLU BBB CA  1 
ATOM   1903  C C   . GLU B 2 47  ? -45.558 -58.194 27.000  1.000 137.649 ? 46  GLU BBB C   1 
ATOM   1904  O O   . GLU B 2 47  ? -44.386 -57.841 27.220  1.000 135.883 ? 46  GLU BBB O   1 
ATOM   1905  C CB  . GLU B 2 47  ? -45.213 -60.557 26.176  1.000 147.806 ? 46  GLU BBB CB  1 
ATOM   1906  C CG  . GLU B 2 47  ? -45.073 -61.480 24.971  1.000 152.119 ? 46  GLU BBB CG  1 
ATOM   1907  C CD  . GLU B 2 47  ? -44.131 -62.655 25.191  1.000 155.208 ? 46  GLU BBB CD  1 
ATOM   1908  O OE1 . GLU B 2 47  ? -44.465 -63.532 26.019  1.000 157.894 ? 46  GLU BBB OE1 1 
ATOM   1909  O OE2 . GLU B 2 47  ? -43.054 -62.681 24.546  1.000 156.630 ? 46  GLU BBB OE2 1 
ATOM   1910  N N   . TRP B 2 48  ? -46.606 -57.735 27.677  1.000 137.035 ? 47  TRP BBB N   1 
ATOM   1911  C CA  . TRP B 2 48  ? -46.475 -56.885 28.886  1.000 136.087 ? 47  TRP BBB CA  1 
ATOM   1912  C C   . TRP B 2 48  ? -46.094 -57.776 30.068  1.000 133.478 ? 47  TRP BBB C   1 
ATOM   1913  O O   . TRP B 2 48  ? -46.837 -58.730 30.348  1.000 134.653 ? 47  TRP BBB O   1 
ATOM   1914  C CB  . TRP B 2 48  ? -47.768 -56.118 29.152  1.000 142.180 ? 47  TRP BBB CB  1 
ATOM   1915  C CG  . TRP B 2 48  ? -47.668 -55.163 30.299  1.000 146.444 ? 47  TRP BBB CG  1 
ATOM   1916  C CD1 . TRP B 2 48  ? -47.171 -53.892 30.275  1.000 147.636 ? 47  TRP BBB CD1 1 
ATOM   1917  C CD2 . TRP B 2 48  ? -48.088 -55.400 31.653  1.000 149.505 ? 47  TRP BBB CD2 1 
ATOM   1918  N NE1 . TRP B 2 48  ? -47.252 -53.324 31.520  1.000 147.286 ? 47  TRP BBB NE1 1 
ATOM   1919  C CE2 . TRP B 2 48  ? -47.812 -54.224 32.382  1.000 147.915 ? 47  TRP BBB CE2 1 
ATOM   1920  C CE3 . TRP B 2 48  ? -48.677 -56.482 32.313  1.000 153.904 ? 47  TRP BBB CE3 1 
ATOM   1921  C CZ2 . TRP B 2 48  ? -48.102 -54.105 33.737  1.000 149.195 ? 47  TRP BBB CZ2 1 
ATOM   1922  C CZ3 . TRP B 2 48  ? -48.962 -56.364 33.655  1.000 156.598 ? 47  TRP BBB CZ3 1 
ATOM   1923  C CH2 . TRP B 2 48  ? -48.680 -55.189 34.354  1.000 154.090 ? 47  TRP BBB CH2 1 
ATOM   1924  N N   . MET B 2 49  ? -44.976 -57.472 30.725  1.000 130.816 ? 48  MET BBB N   1 
ATOM   1925  C CA  . MET B 2 49  ? -44.393 -58.308 31.808  1.000 132.097 ? 48  MET BBB CA  1 
ATOM   1926  C C   . MET B 2 49  ? -44.949 -57.864 33.163  1.000 131.437 ? 48  MET BBB C   1 
ATOM   1927  O O   . MET B 2 49  ? -45.479 -58.718 33.900  1.000 133.653 ? 48  MET BBB O   1 
ATOM   1928  C CB  . MET B 2 49  ? -42.867 -58.180 31.838  1.000 130.843 ? 48  MET BBB CB  1 
ATOM   1929  C CG  . MET B 2 49  ? -42.191 -58.599 30.548  1.000 130.748 ? 48  MET BBB CG  1 
ATOM   1930  S SD  . MET B 2 49  ? -40.387 -58.532 30.684  1.000 129.349 ? 48  MET BBB SD  1 
ATOM   1931  C CE  . MET B 2 49  ? -40.069 -60.008 31.651  1.000 131.066 ? 48  MET BBB CE  1 
ATOM   1932  N N   . GLY B 2 50  ? -44.800 -56.573 33.469  1.000 129.789 ? 49  GLY BBB N   1 
ATOM   1933  C CA  . GLY B 2 50  ? -45.155 -55.967 34.766  1.000 131.618 ? 49  GLY BBB CA  1 
ATOM   1934  C C   . GLY B 2 50  ? -44.877 -54.471 34.796  1.000 130.359 ? 49  GLY BBB C   1 
ATOM   1935  O O   . GLY B 2 50  ? -44.104 -53.990 33.951  1.000 131.678 ? 49  GLY BBB O   1 
ATOM   1936  N N   . ILE B 2 51  ? -45.488 -53.761 35.747  1.000 130.740 ? 50  ILE BBB N   1 
ATOM   1937  C CA  . ILE B 2 51  ? -45.281 -52.303 35.986  1.000 128.580 ? 50  ILE BBB CA  1 
ATOM   1938  C C   . ILE B 2 51  ? -44.907 -52.107 37.452  1.000 127.792 ? 50  ILE BBB C   1 
ATOM   1939  O O   . ILE B 2 51  ? -45.364 -52.905 38.295  1.000 128.691 ? 50  ILE BBB O   1 
ATOM   1940  C CB  . ILE B 2 51  ? -46.529 -51.482 35.603  1.000 130.633 ? 50  ILE BBB CB  1 
ATOM   1941  C CG1 . ILE B 2 51  ? -46.242 -49.980 35.532  1.000 132.233 ? 50  ILE BBB CG1 1 
ATOM   1942  C CG2 . ILE B 2 51  ? -47.686 -51.777 36.543  1.000 131.982 ? 50  ILE BBB CG2 1 
ATOM   1943  C CD1 . ILE B 2 51  ? -46.956 -49.269 34.387  1.000 134.812 ? 50  ILE BBB CD1 1 
ATOM   1944  N N   . ILE B 2 52  ? -44.105 -51.078 37.722  1.000 126.276 ? 51  ILE BBB N   1 
ATOM   1945  C CA  . ILE B 2 52  ? -43.769 -50.623 39.099  1.000 125.921 ? 51  ILE BBB CA  1 
ATOM   1946  C C   . ILE B 2 52  ? -43.938 -49.109 39.174  1.000 124.124 ? 51  ILE BBB C   1 
ATOM   1947  O O   . ILE B 2 52  ? -43.631 -48.422 38.177  1.000 121.965 ? 51  ILE BBB O   1 
ATOM   1948  C CB  . ILE B 2 52  ? -42.343 -51.025 39.491  1.000 125.799 ? 51  ILE BBB CB  1 
ATOM   1949  C CG1 . ILE B 2 52  ? -42.111 -50.815 40.986  1.000 127.760 ? 51  ILE BBB CG1 1 
ATOM   1950  C CG2 . ILE B 2 52  ? -41.324 -50.272 38.652  1.000 125.259 ? 51  ILE BBB CG2 1 
ATOM   1951  C CD1 . ILE B 2 52  ? -40.861 -51.487 41.496  1.000 130.083 ? 51  ILE BBB CD1 1 
ATOM   1952  N N   . TYR B 2 53  ? -44.411 -48.630 40.323  1.000 124.478 ? 52  TYR BBB N   1 
ATOM   1953  C CA  . TYR B 2 53  ? -44.426 -47.195 40.685  1.000 124.518 ? 52  TYR BBB CA  1 
ATOM   1954  C C   . TYR B 2 53  ? -43.240 -46.944 41.611  1.000 124.033 ? 52  TYR BBB C   1 
ATOM   1955  O O   . TYR B 2 53  ? -43.300 -47.250 42.795  1.000 125.221 ? 52  TYR BBB O   1 
ATOM   1956  C CB  . TYR B 2 53  ? -45.759 -46.776 41.310  1.000 126.154 ? 52  TYR BBB CB  1 
ATOM   1957  C CG  . TYR B 2 53  ? -45.754 -45.338 41.756  1.000 127.885 ? 52  TYR BBB CG  1 
ATOM   1958  C CD1 . TYR B 2 53  ? -45.392 -44.328 40.883  1.000 126.948 ? 52  TYR BBB CD1 1 
ATOM   1959  C CD2 . TYR B 2 53  ? -46.051 -44.982 43.059  1.000 131.668 ? 52  TYR BBB CD2 1 
ATOM   1960  C CE1 . TYR B 2 53  ? -45.349 -43.003 41.281  1.000 127.898 ? 52  TYR BBB CE1 1 
ATOM   1961  C CE2 . TYR B 2 53  ? -46.004 -43.661 43.478  1.000 131.736 ? 52  TYR BBB CE2 1 
ATOM   1962  C CZ  . TYR B 2 53  ? -45.657 -42.664 42.584  1.000 129.182 ? 52  TYR BBB CZ  1 
ATOM   1963  O OH  . TYR B 2 53  ? -45.615 -41.360 42.981  1.000 128.158 ? 52  TYR BBB OH  1 
ATOM   1964  N N   . PRO B 2 54  ? -42.128 -46.378 41.095  1.000 123.040 ? 53  PRO BBB N   1 
ATOM   1965  C CA  . PRO B 2 54  ? -40.924 -46.166 41.897  1.000 124.044 ? 53  PRO BBB CA  1 
ATOM   1966  C C   . PRO B 2 54  ? -41.199 -45.527 43.267  1.000 126.301 ? 53  PRO BBB C   1 
ATOM   1967  O O   . PRO B 2 54  ? -40.492 -45.857 44.217  1.000 126.454 ? 53  PRO BBB O   1 
ATOM   1968  C CB  . PRO B 2 54  ? -40.100 -45.188 41.051  1.000 122.927 ? 53  PRO BBB CB  1 
ATOM   1969  C CG  . PRO B 2 54  ? -40.553 -45.439 39.624  1.000 120.482 ? 53  PRO BBB CG  1 
ATOM   1970  C CD  . PRO B 2 54  ? -41.993 -45.880 39.719  1.000 121.349 ? 53  PRO BBB CD  1 
ATOM   1971  N N   . GLY B 2 55  ? -42.196 -44.633 43.318  1.000 127.468 ? 54  GLY BBB N   1 
ATOM   1972  C CA  . GLY B 2 55  ? -42.611 -43.886 44.522  1.000 131.464 ? 54  GLY BBB CA  1 
ATOM   1973  C C   . GLY B 2 55  ? -42.684 -44.777 45.749  1.000 133.973 ? 54  GLY BBB C   1 
ATOM   1974  O O   . GLY B 2 55  ? -41.795 -44.669 46.611  1.000 137.030 ? 54  GLY BBB O   1 
ATOM   1975  N N   . ASP B 2 56  ? -43.693 -45.642 45.818  1.000 135.433 ? 55  ASP BBB N   1 
ATOM   1976  C CA  . ASP B 2 56  ? -43.877 -46.604 46.935  1.000 141.368 ? 55  ASP BBB CA  1 
ATOM   1977  C C   . ASP B 2 56  ? -43.564 -48.019 46.442  1.000 137.946 ? 55  ASP BBB C   1 
ATOM   1978  O O   . ASP B 2 56  ? -44.017 -48.977 47.093  1.000 143.247 ? 55  ASP BBB O   1 
ATOM   1979  C CB  . ASP B 2 56  ? -45.278 -46.491 47.555  1.000 149.263 ? 55  ASP BBB CB  1 
ATOM   1980  C CG  . ASP B 2 56  ? -46.451 -46.693 46.606  1.000 150.718 ? 55  ASP BBB CG  1 
ATOM   1981  O OD1 . ASP B 2 56  ? -46.230 -47.154 45.472  1.000 149.163 ? 55  ASP BBB OD1 1 
ATOM   1982  O OD2 . ASP B 2 56  ? -47.590 -46.376 47.014  1.000 154.865 ? 55  ASP BBB OD2 1 
ATOM   1983  N N   . SER B 2 57  ? -42.823 -48.142 45.339  1.000 130.825 ? 56  SER BBB N   1 
ATOM   1984  C CA  . SER B 2 57  ? -42.405 -49.435 44.741  1.000 130.056 ? 56  SER BBB CA  1 
ATOM   1985  C C   . SER B 2 57  ? -43.595 -50.410 44.707  1.000 133.530 ? 56  SER BBB C   1 
ATOM   1986  O O   . SER B 2 57  ? -43.394 -51.606 45.004  1.000 137.308 ? 56  SER BBB O   1 
ATOM   1987  C CB  . SER B 2 57  ? -41.218 -49.983 45.492  1.000 129.429 ? 56  SER BBB CB  1 
ATOM   1988  O OG  . SER B 2 57  ? -40.147 -49.047 45.488  1.000 127.328 ? 56  SER BBB OG  1 
ATOM   1989  N N   . GLU B 2 58  ? -44.790 -49.904 44.364  1.000 136.055 ? 57  GLU BBB N   1 
ATOM   1990  C CA  . GLU B 2 58  ? -46.042 -50.689 44.152  1.000 138.053 ? 57  GLU BBB CA  1 
ATOM   1991  C C   . GLU B 2 58  ? -45.900 -51.437 42.828  1.000 136.721 ? 57  GLU BBB C   1 
ATOM   1992  O O   . GLU B 2 58  ? -45.954 -50.785 41.780  1.000 135.466 ? 57  GLU BBB O   1 
ATOM   1993  C CB  . GLU B 2 58  ? -47.278 -49.779 44.138  1.000 138.781 ? 57  GLU BBB CB  1 
ATOM   1994  C CG  . GLU B 2 58  ? -48.564 -50.461 43.687  1.000 140.638 ? 57  GLU BBB CG  1 
ATOM   1995  C CD  . GLU B 2 58  ? -49.823 -49.607 43.783  1.000 142.649 ? 57  GLU BBB CD  1 
ATOM   1996  O OE1 . GLU B 2 58  ? -49.700 -48.352 43.842  1.000 140.520 ? 57  GLU BBB OE1 1 
ATOM   1997  O OE2 . GLU B 2 58  ? -50.930 -50.204 43.816  1.000 144.768 ? 57  GLU BBB OE2 1 
ATOM   1998  N N   . THR B 2 59  ? -45.720 -52.753 42.891  1.000 139.328 ? 58  THR BBB N   1 
ATOM   1999  C CA  . THR B 2 59  ? -45.318 -53.613 41.751  1.000 139.837 ? 58  THR BBB CA  1 
ATOM   2000  C C   . THR B 2 59  ? -46.477 -54.546 41.389  1.000 141.413 ? 58  THR BBB C   1 
ATOM   2001  O O   . THR B 2 59  ? -47.066 -55.132 42.323  1.000 149.673 ? 58  THR BBB O   1 
ATOM   2002  C CB  . THR B 2 59  ? -44.063 -54.409 42.121  1.000 142.337 ? 58  THR BBB CB  1 
ATOM   2003  O OG1 . THR B 2 59  ? -43.216 -53.549 42.884  1.000 144.742 ? 58  THR BBB OG1 1 
ATOM   2004  C CG2 . THR B 2 59  ? -43.325 -54.949 40.918  1.000 141.750 ? 58  THR BBB CG2 1 
ATOM   2005  N N   . ARG B 2 60  ? -46.791 -54.675 40.095  1.000 135.994 ? 59  ARG BBB N   1 
ATOM   2006  C CA  . ARG B 2 60  ? -47.783 -55.651 39.566  1.000 134.863 ? 59  ARG BBB CA  1 
ATOM   2007  C C   . ARG B 2 60  ? -47.120 -56.462 38.455  1.000 133.440 ? 59  ARG BBB C   1 
ATOM   2008  O O   . ARG B 2 60  ? -46.333 -55.874 37.703  1.000 133.994 ? 59  ARG BBB O   1 
ATOM   2009  C CB  . ARG B 2 60  ? -49.025 -54.931 39.040  1.000 133.596 ? 59  ARG BBB CB  1 
ATOM   2010  C CG  . ARG B 2 60  ? -49.558 -53.874 39.993  1.000 133.295 ? 59  ARG BBB CG  1 
ATOM   2011  C CD  . ARG B 2 60  ? -50.913 -53.337 39.604  1.000 133.340 ? 59  ARG BBB CD  1 
ATOM   2012  N NE  . ARG B 2 60  ? -51.237 -52.189 40.429  1.000 132.446 ? 59  ARG BBB NE  1 
ATOM   2013  C CZ  . ARG B 2 60  ? -52.387 -51.539 40.395  1.000 134.750 ? 59  ARG BBB CZ  1 
ATOM   2014  N NH1 . ARG B 2 60  ? -53.350 -51.918 39.570  1.000 136.356 ? 59  ARG BBB NH1 1 
ATOM   2015  N NH2 . ARG B 2 60  ? -52.569 -50.508 41.199  1.000 136.551 ? 59  ARG BBB NH2 1 
ATOM   2016  N N   . TYR B 2 61  ? -47.415 -57.758 38.373  1.000 134.734 ? 60  TYR BBB N   1 
ATOM   2017  C CA  . TYR B 2 61  ? -46.823 -58.690 37.381  1.000 134.813 ? 60  TYR BBB CA  1 
ATOM   2018  C C   . TYR B 2 61  ? -47.933 -59.251 36.491  1.000 136.536 ? 60  TYR BBB C   1 
ATOM   2019  O O   . TYR B 2 61  ? -49.093 -59.337 36.931  1.000 139.791 ? 60  TYR BBB O   1 
ATOM   2020  C CB  . TYR B 2 61  ? -46.064 -59.815 38.092  1.000 137.761 ? 60  TYR BBB CB  1 
ATOM   2021  C CG  . TYR B 2 61  ? -44.839 -59.373 38.857  1.000 136.176 ? 60  TYR BBB CG  1 
ATOM   2022  C CD1 . TYR B 2 61  ? -43.708 -58.933 38.190  1.000 133.118 ? 60  TYR BBB CD1 1 
ATOM   2023  C CD2 . TYR B 2 61  ? -44.798 -59.401 40.243  1.000 137.710 ? 60  TYR BBB CD2 1 
ATOM   2024  C CE1 . TYR B 2 61  ? -42.575 -58.527 38.874  1.000 131.759 ? 60  TYR BBB CE1 1 
ATOM   2025  C CE2 . TYR B 2 61  ? -43.672 -58.999 40.944  1.000 136.354 ? 60  TYR BBB CE2 1 
ATOM   2026  C CZ  . TYR B 2 61  ? -42.555 -58.562 40.255  1.000 133.444 ? 60  TYR BBB CZ  1 
ATOM   2027  O OH  . TYR B 2 61  ? -41.440 -58.151 40.924  1.000 133.507 ? 60  TYR BBB OH  1 
ATOM   2028  N N   . SER B 2 62  ? -47.584 -59.606 35.258  1.000 136.387 ? 61  SER BBB N   1 
ATOM   2029  C CA  . SER B 2 62  ? -48.393 -60.514 34.408  1.000 140.720 ? 61  SER BBB CA  1 
ATOM   2030  C C   . SER B 2 62  ? -48.357 -61.887 35.064  1.000 146.426 ? 61  SER BBB C   1 
ATOM   2031  O O   . SER B 2 62  ? -47.316 -62.279 35.583  1.000 148.742 ? 61  SER BBB O   1 
ATOM   2032  C CB  . SER B 2 62  ? -47.874 -60.566 32.997  1.000 139.254 ? 61  SER BBB CB  1 
ATOM   2033  O OG  . SER B 2 62  ? -48.457 -61.642 32.275  1.000 141.550 ? 61  SER BBB OG  1 
ATOM   2034  N N   . PRO B 2 63  ? -49.473 -62.649 35.076  1.000 151.330 ? 62  PRO BBB N   1 
ATOM   2035  C CA  . PRO B 2 63  ? -49.455 -64.032 35.560  1.000 156.147 ? 62  PRO BBB CA  1 
ATOM   2036  C C   . PRO B 2 63  ? -48.349 -64.868 34.896  1.000 157.545 ? 62  PRO BBB C   1 
ATOM   2037  O O   . PRO B 2 63  ? -47.840 -65.781 35.519  1.000 159.824 ? 62  PRO BBB O   1 
ATOM   2038  C CB  . PRO B 2 63  ? -50.837 -64.578 35.175  1.000 159.230 ? 62  PRO BBB CB  1 
ATOM   2039  C CG  . PRO B 2 63  ? -51.717 -63.346 35.072  1.000 157.861 ? 62  PRO BBB CG  1 
ATOM   2040  C CD  . PRO B 2 63  ? -50.805 -62.221 34.626  1.000 152.356 ? 62  PRO BBB CD  1 
ATOM   2041  N N   . SER B 2 64  ? -47.992 -64.506 33.660  1.000 157.116 ? 63  SER BBB N   1 
ATOM   2042  C CA  . SER B 2 64  ? -46.960 -65.165 32.819  1.000 158.199 ? 63  SER BBB CA  1 
ATOM   2043  C C   . SER B 2 64  ? -45.541 -64.791 33.268  1.000 155.557 ? 63  SER BBB C   1 
ATOM   2044  O O   . SER B 2 64  ? -44.598 -65.139 32.522  1.000 156.775 ? 63  SER BBB O   1 
ATOM   2045  C CB  . SER B 2 64  ? -47.166 -64.804 31.372  1.000 158.576 ? 63  SER BBB CB  1 
ATOM   2046  O OG  . SER B 2 64  ? -48.541 -64.879 31.027  1.000 162.233 ? 63  SER BBB OG  1 
ATOM   2047  N N   . PHE B 2 65  ? -45.381 -64.095 34.403  1.000 152.770 ? 64  PHE BBB N   1 
ATOM   2048  C CA  . PHE B 2 65  ? -44.057 -63.665 34.935  1.000 149.124 ? 64  PHE BBB CA  1 
ATOM   2049  C C   . PHE B 2 65  ? -44.007 -63.729 36.477  1.000 150.397 ? 64  PHE BBB C   1 
ATOM   2050  O O   . PHE B 2 65  ? -42.897 -63.952 37.006  1.000 152.472 ? 64  PHE BBB O   1 
ATOM   2051  C CB  . PHE B 2 65  ? -43.697 -62.299 34.338  1.000 143.227 ? 64  PHE BBB CB  1 
ATOM   2052  C CG  . PHE B 2 65  ? -43.458 -62.337 32.846  1.000 141.991 ? 64  PHE BBB CG  1 
ATOM   2053  C CD1 . PHE B 2 65  ? -42.298 -62.888 32.321  1.000 142.282 ? 64  PHE BBB CD1 1 
ATOM   2054  C CD2 . PHE B 2 65  ? -44.403 -61.854 31.955  1.000 141.939 ? 64  PHE BBB CD2 1 
ATOM   2055  C CE1 . PHE B 2 65  ? -42.086 -62.942 30.949  1.000 141.357 ? 64  PHE BBB CE1 1 
ATOM   2056  C CE2 . PHE B 2 65  ? -44.190 -61.904 30.584  1.000 141.360 ? 64  PHE BBB CE2 1 
ATOM   2057  C CZ  . PHE B 2 65  ? -43.030 -62.445 30.082  1.000 140.042 ? 64  PHE BBB CZ  1 
ATOM   2058  N N   . GLN B 2 66  ? -45.139 -63.580 37.178  1.000 149.851 ? 65  GLN BBB N   1 
ATOM   2059  C CA  . GLN B 2 66  ? -45.210 -63.503 38.666  1.000 151.468 ? 65  GLN BBB CA  1 
ATOM   2060  C C   . GLN B 2 66  ? -43.892 -64.000 39.277  1.000 151.860 ? 65  GLN BBB C   1 
ATOM   2061  O O   . GLN B 2 66  ? -43.115 -63.153 39.759  1.000 150.673 ? 65  GLN BBB O   1 
ATOM   2062  C CB  . GLN B 2 66  ? -46.417 -64.290 39.193  1.000 156.544 ? 65  GLN BBB CB  1 
ATOM   2063  C CG  . GLN B 2 66  ? -46.608 -64.235 40.708  1.000 158.886 ? 65  GLN BBB CG  1 
ATOM   2064  C CD  . GLN B 2 66  ? -46.890 -62.841 41.218  1.000 156.961 ? 65  GLN BBB CD  1 
ATOM   2065  O OE1 . GLN B 2 66  ? -46.250 -62.375 42.154  1.000 158.115 ? 65  GLN BBB OE1 1 
ATOM   2066  N NE2 . GLN B 2 66  ? -47.834 -62.155 40.593  1.000 154.405 ? 65  GLN BBB NE2 1 
ATOM   2067  N N   . GLY B 2 67  ? -43.639 -65.311 39.220  1.000 153.981 ? 66  GLY BBB N   1 
ATOM   2068  C CA  . GLY B 2 67  ? -42.593 -65.992 40.010  1.000 155.990 ? 66  GLY BBB CA  1 
ATOM   2069  C C   . GLY B 2 67  ? -41.350 -66.305 39.197  1.000 154.805 ? 66  GLY BBB C   1 
ATOM   2070  O O   . GLY B 2 67  ? -40.612 -67.238 39.577  1.000 157.088 ? 66  GLY BBB O   1 
ATOM   2071  N N   . GLN B 2 68  ? -41.124 -65.567 38.112  1.000 152.338 ? 67  GLN BBB N   1 
ATOM   2072  C CA  . GLN B 2 68  ? -39.910 -65.699 37.266  1.000 153.802 ? 67  GLN BBB CA  1 
ATOM   2073  C C   . GLN B 2 68  ? -38.945 -64.566 37.620  1.000 151.944 ? 67  GLN BBB C   1 
ATOM   2074  O O   . GLN B 2 68  ? -37.831 -64.854 38.131  1.000 154.279 ? 67  GLN BBB O   1 
ATOM   2075  C CB  . GLN B 2 68  ? -40.304 -65.675 35.789  1.000 152.846 ? 67  GLN BBB CB  1 
ATOM   2076  C CG  . GLN B 2 68  ? -41.315 -66.756 35.428  1.000 157.105 ? 67  GLN BBB CG  1 
ATOM   2077  C CD  . GLN B 2 68  ? -40.668 -68.110 35.277  1.000 161.746 ? 67  GLN BBB CD  1 
ATOM   2078  O OE1 . GLN B 2 68  ? -39.889 -68.338 34.351  1.000 163.114 ? 67  GLN BBB OE1 1 
ATOM   2079  N NE2 . GLN B 2 68  ? -40.988 -69.019 36.188  1.000 164.277 ? 67  GLN BBB NE2 1 
ATOM   2080  N N   . VAL B 2 69  ? -39.413 -63.329 37.437  1.000 147.824 ? 68  VAL BBB N   1 
ATOM   2081  C CA  . VAL B 2 69  ? -38.577 -62.098 37.382  1.000 143.689 ? 68  VAL BBB CA  1 
ATOM   2082  C C   . VAL B 2 69  ? -39.020 -61.105 38.463  1.000 142.767 ? 68  VAL BBB C   1 
ATOM   2083  O O   . VAL B 2 69  ? -40.224 -61.076 38.806  1.000 141.245 ? 68  VAL BBB O   1 
ATOM   2084  C CB  . VAL B 2 69  ? -38.656 -61.484 35.974  1.000 140.266 ? 68  VAL BBB CB  1 
ATOM   2085  C CG1 . VAL B 2 69  ? -38.318 -62.531 34.928  1.000 141.109 ? 68  VAL BBB CG1 1 
ATOM   2086  C CG2 . VAL B 2 69  ? -40.017 -60.865 35.691  1.000 138.948 ? 68  VAL BBB CG2 1 
ATOM   2087  N N   . THR B 2 70  ? -38.058 -60.322 38.959  1.000 143.254 ? 69  THR BBB N   1 
ATOM   2088  C CA  . THR B 2 70  ? -38.236 -59.229 39.951  1.000 143.537 ? 69  THR BBB CA  1 
ATOM   2089  C C   . THR B 2 70  ? -38.070 -57.886 39.229  1.000 138.288 ? 69  THR BBB C   1 
ATOM   2090  O O   . THR B 2 70  ? -37.022 -57.663 38.582  1.000 135.692 ? 69  THR BBB O   1 
ATOM   2091  C CB  . THR B 2 70  ? -37.272 -59.394 41.139  1.000 146.995 ? 69  THR BBB CB  1 
ATOM   2092  O OG1 . THR B 2 70  ? -37.636 -60.564 41.874  1.000 151.586 ? 69  THR BBB OG1 1 
ATOM   2093  C CG2 . THR B 2 70  ? -37.261 -58.212 42.086  1.000 146.702 ? 69  THR BBB CG2 1 
ATOM   2094  N N   . ILE B 2 71  ? -39.092 -57.040 39.323  1.000 135.732 ? 70  ILE BBB N   1 
ATOM   2095  C CA  . ILE B 2 71  ? -39.043 -55.608 38.925  1.000 133.827 ? 70  ILE BBB CA  1 
ATOM   2096  C C   . ILE B 2 71  ? -38.794 -54.796 40.196  1.000 135.309 ? 70  ILE BBB C   1 
ATOM   2097  O O   . ILE B 2 71  ? -39.675 -54.813 41.070  1.000 137.075 ? 70  ILE BBB O   1 
ATOM   2098  C CB  . ILE B 2 71  ? -40.349 -55.203 38.221  1.000 133.530 ? 70  ILE BBB CB  1 
ATOM   2099  C CG1 . ILE B 2 71  ? -40.547 -55.977 36.916  1.000 134.822 ? 70  ILE BBB CG1 1 
ATOM   2100  C CG2 . ILE B 2 71  ? -40.396 -53.702 38.000  1.000 132.161 ? 70  ILE BBB CG2 1 
ATOM   2101  C CD1 . ILE B 2 71  ? -41.942 -55.858 36.330  1.000 135.440 ? 70  ILE BBB CD1 1 
ATOM   2102  N N   . SER B 2 72  ? -37.627 -54.151 40.302  1.000 136.082 ? 71  SER BBB N   1 
ATOM   2103  C CA  . SER B 2 72  ? -37.243 -53.260 41.430  1.000 136.323 ? 71  SER BBB CA  1 
ATOM   2104  C C   . SER B 2 72  ? -37.218 -51.807 40.943  1.000 133.627 ? 71  SER BBB C   1 
ATOM   2105  O O   . SER B 2 72  ? -37.354 -51.570 39.727  1.000 130.123 ? 71  SER BBB O   1 
ATOM   2106  C CB  . SER B 2 72  ? -35.925 -53.677 42.068  1.000 137.962 ? 71  SER BBB CB  1 
ATOM   2107  O OG  . SER B 2 72  ? -35.079 -54.338 41.138  1.000 138.402 ? 71  SER BBB OG  1 
ATOM   2108  N N   . ALA B 2 73  ? -37.085 -50.863 41.869  1.000 134.669 ? 72  ALA BBB N   1 
ATOM   2109  C CA  . ALA B 2 73  ? -37.005 -49.422 41.560  1.000 133.391 ? 72  ALA BBB CA  1 
ATOM   2110  C C   . ALA B 2 73  ? -36.218 -48.715 42.662  1.000 135.782 ? 72  ALA BBB C   1 
ATOM   2111  O O   . ALA B 2 73  ? -36.667 -48.717 43.830  1.000 138.655 ? 72  ALA BBB O   1 
ATOM   2112  C CB  . ALA B 2 73  ? -38.388 -48.849 41.409  1.000 132.522 ? 72  ALA BBB CB  1 
ATOM   2113  N N   . ASP B 2 74  ? -35.071 -48.159 42.284  1.000 135.648 ? 73  ASP BBB N   1 
ATOM   2114  C CA  . ASP B 2 74  ? -34.267 -47.243 43.124  1.000 140.354 ? 73  ASP BBB CA  1 
ATOM   2115  C C   . ASP B 2 74  ? -34.718 -45.824 42.781  1.000 138.700 ? 73  ASP BBB C   1 
ATOM   2116  O O   . ASP B 2 74  ? -34.091 -45.193 41.921  1.000 138.306 ? 73  ASP BBB O   1 
ATOM   2117  C CB  . ASP B 2 74  ? -32.774 -47.487 42.898  1.000 145.759 ? 73  ASP BBB CB  1 
ATOM   2118  C CG  . ASP B 2 74  ? -31.860 -46.931 43.976  1.000 153.047 ? 73  ASP BBB CG  1 
ATOM   2119  O OD1 . ASP B 2 74  ? -32.373 -46.270 44.909  1.000 158.928 ? 73  ASP BBB OD1 1 
ATOM   2120  O OD2 . ASP B 2 74  ? -30.636 -47.184 43.879  1.000 156.786 ? 73  ASP BBB OD2 1 
ATOM   2121  N N   . LYS B 2 75  ? -35.795 -45.366 43.420  1.000 139.380 ? 74  LYS BBB N   1 
ATOM   2122  C CA  . LYS B 2 75  ? -36.473 -44.078 43.112  1.000 138.366 ? 74  LYS BBB CA  1 
ATOM   2123  C C   . LYS B 2 75  ? -35.502 -42.900 43.267  1.000 137.106 ? 74  LYS BBB C   1 
ATOM   2124  O O   . LYS B 2 75  ? -35.761 -41.857 42.639  1.000 137.038 ? 74  LYS BBB O   1 
ATOM   2125  C CB  . LYS B 2 75  ? -37.685 -43.888 44.026  1.000 140.923 ? 74  LYS BBB CB  1 
ATOM   2126  C CG  . LYS B 2 75  ? -37.357 -43.765 45.505  1.000 145.647 ? 74  LYS BBB CG  1 
ATOM   2127  C CD  . LYS B 2 75  ? -38.561 -43.468 46.355  1.000 149.373 ? 74  LYS BBB CD  1 
ATOM   2128  C CE  . LYS B 2 75  ? -38.187 -43.100 47.775  1.000 154.435 ? 74  LYS BBB CE  1 
ATOM   2129  N NZ  . LYS B 2 75  ? -39.361 -42.650 48.562  1.000 157.110 ? 74  LYS BBB NZ  1 
ATOM   2130  N N   . SER B 2 76  ? -34.435 -43.070 44.058  1.000 135.955 ? 75  SER BBB N   1 
ATOM   2131  C CA  . SER B 2 76  ? -33.425 -42.028 44.383  1.000 135.954 ? 75  SER BBB CA  1 
ATOM   2132  C C   . SER B 2 76  ? -32.541 -41.701 43.173  1.000 133.127 ? 75  SER BBB C   1 
ATOM   2133  O O   . SER B 2 76  ? -31.732 -40.767 43.301  1.000 134.058 ? 75  SER BBB O   1 
ATOM   2134  C CB  . SER B 2 76  ? -32.566 -42.449 45.547  1.000 139.907 ? 75  SER BBB CB  1 
ATOM   2135  O OG  . SER B 2 76  ? -31.411 -43.150 45.101  1.000 140.344 ? 75  SER BBB OG  1 
ATOM   2136  N N   . ILE B 2 77  ? -32.633 -42.466 42.080  1.000 129.838 ? 76  ILE BBB N   1 
ATOM   2137  C CA  . ILE B 2 77  ? -31.954 -42.148 40.786  1.000 128.753 ? 76  ILE BBB CA  1 
ATOM   2138  C C   . ILE B 2 77  ? -32.935 -42.335 39.621  1.000 123.269 ? 76  ILE BBB C   1 
ATOM   2139  O O   . ILE B 2 77  ? -32.472 -42.530 38.481  1.000 119.328 ? 76  ILE BBB O   1 
ATOM   2140  C CB  . ILE B 2 77  ? -30.665 -42.980 40.609  1.000 131.902 ? 76  ILE BBB CB  1 
ATOM   2141  C CG1 . ILE B 2 77  ? -30.884 -44.473 40.871  1.000 131.861 ? 76  ILE BBB CG1 1 
ATOM   2142  C CG2 . ILE B 2 77  ? -29.553 -42.414 41.478  1.000 135.951 ? 76  ILE BBB CG2 1 
ATOM   2143  C CD1 . ILE B 2 77  ? -29.810 -45.371 40.282  1.000 132.631 ? 76  ILE BBB CD1 1 
ATOM   2144  N N   . ASN B 2 78  ? -34.239 -42.227 39.889  1.000 121.926 ? 77  ASN BBB N   1 
ATOM   2145  C CA  . ASN B 2 78  ? -35.297 -42.351 38.857  1.000 121.015 ? 77  ASN BBB CA  1 
ATOM   2146  C C   . ASN B 2 78  ? -34.985 -43.572 37.986  1.000 121.733 ? 77  ASN BBB C   1 
ATOM   2147  O O   . ASN B 2 78  ? -35.153 -43.476 36.748  1.000 129.657 ? 77  ASN BBB O   1 
ATOM   2148  C CB  . ASN B 2 78  ? -35.377 -41.087 37.993  1.000 120.586 ? 77  ASN BBB CB  1 
ATOM   2149  C CG  . ASN B 2 78  ? -36.004 -39.918 38.718  1.000 121.712 ? 77  ASN BBB CG  1 
ATOM   2150  O OD1 . ASN B 2 78  ? -36.039 -38.807 38.188  1.000 123.257 ? 77  ASN BBB OD1 1 
ATOM   2151  N ND2 . ASN B 2 78  ? -36.523 -40.174 39.911  1.000 121.359 ? 77  ASN BBB ND2 1 
ATOM   2152  N N   . THR B 2 79  ? -34.514 -44.665 38.591  1.000 118.356 ? 78  THR BBB N   1 
ATOM   2153  C CA  . THR B 2 79  ? -34.108 -45.886 37.854  1.000 115.813 ? 78  THR BBB CA  1 
ATOM   2154  C C   . THR B 2 79  ? -34.999 -47.051 38.269  1.000 115.725 ? 78  THR BBB C   1 
ATOM   2155  O O   . THR B 2 79  ? -34.923 -47.473 39.439  1.000 118.022 ? 78  THR BBB O   1 
ATOM   2156  C CB  . THR B 2 79  ? -32.631 -46.217 38.073  1.000 117.055 ? 78  THR BBB CB  1 
ATOM   2157  O OG1 . THR B 2 79  ? -31.859 -45.068 37.720  1.000 116.019 ? 78  THR BBB OG1 1 
ATOM   2158  C CG2 . THR B 2 79  ? -32.187 -47.415 37.263  1.000 117.302 ? 78  THR BBB CG2 1 
ATOM   2159  N N   . ALA B 2 80  ? -35.814 -47.534 37.333  1.000 115.416 ? 79  ALA BBB N   1 
ATOM   2160  C CA  . ALA B 2 80  ? -36.522 -48.827 37.435  1.000 117.634 ? 79  ALA BBB CA  1 
ATOM   2161  C C   . ALA B 2 80  ? -35.616 -49.913 36.854  1.000 119.651 ? 79  ALA BBB C   1 
ATOM   2162  O O   . ALA B 2 80  ? -34.866 -49.629 35.884  1.000 118.431 ? 79  ALA BBB O   1 
ATOM   2163  C CB  . ALA B 2 80  ? -37.851 -48.764 36.733  1.000 116.388 ? 79  ALA BBB CB  1 
ATOM   2164  N N   . TYR B 2 81  ? -35.653 -51.093 37.474  1.000 123.158 ? 80  TYR BBB N   1 
ATOM   2165  C CA  . TYR B 2 81  ? -34.843 -52.278 37.108  1.000 125.825 ? 80  TYR BBB CA  1 
ATOM   2166  C C   . TYR B 2 81  ? -35.770 -53.452 36.808  1.000 126.995 ? 80  TYR BBB C   1 
ATOM   2167  O O   . TYR B 2 81  ? -36.929 -53.457 37.259  1.000 126.309 ? 80  TYR BBB O   1 
ATOM   2168  C CB  . TYR B 2 81  ? -33.915 -52.708 38.245  1.000 128.536 ? 80  TYR BBB CB  1 
ATOM   2169  C CG  . TYR B 2 81  ? -32.919 -51.673 38.693  1.000 129.301 ? 80  TYR BBB CG  1 
ATOM   2170  C CD1 . TYR B 2 81  ? -31.916 -51.229 37.850  1.000 129.090 ? 80  TYR BBB CD1 1 
ATOM   2171  C CD2 . TYR B 2 81  ? -32.956 -51.168 39.980  1.000 132.059 ? 80  TYR BBB CD2 1 
ATOM   2172  C CE1 . TYR B 2 81  ? -30.986 -50.291 38.268  1.000 131.530 ? 80  TYR BBB CE1 1 
ATOM   2173  C CE2 . TYR B 2 81  ? -32.028 -50.237 40.417  1.000 133.834 ? 80  TYR BBB CE2 1 
ATOM   2174  C CZ  . TYR B 2 81  ? -31.047 -49.783 39.555  1.000 133.335 ? 80  TYR BBB CZ  1 
ATOM   2175  O OH  . TYR B 2 81  ? -30.146 -48.853 39.994  1.000 134.600 ? 80  TYR BBB OH  1 
ATOM   2176  N N   . LEU B 2 82  ? -35.225 -54.421 36.077  1.000 128.826 ? 81  LEU BBB N   1 
ATOM   2177  C CA  . LEU B 2 82  ? -35.796 -55.768 35.826  1.000 129.147 ? 81  LEU BBB CA  1 
ATOM   2178  C C   . LEU B 2 82  ? -34.646 -56.772 35.950  1.000 129.809 ? 81  LEU BBB C   1 
ATOM   2179  O O   . LEU B 2 82  ? -33.588 -56.521 35.335  1.000 129.241 ? 81  LEU BBB O   1 
ATOM   2180  C CB  . LEU B 2 82  ? -36.404 -55.778 34.420  1.000 127.316 ? 81  LEU BBB CB  1 
ATOM   2181  C CG  . LEU B 2 82  ? -36.829 -57.147 33.899  1.000 128.698 ? 81  LEU BBB CG  1 
ATOM   2182  C CD1 . LEU B 2 82  ? -38.074 -57.633 34.628  1.000 131.543 ? 81  LEU BBB CD1 1 
ATOM   2183  C CD2 . LEU B 2 82  ? -37.049 -57.105 32.397  1.000 126.408 ? 81  LEU BBB CD2 1 
ATOM   2184  N N   . GLN B 2 83  ? -34.818 -57.847 36.720  1.000 131.649 ? 82  GLN BBB N   1 
ATOM   2185  C CA  . GLN B 2 83  ? -33.719 -58.821 36.956  1.000 134.865 ? 82  GLN BBB CA  1 
ATOM   2186  C C   . GLN B 2 83  ? -34.228 -60.260 36.854  1.000 134.916 ? 82  GLN BBB C   1 
ATOM   2187  O O   . GLN B 2 83  ? -35.453 -60.464 36.889  1.000 135.834 ? 82  GLN BBB O   1 
ATOM   2188  C CB  . GLN B 2 83  ? -33.027 -58.569 38.297  1.000 139.535 ? 82  GLN BBB CB  1 
ATOM   2189  C CG  . GLN B 2 83  ? -33.950 -58.133 39.419  1.000 141.753 ? 82  GLN BBB CG  1 
ATOM   2190  C CD  . GLN B 2 83  ? -33.216 -58.112 40.739  1.000 145.703 ? 82  GLN BBB CD  1 
ATOM   2191  O OE1 . GLN B 2 83  ? -32.430 -59.008 41.048  1.000 146.706 ? 82  GLN BBB OE1 1 
ATOM   2192  N NE2 . GLN B 2 83  ? -33.455 -57.071 41.525  1.000 147.680 ? 82  GLN BBB NE2 1 
ATOM   2193  N N   . TRP B 2 84  ? -33.288 -61.201 36.705  1.000 134.295 ? 83  TRP BBB N   1 
ATOM   2194  C CA  . TRP B 2 84  ? -33.523 -62.658 36.529  1.000 135.288 ? 83  TRP BBB CA  1 
ATOM   2195  C C   . TRP B 2 84  ? -32.729 -63.441 37.578  1.000 138.795 ? 83  TRP BBB C   1 
ATOM   2196  O O   . TRP B 2 84  ? -31.491 -63.276 37.641  1.000 138.917 ? 83  TRP BBB O   1 
ATOM   2197  C CB  . TRP B 2 84  ? -33.160 -63.106 35.106  1.000 133.148 ? 83  TRP BBB CB  1 
ATOM   2198  C CG  . TRP B 2 84  ? -34.235 -62.809 34.110  1.000 129.696 ? 83  TRP BBB CG  1 
ATOM   2199  C CD1 . TRP B 2 84  ? -35.347 -63.556 33.858  1.000 130.968 ? 83  TRP BBB CD1 1 
ATOM   2200  C CD2 . TRP B 2 84  ? -34.312 -61.663 33.249  1.000 125.520 ? 83  TRP BBB CD2 1 
ATOM   2201  N NE1 . TRP B 2 84  ? -36.109 -62.954 32.895  1.000 128.663 ? 83  TRP BBB NE1 1 
ATOM   2202  C CE2 . TRP B 2 84  ? -35.505 -61.787 32.509  1.000 125.408 ? 83  TRP BBB CE2 1 
ATOM   2203  C CE3 . TRP B 2 84  ? -33.496 -60.547 33.035  1.000 123.875 ? 83  TRP BBB CE3 1 
ATOM   2204  C CZ2 . TRP B 2 84  ? -35.897 -60.833 31.570  1.000 123.573 ? 83  TRP BBB CZ2 1 
ATOM   2205  C CZ3 . TRP B 2 84  ? -33.885 -59.604 32.110  1.000 121.854 ? 83  TRP BBB CZ3 1 
ATOM   2206  C CH2 . TRP B 2 84  ? -35.070 -59.747 31.388  1.000 121.909 ? 83  TRP BBB CH2 1 
ATOM   2207  N N   . SER B 2 85  ? -33.433 -64.271 38.347  1.000 142.295 ? 84  SER BBB N   1 
ATOM   2208  C CA  . SER B 2 85  ? -32.875 -65.227 39.338  1.000 147.597 ? 84  SER BBB CA  1 
ATOM   2209  C C   . SER B 2 85  ? -31.844 -66.137 38.655  1.000 148.615 ? 84  SER BBB C   1 
ATOM   2210  O O   . SER B 2 85  ? -30.800 -66.413 39.262  1.000 150.246 ? 84  SER BBB O   1 
ATOM   2211  C CB  . SER B 2 85  ? -33.992 -66.029 39.976  1.000 151.766 ? 84  SER BBB CB  1 
ATOM   2212  O OG  . SER B 2 85  ? -35.245 -65.349 39.882  1.000 149.903 ? 84  SER BBB OG  1 
ATOM   2213  N N   . SER B 2 86  ? -32.149 -66.573 37.431  1.000 149.189 ? 85  SER BBB N   1 
ATOM   2214  C CA  . SER B 2 86  ? -31.355 -67.525 36.613  1.000 152.493 ? 85  SER BBB CA  1 
ATOM   2215  C C   . SER B 2 86  ? -31.969 -67.602 35.212  1.000 151.460 ? 85  SER BBB C   1 
ATOM   2216  O O   . SER B 2 86  ? -33.172 -67.892 35.110  1.000 153.540 ? 85  SER BBB O   1 
ATOM   2217  C CB  . SER B 2 86  ? -31.299 -68.870 37.272  1.000 158.714 ? 85  SER BBB CB  1 
ATOM   2218  O OG  . SER B 2 86  ? -30.611 -69.798 36.453  1.000 161.921 ? 85  SER BBB OG  1 
ATOM   2219  N N   . LEU B 2 87  ? -31.172 -67.337 34.177  1.000 152.376 ? 86  LEU BBB N   1 
ATOM   2220  C CA  . LEU B 2 87  ? -31.658 -67.019 32.806  1.000 153.720 ? 86  LEU BBB CA  1 
ATOM   2221  C C   . LEU B 2 87  ? -31.901 -68.295 31.999  1.000 157.002 ? 86  LEU BBB C   1 
ATOM   2222  O O   . LEU B 2 87  ? -30.966 -69.101 31.876  1.000 161.069 ? 86  LEU BBB O   1 
ATOM   2223  C CB  . LEU B 2 87  ? -30.618 -66.157 32.086  1.000 153.868 ? 86  LEU BBB CB  1 
ATOM   2224  C CG  . LEU B 2 87  ? -30.651 -64.665 32.400  1.000 152.858 ? 86  LEU BBB CG  1 
ATOM   2225  C CD1 . LEU B 2 87  ? -29.396 -63.983 31.861  1.000 152.503 ? 86  LEU BBB CD1 1 
ATOM   2226  C CD2 . LEU B 2 87  ? -31.914 -64.019 31.838  1.000 150.970 ? 86  LEU BBB CD2 1 
ATOM   2227  N N   . LYS B 2 88  ? -33.094 -68.425 31.417  1.000 156.642 ? 87  LYS BBB N   1 
ATOM   2228  C CA  . LYS B 2 88  ? -33.408 -69.440 30.380  1.000 158.038 ? 87  LYS BBB CA  1 
ATOM   2229  C C   . LYS B 2 88  ? -32.889 -68.955 29.020  1.000 154.440 ? 87  LYS BBB C   1 
ATOM   2230  O O   . LYS B 2 88  ? -32.736 -67.731 28.837  1.000 148.709 ? 87  LYS BBB O   1 
ATOM   2231  C CB  . LYS B 2 88  ? -34.919 -69.663 30.284  1.000 159.918 ? 87  LYS BBB CB  1 
ATOM   2232  C CG  . LYS B 2 88  ? -35.599 -70.182 31.539  1.000 163.443 ? 87  LYS BBB CG  1 
ATOM   2233  C CD  . LYS B 2 88  ? -36.950 -70.780 31.228  1.000 166.589 ? 87  LYS BBB CD  1 
ATOM   2234  C CE  . LYS B 2 88  ? -37.453 -71.706 32.311  1.000 171.970 ? 87  LYS BBB CE  1 
ATOM   2235  N NZ  . LYS B 2 88  ? -38.177 -70.960 33.367  1.000 172.620 ? 87  LYS BBB NZ  1 
ATOM   2236  N N   . ALA B 2 89  ? -32.656 -69.883 28.091  1.000 156.601 ? 88  ALA BBB N   1 
ATOM   2237  C CA  . ALA B 2 89  ? -32.511 -69.590 26.647  1.000 154.180 ? 88  ALA BBB CA  1 
ATOM   2238  C C   . ALA B 2 89  ? -33.737 -68.786 26.206  1.000 151.632 ? 88  ALA BBB C   1 
ATOM   2239  O O   . ALA B 2 89  ? -33.544 -67.713 25.644  1.000 149.008 ? 88  ALA BBB O   1 
ATOM   2240  C CB  . ALA B 2 89  ? -32.360 -70.866 25.852  1.000 157.141 ? 88  ALA BBB CB  1 
ATOM   2241  N N   . SER B 2 90  ? -34.943 -69.274 26.518  1.000 154.719 ? 89  SER BBB N   1 
ATOM   2242  C CA  . SER B 2 90  ? -36.250 -68.637 26.190  1.000 154.176 ? 89  SER BBB CA  1 
ATOM   2243  C C   . SER B 2 90  ? -36.182 -67.129 26.454  1.000 151.227 ? 89  SER BBB C   1 
ATOM   2244  O O   . SER B 2 90  ? -36.633 -66.358 25.581  1.000 151.468 ? 89  SER BBB O   1 
ATOM   2245  C CB  . SER B 2 90  ? -37.400 -69.266 26.955  1.000 157.143 ? 89  SER BBB CB  1 
ATOM   2246  O OG  . SER B 2 90  ? -37.710 -68.531 28.134  1.000 156.068 ? 89  SER BBB OG  1 
ATOM   2247  N N   . ASP B 2 91  ? -35.618 -66.730 27.600  1.000 149.917 ? 90  ASP BBB N   1 
ATOM   2248  C CA  . ASP B 2 91  ? -35.559 -65.314 28.061  1.000 147.100 ? 90  ASP BBB CA  1 
ATOM   2249  C C   . ASP B 2 91  ? -34.713 -64.477 27.087  1.000 144.374 ? 90  ASP BBB C   1 
ATOM   2250  O O   . ASP B 2 91  ? -34.589 -63.255 27.326  1.000 140.764 ? 90  ASP BBB O   1 
ATOM   2251  C CB  . ASP B 2 91  ? -35.059 -65.221 29.508  1.000 147.801 ? 90  ASP BBB CB  1 
ATOM   2252  C CG  . ASP B 2 91  ? -36.032 -65.784 30.534  1.000 150.890 ? 90  ASP BBB CG  1 
ATOM   2253  O OD1 . ASP B 2 91  ? -37.264 -65.683 30.297  1.000 151.973 ? 90  ASP BBB OD1 1 
ATOM   2254  O OD2 . ASP B 2 91  ? -35.555 -66.317 31.568  1.000 151.979 ? 90  ASP BBB OD2 1 
ATOM   2255  N N   . THR B 2 92  ? -34.153 -65.092 26.034  1.000 145.250 ? 91  THR BBB N   1 
ATOM   2256  C CA  . THR B 2 92  ? -33.593 -64.379 24.854  1.000 141.768 ? 91  THR BBB CA  1 
ATOM   2257  C C   . THR B 2 92  ? -34.717 -63.602 24.181  1.000 135.408 ? 91  THR BBB C   1 
ATOM   2258  O O   . THR B 2 92  ? -35.712 -64.226 23.753  1.000 132.444 ? 91  THR BBB O   1 
ATOM   2259  C CB  . THR B 2 92  ? -32.961 -65.294 23.797  1.000 145.846 ? 91  THR BBB CB  1 
ATOM   2260  O OG1 . THR B 2 92  ? -31.837 -65.978 24.352  1.000 151.481 ? 91  THR BBB OG1 1 
ATOM   2261  C CG2 . THR B 2 92  ? -32.506 -64.518 22.580  1.000 144.026 ? 91  THR BBB CG2 1 
ATOM   2262  N N   . ALA B 2 93  ? -34.528 -62.292 24.086  1.000 132.509 ? 92  ALA BBB N   1 
ATOM   2263  C CA  . ALA B 2 93  ? -35.532 -61.324 23.606  1.000 132.538 ? 92  ALA BBB CA  1 
ATOM   2264  C C   . ALA B 2 93  ? -34.939 -59.917 23.700  1.000 130.088 ? 92  ALA BBB C   1 
ATOM   2265  O O   . ALA B 2 93  ? -33.807 -59.763 24.219  1.000 128.508 ? 92  ALA BBB O   1 
ATOM   2266  C CB  . ALA B 2 93  ? -36.795 -61.444 24.425  1.000 132.752 ? 92  ALA BBB CB  1 
ATOM   2267  N N   . ILE B 2 94  ? -35.687 -58.938 23.199  1.000 128.288 ? 93  ILE BBB N   1 
ATOM   2268  C CA  . ILE B 2 94  ? -35.422 -57.491 23.431  1.000 125.183 ? 93  ILE BBB CA  1 
ATOM   2269  C C   . ILE B 2 94  ? -36.479 -57.016 24.431  1.000 122.538 ? 93  ILE BBB C   1 
ATOM   2270  O O   . ILE B 2 94  ? -37.659 -57.422 24.297  1.000 124.454 ? 93  ILE BBB O   1 
ATOM   2271  C CB  . ILE B 2 94  ? -35.398 -56.677 22.120  1.000 126.747 ? 93  ILE BBB CB  1 
ATOM   2272  C CG1 . ILE B 2 94  ? -35.315 -55.178 22.421  1.000 128.029 ? 93  ILE BBB CG1 1 
ATOM   2273  C CG2 . ILE B 2 94  ? -36.578 -57.008 21.214  1.000 127.766 ? 93  ILE BBB CG2 1 
ATOM   2274  C CD1 . ILE B 2 94  ? -34.731 -54.347 21.302  1.000 130.082 ? 93  ILE BBB CD1 1 
ATOM   2275  N N   . TYR B 2 95  ? -36.043 -56.248 25.431  1.000 117.987 ? 94  TYR BBB N   1 
ATOM   2276  C CA  . TYR B 2 95  ? -36.854 -55.825 26.598  1.000 115.218 ? 94  TYR BBB CA  1 
ATOM   2277  C C   . TYR B 2 95  ? -36.952 -54.301 26.577  1.000 111.049 ? 94  TYR BBB C   1 
ATOM   2278  O O   . TYR B 2 95  ? -35.932 -53.631 26.764  1.000 110.690 ? 94  TYR BBB O   1 
ATOM   2279  C CB  . TYR B 2 95  ? -36.248 -56.391 27.887  1.000 115.752 ? 94  TYR BBB CB  1 
ATOM   2280  C CG  . TYR B 2 95  ? -36.319 -57.895 27.990  1.000 116.860 ? 94  TYR BBB CG  1 
ATOM   2281  C CD1 . TYR B 2 95  ? -37.455 -58.525 28.468  1.000 117.729 ? 94  TYR BBB CD1 1 
ATOM   2282  C CD2 . TYR B 2 95  ? -35.265 -58.695 27.577  1.000 117.453 ? 94  TYR BBB CD2 1 
ATOM   2283  C CE1 . TYR B 2 95  ? -37.542 -59.906 28.541  1.000 119.879 ? 94  TYR BBB CE1 1 
ATOM   2284  C CE2 . TYR B 2 95  ? -35.334 -60.080 27.645  1.000 119.237 ? 94  TYR BBB CE2 1 
ATOM   2285  C CZ  . TYR B 2 95  ? -36.479 -60.689 28.129  1.000 120.599 ? 94  TYR BBB CZ  1 
ATOM   2286  O OH  . TYR B 2 95  ? -36.564 -62.052 28.208  1.000 123.767 ? 94  TYR BBB OH  1 
ATOM   2287  N N   . TYR B 2 96  ? -38.145 -53.785 26.303  1.000 110.010 ? 95  TYR BBB N   1 
ATOM   2288  C CA  . TYR B 2 96  ? -38.452 -52.337 26.317  1.000 111.511 ? 95  TYR BBB CA  1 
ATOM   2289  C C   . TYR B 2 96  ? -38.961 -51.966 27.709  1.000 111.995 ? 95  TYR BBB C   1 
ATOM   2290  O O   . TYR B 2 96  ? -39.871 -52.650 28.189  1.000 114.888 ? 95  TYR BBB O   1 
ATOM   2291  C CB  . TYR B 2 96  ? -39.515 -52.010 25.267  1.000 113.688 ? 95  TYR BBB CB  1 
ATOM   2292  C CG  . TYR B 2 96  ? -39.132 -52.274 23.829  1.000 117.035 ? 95  TYR BBB CG  1 
ATOM   2293  C CD1 . TYR B 2 96  ? -38.250 -51.440 23.153  1.000 118.775 ? 95  TYR BBB CD1 1 
ATOM   2294  C CD2 . TYR B 2 96  ? -39.690 -53.326 23.116  1.000 118.624 ? 95  TYR BBB CD2 1 
ATOM   2295  C CE1 . TYR B 2 96  ? -37.918 -51.652 21.822  1.000 118.836 ? 95  TYR BBB CE1 1 
ATOM   2296  C CE2 . TYR B 2 96  ? -39.365 -53.557 21.787  1.000 119.089 ? 95  TYR BBB CE2 1 
ATOM   2297  C CZ  . TYR B 2 96  ? -38.475 -52.716 21.137  1.000 119.538 ? 95  TYR BBB CZ  1 
ATOM   2298  O OH  . TYR B 2 96  ? -38.140 -52.914 19.830  1.000 122.720 ? 95  TYR BBB OH  1 
ATOM   2299  N N   . CYS B 2 97  ? -38.395 -50.939 28.341  1.000 112.444 ? 96  CYS BBB N   1 
ATOM   2300  C CA  . CYS B 2 97  ? -39.025 -50.255 29.502  1.000 114.447 ? 96  CYS BBB CA  1 
ATOM   2301  C C   . CYS B 2 97  ? -39.893 -49.124 28.937  1.000 117.064 ? 96  CYS BBB C   1 
ATOM   2302  O O   . CYS B 2 97  ? -39.452 -48.480 27.965  1.000 120.369 ? 96  CYS BBB O   1 
ATOM   2303  C CB  . CYS B 2 97  ? -37.997 -49.778 30.526  1.000 113.690 ? 96  CYS BBB CB  1 
ATOM   2304  S SG  . CYS B 2 97  ? -37.271 -48.151 30.188  1.000 112.254 ? 96  CYS BBB SG  1 
ATOM   2305  N N   . ALA B 2 98  ? -41.100 -48.934 29.475  1.000 118.917 ? 97  ALA BBB N   1 
ATOM   2306  C CA  . ALA B 2 98  ? -42.119 -48.011 28.921  1.000 120.898 ? 97  ALA BBB CA  1 
ATOM   2307  C C   . ALA B 2 98  ? -42.894 -47.327 30.050  1.000 123.100 ? 97  ALA BBB C   1 
ATOM   2308  O O   . ALA B 2 98  ? -43.614 -48.018 30.805  1.000 127.263 ? 97  ALA BBB O   1 
ATOM   2309  C CB  . ALA B 2 98  ? -43.052 -48.758 28.001  1.000 122.564 ? 97  ALA BBB CB  1 
ATOM   2310  N N   . GLY B 2 99  ? -42.779 -46.002 30.123  1.000 123.087 ? 98  GLY BBB N   1 
ATOM   2311  C CA  . GLY B 2 99  ? -43.470 -45.174 31.124  1.000 124.536 ? 98  GLY BBB CA  1 
ATOM   2312  C C   . GLY B 2 99  ? -44.833 -44.702 30.642  1.000 125.335 ? 98  GLY BBB C   1 
ATOM   2313  O O   . GLY B 2 99  ? -44.958 -44.302 29.477  1.000 123.050 ? 98  GLY BBB O   1 
ATOM   2314  N N   . GLY B 2 100 ? -45.831 -44.765 31.519  1.000 127.036 ? 99  GLY BBB N   1 
ATOM   2315  C CA  . GLY B 2 100 ? -46.960 -43.823 31.512  1.000 129.219 ? 99  GLY BBB CA  1 
ATOM   2316  C C   . GLY B 2 100 ? -46.863 -42.909 32.718  1.000 129.234 ? 99  GLY BBB C   1 
ATOM   2317  O O   . GLY B 2 100 ? -46.188 -43.298 33.687  1.000 128.051 ? 99  GLY BBB O   1 
ATOM   2318  N N   . SER B 2 101 ? -47.471 -41.725 32.657  1.000 130.600 ? 100 SER BBB N   1 
ATOM   2319  C CA  . SER B 2 101 ? -47.646 -40.825 33.824  1.000 132.311 ? 100 SER BBB CA  1 
ATOM   2320  C C   . SER B 2 101 ? -48.920 -41.245 34.554  1.000 131.874 ? 100 SER BBB C   1 
ATOM   2321  O O   . SER B 2 101 ? -49.979 -40.715 34.241  1.000 134.711 ? 100 SER BBB O   1 
ATOM   2322  C CB  . SER B 2 101 ? -47.678 -39.377 33.413  1.000 136.372 ? 100 SER BBB CB  1 
ATOM   2323  O OG  . SER B 2 101 ? -48.524 -39.181 32.286  1.000 142.133 ? 100 SER BBB OG  1 
ATOM   2324  N N   . GLY B 2 102 ? -48.814 -42.210 35.462  1.000 131.494 ? 101 GLY BBB N   1 
ATOM   2325  C CA  . GLY B 2 102 ? -49.973 -42.812 36.145  1.000 133.808 ? 101 GLY BBB CA  1 
ATOM   2326  C C   . GLY B 2 102 ? -50.264 -44.216 35.645  1.000 134.200 ? 101 GLY BBB C   1 
ATOM   2327  O O   . GLY B 2 102 ? -49.761 -44.598 34.579  1.000 133.456 ? 101 GLY BBB O   1 
ATOM   2328  N N   . ILE B 2 103 ? -51.042 -44.968 36.417  1.000 137.432 ? 102 ILE BBB N   1 
ATOM   2329  C CA  . ILE B 2 103 ? -51.475 -46.360 36.101  1.000 140.529 ? 102 ILE BBB CA  1 
ATOM   2330  C C   . ILE B 2 103 ? -52.840 -46.292 35.402  1.000 142.081 ? 102 ILE BBB C   1 
ATOM   2331  O O   . ILE B 2 103 ? -53.485 -45.231 35.484  1.000 146.006 ? 102 ILE BBB O   1 
ATOM   2332  C CB  . ILE B 2 103 ? -51.483 -47.203 37.395  1.000 144.864 ? 102 ILE BBB CB  1 
ATOM   2333  C CG1 . ILE B 2 103 ? -51.541 -48.711 37.125  1.000 148.964 ? 102 ILE BBB CG1 1 
ATOM   2334  C CG2 . ILE B 2 103 ? -52.599 -46.760 38.329  1.000 147.647 ? 102 ILE BBB CG2 1 
ATOM   2335  C CD1 . ILE B 2 103 ? -50.463 -49.236 36.197  1.000 149.007 ? 102 ILE BBB CD1 1 
ATOM   2336  N N   . SER B 2 104 ? -53.259 -47.375 34.737  1.000 140.691 ? 103 SER BBB N   1 
ATOM   2337  C CA  . SER B 2 104 ? -54.379 -47.391 33.759  1.000 141.357 ? 103 SER BBB CA  1 
ATOM   2338  C C   . SER B 2 104 ? -54.201 -46.199 32.816  1.000 142.110 ? 103 SER BBB C   1 
ATOM   2339  O O   . SER B 2 104 ? -55.153 -45.409 32.624  1.000 141.022 ? 103 SER BBB O   1 
ATOM   2340  C CB  . SER B 2 104 ? -55.719 -47.408 34.431  1.000 142.406 ? 103 SER BBB CB  1 
ATOM   2341  O OG  . SER B 2 104 ? -56.291 -48.706 34.333  1.000 142.864 ? 103 SER BBB OG  1 
ATOM   2342  N N   . THR B 2 105 ? -52.986 -46.090 32.279  1.000 142.768 ? 104 THR BBB N   1 
ATOM   2343  C CA  . THR B 2 105 ? -52.559 -45.039 31.329  1.000 143.427 ? 104 THR BBB CA  1 
ATOM   2344  C C   . THR B 2 105 ? -51.843 -45.697 30.155  1.000 141.526 ? 104 THR BBB C   1 
ATOM   2345  O O   . THR B 2 105 ? -51.068 -46.645 30.315  1.000 137.805 ? 104 THR BBB O   1 
ATOM   2346  C CB  . THR B 2 105 ? -51.689 -43.991 32.032  1.000 144.657 ? 104 THR BBB CB  1 
ATOM   2347  O OG1 . THR B 2 105 ? -52.051 -42.699 31.553  1.000 149.359 ? 104 THR BBB OG1 1 
ATOM   2348  C CG2 . THR B 2 105 ? -50.210 -44.196 31.806  1.000 144.339 ? 104 THR BBB CG2 1 
ATOM   2349  N N   . PRO B 2 106 ? -52.049 -45.162 28.937  1.000 143.893 ? 105 PRO BBB N   1 
ATOM   2350  C CA  . PRO B 2 106 ? -51.389 -45.689 27.756  1.000 142.874 ? 105 PRO BBB CA  1 
ATOM   2351  C C   . PRO B 2 106 ? -49.914 -45.353 27.936  1.000 138.525 ? 105 PRO BBB C   1 
ATOM   2352  O O   . PRO B 2 106 ? -49.637 -44.281 28.430  1.000 135.193 ? 105 PRO BBB O   1 
ATOM   2353  C CB  . PRO B 2 106 ? -52.010 -44.913 26.591  1.000 147.315 ? 105 PRO BBB CB  1 
ATOM   2354  C CG  . PRO B 2 106 ? -52.453 -43.602 27.218  1.000 149.523 ? 105 PRO BBB CG  1 
ATOM   2355  C CD  . PRO B 2 106 ? -52.826 -43.946 28.646  1.000 148.688 ? 105 PRO BBB CD  1 
ATOM   2356  N N   . MET B 2 107 ? -49.036 -46.280 27.571  1.000 138.593 ? 106 MET BBB N   1 
ATOM   2357  C CA  . MET B 2 107 ? -47.569 -46.074 27.620  1.000 138.100 ? 106 MET BBB CA  1 
ATOM   2358  C C   . MET B 2 107 ? -47.187 -45.059 26.539  1.000 134.267 ? 106 MET BBB C   1 
ATOM   2359  O O   . MET B 2 107 ? -47.142 -45.446 25.366  1.000 130.519 ? 106 MET BBB O   1 
ATOM   2360  C CB  . MET B 2 107 ? -46.849 -47.413 27.439  1.000 139.247 ? 106 MET BBB CB  1 
ATOM   2361  C CG  . MET B 2 107 ? -47.039 -48.283 28.667  1.000 141.035 ? 106 MET BBB CG  1 
ATOM   2362  S SD  . MET B 2 107 ? -47.086 -50.054 28.342  1.000 142.439 ? 106 MET BBB SD  1 
ATOM   2363  C CE  . MET B 2 107 ? -46.745 -50.627 30.002  1.000 142.180 ? 106 MET BBB CE  1 
ATOM   2364  N N   . ASP B 2 108 ? -46.967 -43.800 26.946  1.000 133.793 ? 107 ASP BBB N   1 
ATOM   2365  C CA  . ASP B 2 108 ? -46.809 -42.630 26.039  1.000 134.620 ? 107 ASP BBB CA  1 
ATOM   2366  C C   . ASP B 2 108 ? -45.320 -42.323 25.836  1.000 127.824 ? 107 ASP BBB C   1 
ATOM   2367  O O   . ASP B 2 108 ? -45.044 -41.392 25.063  1.000 130.274 ? 107 ASP BBB O   1 
ATOM   2368  C CB  . ASP B 2 108 ? -47.622 -41.397 26.489  1.000 142.460 ? 107 ASP BBB CB  1 
ATOM   2369  C CG  . ASP B 2 108 ? -47.457 -40.888 27.923  1.000 146.602 ? 107 ASP BBB CG  1 
ATOM   2370  O OD1 . ASP B 2 108 ? -48.149 -41.428 28.829  1.000 149.880 ? 107 ASP BBB OD1 1 
ATOM   2371  O OD2 . ASP B 2 108 ? -46.696 -39.905 28.126  1.000 147.284 ? 107 ASP BBB OD2 1 
ATOM   2372  N N   . VAL B 2 109 ? -44.410 -43.096 26.449  1.000 121.163 ? 108 VAL BBB N   1 
ATOM   2373  C CA  . VAL B 2 109 ? -42.925 -42.907 26.338  1.000 116.591 ? 108 VAL BBB CA  1 
ATOM   2374  C C   . VAL B 2 109 ? -42.216 -44.270 26.421  1.000 112.678 ? 108 VAL BBB C   1 
ATOM   2375  O O   . VAL B 2 109 ? -42.530 -45.043 27.341  1.000 113.013 ? 108 VAL BBB O   1 
ATOM   2376  C CB  . VAL B 2 109 ? -42.409 -41.910 27.398  1.000 115.537 ? 108 VAL BBB CB  1 
ATOM   2377  C CG1 . VAL B 2 109 ? -43.184 -41.989 28.705  1.000 116.704 ? 108 VAL BBB CG1 1 
ATOM   2378  C CG2 . VAL B 2 109 ? -40.919 -42.056 27.652  1.000 113.699 ? 108 VAL BBB CG2 1 
ATOM   2379  N N   . TRP B 2 110 ? -41.287 -44.545 25.498  1.000 109.296 ? 109 TRP BBB N   1 
ATOM   2380  C CA  . TRP B 2 110 ? -40.609 -45.861 25.337  1.000 107.770 ? 109 TRP BBB CA  1 
ATOM   2381  C C   . TRP B 2 110 ? -39.097 -45.666 25.292  1.000 107.078 ? 109 TRP BBB C   1 
ATOM   2382  O O   . TRP B 2 110 ? -38.643 -44.768 24.576  1.000 107.290 ? 109 TRP BBB O   1 
ATOM   2383  C CB  . TRP B 2 110 ? -41.080 -46.568 24.061  1.000 109.054 ? 109 TRP BBB CB  1 
ATOM   2384  C CG  . TRP B 2 110 ? -42.475 -47.105 24.136  1.000 110.789 ? 109 TRP BBB CG  1 
ATOM   2385  C CD1 . TRP B 2 110 ? -43.633 -46.392 24.037  1.000 114.067 ? 109 TRP BBB CD1 1 
ATOM   2386  C CD2 . TRP B 2 110 ? -42.870 -48.476 24.322  1.000 110.383 ? 109 TRP BBB CD2 1 
ATOM   2387  N NE1 . TRP B 2 110 ? -44.718 -47.219 24.162  1.000 115.096 ? 109 TRP BBB NE1 1 
ATOM   2388  C CE2 . TRP B 2 110 ? -44.282 -48.504 24.338  1.000 112.347 ? 109 TRP BBB CE2 1 
ATOM   2389  C CE3 . TRP B 2 110 ? -42.173 -49.677 24.493  1.000 109.710 ? 109 TRP BBB CE3 1 
ATOM   2390  C CZ2 . TRP B 2 110 ? -45.006 -49.681 24.512  1.000 112.249 ? 109 TRP BBB CZ2 1 
ATOM   2391  C CZ3 . TRP B 2 110 ? -42.888 -50.843 24.662  1.000 110.582 ? 109 TRP BBB CZ3 1 
ATOM   2392  C CH2 . TRP B 2 110 ? -44.286 -50.842 24.669  1.000 111.786 ? 109 TRP BBB CH2 1 
ATOM   2393  N N   . GLY B 2 111 ? -38.355 -46.505 26.010  1.000 109.404 ? 110 GLY BBB N   1 
ATOM   2394  C CA  . GLY B 2 111 ? -36.899 -46.654 25.832  1.000 113.117 ? 110 GLY BBB CA  1 
ATOM   2395  C C   . GLY B 2 111 ? -36.611 -47.427 24.562  1.000 115.751 ? 110 GLY BBB C   1 
ATOM   2396  O O   . GLY B 2 111 ? -37.491 -48.187 24.143  1.000 116.512 ? 110 GLY BBB O   1 
ATOM   2397  N N   . GLN B 2 112 ? -35.431 -47.255 23.966  1.000 118.066 ? 111 GLN BBB N   1 
ATOM   2398  C CA  . GLN B 2 112 ? -35.109 -47.873 22.650  1.000 118.608 ? 111 GLN BBB CA  1 
ATOM   2399  C C   . GLN B 2 112 ? -35.054 -49.398 22.796  1.000 117.844 ? 111 GLN BBB C   1 
ATOM   2400  O O   . GLN B 2 112 ? -35.101 -50.094 21.760  1.000 119.714 ? 111 GLN BBB O   1 
ATOM   2401  C CB  . GLN B 2 112 ? -33.828 -47.290 22.044  1.000 119.768 ? 111 GLN BBB CB  1 
ATOM   2402  C CG  . GLN B 2 112 ? -32.537 -47.587 22.785  1.000 118.965 ? 111 GLN BBB CG  1 
ATOM   2403  C CD  . GLN B 2 112 ? -31.379 -46.914 22.084  1.000 120.744 ? 111 GLN BBB CD  1 
ATOM   2404  O OE1 . GLN B 2 112 ? -31.450 -45.761 21.648  1.000 120.914 ? 111 GLN BBB OE1 1 
ATOM   2405  N NE2 . GLN B 2 112 ? -30.291 -47.649 21.952  1.000 122.176 ? 111 GLN BBB NE2 1 
ATOM   2406  N N   . GLY B 2 113 ? -34.988 -49.892 24.030  1.000 117.710 ? 112 GLY BBB N   1 
ATOM   2407  C CA  . GLY B 2 113 ? -35.004 -51.331 24.330  1.000 120.524 ? 112 GLY BBB CA  1 
ATOM   2408  C C   . GLY B 2 113 ? -33.606 -51.855 24.596  1.000 123.937 ? 112 GLY BBB C   1 
ATOM   2409  O O   . GLY B 2 113 ? -32.650 -51.341 23.981  1.000 124.149 ? 112 GLY BBB O   1 
ATOM   2410  N N   . THR B 2 114 ? -33.504 -52.826 25.506  1.000 128.769 ? 113 THR BBB N   1 
ATOM   2411  C CA  . THR B 2 114 ? -32.280 -53.595 25.847  1.000 131.635 ? 113 THR BBB CA  1 
ATOM   2412  C C   . THR B 2 114 ? -32.396 -54.976 25.191  1.000 132.268 ? 113 THR BBB C   1 
ATOM   2413  O O   . THR B 2 114 ? -33.403 -55.667 25.478  1.000 133.012 ? 113 THR BBB O   1 
ATOM   2414  C CB  . THR B 2 114 ? -32.124 -53.719 27.372  1.000 134.482 ? 113 THR BBB CB  1 
ATOM   2415  O OG1 . THR B 2 114 ? -32.172 -52.429 27.988  1.000 132.509 ? 113 THR BBB OG1 1 
ATOM   2416  C CG2 . THR B 2 114 ? -30.843 -54.422 27.770  1.000 135.705 ? 113 THR BBB CG2 1 
ATOM   2417  N N   . THR B 2 115 ? -31.434 -55.354 24.339  1.000 132.343 ? 114 THR BBB N   1 
ATOM   2418  C CA  . THR B 2 115 ? -31.334 -56.711 23.725  1.000 134.355 ? 114 THR BBB CA  1 
ATOM   2419  C C   . THR B 2 115 ? -30.560 -57.641 24.666  1.000 135.878 ? 114 THR BBB C   1 
ATOM   2420  O O   . THR B 2 115 ? -29.380 -57.339 24.968  1.000 138.188 ? 114 THR BBB O   1 
ATOM   2421  C CB  . THR B 2 115 ? -30.663 -56.689 22.344  1.000 134.030 ? 114 THR BBB CB  1 
ATOM   2422  O OG1 . THR B 2 115 ? -30.101 -55.392 22.143  1.000 133.445 ? 114 THR BBB OG1 1 
ATOM   2423  C CG2 . THR B 2 115 ? -31.621 -57.015 21.217  1.000 133.808 ? 114 THR BBB CG2 1 
ATOM   2424  N N   . VAL B 2 116 ? -31.207 -58.718 25.117  1.000 135.570 ? 115 VAL BBB N   1 
ATOM   2425  C CA  . VAL B 2 116 ? -30.599 -59.772 25.980  1.000 136.659 ? 115 VAL BBB CA  1 
ATOM   2426  C C   . VAL B 2 116 ? -30.567 -61.064 25.163  1.000 136.503 ? 115 VAL BBB C   1 
ATOM   2427  O O   . VAL B 2 116 ? -31.644 -61.472 24.662  1.000 137.731 ? 115 VAL BBB O   1 
ATOM   2428  C CB  . VAL B 2 116 ? -31.388 -59.950 27.294  1.000 138.582 ? 115 VAL BBB CB  1 
ATOM   2429  C CG1 . VAL B 2 116 ? -30.824 -61.074 28.153  1.000 140.691 ? 115 VAL BBB CG1 1 
ATOM   2430  C CG2 . VAL B 2 116 ? -31.457 -58.653 28.087  1.000 137.747 ? 115 VAL BBB CG2 1 
ATOM   2431  N N   . THR B 2 117 ? -29.384 -61.671 25.027  1.000 135.180 ? 116 THR BBB N   1 
ATOM   2432  C CA  . THR B 2 117 ? -29.163 -62.940 24.283  1.000 134.846 ? 116 THR BBB CA  1 
ATOM   2433  C C   . THR B 2 117 ? -28.504 -63.956 25.239  1.000 134.665 ? 116 THR BBB C   1 
ATOM   2434  O O   . THR B 2 117 ? -27.327 -63.762 25.618  1.000 135.245 ? 116 THR BBB O   1 
ATOM   2435  C CB  . THR B 2 117 ? -28.459 -62.615 22.953  1.000 134.305 ? 116 THR BBB CB  1 
ATOM   2436  O OG1 . THR B 2 117 ? -28.531 -63.757 22.105  1.000 137.818 ? 116 THR BBB OG1 1 
ATOM   2437  C CG2 . THR B 2 117 ? -27.017 -62.178 23.083  1.000 135.834 ? 116 THR BBB CG2 1 
ATOM   2438  N N   . VAL B 2 118 ? -29.269 -64.972 25.651  1.000 133.528 ? 117 VAL BBB N   1 
ATOM   2439  C CA  . VAL B 2 118 ? -28.864 -66.043 26.607  1.000 137.128 ? 117 VAL BBB CA  1 
ATOM   2440  C C   . VAL B 2 118 ? -28.453 -67.265 25.792  1.000 140.298 ? 117 VAL BBB C   1 
ATOM   2441  O O   . VAL B 2 118 ? -29.346 -68.073 25.472  1.000 142.970 ? 117 VAL BBB O   1 
ATOM   2442  C CB  . VAL B 2 118 ? -30.014 -66.409 27.567  1.000 138.289 ? 117 VAL BBB CB  1 
ATOM   2443  C CG1 . VAL B 2 118 ? -29.604 -67.471 28.577  1.000 141.787 ? 117 VAL BBB CG1 1 
ATOM   2444  C CG2 . VAL B 2 118 ? -30.559 -65.183 28.275  1.000 136.572 ? 117 VAL BBB CG2 1 
ATOM   2445  N N   . ALA B 2 119 ? -27.169 -67.396 25.457  1.000 142.292 ? 118 ALA BBB N   1 
ATOM   2446  C CA  . ALA B 2 119 ? -26.631 -68.602 24.785  1.000 145.932 ? 118 ALA BBB CA  1 
ATOM   2447  C C   . ALA B 2 119 ? -25.108 -68.623 24.859  1.000 147.351 ? 118 ALA BBB C   1 
ATOM   2448  O O   . ALA B 2 119 ? -24.496 -67.547 24.743  1.000 146.310 ? 118 ALA BBB O   1 
ATOM   2449  C CB  . ALA B 2 119 ? -27.091 -68.654 23.355  1.000 144.947 ? 118 ALA BBB CB  1 
ATOM   2450  N N   . SER B 2 120 ? -24.542 -69.818 25.032  1.000 151.068 ? 119 SER BBB N   1 
ATOM   2451  C CA  . SER B 2 120 ? -23.117 -70.114 24.749  1.000 154.144 ? 119 SER BBB CA  1 
ATOM   2452  C C   . SER B 2 120 ? -22.863 -69.824 23.268  1.000 152.922 ? 119 SER BBB C   1 
ATOM   2453  O O   . SER B 2 120 ? -23.803 -69.984 22.457  1.000 149.309 ? 119 SER BBB O   1 
ATOM   2454  C CB  . SER B 2 120 ? -22.744 -71.524 25.133  1.000 158.768 ? 119 SER BBB CB  1 
ATOM   2455  O OG  . SER B 2 120 ? -23.836 -72.404 24.930  1.000 161.141 ? 119 SER BBB OG  1 
ATOM   2456  N N   . THR B 2 121 ? -21.643 -69.393 22.950  1.000 155.783 ? 120 THR BBB N   1 
ATOM   2457  C CA  . THR B 2 121 ? -21.259 -68.840 21.627  1.000 156.566 ? 120 THR BBB CA  1 
ATOM   2458  C C   . THR B 2 121 ? -20.631 -69.931 20.754  1.000 160.590 ? 120 THR BBB C   1 
ATOM   2459  O O   . THR B 2 121 ? -20.229 -70.986 21.287  1.000 164.706 ? 120 THR BBB O   1 
ATOM   2460  C CB  . THR B 2 121 ? -20.310 -67.641 21.764  1.000 155.852 ? 120 THR BBB CB  1 
ATOM   2461  O OG1 . THR B 2 121 ? -18.980 -68.107 22.000  1.000 159.500 ? 120 THR BBB OG1 1 
ATOM   2462  C CG2 . THR B 2 121 ? -20.725 -66.685 22.861  1.000 153.486 ? 120 THR BBB CG2 1 
ATOM   2463  N N   . LYS B 2 122 ? -20.570 -69.658 19.452  1.000 159.611 ? 121 LYS BBB N   1 
ATOM   2464  C CA  . LYS B 2 122 ? -19.892 -70.483 18.423  1.000 162.764 ? 121 LYS BBB CA  1 
ATOM   2465  C C   . LYS B 2 122 ? -19.743 -69.592 17.187  1.000 161.341 ? 121 LYS BBB C   1 
ATOM   2466  O O   . LYS B 2 122 ? -20.767 -69.035 16.728  1.000 159.595 ? 121 LYS BBB O   1 
ATOM   2467  C CB  . LYS B 2 122 ? -20.685 -71.769 18.157  1.000 165.676 ? 121 LYS BBB CB  1 
ATOM   2468  C CG  . LYS B 2 122 ? -19.934 -72.872 17.417  1.000 169.588 ? 121 LYS BBB CG  1 
ATOM   2469  C CD  . LYS B 2 122 ? -20.091 -72.831 15.906  1.000 167.929 ? 121 LYS BBB CD  1 
ATOM   2470  C CE  . LYS B 2 122 ? -19.778 -74.152 15.233  1.000 171.273 ? 121 LYS BBB CE  1 
ATOM   2471  N NZ  . LYS B 2 122 ? -18.338 -74.489 15.323  1.000 174.063 ? 121 LYS BBB NZ  1 
ATOM   2472  N N   . GLY B 2 123 ? -18.507 -69.428 16.710  1.000 163.163 ? 122 GLY BBB N   1 
ATOM   2473  C CA  . GLY B 2 123 ? -18.142 -68.482 15.638  1.000 160.372 ? 122 GLY BBB CA  1 
ATOM   2474  C C   . GLY B 2 123 ? -18.566 -68.977 14.258  1.000 159.363 ? 122 GLY BBB C   1 
ATOM   2475  O O   . GLY B 2 123 ? -18.520 -70.175 13.973  1.000 162.784 ? 122 GLY BBB O   1 
ATOM   2476  N N   . PRO B 2 124 ? -18.945 -68.055 13.345  1.000 153.350 ? 123 PRO BBB N   1 
ATOM   2477  C CA  . PRO B 2 124 ? -19.454 -68.431 12.031  1.000 151.430 ? 123 PRO BBB CA  1 
ATOM   2478  C C   . PRO B 2 124 ? -18.341 -68.839 11.060  1.000 151.675 ? 123 PRO BBB C   1 
ATOM   2479  O O   . PRO B 2 124 ? -17.334 -68.165 11.034  1.000 151.114 ? 123 PRO BBB O   1 
ATOM   2480  C CB  . PRO B 2 124 ? -20.093 -67.133 11.527  1.000 148.496 ? 123 PRO BBB CB  1 
ATOM   2481  C CG  . PRO B 2 124 ? -19.256 -66.052 12.154  1.000 148.076 ? 123 PRO BBB CG  1 
ATOM   2482  C CD  . PRO B 2 124 ? -18.854 -66.597 13.510  1.000 150.382 ? 123 PRO BBB CD  1 
ATOM   2483  N N   . SER B 2 125 ? -18.558 -69.912 10.295  1.000 151.942 ? 124 SER BBB N   1 
ATOM   2484  C CA  . SER B 2 125 ? -17.799 -70.211 9.054   1.000 153.519 ? 124 SER BBB CA  1 
ATOM   2485  C C   . SER B 2 125 ? -18.288 -69.265 7.954   1.000 151.628 ? 124 SER BBB C   1 
ATOM   2486  O O   . SER B 2 125 ? -19.507 -69.015 7.881   1.000 150.411 ? 124 SER BBB O   1 
ATOM   2487  C CB  . SER B 2 125 ? -17.927 -71.650 8.647   1.000 156.299 ? 124 SER BBB CB  1 
ATOM   2488  O OG  . SER B 2 125 ? -16.882 -72.421 9.215   1.000 160.278 ? 124 SER BBB OG  1 
ATOM   2489  N N   . VAL B 2 126 ? -17.365 -68.741 7.150   1.000 151.941 ? 125 VAL BBB N   1 
ATOM   2490  C CA  . VAL B 2 126 ? -17.689 -67.804 6.037   1.000 150.236 ? 125 VAL BBB CA  1 
ATOM   2491  C C   . VAL B 2 126 ? -17.168 -68.411 4.737   1.000 151.702 ? 125 VAL BBB C   1 
ATOM   2492  O O   . VAL B 2 126 ? -15.933 -68.527 4.581   1.000 153.231 ? 125 VAL BBB O   1 
ATOM   2493  C CB  . VAL B 2 126 ? -17.110 -66.400 6.279   1.000 150.096 ? 125 VAL BBB CB  1 
ATOM   2494  C CG1 . VAL B 2 126 ? -17.469 -65.447 5.148   1.000 149.672 ? 125 VAL BBB CG1 1 
ATOM   2495  C CG2 . VAL B 2 126 ? -17.558 -65.835 7.617   1.000 148.652 ? 125 VAL BBB CG2 1 
ATOM   2496  N N   . PHE B 2 127 ? -18.100 -68.796 3.867   1.000 150.505 ? 126 PHE BBB N   1 
ATOM   2497  C CA  . PHE B 2 127 ? -17.843 -69.346 2.518   1.000 152.317 ? 126 PHE BBB CA  1 
ATOM   2498  C C   . PHE B 2 127 ? -18.310 -68.319 1.490   1.000 150.867 ? 126 PHE BBB C   1 
ATOM   2499  O O   . PHE B 2 127 ? -19.281 -67.598 1.717   1.000 147.586 ? 126 PHE BBB O   1 
ATOM   2500  C CB  . PHE B 2 127 ? -18.541 -70.699 2.371   1.000 154.263 ? 126 PHE BBB CB  1 
ATOM   2501  C CG  . PHE B 2 127 ? -18.285 -71.668 3.500   1.000 155.807 ? 126 PHE BBB CG  1 
ATOM   2502  C CD1 . PHE B 2 127 ? -16.997 -72.080 3.809   1.000 157.608 ? 126 PHE BBB CD1 1 
ATOM   2503  C CD2 . PHE B 2 127 ? -19.334 -72.194 4.241   1.000 156.178 ? 126 PHE BBB CD2 1 
ATOM   2504  C CE1 . PHE B 2 127 ? -16.766 -72.985 4.836   1.000 158.910 ? 126 PHE BBB CE1 1 
ATOM   2505  C CE2 . PHE B 2 127 ? -19.102 -73.108 5.260   1.000 157.284 ? 126 PHE BBB CE2 1 
ATOM   2506  C CZ  . PHE B 2 127 ? -17.818 -73.503 5.555   1.000 158.558 ? 126 PHE BBB CZ  1 
ATOM   2507  N N   . PRO B 2 128 ? -17.606 -68.198 0.344   1.000 152.538 ? 127 PRO BBB N   1 
ATOM   2508  C CA  . PRO B 2 128 ? -18.041 -67.325 -0.742  1.000 152.302 ? 127 PRO BBB CA  1 
ATOM   2509  C C   . PRO B 2 128 ? -19.055 -67.996 -1.683  1.000 154.778 ? 127 PRO BBB C   1 
ATOM   2510  O O   . PRO B 2 128 ? -19.186 -69.221 -1.656  1.000 154.930 ? 127 PRO BBB O   1 
ATOM   2511  C CB  . PRO B 2 128 ? -16.713 -67.043 -1.454  1.000 153.685 ? 127 PRO BBB CB  1 
ATOM   2512  C CG  . PRO B 2 128 ? -15.934 -68.323 -1.305  1.000 156.074 ? 127 PRO BBB CG  1 
ATOM   2513  C CD  . PRO B 2 128 ? -16.337 -68.875 0.045   1.000 155.056 ? 127 PRO BBB CD  1 
ATOM   2514  N N   . LEU B 2 129 ? -19.747 -67.173 -2.479  1.000 155.458 ? 128 LEU BBB N   1 
ATOM   2515  C CA  . LEU B 2 129 ? -20.729 -67.599 -3.513  1.000 156.843 ? 128 LEU BBB CA  1 
ATOM   2516  C C   . LEU B 2 129 ? -20.364 -66.933 -4.850  1.000 157.376 ? 128 LEU BBB C   1 
ATOM   2517  O O   . LEU B 2 129 ? -20.874 -65.835 -5.134  1.000 155.183 ? 128 LEU BBB O   1 
ATOM   2518  C CB  . LEU B 2 129 ? -22.140 -67.212 -3.052  1.000 155.450 ? 128 LEU BBB CB  1 
ATOM   2519  C CG  . LEU B 2 129 ? -22.610 -67.804 -1.721  1.000 154.326 ? 128 LEU BBB CG  1 
ATOM   2520  C CD1 . LEU B 2 129 ? -23.920 -67.153 -1.291  1.000 151.327 ? 128 LEU BBB CD1 1 
ATOM   2521  C CD2 . LEU B 2 129 ? -22.760 -69.324 -1.797  1.000 157.005 ? 128 LEU BBB CD2 1 
ATOM   2522  N N   . ALA B 2 130 ? -19.502 -67.573 -5.640  1.000 160.361 ? 129 ALA BBB N   1 
ATOM   2523  C CA  . ALA B 2 130 ? -18.944 -67.024 -6.897  1.000 164.643 ? 129 ALA BBB CA  1 
ATOM   2524  C C   . ALA B 2 130 ? -20.011 -66.974 -7.989  1.000 167.923 ? 129 ALA BBB C   1 
ATOM   2525  O O   . ALA B 2 130 ? -20.820 -67.891 -8.126  1.000 170.480 ? 129 ALA BBB O   1 
ATOM   2526  C CB  . ALA B 2 130 ? -17.773 -67.860 -7.335  1.000 168.479 ? 129 ALA BBB CB  1 
ATOM   2527  N N   . PRO B 2 131 ? -20.013 -65.914 -8.827  1.000 168.635 ? 130 PRO BBB N   1 
ATOM   2528  C CA  . PRO B 2 131 ? -21.049 -65.732 -9.849  1.000 169.436 ? 130 PRO BBB CA  1 
ATOM   2529  C C   . PRO B 2 131 ? -20.849 -66.481 -11.178 1.000 171.160 ? 130 PRO BBB C   1 
ATOM   2530  O O   . PRO B 2 131 ? -19.807 -67.099 -11.363 1.000 168.805 ? 130 PRO BBB O   1 
ATOM   2531  C CB  . PRO B 2 131 ? -20.965 -64.221 -10.107 1.000 170.273 ? 130 PRO BBB CB  1 
ATOM   2532  C CG  . PRO B 2 131 ? -19.503 -63.883 -9.889  1.000 170.345 ? 130 PRO BBB CG  1 
ATOM   2533  C CD  . PRO B 2 131 ? -19.025 -64.823 -8.804  1.000 167.707 ? 130 PRO BBB CD  1 
ATOM   2534  N N   . SER B 2 132 ? -21.864 -66.403 -12.049 1.000 172.975 ? 131 SER BBB N   1 
ATOM   2535  C CA  . SER B 2 132 ? -21.839 -66.826 -13.477 1.000 177.310 ? 131 SER BBB CA  1 
ATOM   2536  C C   . SER B 2 132 ? -22.448 -65.723 -14.360 1.000 180.438 ? 131 SER BBB C   1 
ATOM   2537  O O   . SER B 2 132 ? -23.247 -64.895 -13.838 1.000 177.305 ? 131 SER BBB O   1 
ATOM   2538  C CB  A SER B 2 132 ? -22.543 -68.146 -13.685 0.500 178.181 ? 131 SER BBB CB  1 
ATOM   2539  C CB  B SER B 2 132 ? -22.559 -68.144 -13.671 0.500 177.428 ? 131 SER BBB CB  1 
ATOM   2540  O OG  A SER B 2 132 ? -23.890 -68.079 -13.249 0.500 176.244 ? 131 SER BBB OG  1 
ATOM   2541  O OG  B SER B 2 132 ? -22.381 -68.639 -14.989 0.500 179.459 ? 131 SER BBB OG  1 
ATOM   2542  N N   . SER B 2 133 ? -22.073 -65.724 -15.645 1.000 185.268 ? 132 SER BBB N   1 
ATOM   2543  C CA  . SER B 2 133 ? -22.571 -64.813 -16.711 1.000 186.534 ? 132 SER BBB CA  1 
ATOM   2544  C C   . SER B 2 133 ? -22.600 -65.552 -18.058 1.000 187.494 ? 132 SER BBB C   1 
ATOM   2545  O O   . SER B 2 133 ? -22.789 -66.785 -18.039 1.000 183.302 ? 132 SER BBB O   1 
ATOM   2546  C CB  . SER B 2 133 ? -21.730 -63.561 -16.793 1.000 186.746 ? 132 SER BBB CB  1 
ATOM   2547  O OG  . SER B 2 133 ? -22.234 -62.678 -17.786 1.000 190.467 ? 132 SER BBB OG  1 
ATOM   2548  N N   . GLY B 2 138 ? -23.452 -60.961 -21.997 1.000 205.710 ? 137 GLY BBB N   1 
ATOM   2549  C CA  . GLY B 2 138 ? -23.617 -60.836 -20.533 1.000 200.955 ? 137 GLY BBB CA  1 
ATOM   2550  C C   . GLY B 2 138 ? -24.155 -59.468 -20.133 1.000 199.093 ? 137 GLY BBB C   1 
ATOM   2551  O O   . GLY B 2 138 ? -23.680 -58.455 -20.700 1.000 199.837 ? 137 GLY BBB O   1 
ATOM   2552  N N   . GLY B 2 139 ? -25.104 -59.443 -19.184 1.000 194.924 ? 138 GLY BBB N   1 
ATOM   2553  C CA  . GLY B 2 139 ? -25.802 -58.236 -18.695 1.000 192.048 ? 138 GLY BBB CA  1 
ATOM   2554  C C   . GLY B 2 139 ? -25.458 -57.940 -17.245 1.000 186.221 ? 138 GLY BBB C   1 
ATOM   2555  O O   . GLY B 2 139 ? -24.450 -57.249 -17.010 1.000 184.464 ? 138 GLY BBB O   1 
ATOM   2556  N N   . THR B 2 140 ? -26.265 -58.437 -16.302 1.000 183.118 ? 139 THR BBB N   1 
ATOM   2557  C CA  . THR B 2 140 ? -25.982 -58.382 -14.840 1.000 176.897 ? 139 THR BBB CA  1 
ATOM   2558  C C   . THR B 2 140 ? -25.521 -59.767 -14.370 1.000 176.445 ? 139 THR BBB C   1 
ATOM   2559  O O   . THR B 2 140 ? -25.956 -60.785 -14.977 1.000 182.023 ? 139 THR BBB O   1 
ATOM   2560  C CB  . THR B 2 140 ? -27.187 -57.875 -14.031 1.000 172.393 ? 139 THR BBB CB  1 
ATOM   2561  O OG1 . THR B 2 140 ? -26.828 -57.930 -12.652 1.000 162.735 ? 139 THR BBB OG1 1 
ATOM   2562  C CG2 . THR B 2 140 ? -28.455 -58.673 -14.251 1.000 174.243 ? 139 THR BBB CG2 1 
ATOM   2563  N N   . ALA B 2 141 ? -24.667 -59.794 -13.341 1.000 170.561 ? 140 ALA BBB N   1 
ATOM   2564  C CA  . ALA B 2 141 ? -24.198 -61.012 -12.638 1.000 168.184 ? 140 ALA BBB CA  1 
ATOM   2565  C C   . ALA B 2 141 ? -23.976 -60.663 -11.164 1.000 162.669 ? 140 ALA BBB C   1 
ATOM   2566  O O   . ALA B 2 141 ? -23.455 -59.572 -10.903 1.000 160.978 ? 140 ALA BBB O   1 
ATOM   2567  C CB  . ALA B 2 141 ? -22.943 -61.550 -13.281 1.000 170.550 ? 140 ALA BBB CB  1 
ATOM   2568  N N   . ALA B 2 142 ? -24.367 -61.561 -10.253 1.000 160.647 ? 141 ALA BBB N   1 
ATOM   2569  C CA  . ALA B 2 142 ? -24.454 -61.333 -8.790  1.000 156.674 ? 141 ALA BBB CA  1 
ATOM   2570  C C   . ALA B 2 142 ? -23.598 -62.361 -8.041  1.000 156.805 ? 141 ALA BBB C   1 
ATOM   2571  O O   . ALA B 2 142 ? -23.439 -63.480 -8.555  1.000 158.774 ? 141 ALA BBB O   1 
ATOM   2572  C CB  . ALA B 2 142 ? -25.893 -61.414 -8.355  1.000 154.342 ? 141 ALA BBB CB  1 
ATOM   2573  N N   . LEU B 2 143 ? -23.097 -61.986 -6.858  1.000 156.053 ? 142 LEU BBB N   1 
ATOM   2574  C CA  . LEU B 2 143 ? -22.201 -62.804 -5.990  1.000 155.309 ? 142 LEU BBB CA  1 
ATOM   2575  C C   . LEU B 2 143 ? -22.503 -62.493 -4.516  1.000 152.472 ? 142 LEU BBB C   1 
ATOM   2576  O O   . LEU B 2 143 ? -23.231 -61.510 -4.267  1.000 150.344 ? 142 LEU BBB O   1 
ATOM   2577  C CB  . LEU B 2 143 ? -20.742 -62.486 -6.339  1.000 156.196 ? 142 LEU BBB CB  1 
ATOM   2578  C CG  . LEU B 2 143 ? -20.306 -61.027 -6.189  1.000 154.306 ? 142 LEU BBB CG  1 
ATOM   2579  C CD1 . LEU B 2 143 ? -19.807 -60.733 -4.781  1.000 150.034 ? 142 LEU BBB CD1 1 
ATOM   2580  C CD2 . LEU B 2 143 ? -19.228 -60.688 -7.211  1.000 157.625 ? 142 LEU BBB CD2 1 
ATOM   2581  N N   . GLY B 2 144 ? -21.964 -63.286 -3.578  1.000 152.250 ? 143 GLY BBB N   1 
ATOM   2582  C CA  . GLY B 2 144 ? -22.262 -63.138 -2.141  1.000 149.412 ? 143 GLY BBB CA  1 
ATOM   2583  C C   . GLY B 2 144 ? -21.411 -63.998 -1.218  1.000 149.221 ? 143 GLY BBB C   1 
ATOM   2584  O O   . GLY B 2 144 ? -20.516 -64.724 -1.697  1.000 149.200 ? 143 GLY BBB O   1 
ATOM   2585  N N   . CYS B 2 145 ? -21.703 -63.889 0.081   1.000 155.095 ? 144 CYS BBB N   1 
ATOM   2586  C CA  . CYS B 2 145 ? -21.104 -64.652 1.206   1.000 155.596 ? 144 CYS BBB CA  1 
ATOM   2587  C C   . CYS B 2 145 ? -22.170 -65.556 1.829   1.000 152.668 ? 144 CYS BBB C   1 
ATOM   2588  O O   . CYS B 2 145 ? -23.350 -65.153 1.870   1.000 152.079 ? 144 CYS BBB O   1 
ATOM   2589  C CB  . CYS B 2 145 ? -20.538 -63.714 2.270   1.000 158.334 ? 144 CYS BBB CB  1 
ATOM   2590  S SG  . CYS B 2 145 ? -18.800 -63.293 1.976   1.000 165.005 ? 144 CYS BBB SG  1 
ATOM   2591  N N   . LEU B 2 146 ? -21.765 -66.742 2.279   1.000 151.226 ? 145 LEU BBB N   1 
ATOM   2592  C CA  . LEU B 2 146 ? -22.599 -67.614 3.139   1.000 149.722 ? 145 LEU BBB CA  1 
ATOM   2593  C C   . LEU B 2 146 ? -21.976 -67.680 4.535   1.000 151.030 ? 145 LEU BBB C   1 
ATOM   2594  O O   . LEU B 2 146 ? -20.818 -68.118 4.652   1.000 151.711 ? 145 LEU BBB O   1 
ATOM   2595  C CB  . LEU B 2 146 ? -22.703 -69.006 2.520   1.000 149.169 ? 145 LEU BBB CB  1 
ATOM   2596  C CG  . LEU B 2 146 ? -23.657 -69.945 3.247   1.000 148.474 ? 145 LEU BBB CG  1 
ATOM   2597  C CD1 . LEU B 2 146 ? -25.082 -69.410 3.193   1.000 147.333 ? 145 LEU BBB CD1 1 
ATOM   2598  C CD2 . LEU B 2 146 ? -23.585 -71.345 2.654   1.000 150.156 ? 145 LEU BBB CD2 1 
ATOM   2599  N N   . VAL B 2 147 ? -22.732 -67.252 5.547   1.000 150.710 ? 146 VAL BBB N   1 
ATOM   2600  C CA  . VAL B 2 147 ? -22.330 -67.236 6.981   1.000 150.961 ? 146 VAL BBB CA  1 
ATOM   2601  C C   . VAL B 2 147 ? -23.069 -68.378 7.683   1.000 151.294 ? 146 VAL BBB C   1 
ATOM   2602  O O   . VAL B 2 147 ? -24.267 -68.206 7.982   1.000 149.701 ? 146 VAL BBB O   1 
ATOM   2603  C CB  . VAL B 2 147 ? -22.653 -65.870 7.609   1.000 152.661 ? 146 VAL BBB CB  1 
ATOM   2604  C CG1 . VAL B 2 147 ? -22.273 -65.814 9.077   1.000 154.759 ? 146 VAL BBB CG1 1 
ATOM   2605  C CG2 . VAL B 2 147 ? -21.997 -64.734 6.838   1.000 153.963 ? 146 VAL BBB CG2 1 
ATOM   2606  N N   . LYS B 2 148 ? -22.376 -69.494 7.930   1.000 154.202 ? 147 LYS BBB N   1 
ATOM   2607  C CA  . LYS B 2 148 ? -22.980 -70.803 8.303   1.000 156.052 ? 147 LYS BBB CA  1 
ATOM   2608  C C   . LYS B 2 148 ? -22.552 -71.209 9.720   1.000 155.963 ? 147 LYS BBB C   1 
ATOM   2609  O O   . LYS B 2 148 ? -21.400 -70.932 10.100  1.000 154.245 ? 147 LYS BBB O   1 
ATOM   2610  C CB  . LYS B 2 148 ? -22.569 -71.881 7.291   1.000 158.864 ? 147 LYS BBB CB  1 
ATOM   2611  C CG  . LYS B 2 148 ? -23.382 -73.172 7.345   1.000 161.392 ? 147 LYS BBB CG  1 
ATOM   2612  C CD  . LYS B 2 148 ? -22.746 -74.351 6.616   1.000 163.960 ? 147 LYS BBB CD  1 
ATOM   2613  C CE  . LYS B 2 148 ? -23.447 -75.675 6.863   1.000 165.282 ? 147 LYS BBB CE  1 
ATOM   2614  N NZ  . LYS B 2 148 ? -24.768 -75.756 6.194   1.000 164.624 ? 147 LYS BBB NZ  1 
ATOM   2615  N N   . ASP B 2 149 ? -23.465 -71.859 10.451  1.000 156.491 ? 148 ASP BBB N   1 
ATOM   2616  C CA  . ASP B 2 149 ? -23.207 -72.580 11.728  1.000 158.610 ? 148 ASP BBB CA  1 
ATOM   2617  C C   . ASP B 2 149 ? -22.572 -71.621 12.748  1.000 158.855 ? 148 ASP BBB C   1 
ATOM   2618  O O   . ASP B 2 149 ? -21.398 -71.821 13.105  1.000 159.729 ? 148 ASP BBB O   1 
ATOM   2619  C CB  . ASP B 2 149 ? -22.372 -73.842 11.473  1.000 161.021 ? 148 ASP BBB CB  1 
ATOM   2620  C CG  . ASP B 2 149 ? -23.096 -74.957 10.726  1.000 161.770 ? 148 ASP BBB CG  1 
ATOM   2621  O OD1 . ASP B 2 149 ? -24.346 -75.036 10.825  1.000 159.747 ? 148 ASP BBB OD1 1 
ATOM   2622  O OD2 . ASP B 2 149 ? -22.400 -75.757 10.062  1.000 164.900 ? 148 ASP BBB OD2 1 
ATOM   2623  N N   . TYR B 2 150 ? -23.343 -70.620 13.195  1.000 157.807 ? 149 TYR BBB N   1 
ATOM   2624  C CA  . TYR B 2 150 ? -22.991 -69.652 14.271  1.000 157.766 ? 149 TYR BBB CA  1 
ATOM   2625  C C   . TYR B 2 150 ? -24.153 -69.537 15.260  1.000 157.673 ? 149 TYR BBB C   1 
ATOM   2626  O O   . TYR B 2 150 ? -25.309 -69.837 14.889  1.000 155.778 ? 149 TYR BBB O   1 
ATOM   2627  C CB  . TYR B 2 150 ? -22.653 -68.277 13.693  1.000 157.303 ? 149 TYR BBB CB  1 
ATOM   2628  C CG  . TYR B 2 150 ? -23.821 -67.488 13.154  1.000 157.406 ? 149 TYR BBB CG  1 
ATOM   2629  C CD1 . TYR B 2 150 ? -24.582 -66.675 13.978  1.000 158.999 ? 149 TYR BBB CD1 1 
ATOM   2630  C CD2 . TYR B 2 150 ? -24.161 -67.535 11.809  1.000 157.382 ? 149 TYR BBB CD2 1 
ATOM   2631  C CE1 . TYR B 2 150 ? -25.653 -65.941 13.490  1.000 158.715 ? 149 TYR BBB CE1 1 
ATOM   2632  C CE2 . TYR B 2 150 ? -25.225 -66.804 11.301  1.000 156.805 ? 149 TYR BBB CE2 1 
ATOM   2633  C CZ  . TYR B 2 150 ? -25.974 -66.001 12.144  1.000 157.155 ? 149 TYR BBB CZ  1 
ATOM   2634  O OH  . TYR B 2 150 ? -27.022 -65.277 11.652  1.000 156.405 ? 149 TYR BBB OH  1 
ATOM   2635  N N   . PHE B 2 151 ? -23.844 -69.094 16.479  1.000 159.717 ? 150 PHE BBB N   1 
ATOM   2636  C CA  . PHE B 2 151 ? -24.778 -69.045 17.634  1.000 161.154 ? 150 PHE BBB CA  1 
ATOM   2637  C C   . PHE B 2 151 ? -24.137 -68.220 18.743  1.000 162.107 ? 150 PHE BBB C   1 
ATOM   2638  O O   . PHE B 2 151 ? -22.930 -68.291 18.944  1.000 162.159 ? 150 PHE BBB O   1 
ATOM   2639  C CB  . PHE B 2 151 ? -25.093 -70.467 18.110  1.000 163.933 ? 150 PHE BBB CB  1 
ATOM   2640  C CG  . PHE B 2 151 ? -26.337 -70.640 18.947  1.000 166.464 ? 150 PHE BBB CG  1 
ATOM   2641  C CD1 . PHE B 2 151 ? -27.586 -70.276 18.460  1.000 166.169 ? 150 PHE BBB CD1 1 
ATOM   2642  C CD2 . PHE B 2 151 ? -26.267 -71.237 20.198  1.000 169.861 ? 150 PHE BBB CD2 1 
ATOM   2643  C CE1 . PHE B 2 151 ? -28.728 -70.458 19.226  1.000 168.583 ? 150 PHE BBB CE1 1 
ATOM   2644  C CE2 . PHE B 2 151 ? -27.411 -71.429 20.957  1.000 172.053 ? 150 PHE BBB CE2 1 
ATOM   2645  C CZ  . PHE B 2 151 ? -28.639 -71.039 20.469  1.000 171.545 ? 150 PHE BBB CZ  1 
ATOM   2646  N N   . PRO B 2 152 ? -24.896 -67.365 19.460  1.000 163.538 ? 151 PRO BBB N   1 
ATOM   2647  C CA  . PRO B 2 152 ? -26.250 -66.986 19.065  1.000 161.946 ? 151 PRO BBB CA  1 
ATOM   2648  C C   . PRO B 2 152 ? -26.198 -65.872 18.017  1.000 159.245 ? 151 PRO BBB C   1 
ATOM   2649  O O   . PRO B 2 152 ? -25.114 -65.517 17.613  1.000 158.390 ? 151 PRO BBB O   1 
ATOM   2650  C CB  . PRO B 2 152 ? -26.849 -66.458 20.370  1.000 166.065 ? 151 PRO BBB CB  1 
ATOM   2651  C CG  . PRO B 2 152 ? -25.661 -65.846 21.089  1.000 168.740 ? 151 PRO BBB CG  1 
ATOM   2652  C CD  . PRO B 2 152 ? -24.477 -66.708 20.706  1.000 167.592 ? 151 PRO BBB CD  1 
ATOM   2653  N N   . GLU B 2 153 ? -27.365 -65.355 17.636  1.000 157.696 ? 152 GLU BBB N   1 
ATOM   2654  C CA  . GLU B 2 153 ? -27.531 -64.123 16.830  1.000 157.363 ? 152 GLU BBB CA  1 
ATOM   2655  C C   . GLU B 2 153 ? -27.064 -62.896 17.617  1.000 159.763 ? 152 GLU BBB C   1 
ATOM   2656  O O   . GLU B 2 153 ? -27.035 -62.931 18.844  1.000 161.748 ? 152 GLU BBB O   1 
ATOM   2657  C CB  . GLU B 2 153 ? -29.015 -63.996 16.490  1.000 157.165 ? 152 GLU BBB CB  1 
ATOM   2658  C CG  . GLU B 2 153 ? -29.430 -64.734 15.238  1.000 154.328 ? 152 GLU BBB CG  1 
ATOM   2659  C CD  . GLU B 2 153 ? -29.844 -63.807 14.110  1.000 153.794 ? 152 GLU BBB CD  1 
ATOM   2660  O OE1 . GLU B 2 153 ? -28.948 -63.207 13.478  1.000 153.549 ? 152 GLU BBB OE1 1 
ATOM   2661  O OE2 . GLU B 2 153 ? -31.066 -63.658 13.893  1.000 154.082 ? 152 GLU BBB OE2 1 
ATOM   2662  N N   . PRO B 2 154 ? -26.744 -61.754 16.964  1.000 160.005 ? 153 PRO BBB N   1 
ATOM   2663  C CA  . PRO B 2 154 ? -26.720 -61.631 15.506  1.000 157.897 ? 153 PRO BBB CA  1 
ATOM   2664  C C   . PRO B 2 154 ? -25.325 -61.506 14.872  1.000 156.920 ? 153 PRO BBB C   1 
ATOM   2665  O O   . PRO B 2 154 ? -24.355 -61.392 15.609  1.000 157.294 ? 153 PRO BBB O   1 
ATOM   2666  C CB  . PRO B 2 154 ? -27.459 -60.293 15.347  1.000 159.961 ? 153 PRO BBB CB  1 
ATOM   2667  C CG  . PRO B 2 154 ? -27.009 -59.466 16.553  1.000 163.829 ? 153 PRO BBB CG  1 
ATOM   2668  C CD  . PRO B 2 154 ? -26.527 -60.450 17.605  1.000 163.634 ? 153 PRO BBB CD  1 
ATOM   2669  N N   . VAL B 2 155 ? -25.274 -61.487 13.532  1.000 155.094 ? 154 VAL BBB N   1 
ATOM   2670  C CA  . VAL B 2 155 ? -24.050 -61.235 12.708  1.000 155.296 ? 154 VAL BBB CA  1 
ATOM   2671  C C   . VAL B 2 155 ? -24.313 -60.034 11.799  1.000 154.856 ? 154 VAL BBB C   1 
ATOM   2672  O O   . VAL B 2 155 ? -25.485 -59.845 11.408  1.000 152.007 ? 154 VAL BBB O   1 
ATOM   2673  C CB  . VAL B 2 155 ? -23.635 -62.454 11.862  1.000 154.885 ? 154 VAL BBB CB  1 
ATOM   2674  C CG1 . VAL B 2 155 ? -23.153 -63.600 12.733  1.000 156.756 ? 154 VAL BBB CG1 1 
ATOM   2675  C CG2 . VAL B 2 155 ? -24.743 -62.917 10.925  1.000 153.428 ? 154 VAL BBB CG2 1 
ATOM   2676  N N   . THR B 2 156 ? -23.247 -59.291 11.470  1.000 157.165 ? 155 THR BBB N   1 
ATOM   2677  C CA  . THR B 2 156 ? -23.240 -58.080 10.599  1.000 158.842 ? 155 THR BBB CA  1 
ATOM   2678  C C   . THR B 2 156 ? -22.218 -58.260 9.469   1.000 156.382 ? 155 THR BBB C   1 
ATOM   2679  O O   . THR B 2 156 ? -21.127 -58.795 9.738   1.000 155.340 ? 155 THR BBB O   1 
ATOM   2680  C CB  . THR B 2 156 ? -22.908 -56.805 11.393  1.000 163.978 ? 155 THR BBB CB  1 
ATOM   2681  O OG1 . THR B 2 156 ? -21.567 -56.905 11.870  1.000 165.790 ? 155 THR BBB OG1 1 
ATOM   2682  C CG2 . THR B 2 156 ? -23.827 -56.559 12.571  1.000 165.783 ? 155 THR BBB CG2 1 
ATOM   2683  N N   . VAL B 2 157 ? -22.553 -57.797 8.263   1.000 155.473 ? 156 VAL BBB N   1 
ATOM   2684  C CA  . VAL B 2 157 ? -21.745 -57.985 7.022   1.000 155.577 ? 156 VAL BBB CA  1 
ATOM   2685  C C   . VAL B 2 157 ? -21.556 -56.631 6.331   1.000 157.836 ? 156 VAL BBB C   1 
ATOM   2686  O O   . VAL B 2 157 ? -22.494 -55.822 6.373   1.000 160.188 ? 156 VAL BBB O   1 
ATOM   2687  C CB  . VAL B 2 157 ? -22.432 -58.976 6.068   1.000 154.182 ? 156 VAL BBB CB  1 
ATOM   2688  C CG1 . VAL B 2 157 ? -21.497 -59.417 4.955   1.000 155.480 ? 156 VAL BBB CG1 1 
ATOM   2689  C CG2 . VAL B 2 157 ? -22.996 -60.184 6.801   1.000 153.080 ? 156 VAL BBB CG2 1 
ATOM   2690  N N   . SER B 2 158 ? -20.403 -56.410 5.692   1.000 158.895 ? 157 SER BBB N   1 
ATOM   2691  C CA  . SER B 2 158 ? -20.137 -55.253 4.792   1.000 161.219 ? 157 SER BBB CA  1 
ATOM   2692  C C   . SER B 2 158 ? -19.249 -55.707 3.624   1.000 160.934 ? 157 SER BBB C   1 
ATOM   2693  O O   . SER B 2 158 ? -18.666 -56.802 3.723   1.000 159.340 ? 157 SER BBB O   1 
ATOM   2694  C CB  . SER B 2 158 ? -19.549 -54.076 5.547   1.000 164.699 ? 157 SER BBB CB  1 
ATOM   2695  O OG  . SER B 2 158 ? -18.194 -54.302 5.902   1.000 165.972 ? 157 SER BBB OG  1 
ATOM   2696  N N   . TRP B 2 159 ? -19.170 -54.913 2.551   1.000 162.450 ? 158 TRP BBB N   1 
ATOM   2697  C CA  . TRP B 2 159 ? -18.525 -55.308 1.272   1.000 162.706 ? 158 TRP BBB CA  1 
ATOM   2698  C C   . TRP B 2 159 ? -17.426 -54.314 0.886   1.000 165.978 ? 158 TRP BBB C   1 
ATOM   2699  O O   . TRP B 2 159 ? -17.703 -53.101 0.881   1.000 167.762 ? 158 TRP BBB O   1 
ATOM   2700  C CB  . TRP B 2 159 ? -19.585 -55.448 0.177   1.000 162.225 ? 158 TRP BBB CB  1 
ATOM   2701  C CG  . TRP B 2 159 ? -20.410 -56.690 0.308   1.000 159.024 ? 158 TRP BBB CG  1 
ATOM   2702  C CD1 . TRP B 2 159 ? -21.619 -56.821 0.924   1.000 157.034 ? 158 TRP BBB CD1 1 
ATOM   2703  C CD2 . TRP B 2 159 ? -20.069 -57.997 -0.183  1.000 158.107 ? 158 TRP BBB CD2 1 
ATOM   2704  N NE1 . TRP B 2 159 ? -22.064 -58.112 0.835   1.000 153.736 ? 158 TRP BBB NE1 1 
ATOM   2705  C CE2 . TRP B 2 159 ? -21.130 -58.859 0.169   1.000 155.016 ? 158 TRP BBB CE2 1 
ATOM   2706  C CE3 . TRP B 2 159 ? -18.978 -58.519 -0.886  1.000 160.218 ? 158 TRP BBB CE3 1 
ATOM   2707  C CZ2 . TRP B 2 159 ? -21.126 -60.211 -0.162  1.000 154.353 ? 158 TRP BBB CZ2 1 
ATOM   2708  C CZ3 . TRP B 2 159 ? -18.976 -59.856 -1.214  1.000 159.362 ? 158 TRP BBB CZ3 1 
ATOM   2709  C CH2 . TRP B 2 159 ? -20.038 -60.687 -0.858  1.000 156.413 ? 158 TRP BBB CH2 1 
ATOM   2710  N N   . ASN B 2 160 ? -16.240 -54.838 0.554   1.000 166.689 ? 159 ASN BBB N   1 
ATOM   2711  C CA  . ASN B 2 160 ? -14.994 -54.083 0.241   1.000 170.892 ? 159 ASN BBB CA  1 
ATOM   2712  C C   . ASN B 2 160 ? -14.661 -53.164 1.425   1.000 172.262 ? 159 ASN BBB C   1 
ATOM   2713  O O   . ASN B 2 160 ? -14.242 -52.021 1.185   1.000 174.092 ? 159 ASN BBB O   1 
ATOM   2714  C CB  . ASN B 2 160 ? -15.102 -53.331 -1.090  1.000 174.121 ? 159 ASN BBB CB  1 
ATOM   2715  C CG  . ASN B 2 160 ? -14.903 -54.218 -2.303  1.000 173.981 ? 159 ASN BBB CG  1 
ATOM   2716  O OD1 . ASN B 2 160 ? -15.382 -55.348 -2.342  1.000 170.443 ? 159 ASN BBB OD1 1 
ATOM   2717  N ND2 . ASN B 2 160 ? -14.219 -53.708 -3.314  1.000 178.041 ? 159 ASN BBB ND2 1 
ATOM   2718  N N   . SER B 2 161 ? -14.845 -53.661 2.654   1.000 171.122 ? 160 SER BBB N   1 
ATOM   2719  C CA  . SER B 2 161 ? -14.618 -52.939 3.935   1.000 173.874 ? 160 SER BBB CA  1 
ATOM   2720  C C   . SER B 2 161 ? -15.870 -52.153 4.350   1.000 173.660 ? 160 SER BBB C   1 
ATOM   2721  O O   . SER B 2 161 ? -15.966 -51.793 5.537   1.000 176.579 ? 160 SER BBB O   1 
ATOM   2722  C CB  . SER B 2 161 ? -13.403 -52.058 3.862   1.000 178.511 ? 160 SER BBB CB  1 
ATOM   2723  O OG  . SER B 2 161 ? -12.850 -51.873 5.159   1.000 180.739 ? 160 SER BBB OG  1 
ATOM   2724  N N   . GLY B 2 162 ? -16.807 -51.928 3.424   1.000 170.901 ? 161 GLY BBB N   1 
ATOM   2725  C CA  . GLY B 2 162 ? -18.035 -51.145 3.659   1.000 171.017 ? 161 GLY BBB CA  1 
ATOM   2726  C C   . GLY B 2 162 ? -18.237 -50.067 2.607   1.000 174.432 ? 161 GLY BBB C   1 
ATOM   2727  O O   . GLY B 2 162 ? -19.263 -49.370 2.688   1.000 174.126 ? 161 GLY BBB O   1 
ATOM   2728  N N   . ALA B 2 163 ? -17.305 -49.937 1.654   1.000 178.325 ? 162 ALA BBB N   1 
ATOM   2729  C CA  . ALA B 2 163 ? -17.368 -48.999 0.506   1.000 182.386 ? 162 ALA BBB CA  1 
ATOM   2730  C C   . ALA B 2 163 ? -17.928 -49.724 -0.729  1.000 180.754 ? 162 ALA BBB C   1 
ATOM   2731  O O   . ALA B 2 163 ? -17.284 -49.687 -1.808  1.000 179.449 ? 162 ALA BBB O   1 
ATOM   2732  C CB  . ALA B 2 163 ? -16.002 -48.410 0.246   1.000 186.721 ? 162 ALA BBB CB  1 
ATOM   2733  N N   . LEU B 2 164 ? -19.085 -50.373 -0.562  1.000 180.397 ? 163 LEU BBB N   1 
ATOM   2734  C CA  . LEU B 2 164 ? -19.920 -50.931 -1.658  1.000 180.745 ? 163 LEU BBB CA  1 
ATOM   2735  C C   . LEU B 2 164 ? -21.264 -51.409 -1.087  1.000 177.693 ? 163 LEU BBB C   1 
ATOM   2736  O O   . LEU B 2 164 ? -21.389 -52.612 -0.783  1.000 171.938 ? 163 LEU BBB O   1 
ATOM   2737  C CB  . LEU B 2 164 ? -19.176 -52.063 -2.377  1.000 180.581 ? 163 LEU BBB CB  1 
ATOM   2738  C CG  . LEU B 2 164 ? -19.666 -52.334 -3.802  1.000 181.066 ? 163 LEU BBB CG  1 
ATOM   2739  C CD1 . LEU B 2 164 ? -18.911 -51.476 -4.818  1.000 184.330 ? 163 LEU BBB CD1 1 
ATOM   2740  C CD2 . LEU B 2 164 ? -19.557 -53.814 -4.137  1.000 178.116 ? 163 LEU BBB CD2 1 
ATOM   2741  N N   . THR B 2 165 ? -22.217 -50.476 -0.956  1.000 180.170 ? 164 THR BBB N   1 
ATOM   2742  C CA  . THR B 2 165 ? -23.646 -50.703 -0.597  1.000 177.949 ? 164 THR BBB CA  1 
ATOM   2743  C C   . THR B 2 165 ? -24.526 -50.581 -1.847  1.000 177.790 ? 164 THR BBB C   1 
ATOM   2744  O O   . THR B 2 165 ? -25.762 -50.725 -1.720  1.000 175.956 ? 164 THR BBB O   1 
ATOM   2745  C CB  . THR B 2 165 ? -24.127 -49.694 0.451   1.000 180.377 ? 164 THR BBB CB  1 
ATOM   2746  O OG1 . THR B 2 165 ? -24.016 -48.385 -0.114  1.000 184.199 ? 164 THR BBB OG1 1 
ATOM   2747  C CG2 . THR B 2 165 ? -23.354 -49.786 1.749   1.000 180.333 ? 164 THR BBB CG2 1 
ATOM   2748  N N   . SER B 2 166 ? -23.902 -50.309 -2.996  1.000 178.535 ? 165 SER BBB N   1 
ATOM   2749  C CA  . SER B 2 166 ? -24.519 -50.244 -4.344  1.000 177.442 ? 165 SER BBB CA  1 
ATOM   2750  C C   . SER B 2 166 ? -25.283 -51.551 -4.637  1.000 172.688 ? 165 SER BBB C   1 
ATOM   2751  O O   . SER B 2 166 ? -24.708 -52.438 -5.303  1.000 169.232 ? 165 SER BBB O   1 
ATOM   2752  C CB  . SER B 2 166 ? -23.445 -49.939 -5.386  1.000 178.608 ? 165 SER BBB CB  1 
ATOM   2753  O OG  . SER B 2 166 ? -22.518 -48.956 -4.923  1.000 178.506 ? 165 SER BBB OG  1 
ATOM   2754  N N   . GLY B 2 167 ? -26.515 -51.672 -4.112  1.000 170.355 ? 166 GLY BBB N   1 
ATOM   2755  C CA  . GLY B 2 167 ? -27.498 -52.730 -4.433  1.000 168.189 ? 166 GLY BBB CA  1 
ATOM   2756  C C   . GLY B 2 167 ? -27.237 -54.040 -3.705  1.000 164.966 ? 166 GLY BBB C   1 
ATOM   2757  O O   . GLY B 2 167 ? -27.143 -55.083 -4.402  1.000 162.170 ? 166 GLY BBB O   1 
ATOM   2758  N N   . VAL B 2 168 ? -27.165 -54.010 -2.365  1.000 165.419 ? 167 VAL BBB N   1 
ATOM   2759  C CA  . VAL B 2 168 ? -26.744 -55.174 -1.518  1.000 163.614 ? 167 VAL BBB CA  1 
ATOM   2760  C C   . VAL B 2 168 ? -27.880 -55.608 -0.583  1.000 162.426 ? 167 VAL BBB C   1 
ATOM   2761  O O   . VAL B 2 168 ? -28.294 -54.795 0.254   1.000 163.787 ? 167 VAL BBB O   1 
ATOM   2762  C CB  . VAL B 2 168 ? -25.478 -54.861 -0.697  1.000 164.183 ? 167 VAL BBB CB  1 
ATOM   2763  C CG1 . VAL B 2 168 ? -24.888 -56.123 -0.080  1.000 161.041 ? 167 VAL BBB CG1 1 
ATOM   2764  C CG2 . VAL B 2 168 ? -24.428 -54.140 -1.525  1.000 167.587 ? 167 VAL BBB CG2 1 
ATOM   2765  N N   . HIS B 2 169 ? -28.316 -56.866 -0.707  1.000 161.601 ? 168 HIS BBB N   1 
ATOM   2766  C CA  . HIS B 2 169 ? -29.369 -57.510 0.122   1.000 161.339 ? 168 HIS BBB CA  1 
ATOM   2767  C C   . HIS B 2 169 ? -28.716 -58.544 1.047   1.000 158.494 ? 168 HIS BBB C   1 
ATOM   2768  O O   . HIS B 2 169 ? -28.036 -59.458 0.536   1.000 154.974 ? 168 HIS BBB O   1 
ATOM   2769  C CB  . HIS B 2 169 ? -30.434 -58.178 -0.761  1.000 163.493 ? 168 HIS BBB CB  1 
ATOM   2770  C CG  . HIS B 2 169 ? -30.952 -57.343 -1.889  1.000 169.190 ? 168 HIS BBB CG  1 
ATOM   2771  N ND1 . HIS B 2 169 ? -30.142 -56.882 -2.922  1.000 172.861 ? 168 HIS BBB ND1 1 
ATOM   2772  C CD2 . HIS B 2 169 ? -32.204 -56.933 -2.192  1.000 172.332 ? 168 HIS BBB CD2 1 
ATOM   2773  C CE1 . HIS B 2 169 ? -30.869 -56.200 -3.788  1.000 174.515 ? 168 HIS BBB CE1 1 
ATOM   2774  N NE2 . HIS B 2 169 ? -32.139 -56.220 -3.365  1.000 174.825 ? 168 HIS BBB NE2 1 
ATOM   2775  N N   . THR B 2 170 ? -28.927 -58.410 2.358   1.000 160.009 ? 169 THR BBB N   1 
ATOM   2776  C CA  . THR B 2 170 ? -28.437 -59.351 3.404   1.000 159.630 ? 169 THR BBB CA  1 
ATOM   2777  C C   . THR B 2 170 ? -29.634 -59.904 4.185   1.000 157.274 ? 169 THR BBB C   1 
ATOM   2778  O O   . THR B 2 170 ? -30.286 -59.123 4.906   1.000 158.509 ? 169 THR BBB O   1 
ATOM   2779  C CB  . THR B 2 170 ? -27.401 -58.664 4.298   1.000 163.319 ? 169 THR BBB CB  1 
ATOM   2780  O OG1 . THR B 2 170 ? -26.217 -58.590 3.502   1.000 166.396 ? 169 THR BBB OG1 1 
ATOM   2781  C CG2 . THR B 2 170 ? -27.129 -59.392 5.597   1.000 162.850 ? 169 THR BBB CG2 1 
ATOM   2782  N N   . PHE B 2 171 ? -29.872 -61.211 4.060   1.000 153.737 ? 170 PHE BBB N   1 
ATOM   2783  C CA  . PHE B 2 171 ? -31.144 -61.889 4.415   1.000 152.435 ? 170 PHE BBB CA  1 
ATOM   2784  C C   . PHE B 2 171 ? -31.237 -62.106 5.917   1.000 151.093 ? 170 PHE BBB C   1 
ATOM   2785  O O   . PHE B 2 171 ? -30.230 -62.064 6.622   1.000 150.450 ? 170 PHE BBB O   1 
ATOM   2786  C CB  . PHE B 2 171 ? -31.261 -63.219 3.668   1.000 151.958 ? 170 PHE BBB CB  1 
ATOM   2787  C CG  . PHE B 2 171 ? -31.324 -63.035 2.179   1.000 153.444 ? 170 PHE BBB CG  1 
ATOM   2788  C CD1 . PHE B 2 171 ? -32.516 -62.679 1.570   1.000 155.716 ? 170 PHE BBB CD1 1 
ATOM   2789  C CD2 . PHE B 2 171 ? -30.183 -63.152 1.400   1.000 153.609 ? 170 PHE BBB CD2 1 
ATOM   2790  C CE1 . PHE B 2 171 ? -32.572 -62.470 0.202   1.000 157.628 ? 170 PHE BBB CE1 1 
ATOM   2791  C CE2 . PHE B 2 171 ? -30.243 -62.943 0.032   1.000 155.526 ? 170 PHE BBB CE2 1 
ATOM   2792  C CZ  . PHE B 2 171 ? -31.438 -62.608 -0.563  1.000 157.369 ? 170 PHE BBB CZ  1 
ATOM   2793  N N   . PRO B 2 172 ? -32.465 -62.331 6.435   1.000 151.606 ? 171 PRO BBB N   1 
ATOM   2794  C CA  . PRO B 2 172 ? -32.654 -62.795 7.807   1.000 151.928 ? 171 PRO BBB CA  1 
ATOM   2795  C C   . PRO B 2 172 ? -31.875 -64.089 8.065   1.000 149.355 ? 171 PRO BBB C   1 
ATOM   2796  O O   . PRO B 2 172 ? -31.729 -64.867 7.151   1.000 149.075 ? 171 PRO BBB O   1 
ATOM   2797  C CB  . PRO B 2 172 ? -34.162 -63.076 7.904   1.000 153.636 ? 171 PRO BBB CB  1 
ATOM   2798  C CG  . PRO B 2 172 ? -34.790 -62.237 6.810   1.000 154.931 ? 171 PRO BBB CG  1 
ATOM   2799  C CD  . PRO B 2 172 ? -33.739 -62.130 5.727   1.000 153.382 ? 171 PRO BBB CD  1 
ATOM   2800  N N   . ALA B 2 173 ? -31.396 -64.290 9.290   1.000 149.461 ? 172 ALA BBB N   1 
ATOM   2801  C CA  . ALA B 2 173 ? -30.786 -65.567 9.721   1.000 149.145 ? 172 ALA BBB CA  1 
ATOM   2802  C C   . ALA B 2 173 ? -31.890 -66.619 9.795   1.000 149.406 ? 172 ALA BBB C   1 
ATOM   2803  O O   . ALA B 2 173 ? -33.042 -66.254 10.091  1.000 148.238 ? 172 ALA BBB O   1 
ATOM   2804  C CB  . ALA B 2 173 ? -30.090 -65.408 11.047  1.000 151.615 ? 172 ALA BBB CB  1 
ATOM   2805  N N   . VAL B 2 174 ? -31.543 -67.870 9.508   1.000 151.688 ? 173 VAL BBB N   1 
ATOM   2806  C CA  . VAL B 2 174 ? -32.458 -69.038 9.640   1.000 155.851 ? 173 VAL BBB CA  1 
ATOM   2807  C C   . VAL B 2 174 ? -31.737 -70.072 10.506  1.000 157.416 ? 173 VAL BBB C   1 
ATOM   2808  O O   . VAL B 2 174 ? -30.540 -70.304 10.267  1.000 158.238 ? 173 VAL BBB O   1 
ATOM   2809  C CB  . VAL B 2 174 ? -32.883 -69.592 8.264   1.000 156.326 ? 173 VAL BBB CB  1 
ATOM   2810  C CG1 . VAL B 2 174 ? -33.864 -68.657 7.569   1.000 157.551 ? 173 VAL BBB CG1 1 
ATOM   2811  C CG2 . VAL B 2 174 ? -31.699 -69.892 7.351   1.000 154.257 ? 173 VAL BBB CG2 1 
ATOM   2812  N N   . LEU B 2 175 ? -32.425 -70.620 11.508  1.000 159.229 ? 174 LEU BBB N   1 
ATOM   2813  C CA  . LEU B 2 175 ? -31.851 -71.615 12.449  1.000 159.763 ? 174 LEU BBB CA  1 
ATOM   2814  C C   . LEU B 2 175 ? -31.905 -73.002 11.797  1.000 158.170 ? 174 LEU BBB C   1 
ATOM   2815  O O   . LEU B 2 175 ? -33.008 -73.571 11.699  1.000 159.223 ? 174 LEU BBB O   1 
ATOM   2816  C CB  . LEU B 2 175 ? -32.635 -71.557 13.765  1.000 162.945 ? 174 LEU BBB CB  1 
ATOM   2817  C CG  . LEU B 2 175 ? -32.277 -72.623 14.800  1.000 165.020 ? 174 LEU BBB CG  1 
ATOM   2818  C CD1 . LEU B 2 175 ? -30.827 -72.500 15.222  1.000 165.123 ? 174 LEU BBB CD1 1 
ATOM   2819  C CD2 . LEU B 2 175 ? -33.178 -72.530 16.020  1.000 168.065 ? 174 LEU BBB CD2 1 
ATOM   2820  N N   . GLN B 2 176 ? -30.759 -73.508 11.329  1.000 155.552 ? 175 GLN BBB N   1 
ATOM   2821  C CA  . GLN B 2 176 ? -30.627 -74.861 10.727  1.000 155.916 ? 175 GLN BBB CA  1 
ATOM   2822  C C   . GLN B 2 176 ? -31.092 -75.914 11.737  1.000 158.172 ? 175 GLN BBB C   1 
ATOM   2823  O O   . GLN B 2 176 ? -31.187 -75.584 12.938  1.000 159.681 ? 175 GLN BBB O   1 
ATOM   2824  C CB  . GLN B 2 176 ? -29.174 -75.143 10.340  1.000 155.566 ? 175 GLN BBB CB  1 
ATOM   2825  C CG  . GLN B 2 176 ? -28.743 -74.485 9.039   1.000 153.365 ? 175 GLN BBB CG  1 
ATOM   2826  C CD  . GLN B 2 176 ? -27.245 -74.333 8.973   1.000 152.174 ? 175 GLN BBB CD  1 
ATOM   2827  O OE1 . GLN B 2 176 ? -26.572 -74.941 8.144   1.000 152.049 ? 175 GLN BBB OE1 1 
ATOM   2828  N NE2 . GLN B 2 176 ? -26.712 -73.521 9.870   1.000 150.583 ? 175 GLN BBB NE2 1 
ATOM   2829  N N   . SER B 2 177 ? -31.348 -77.136 11.260  1.000 159.538 ? 176 SER BBB N   1 
ATOM   2830  C CA  . SER B 2 177 ? -31.560 -78.357 12.085  1.000 161.658 ? 176 SER BBB CA  1 
ATOM   2831  C C   . SER B 2 177 ? -30.464 -78.449 13.156  1.000 160.668 ? 176 SER BBB C   1 
ATOM   2832  O O   . SER B 2 177 ? -30.792 -78.755 14.326  1.000 161.576 ? 176 SER BBB O   1 
ATOM   2833  C CB  . SER B 2 177 ? -31.590 -79.593 11.213  1.000 163.414 ? 176 SER BBB CB  1 
ATOM   2834  O OG  . SER B 2 177 ? -30.528 -79.572 10.269  1.000 162.033 ? 176 SER BBB OG  1 
ATOM   2835  N N   . SER B 2 178 ? -29.221 -78.141 12.768  1.000 158.262 ? 177 SER BBB N   1 
ATOM   2836  C CA  . SER B 2 178 ? -28.003 -78.193 13.620  1.000 158.136 ? 177 SER BBB CA  1 
ATOM   2837  C C   . SER B 2 178 ? -28.215 -77.451 14.948  1.000 157.574 ? 177 SER BBB C   1 
ATOM   2838  O O   . SER B 2 178 ? -27.474 -77.751 15.897  1.000 159.359 ? 177 SER BBB O   1 
ATOM   2839  C CB  . SER B 2 178 ? -26.796 -77.666 12.871  1.000 157.247 ? 177 SER BBB CB  1 
ATOM   2840  O OG  . SER B 2 178 ? -27.021 -76.367 12.340  1.000 154.575 ? 177 SER BBB OG  1 
ATOM   2841  N N   . GLY B 2 179 ? -29.171 -76.516 15.012  1.000 156.561 ? 178 GLY BBB N   1 
ATOM   2842  C CA  . GLY B 2 179 ? -29.443 -75.688 16.205  1.000 157.509 ? 178 GLY BBB CA  1 
ATOM   2843  C C   . GLY B 2 179 ? -28.539 -74.464 16.252  1.000 156.195 ? 178 GLY BBB C   1 
ATOM   2844  O O   . GLY B 2 179 ? -28.500 -73.796 17.310  1.000 155.725 ? 178 GLY BBB O   1 
ATOM   2845  N N   . LEU B 2 180 ? -27.857 -74.190 15.129  1.000 155.168 ? 179 LEU BBB N   1 
ATOM   2846  C CA  . LEU B 2 180 ? -27.029 -72.981 14.865  1.000 154.484 ? 179 LEU BBB CA  1 
ATOM   2847  C C   . LEU B 2 180 ? -27.572 -72.250 13.626  1.000 154.186 ? 179 LEU BBB C   1 
ATOM   2848  O O   . LEU B 2 180 ? -27.989 -72.936 12.662  1.000 154.125 ? 179 LEU BBB O   1 
ATOM   2849  C CB  . LEU B 2 180 ? -25.576 -73.399 14.620  1.000 152.949 ? 179 LEU BBB CB  1 
ATOM   2850  C CG  . LEU B 2 180 ? -25.024 -74.521 15.496  1.000 154.333 ? 179 LEU BBB CG  1 
ATOM   2851  C CD1 . LEU B 2 180 ? -23.573 -74.779 15.133  1.000 154.532 ? 179 LEU BBB CD1 1 
ATOM   2852  C CD2 . LEU B 2 180 ? -25.149 -74.196 16.978  1.000 156.808 ? 179 LEU BBB CD2 1 
ATOM   2853  N N   . TYR B 2 181 ? -27.508 -70.913 13.630  1.000 154.445 ? 180 TYR BBB N   1 
ATOM   2854  C CA  . TYR B 2 181 ? -28.056 -70.026 12.567  1.000 152.769 ? 180 TYR BBB CA  1 
ATOM   2855  C C   . TYR B 2 181 ? -27.149 -70.030 11.327  1.000 151.661 ? 180 TYR BBB C   1 
ATOM   2856  O O   . TYR B 2 181 ? -25.943 -70.294 11.440  1.000 151.680 ? 180 TYR BBB O   1 
ATOM   2857  C CB  . TYR B 2 181 ? -28.224 -68.597 13.088  1.000 152.785 ? 180 TYR BBB CB  1 
ATOM   2858  C CG  . TYR B 2 181 ? -29.231 -68.438 14.198  1.000 154.400 ? 180 TYR BBB CG  1 
ATOM   2859  C CD1 . TYR B 2 181 ? -30.593 -68.536 13.957  1.000 153.679 ? 180 TYR BBB CD1 1 
ATOM   2860  C CD2 . TYR B 2 181 ? -28.817 -68.169 15.493  1.000 157.489 ? 180 TYR BBB CD2 1 
ATOM   2861  C CE1 . TYR B 2 181 ? -31.518 -68.385 14.978  1.000 156.107 ? 180 TYR BBB CE1 1 
ATOM   2862  C CE2 . TYR B 2 181 ? -29.729 -68.003 16.523  1.000 160.060 ? 180 TYR BBB CE2 1 
ATOM   2863  C CZ  . TYR B 2 181 ? -31.084 -68.119 16.266  1.000 159.581 ? 180 TYR BBB CZ  1 
ATOM   2864  O OH  . TYR B 2 181 ? -31.975 -67.959 17.289  1.000 162.902 ? 180 TYR BBB OH  1 
ATOM   2865  N N   . SER B 2 182 ? -27.742 -69.739 10.165  1.000 151.712 ? 181 SER BBB N   1 
ATOM   2866  C CA  . SER B 2 182 ? -27.055 -69.452 8.876   1.000 152.090 ? 181 SER BBB CA  1 
ATOM   2867  C C   . SER B 2 182 ? -27.753 -68.275 8.186   1.000 151.533 ? 181 SER BBB C   1 
ATOM   2868  O O   . SER B 2 182 ? -28.960 -68.061 8.423   1.000 150.908 ? 181 SER BBB O   1 
ATOM   2869  C CB  . SER B 2 182 ? -27.006 -70.668 7.984   1.000 153.424 ? 181 SER BBB CB  1 
ATOM   2870  O OG  . SER B 2 182 ? -26.637 -70.318 6.655   1.000 153.089 ? 181 SER BBB OG  1 
ATOM   2871  N N   . LEU B 2 183 ? -27.017 -67.552 7.347   1.000 151.281 ? 182 LEU BBB N   1 
ATOM   2872  C CA  . LEU B 2 183 ? -27.441 -66.233 6.825   1.000 151.711 ? 182 LEU BBB CA  1 
ATOM   2873  C C   . LEU B 2 183 ? -26.594 -65.893 5.601   1.000 150.090 ? 182 LEU BBB C   1 
ATOM   2874  O O   . LEU B 2 183 ? -25.359 -65.909 5.721   1.000 150.280 ? 182 LEU BBB O   1 
ATOM   2875  C CB  . LEU B 2 183 ? -27.260 -65.219 7.958   1.000 154.791 ? 182 LEU BBB CB  1 
ATOM   2876  C CG  . LEU B 2 183 ? -27.414 -63.748 7.580   1.000 157.857 ? 182 LEU BBB CG  1 
ATOM   2877  C CD1 . LEU B 2 183 ? -27.867 -62.929 8.789   1.000 160.057 ? 182 LEU BBB CD1 1 
ATOM   2878  C CD2 . LEU B 2 183 ? -26.116 -63.190 7.005   1.000 158.248 ? 182 LEU BBB CD2 1 
ATOM   2879  N N   . SER B 2 184 ? -27.252 -65.615 4.475   1.000 149.935 ? 183 SER BBB N   1 
ATOM   2880  C CA  . SER B 2 184 ? -26.625 -65.304 3.166   1.000 151.931 ? 183 SER BBB CA  1 
ATOM   2881  C C   . SER B 2 184 ? -26.628 -63.784 2.960   1.000 153.636 ? 183 SER BBB C   1 
ATOM   2882  O O   . SER B 2 184 ? -27.554 -63.128 3.468   1.000 156.864 ? 183 SER BBB O   1 
ATOM   2883  C CB  . SER B 2 184 ? -27.344 -66.021 2.042   1.000 152.660 ? 183 SER BBB CB  1 
ATOM   2884  O OG  . SER B 2 184 ? -27.710 -67.347 2.413   1.000 151.801 ? 183 SER BBB OG  1 
ATOM   2885  N N   . SER B 2 185 ? -25.616 -63.252 2.262   1.000 153.174 ? 184 SER BBB N   1 
ATOM   2886  C CA  . SER B 2 185 ? -25.488 -61.824 1.856   1.000 152.397 ? 184 SER BBB CA  1 
ATOM   2887  C C   . SER B 2 185 ? -24.944 -61.748 0.430   1.000 153.635 ? 184 SER BBB C   1 
ATOM   2888  O O   . SER B 2 185 ? -23.919 -62.400 0.169   1.000 154.908 ? 184 SER BBB O   1 
ATOM   2889  C CB  . SER B 2 185 ? -24.593 -61.059 2.785   1.000 152.239 ? 184 SER BBB CB  1 
ATOM   2890  O OG  . SER B 2 185 ? -24.267 -59.800 2.216   1.000 151.120 ? 184 SER BBB OG  1 
ATOM   2891  N N   . VAL B 2 186 ? -25.578 -60.956 -0.437  1.000 155.681 ? 185 VAL BBB N   1 
ATOM   2892  C CA  . VAL B 2 186 ? -25.314 -60.951 -1.909  1.000 157.026 ? 185 VAL BBB CA  1 
ATOM   2893  C C   . VAL B 2 186 ? -25.371 -59.509 -2.440  1.000 158.393 ? 185 VAL BBB C   1 
ATOM   2894  O O   . VAL B 2 186 ? -26.048 -58.668 -1.801  1.000 161.895 ? 185 VAL BBB O   1 
ATOM   2895  C CB  . VAL B 2 186 ? -26.317 -61.874 -2.629  1.000 156.944 ? 185 VAL BBB CB  1 
ATOM   2896  C CG1 . VAL B 2 186 ? -26.094 -63.340 -2.277  1.000 155.795 ? 185 VAL BBB CG1 1 
ATOM   2897  C CG2 . VAL B 2 186 ? -27.758 -61.479 -2.338  1.000 157.372 ? 185 VAL BBB CG2 1 
ATOM   2898  N N   . VAL B 2 187 ? -24.688 -59.234 -3.559  1.000 157.645 ? 186 VAL BBB N   1 
ATOM   2899  C CA  . VAL B 2 187 ? -24.609 -57.885 -4.204  1.000 159.219 ? 186 VAL BBB CA  1 
ATOM   2900  C C   . VAL B 2 187 ? -24.712 -58.043 -5.728  1.000 160.043 ? 186 VAL BBB C   1 
ATOM   2901  O O   . VAL B 2 187 ? -24.037 -58.934 -6.281  1.000 160.737 ? 186 VAL BBB O   1 
ATOM   2902  C CB  . VAL B 2 187 ? -23.315 -57.145 -3.806  1.000 161.650 ? 186 VAL BBB CB  1 
ATOM   2903  C CG1 . VAL B 2 187 ? -22.074 -58.007 -3.978  1.000 161.216 ? 186 VAL BBB CG1 1 
ATOM   2904  C CG2 . VAL B 2 187 ? -23.149 -55.837 -4.569  1.000 165.948 ? 186 VAL BBB CG2 1 
ATOM   2905  N N   . THR B 2 188 ? -25.525 -57.204 -6.376  1.000 160.606 ? 187 THR BBB N   1 
ATOM   2906  C CA  . THR B 2 188 ? -25.708 -57.161 -7.851  1.000 161.879 ? 187 THR BBB CA  1 
ATOM   2907  C C   . THR B 2 188 ? -24.574 -56.320 -8.449  1.000 165.200 ? 187 THR BBB C   1 
ATOM   2908  O O   . THR B 2 188 ? -24.389 -55.175 -7.979  1.000 166.958 ? 187 THR BBB O   1 
ATOM   2909  C CB  . THR B 2 188 ? -27.090 -56.602 -8.225  1.000 162.139 ? 187 THR BBB CB  1 
ATOM   2910  O OG1 . THR B 2 188 ? -28.007 -56.805 -7.148  1.000 157.639 ? 187 THR BBB OG1 1 
ATOM   2911  C CG2 . THR B 2 188 ? -27.646 -57.227 -9.485  1.000 163.813 ? 187 THR BBB CG2 1 
ATOM   2912  N N   . VAL B 2 189 ? -23.842 -56.864 -9.429  1.000 167.252 ? 188 VAL BBB N   1 
ATOM   2913  C CA  . VAL B 2 189 ? -22.666 -56.194 -10.070 1.000 170.455 ? 188 VAL BBB CA  1 
ATOM   2914  C C   . VAL B 2 189 ? -22.747 -56.365 -11.586 1.000 175.460 ? 188 VAL BBB C   1 
ATOM   2915  O O   . VAL B 2 189 ? -23.192 -57.407 -12.063 1.000 177.535 ? 188 VAL BBB O   1 
ATOM   2916  C CB  . VAL B 2 189 ? -21.334 -56.734 -9.514  1.000 168.394 ? 188 VAL BBB CB  1 
ATOM   2917  C CG1 . VAL B 2 189 ? -21.186 -56.434 -8.034  1.000 165.609 ? 188 VAL BBB CG1 1 
ATOM   2918  C CG2 . VAL B 2 189 ? -21.147 -58.217 -9.780  1.000 167.723 ? 188 VAL BBB CG2 1 
ATOM   2919  N N   . PRO B 2 190 ? -22.352 -55.344 -12.386 1.000 179.110 ? 189 PRO BBB N   1 
ATOM   2920  C CA  . PRO B 2 190 ? -22.301 -55.475 -13.845 1.000 182.980 ? 189 PRO BBB CA  1 
ATOM   2921  C C   . PRO B 2 190 ? -21.442 -56.665 -14.305 1.000 183.664 ? 189 PRO BBB C   1 
ATOM   2922  O O   . PRO B 2 190 ? -20.403 -56.890 -13.723 1.000 183.045 ? 189 PRO BBB O   1 
ATOM   2923  C CB  . PRO B 2 190 ? -21.685 -54.151 -14.324 1.000 186.126 ? 189 PRO BBB CB  1 
ATOM   2924  C CG  . PRO B 2 190 ? -21.993 -53.171 -13.212 1.000 184.582 ? 189 PRO BBB CG  1 
ATOM   2925  C CD  . PRO B 2 190 ? -21.992 -53.990 -11.938 1.000 179.674 ? 189 PRO BBB CD  1 
ATOM   2926  N N   . SER B 2 191 ? -21.911 -57.388 -15.327 1.000 184.881 ? 190 SER BBB N   1 
ATOM   2927  C CA  . SER B 2 191 ? -21.287 -58.626 -15.866 1.000 184.887 ? 190 SER BBB CA  1 
ATOM   2928  C C   . SER B 2 191 ? -19.758 -58.538 -15.770 1.000 184.029 ? 190 SER BBB C   1 
ATOM   2929  O O   . SER B 2 191 ? -19.170 -59.306 -14.987 1.000 182.736 ? 190 SER BBB O   1 
ATOM   2930  C CB  . SER B 2 191 ? -21.753 -58.907 -17.279 1.000 188.992 ? 190 SER BBB CB  1 
ATOM   2931  O OG  . SER B 2 191 ? -22.919 -59.718 -17.260 1.000 188.933 ? 190 SER BBB OG  1 
ATOM   2932  N N   . SER B 2 192 ? -19.149 -57.597 -16.492 1.000 184.785 ? 191 SER BBB N   1 
ATOM   2933  C CA  . SER B 2 192 ? -17.684 -57.538 -16.748 1.000 186.171 ? 191 SER BBB CA  1 
ATOM   2934  C C   . SER B 2 192 ? -16.918 -56.914 -15.572 1.000 184.368 ? 191 SER BBB C   1 
ATOM   2935  O O   . SER B 2 192 ? -15.731 -56.600 -15.756 1.000 184.634 ? 191 SER BBB O   1 
ATOM   2936  C CB  . SER B 2 192 ? -17.427 -56.788 -18.020 1.000 191.129 ? 191 SER BBB CB  1 
ATOM   2937  O OG  . SER B 2 192 ? -18.087 -55.532 -17.987 1.000 191.484 ? 191 SER BBB OG  1 
ATOM   2938  N N   . SER B 2 193 ? -17.559 -56.746 -14.410 1.000 182.622 ? 192 SER BBB N   1 
ATOM   2939  C CA  . SER B 2 193 ? -16.936 -56.211 -13.168 1.000 182.294 ? 192 SER BBB CA  1 
ATOM   2940  C C   . SER B 2 193 ? -15.966 -57.240 -12.579 1.000 182.823 ? 192 SER BBB C   1 
ATOM   2941  O O   . SER B 2 193 ? -14.922 -56.814 -12.060 1.000 183.054 ? 192 SER BBB O   1 
ATOM   2942  C CB  . SER B 2 193 ? -17.980 -55.832 -12.151 1.000 178.309 ? 192 SER BBB CB  1 
ATOM   2943  O OG  . SER B 2 193 ? -18.998 -55.033 -12.732 1.000 178.504 ? 192 SER BBB OG  1 
ATOM   2944  N N   . LEU B 2 194 ? -16.312 -58.533 -12.666 1.000 183.472 ? 193 LEU BBB N   1 
ATOM   2945  C CA  . LEU B 2 194 ? -15.593 -59.671 -12.018 1.000 183.305 ? 193 LEU BBB CA  1 
ATOM   2946  C C   . LEU B 2 194 ? -14.149 -59.737 -12.530 1.000 187.411 ? 193 LEU BBB C   1 
ATOM   2947  O O   . LEU B 2 194 ? -13.237 -60.031 -11.719 1.000 186.698 ? 193 LEU BBB O   1 
ATOM   2948  C CB  . LEU B 2 194 ? -16.302 -60.995 -12.334 1.000 182.870 ? 193 LEU BBB CB  1 
ATOM   2949  C CG  . LEU B 2 194 ? -17.828 -61.007 -12.241 1.000 181.803 ? 193 LEU BBB CG  1 
ATOM   2950  C CD1 . LEU B 2 194 ? -18.385 -62.326 -12.769 1.000 182.354 ? 193 LEU BBB CD1 1 
ATOM   2951  C CD2 . LEU B 2 194 ? -18.276 -60.753 -10.808 1.000 178.676 ? 193 LEU BBB CD2 1 
ATOM   2952  N N   . GLY B 2 195 ? -13.971 -59.469 -13.830 1.000 191.950 ? 194 GLY BBB N   1 
ATOM   2953  C CA  . GLY B 2 195 ? -12.709 -59.608 -14.579 1.000 197.401 ? 194 GLY BBB CA  1 
ATOM   2954  C C   . GLY B 2 195 ? -11.535 -58.923 -13.900 1.000 200.874 ? 194 GLY BBB C   1 
ATOM   2955  O O   . GLY B 2 195 ? -10.393 -59.341 -14.173 1.000 203.976 ? 194 GLY BBB O   1 
ATOM   2956  N N   . THR B 2 196 ? -11.791 -57.893 -13.078 1.000 202.065 ? 195 THR BBB N   1 
ATOM   2957  C CA  . THR B 2 196 ? -10.769 -57.147 -12.290 1.000 204.712 ? 195 THR BBB CA  1 
ATOM   2958  C C   . THR B 2 196 ? -11.288 -56.867 -10.870 1.000 199.360 ? 195 THR BBB C   1 
ATOM   2959  O O   . THR B 2 196 ? -10.808 -57.526 -9.927  1.000 197.633 ? 195 THR BBB O   1 
ATOM   2960  C CB  . THR B 2 196 ? -10.374 -55.835 -12.986 1.000 210.669 ? 195 THR BBB CB  1 
ATOM   2961  O OG1 . THR B 2 196 ? -11.566 -55.090 -13.239 1.000 210.871 ? 195 THR BBB OG1 1 
ATOM   2962  C CG2 . THR B 2 196 ? -9.628  -56.040 -14.289 1.000 215.461 ? 195 THR BBB CG2 1 
ATOM   2963  N N   . GLN B 2 197 ? -12.237 -55.931 -10.734 1.000 196.331 ? 196 GLN BBB N   1 
ATOM   2964  C CA  . GLN B 2 197 ? -12.693 -55.345 -9.441  1.000 192.319 ? 196 GLN BBB CA  1 
ATOM   2965  C C   . GLN B 2 197 ? -12.798 -56.441 -8.376  1.000 187.017 ? 196 GLN BBB C   1 
ATOM   2966  O O   . GLN B 2 197 ? -13.581 -57.388 -8.579  1.000 183.651 ? 196 GLN BBB O   1 
ATOM   2967  C CB  . GLN B 2 197 ? -14.036 -54.628 -9.612  1.000 191.683 ? 196 GLN BBB CB  1 
ATOM   2968  C CG  . GLN B 2 197 ? -14.647 -54.112 -8.310  1.000 190.430 ? 196 GLN BBB CG  1 
ATOM   2969  C CD  . GLN B 2 197 ? -13.789 -53.092 -7.593  1.000 194.393 ? 196 GLN BBB CD  1 
ATOM   2970  O OE1 . GLN B 2 197 ? -12.950 -52.413 -8.189  1.000 198.837 ? 196 GLN BBB OE1 1 
ATOM   2971  N NE2 . GLN B 2 197 ? -14.009 -52.955 -6.292  1.000 193.498 ? 196 GLN BBB NE2 1 
ATOM   2972  N N   . THR B 2 198 ? -12.027 -56.302 -7.295  1.000 186.104 ? 197 THR BBB N   1 
ATOM   2973  C CA  . THR B 2 198 ? -12.093 -57.145 -6.073  1.000 181.666 ? 197 THR BBB CA  1 
ATOM   2974  C C   . THR B 2 198 ? -13.469 -57.008 -5.411  1.000 177.993 ? 197 THR BBB C   1 
ATOM   2975  O O   . THR B 2 198 ? -14.056 -55.911 -5.470  1.000 177.753 ? 197 THR BBB O   1 
ATOM   2976  C CB  . THR B 2 198 ? -11.027 -56.757 -5.040  1.000 182.271 ? 197 THR BBB CB  1 
ATOM   2977  O OG1 . THR B 2 198 ? -9.759  -56.697 -5.688  1.000 185.945 ? 197 THR BBB OG1 1 
ATOM   2978  C CG2 . THR B 2 198 ? -10.961 -57.734 -3.886  1.000 179.792 ? 197 THR BBB CG2 1 
ATOM   2979  N N   . TYR B 2 199 ? -13.949 -58.100 -4.816  1.000 174.485 ? 198 TYR BBB N   1 
ATOM   2980  C CA  . TYR B 2 199 ? -15.155 -58.149 -3.956  1.000 171.310 ? 198 TYR BBB CA  1 
ATOM   2981  C C   . TYR B 2 199 ? -14.823 -59.002 -2.729  1.000 169.215 ? 198 TYR BBB C   1 
ATOM   2982  O O   . TYR B 2 199 ? -14.906 -60.238 -2.807  1.000 167.956 ? 198 TYR BBB O   1 
ATOM   2983  C CB  . TYR B 2 199 ? -16.369 -58.652 -4.742  1.000 170.216 ? 198 TYR BBB CB  1 
ATOM   2984  C CG  . TYR B 2 199 ? -16.828 -57.707 -5.821  1.000 172.707 ? 198 TYR BBB CG  1 
ATOM   2985  C CD1 . TYR B 2 199 ? -17.545 -56.559 -5.517  1.000 173.409 ? 198 TYR BBB CD1 1 
ATOM   2986  C CD2 . TYR B 2 199 ? -16.526 -57.950 -7.152  1.000 175.185 ? 198 TYR BBB CD2 1 
ATOM   2987  C CE1 . TYR B 2 199 ? -17.952 -55.683 -6.510  1.000 176.414 ? 198 TYR BBB CE1 1 
ATOM   2988  C CE2 . TYR B 2 199 ? -16.932 -57.087 -8.156  1.000 177.940 ? 198 TYR BBB CE2 1 
ATOM   2989  C CZ  . TYR B 2 199 ? -17.642 -55.945 -7.832  1.000 178.544 ? 198 TYR BBB CZ  1 
ATOM   2990  O OH  . TYR B 2 199 ? -18.046 -55.080 -8.804  1.000 182.035 ? 198 TYR BBB OH  1 
ATOM   2991  N N   . ILE B 2 200 ? -14.400 -58.339 -1.650  1.000 169.664 ? 199 ILE BBB N   1 
ATOM   2992  C CA  . ILE B 2 200 ? -14.237 -58.924 -0.286  1.000 168.134 ? 199 ILE BBB CA  1 
ATOM   2993  C C   . ILE B 2 200 ? -15.542 -58.682 0.479   1.000 165.616 ? 199 ILE BBB C   1 
ATOM   2994  O O   . ILE B 2 200 ? -16.184 -57.654 0.217   1.000 165.482 ? 199 ILE BBB O   1 
ATOM   2995  C CB  . ILE B 2 200 ? -13.016 -58.302 0.429   1.000 170.747 ? 199 ILE BBB CB  1 
ATOM   2996  C CG1 . ILE B 2 200 ? -11.694 -58.796 -0.169  1.000 172.724 ? 199 ILE BBB CG1 1 
ATOM   2997  C CG2 . ILE B 2 200 ? -13.077 -58.544 1.930   1.000 170.093 ? 199 ILE BBB CG2 1 
ATOM   2998  C CD1 . ILE B 2 200 ? -10.471 -58.027 0.297   1.000 175.904 ? 199 ILE BBB CD1 1 
ATOM   2999  N N   . CYS B 2 201 ? -15.914 -59.584 1.388   1.000 164.313 ? 200 CYS BBB N   1 
ATOM   3000  C CA  . CYS B 2 201 ? -17.023 -59.376 2.356   1.000 164.864 ? 200 CYS BBB CA  1 
ATOM   3001  C C   . CYS B 2 201 ? -16.460 -59.472 3.782   1.000 165.856 ? 200 CYS BBB C   1 
ATOM   3002  O O   . CYS B 2 201 ? -15.687 -60.412 4.050   1.000 166.325 ? 200 CYS BBB O   1 
ATOM   3003  C CB  . CYS B 2 201 ? -18.177 -60.336 2.079   1.000 164.034 ? 200 CYS BBB CB  1 
ATOM   3004  S SG  . CYS B 2 201 ? -18.321 -61.745 3.212   1.000 165.029 ? 200 CYS BBB SG  1 
ATOM   3005  N N   . ASN B 2 202 ? -16.801 -58.498 4.636   1.000 167.752 ? 201 ASN BBB N   1 
ATOM   3006  C CA  . ASN B 2 202 ? -16.315 -58.355 6.037   1.000 170.567 ? 201 ASN BBB CA  1 
ATOM   3007  C C   . ASN B 2 202 ? -17.447 -58.759 6.994   1.000 168.610 ? 201 ASN BBB C   1 
ATOM   3008  O O   . ASN B 2 202 ? -18.516 -58.112 6.944   1.000 166.935 ? 201 ASN BBB O   1 
ATOM   3009  C CB  . ASN B 2 202 ? -15.814 -56.932 6.322   1.000 174.615 ? 201 ASN BBB CB  1 
ATOM   3010  C CG  . ASN B 2 202 ? -14.969 -56.344 5.208   1.000 176.777 ? 201 ASN BBB CG  1 
ATOM   3011  O OD1 . ASN B 2 202 ? -15.475 -56.004 4.140   1.000 177.096 ? 201 ASN BBB OD1 1 
ATOM   3012  N ND2 . ASN B 2 202 ? -13.685 -56.178 5.464   1.000 179.353 ? 201 ASN BBB ND2 1 
ATOM   3013  N N   . VAL B 2 203 ? -17.225 -59.786 7.823   1.000 168.915 ? 202 VAL BBB N   1 
ATOM   3014  C CA  . VAL B 2 203 ? -18.278 -60.431 8.664   1.000 168.810 ? 202 VAL BBB CA  1 
ATOM   3015  C C   . VAL B 2 203 ? -17.842 -60.408 10.130  1.000 171.284 ? 202 VAL BBB C   1 
ATOM   3016  O O   . VAL B 2 203 ? -16.784 -60.989 10.426  1.000 171.422 ? 202 VAL BBB O   1 
ATOM   3017  C CB  . VAL B 2 203 ? -18.557 -61.876 8.209   1.000 167.864 ? 202 VAL BBB CB  1 
ATOM   3018  C CG1 . VAL B 2 203 ? -19.669 -62.520 9.028   1.000 166.817 ? 202 VAL BBB CG1 1 
ATOM   3019  C CG2 . VAL B 2 203 ? -18.879 -61.947 6.723   1.000 166.718 ? 202 VAL BBB CG2 1 
ATOM   3020  N N   . ASN B 2 204 ? -18.662 -59.815 11.009  1.000 174.274 ? 203 ASN BBB N   1 
ATOM   3021  C CA  . ASN B 2 204 ? -18.395 -59.666 12.469  1.000 177.000 ? 203 ASN BBB CA  1 
ATOM   3022  C C   . ASN B 2 204 ? -19.488 -60.383 13.277  1.000 173.554 ? 203 ASN BBB C   1 
ATOM   3023  O O   . ASN B 2 204 ? -20.678 -60.193 12.968  1.000 171.190 ? 203 ASN BBB O   1 
ATOM   3024  C CB  . ASN B 2 204 ? -18.292 -58.195 12.885  1.000 182.252 ? 203 ASN BBB CB  1 
ATOM   3025  C CG  . ASN B 2 204 ? -17.402 -57.378 11.970  1.000 185.931 ? 203 ASN BBB CG  1 
ATOM   3026  O OD1 . ASN B 2 204 ? -16.468 -57.900 11.364  1.000 188.355 ? 203 ASN BBB OD1 1 
ATOM   3027  N ND2 . ASN B 2 204 ? -17.682 -56.089 11.861  1.000 187.965 ? 203 ASN BBB ND2 1 
ATOM   3028  N N   . HIS B 2 205 ? -19.080 -61.189 14.262  1.000 172.339 ? 204 HIS BBB N   1 
ATOM   3029  C CA  . HIS B 2 205 ? -19.956 -61.869 15.255  1.000 171.687 ? 204 HIS BBB CA  1 
ATOM   3030  C C   . HIS B 2 205 ? -19.522 -61.398 16.640  1.000 176.133 ? 204 HIS BBB C   1 
ATOM   3031  O O   . HIS B 2 205 ? -18.384 -61.732 17.033  1.000 178.193 ? 204 HIS BBB O   1 
ATOM   3032  C CB  . HIS B 2 205 ? -19.865 -63.396 15.115  1.000 169.023 ? 204 HIS BBB CB  1 
ATOM   3033  C CG  . HIS B 2 205 ? -20.842 -64.168 15.946  1.000 166.978 ? 204 HIS BBB CG  1 
ATOM   3034  N ND1 . HIS B 2 205 ? -20.477 -65.290 16.664  1.000 166.430 ? 204 HIS BBB ND1 1 
ATOM   3035  C CD2 . HIS B 2 205 ? -22.166 -64.013 16.156  1.000 165.292 ? 204 HIS BBB CD2 1 
ATOM   3036  C CE1 . HIS B 2 205 ? -21.528 -65.779 17.291  1.000 165.248 ? 204 HIS BBB CE1 1 
ATOM   3037  N NE2 . HIS B 2 205 ? -22.576 -65.016 16.995  1.000 164.488 ? 204 HIS BBB NE2 1 
ATOM   3038  N N   . LYS B 2 206 ? -20.370 -60.629 17.324  1.000 179.024 ? 205 LYS BBB N   1 
ATOM   3039  C CA  . LYS B 2 206 ? -20.007 -59.961 18.602  1.000 185.070 ? 205 LYS BBB CA  1 
ATOM   3040  C C   . LYS B 2 206 ? -19.732 -61.034 19.657  1.000 185.665 ? 205 LYS BBB C   1 
ATOM   3041  O O   . LYS B 2 206 ? -18.635 -61.079 20.213  1.000 188.553 ? 205 LYS BBB O   1 
ATOM   3042  C CB  . LYS B 2 206 ? -21.079 -58.951 19.031  1.000 188.117 ? 205 LYS BBB CB  1 
ATOM   3043  C CG  . LYS B 2 206 ? -21.602 -58.051 17.919  1.000 187.946 ? 205 LYS BBB CG  1 
ATOM   3044  C CD  . LYS B 2 206 ? -22.326 -56.818 18.418  1.000 191.137 ? 205 LYS BBB CD  1 
ATOM   3045  C CE  . LYS B 2 206 ? -21.388 -55.725 18.891  1.000 196.332 ? 205 LYS BBB CE  1 
ATOM   3046  N NZ  . LYS B 2 206 ? -22.112 -54.466 19.187  1.000 199.631 ? 205 LYS BBB NZ  1 
ATOM   3047  N N   . PRO B 2 207 ? -20.683 -61.959 19.933  1.000 182.761 ? 206 PRO BBB N   1 
ATOM   3048  C CA  . PRO B 2 207 ? -20.516 -62.935 21.013  1.000 183.571 ? 206 PRO BBB CA  1 
ATOM   3049  C C   . PRO B 2 207 ? -19.182 -63.701 20.995  1.000 182.940 ? 206 PRO BBB C   1 
ATOM   3050  O O   . PRO B 2 207 ? -18.647 -63.941 22.065  1.000 188.250 ? 206 PRO BBB O   1 
ATOM   3051  C CB  . PRO B 2 207 ? -21.692 -63.899 20.797  1.000 181.018 ? 206 PRO BBB CB  1 
ATOM   3052  C CG  . PRO B 2 207 ? -22.749 -63.049 20.130  1.000 179.936 ? 206 PRO BBB CG  1 
ATOM   3053  C CD  . PRO B 2 207 ? -21.968 -62.115 19.232  1.000 179.970 ? 206 PRO BBB CD  1 
ATOM   3054  N N   . SER B 2 208 ? -18.673 -64.048 19.807  1.000 178.057 ? 207 SER BBB N   1 
ATOM   3055  C CA  . SER B 2 208 ? -17.427 -64.839 19.615  1.000 178.212 ? 207 SER BBB CA  1 
ATOM   3056  C C   . SER B 2 208 ? -16.249 -63.937 19.212  1.000 179.058 ? 207 SER BBB C   1 
ATOM   3057  O O   . SER B 2 208 ? -15.176 -64.495 18.891  1.000 180.850 ? 207 SER BBB O   1 
ATOM   3058  C CB  . SER B 2 208 ? -17.636 -65.955 18.616  1.000 174.999 ? 207 SER BBB CB  1 
ATOM   3059  O OG  . SER B 2 208 ? -17.781 -65.460 17.289  1.000 172.110 ? 207 SER BBB OG  1 
ATOM   3060  N N   . ASN B 2 209 ? -16.425 -62.608 19.239  1.000 177.860 ? 208 ASN BBB N   1 
ATOM   3061  C CA  . ASN B 2 209 ? -15.352 -61.606 18.986  1.000 179.624 ? 208 ASN BBB CA  1 
ATOM   3062  C C   . ASN B 2 209 ? -14.478 -62.096 17.816  1.000 177.793 ? 208 ASN BBB C   1 
ATOM   3063  O O   . ASN B 2 209 ? -13.248 -62.199 18.011  1.000 178.650 ? 208 ASN BBB O   1 
ATOM   3064  C CB  . ASN B 2 209 ? -14.550 -61.352 20.274  1.000 184.958 ? 208 ASN BBB CB  1 
ATOM   3065  C CG  . ASN B 2 209 ? -14.071 -59.927 20.476  1.000 189.284 ? 208 ASN BBB CG  1 
ATOM   3066  O OD1 . ASN B 2 209 ? -14.701 -58.973 20.027  1.000 189.061 ? 208 ASN BBB OD1 1 
ATOM   3067  N ND2 . ASN B 2 209 ? -12.980 -59.772 21.210  1.000 193.805 ? 208 ASN BBB ND2 1 
ATOM   3068  N N   . THR B 2 210 ? -15.092 -62.416 16.661  1.000 175.095 ? 209 THR BBB N   1 
ATOM   3069  C CA  . THR B 2 210 ? -14.409 -62.825 15.394  1.000 173.340 ? 209 THR BBB CA  1 
ATOM   3070  C C   . THR B 2 210 ? -14.932 -62.023 14.194  1.000 171.510 ? 209 THR BBB C   1 
ATOM   3071  O O   . THR B 2 210 ? -16.136 -62.127 13.896  1.000 166.222 ? 209 THR BBB O   1 
ATOM   3072  C CB  . THR B 2 210 ? -14.582 -64.319 15.079  1.000 170.043 ? 209 THR BBB CB  1 
ATOM   3073  O OG1 . THR B 2 210 ? -15.927 -64.708 15.368  1.000 166.389 ? 209 THR BBB OG1 1 
ATOM   3074  C CG2 . THR B 2 210 ? -13.604 -65.190 15.838  1.000 172.828 ? 209 THR BBB CG2 1 
ATOM   3075  N N   . LYS B 2 211 ? -14.045 -61.264 13.541  1.000 175.809 ? 210 LYS BBB N   1 
ATOM   3076  C CA  . LYS B 2 211 ? -14.234 -60.669 12.188  1.000 177.117 ? 210 LYS BBB CA  1 
ATOM   3077  C C   . LYS B 2 211 ? -13.792 -61.726 11.167  1.000 176.789 ? 210 LYS BBB C   1 
ATOM   3078  O O   . LYS B 2 211 ? -13.125 -62.693 11.593  1.000 177.409 ? 210 LYS BBB O   1 
ATOM   3079  C CB  . LYS B 2 211 ? -13.442 -59.356 12.065  1.000 181.963 ? 210 LYS BBB CB  1 
ATOM   3080  C CG  . LYS B 2 211 ? -13.406 -58.695 10.683  1.000 182.047 ? 210 LYS BBB CG  1 
ATOM   3081  C CD  . LYS B 2 211 ? -13.212 -57.179 10.701  1.000 185.672 ? 210 LYS BBB CD  1 
ATOM   3082  C CE  . LYS B 2 211 ? -11.906 -56.709 11.318  1.000 190.234 ? 210 LYS BBB CE  1 
ATOM   3083  N NZ  . LYS B 2 211 ? -10.777 -56.734 10.358  1.000 191.223 ? 210 LYS BBB NZ  1 
ATOM   3084  N N   . VAL B 2 212 ? -14.186 -61.574 9.894   1.000 175.393 ? 211 VAL BBB N   1 
ATOM   3085  C CA  . VAL B 2 212 ? -13.657 -62.367 8.742   1.000 173.867 ? 211 VAL BBB CA  1 
ATOM   3086  C C   . VAL B 2 212 ? -13.663 -61.482 7.490   1.000 173.954 ? 211 VAL BBB C   1 
ATOM   3087  O O   . VAL B 2 212 ? -14.760 -61.026 7.096   1.000 173.343 ? 211 VAL BBB O   1 
ATOM   3088  C CB  . VAL B 2 212 ? -14.476 -63.648 8.497   1.000 171.482 ? 211 VAL BBB CB  1 
ATOM   3089  C CG1 . VAL B 2 212 ? -13.855 -64.502 7.402   1.000 172.396 ? 211 VAL BBB CG1 1 
ATOM   3090  C CG2 . VAL B 2 212 ? -14.666 -64.465 9.763   1.000 171.730 ? 211 VAL BBB CG2 1 
ATOM   3091  N N   . ASP B 2 213 ? -12.487 -61.269 6.890   1.000 175.660 ? 212 ASP BBB N   1 
ATOM   3092  C CA  . ASP B 2 213 ? -12.310 -60.582 5.581   1.000 175.986 ? 212 ASP BBB CA  1 
ATOM   3093  C C   . ASP B 2 213 ? -12.160 -61.661 4.500   1.000 174.828 ? 212 ASP BBB C   1 
ATOM   3094  O O   . ASP B 2 213 ? -11.006 -62.041 4.196   1.000 176.353 ? 212 ASP BBB O   1 
ATOM   3095  C CB  . ASP B 2 213 ? -11.115 -59.622 5.603   1.000 180.003 ? 212 ASP BBB CB  1 
ATOM   3096  C CG  . ASP B 2 213 ? -11.270 -58.435 6.542   1.000 181.965 ? 212 ASP BBB CG  1 
ATOM   3097  O OD1 . ASP B 2 213 ? -12.357 -58.287 7.146   1.000 179.634 ? 212 ASP BBB OD1 1 
ATOM   3098  O OD2 . ASP B 2 213 ? -10.296 -57.659 6.662   1.000 186.078 ? 212 ASP BBB OD2 1 
ATOM   3099  N N   . LYS B 2 214 ? -13.287 -62.135 3.952   1.000 172.421 ? 213 LYS BBB N   1 
ATOM   3100  C CA  . LYS B 2 214 ? -13.345 -63.284 3.007   1.000 170.670 ? 213 LYS BBB CA  1 
ATOM   3101  C C   . LYS B 2 214 ? -13.481 -62.785 1.563   1.000 169.109 ? 213 LYS BBB C   1 
ATOM   3102  O O   . LYS B 2 214 ? -14.573 -62.288 1.195   1.000 165.017 ? 213 LYS BBB O   1 
ATOM   3103  C CB  . LYS B 2 214 ? -14.505 -64.221 3.358   1.000 169.255 ? 213 LYS BBB CB  1 
ATOM   3104  C CG  . LYS B 2 214 ? -14.546 -65.508 2.550   1.000 169.954 ? 213 LYS BBB CG  1 
ATOM   3105  C CD  . LYS B 2 214 ? -13.222 -66.237 2.515   1.000 173.876 ? 213 LYS BBB CD  1 
ATOM   3106  C CE  . LYS B 2 214 ? -13.281 -67.493 1.676   1.000 175.822 ? 213 LYS BBB CE  1 
ATOM   3107  N NZ  . LYS B 2 214 ? -11.928 -67.998 1.344   1.000 180.353 ? 213 LYS BBB NZ  1 
ATOM   3108  N N   . LYS B 2 215 ? -12.404 -62.937 0.785   1.000 170.917 ? 214 LYS BBB N   1 
ATOM   3109  C CA  . LYS B 2 215 ? -12.334 -62.599 -0.662  1.000 172.051 ? 214 LYS BBB CA  1 
ATOM   3110  C C   . LYS B 2 215 ? -13.256 -63.561 -1.427  1.000 168.993 ? 214 LYS BBB C   1 
ATOM   3111  O O   . LYS B 2 215 ? -13.234 -64.772 -1.136  1.000 168.197 ? 214 LYS BBB O   1 
ATOM   3112  C CB  . LYS B 2 215 ? -10.873 -62.648 -1.132  1.000 176.586 ? 214 LYS BBB CB  1 
ATOM   3113  C CG  . LYS B 2 215 ? -10.638 -62.759 -2.636  1.000 178.854 ? 214 LYS BBB CG  1 
ATOM   3114  C CD  . LYS B 2 215 ? -10.217 -61.479 -3.326  1.000 181.543 ? 214 LYS BBB CD  1 
ATOM   3115  C CE  . LYS B 2 215 ? -9.785  -61.729 -4.758  1.000 183.958 ? 214 LYS BBB CE  1 
ATOM   3116  N NZ  . LYS B 2 215 ? -9.589  -60.471 -5.518  1.000 186.497 ? 214 LYS BBB NZ  1 
ATOM   3117  N N   . VAL B 2 216 ? -14.048 -63.020 -2.354  1.000 166.557 ? 215 VAL BBB N   1 
ATOM   3118  C CA  . VAL B 2 216 ? -14.920 -63.776 -3.301  1.000 163.660 ? 215 VAL BBB CA  1 
ATOM   3119  C C   . VAL B 2 216 ? -14.349 -63.567 -4.705  1.000 166.160 ? 215 VAL BBB C   1 
ATOM   3120  O O   . VAL B 2 216 ? -13.816 -62.475 -4.959  1.000 167.889 ? 215 VAL BBB O   1 
ATOM   3121  C CB  . VAL B 2 216 ? -16.379 -63.292 -3.214  1.000 161.055 ? 215 VAL BBB CB  1 
ATOM   3122  C CG1 . VAL B 2 216 ? -17.313 -64.130 -4.073  1.000 161.187 ? 215 VAL BBB CG1 1 
ATOM   3123  C CG2 . VAL B 2 216 ? -16.876 -63.237 -1.779  1.000 158.997 ? 215 VAL BBB CG2 1 
ATOM   3124  N N   . GLU B 2 217 ? -14.449 -64.571 -5.577  1.000 167.509 ? 216 GLU BBB N   1 
ATOM   3125  C CA  . GLU B 2 217 ? -13.942 -64.489 -6.974  1.000 171.846 ? 216 GLU BBB CA  1 
ATOM   3126  C C   . GLU B 2 217 ? -14.558 -65.610 -7.808  1.000 172.138 ? 216 GLU BBB C   1 
ATOM   3127  O O   . GLU B 2 217 ? -15.015 -66.608 -7.259  1.000 173.064 ? 216 GLU BBB O   1 
ATOM   3128  C CB  . GLU B 2 217 ? -12.409 -64.525 -6.986  1.000 176.147 ? 216 GLU BBB CB  1 
ATOM   3129  C CG  . GLU B 2 217 ? -11.798 -65.626 -6.133  1.000 176.397 ? 216 GLU BBB CG  1 
ATOM   3130  C CD  . GLU B 2 217 ? -10.280 -65.720 -6.192  1.000 180.824 ? 216 GLU BBB CD  1 
ATOM   3131  O OE1 . GLU B 2 217 ? -9.599  -64.723 -5.857  1.000 182.648 ? 216 GLU BBB OE1 1 
ATOM   3132  O OE2 . GLU B 2 217 ? -9.777  -66.792 -6.578  1.000 182.713 ? 216 GLU BBB OE2 1 
ATOM   3133  N N   . PRO B 2 218 ? -14.602 -65.482 -9.155  1.000 172.775 ? 217 PRO BBB N   1 
ATOM   3134  C CA  . PRO B 2 218 ? -15.120 -66.555 -10.010 1.000 172.971 ? 217 PRO BBB CA  1 
ATOM   3135  C C   . PRO B 2 218 ? -14.232 -67.812 -9.996  1.000 174.576 ? 217 PRO BBB C   1 
ATOM   3136  O O   . PRO B 2 218 ? -13.063 -67.701 -9.684  1.000 175.312 ? 217 PRO BBB O   1 
ATOM   3137  C CB  . PRO B 2 218 ? -15.161 -65.912 -11.403 1.000 176.109 ? 217 PRO BBB CB  1 
ATOM   3138  C CG  . PRO B 2 218 ? -14.113 -64.816 -11.339 1.000 177.704 ? 217 PRO BBB CG  1 
ATOM   3139  C CD  . PRO B 2 218 ? -14.172 -64.300 -9.919  1.000 174.248 ? 217 PRO BBB CD  1 
ATOM   3140  N N   . LYS B 2 219 ? -14.803 -68.966 -10.360 1.000 175.790 ? 218 LYS BBB N   1 
ATOM   3141  C CA  . LYS B 2 219 ? -14.146 -70.306 -10.329 1.000 180.316 ? 218 LYS BBB CA  1 
ATOM   3142  C C   . LYS B 2 219 ? -13.450 -70.599 -11.674 1.000 185.859 ? 218 LYS BBB C   1 
ATOM   3143  O O   . LYS B 2 219 ? -13.558 -69.762 -12.600 1.000 188.493 ? 218 LYS BBB O   1 
ATOM   3144  C CB  . LYS B 2 219 ? -15.211 -71.361 -10.004 1.000 180.061 ? 218 LYS BBB CB  1 
ATOM   3145  C CG  . LYS B 2 219 ? -14.714 -72.675 -9.407  1.000 182.581 ? 218 LYS BBB CG  1 
ATOM   3146  C CD  . LYS B 2 219 ? -15.661 -73.861 -9.605  1.000 183.168 ? 218 LYS BBB CD  1 
ATOM   3147  C CE  . LYS B 2 219 ? -17.055 -73.649 -9.043  1.000 179.037 ? 218 LYS BBB CE  1 
ATOM   3148  N NZ  . LYS B 2 219 ? -17.051 -73.417 -7.576  1.000 174.898 ? 218 LYS BBB NZ  1 
ATOM   3149  N N   . SER B 2 220 ? -12.719 -71.719 -11.758 1.000 187.942 ? 219 SER BBB N   1 
ATOM   3150  C CA  . SER B 2 220 ? -12.273 -72.363 -13.025 1.000 192.102 ? 219 SER BBB CA  1 
ATOM   3151  C C   . SER B 2 220 ? -12.440 -73.884 -12.911 1.000 192.519 ? 219 SER BBB C   1 
ATOM   3152  O O   . SER B 2 220 ? -13.168 -74.534 -13.666 1.000 192.182 ? 219 SER BBB O   1 
ATOM   3153  C CB  . SER B 2 220 ? -10.851 -72.000 -13.371 1.000 195.657 ? 219 SER BBB CB  1 
ATOM   3154  O OG  . SER B 2 220 ? -10.604 -72.235 -14.749 1.000 199.673 ? 219 SER BBB OG  1 
ATOM   3155  N N   . ASP C 3 1   ? -58.949 -59.245 33.744  1.000 156.120 ? 1   ASP CCC N   1 
ATOM   3156  C CA  . ASP C 3 1   ? -58.771 -60.654 33.284  1.000 158.796 ? 1   ASP CCC CA  1 
ATOM   3157  C C   . ASP C 3 1   ? -58.687 -60.723 31.745  1.000 157.855 ? 1   ASP CCC C   1 
ATOM   3158  O O   . ASP C 3 1   ? -58.813 -61.831 31.219  1.000 159.428 ? 1   ASP CCC O   1 
ATOM   3159  C CB  . ASP C 3 1   ? -59.930 -61.512 33.808  1.000 164.620 ? 1   ASP CCC CB  1 
ATOM   3160  C CG  . ASP C 3 1   ? -59.606 -62.988 33.905  1.000 168.908 ? 1   ASP CCC CG  1 
ATOM   3161  O OD1 . ASP C 3 1   ? -58.441 -63.342 33.642  1.000 167.453 ? 1   ASP CCC OD1 1 
ATOM   3162  O OD2 . ASP C 3 1   ? -60.518 -63.764 34.263  1.000 173.405 ? 1   ASP CCC OD2 1 
ATOM   3163  N N   . ILE C 3 2   ? -58.431 -59.588 31.063  1.000 156.052 ? 2   ILE CCC N   1 
ATOM   3164  C CA  . ILE C 3 2   ? -58.859 -59.254 29.661  1.000 154.818 ? 2   ILE CCC CA  1 
ATOM   3165  C C   . ILE C 3 2   ? -57.923 -59.894 28.629  1.000 153.506 ? 2   ILE CCC C   1 
ATOM   3166  O O   . ILE C 3 2   ? -56.772 -60.191 28.969  1.000 153.227 ? 2   ILE CCC O   1 
ATOM   3167  C CB  . ILE C 3 2   ? -58.931 -57.719 29.463  1.000 149.937 ? 2   ILE CCC CB  1 
ATOM   3168  C CG1 . ILE C 3 2   ? -59.904 -57.069 30.452  1.000 153.079 ? 2   ILE CCC CG1 1 
ATOM   3169  C CG2 . ILE C 3 2   ? -59.273 -57.350 28.024  1.000 147.181 ? 2   ILE CCC CG2 1 
ATOM   3170  C CD1 . ILE C 3 2   ? -59.901 -55.559 30.435  1.000 150.239 ? 2   ILE CCC CD1 1 
ATOM   3171  N N   . GLN C 3 3   ? -58.397 -60.049 27.389  1.000 154.677 ? 3   GLN CCC N   1 
ATOM   3172  C CA  . GLN C 3 3   ? -57.637 -60.691 26.288  1.000 156.262 ? 3   GLN CCC CA  1 
ATOM   3173  C C   . GLN C 3 3   ? -58.104 -60.141 24.935  1.000 156.620 ? 3   GLN CCC C   1 
ATOM   3174  O O   . GLN C 3 3   ? -59.325 -59.962 24.763  1.000 158.834 ? 3   GLN CCC O   1 
ATOM   3175  C CB  . GLN C 3 3   ? -57.853 -62.194 26.396  1.000 163.291 ? 3   GLN CCC CB  1 
ATOM   3176  C CG  . GLN C 3 3   ? -56.974 -63.020 25.475  1.000 164.836 ? 3   GLN CCC CG  1 
ATOM   3177  C CD  . GLN C 3 3   ? -57.537 -64.413 25.343  1.000 172.631 ? 3   GLN CCC CD  1 
ATOM   3178  O OE1 . GLN C 3 3   ? -58.272 -64.889 26.209  1.000 176.891 ? 3   GLN CCC OE1 1 
ATOM   3179  N NE2 . GLN C 3 3   ? -57.208 -65.075 24.244  1.000 175.535 ? 3   GLN CCC NE2 1 
ATOM   3180  N N   . LEU C 3 4   ? -57.161 -59.938 24.004  1.000 154.982 ? 4   LEU CCC N   1 
ATOM   3181  C CA  . LEU C 3 4   ? -57.370 -59.250 22.698  1.000 153.370 ? 4   LEU CCC CA  1 
ATOM   3182  C C   . LEU C 3 4   ? -57.037 -60.183 21.528  1.000 155.470 ? 4   LEU CCC C   1 
ATOM   3183  O O   . LEU C 3 4   ? -56.095 -60.992 21.661  1.000 156.438 ? 4   LEU CCC O   1 
ATOM   3184  C CB  . LEU C 3 4   ? -56.481 -58.002 22.637  1.000 147.505 ? 4   LEU CCC CB  1 
ATOM   3185  C CG  . LEU C 3 4   ? -56.877 -56.860 23.571  1.000 146.537 ? 4   LEU CCC CG  1 
ATOM   3186  C CD1 . LEU C 3 4   ? -55.980 -55.645 23.374  1.000 142.120 ? 4   LEU CCC CD1 1 
ATOM   3187  C CD2 . LEU C 3 4   ? -58.332 -56.465 23.378  1.000 149.214 ? 4   LEU CCC CD2 1 
ATOM   3188  N N   . THR C 3 5   ? -57.778 -60.034 20.420  1.000 156.043 ? 5   THR CCC N   1 
ATOM   3189  C CA  . THR C 3 5   ? -57.542 -60.683 19.099  1.000 155.435 ? 5   THR CCC CA  1 
ATOM   3190  C C   . THR C 3 5   ? -57.731 -59.628 17.996  1.000 151.004 ? 5   THR CCC C   1 
ATOM   3191  O O   . THR C 3 5   ? -58.856 -59.113 17.865  1.000 149.514 ? 5   THR CCC O   1 
ATOM   3192  C CB  . THR C 3 5   ? -58.482 -61.884 18.895  1.000 162.064 ? 5   THR CCC CB  1 
ATOM   3193  O OG1 . THR C 3 5   ? -58.959 -62.355 20.158  1.000 164.930 ? 5   THR CCC OG1 1 
ATOM   3194  C CG2 . THR C 3 5   ? -57.827 -63.020 18.138  1.000 164.107 ? 5   THR CCC CG2 1 
ATOM   3195  N N   . GLN C 3 6   ? -56.665 -59.298 17.257  1.000 147.973 ? 6   GLN CCC N   1 
ATOM   3196  C CA  . GLN C 3 6   ? -56.695 -58.389 16.076  1.000 147.919 ? 6   GLN CCC CA  1 
ATOM   3197  C C   . GLN C 3 6   ? -57.063 -59.204 14.834  1.000 152.704 ? 6   GLN CCC C   1 
ATOM   3198  O O   . GLN C 3 6   ? -56.984 -60.436 14.913  1.000 159.068 ? 6   GLN CCC O   1 
ATOM   3199  C CB  . GLN C 3 6   ? -55.336 -57.719 15.850  1.000 145.424 ? 6   GLN CCC CB  1 
ATOM   3200  C CG  . GLN C 3 6   ? -54.951 -56.719 16.934  1.000 143.156 ? 6   GLN CCC CG  1 
ATOM   3201  C CD  . GLN C 3 6   ? -53.559 -56.157 16.769  1.000 139.775 ? 6   GLN CCC CD  1 
ATOM   3202  O OE1 . GLN C 3 6   ? -52.659 -56.449 17.553  1.000 139.077 ? 6   GLN CCC OE1 1 
ATOM   3203  N NE2 . GLN C 3 6   ? -53.369 -55.335 15.748  1.000 138.981 ? 6   GLN CCC NE2 1 
ATOM   3204  N N   . SER C 3 7   ? -57.438 -58.540 13.737  1.000 153.666 ? 7   SER CCC N   1 
ATOM   3205  C CA  . SER C 3 7   ? -57.650 -59.151 12.395  1.000 157.914 ? 7   SER CCC CA  1 
ATOM   3206  C C   . SER C 3 7   ? -57.751 -58.045 11.346  1.000 156.935 ? 7   SER CCC C   1 
ATOM   3207  O O   . SER C 3 7   ? -58.330 -56.998 11.623  1.000 157.829 ? 7   SER CCC O   1 
ATOM   3208  C CB  . SER C 3 7   ? -58.866 -60.053 12.375  1.000 164.192 ? 7   SER CCC CB  1 
ATOM   3209  O OG  . SER C 3 7   ? -60.020 -59.377 12.850  1.000 165.545 ? 7   SER CCC OG  1 
ATOM   3210  N N   . PRO C 3 8   ? -57.186 -58.209 10.126  1.000 156.656 ? 8   PRO CCC N   1 
ATOM   3211  C CA  . PRO C 3 8   ? -56.483 -59.426 9.727   1.000 158.671 ? 8   PRO CCC CA  1 
ATOM   3212  C C   . PRO C 3 8   ? -55.043 -59.399 10.256  1.000 155.195 ? 8   PRO CCC C   1 
ATOM   3213  O O   . PRO C 3 8   ? -54.683 -58.420 10.873  1.000 152.281 ? 8   PRO CCC O   1 
ATOM   3214  C CB  . PRO C 3 8   ? -56.534 -59.337 8.195   1.000 161.470 ? 8   PRO CCC CB  1 
ATOM   3215  C CG  . PRO C 3 8   ? -56.434 -57.851 7.917   1.000 157.474 ? 8   PRO CCC CG  1 
ATOM   3216  C CD  . PRO C 3 8   ? -57.161 -57.187 9.067   1.000 155.854 ? 8   PRO CCC CD  1 
ATOM   3217  N N   . ASP C 3 9   ? -54.265 -60.456 9.999   1.000 157.387 ? 9   ASP CCC N   1 
ATOM   3218  C CA  . ASP C 3 9   ? -52.832 -60.572 10.391  1.000 154.483 ? 9   ASP CCC CA  1 
ATOM   3219  C C   . ASP C 3 9   ? -51.956 -59.790 9.397   1.000 150.945 ? 9   ASP CCC C   1 
ATOM   3220  O O   . ASP C 3 9   ? -50.980 -59.159 9.837   1.000 144.826 ? 9   ASP CCC O   1 
ATOM   3221  C CB  . ASP C 3 9   ? -52.423 -62.044 10.504  1.000 159.800 ? 9   ASP CCC CB  1 
ATOM   3222  C CG  . ASP C 3 9   ? -53.034 -62.772 11.694  1.000 162.959 ? 9   ASP CCC CG  1 
ATOM   3223  O OD1 . ASP C 3 9   ? -52.608 -62.488 12.839  1.000 159.265 ? 9   ASP CCC OD1 1 
ATOM   3224  O OD2 . ASP C 3 9   ? -53.927 -63.626 11.467  1.000 168.922 ? 9   ASP CCC OD2 1 
ATOM   3225  N N   . SER C 3 10  ? -52.296 -59.834 8.105   1.000 152.991 ? 10  SER CCC N   1 
ATOM   3226  C CA  . SER C 3 10  ? -51.595 -59.139 6.991   1.000 150.595 ? 10  SER CCC CA  1 
ATOM   3227  C C   . SER C 3 10  ? -52.552 -58.165 6.294   1.000 149.765 ? 10  SER CCC C   1 
ATOM   3228  O O   . SER C 3 10  ? -53.774 -58.412 6.322   1.000 153.042 ? 10  SER CCC O   1 
ATOM   3229  C CB  . SER C 3 10  ? -51.050 -60.146 6.011   1.000 153.622 ? 10  SER CCC CB  1 
ATOM   3230  O OG  . SER C 3 10  ? -50.642 -59.513 4.807   1.000 153.447 ? 10  SER CCC OG  1 
ATOM   3231  N N   . LEU C 3 11  ? -52.015 -57.117 5.667   1.000 146.037 ? 11  LEU CCC N   1 
ATOM   3232  C CA  . LEU C 3 11  ? -52.818 -56.151 4.873   1.000 146.981 ? 11  LEU CCC CA  1 
ATOM   3233  C C   . LEU C 3 11  ? -51.931 -55.476 3.821   1.000 144.819 ? 11  LEU CCC C   1 
ATOM   3234  O O   . LEU C 3 11  ? -51.027 -54.718 4.190   1.000 141.370 ? 11  LEU CCC O   1 
ATOM   3235  C CB  . LEU C 3 11  ? -53.451 -55.134 5.828   1.000 146.913 ? 11  LEU CCC CB  1 
ATOM   3236  C CG  . LEU C 3 11  ? -54.604 -54.300 5.269   1.000 152.239 ? 11  LEU CCC CG  1 
ATOM   3237  C CD1 . LEU C 3 11  ? -55.699 -55.162 4.638   1.000 158.108 ? 11  LEU CCC CD1 1 
ATOM   3238  C CD2 . LEU C 3 11  ? -55.204 -53.430 6.369   1.000 150.760 ? 11  LEU CCC CD2 1 
ATOM   3239  N N   . ALA C 3 12  ? -52.192 -55.761 2.546   1.000 148.195 ? 12  ALA CCC N   1 
ATOM   3240  C CA  . ALA C 3 12  ? -51.501 -55.175 1.372   1.000 147.993 ? 12  ALA CCC CA  1 
ATOM   3241  C C   . ALA C 3 12  ? -52.433 -54.161 0.698   1.000 147.607 ? 12  ALA CCC C   1 
ATOM   3242  O O   . ALA C 3 12  ? -53.559 -54.553 0.336   1.000 151.280 ? 12  ALA CCC O   1 
ATOM   3243  C CB  . ALA C 3 12  ? -51.096 -56.274 0.419   1.000 152.452 ? 12  ALA CCC CB  1 
ATOM   3244  N N   . VAL C 3 13  ? -51.991 -52.909 0.552   1.000 143.248 ? 13  VAL CCC N   1 
ATOM   3245  C CA  . VAL C 3 13  ? -52.849 -51.772 0.103   1.000 143.063 ? 13  VAL CCC CA  1 
ATOM   3246  C C   . VAL C 3 13  ? -52.062 -50.891 -0.871  1.000 143.310 ? 13  VAL CCC C   1 
ATOM   3247  O O   . VAL C 3 13  ? -50.883 -50.597 -0.580  1.000 140.953 ? 13  VAL CCC O   1 
ATOM   3248  C CB  . VAL C 3 13  ? -53.349 -50.965 1.318   1.000 139.375 ? 13  VAL CCC CB  1 
ATOM   3249  C CG1 . VAL C 3 13  ? -53.984 -49.647 0.916   1.000 141.099 ? 13  VAL CCC CG1 1 
ATOM   3250  C CG2 . VAL C 3 13  ? -54.311 -51.768 2.174   1.000 139.620 ? 13  VAL CCC CG2 1 
ATOM   3251  N N   . SER C 3 14  ? -52.700 -50.487 -1.977  1.000 146.186 ? 14  SER CCC N   1 
ATOM   3252  C CA  . SER C 3 14  ? -52.173 -49.506 -2.961  1.000 147.301 ? 14  SER CCC CA  1 
ATOM   3253  C C   . SER C 3 14  ? -52.055 -48.132 -2.286  1.000 144.481 ? 14  SER CCC C   1 
ATOM   3254  O O   . SER C 3 14  ? -53.027 -47.706 -1.627  1.000 143.811 ? 14  SER CCC O   1 
ATOM   3255  C CB  . SER C 3 14  ? -53.043 -49.449 -4.196  1.000 152.896 ? 14  SER CCC CB  1 
ATOM   3256  O OG  . SER C 3 14  ? -52.708 -50.487 -5.107  1.000 156.012 ? 14  SER CCC OG  1 
ATOM   3257  N N   . LEU C 3 15  ? -50.902 -47.478 -2.439  1.000 144.226 ? 15  LEU CCC N   1 
ATOM   3258  C CA  . LEU C 3 15  ? -50.599 -46.132 -1.881  1.000 144.279 ? 15  LEU CCC CA  1 
ATOM   3259  C C   . LEU C 3 15  ? -51.812 -45.212 -2.036  1.000 147.309 ? 15  LEU CCC C   1 
ATOM   3260  O O   . LEU C 3 15  ? -52.159 -44.897 -3.185  1.000 152.506 ? 15  LEU CCC O   1 
ATOM   3261  C CB  . LEU C 3 15  ? -49.391 -45.552 -2.625  1.000 146.690 ? 15  LEU CCC CB  1 
ATOM   3262  C CG  . LEU C 3 15  ? -48.025 -45.964 -2.074  1.000 145.756 ? 15  LEU CCC CG  1 
ATOM   3263  C CD1 . LEU C 3 15  ? -47.009 -46.191 -3.198  1.000 148.632 ? 15  LEU CCC CD1 1 
ATOM   3264  C CD2 . LEU C 3 15  ? -47.527 -44.930 -1.063  1.000 143.258 ? 15  LEU CCC CD2 1 
ATOM   3265  N N   . GLY C 3 16  ? -52.426 -44.794 -0.926  1.000 147.208 ? 16  GLY CCC N   1 
ATOM   3266  C CA  . GLY C 3 16  ? -53.463 -43.743 -0.934  1.000 152.378 ? 16  GLY CCC CA  1 
ATOM   3267  C C   . GLY C 3 16  ? -54.875 -44.304 -0.907  1.000 156.837 ? 16  GLY CCC C   1 
ATOM   3268  O O   . GLY C 3 16  ? -55.829 -43.490 -1.033  1.000 160.392 ? 16  GLY CCC O   1 
ATOM   3269  N N   . GLU C 3 17  ? -55.020 -45.629 -0.774  1.000 157.945 ? 17  GLU CCC N   1 
ATOM   3270  C CA  . GLU C 3 17  ? -56.323 -46.284 -0.468  1.000 161.203 ? 17  GLU CCC CA  1 
ATOM   3271  C C   . GLU C 3 17  ? -56.429 -46.389 1.058   1.000 156.632 ? 17  GLU CCC C   1 
ATOM   3272  O O   . GLU C 3 17  ? -55.385 -46.255 1.729   1.000 150.762 ? 17  GLU CCC O   1 
ATOM   3273  C CB  . GLU C 3 17  ? -56.459 -47.667 -1.116  1.000 165.338 ? 17  GLU CCC CB  1 
ATOM   3274  C CG  . GLU C 3 17  ? -56.096 -47.739 -2.597  1.000 171.490 ? 17  GLU CCC CG  1 
ATOM   3275  C CD  . GLU C 3 17  ? -57.082 -47.156 -3.604  1.000 179.402 ? 17  GLU CCC CD  1 
ATOM   3276  O OE1 . GLU C 3 17  ? -57.649 -46.083 -3.323  1.000 183.458 ? 17  GLU CCC OE1 1 
ATOM   3277  O OE2 . GLU C 3 17  ? -57.263 -47.763 -4.691  1.000 182.103 ? 17  GLU CCC OE2 1 
ATOM   3278  N N   . ARG C 3 18  ? -57.638 -46.606 1.581   1.000 159.993 ? 18  ARG CCC N   1 
ATOM   3279  C CA  . ARG C 3 18  ? -57.898 -46.800 3.036   1.000 157.649 ? 18  ARG CCC CA  1 
ATOM   3280  C C   . ARG C 3 18  ? -57.303 -48.148 3.464   1.000 151.430 ? 18  ARG CCC C   1 
ATOM   3281  O O   . ARG C 3 18  ? -56.946 -48.949 2.580   1.000 152.229 ? 18  ARG CCC O   1 
ATOM   3282  C CB  . ARG C 3 18  ? -59.404 -46.707 3.321   1.000 165.064 ? 18  ARG CCC CB  1 
ATOM   3283  C CG  . ARG C 3 18  ? -59.797 -46.638 4.794   1.000 164.335 ? 18  ARG CCC CG  1 
ATOM   3284  C CD  . ARG C 3 18  ? -61.313 -46.608 4.961   1.000 169.822 ? 18  ARG CCC CD  1 
ATOM   3285  N NE  . ARG C 3 18  ? -61.936 -45.527 4.204   1.000 174.563 ? 18  ARG CCC NE  1 
ATOM   3286  C CZ  . ARG C 3 18  ? -62.098 -44.273 4.625   1.000 174.061 ? 18  ARG CCC CZ  1 
ATOM   3287  N NH1 . ARG C 3 18  ? -61.705 -43.897 5.833   1.000 169.682 ? 18  ARG CCC NH1 1 
ATOM   3288  N NH2 . ARG C 3 18  ? -62.678 -43.391 3.830   1.000 178.153 ? 18  ARG CCC NH2 1 
ATOM   3289  N N   . ALA C 3 19  ? -57.151 -48.361 4.770   1.000 145.122 ? 19  ALA CCC N   1 
ATOM   3290  C CA  . ALA C 3 19  ? -56.712 -49.634 5.381   1.000 143.237 ? 19  ALA CCC CA  1 
ATOM   3291  C C   . ALA C 3 19  ? -57.297 -49.716 6.789   1.000 142.740 ? 19  ALA CCC C   1 
ATOM   3292  O O   . ALA C 3 19  ? -56.968 -48.839 7.612   1.000 140.528 ? 19  ALA CCC O   1 
ATOM   3293  C CB  . ALA C 3 19  ? -55.206 -49.703 5.406   1.000 140.332 ? 19  ALA CCC CB  1 
ATOM   3294  N N   . THR C 3 20  ? -58.146 -50.714 7.040   1.000 147.189 ? 20  THR CCC N   1 
ATOM   3295  C CA  . THR C 3 20  ? -58.830 -50.936 8.344   1.000 147.641 ? 20  THR CCC CA  1 
ATOM   3296  C C   . THR C 3 20  ? -58.181 -52.134 9.053   1.000 144.777 ? 20  THR CCC C   1 
ATOM   3297  O O   . THR C 3 20  ? -57.730 -53.077 8.362   1.000 142.531 ? 20  THR CCC O   1 
ATOM   3298  C CB  . THR C 3 20  ? -60.351 -51.059 8.155   1.000 153.600 ? 20  THR CCC CB  1 
ATOM   3299  O OG1 . THR C 3 20  ? -60.621 -51.783 6.955   1.000 160.125 ? 20  THR CCC OG1 1 
ATOM   3300  C CG2 . THR C 3 20  ? -61.048 -49.717 8.075   1.000 154.739 ? 20  THR CCC CG2 1 
ATOM   3301  N N   . ILE C 3 21  ? -58.091 -52.067 10.385  1.000 142.839 ? 21  ILE CCC N   1 
ATOM   3302  C CA  . ILE C 3 21  ? -57.601 -53.175 11.259  1.000 141.352 ? 21  ILE CCC CA  1 
ATOM   3303  C C   . ILE C 3 21  ? -58.556 -53.323 12.449  1.000 142.898 ? 21  ILE CCC C   1 
ATOM   3304  O O   . ILE C 3 21  ? -58.724 -52.341 13.194  1.000 141.950 ? 21  ILE CCC O   1 
ATOM   3305  C CB  . ILE C 3 21  ? -56.156 -52.933 11.728  1.000 135.961 ? 21  ILE CCC CB  1 
ATOM   3306  C CG1 . ILE C 3 21  ? -55.243 -52.563 10.558  1.000 136.225 ? 21  ILE CCC CG1 1 
ATOM   3307  C CG2 . ILE C 3 21  ? -55.643 -54.144 12.492  1.000 134.947 ? 21  ILE CCC CG2 1 
ATOM   3308  C CD1 . ILE C 3 21  ? -53.850 -52.151 10.965  1.000 134.029 ? 21  ILE CCC CD1 1 
ATOM   3309  N N   . ASN C 3 22  ? -59.135 -54.517 12.614  1.000 144.992 ? 22  ASN CCC N   1 
ATOM   3310  C CA  . ASN C 3 22  ? -60.080 -54.879 13.703  1.000 145.412 ? 22  ASN CCC CA  1 
ATOM   3311  C C   . ASN C 3 22  ? -59.292 -55.437 14.892  1.000 143.204 ? 22  ASN CCC C   1 
ATOM   3312  O O   . ASN C 3 22  ? -58.297 -56.152 14.664  1.000 141.316 ? 22  ASN CCC O   1 
ATOM   3313  C CB  . ASN C 3 22  ? -61.131 -55.889 13.236  1.000 150.301 ? 22  ASN CCC CB  1 
ATOM   3314  C CG  . ASN C 3 22  ? -62.179 -55.274 12.335  1.000 153.801 ? 22  ASN CCC CG  1 
ATOM   3315  O OD1 . ASN C 3 22  ? -62.294 -54.054 12.260  1.000 152.082 ? 22  ASN CCC OD1 1 
ATOM   3316  N ND2 . ASN C 3 22  ? -62.948 -56.107 11.652  1.000 159.429 ? 22  ASN CCC ND2 1 
ATOM   3317  N N   . CYS C 3 23  ? -59.746 -55.113 16.106  1.000 143.483 ? 23  CYS CCC N   1 
ATOM   3318  C CA  . CYS C 3 23  ? -59.182 -55.545 17.412  1.000 142.795 ? 23  CYS CCC CA  1 
ATOM   3319  C C   . CYS C 3 23  ? -60.349 -55.783 18.373  1.000 146.008 ? 23  CYS CCC C   1 
ATOM   3320  O O   . CYS C 3 23  ? -61.007 -54.786 18.731  1.000 147.502 ? 23  CYS CCC O   1 
ATOM   3321  C CB  . CYS C 3 23  ? -58.236 -54.477 17.949  1.000 140.986 ? 23  CYS CCC CB  1 
ATOM   3322  S SG  . CYS C 3 23  ? -57.769 -54.639 19.696  1.000 143.455 ? 23  CYS CCC SG  1 
ATOM   3323  N N   . LYS C 3 24  ? -60.626 -57.044 18.721  1.000 148.479 ? 24  LYS CCC N   1 
ATOM   3324  C CA  . LYS C 3 24  ? -61.786 -57.430 19.571  1.000 151.977 ? 24  LYS CCC CA  1 
ATOM   3325  C C   . LYS C 3 24  ? -61.282 -57.846 20.957  1.000 150.274 ? 24  LYS CCC C   1 
ATOM   3326  O O   . LYS C 3 24  ? -60.246 -58.533 21.028  1.000 146.455 ? 24  LYS CCC O   1 
ATOM   3327  C CB  . LYS C 3 24  ? -62.605 -58.548 18.921  1.000 157.501 ? 24  LYS CCC CB  1 
ATOM   3328  C CG  . LYS C 3 24  ? -63.912 -58.847 19.641  1.000 163.979 ? 24  LYS CCC CG  1 
ATOM   3329  C CD  . LYS C 3 24  ? -64.696 -60.004 19.064  1.000 171.365 ? 24  LYS CCC CD  1 
ATOM   3330  C CE  . LYS C 3 24  ? -65.729 -60.553 20.028  1.000 177.169 ? 24  LYS CCC CE  1 
ATOM   3331  N NZ  . LYS C 3 24  ? -66.724 -59.529 20.430  1.000 178.868 ? 24  LYS CCC NZ  1 
ATOM   3332  N N   . SER C 3 25  ? -62.003 -57.439 22.007  1.000 152.868 ? 25  SER CCC N   1 
ATOM   3333  C CA  . SER C 3 25  ? -61.684 -57.697 23.436  1.000 154.518 ? 25  SER CCC CA  1 
ATOM   3334  C C   . SER C 3 25  ? -62.781 -58.560 24.065  1.000 161.645 ? 25  SER CCC C   1 
ATOM   3335  O O   . SER C 3 25  ? -63.970 -58.250 23.859  1.000 166.456 ? 25  SER CCC O   1 
ATOM   3336  C CB  . SER C 3 25  ? -61.539 -56.416 24.200  1.000 152.426 ? 25  SER CCC CB  1 
ATOM   3337  O OG  . SER C 3 25  ? -62.817 -55.899 24.538  1.000 157.666 ? 25  SER CCC OG  1 
ATOM   3338  N N   . SER C 3 26  ? -62.384 -59.571 24.840  1.000 162.932 ? 26  SER CCC N   1 
ATOM   3339  C CA  . SER C 3 26  ? -63.289 -60.557 25.489  1.000 168.361 ? 26  SER CCC CA  1 
ATOM   3340  C C   . SER C 3 26  ? -64.101 -59.890 26.609  1.000 168.665 ? 26  SER CCC C   1 
ATOM   3341  O O   . SER C 3 26  ? -65.165 -60.436 26.953  1.000 175.861 ? 26  SER CCC O   1 
ATOM   3342  C CB  . SER C 3 26  ? -62.509 -61.752 25.988  1.000 170.274 ? 26  SER CCC CB  1 
ATOM   3343  O OG  . SER C 3 26  ? -61.184 -61.386 26.354  1.000 166.338 ? 26  SER CCC OG  1 
ATOM   3344  N N   . GLN C 3 27  ? -63.621 -58.761 27.148  1.000 162.005 ? 27  GLN CCC N   1 
ATOM   3345  C CA  . GLN C 3 27  ? -64.273 -57.982 28.239  1.000 161.924 ? 27  GLN CCC CA  1 
ATOM   3346  C C   . GLN C 3 27  ? -64.407 -56.528 27.774  1.000 157.306 ? 27  GLN CCC C   1 
ATOM   3347  O O   . GLN C 3 27  ? -63.541 -56.083 27.007  1.000 151.518 ? 27  GLN CCC O   1 
ATOM   3348  C CB  . GLN C 3 27  ? -63.451 -58.101 29.529  1.000 160.161 ? 27  GLN CCC CB  1 
ATOM   3349  C CG  . GLN C 3 27  ? -64.245 -57.915 30.821  1.000 164.031 ? 27  GLN CCC CG  1 
ATOM   3350  C CD  . GLN C 3 27  ? -63.594 -58.568 32.023  1.000 165.336 ? 27  GLN CCC CD  1 
ATOM   3351  O OE1 . GLN C 3 27  ? -62.372 -58.680 32.113  1.000 161.226 ? 27  GLN CCC OE1 1 
ATOM   3352  N NE2 . GLN C 3 27  ? -64.412 -59.008 32.969  1.000 171.655 ? 27  GLN CCC NE2 1 
ATOM   3353  N N   . SER C 3 28  ? -65.464 -55.828 28.196  1.000 161.255 ? 28  SER CCC N   1 
ATOM   3354  C CA  . SER C 3 28  ? -65.678 -54.381 27.924  1.000 160.140 ? 28  SER CCC CA  1 
ATOM   3355  C C   . SER C 3 28  ? -64.597 -53.588 28.653  1.000 155.402 ? 28  SER CCC C   1 
ATOM   3356  O O   . SER C 3 28  ? -64.200 -54.016 29.755  1.000 155.203 ? 28  SER CCC O   1 
ATOM   3357  C CB  . SER C 3 28  ? -67.048 -53.910 28.335  1.000 166.855 ? 28  SER CCC CB  1 
ATOM   3358  O OG  . SER C 3 28  ? -67.168 -52.504 28.148  1.000 165.456 ? 28  SER CCC OG  1 
ATOM   3359  N N   . VAL C 3 29  ? -64.159 -52.477 28.056  1.000 151.960 ? 29  VAL CCC N   1 
ATOM   3360  C CA  . VAL C 3 29  ? -63.037 -51.636 28.568  1.000 148.065 ? 29  VAL CCC CA  1 
ATOM   3361  C C   . VAL C 3 29  ? -63.549 -50.216 28.825  1.000 149.702 ? 29  VAL CCC C   1 
ATOM   3362  O O   . VAL C 3 29  ? -62.711 -49.318 29.005  1.000 147.132 ? 29  VAL CCC O   1 
ATOM   3363  C CB  . VAL C 3 29  ? -61.861 -51.645 27.575  1.000 142.740 ? 29  VAL CCC CB  1 
ATOM   3364  C CG1 . VAL C 3 29  ? -61.477 -53.063 27.180  1.000 142.741 ? 29  VAL CCC CG1 1 
ATOM   3365  C CG2 . VAL C 3 29  ? -62.158 -50.820 26.334  1.000 142.090 ? 29  VAL CCC CG2 1 
ATOM   3366  N N   . LEU C 3 30  ? -64.870 -50.030 28.854  1.000 155.086 ? 30  LEU CCC N   1 
ATOM   3367  C CA  . LEU C 3 30  ? -65.520 -48.712 29.068  1.000 158.133 ? 30  LEU CCC CA  1 
ATOM   3368  C C   . LEU C 3 30  ? -65.356 -48.298 30.540  1.000 160.739 ? 30  LEU CCC C   1 
ATOM   3369  O O   . LEU C 3 30  ? -65.666 -49.119 31.424  1.000 164.184 ? 30  LEU CCC O   1 
ATOM   3370  C CB  . LEU C 3 30  ? -66.991 -48.833 28.656  1.000 163.679 ? 30  LEU CCC CB  1 
ATOM   3371  C CG  . LEU C 3 30  ? -67.802 -47.536 28.591  1.000 167.033 ? 30  LEU CCC CG  1 
ATOM   3372  C CD1 . LEU C 3 30  ? -68.451 -47.219 29.934  1.000 171.546 ? 30  LEU CCC CD1 1 
ATOM   3373  C CD2 . LEU C 3 30  ? -66.965 -46.359 28.102  1.000 162.426 ? 30  LEU CCC CD2 1 
ATOM   3374  N N   . TYR C 3 31  ? -64.855 -47.080 30.784  1.000 161.292 ? 31  TYR CCC N   1 
ATOM   3375  C CA  . TYR C 3 31  ? -64.825 -46.404 32.111  1.000 164.817 ? 31  TYR CCC CA  1 
ATOM   3376  C C   . TYR C 3 31  ? -66.181 -45.719 32.331  1.000 170.946 ? 31  TYR CCC C   1 
ATOM   3377  O O   . TYR C 3 31  ? -66.343 -44.558 31.908  1.000 170.696 ? 31  TYR CCC O   1 
ATOM   3378  C CB  . TYR C 3 31  ? -63.653 -45.412 32.204  1.000 162.385 ? 31  TYR CCC CB  1 
ATOM   3379  C CG  . TYR C 3 31  ? -62.524 -45.815 33.124  1.000 161.649 ? 31  TYR CCC CG  1 
ATOM   3380  C CD1 . TYR C 3 31  ? -61.665 -46.856 32.799  1.000 159.439 ? 31  TYR CCC CD1 1 
ATOM   3381  C CD2 . TYR C 3 31  ? -62.299 -45.147 34.319  1.000 162.388 ? 31  TYR CCC CD2 1 
ATOM   3382  C CE1 . TYR C 3 31  ? -60.631 -47.236 33.641  1.000 155.940 ? 31  TYR CCC CE1 1 
ATOM   3383  C CE2 . TYR C 3 31  ? -61.267 -45.510 35.172  1.000 159.271 ? 31  TYR CCC CE2 1 
ATOM   3384  C CZ  . TYR C 3 31  ? -60.431 -46.557 34.829  1.000 155.886 ? 31  TYR CCC CZ  1 
ATOM   3385  O OH  . TYR C 3 31  ? -59.418 -46.932 35.656  1.000 154.861 ? 31  TYR CCC OH  1 
ATOM   3386  N N   . SER C 3 32  ? -67.134 -46.425 32.952  1.000 176.488 ? 32  SER CCC N   1 
ATOM   3387  C CA  . SER C 3 32  ? -68.506 -45.929 33.239  1.000 181.284 ? 32  SER CCC CA  1 
ATOM   3388  C C   . SER C 3 32  ? -68.422 -44.457 33.660  1.000 180.497 ? 32  SER CCC C   1 
ATOM   3389  O O   . SER C 3 32  ? -69.159 -43.639 33.079  1.000 182.245 ? 32  SER CCC O   1 
ATOM   3390  C CB  . SER C 3 32  ? -69.191 -46.771 34.291  1.000 186.272 ? 32  SER CCC CB  1 
ATOM   3391  O OG  . SER C 3 32  ? -70.520 -46.323 34.524  1.000 193.331 ? 32  SER CCC OG  1 
ATOM   3392  N N   . SER C 3 33  ? -67.515 -44.147 34.597  1.000 177.153 ? 33  SER CCC N   1 
ATOM   3393  C CA  . SER C 3 33  ? -67.278 -42.794 35.169  1.000 176.341 ? 33  SER CCC CA  1 
ATOM   3394  C C   . SER C 3 33  ? -67.267 -41.746 34.052  1.000 175.628 ? 33  SER CCC C   1 
ATOM   3395  O O   . SER C 3 33  ? -68.206 -40.934 34.010  1.000 180.844 ? 33  SER CCC O   1 
ATOM   3396  C CB  . SER C 3 33  ? -66.009 -42.744 35.983  1.000 171.500 ? 33  SER CCC CB  1 
ATOM   3397  O OG  . SER C 3 33  ? -64.866 -43.024 35.189  1.000 163.734 ? 33  SER CCC OG  1 
ATOM   3398  N N   . ILE C 3 34  ? -66.252 -41.776 33.184  1.000 170.878 ? 34  ILE CCC N   1 
ATOM   3399  C CA  . ILE C 3 34  ? -66.101 -40.830 32.037  1.000 168.943 ? 34  ILE CCC CA  1 
ATOM   3400  C C   . ILE C 3 34  ? -66.203 -41.638 30.736  1.000 166.421 ? 34  ILE CCC C   1 
ATOM   3401  O O   . ILE C 3 34  ? -65.193 -42.217 30.307  1.000 162.667 ? 34  ILE CCC O   1 
ATOM   3402  C CB  . ILE C 3 34  ? -64.797 -40.003 32.145  1.000 164.652 ? 34  ILE CCC CB  1 
ATOM   3403  C CG1 . ILE C 3 34  ? -63.585 -40.831 32.579  1.000 159.316 ? 34  ILE CCC CG1 1 
ATOM   3404  C CG2 . ILE C 3 34  ? -64.993 -38.819 33.081  1.000 168.554 ? 34  ILE CCC CG2 1 
ATOM   3405  C CD1 . ILE C 3 34  ? -62.263 -40.087 32.463  1.000 154.909 ? 34  ILE CCC CD1 1 
ATOM   3406  N N   . ASN C 3 35  ? -67.406 -41.700 30.159  1.000 168.717 ? 35  ASN CCC N   1 
ATOM   3407  C CA  . ASN C 3 35  ? -67.749 -42.528 28.972  1.000 166.790 ? 35  ASN CCC CA  1 
ATOM   3408  C C   . ASN C 3 35  ? -66.592 -42.488 27.962  1.000 158.729 ? 35  ASN CCC C   1 
ATOM   3409  O O   . ASN C 3 35  ? -66.757 -41.849 26.905  1.000 155.940 ? 35  ASN CCC O   1 
ATOM   3410  C CB  . ASN C 3 35  ? -69.087 -42.062 28.388  1.000 173.247 ? 35  ASN CCC CB  1 
ATOM   3411  C CG  . ASN C 3 35  ? -69.663 -43.017 27.368  1.000 175.513 ? 35  ASN CCC CG  1 
ATOM   3412  O OD1 . ASN C 3 35  ? -68.922 -43.601 26.579  1.000 172.074 ? 35  ASN CCC OD1 1 
ATOM   3413  N ND2 . ASN C 3 35  ? -70.980 -43.171 27.378  1.000 181.277 ? 35  ASN CCC ND2 1 
ATOM   3414  N N   . LYS C 3 36  ? -65.486 -43.170 28.283  1.000 154.459 ? 36  LYS CCC N   1 
ATOM   3415  C CA  . LYS C 3 36  ? -64.297 -43.376 27.407  1.000 150.235 ? 36  LYS CCC CA  1 
ATOM   3416  C C   . LYS C 3 36  ? -63.853 -44.837 27.511  1.000 145.935 ? 36  LYS CCC C   1 
ATOM   3417  O O   . LYS C 3 36  ? -63.796 -45.339 28.640  1.000 145.681 ? 36  LYS CCC O   1 
ATOM   3418  C CB  . LYS C 3 36  ? -63.114 -42.497 27.826  1.000 150.143 ? 36  LYS CCC CB  1 
ATOM   3419  C CG  . LYS C 3 36  ? -63.397 -41.007 27.905  1.000 156.053 ? 36  LYS CCC CG  1 
ATOM   3420  C CD  . LYS C 3 36  ? -63.677 -40.380 26.565  1.000 159.341 ? 36  LYS CCC CD  1 
ATOM   3421  C CE  . LYS C 3 36  ? -63.926 -38.890 26.658  1.000 164.076 ? 36  LYS CCC CE  1 
ATOM   3422  N NZ  . LYS C 3 36  ? -64.092 -38.288 25.312  1.000 165.947 ? 36  LYS CCC NZ  1 
ATOM   3423  N N   . ASN C 3 37  ? -63.556 -45.486 26.383  1.000 143.724 ? 37  ASN CCC N   1 
ATOM   3424  C CA  . ASN C 3 37  ? -62.996 -46.863 26.350  1.000 144.118 ? 37  ASN CCC CA  1 
ATOM   3425  C C   . ASN C 3 37  ? -61.476 -46.753 26.514  1.000 139.145 ? 37  ASN CCC C   1 
ATOM   3426  O O   . ASN C 3 37  ? -60.877 -45.935 25.801  1.000 136.835 ? 37  ASN CCC O   1 
ATOM   3427  C CB  . ASN C 3 37  ? -63.404 -47.619 25.080  1.000 148.275 ? 37  ASN CCC CB  1 
ATOM   3428  C CG  . ASN C 3 37  ? -64.807 -48.189 25.139  1.000 157.548 ? 37  ASN CCC CG  1 
ATOM   3429  O OD1 . ASN C 3 37  ? -65.655 -47.830 24.320  1.000 163.492 ? 37  ASN CCC OD1 1 
ATOM   3430  N ND2 . ASN C 3 37  ? -65.060 -49.083 26.087  1.000 160.738 ? 37  ASN CCC ND2 1 
ATOM   3431  N N   . TYR C 3 38  ? -60.891 -47.533 27.431  1.000 138.037 ? 38  TYR CCC N   1 
ATOM   3432  C CA  . TYR C 3 38  ? -59.455 -47.469 27.820  1.000 133.721 ? 38  TYR CCC CA  1 
ATOM   3433  C C   . TYR C 3 38  ? -58.672 -48.457 26.942  1.000 132.241 ? 38  TYR CCC C   1 
ATOM   3434  O O   . TYR C 3 38  ? -58.148 -49.475 27.441  1.000 130.289 ? 38  TYR CCC O   1 
ATOM   3435  C CB  . TYR C 3 38  ? -59.313 -47.624 29.342  1.000 131.958 ? 38  TYR CCC CB  1 
ATOM   3436  C CG  . TYR C 3 38  ? -59.419 -46.313 30.087  1.000 131.101 ? 38  TYR CCC CG  1 
ATOM   3437  C CD1 . TYR C 3 38  ? -60.440 -45.415 29.808  1.000 133.680 ? 38  TYR CCC CD1 1 
ATOM   3438  C CD2 . TYR C 3 38  ? -58.479 -45.938 31.033  1.000 129.323 ? 38  TYR CCC CD2 1 
ATOM   3439  C CE1 . TYR C 3 38  ? -60.530 -44.191 30.453  1.000 135.062 ? 38  TYR CCC CE1 1 
ATOM   3440  C CE2 . TYR C 3 38  ? -58.555 -44.717 31.688  1.000 130.954 ? 38  TYR CCC CE2 1 
ATOM   3441  C CZ  . TYR C 3 38  ? -59.587 -43.839 31.402  1.000 133.670 ? 38  TYR CCC CZ  1 
ATOM   3442  O OH  . TYR C 3 38  ? -59.675 -42.627 32.029  1.000 134.279 ? 38  TYR CCC OH  1 
ATOM   3443  N N   . LEU C 3 39  ? -58.601 -48.126 25.647  1.000 133.595 ? 39  LEU CCC N   1 
ATOM   3444  C CA  . LEU C 3 39  ? -58.001 -48.941 24.552  1.000 135.100 ? 39  LEU CCC CA  1 
ATOM   3445  C C   . LEU C 3 39  ? -57.083 -48.028 23.730  1.000 130.174 ? 39  LEU CCC C   1 
ATOM   3446  O O   . LEU C 3 39  ? -57.459 -46.856 23.513  1.000 129.882 ? 39  LEU CCC O   1 
ATOM   3447  C CB  . LEU C 3 39  ? -59.153 -49.529 23.719  1.000 142.447 ? 39  LEU CCC CB  1 
ATOM   3448  C CG  . LEU C 3 39  ? -58.827 -50.424 22.512  1.000 144.446 ? 39  LEU CCC CG  1 
ATOM   3449  C CD1 . LEU C 3 39  ? -58.496 -49.603 21.268  1.000 143.412 ? 39  LEU CCC CD1 1 
ATOM   3450  C CD2 . LEU C 3 39  ? -57.726 -51.437 22.812  1.000 143.553 ? 39  LEU CCC CD2 1 
ATOM   3451  N N   . ALA C 3 40  ? -55.914 -48.532 23.321  1.000 126.303 ? 40  ALA CCC N   1 
ATOM   3452  C CA  . ALA C 3 40  ? -54.872 -47.774 22.591  1.000 123.555 ? 40  ALA CCC CA  1 
ATOM   3453  C C   . ALA C 3 40  ? -54.376 -48.555 21.365  1.000 123.699 ? 40  ALA CCC C   1 
ATOM   3454  O O   . ALA C 3 40  ? -54.692 -49.763 21.235  1.000 124.992 ? 40  ALA CCC O   1 
ATOM   3455  C CB  . ALA C 3 40  ? -53.733 -47.443 23.524  1.000 121.388 ? 40  ALA CCC CB  1 
ATOM   3456  N N   . TRP C 3 41  ? -53.616 -47.859 20.509  1.000 123.013 ? 41  TRP CCC N   1 
ATOM   3457  C CA  . TRP C 3 41  ? -53.070 -48.337 19.208  1.000 121.781 ? 41  TRP CCC CA  1 
ATOM   3458  C C   . TRP C 3 41  ? -51.590 -47.936 19.096  1.000 120.653 ? 41  TRP CCC C   1 
ATOM   3459  O O   . TRP C 3 41  ? -51.281 -46.731 19.287  1.000 120.184 ? 41  TRP CCC O   1 
ATOM   3460  C CB  . TRP C 3 41  ? -53.892 -47.755 18.051  1.000 121.994 ? 41  TRP CCC CB  1 
ATOM   3461  C CG  . TRP C 3 41  ? -55.233 -48.390 17.837  1.000 124.395 ? 41  TRP CCC CG  1 
ATOM   3462  C CD1 . TRP C 3 41  ? -56.463 -47.873 18.141  1.000 127.644 ? 41  TRP CCC CD1 1 
ATOM   3463  C CD2 . TRP C 3 41  ? -55.481 -49.664 17.224  1.000 124.206 ? 41  TRP CCC CD2 1 
ATOM   3464  N NE1 . TRP C 3 41  ? -57.458 -48.740 17.768  1.000 128.795 ? 41  TRP CCC NE1 1 
ATOM   3465  C CE2 . TRP C 3 41  ? -56.881 -49.846 17.200  1.000 127.531 ? 41  TRP CCC CE2 1 
ATOM   3466  C CE3 . TRP C 3 41  ? -54.654 -50.661 16.697  1.000 123.605 ? 41  TRP CCC CE3 1 
ATOM   3467  C CZ2 . TRP C 3 41  ? -57.464 -50.988 16.660  1.000 130.352 ? 41  TRP CCC CZ2 1 
ATOM   3468  C CZ3 . TRP C 3 41  ? -55.233 -51.788 16.161  1.000 126.655 ? 41  TRP CCC CZ3 1 
ATOM   3469  C CH2 . TRP C 3 41  ? -56.619 -51.946 16.145  1.000 129.843 ? 41  TRP CCC CH2 1 
ATOM   3470  N N   . TYR C 3 42  ? -50.712 -48.901 18.799  1.000 119.621 ? 42  TYR CCC N   1 
ATOM   3471  C CA  . TYR C 3 42  ? -49.243 -48.704 18.672  1.000 117.502 ? 42  TYR CCC CA  1 
ATOM   3472  C C   . TYR C 3 42  ? -48.789 -49.128 17.265  1.000 117.513 ? 42  TYR CCC C   1 
ATOM   3473  O O   . TYR C 3 42  ? -49.261 -50.171 16.752  1.000 119.124 ? 42  TYR CCC O   1 
ATOM   3474  C CB  . TYR C 3 42  ? -48.502 -49.482 19.768  1.000 117.931 ? 42  TYR CCC CB  1 
ATOM   3475  C CG  . TYR C 3 42  ? -48.791 -49.073 21.194  1.000 119.462 ? 42  TYR CCC CG  1 
ATOM   3476  C CD1 . TYR C 3 42  ? -48.030 -48.103 21.829  1.000 121.086 ? 42  TYR CCC CD1 1 
ATOM   3477  C CD2 . TYR C 3 42  ? -49.797 -49.681 21.935  1.000 120.418 ? 42  TYR CCC CD2 1 
ATOM   3478  C CE1 . TYR C 3 42  ? -48.278 -47.727 23.142  1.000 122.715 ? 42  TYR CCC CE1 1 
ATOM   3479  C CE2 . TYR C 3 42  ? -50.061 -49.313 23.247  1.000 121.366 ? 42  TYR CCC CE2 1 
ATOM   3480  C CZ  . TYR C 3 42  ? -49.296 -48.334 23.857  1.000 123.551 ? 42  TYR CCC CZ  1 
ATOM   3481  O OH  . TYR C 3 42  ? -49.534 -47.965 25.152  1.000 126.862 ? 42  TYR CCC OH  1 
ATOM   3482  N N   . GLN C 3 43  ? -47.922 -48.318 16.644  1.000 116.226 ? 43  GLN CCC N   1 
ATOM   3483  C CA  . GLN C 3 43  ? -47.150 -48.664 15.417  1.000 114.716 ? 43  GLN CCC CA  1 
ATOM   3484  C C   . GLN C 3 43  ? -45.726 -49.028 15.852  1.000 114.876 ? 43  GLN CCC C   1 
ATOM   3485  O O   . GLN C 3 43  ? -45.188 -48.345 16.748  1.000 114.665 ? 43  GLN CCC O   1 
ATOM   3486  C CB  . GLN C 3 43  ? -47.139 -47.499 14.418  1.000 112.630 ? 43  GLN CCC CB  1 
ATOM   3487  C CG  . GLN C 3 43  ? -45.803 -47.302 13.711  1.000 112.601 ? 43  GLN CCC CG  1 
ATOM   3488  C CD  . GLN C 3 43  ? -45.765 -46.062 12.850  1.000 112.052 ? 43  GLN CCC CD  1 
ATOM   3489  O OE1 . GLN C 3 43  ? -44.866 -45.222 12.964  1.000 111.388 ? 43  GLN CCC OE1 1 
ATOM   3490  N NE2 . GLN C 3 43  ? -46.760 -45.936 11.987  1.000 109.878 ? 43  GLN CCC NE2 1 
ATOM   3491  N N   . GLN C 3 44  ? -45.133 -50.050 15.240  1.000 115.083 ? 44  GLN CCC N   1 
ATOM   3492  C CA  . GLN C 3 44  ? -43.709 -50.394 15.457  1.000 116.872 ? 44  GLN CCC CA  1 
ATOM   3493  C C   . GLN C 3 44  ? -43.058 -50.617 14.094  1.000 118.904 ? 44  GLN CCC C   1 
ATOM   3494  O O   . GLN C 3 44  ? -43.284 -51.688 13.498  1.000 119.219 ? 44  GLN CCC O   1 
ATOM   3495  C CB  . GLN C 3 44  ? -43.579 -51.621 16.360  1.000 118.365 ? 44  GLN CCC CB  1 
ATOM   3496  C CG  . GLN C 3 44  ? -42.175 -52.212 16.364  1.000 121.721 ? 44  GLN CCC CG  1 
ATOM   3497  C CD  . GLN C 3 44  ? -41.992 -53.246 17.440  1.000 123.477 ? 44  GLN CCC CD  1 
ATOM   3498  O OE1 . GLN C 3 44  ? -42.738 -54.220 17.507  1.000 123.828 ? 44  GLN CCC OE1 1 
ATOM   3499  N NE2 . GLN C 3 44  ? -40.989 -53.038 18.281  1.000 125.336 ? 44  GLN CCC NE2 1 
ATOM   3500  N N   . LYS C 3 45  ? -42.313 -49.621 13.613  1.000 121.022 ? 45  LYS CCC N   1 
ATOM   3501  C CA  . LYS C 3 45  ? -41.376 -49.795 12.478  1.000 125.067 ? 45  LYS CCC CA  1 
ATOM   3502  C C   . LYS C 3 45  ? -40.194 -50.592 13.032  1.000 125.546 ? 45  LYS CCC C   1 
ATOM   3503  O O   . LYS C 3 45  ? -39.693 -50.276 14.109  1.000 124.081 ? 45  LYS CCC O   1 
ATOM   3504  C CB  . LYS C 3 45  ? -41.005 -48.441 11.853  1.000 129.270 ? 45  LYS CCC CB  1 
ATOM   3505  C CG  . LYS C 3 45  ? -41.965 -47.921 10.778  1.000 131.079 ? 45  LYS CCC CG  1 
ATOM   3506  C CD  . LYS C 3 45  ? -41.682 -46.493 10.289  1.000 134.310 ? 45  LYS CCC CD  1 
ATOM   3507  C CE  . LYS C 3 45  ? -42.352 -45.410 11.121  1.000 133.710 ? 45  LYS CCC CE  1 
ATOM   3508  N NZ  . LYS C 3 45  ? -42.003 -44.038 10.671  1.000 134.539 ? 45  LYS CCC NZ  1 
ATOM   3509  N N   . PRO C 3 46  ? -39.787 -51.701 12.368  1.000 127.485 ? 46  PRO CCC N   1 
ATOM   3510  C CA  . PRO C 3 46  ? -38.655 -52.521 12.813  1.000 128.591 ? 46  PRO CCC CA  1 
ATOM   3511  C C   . PRO C 3 46  ? -37.379 -51.752 13.191  1.000 129.817 ? 46  PRO CCC C   1 
ATOM   3512  O O   . PRO C 3 46  ? -37.017 -50.834 12.486  1.000 127.885 ? 46  PRO CCC O   1 
ATOM   3513  C CB  . PRO C 3 46  ? -38.355 -53.378 11.576  1.000 130.624 ? 46  PRO CCC CB  1 
ATOM   3514  C CG  . PRO C 3 46  ? -39.702 -53.552 10.908  1.000 130.622 ? 46  PRO CCC CG  1 
ATOM   3515  C CD  . PRO C 3 46  ? -40.450 -52.264 11.178  1.000 128.556 ? 46  PRO CCC CD  1 
ATOM   3516  N N   . GLY C 3 47  ? -36.728 -52.160 14.286  1.000 132.240 ? 47  GLY CCC N   1 
ATOM   3517  C CA  . GLY C 3 47  ? -35.473 -51.557 14.781  1.000 134.484 ? 47  GLY CCC CA  1 
ATOM   3518  C C   . GLY C 3 47  ? -35.747 -50.506 15.837  1.000 131.350 ? 47  GLY CCC C   1 
ATOM   3519  O O   . GLY C 3 47  ? -34.839 -50.194 16.621  1.000 131.334 ? 47  GLY CCC O   1 
ATOM   3520  N N   . GLN C 3 48  ? -36.977 -49.996 15.848  1.000 129.439 ? 48  GLN CCC N   1 
ATOM   3521  C CA  . GLN C 3 48  ? -37.459 -48.924 16.747  1.000 130.093 ? 48  GLN CCC CA  1 
ATOM   3522  C C   . GLN C 3 48  ? -38.271 -49.562 17.868  1.000 125.057 ? 48  GLN CCC C   1 
ATOM   3523  O O   . GLN C 3 48  ? -38.667 -50.722 17.770  1.000 124.473 ? 48  GLN CCC O   1 
ATOM   3524  C CB  . GLN C 3 48  ? -38.313 -47.929 15.952  1.000 132.970 ? 48  GLN CCC CB  1 
ATOM   3525  C CG  . GLN C 3 48  ? -37.615 -47.355 14.721  1.000 136.647 ? 48  GLN CCC CG  1 
ATOM   3526  C CD  . GLN C 3 48  ? -38.524 -46.483 13.885  1.000 137.208 ? 48  GLN CCC CD  1 
ATOM   3527  O OE1 . GLN C 3 48  ? -39.690 -46.257 14.213  1.000 137.653 ? 48  GLN CCC OE1 1 
ATOM   3528  N NE2 . GLN C 3 48  ? -37.992 -45.978 12.784  1.000 139.932 ? 48  GLN CCC NE2 1 
ATOM   3529  N N   . PRO C 3 49  ? -38.549 -48.818 18.960  1.000 120.878 ? 49  PRO CCC N   1 
ATOM   3530  C CA  . PRO C 3 49  ? -39.567 -49.221 19.917  1.000 118.128 ? 49  PRO CCC CA  1 
ATOM   3531  C C   . PRO C 3 49  ? -40.928 -48.900 19.319  1.000 116.384 ? 49  PRO CCC C   1 
ATOM   3532  O O   . PRO C 3 49  ? -40.995 -48.280 18.256  1.000 117.419 ? 49  PRO CCC O   1 
ATOM   3533  C CB  . PRO C 3 49  ? -39.272 -48.340 21.132  1.000 118.887 ? 49  PRO CCC CB  1 
ATOM   3534  C CG  . PRO C 3 49  ? -38.732 -47.069 20.521  1.000 120.118 ? 49  PRO CCC CG  1 
ATOM   3535  C CD  . PRO C 3 49  ? -37.930 -47.534 19.323  1.000 121.992 ? 49  PRO CCC CD  1 
ATOM   3536  N N   . PRO C 3 50  ? -42.031 -49.357 19.956  1.000 115.440 ? 50  PRO CCC N   1 
ATOM   3537  C CA  . PRO C 3 50  ? -43.385 -48.931 19.604  1.000 114.390 ? 50  PRO CCC CA  1 
ATOM   3538  C C   . PRO C 3 50  ? -43.677 -47.443 19.840  1.000 115.212 ? 50  PRO CCC C   1 
ATOM   3539  O O   . PRO C 3 50  ? -43.222 -46.860 20.824  1.000 114.586 ? 50  PRO CCC O   1 
ATOM   3540  C CB  . PRO C 3 50  ? -44.298 -49.756 20.517  1.000 112.887 ? 50  PRO CCC CB  1 
ATOM   3541  C CG  . PRO C 3 50  ? -43.458 -50.958 20.850  1.000 114.899 ? 50  PRO CCC CG  1 
ATOM   3542  C CD  . PRO C 3 50  ? -42.049 -50.415 20.970  1.000 116.331 ? 50  PRO CCC CD  1 
ATOM   3543  N N   . LYS C 3 51  ? -44.435 -46.885 18.898  1.000 116.344 ? 51  LYS CCC N   1 
ATOM   3544  C CA  . LYS C 3 51  ? -44.936 -45.494 18.899  1.000 119.170 ? 51  LYS CCC CA  1 
ATOM   3545  C C   . LYS C 3 51  ? -46.422 -45.568 19.244  1.000 120.886 ? 51  LYS CCC C   1 
ATOM   3546  O O   . LYS C 3 51  ? -47.112 -46.450 18.692  1.000 119.254 ? 51  LYS CCC O   1 
ATOM   3547  C CB  . LYS C 3 51  ? -44.677 -44.848 17.533  1.000 120.858 ? 51  LYS CCC CB  1 
ATOM   3548  C CG  . LYS C 3 51  ? -45.015 -43.366 17.408  1.000 122.487 ? 51  LYS CCC CG  1 
ATOM   3549  C CD  . LYS C 3 51  ? -44.475 -42.747 16.130  1.000 125.809 ? 51  LYS CCC CD  1 
ATOM   3550  C CE  . LYS C 3 51  ? -45.025 -41.366 15.823  1.000 129.290 ? 51  LYS CCC CE  1 
ATOM   3551  N NZ  . LYS C 3 51  ? -44.245 -40.288 16.478  1.000 133.014 ? 51  LYS CCC NZ  1 
ATOM   3552  N N   . LEU C 3 52  ? -46.870 -44.724 20.174  1.000 124.439 ? 52  LEU CCC N   1 
ATOM   3553  C CA  . LEU C 3 52  ? -48.307 -44.531 20.495  1.000 124.797 ? 52  LEU CCC CA  1 
ATOM   3554  C C   . LEU C 3 52  ? -48.939 -43.685 19.381  1.000 125.566 ? 52  LEU CCC C   1 
ATOM   3555  O O   . LEU C 3 52  ? -48.421 -42.578 19.104  1.000 126.255 ? 52  LEU CCC O   1 
ATOM   3556  C CB  . LEU C 3 52  ? -48.426 -43.854 21.864  1.000 126.025 ? 52  LEU CCC CB  1 
ATOM   3557  C CG  . LEU C 3 52  ? -49.845 -43.701 22.411  1.000 127.629 ? 52  LEU CCC CG  1 
ATOM   3558  C CD1 . LEU C 3 52  ? -50.448 -45.050 22.775  1.000 126.668 ? 52  LEU CCC CD1 1 
ATOM   3559  C CD2 . LEU C 3 52  ? -49.863 -42.769 23.615  1.000 129.483 ? 52  LEU CCC CD2 1 
ATOM   3560  N N   . LEU C 3 53  ? -49.995 -44.205 18.749  1.000 125.013 ? 53  LEU CCC N   1 
ATOM   3561  C CA  . LEU C 3 53  ? -50.780 -43.492 17.704  1.000 127.275 ? 53  LEU CCC CA  1 
ATOM   3562  C C   . LEU C 3 53  ? -52.069 -42.937 18.322  1.000 129.549 ? 53  LEU CCC C   1 
ATOM   3563  O O   . LEU C 3 53  ? -52.351 -41.732 18.108  1.000 132.227 ? 53  LEU CCC O   1 
ATOM   3564  C CB  . LEU C 3 53  ? -51.102 -44.455 16.557  1.000 128.713 ? 53  LEU CCC CB  1 
ATOM   3565  C CG  . LEU C 3 53  ? -49.907 -45.009 15.777  1.000 129.160 ? 53  LEU CCC CG  1 
ATOM   3566  C CD1 . LEU C 3 53  ? -50.352 -46.054 14.764  1.000 129.784 ? 53  LEU CCC CD1 1 
ATOM   3567  C CD2 . LEU C 3 53  ? -49.140 -43.903 15.073  1.000 130.811 ? 53  LEU CCC CD2 1 
ATOM   3568  N N   . ILE C 3 54  ? -52.823 -43.770 19.053  1.000 128.276 ? 54  ILE CCC N   1 
ATOM   3569  C CA  . ILE C 3 54  ? -54.181 -43.411 19.565  1.000 127.427 ? 54  ILE CCC CA  1 
ATOM   3570  C C   . ILE C 3 54  ? -54.422 -43.956 20.983  1.000 124.349 ? 54  ILE CCC C   1 
ATOM   3571  O O   . ILE C 3 54  ? -54.039 -45.111 21.249  1.000 124.762 ? 54  ILE CCC O   1 
ATOM   3572  C CB  . ILE C 3 54  ? -55.228 -43.903 18.554  1.000 129.934 ? 54  ILE CCC CB  1 
ATOM   3573  C CG1 . ILE C 3 54  ? -55.216 -43.009 17.311  1.000 133.123 ? 54  ILE CCC CG1 1 
ATOM   3574  C CG2 . ILE C 3 54  ? -56.602 -43.992 19.194  1.000 133.165 ? 54  ILE CCC CG2 1 
ATOM   3575  C CD1 . ILE C 3 54  ? -56.202 -43.404 16.235  1.000 137.312 ? 54  ILE CCC CD1 1 
ATOM   3576  N N   . TYR C 3 55  ? -55.050 -43.143 21.845  1.000 120.774 ? 55  TYR CCC N   1 
ATOM   3577  C CA  . TYR C 3 55  ? -55.496 -43.503 23.217  1.000 120.103 ? 55  TYR CCC CA  1 
ATOM   3578  C C   . TYR C 3 55  ? -56.990 -43.173 23.353  1.000 124.202 ? 55  TYR CCC C   1 
ATOM   3579  O O   . TYR C 3 55  ? -57.535 -42.576 22.416  1.000 126.192 ? 55  TYR CCC O   1 
ATOM   3580  C CB  . TYR C 3 55  ? -54.608 -42.807 24.250  1.000 117.954 ? 55  TYR CCC CB  1 
ATOM   3581  C CG  . TYR C 3 55  ? -54.729 -41.306 24.318  1.000 118.349 ? 55  TYR CCC CG  1 
ATOM   3582  C CD1 . TYR C 3 55  ? -53.920 -40.483 23.560  1.000 117.324 ? 55  TYR CCC CD1 1 
ATOM   3583  C CD2 . TYR C 3 55  ? -55.632 -40.702 25.178  1.000 122.034 ? 55  TYR CCC CD2 1 
ATOM   3584  C CE1 . TYR C 3 55  ? -54.027 -39.102 23.633  1.000 120.395 ? 55  TYR CCC CE1 1 
ATOM   3585  C CE2 . TYR C 3 55  ? -55.769 -39.326 25.249  1.000 123.560 ? 55  TYR CCC CE2 1 
ATOM   3586  C CZ  . TYR C 3 55  ? -54.947 -38.518 24.488  1.000 122.653 ? 55  TYR CCC CZ  1 
ATOM   3587  O OH  . TYR C 3 55  ? -55.066 -37.158 24.561  1.000 124.802 ? 55  TYR CCC OH  1 
ATOM   3588  N N   . TRP C 3 56  ? -57.619 -43.544 24.478  1.000 128.771 ? 56  TRP CCC N   1 
ATOM   3589  C CA  . TRP C 3 56  ? -59.100 -43.617 24.673  1.000 133.319 ? 56  TRP CCC CA  1 
ATOM   3590  C C   . TRP C 3 56  ? -59.769 -43.860 23.309  1.000 130.925 ? 56  TRP CCC C   1 
ATOM   3591  O O   . TRP C 3 56  ? -60.661 -43.074 22.929  1.000 130.562 ? 56  TRP CCC O   1 
ATOM   3592  C CB  . TRP C 3 56  ? -59.703 -42.394 25.403  1.000 140.172 ? 56  TRP CCC CB  1 
ATOM   3593  C CG  . TRP C 3 56  ? -59.076 -42.024 26.717  1.000 143.687 ? 56  TRP CCC CG  1 
ATOM   3594  C CD1 . TRP C 3 56  ? -58.272 -42.795 27.509  1.000 143.876 ? 56  TRP CCC CD1 1 
ATOM   3595  C CD2 . TRP C 3 56  ? -59.193 -40.758 27.393  1.000 147.074 ? 56  TRP CCC CD2 1 
ATOM   3596  N NE1 . TRP C 3 56  ? -57.850 -42.088 28.604  1.000 146.349 ? 56  TRP CCC NE1 1 
ATOM   3597  C CE2 . TRP C 3 56  ? -58.415 -40.840 28.570  1.000 149.403 ? 56  TRP CCC CE2 1 
ATOM   3598  C CE3 . TRP C 3 56  ? -59.853 -39.560 27.107  1.000 148.887 ? 56  TRP CCC CE3 1 
ATOM   3599  C CZ2 . TRP C 3 56  ? -58.294 -39.772 29.460  1.000 152.095 ? 56  TRP CCC CZ2 1 
ATOM   3600  C CZ3 . TRP C 3 56  ? -59.741 -38.511 27.992  1.000 152.853 ? 56  TRP CCC CZ3 1 
ATOM   3601  C CH2 . TRP C 3 56  ? -58.972 -38.615 29.152  1.000 153.425 ? 56  TRP CCC CH2 1 
ATOM   3602  N N   . ALA C 3 57  ? -59.282 -44.875 22.579  1.000 127.742 ? 57  ALA CCC N   1 
ATOM   3603  C CA  . ALA C 3 57  ? -59.939 -45.556 21.435  1.000 128.206 ? 57  ALA CCC CA  1 
ATOM   3604  C C   . ALA C 3 57  ? -59.888 -44.745 20.132  1.000 126.201 ? 57  ALA CCC C   1 
ATOM   3605  O O   . ALA C 3 57  ? -59.943 -45.399 19.044  1.000 121.998 ? 57  ALA CCC O   1 
ATOM   3606  C CB  . ALA C 3 57  ? -61.362 -45.877 21.810  1.000 133.516 ? 57  ALA CCC CB  1 
ATOM   3607  N N   . SER C 3 58  ? -59.792 -43.407 20.229  1.000 127.369 ? 58  SER CCC N   1 
ATOM   3608  C CA  . SER C 3 58  ? -60.103 -42.439 19.138  1.000 130.780 ? 58  SER CCC CA  1 
ATOM   3609  C C   . SER C 3 58  ? -59.251 -41.152 19.172  1.000 130.600 ? 58  SER CCC C   1 
ATOM   3610  O O   . SER C 3 58  ? -59.169 -40.502 18.115  1.000 131.220 ? 58  SER CCC O   1 
ATOM   3611  C CB  . SER C 3 58  ? -61.558 -42.087 19.194  1.000 135.838 ? 58  SER CCC CB  1 
ATOM   3612  O OG  . SER C 3 58  ? -61.872 -41.492 20.445  1.000 138.077 ? 58  SER CCC OG  1 
ATOM   3613  N N   . THR C 3 59  ? -58.688 -40.747 20.318  1.000 131.868 ? 59  THR CCC N   1 
ATOM   3614  C CA  . THR C 3 59  ? -57.876 -39.501 20.462  1.000 132.139 ? 59  THR CCC CA  1 
ATOM   3615  C C   . THR C 3 59  ? -56.455 -39.751 19.938  1.000 127.728 ? 59  THR CCC C   1 
ATOM   3616  O O   . THR C 3 59  ? -55.862 -40.771 20.325  1.000 124.893 ? 59  THR CCC O   1 
ATOM   3617  C CB  . THR C 3 59  ? -57.816 -39.018 21.920  1.000 134.988 ? 59  THR CCC CB  1 
ATOM   3618  O OG1 . THR C 3 59  ? -59.014 -39.378 22.611  1.000 139.706 ? 59  THR CCC OG1 1 
ATOM   3619  C CG2 . THR C 3 59  ? -57.609 -37.523 22.028  1.000 137.180 ? 59  THR CCC CG2 1 
ATOM   3620  N N   . ARG C 3 60  ? -55.920 -38.858 19.103  1.000 127.250 ? 60  ARG CCC N   1 
ATOM   3621  C CA  . ARG C 3 60  ? -54.572 -39.024 18.493  1.000 125.270 ? 60  ARG CCC CA  1 
ATOM   3622  C C   . ARG C 3 60  ? -53.504 -38.456 19.430  1.000 124.639 ? 60  ARG CCC C   1 
ATOM   3623  O O   . ARG C 3 60  ? -53.770 -37.433 20.082  1.000 126.052 ? 60  ARG CCC O   1 
ATOM   3624  C CB  . ARG C 3 60  ? -54.510 -38.334 17.129  1.000 127.219 ? 60  ARG CCC CB  1 
ATOM   3625  C CG  . ARG C 3 60  ? -55.626 -38.753 16.185  1.000 129.472 ? 60  ARG CCC CG  1 
ATOM   3626  C CD  . ARG C 3 60  ? -55.231 -38.706 14.723  1.000 130.434 ? 60  ARG CCC CD  1 
ATOM   3627  N NE  . ARG C 3 60  ? -54.714 -37.407 14.326  1.000 133.061 ? 60  ARG CCC NE  1 
ATOM   3628  C CZ  . ARG C 3 60  ? -55.456 -36.318 14.159  1.000 138.518 ? 60  ARG CCC CZ  1 
ATOM   3629  N NH1 . ARG C 3 60  ? -56.764 -36.358 14.370  1.000 141.689 ? 60  ARG CCC NH1 1 
ATOM   3630  N NH2 . ARG C 3 60  ? -54.881 -35.186 13.787  1.000 140.814 ? 60  ARG CCC NH2 1 
ATOM   3631  N N   . GLU C 3 61  ? -52.338 -39.102 19.482  1.000 124.037 ? 61  GLU CCC N   1 
ATOM   3632  C CA  . GLU C 3 61  ? -51.132 -38.596 20.189  1.000 127.647 ? 61  GLU CCC CA  1 
ATOM   3633  C C   . GLU C 3 61  ? -50.464 -37.523 19.315  1.000 129.905 ? 61  GLU CCC C   1 
ATOM   3634  O O   . GLU C 3 61  ? -50.635 -37.548 18.082  1.000 128.406 ? 61  GLU CCC O   1 
ATOM   3635  C CB  . GLU C 3 61  ? -50.197 -39.765 20.515  1.000 129.007 ? 61  GLU CCC CB  1 
ATOM   3636  C CG  . GLU C 3 61  ? -48.917 -39.382 21.258  1.000 133.783 ? 61  GLU CCC CG  1 
ATOM   3637  C CD  . GLU C 3 61  ? -49.083 -38.850 22.677  1.000 137.582 ? 61  GLU CCC CD  1 
ATOM   3638  O OE1 . GLU C 3 61  ? -49.507 -37.680 22.832  1.000 141.239 ? 61  GLU CCC OE1 1 
ATOM   3639  O OE2 . GLU C 3 61  ? -48.781 -39.603 23.634  1.000 138.346 ? 61  GLU CCC OE2 1 
ATOM   3640  N N   . SER C 3 62  ? -49.751 -36.589 19.945  1.000 134.413 ? 62  SER CCC N   1 
ATOM   3641  C CA  . SER C 3 62  ? -48.896 -35.581 19.272  1.000 136.289 ? 62  SER CCC CA  1 
ATOM   3642  C C   . SER C 3 62  ? -47.931 -36.306 18.329  1.000 132.266 ? 62  SER CCC C   1 
ATOM   3643  O O   . SER C 3 62  ? -47.369 -37.346 18.747  1.000 126.983 ? 62  SER CCC O   1 
ATOM   3644  C CB  . SER C 3 62  ? -48.158 -34.731 20.288  1.000 141.518 ? 62  SER CCC CB  1 
ATOM   3645  O OG  . SER C 3 62  ? -47.589 -35.533 21.322  1.000 141.068 ? 62  SER CCC OG  1 
ATOM   3646  N N   . GLY C 3 63  ? -47.775 -35.783 17.107  1.000 133.909 ? 63  GLY CCC N   1 
ATOM   3647  C CA  . GLY C 3 63  ? -46.790 -36.239 16.100  1.000 133.625 ? 63  GLY CCC CA  1 
ATOM   3648  C C   . GLY C 3 63  ? -47.345 -37.316 15.183  1.000 129.817 ? 63  GLY CCC C   1 
ATOM   3649  O O   . GLY C 3 63  ? -46.530 -38.054 14.560  1.000 127.620 ? 63  GLY CCC O   1 
ATOM   3650  N N   . VAL C 3 64  ? -48.679 -37.384 15.096  1.000 126.502 ? 64  VAL CCC N   1 
ATOM   3651  C CA  . VAL C 3 64  ? -49.453 -38.445 14.394  1.000 122.360 ? 64  VAL CCC CA  1 
ATOM   3652  C C   . VAL C 3 64  ? -50.333 -37.780 13.351  1.000 124.124 ? 64  VAL CCC C   1 
ATOM   3653  O O   . VAL C 3 64  ? -51.155 -36.932 13.682  1.000 123.396 ? 64  VAL CCC O   1 
ATOM   3654  C CB  . VAL C 3 64  ? -50.309 -39.265 15.371  1.000 120.023 ? 64  VAL CCC CB  1 
ATOM   3655  C CG1 . VAL C 3 64  ? -51.104 -40.341 14.648  1.000 118.828 ? 64  VAL CCC CG1 1 
ATOM   3656  C CG2 . VAL C 3 64  ? -49.464 -39.872 16.478  1.000 119.344 ? 64  VAL CCC CG2 1 
ATOM   3657  N N   . PRO C 3 65  ? -50.189 -38.165 12.069  1.000 127.973 ? 65  PRO CCC N   1 
ATOM   3658  C CA  . PRO C 3 65  ? -50.984 -37.577 10.993  1.000 133.400 ? 65  PRO CCC CA  1 
ATOM   3659  C C   . PRO C 3 65  ? -52.506 -37.719 11.173  1.000 135.711 ? 65  PRO CCC C   1 
ATOM   3660  O O   . PRO C 3 65  ? -52.937 -38.571 11.927  1.000 133.653 ? 65  PRO CCC O   1 
ATOM   3661  C CB  . PRO C 3 65  ? -50.521 -38.349 9.744   1.000 134.096 ? 65  PRO CCC CB  1 
ATOM   3662  C CG  . PRO C 3 65  ? -49.143 -38.866 10.101  1.000 131.589 ? 65  PRO CCC CG  1 
ATOM   3663  C CD  . PRO C 3 65  ? -49.218 -39.157 11.582  1.000 128.131 ? 65  PRO CCC CD  1 
ATOM   3664  N N   . ASP C 3 66  ? -53.258 -36.876 10.451  1.000 140.772 ? 66  ASP CCC N   1 
ATOM   3665  C CA  . ASP C 3 66  ? -54.747 -36.810 10.409  1.000 142.963 ? 66  ASP CCC CA  1 
ATOM   3666  C C   . ASP C 3 66  ? -55.321 -38.132 9.889   1.000 140.893 ? 66  ASP CCC C   1 
ATOM   3667  O O   . ASP C 3 66  ? -56.396 -38.536 10.372  1.000 141.261 ? 66  ASP CCC O   1 
ATOM   3668  C CB  . ASP C 3 66  ? -55.241 -35.679 9.497   1.000 149.050 ? 66  ASP CCC CB  1 
ATOM   3669  C CG  . ASP C 3 66  ? -54.327 -34.463 9.429   1.000 152.066 ? 66  ASP CCC CG  1 
ATOM   3670  O OD1 . ASP C 3 66  ? -53.349 -34.509 8.650   1.000 153.128 ? 66  ASP CCC OD1 1 
ATOM   3671  O OD2 . ASP C 3 66  ? -54.592 -33.476 10.154  1.000 154.668 ? 66  ASP CCC OD2 1 
ATOM   3672  N N   . ARG C 3 67  ? -54.637 -38.767 8.932   1.000 138.078 ? 67  ARG CCC N   1 
ATOM   3673  C CA  . ARG C 3 67  ? -55.135 -39.954 8.183   1.000 136.493 ? 67  ARG CCC CA  1 
ATOM   3674  C C   . ARG C 3 67  ? -55.365 -41.132 9.138   1.000 129.937 ? 67  ARG CCC C   1 
ATOM   3675  O O   . ARG C 3 67  ? -56.148 -42.031 8.785   1.000 128.497 ? 67  ARG CCC O   1 
ATOM   3676  C CB  . ARG C 3 67  ? -54.179 -40.314 7.040   1.000 138.156 ? 67  ARG CCC CB  1 
ATOM   3677  C CG  . ARG C 3 67  ? -52.743 -40.609 7.444   1.000 135.062 ? 67  ARG CCC CG  1 
ATOM   3678  C CD  . ARG C 3 67  ? -51.984 -41.209 6.270   1.000 135.726 ? 67  ARG CCC CD  1 
ATOM   3679  N NE  . ARG C 3 67  ? -50.580 -41.455 6.560   1.000 134.167 ? 67  ARG CCC NE  1 
ATOM   3680  C CZ  . ARG C 3 67  ? -49.613 -40.547 6.473   1.000 136.867 ? 67  ARG CCC CZ  1 
ATOM   3681  N NH1 . ARG C 3 67  ? -49.889 -39.307 6.100   1.000 140.603 ? 67  ARG CCC NH1 1 
ATOM   3682  N NH2 . ARG C 3 67  ? -48.365 -40.879 6.763   1.000 137.067 ? 67  ARG CCC NH2 1 
ATOM   3683  N N   . PHE C 3 68  ? -54.705 -41.129 10.296  1.000 125.873 ? 68  PHE CCC N   1 
ATOM   3684  C CA  . PHE C 3 68  ? -54.935 -42.100 11.397  1.000 124.296 ? 68  PHE CCC CA  1 
ATOM   3685  C C   . PHE C 3 68  ? -56.150 -41.670 12.224  1.000 125.907 ? 68  PHE CCC C   1 
ATOM   3686  O O   . PHE C 3 68  ? -56.223 -40.497 12.641  1.000 125.719 ? 68  PHE CCC O   1 
ATOM   3687  C CB  . PHE C 3 68  ? -53.703 -42.214 12.296  1.000 120.706 ? 68  PHE CCC CB  1 
ATOM   3688  C CG  . PHE C 3 68  ? -52.571 -42.992 11.682  1.000 118.818 ? 68  PHE CCC CG  1 
ATOM   3689  C CD1 . PHE C 3 68  ? -52.516 -44.369 11.803  1.000 117.691 ? 68  PHE CCC CD1 1 
ATOM   3690  C CD2 . PHE C 3 68  ? -51.569 -42.348 10.975  1.000 119.755 ? 68  PHE CCC CD2 1 
ATOM   3691  C CE1 . PHE C 3 68  ? -51.475 -45.088 11.239  1.000 117.997 ? 68  PHE CCC CE1 1 
ATOM   3692  C CE2 . PHE C 3 68  ? -50.525 -43.068 10.414  1.000 119.788 ? 68  PHE CCC CE2 1 
ATOM   3693  C CZ  . PHE C 3 68  ? -50.480 -44.437 10.547  1.000 119.028 ? 68  PHE CCC CZ  1 
ATOM   3694  N N   . SER C 3 69  ? -57.069 -42.606 12.461  1.000 126.787 ? 69  SER CCC N   1 
ATOM   3695  C CA  . SER C 3 69  ? -58.314 -42.387 13.235  1.000 129.364 ? 69  SER CCC CA  1 
ATOM   3696  C C   . SER C 3 69  ? -58.850 -43.733 13.719  1.000 129.670 ? 69  SER CCC C   1 
ATOM   3697  O O   . SER C 3 69  ? -58.923 -44.677 12.906  1.000 130.629 ? 69  SER CCC O   1 
ATOM   3698  C CB  . SER C 3 69  ? -59.338 -41.658 12.415  1.000 134.265 ? 69  SER CCC CB  1 
ATOM   3699  O OG  . SER C 3 69  ? -59.581 -42.346 11.198  1.000 136.894 ? 69  SER CCC OG  1 
ATOM   3700  N N   . GLY C 3 70  ? -59.197 -43.801 15.001  1.000 129.403 ? 70  GLY CCC N   1 
ATOM   3701  C CA  . GLY C 3 70  ? -59.743 -45.004 15.649  1.000 130.647 ? 70  GLY CCC CA  1 
ATOM   3702  C C   . GLY C 3 70  ? -61.198 -44.791 15.994  1.000 134.840 ? 70  GLY CCC C   1 
ATOM   3703  O O   . GLY C 3 70  ? -61.577 -43.642 16.271  1.000 133.795 ? 70  GLY CCC O   1 
ATOM   3704  N N   . SER C 3 71  ? -61.991 -45.857 15.919  1.000 139.950 ? 71  SER CCC N   1 
ATOM   3705  C CA  . SER C 3 71  ? -63.392 -45.917 16.404  1.000 147.174 ? 71  SER CCC CA  1 
ATOM   3706  C C   . SER C 3 71  ? -63.539 -47.180 17.254  1.000 148.648 ? 71  SER CCC C   1 
ATOM   3707  O O   . SER C 3 71  ? -62.542 -47.948 17.331  1.000 146.272 ? 71  SER CCC O   1 
ATOM   3708  C CB  . SER C 3 71  ? -64.370 -45.891 15.264  1.000 152.615 ? 71  SER CCC CB  1 
ATOM   3709  O OG  . SER C 3 71  ? -64.145 -46.983 14.387  1.000 153.287 ? 71  SER CCC OG  1 
ATOM   3710  N N   . GLY C 3 72  ? -64.703 -47.370 17.887  1.000 152.598 ? 72  GLY CCC N   1 
ATOM   3711  C CA  . GLY C 3 72  ? -64.952 -48.552 18.729  1.000 153.279 ? 72  GLY CCC CA  1 
ATOM   3712  C C   . GLY C 3 72  ? -66.089 -48.379 19.717  1.000 157.253 ? 72  GLY CCC C   1 
ATOM   3713  O O   . GLY C 3 72  ? -66.203 -47.298 20.330  1.000 155.423 ? 72  GLY CCC O   1 
ATOM   3714  N N   . SER C 3 73  ? -66.857 -49.457 19.892  1.000 161.736 ? 73  SER CCC N   1 
ATOM   3715  C CA  . SER C 3 73  ? -68.082 -49.549 20.722  1.000 166.897 ? 73  SER CCC CA  1 
ATOM   3716  C C   . SER C 3 73  ? -67.966 -50.775 21.637  1.000 166.988 ? 73  SER CCC C   1 
ATOM   3717  O O   . SER C 3 73  ? -68.451 -51.856 21.241  1.000 171.164 ? 73  SER CCC O   1 
ATOM   3718  C CB  . SER C 3 73  ? -69.309 -49.594 19.825  1.000 172.989 ? 73  SER CCC CB  1 
ATOM   3719  O OG  . SER C 3 73  ? -70.508 -49.791 20.563  1.000 178.280 ? 73  SER CCC OG  1 
ATOM   3720  N N   . GLY C 3 74  ? -67.289 -50.620 22.782  1.000 162.522 ? 74  GLY CCC N   1 
ATOM   3721  C CA  . GLY C 3 74  ? -67.331 -51.566 23.917  1.000 164.204 ? 74  GLY CCC CA  1 
ATOM   3722  C C   . GLY C 3 74  ? -66.338 -52.712 23.799  1.000 161.190 ? 74  GLY CCC C   1 
ATOM   3723  O O   . GLY C 3 74  ? -65.357 -52.704 24.562  1.000 155.473 ? 74  GLY CCC O   1 
ATOM   3724  N N   . THR C 3 75  ? -66.616 -53.685 22.920  1.000 165.101 ? 75  THR CCC N   1 
ATOM   3725  C CA  . THR C 3 75  ? -65.846 -54.949 22.741  1.000 163.980 ? 75  THR CCC CA  1 
ATOM   3726  C C   . THR C 3 75  ? -65.171 -54.993 21.362  1.000 161.888 ? 75  THR CCC C   1 
ATOM   3727  O O   . THR C 3 75  ? -64.357 -55.917 21.157  1.000 158.564 ? 75  THR CCC O   1 
ATOM   3728  C CB  . THR C 3 75  ? -66.747 -56.180 22.922  1.000 170.426 ? 75  THR CCC CB  1 
ATOM   3729  O OG1 . THR C 3 75  ? -67.691 -56.238 21.849  1.000 174.660 ? 75  THR CCC OG1 1 
ATOM   3730  C CG2 . THR C 3 75  ? -67.479 -56.184 24.247  1.000 174.560 ? 75  THR CCC CG2 1 
ATOM   3731  N N   . ASP C 3 76  ? -65.501 -54.044 20.471  1.000 163.804 ? 76  ASP CCC N   1 
ATOM   3732  C CA  . ASP C 3 76  ? -65.069 -53.987 19.045  1.000 162.382 ? 76  ASP CCC CA  1 
ATOM   3733  C C   . ASP C 3 76  ? -64.456 -52.621 18.735  1.000 157.266 ? 76  ASP CCC C   1 
ATOM   3734  O O   . ASP C 3 76  ? -65.180 -51.622 18.900  1.000 158.238 ? 76  ASP CCC O   1 
ATOM   3735  C CB  . ASP C 3 76  ? -66.253 -54.221 18.107  1.000 168.968 ? 76  ASP CCC CB  1 
ATOM   3736  C CG  . ASP C 3 76  ? -66.723 -55.658 18.117  1.000 176.932 ? 76  ASP CCC CG  1 
ATOM   3737  O OD1 . ASP C 3 76  ? -65.867 -56.533 17.893  1.000 176.102 ? 76  ASP CCC OD1 1 
ATOM   3738  O OD2 . ASP C 3 76  ? -67.931 -55.885 18.356  1.000 187.138 ? 76  ASP CCC OD2 1 
ATOM   3739  N N   . PHE C 3 77  ? -63.195 -52.596 18.275  1.000 152.324 ? 77  PHE CCC N   1 
ATOM   3740  C CA  . PHE C 3 77  ? -62.409 -51.371 17.953  1.000 148.512 ? 77  PHE CCC CA  1 
ATOM   3741  C C   . PHE C 3 77  ? -61.705 -51.531 16.604  1.000 145.440 ? 77  PHE CCC C   1 
ATOM   3742  O O   . PHE C 3 77  ? -61.271 -52.652 16.269  1.000 143.017 ? 77  PHE CCC O   1 
ATOM   3743  C CB  . PHE C 3 77  ? -61.391 -51.073 19.055  1.000 146.504 ? 77  PHE CCC CB  1 
ATOM   3744  C CG  . PHE C 3 77  ? -62.020 -51.028 20.420  1.000 150.691 ? 77  PHE CCC CG  1 
ATOM   3745  C CD1 . PHE C 3 77  ? -62.642 -49.876 20.877  1.000 153.209 ? 77  PHE CCC CD1 1 
ATOM   3746  C CD2 . PHE C 3 77  ? -62.061 -52.162 21.215  1.000 153.715 ? 77  PHE CCC CD2 1 
ATOM   3747  C CE1 . PHE C 3 77  ? -63.261 -49.844 22.118  1.000 156.082 ? 77  PHE CCC CE1 1 
ATOM   3748  C CE2 . PHE C 3 77  ? -62.677 -52.131 22.457  1.000 156.873 ? 77  PHE CCC CE2 1 
ATOM   3749  C CZ  . PHE C 3 77  ? -63.266 -50.970 22.910  1.000 157.970 ? 77  PHE CCC CZ  1 
ATOM   3750  N N   . THR C 3 78  ? -61.585 -50.423 15.867  1.000 143.961 ? 78  THR CCC N   1 
ATOM   3751  C CA  . THR C 3 78  ? -60.975 -50.374 14.516  1.000 142.721 ? 78  THR CCC CA  1 
ATOM   3752  C C   . THR C 3 78  ? -60.018 -49.191 14.403  1.000 140.349 ? 78  THR CCC C   1 
ATOM   3753  O O   . THR C 3 78  ? -60.336 -48.107 14.933  1.000 140.564 ? 78  THR CCC O   1 
ATOM   3754  C CB  . THR C 3 78  ? -62.026 -50.247 13.414  1.000 146.972 ? 78  THR CCC CB  1 
ATOM   3755  O OG1 . THR C 3 78  ? -63.108 -51.109 13.760  1.000 152.456 ? 78  THR CCC OG1 1 
ATOM   3756  C CG2 . THR C 3 78  ? -61.475 -50.603 12.053  1.000 146.863 ? 78  THR CCC CG2 1 
ATOM   3757  N N   . LEU C 3 79  ? -58.896 -49.425 13.722  1.000 139.353 ? 79  LEU CCC N   1 
ATOM   3758  C CA  . LEU C 3 79  ? -57.913 -48.397 13.301  1.000 135.978 ? 79  LEU CCC CA  1 
ATOM   3759  C C   . LEU C 3 79  ? -58.000 -48.247 11.785  1.000 136.101 ? 79  LEU CCC C   1 
ATOM   3760  O O   . LEU C 3 79  ? -57.800 -49.252 11.077  1.000 137.933 ? 79  LEU CCC O   1 
ATOM   3761  C CB  . LEU C 3 79  ? -56.505 -48.830 13.713  1.000 132.900 ? 79  LEU CCC CB  1 
ATOM   3762  C CG  . LEU C 3 79  ? -55.376 -47.916 13.238  1.000 130.382 ? 79  LEU CCC CG  1 
ATOM   3763  C CD1 . LEU C 3 79  ? -55.708 -46.455 13.491  1.000 130.340 ? 79  LEU CCC CD1 1 
ATOM   3764  C CD2 . LEU C 3 79  ? -54.066 -48.278 13.917  1.000 127.730 ? 79  LEU CCC CD2 1 
ATOM   3765  N N   . THR C 3 80  ? -58.278 -47.033 11.321  1.000 134.753 ? 80  THR CCC N   1 
ATOM   3766  C CA  . THR C 3 80  ? -58.437 -46.721 9.886   1.000 136.981 ? 80  THR CCC CA  1 
ATOM   3767  C C   . THR C 3 80  ? -57.345 -45.743 9.461   1.000 135.027 ? 80  THR CCC C   1 
ATOM   3768  O O   . THR C 3 80  ? -57.238 -44.667 10.088  1.000 133.785 ? 80  THR CCC O   1 
ATOM   3769  C CB  . THR C 3 80  ? -59.841 -46.182 9.620   1.000 141.474 ? 80  THR CCC CB  1 
ATOM   3770  O OG1 . THR C 3 80  ? -60.708 -46.921 10.481  1.000 140.846 ? 80  THR CCC OG1 1 
ATOM   3771  C CG2 . THR C 3 80  ? -60.236 -46.308 8.165   1.000 145.599 ? 80  THR CCC CG2 1 
ATOM   3772  N N   . ILE C 3 81  ? -56.580 -46.131 8.438   1.000 135.277 ? 81  ILE CCC N   1 
ATOM   3773  C CA  . ILE C 3 81  ? -55.481 -45.332 7.817   1.000 133.553 ? 81  ILE CCC CA  1 
ATOM   3774  C C   . ILE C 3 81  ? -55.933 -44.901 6.420   1.000 136.558 ? 81  ILE CCC C   1 
ATOM   3775  O O   . ILE C 3 81  ? -55.450 -45.504 5.443   1.000 138.230 ? 81  ILE CCC O   1 
ATOM   3776  C CB  . ILE C 3 81  ? -54.176 -46.158 7.741   1.000 130.472 ? 81  ILE CCC CB  1 
ATOM   3777  C CG1 . ILE C 3 81  ? -53.918 -46.970 9.015   1.000 126.086 ? 81  ILE CCC CG1 1 
ATOM   3778  C CG2 . ILE C 3 81  ? -53.000 -45.258 7.373   1.000 129.932 ? 81  ILE CCC CG2 1 
ATOM   3779  C CD1 . ILE C 3 81  ? -52.685 -47.839 8.953   1.000 123.486 ? 81  ILE CCC CD1 1 
ATOM   3780  N N   . SER C 3 82  ? -56.824 -43.914 6.306   1.000 138.987 ? 82  SER CCC N   1 
ATOM   3781  C CA  . SER C 3 82  ? -57.196 -43.339 4.988   1.000 144.884 ? 82  SER CCC CA  1 
ATOM   3782  C C   . SER C 3 82  ? -55.905 -42.840 4.325   1.000 144.682 ? 82  SER CCC C   1 
ATOM   3783  O O   . SER C 3 82  ? -55.001 -42.428 5.070   1.000 141.669 ? 82  SER CCC O   1 
ATOM   3784  C CB  . SER C 3 82  ? -58.256 -42.263 5.104   1.000 149.324 ? 82  SER CCC CB  1 
ATOM   3785  O OG  . SER C 3 82  ? -57.707 -41.015 5.502   1.000 149.905 ? 82  SER CCC OG  1 
ATOM   3786  N N   . SER C 3 83  ? -55.789 -42.960 2.996   1.000 148.307 ? 83  SER CCC N   1 
ATOM   3787  C CA  . SER C 3 83  ? -54.647 -42.446 2.189   1.000 148.070 ? 83  SER CCC CA  1 
ATOM   3788  C C   . SER C 3 83  ? -53.318 -43.014 2.700   1.000 142.255 ? 83  SER CCC C   1 
ATOM   3789  O O   . SER C 3 83  ? -52.478 -42.214 3.148   1.000 138.855 ? 83  SER CCC O   1 
ATOM   3790  C CB  . SER C 3 83  ? -54.611 -40.935 2.200   1.000 151.065 ? 83  SER CCC CB  1 
ATOM   3791  O OG  . SER C 3 83  ? -55.816 -40.393 1.686   1.000 158.749 ? 83  SER CCC OG  1 
ATOM   3792  N N   . LEU C 3 84  ? -53.125 -44.336 2.633   1.000 140.957 ? 84  LEU CCC N   1 
ATOM   3793  C CA  . LEU C 3 84  ? -51.884 -45.000 3.125   1.000 137.484 ? 84  LEU CCC CA  1 
ATOM   3794  C C   . LEU C 3 84  ? -50.683 -44.356 2.433   1.000 139.840 ? 84  LEU CCC C   1 
ATOM   3795  O O   . LEU C 3 84  ? -50.825 -43.953 1.265   1.000 146.194 ? 84  LEU CCC O   1 
ATOM   3796  C CB  . LEU C 3 84  ? -51.918 -46.507 2.847   1.000 136.623 ? 84  LEU CCC CB  1 
ATOM   3797  C CG  . LEU C 3 84  ? -50.752 -47.308 3.433   1.000 132.251 ? 84  LEU CCC CG  1 
ATOM   3798  C CD1 . LEU C 3 84  ? -50.789 -47.282 4.948   1.000 128.629 ? 84  LEU CCC CD1 1 
ATOM   3799  C CD2 . LEU C 3 84  ? -50.763 -48.745 2.938   1.000 133.630 ? 84  LEU CCC CD2 1 
ATOM   3800  N N   . GLN C 3 85  ? -49.548 -44.267 3.126   1.000 138.274 ? 85  GLN CCC N   1 
ATOM   3801  C CA  . GLN C 3 85  ? -48.326 -43.603 2.603   1.000 141.599 ? 85  GLN CCC CA  1 
ATOM   3802  C C   . GLN C 3 85  ? -47.119 -44.529 2.758   1.000 139.733 ? 85  GLN CCC C   1 
ATOM   3803  O O   . GLN C 3 85  ? -47.239 -45.559 3.444   1.000 135.984 ? 85  GLN CCC O   1 
ATOM   3804  C CB  . GLN C 3 85  ? -48.088 -42.264 3.310   1.000 142.974 ? 85  GLN CCC CB  1 
ATOM   3805  C CG  . GLN C 3 85  ? -49.129 -41.196 2.988   1.000 146.985 ? 85  GLN CCC CG  1 
ATOM   3806  C CD  . GLN C 3 85  ? -49.091 -40.603 1.598   1.000 152.927 ? 85  GLN CCC CD  1 
ATOM   3807  O OE1 . GLN C 3 85  ? -49.335 -39.411 1.416   1.000 156.895 ? 85  GLN CCC OE1 1 
ATOM   3808  N NE2 . GLN C 3 85  ? -48.819 -41.429 0.599   1.000 154.096 ? 85  GLN CCC NE2 1 
ATOM   3809  N N   . ALA C 3 86  ? -46.016 -44.154 2.108   1.000 142.240 ? 86  ALA CCC N   1 
ATOM   3810  C CA  . ALA C 3 86  ? -44.675 -44.765 2.222   1.000 143.775 ? 86  ALA CCC CA  1 
ATOM   3811  C C   . ALA C 3 86  ? -44.423 -45.242 3.660   1.000 143.511 ? 86  ALA CCC C   1 
ATOM   3812  O O   . ALA C 3 86  ? -44.495 -46.463 3.907   1.000 142.288 ? 86  ALA CCC O   1 
ATOM   3813  C CB  . ALA C 3 86  ? -43.640 -43.752 1.786   1.000 145.997 ? 86  ALA CCC CB  1 
ATOM   3814  N N   . GLU C 3 87  ? -44.190 -44.301 4.582   1.000 145.443 ? 87  GLU CCC N   1 
ATOM   3815  C CA  . GLU C 3 87  ? -43.569 -44.558 5.915   1.000 142.011 ? 87  GLU CCC CA  1 
ATOM   3816  C C   . GLU C 3 87  ? -44.588 -45.169 6.889   1.000 133.029 ? 87  GLU CCC C   1 
ATOM   3817  O O   . GLU C 3 87  ? -44.226 -45.313 8.075   1.000 128.835 ? 87  GLU CCC O   1 
ATOM   3818  C CB  . GLU C 3 87  ? -42.940 -43.274 6.475   1.000 148.279 ? 87  GLU CCC CB  1 
ATOM   3819  C CG  . GLU C 3 87  ? -43.870 -42.064 6.496   1.000 152.019 ? 87  GLU CCC CG  1 
ATOM   3820  C CD  . GLU C 3 87  ? -43.339 -40.842 7.234   1.000 154.828 ? 87  GLU CCC CD  1 
ATOM   3821  O OE1 . GLU C 3 87  ? -42.592 -41.020 8.231   1.000 154.216 ? 87  GLU CCC OE1 1 
ATOM   3822  O OE2 . GLU C 3 87  ? -43.676 -39.708 6.812   1.000 158.042 ? 87  GLU CCC OE2 1 
ATOM   3823  N N   . ASP C 3 88  ? -45.789 -45.530 6.415   1.000 129.263 ? 88  ASP CCC N   1 
ATOM   3824  C CA  . ASP C 3 88  ? -46.864 -46.169 7.224   1.000 126.892 ? 88  ASP CCC CA  1 
ATOM   3825  C C   . ASP C 3 88  ? -46.677 -47.688 7.275   1.000 126.136 ? 88  ASP CCC C   1 
ATOM   3826  O O   . ASP C 3 88  ? -47.370 -48.334 8.091   1.000 123.867 ? 88  ASP CCC O   1 
ATOM   3827  C CB  . ASP C 3 88  ? -48.260 -45.874 6.674   1.000 127.925 ? 88  ASP CCC CB  1 
ATOM   3828  C CG  . ASP C 3 88  ? -48.708 -44.435 6.845   1.000 129.180 ? 88  ASP CCC CG  1 
ATOM   3829  O OD1 . ASP C 3 88  ? -48.424 -43.852 7.902   1.000 128.160 ? 88  ASP CCC OD1 1 
ATOM   3830  O OD2 . ASP C 3 88  ? -49.354 -43.912 5.922   1.000 133.545 ? 88  ASP CCC OD2 1 
ATOM   3831  N N   . VAL C 3 89  ? -45.803 -48.242 6.430   1.000 128.061 ? 89  VAL CCC N   1 
ATOM   3832  C CA  . VAL C 3 89  ? -45.439 -49.689 6.460   1.000 129.731 ? 89  VAL CCC CA  1 
ATOM   3833  C C   . VAL C 3 89  ? -44.836 -49.989 7.836   1.000 128.575 ? 89  VAL CCC C   1 
ATOM   3834  O O   . VAL C 3 89  ? -43.835 -49.321 8.203   1.000 127.671 ? 89  VAL CCC O   1 
ATOM   3835  C CB  . VAL C 3 89  ? -44.459 -50.070 5.334   1.000 132.551 ? 89  VAL CCC CB  1 
ATOM   3836  C CG1 . VAL C 3 89  ? -43.971 -51.508 5.457   1.000 134.355 ? 89  VAL CCC CG1 1 
ATOM   3837  C CG2 . VAL C 3 89  ? -45.063 -49.849 3.966   1.000 134.441 ? 89  VAL CCC CG2 1 
ATOM   3838  N N   . ALA C 3 90  ? -45.420 -50.958 8.550   1.000 127.444 ? 90  ALA CCC N   1 
ATOM   3839  C CA  . ALA C 3 90  ? -44.983 -51.417 9.886   1.000 125.437 ? 90  ALA CCC CA  1 
ATOM   3840  C C   . ALA C 3 90  ? -45.966 -52.459 10.436  1.000 125.147 ? 90  ALA CCC C   1 
ATOM   3841  O O   . ALA C 3 90  ? -46.969 -52.771 9.761   1.000 122.621 ? 90  ALA CCC O   1 
ATOM   3842  C CB  . ALA C 3 90  ? -44.880 -50.232 10.818  1.000 124.248 ? 90  ALA CCC CB  1 
ATOM   3843  N N   . VAL C 3 91  ? -45.667 -52.962 11.638  1.000 125.228 ? 91  VAL CCC N   1 
ATOM   3844  C CA  . VAL C 3 91  ? -46.557 -53.821 12.476  1.000 124.022 ? 91  VAL CCC CA  1 
ATOM   3845  C C   . VAL C 3 91  ? -47.415 -52.903 13.355  1.000 121.393 ? 91  VAL CCC C   1 
ATOM   3846  O O   . VAL C 3 91  ? -46.876 -51.899 13.874  1.000 119.478 ? 91  VAL CCC O   1 
ATOM   3847  C CB  . VAL C 3 91  ? -45.748 -54.792 13.354  1.000 126.585 ? 91  VAL CCC CB  1 
ATOM   3848  C CG1 . VAL C 3 91  ? -46.615 -55.953 13.820  1.000 128.103 ? 91  VAL CCC CG1 1 
ATOM   3849  C CG2 . VAL C 3 91  ? -44.480 -55.291 12.668  1.000 129.722 ? 91  VAL CCC CG2 1 
ATOM   3850  N N   . TYR C 3 92  ? -48.694 -53.235 13.531  1.000 120.874 ? 92  TYR CCC N   1 
ATOM   3851  C CA  . TYR C 3 92  ? -49.670 -52.437 14.319  1.000 119.010 ? 92  TYR CCC CA  1 
ATOM   3852  C C   . TYR C 3 92  ? -50.261 -53.336 15.404  1.000 120.680 ? 92  TYR CCC C   1 
ATOM   3853  O O   . TYR C 3 92  ? -50.797 -54.410 15.062  1.000 124.572 ? 92  TYR CCC O   1 
ATOM   3854  C CB  . TYR C 3 92  ? -50.746 -51.840 13.406  1.000 119.668 ? 92  TYR CCC CB  1 
ATOM   3855  C CG  . TYR C 3 92  ? -50.240 -50.730 12.524  1.000 119.418 ? 92  TYR CCC CG  1 
ATOM   3856  C CD1 . TYR C 3 92  ? -49.604 -51.000 11.323  1.000 122.839 ? 92  TYR CCC CD1 1 
ATOM   3857  C CD2 . TYR C 3 92  ? -50.359 -49.408 12.905  1.000 118.604 ? 92  TYR CCC CD2 1 
ATOM   3858  C CE1 . TYR C 3 92  ? -49.106 -49.984 10.520  1.000 124.352 ? 92  TYR CCC CE1 1 
ATOM   3859  C CE2 . TYR C 3 92  ? -49.873 -48.381 12.113  1.000 120.433 ? 92  TYR CCC CE2 1 
ATOM   3860  C CZ  . TYR C 3 92  ? -49.236 -48.665 10.918  1.000 122.728 ? 92  TYR CCC CZ  1 
ATOM   3861  O OH  . TYR C 3 92  ? -48.758 -47.655 10.130  1.000 123.124 ? 92  TYR CCC OH  1 
ATOM   3862  N N   . TYR C 3 93  ? -50.124 -52.924 16.668  1.000 120.849 ? 93  TYR CCC N   1 
ATOM   3863  C CA  . TYR C 3 93  ? -50.679 -53.616 17.863  1.000 122.284 ? 93  TYR CCC CA  1 
ATOM   3864  C C   . TYR C 3 93  ? -51.738 -52.712 18.513  1.000 121.843 ? 93  TYR CCC C   1 
ATOM   3865  O O   . TYR C 3 93  ? -51.530 -51.486 18.581  1.000 119.998 ? 93  TYR CCC O   1 
ATOM   3866  C CB  . TYR C 3 93  ? -49.572 -53.986 18.863  1.000 121.325 ? 93  TYR CCC CB  1 
ATOM   3867  C CG  . TYR C 3 93  ? -48.381 -54.729 18.302  1.000 121.301 ? 93  TYR CCC CG  1 
ATOM   3868  C CD1 . TYR C 3 93  ? -47.305 -54.038 17.773  1.000 121.969 ? 93  TYR CCC CD1 1 
ATOM   3869  C CD2 . TYR C 3 93  ? -48.295 -56.111 18.326  1.000 123.411 ? 93  TYR CCC CD2 1 
ATOM   3870  C CE1 . TYR C 3 93  ? -46.190 -54.687 17.264  1.000 124.437 ? 93  TYR CCC CE1 1 
ATOM   3871  C CE2 . TYR C 3 93  ? -47.191 -56.779 17.811  1.000 126.702 ? 93  TYR CCC CE2 1 
ATOM   3872  C CZ  . TYR C 3 93  ? -46.133 -56.069 17.266  1.000 126.658 ? 93  TYR CCC CZ  1 
ATOM   3873  O OH  . TYR C 3 93  ? -45.031 -56.691 16.738  1.000 127.414 ? 93  TYR CCC OH  1 
ATOM   3874  N N   . CYS C 3 94  ? -52.852 -53.293 18.963  1.000 124.182 ? 94  CYS CCC N   1 
ATOM   3875  C CA  . CYS C 3 94  ? -53.784 -52.663 19.935  1.000 126.608 ? 94  CYS CCC CA  1 
ATOM   3876  C C   . CYS C 3 94  ? -53.493 -53.223 21.336  1.000 128.810 ? 94  CYS CCC C   1 
ATOM   3877  O O   . CYS C 3 94  ? -53.130 -54.421 21.436  1.000 130.988 ? 94  CYS CCC O   1 
ATOM   3878  C CB  . CYS C 3 94  ? -55.237 -52.907 19.558  1.000 130.534 ? 94  CYS CCC CB  1 
ATOM   3879  S SG  . CYS C 3 94  ? -55.710 -54.652 19.639  1.000 137.417 ? 94  CYS CCC SG  1 
ATOM   3880  N N   . GLN C 3 95  ? -53.641 -52.383 22.368  1.000 128.789 ? 95  GLN CCC N   1 
ATOM   3881  C CA  . GLN C 3 95  ? -53.395 -52.701 23.801  1.000 129.243 ? 95  GLN CCC CA  1 
ATOM   3882  C C   . GLN C 3 95  ? -54.578 -52.190 24.627  1.000 130.608 ? 95  GLN CCC C   1 
ATOM   3883  O O   . GLN C 3 95  ? -54.964 -51.026 24.420  1.000 131.902 ? 95  GLN CCC O   1 
ATOM   3884  C CB  . GLN C 3 95  ? -52.129 -51.995 24.291  1.000 128.705 ? 95  GLN CCC CB  1 
ATOM   3885  C CG  . GLN C 3 95  ? -51.768 -52.277 25.746  1.000 132.226 ? 95  GLN CCC CG  1 
ATOM   3886  C CD  . GLN C 3 95  ? -51.319 -51.046 26.505  1.000 133.264 ? 95  GLN CCC CD  1 
ATOM   3887  O OE1 . GLN C 3 95  ? -50.151 -50.894 26.867  1.000 135.189 ? 95  GLN CCC OE1 1 
ATOM   3888  N NE2 . GLN C 3 95  ? -52.253 -50.145 26.763  1.000 132.943 ? 95  GLN CCC NE2 1 
ATOM   3889  N N   . GLN C 3 96  ? -55.115 -53.001 25.540  1.000 132.480 ? 96  GLN CCC N   1 
ATOM   3890  C CA  . GLN C 3 96  ? -56.100 -52.532 26.552  1.000 133.480 ? 96  GLN CCC CA  1 
ATOM   3891  C C   . GLN C 3 96  ? -55.329 -52.048 27.782  1.000 133.406 ? 96  GLN CCC C   1 
ATOM   3892  O O   . GLN C 3 96  ? -54.293 -52.660 28.110  1.000 133.951 ? 96  GLN CCC O   1 
ATOM   3893  C CB  . GLN C 3 96  ? -57.096 -53.634 26.914  1.000 136.220 ? 96  GLN CCC CB  1 
ATOM   3894  C CG  . GLN C 3 96  ? -56.521 -54.732 27.798  1.000 136.256 ? 96  GLN CCC CG  1 
ATOM   3895  C CD  . GLN C 3 96  ? -56.426 -54.349 29.254  1.000 136.482 ? 96  GLN CCC CD  1 
ATOM   3896  O OE1 . GLN C 3 96  ? -57.115 -53.455 29.737  1.000 135.707 ? 96  GLN CCC OE1 1 
ATOM   3897  N NE2 . GLN C 3 96  ? -55.559 -55.042 29.973  1.000 138.763 ? 96  GLN CCC NE2 1 
ATOM   3898  N N   . TYR C 3 97  ? -55.811 -50.988 28.429  1.000 134.666 ? 97  TYR CCC N   1 
ATOM   3899  C CA  . TYR C 3 97  ? -55.277 -50.500 29.726  1.000 135.031 ? 97  TYR CCC CA  1 
ATOM   3900  C C   . TYR C 3 97  ? -56.454 -50.104 30.629  1.000 138.199 ? 97  TYR CCC C   1 
ATOM   3901  O O   . TYR C 3 97  ? -56.331 -49.105 31.363  1.000 140.100 ? 97  TYR CCC O   1 
ATOM   3902  C CB  . TYR C 3 97  ? -54.245 -49.390 29.488  1.000 131.152 ? 97  TYR CCC CB  1 
ATOM   3903  C CG  . TYR C 3 97  ? -54.769 -48.156 28.793  1.000 130.106 ? 97  TYR CCC CG  1 
ATOM   3904  C CD1 . TYR C 3 97  ? -54.897 -48.091 27.413  1.000 128.213 ? 97  TYR CCC CD1 1 
ATOM   3905  C CD2 . TYR C 3 97  ? -55.132 -47.035 29.522  1.000 131.698 ? 97  TYR CCC CD2 1 
ATOM   3906  C CE1 . TYR C 3 97  ? -55.379 -46.950 26.782  1.000 127.374 ? 97  TYR CCC CE1 1 
ATOM   3907  C CE2 . TYR C 3 97  ? -55.620 -45.890 28.909  1.000 131.559 ? 97  TYR CCC CE2 1 
ATOM   3908  C CZ  . TYR C 3 97  ? -55.743 -45.841 27.532  1.000 128.227 ? 97  TYR CCC CZ  1 
ATOM   3909  O OH  . TYR C 3 97  ? -56.209 -44.694 26.956  1.000 124.285 ? 97  TYR CCC OH  1 
ATOM   3910  N N   . TYR C 3 98  ? -57.552 -50.873 30.590  1.000 139.506 ? 98  TYR CCC N   1 
ATOM   3911  C CA  . TYR C 3 98  ? -58.685 -50.755 31.548  1.000 142.878 ? 98  TYR CCC CA  1 
ATOM   3912  C C   . TYR C 3 98  ? -58.181 -51.185 32.928  1.000 144.562 ? 98  TYR CCC C   1 
ATOM   3913  O O   . TYR C 3 98  ? -58.565 -50.542 33.936  1.000 148.862 ? 98  TYR CCC O   1 
ATOM   3914  C CB  . TYR C 3 98  ? -59.915 -51.575 31.131  1.000 145.352 ? 98  TYR CCC CB  1 
ATOM   3915  C CG  . TYR C 3 98  ? -61.077 -51.467 32.095  1.000 149.209 ? 98  TYR CCC CG  1 
ATOM   3916  C CD1 . TYR C 3 98  ? -61.956 -50.395 32.045  1.000 149.207 ? 98  TYR CCC CD1 1 
ATOM   3917  C CD2 . TYR C 3 98  ? -61.283 -52.415 33.086  1.000 153.180 ? 98  TYR CCC CD2 1 
ATOM   3918  C CE1 . TYR C 3 98  ? -63.009 -50.276 32.938  1.000 153.028 ? 98  TYR CCC CE1 1 
ATOM   3919  C CE2 . TYR C 3 98  ? -62.327 -52.307 33.992  1.000 157.618 ? 98  TYR CCC CE2 1 
ATOM   3920  C CZ  . TYR C 3 98  ? -63.192 -51.231 33.919  1.000 157.994 ? 98  TYR CCC CZ  1 
ATOM   3921  O OH  . TYR C 3 98  ? -64.226 -51.124 34.802  1.000 164.393 ? 98  TYR CCC OH  1 
ATOM   3922  N N   . SER C 3 99  ? -57.350 -52.231 32.964  1.000 142.635 ? 99  SER CCC N   1 
ATOM   3923  C CA  . SER C 3 99  ? -56.807 -52.819 34.215  1.000 145.448 ? 99  SER CCC CA  1 
ATOM   3924  C C   . SER C 3 99  ? -55.598 -53.704 33.911  1.000 142.144 ? 99  SER CCC C   1 
ATOM   3925  O O   . SER C 3 99  ? -55.502 -54.203 32.780  1.000 138.795 ? 99  SER CCC O   1 
ATOM   3926  C CB  . SER C 3 99  ? -57.867 -53.602 34.954  1.000 152.246 ? 99  SER CCC CB  1 
ATOM   3927  O OG  . SER C 3 99  ? -58.077 -54.875 34.357  1.000 154.314 ? 99  SER CCC OG  1 
ATOM   3928  N N   . THR C 3 100 ? -54.736 -53.898 34.911  1.000 143.090 ? 100 THR CCC N   1 
ATOM   3929  C CA  . THR C 3 100 ? -53.615 -54.869 34.878  1.000 142.489 ? 100 THR CCC CA  1 
ATOM   3930  C C   . THR C 3 100 ? -54.210 -56.272 34.920  1.000 147.254 ? 100 THR CCC C   1 
ATOM   3931  O O   . THR C 3 100 ? -55.237 -56.490 35.559  1.000 150.172 ? 100 THR CCC O   1 
ATOM   3932  C CB  . THR C 3 100 ? -52.614 -54.627 36.016  1.000 141.373 ? 100 THR CCC CB  1 
ATOM   3933  O OG1 . THR C 3 100 ? -53.271 -54.845 37.266  1.000 143.414 ? 100 THR CCC OG1 1 
ATOM   3934  C CG2 . THR C 3 100 ? -52.012 -53.240 35.952  1.000 137.807 ? 100 THR CCC CG2 1 
ATOM   3935  N N   . PRO C 3 101 ? -53.601 -57.255 34.222  1.000 149.493 ? 101 PRO CCC N   1 
ATOM   3936  C CA  . PRO C 3 101 ? -52.410 -57.011 33.411  1.000 147.299 ? 101 PRO CCC CA  1 
ATOM   3937  C C   . PRO C 3 101 ? -52.808 -56.389 32.065  1.000 145.119 ? 101 PRO CCC C   1 
ATOM   3938  O O   . PRO C 3 101 ? -53.671 -56.941 31.420  1.000 146.378 ? 101 PRO CCC O   1 
ATOM   3939  C CB  . PRO C 3 101 ? -51.816 -58.414 33.237  1.000 149.034 ? 101 PRO CCC CB  1 
ATOM   3940  C CG  . PRO C 3 101 ? -53.023 -59.326 33.253  1.000 152.717 ? 101 PRO CCC CG  1 
ATOM   3941  C CD  . PRO C 3 101 ? -54.042 -58.654 34.154  1.000 153.611 ? 101 PRO CCC CD  1 
ATOM   3942  N N   . TYR C 3 102 ? -52.196 -55.259 31.695  1.000 143.256 ? 102 TYR CCC N   1 
ATOM   3943  C CA  . TYR C 3 102 ? -52.259 -54.701 30.318  1.000 141.380 ? 102 TYR CCC CA  1 
ATOM   3944  C C   . TYR C 3 102 ? -52.029 -55.880 29.358  1.000 142.059 ? 102 TYR CCC C   1 
ATOM   3945  O O   . TYR C 3 102 ? -51.202 -56.756 29.701  1.000 143.873 ? 102 TYR CCC O   1 
ATOM   3946  C CB  . TYR C 3 102 ? -51.203 -53.610 30.092  1.000 139.346 ? 102 TYR CCC CB  1 
ATOM   3947  C CG  . TYR C 3 102 ? -51.307 -52.317 30.872  1.000 140.112 ? 102 TYR CCC CG  1 
ATOM   3948  C CD1 . TYR C 3 102 ? -52.184 -52.126 31.934  1.000 140.824 ? 102 TYR CCC CD1 1 
ATOM   3949  C CD2 . TYR C 3 102 ? -50.447 -51.273 30.559  1.000 141.195 ? 102 TYR CCC CD2 1 
ATOM   3950  C CE1 . TYR C 3 102 ? -52.223 -50.926 32.631  1.000 141.342 ? 102 TYR CCC CE1 1 
ATOM   3951  C CE2 . TYR C 3 102 ? -50.462 -50.075 31.254  1.000 141.683 ? 102 TYR CCC CE2 1 
ATOM   3952  C CZ  . TYR C 3 102 ? -51.356 -49.899 32.292  1.000 141.692 ? 102 TYR CCC CZ  1 
ATOM   3953  O OH  . TYR C 3 102 ? -51.343 -48.704 32.952  1.000 142.611 ? 102 TYR CCC OH  1 
ATOM   3954  N N   . THR C 3 103 ? -52.743 -55.949 28.229  1.000 140.898 ? 103 THR CCC N   1 
ATOM   3955  C CA  . THR C 3 103 ? -52.589 -57.031 27.215  1.000 139.587 ? 103 THR CCC CA  1 
ATOM   3956  C C   . THR C 3 103 ? -52.627 -56.444 25.804  1.000 135.638 ? 103 THR CCC C   1 
ATOM   3957  O O   . THR C 3 103 ? -53.426 -55.524 25.572  1.000 134.120 ? 103 THR CCC O   1 
ATOM   3958  C CB  . THR C 3 103 ? -53.651 -58.123 27.388  1.000 143.271 ? 103 THR CCC CB  1 
ATOM   3959  O OG1 . THR C 3 103 ? -54.949 -57.528 27.400  1.000 141.639 ? 103 THR CCC OG1 1 
ATOM   3960  C CG2 . THR C 3 103 ? -53.443 -58.924 28.655  1.000 146.826 ? 103 THR CCC CG2 1 
ATOM   3961  N N   . PHE C 3 104 ? -51.775 -56.955 24.913  1.000 134.611 ? 104 PHE CCC N   1 
ATOM   3962  C CA  . PHE C 3 104 ? -51.678 -56.540 23.490  1.000 133.823 ? 104 PHE CCC CA  1 
ATOM   3963  C C   . PHE C 3 104 ? -52.345 -57.603 22.620  1.000 136.718 ? 104 PHE CCC C   1 
ATOM   3964  O O   . PHE C 3 104 ? -52.500 -58.746 23.108  1.000 139.747 ? 104 PHE CCC O   1 
ATOM   3965  C CB  . PHE C 3 104 ? -50.223 -56.400 23.041  1.000 134.018 ? 104 PHE CCC CB  1 
ATOM   3966  C CG  . PHE C 3 104 ? -49.424 -55.300 23.693  1.000 133.808 ? 104 PHE CCC CG  1 
ATOM   3967  C CD1 . PHE C 3 104 ? -49.397 -54.029 23.146  1.000 131.755 ? 104 PHE CCC CD1 1 
ATOM   3968  C CD2 . PHE C 3 104 ? -48.650 -55.545 24.820  1.000 136.836 ? 104 PHE CCC CD2 1 
ATOM   3969  C CE1 . PHE C 3 104 ? -48.638 -53.022 23.727  1.000 131.202 ? 104 PHE CCC CE1 1 
ATOM   3970  C CE2 . PHE C 3 104 ? -47.897 -54.535 25.404  1.000 134.684 ? 104 PHE CCC CE2 1 
ATOM   3971  C CZ  . PHE C 3 104 ? -47.888 -53.275 24.854  1.000 131.586 ? 104 PHE CCC CZ  1 
ATOM   3972  N N   . GLY C 3 105 ? -52.707 -57.229 21.385  1.000 135.485 ? 105 GLY CCC N   1 
ATOM   3973  C CA  . GLY C 3 105 ? -53.082 -58.153 20.296  1.000 136.350 ? 105 GLY CCC CA  1 
ATOM   3974  C C   . GLY C 3 105 ? -51.842 -58.722 19.622  1.000 135.487 ? 105 GLY CCC C   1 
ATOM   3975  O O   . GLY C 3 105 ? -50.731 -58.257 19.945  1.000 133.342 ? 105 GLY CCC O   1 
ATOM   3976  N N   . GLN C 3 106 ? -52.014 -59.677 18.703  1.000 137.461 ? 106 GLN CCC N   1 
ATOM   3977  C CA  . GLN C 3 106 ? -50.907 -60.476 18.102  1.000 139.458 ? 106 GLN CCC CA  1 
ATOM   3978  C C   . GLN C 3 106 ? -50.177 -59.667 17.020  1.000 135.600 ? 106 GLN CCC C   1 
ATOM   3979  O O   . GLN C 3 106 ? -49.144 -60.157 16.511  1.000 134.968 ? 106 GLN CCC O   1 
ATOM   3980  C CB  . GLN C 3 106 ? -51.442 -61.804 17.552  1.000 147.393 ? 106 GLN CCC CB  1 
ATOM   3981  C CG  . GLN C 3 106 ? -52.288 -61.691 16.285  1.000 150.844 ? 106 GLN CCC CG  1 
ATOM   3982  C CD  . GLN C 3 106 ? -53.718 -61.257 16.512  1.000 152.770 ? 106 GLN CCC CD  1 
ATOM   3983  O OE1 . GLN C 3 106 ? -54.256 -61.341 17.616  1.000 155.987 ? 106 GLN CCC OE1 1 
ATOM   3984  N NE2 . GLN C 3 106 ? -54.353 -60.788 15.451  1.000 151.957 ? 106 GLN CCC NE2 1 
ATOM   3985  N N   . GLY C 3 107 ? -50.697 -58.489 16.669  1.000 132.808 ? 107 GLY CCC N   1 
ATOM   3986  C CA  . GLY C 3 107 ? -50.075 -57.577 15.691  1.000 130.118 ? 107 GLY CCC CA  1 
ATOM   3987  C C   . GLY C 3 107 ? -50.693 -57.735 14.318  1.000 131.464 ? 107 GLY CCC C   1 
ATOM   3988  O O   . GLY C 3 107 ? -51.309 -58.792 14.072  1.000 134.127 ? 107 GLY CCC O   1 
ATOM   3989  N N   . THR C 3 108 ? -50.537 -56.712 13.467  1.000 130.798 ? 108 THR CCC N   1 
ATOM   3990  C CA  . THR C 3 108 ? -50.979 -56.679 12.044  1.000 132.945 ? 108 THR CCC CA  1 
ATOM   3991  C C   . THR C 3 108 ? -49.867 -56.083 11.160  1.000 133.689 ? 108 THR CCC C   1 
ATOM   3992  O O   . THR C 3 108 ? -49.532 -54.892 11.362  1.000 132.913 ? 108 THR CCC O   1 
ATOM   3993  C CB  . THR C 3 108 ? -52.274 -55.869 11.907  1.000 132.058 ? 108 THR CCC CB  1 
ATOM   3994  O OG1 . THR C 3 108 ? -53.247 -56.401 12.811  1.000 130.354 ? 108 THR CCC OG1 1 
ATOM   3995  C CG2 . THR C 3 108 ? -52.809 -55.875 10.490  1.000 135.926 ? 108 THR CCC CG2 1 
ATOM   3996  N N   . LYS C 3 109 ? -49.296 -56.866 10.232  1.000 136.046 ? 109 LYS CCC N   1 
ATOM   3997  C CA  . LYS C 3 109 ? -48.296 -56.362 9.249   1.000 135.903 ? 109 LYS CCC CA  1 
ATOM   3998  C C   . LYS C 3 109 ? -49.089 -55.591 8.191   1.000 135.642 ? 109 LYS CCC C   1 
ATOM   3999  O O   . LYS C 3 109 ? -50.148 -56.113 7.763   1.000 138.403 ? 109 LYS CCC O   1 
ATOM   4000  C CB  . LYS C 3 109 ? -47.434 -57.495 8.663   1.000 139.319 ? 109 LYS CCC CB  1 
ATOM   4001  C CG  . LYS C 3 109 ? -46.230 -57.067 7.819   1.000 141.964 ? 109 LYS CCC CG  1 
ATOM   4002  C CD  . LYS C 3 109 ? -45.064 -56.472 8.621   1.000 144.474 ? 109 LYS CCC CD  1 
ATOM   4003  C CE  . LYS C 3 109 ? -44.132 -55.563 7.828   1.000 146.964 ? 109 LYS CCC CE  1 
ATOM   4004  N NZ  . LYS C 3 109 ? -43.364 -54.609 8.678   1.000 143.513 ? 109 LYS CCC NZ  1 
ATOM   4005  N N   . VAL C 3 110 ? -48.646 -54.368 7.870   1.000 131.729 ? 110 VAL CCC N   1 
ATOM   4006  C CA  . VAL C 3 110 ? -49.192 -53.525 6.765   1.000 131.868 ? 110 VAL CCC CA  1 
ATOM   4007  C C   . VAL C 3 110 ? -48.057 -53.235 5.784   1.000 131.786 ? 110 VAL CCC C   1 
ATOM   4008  O O   . VAL C 3 110 ? -47.073 -52.586 6.196   1.000 129.144 ? 110 VAL CCC O   1 
ATOM   4009  C CB  . VAL C 3 110 ? -49.840 -52.225 7.283   1.000 130.069 ? 110 VAL CCC CB  1 
ATOM   4010  C CG1 . VAL C 3 110 ? -50.173 -51.255 6.155   1.000 130.686 ? 110 VAL CCC CG1 1 
ATOM   4011  C CG2 . VAL C 3 110 ? -51.082 -52.526 8.106   1.000 131.597 ? 110 VAL CCC CG2 1 
ATOM   4012  N N   . GLU C 3 111 ? -48.216 -53.689 4.537   1.000 136.099 ? 111 GLU CCC N   1 
ATOM   4013  C CA  . GLU C 3 111 ? -47.219 -53.539 3.447   1.000 138.392 ? 111 GLU CCC CA  1 
ATOM   4014  C C   . GLU C 3 111 ? -47.888 -52.873 2.236   1.000 138.355 ? 111 GLU CCC C   1 
ATOM   4015  O O   . GLU C 3 111 ? -49.128 -52.945 2.131   1.000 135.628 ? 111 GLU CCC O   1 
ATOM   4016  C CB  . GLU C 3 111 ? -46.591 -54.902 3.149   1.000 142.905 ? 111 GLU CCC CB  1 
ATOM   4017  C CG  . GLU C 3 111 ? -45.770 -55.438 4.312   1.000 144.209 ? 111 GLU CCC CG  1 
ATOM   4018  C CD  . GLU C 3 111 ? -44.685 -56.456 3.979   1.000 149.115 ? 111 GLU CCC CD  1 
ATOM   4019  O OE1 . GLU C 3 111 ? -45.032 -57.571 3.525   1.000 152.507 ? 111 GLU CCC OE1 1 
ATOM   4020  O OE2 . GLU C 3 111 ? -43.485 -56.134 4.194   1.000 149.423 ? 111 GLU CCC OE2 1 
ATOM   4021  N N   . ILE C 3 112 ? -47.076 -52.224 1.392   1.000 139.186 ? 112 ILE CCC N   1 
ATOM   4022  C CA  . ILE C 3 112 ? -47.501 -51.401 0.220   1.000 142.673 ? 112 ILE CCC CA  1 
ATOM   4023  C C   . ILE C 3 112 ? -47.708 -52.311 -0.988  1.000 147.456 ? 112 ILE CCC C   1 
ATOM   4024  O O   . ILE C 3 112 ? -46.704 -52.817 -1.518  1.000 149.489 ? 112 ILE CCC O   1 
ATOM   4025  C CB  . ILE C 3 112 ? -46.455 -50.319 -0.110  1.000 143.492 ? 112 ILE CCC CB  1 
ATOM   4026  C CG1 . ILE C 3 112 ? -46.370 -49.262 0.994   1.000 141.869 ? 112 ILE CCC CG1 1 
ATOM   4027  C CG2 . ILE C 3 112 ? -46.717 -49.686 -1.474  1.000 147.010 ? 112 ILE CCC CG2 1 
ATOM   4028  C CD1 . ILE C 3 112 ? -47.539 -48.294 1.047   1.000 142.720 ? 112 ILE CCC CD1 1 
ATOM   4029  N N   . LYS C 3 113 ? -48.953 -52.459 -1.436  1.000 151.865 ? 113 LYS CCC N   1 
ATOM   4030  C CA  . LYS C 3 113 ? -49.272 -53.176 -2.695  1.000 157.401 ? 113 LYS CCC CA  1 
ATOM   4031  C C   . LYS C 3 113 ? -48.781 -52.323 -3.865  1.000 158.159 ? 113 LYS CCC C   1 
ATOM   4032  O O   . LYS C 3 113 ? -49.168 -51.140 -3.935  1.000 155.523 ? 113 LYS CCC O   1 
ATOM   4033  C CB  . LYS C 3 113 ? -50.767 -53.497 -2.802  1.000 161.050 ? 113 LYS CCC CB  1 
ATOM   4034  C CG  . LYS C 3 113 ? -51.110 -54.499 -3.903  1.000 166.940 ? 113 LYS CCC CG  1 
ATOM   4035  C CD  . LYS C 3 113 ? -51.990 -55.640 -3.461  1.000 168.918 ? 113 LYS CCC CD  1 
ATOM   4036  C CE  . LYS C 3 113 ? -53.361 -55.164 -3.044  1.000 170.168 ? 113 LYS CCC CE  1 
ATOM   4037  N NZ  . LYS C 3 113 ? -54.290 -56.304 -2.891  1.000 174.685 ? 113 LYS CCC NZ  1 
ATOM   4038  N N   . ARG C 3 114 ? -47.953 -52.917 -4.725  1.000 158.135 ? 114 ARG CCC N   1 
ATOM   4039  C CA  . ARG C 3 114 ? -47.314 -52.236 -5.877  1.000 159.686 ? 114 ARG CCC CA  1 
ATOM   4040  C C   . ARG C 3 114 ? -47.516 -53.063 -7.147  1.000 160.311 ? 114 ARG CCC C   1 
ATOM   4041  O O   . ARG C 3 114 ? -48.016 -54.210 -7.058  1.000 159.983 ? 114 ARG CCC O   1 
ATOM   4042  C CB  . ARG C 3 114 ? -45.822 -52.050 -5.605  1.000 158.169 ? 114 ARG CCC CB  1 
ATOM   4043  C CG  . ARG C 3 114 ? -45.069 -53.348 -5.351  1.000 156.744 ? 114 ARG CCC CG  1 
ATOM   4044  C CD  . ARG C 3 114 ? -43.646 -53.250 -5.858  1.000 156.856 ? 114 ARG CCC CD  1 
ATOM   4045  N NE  . ARG C 3 114 ? -43.582 -53.248 -7.315  1.000 158.543 ? 114 ARG CCC NE  1 
ATOM   4046  C CZ  . ARG C 3 114 ? -42.511 -52.913 -8.030  1.000 159.005 ? 114 ARG CCC CZ  1 
ATOM   4047  N NH1 . ARG C 3 114 ? -41.396 -52.531 -7.428  1.000 158.048 ? 114 ARG CCC NH1 1 
ATOM   4048  N NH2 . ARG C 3 114 ? -42.554 -52.961 -9.350  1.000 161.338 ? 114 ARG CCC NH2 1 
ATOM   4049  N N   . THR C 3 115 ? -47.091 -52.500 -8.275  1.000 160.850 ? 115 THR CCC N   1 
ATOM   4050  C CA  . THR C 3 115 ? -47.106 -53.151 -9.607  1.000 162.424 ? 115 THR CCC CA  1 
ATOM   4051  C C   . THR C 3 115 ? -46.447 -54.532 -9.481  1.000 156.439 ? 115 THR CCC C   1 
ATOM   4052  O O   . THR C 3 115 ? -45.439 -54.628 -8.759  1.000 150.840 ? 115 THR CCC O   1 
ATOM   4053  C CB  . THR C 3 115 ? -46.424 -52.247 -10.642 1.000 166.183 ? 115 THR CCC CB  1 
ATOM   4054  O OG1 . THR C 3 115 ? -45.014 -52.376 -10.468 1.000 166.053 ? 115 THR CCC OG1 1 
ATOM   4055  C CG2 . THR C 3 115 ? -46.813 -50.788 -10.515 1.000 168.887 ? 115 THR CCC CG2 1 
ATOM   4056  N N   . VAL C 3 116 ? -47.012 -55.552 -10.138 1.000 156.863 ? 116 VAL CCC N   1 
ATOM   4057  C CA  . VAL C 3 116 ? -46.426 -56.926 -10.240 1.000 154.600 ? 116 VAL CCC CA  1 
ATOM   4058  C C   . VAL C 3 116 ? -44.971 -56.775 -10.695 1.000 153.614 ? 116 VAL CCC C   1 
ATOM   4059  O O   . VAL C 3 116 ? -44.683 -55.792 -11.408 1.000 157.429 ? 116 VAL CCC O   1 
ATOM   4060  C CB  . VAL C 3 116 ? -47.193 -57.843 -11.219 1.000 155.686 ? 116 VAL CCC CB  1 
ATOM   4061  C CG1 . VAL C 3 116 ? -46.773 -59.297 -11.045 1.000 151.908 ? 116 VAL CCC CG1 1 
ATOM   4062  C CG2 . VAL C 3 116 ? -48.708 -57.697 -11.113 1.000 158.731 ? 116 VAL CCC CG2 1 
ATOM   4063  N N   . ALA C 3 117 ? -44.090 -57.705 -10.316 1.000 150.203 ? 117 ALA CCC N   1 
ATOM   4064  C CA  . ALA C 3 117 ? -42.652 -57.651 -10.674 1.000 149.093 ? 117 ALA CCC CA  1 
ATOM   4065  C C   . ALA C 3 117 ? -42.004 -59.029 -10.517 1.000 145.847 ? 117 ALA CCC C   1 
ATOM   4066  O O   . ALA C 3 117 ? -42.046 -59.581 -9.408  1.000 142.144 ? 117 ALA CCC O   1 
ATOM   4067  C CB  . ALA C 3 117 ? -41.952 -56.614 -9.832  1.000 149.052 ? 117 ALA CCC CB  1 
ATOM   4068  N N   . ALA C 3 118 ? -41.409 -59.539 -11.599 1.000 146.851 ? 118 ALA CCC N   1 
ATOM   4069  C CA  . ALA C 3 118 ? -40.794 -60.882 -11.685 1.000 143.673 ? 118 ALA CCC CA  1 
ATOM   4070  C C   . ALA C 3 118 ? -39.411 -60.849 -11.043 1.000 139.684 ? 118 ALA CCC C   1 
ATOM   4071  O O   . ALA C 3 118 ? -38.762 -59.809 -10.999 1.000 136.866 ? 118 ALA CCC O   1 
ATOM   4072  C CB  . ALA C 3 118 ? -40.730 -61.338 -13.122 1.000 146.294 ? 118 ALA CCC CB  1 
ATOM   4073  N N   . PRO C 3 119 ? -38.927 -61.998 -10.528 1.000 138.869 ? 119 PRO CCC N   1 
ATOM   4074  C CA  . PRO C 3 119 ? -37.671 -62.059 -9.786  1.000 139.044 ? 119 PRO CCC CA  1 
ATOM   4075  C C   . PRO C 3 119 ? -36.448 -62.432 -10.632 1.000 141.495 ? 119 PRO CCC C   1 
ATOM   4076  O O   . PRO C 3 119 ? -36.560 -63.317 -11.448 1.000 144.507 ? 119 PRO CCC O   1 
ATOM   4077  C CB  . PRO C 3 119 ? -37.960 -63.189 -8.790  1.000 137.097 ? 119 PRO CCC CB  1 
ATOM   4078  C CG  . PRO C 3 119 ? -38.889 -64.133 -9.535  1.000 137.590 ? 119 PRO CCC CG  1 
ATOM   4079  C CD  . PRO C 3 119 ? -39.580 -63.311 -10.605 1.000 139.269 ? 119 PRO CCC CD  1 
ATOM   4080  N N   . SER C 3 120 ? -35.321 -61.754 -10.396 1.000 144.155 ? 120 SER CCC N   1 
ATOM   4081  C CA  . SER C 3 120 ? -34.004 -62.008 -11.038 1.000 147.583 ? 120 SER CCC CA  1 
ATOM   4082  C C   . SER C 3 120 ? -33.315 -63.188 -10.345 1.000 145.458 ? 120 SER CCC C   1 
ATOM   4083  O O   . SER C 3 120 ? -32.659 -62.961 -9.303  1.000 145.441 ? 120 SER CCC O   1 
ATOM   4084  C CB  . SER C 3 120 ? -33.128 -60.775 -11.005 1.000 151.842 ? 120 SER CCC CB  1 
ATOM   4085  O OG  . SER C 3 120 ? -33.737 -59.689 -11.687 1.000 156.614 ? 120 SER CCC OG  1 
ATOM   4086  N N   . VAL C 3 121 ? -33.443 -64.394 -10.908 1.000 144.482 ? 121 VAL CCC N   1 
ATOM   4087  C CA  . VAL C 3 121 ? -32.910 -65.644 -10.292 1.000 141.845 ? 121 VAL CCC CA  1 
ATOM   4088  C C   . VAL C 3 121 ? -31.424 -65.788 -10.613 1.000 143.506 ? 121 VAL CCC C   1 
ATOM   4089  O O   . VAL C 3 121 ? -31.012 -65.480 -11.747 1.000 146.277 ? 121 VAL CCC O   1 
ATOM   4090  C CB  . VAL C 3 121 ? -33.681 -66.898 -10.730 1.000 140.348 ? 121 VAL CCC CB  1 
ATOM   4091  C CG1 . VAL C 3 121 ? -33.053 -68.158 -10.155 1.000 139.152 ? 121 VAL CCC CG1 1 
ATOM   4092  C CG2 . VAL C 3 121 ? -35.144 -66.800 -10.339 1.000 139.619 ? 121 VAL CCC CG2 1 
ATOM   4093  N N   . PHE C 3 122 ? -30.682 -66.270 -9.619  1.000 142.448 ? 122 PHE CCC N   1 
ATOM   4094  C CA  . PHE C 3 122 ? -29.241 -66.603 -9.665  1.000 144.016 ? 122 PHE CCC CA  1 
ATOM   4095  C C   . PHE C 3 122 ? -29.034 -67.869 -8.836  1.000 143.346 ? 122 PHE CCC C   1 
ATOM   4096  O O   . PHE C 3 122 ? -29.693 -67.981 -7.782  1.000 141.944 ? 122 PHE CCC O   1 
ATOM   4097  C CB  . PHE C 3 122 ? -28.416 -65.438 -9.116  1.000 144.440 ? 122 PHE CCC CB  1 
ATOM   4098  C CG  . PHE C 3 122 ? -28.106 -64.384 -10.141 1.000 146.823 ? 122 PHE CCC CG  1 
ATOM   4099  C CD1 . PHE C 3 122 ? -27.184 -64.636 -11.149 1.000 151.845 ? 122 PHE CCC CD1 1 
ATOM   4100  C CD2 . PHE C 3 122 ? -28.752 -63.161 -10.110 1.000 145.623 ? 122 PHE CCC CD2 1 
ATOM   4101  C CE1 . PHE C 3 122 ? -26.909 -63.680 -12.113 1.000 156.605 ? 122 PHE CCC CE1 1 
ATOM   4102  C CE2 . PHE C 3 122 ? -28.472 -62.202 -11.069 1.000 151.628 ? 122 PHE CCC CE2 1 
ATOM   4103  C CZ  . PHE C 3 122 ? -27.554 -62.463 -12.067 1.000 157.438 ? 122 PHE CCC CZ  1 
ATOM   4104  N N   . ILE C 3 123 ? -28.173 -68.783 -9.291  1.000 144.250 ? 123 ILE CCC N   1 
ATOM   4105  C CA  . ILE C 3 123 ? -27.794 -69.998 -8.511  1.000 141.969 ? 123 ILE CCC CA  1 
ATOM   4106  C C   . ILE C 3 123 ? -26.300 -69.934 -8.182  1.000 142.793 ? 123 ILE CCC C   1 
ATOM   4107  O O   . ILE C 3 123 ? -25.536 -69.340 -8.961  1.000 143.740 ? 123 ILE CCC O   1 
ATOM   4108  C CB  . ILE C 3 123 ? -28.184 -71.296 -9.245  1.000 140.978 ? 123 ILE CCC CB  1 
ATOM   4109  C CG1 . ILE C 3 123 ? -28.267 -72.479 -8.277  1.000 139.527 ? 123 ILE CCC CG1 1 
ATOM   4110  C CG2 . ILE C 3 123 ? -27.239 -71.588 -10.397 1.000 143.803 ? 123 ILE CCC CG2 1 
ATOM   4111  C CD1 . ILE C 3 123 ? -28.980 -73.687 -8.825  1.000 139.621 ? 123 ILE CCC CD1 1 
ATOM   4112  N N   . PHE C 3 124 ? -25.922 -70.523 -7.048  1.000 143.516 ? 124 PHE CCC N   1 
ATOM   4113  C CA  . PHE C 3 124 ? -24.544 -70.529 -6.508  1.000 147.703 ? 124 PHE CCC CA  1 
ATOM   4114  C C   . PHE C 3 124 ? -24.163 -71.941 -6.091  1.000 146.787 ? 124 PHE CCC C   1 
ATOM   4115  O O   . PHE C 3 124 ? -24.828 -72.541 -5.248  1.000 143.103 ? 124 PHE CCC O   1 
ATOM   4116  C CB  . PHE C 3 124 ? -24.443 -69.591 -5.307  1.000 150.663 ? 124 PHE CCC CB  1 
ATOM   4117  C CG  . PHE C 3 124 ? -24.624 -68.140 -5.655  1.000 152.217 ? 124 PHE CCC CG  1 
ATOM   4118  C CD1 . PHE C 3 124 ? -23.709 -67.498 -6.473  1.000 155.658 ? 124 PHE CCC CD1 1 
ATOM   4119  C CD2 . PHE C 3 124 ? -25.706 -67.424 -5.170  1.000 151.539 ? 124 PHE CCC CD2 1 
ATOM   4120  C CE1 . PHE C 3 124 ? -23.869 -66.162 -6.797  1.000 158.358 ? 124 PHE CCC CE1 1 
ATOM   4121  C CE2 . PHE C 3 124 ? -25.866 -66.086 -5.494  1.000 153.873 ? 124 PHE CCC CE2 1 
ATOM   4122  C CZ  . PHE C 3 124 ? -24.947 -65.458 -6.307  1.000 157.270 ? 124 PHE CCC CZ  1 
ATOM   4123  N N   . PRO C 3 125 ? -23.056 -72.494 -6.631  1.000 149.162 ? 125 PRO CCC N   1 
ATOM   4124  C CA  . PRO C 3 125 ? -22.568 -73.790 -6.179  1.000 149.777 ? 125 PRO CCC CA  1 
ATOM   4125  C C   . PRO C 3 125 ? -22.007 -73.631 -4.773  1.000 150.562 ? 125 PRO CCC C   1 
ATOM   4126  O O   . PRO C 3 125 ? -21.988 -72.531 -4.223  1.000 151.184 ? 125 PRO CCC O   1 
ATOM   4127  C CB  . PRO C 3 125 ? -21.494 -74.152 -7.216  1.000 153.079 ? 125 PRO CCC CB  1 
ATOM   4128  C CG  . PRO C 3 125 ? -20.987 -72.813 -7.704  1.000 154.783 ? 125 PRO CCC CG  1 
ATOM   4129  C CD  . PRO C 3 125 ? -22.191 -71.893 -7.659  1.000 152.276 ? 125 PRO CCC CD  1 
ATOM   4130  N N   . PRO C 3 126 ? -21.565 -74.729 -4.131  1.000 151.376 ? 126 PRO CCC N   1 
ATOM   4131  C CA  . PRO C 3 126 ? -20.760 -74.614 -2.920  1.000 153.043 ? 126 PRO CCC CA  1 
ATOM   4132  C C   . PRO C 3 126 ? -19.344 -74.128 -3.268  1.000 155.157 ? 126 PRO CCC C   1 
ATOM   4133  O O   . PRO C 3 126 ? -18.933 -74.269 -4.413  1.000 153.124 ? 126 PRO CCC O   1 
ATOM   4134  C CB  . PRO C 3 126 ? -20.788 -76.034 -2.333  1.000 153.408 ? 126 PRO CCC CB  1 
ATOM   4135  C CG  . PRO C 3 126 ? -21.072 -76.950 -3.506  1.000 152.101 ? 126 PRO CCC CG  1 
ATOM   4136  C CD  . PRO C 3 126 ? -21.840 -76.122 -4.514  1.000 150.434 ? 126 PRO CCC CD  1 
ATOM   4137  N N   . SER C 3 127 ? -18.653 -73.540 -2.288  1.000 156.838 ? 127 SER CCC N   1 
ATOM   4138  C CA  . SER C 3 127 ? -17.211 -73.185 -2.364  1.000 160.284 ? 127 SER CCC CA  1 
ATOM   4139  C C   . SER C 3 127 ? -16.374 -74.461 -2.251  1.000 162.064 ? 127 SER CCC C   1 
ATOM   4140  O O   . SER C 3 127 ? -16.874 -75.441 -1.675  1.000 160.355 ? 127 SER CCC O   1 
ATOM   4141  C CB  . SER C 3 127 ? -16.845 -72.209 -1.291  1.000 162.118 ? 127 SER CCC CB  1 
ATOM   4142  O OG  . SER C 3 127 ? -17.216 -72.710 -0.019  1.000 161.487 ? 127 SER CCC OG  1 
ATOM   4143  N N   . ASP C 3 128 ? -15.153 -74.455 -2.789  1.000 166.223 ? 128 ASP CCC N   1 
ATOM   4144  C CA  . ASP C 3 128 ? -14.185 -75.566 -2.583  1.000 170.095 ? 128 ASP CCC CA  1 
ATOM   4145  C C   . ASP C 3 128 ? -13.848 -75.602 -1.088  1.000 172.145 ? 128 ASP CCC C   1 
ATOM   4146  O O   . ASP C 3 128 ? -13.876 -76.704 -0.499  1.000 172.459 ? 128 ASP CCC O   1 
ATOM   4147  C CB  . ASP C 3 128 ? -12.947 -75.436 -3.481  1.000 175.550 ? 128 ASP CCC CB  1 
ATOM   4148  C CG  . ASP C 3 128 ? -12.886 -76.431 -4.637  1.000 176.431 ? 128 ASP CCC CG  1 
ATOM   4149  O OD1 . ASP C 3 128 ? -13.949 -76.955 -5.031  1.000 172.283 ? 128 ASP CCC OD1 1 
ATOM   4150  O OD2 . ASP C 3 128 ? -11.764 -76.691 -5.135  1.000 182.286 ? 128 ASP CCC OD2 1 
ATOM   4151  N N   . GLU C 3 129 ? -13.592 -74.431 -0.494  1.000 173.100 ? 129 GLU CCC N   1 
ATOM   4152  C CA  . GLU C 3 129 ? -13.331 -74.270 0.961   1.000 173.664 ? 129 GLU CCC CA  1 
ATOM   4153  C C   . GLU C 3 129 ? -14.359 -75.096 1.745   1.000 168.082 ? 129 GLU CCC C   1 
ATOM   4154  O O   . GLU C 3 129 ? -13.929 -75.997 2.485   1.000 168.777 ? 129 GLU CCC O   1 
ATOM   4155  C CB  . GLU C 3 129 ? -13.384 -72.796 1.362   1.000 176.351 ? 129 GLU CCC CB  1 
ATOM   4156  C CG  . GLU C 3 129 ? -12.748 -72.532 2.716   1.000 183.337 ? 129 GLU CCC CG  1 
ATOM   4157  C CD  . GLU C 3 129 ? -12.940 -71.130 3.278   1.000 186.897 ? 129 GLU CCC CD  1 
ATOM   4158  O OE1 . GLU C 3 129 ? -13.841 -70.420 2.792   1.000 186.952 ? 129 GLU CCC OE1 1 
ATOM   4159  O OE2 . GLU C 3 129 ? -12.195 -70.753 4.211   1.000 191.285 ? 129 GLU CCC OE2 1 
ATOM   4160  N N   . GLN C 3 130 ? -15.657 -74.833 1.543   1.000 161.960 ? 130 GLN CCC N   1 
ATOM   4161  C CA  . GLN C 3 130 ? -16.783 -75.467 2.292   1.000 158.284 ? 130 GLN CCC CA  1 
ATOM   4162  C C   . GLN C 3 130 ? -16.772 -76.990 2.119   1.000 158.852 ? 130 GLN CCC C   1 
ATOM   4163  O O   . GLN C 3 130 ? -17.036 -77.688 3.109   1.000 159.044 ? 130 GLN CCC O   1 
ATOM   4164  C CB  . GLN C 3 130 ? -18.149 -74.946 1.836   1.000 152.313 ? 130 GLN CCC CB  1 
ATOM   4165  C CG  . GLN C 3 130 ? -19.315 -75.672 2.495   1.000 148.875 ? 130 GLN CCC CG  1 
ATOM   4166  C CD  . GLN C 3 130 ? -20.660 -75.070 2.172   1.000 144.873 ? 130 GLN CCC CD  1 
ATOM   4167  O OE1 . GLN C 3 130 ? -20.802 -74.235 1.273   1.000 142.484 ? 130 GLN CCC OE1 1 
ATOM   4168  N NE2 . GLN C 3 130 ? -21.665 -75.502 2.918   1.000 143.382 ? 130 GLN CCC NE2 1 
ATOM   4169  N N   . LEU C 3 131 ? -16.531 -77.488 0.905   1.000 159.838 ? 131 LEU CCC N   1 
ATOM   4170  C CA  . LEU C 3 131 ? -16.632 -78.936 0.583   1.000 160.625 ? 131 LEU CCC CA  1 
ATOM   4171  C C   . LEU C 3 131 ? -15.698 -79.728 1.496   1.000 166.324 ? 131 LEU CCC C   1 
ATOM   4172  O O   . LEU C 3 131 ? -16.138 -80.750 2.038   1.000 167.351 ? 131 LEU CCC O   1 
ATOM   4173  C CB  . LEU C 3 131 ? -16.289 -79.164 -0.891  1.000 160.071 ? 131 LEU CCC CB  1 
ATOM   4174  C CG  . LEU C 3 131 ? -17.416 -78.834 -1.863  1.000 155.888 ? 131 LEU CCC CG  1 
ATOM   4175  C CD1 . LEU C 3 131 ? -16.909 -78.759 -3.291  1.000 156.949 ? 131 LEU CCC CD1 1 
ATOM   4176  C CD2 . LEU C 3 131 ? -18.521 -79.865 -1.747  1.000 153.298 ? 131 LEU CCC CD2 1 
ATOM   4177  N N   . LYS C 3 132 ? -14.468 -79.249 1.667   1.000 172.327 ? 132 LYS CCC N   1 
ATOM   4178  C CA  . LYS C 3 132 ? -13.432 -79.902 2.507   1.000 179.798 ? 132 LYS CCC CA  1 
ATOM   4179  C C   . LYS C 3 132 ? -13.904 -79.973 3.965   1.000 181.853 ? 132 LYS CCC C   1 
ATOM   4180  O O   . LYS C 3 132 ? -13.483 -80.916 4.654   1.000 185.648 ? 132 LYS CCC O   1 
ATOM   4181  C CB  . LYS C 3 132 ? -12.110 -79.144 2.389   1.000 185.921 ? 132 LYS CCC CB  1 
ATOM   4182  C CG  . LYS C 3 132 ? -11.441 -79.236 1.024   1.000 188.176 ? 132 LYS CCC CG  1 
ATOM   4183  C CD  . LYS C 3 132 ? -10.165 -78.426 0.915   1.000 195.264 ? 132 LYS CCC CD  1 
ATOM   4184  C CE  . LYS C 3 132 ? -10.386 -76.930 1.027   1.000 195.973 ? 132 LYS CCC CE  1 
ATOM   4185  N NZ  . LYS C 3 132 ? -9.142  -76.172 0.753   1.000 202.454 ? 132 LYS CCC NZ  1 
ATOM   4186  N N   . SER C 3 133 ? -14.740 -79.026 4.413   1.000 181.633 ? 133 SER CCC N   1 
ATOM   4187  C CA  . SER C 3 133 ? -15.268 -78.943 5.805   1.000 184.800 ? 133 SER CCC CA  1 
ATOM   4188  C C   . SER C 3 133 ? -16.101 -80.190 6.134   1.000 183.281 ? 133 SER CCC C   1 
ATOM   4189  O O   . SER C 3 133 ? -15.967 -80.697 7.271   1.000 188.833 ? 133 SER CCC O   1 
ATOM   4190  C CB  . SER C 3 133 ? -16.063 -77.667 6.052   1.000 184.682 ? 133 SER CCC CB  1 
ATOM   4191  O OG  . SER C 3 133 ? -17.437 -77.808 5.696   1.000 181.258 ? 133 SER CCC OG  1 
ATOM   4192  N N   . GLY C 3 134 ? -16.924 -80.656 5.187   1.000 176.865 ? 134 GLY CCC N   1 
ATOM   4193  C CA  . GLY C 3 134 ? -17.794 -81.837 5.352   1.000 173.482 ? 134 GLY CCC CA  1 
ATOM   4194  C C   . GLY C 3 134 ? -19.148 -81.645 4.694   1.000 166.952 ? 134 GLY CCC C   1 
ATOM   4195  O O   . GLY C 3 134 ? -19.601 -82.575 4.018   1.000 165.583 ? 134 GLY CCC O   1 
ATOM   4196  N N   . THR C 3 135 ? -19.786 -80.491 4.901   1.000 164.275 ? 135 THR CCC N   1 
ATOM   4197  C CA  . THR C 3 135 ? -21.084 -80.130 4.270   1.000 159.556 ? 135 THR CCC CA  1 
ATOM   4198  C C   . THR C 3 135 ? -20.812 -79.477 2.911   1.000 156.475 ? 135 THR CCC C   1 
ATOM   4199  O O   . THR C 3 135 ? -19.642 -79.177 2.604   1.000 156.872 ? 135 THR CCC O   1 
ATOM   4200  C CB  . THR C 3 135 ? -21.939 -79.220 5.169   1.000 159.379 ? 135 THR CCC CB  1 
ATOM   4201  O OG1 . THR C 3 135 ? -21.134 -78.147 5.668   1.000 161.545 ? 135 THR CCC OG1 1 
ATOM   4202  C CG2 . THR C 3 135 ? -22.571 -79.962 6.327   1.000 160.654 ? 135 THR CCC CG2 1 
ATOM   4203  N N   . ALA C 3 136 ? -21.876 -79.287 2.134   1.000 153.695 ? 136 ALA CCC N   1 
ATOM   4204  C CA  . ALA C 3 136 ? -21.894 -78.578 0.836   1.000 153.072 ? 136 ALA CCC CA  1 
ATOM   4205  C C   . ALA C 3 136 ? -23.228 -77.835 0.717   1.000 150.877 ? 136 ALA CCC C   1 
ATOM   4206  O O   . ALA C 3 136 ? -24.264 -78.504 0.732   1.000 149.845 ? 136 ALA CCC O   1 
ATOM   4207  C CB  . ALA C 3 136 ? -21.708 -79.566 -0.289  1.000 153.303 ? 136 ALA CCC CB  1 
ATOM   4208  N N   . SER C 3 137 ? -23.196 -76.505 0.620   1.000 150.548 ? 137 SER CCC N   1 
ATOM   4209  C CA  . SER C 3 137 ? -24.398 -75.634 0.584   1.000 146.655 ? 137 SER CCC CA  1 
ATOM   4210  C C   . SER C 3 137 ? -24.557 -75.056 -0.822  1.000 145.840 ? 137 SER CCC C   1 
ATOM   4211  O O   . SER C 3 137 ? -23.606 -74.437 -1.335  1.000 147.598 ? 137 SER CCC O   1 
ATOM   4212  C CB  . SER C 3 137 ? -24.339 -74.552 1.629   1.000 145.647 ? 137 SER CCC CB  1 
ATOM   4213  O OG  . SER C 3 137 ? -24.560 -75.097 2.920   1.000 145.426 ? 137 SER CCC OG  1 
ATOM   4214  N N   . VAL C 3 138 ? -25.723 -75.281 -1.417  1.000 145.420 ? 138 VAL CCC N   1 
ATOM   4215  C CA  . VAL C 3 138 ? -26.116 -74.728 -2.741  1.000 147.272 ? 138 VAL CCC CA  1 
ATOM   4216  C C   . VAL C 3 138 ? -27.150 -73.630 -2.499  1.000 147.292 ? 138 VAL CCC C   1 
ATOM   4217  O O   . VAL C 3 138 ? -28.238 -73.947 -1.982  1.000 148.860 ? 138 VAL CCC O   1 
ATOM   4218  C CB  . VAL C 3 138 ? -26.680 -75.833 -3.647  1.000 148.752 ? 138 VAL CCC CB  1 
ATOM   4219  C CG1 . VAL C 3 138 ? -26.953 -75.313 -5.047  1.000 149.043 ? 138 VAL CCC CG1 1 
ATOM   4220  C CG2 . VAL C 3 138 ? -25.756 -77.040 -3.683  1.000 151.673 ? 138 VAL CCC CG2 1 
ATOM   4221  N N   . VAL C 3 139 ? -26.820 -72.390 -2.857  1.000 147.956 ? 139 VAL CCC N   1 
ATOM   4222  C CA  . VAL C 3 139 ? -27.701 -71.208 -2.626  1.000 146.851 ? 139 VAL CCC CA  1 
ATOM   4223  C C   . VAL C 3 139 ? -28.368 -70.827 -3.945  1.000 142.272 ? 139 VAL CCC C   1 
ATOM   4224  O O   . VAL C 3 139 ? -27.701 -70.845 -4.993  1.000 140.219 ? 139 VAL CCC O   1 
ATOM   4225  C CB  . VAL C 3 139 ? -26.938 -70.010 -2.030  1.000 151.745 ? 139 VAL CCC CB  1 
ATOM   4226  C CG1 . VAL C 3 139 ? -27.889 -68.941 -1.506  1.000 151.842 ? 139 VAL CCC CG1 1 
ATOM   4227  C CG2 . VAL C 3 139 ? -25.978 -70.447 -0.936  1.000 155.432 ? 139 VAL CCC CG2 1 
ATOM   4228  N N   . CYS C 3 140 ? -29.649 -70.496 -3.853  1.000 140.156 ? 140 CYS CCC N   1 
ATOM   4229  C CA  . CYS C 3 140 ? -30.470 -69.933 -4.941  1.000 140.784 ? 140 CYS CCC CA  1 
ATOM   4230  C C   . CYS C 3 140 ? -31.047 -68.597 -4.476  1.000 140.603 ? 140 CYS CCC C   1 
ATOM   4231  O O   . CYS C 3 140 ? -31.483 -68.521 -3.311  1.000 140.275 ? 140 CYS CCC O   1 
ATOM   4232  C CB  . CYS C 3 140 ? -31.589 -70.893 -5.295  1.000 142.087 ? 140 CYS CCC CB  1 
ATOM   4233  S SG  . CYS C 3 140 ? -32.400 -70.454 -6.845  1.000 145.806 ? 140 CYS CCC SG  1 
ATOM   4234  N N   . LEU C 3 141 ? -31.060 -67.597 -5.360  1.000 141.569 ? 141 LEU CCC N   1 
ATOM   4235  C CA  . LEU C 3 141 ? -31.337 -66.173 -5.024  1.000 140.939 ? 141 LEU CCC CA  1 
ATOM   4236  C C   . LEU C 3 141 ? -32.393 -65.606 -5.981  1.000 137.991 ? 141 LEU CCC C   1 
ATOM   4237  O O   . LEU C 3 141 ? -32.127 -65.586 -7.190  1.000 139.967 ? 141 LEU CCC O   1 
ATOM   4238  C CB  . LEU C 3 141 ? -30.012 -65.405 -5.114  1.000 143.347 ? 141 LEU CCC CB  1 
ATOM   4239  C CG  . LEU C 3 141 ? -30.102 -63.883 -5.209  1.000 143.919 ? 141 LEU CCC CG  1 
ATOM   4240  C CD1 . LEU C 3 141 ? -30.840 -63.290 -4.018  1.000 143.191 ? 141 LEU CCC CD1 1 
ATOM   4241  C CD2 . LEU C 3 141 ? -28.709 -63.291 -5.320  1.000 146.140 ? 141 LEU CCC CD2 1 
ATOM   4242  N N   . LEU C 3 142 ? -33.543 -65.181 -5.446  1.000 133.899 ? 142 LEU CCC N   1 
ATOM   4243  C CA  . LEU C 3 142 ? -34.625 -64.471 -6.181  1.000 132.930 ? 142 LEU CCC CA  1 
ATOM   4244  C C   . LEU C 3 142 ? -34.570 -62.990 -5.799  1.000 133.611 ? 142 LEU CCC C   1 
ATOM   4245  O O   . LEU C 3 142 ? -35.046 -62.660 -4.699  1.000 135.419 ? 142 LEU CCC O   1 
ATOM   4246  C CB  . LEU C 3 142 ? -35.989 -65.053 -5.798  1.000 131.769 ? 142 LEU CCC CB  1 
ATOM   4247  C CG  . LEU C 3 142 ? -36.310 -66.456 -6.306  1.000 132.000 ? 142 LEU CCC CG  1 
ATOM   4248  C CD1 . LEU C 3 142 ? -35.368 -67.492 -5.712  1.000 131.866 ? 142 LEU CCC CD1 1 
ATOM   4249  C CD2 . LEU C 3 142 ? -37.755 -66.812 -5.992  1.000 132.118 ? 142 LEU CCC CD2 1 
ATOM   4250  N N   . ASN C 3 143 ? -34.025 -62.130 -6.662  1.000 133.899 ? 143 ASN CCC N   1 
ATOM   4251  C CA  . ASN C 3 143 ? -33.797 -60.699 -6.333  1.000 134.960 ? 143 ASN CCC CA  1 
ATOM   4252  C C   . ASN C 3 143 ? -34.960 -59.833 -6.834  1.000 136.618 ? 143 ASN CCC C   1 
ATOM   4253  O O   . ASN C 3 143 ? -35.410 -60.058 -7.961  1.000 137.387 ? 143 ASN CCC O   1 
ATOM   4254  C CB  . ASN C 3 143 ? -32.467 -60.198 -6.890  1.000 136.596 ? 143 ASN CCC CB  1 
ATOM   4255  C CG  . ASN C 3 143 ? -31.930 -59.025 -6.096  1.000 139.166 ? 143 ASN CCC CG  1 
ATOM   4256  O OD1 . ASN C 3 143 ? -31.911 -59.066 -4.866  1.000 138.782 ? 143 ASN CCC OD1 1 
ATOM   4257  N ND2 . ASN C 3 143 ? -31.504 -57.975 -6.783  1.000 142.787 ? 143 ASN CCC ND2 1 
ATOM   4258  N N   . ASN C 3 144 ? -35.417 -58.895 -5.997  1.000 140.663 ? 144 ASN CCC N   1 
ATOM   4259  C CA  . ASN C 3 144 ? -36.325 -57.764 -6.341  1.000 144.165 ? 144 ASN CCC CA  1 
ATOM   4260  C C   . ASN C 3 144 ? -37.565 -58.278 -7.075  1.000 143.569 ? 144 ASN CCC C   1 
ATOM   4261  O O   . ASN C 3 144 ? -37.519 -58.368 -8.317  1.000 144.700 ? 144 ASN CCC O   1 
ATOM   4262  C CB  . ASN C 3 144 ? -35.619 -56.701 -7.190  1.000 148.401 ? 144 ASN CCC CB  1 
ATOM   4263  C CG  . ASN C 3 144 ? -34.410 -56.098 -6.506  1.000 151.531 ? 144 ASN CCC CG  1 
ATOM   4264  O OD1 . ASN C 3 144 ? -33.360 -55.940 -7.125  1.000 155.166 ? 144 ASN CCC OD1 1 
ATOM   4265  N ND2 . ASN C 3 144 ? -34.542 -55.759 -5.232  1.000 152.114 ? 144 ASN CCC ND2 1 
ATOM   4266  N N   . PHE C 3 145 ? -38.636 -58.582 -6.339  1.000 143.193 ? 145 PHE CCC N   1 
ATOM   4267  C CA  . PHE C 3 145 ? -39.927 -59.031 -6.919  1.000 143.996 ? 145 PHE CCC CA  1 
ATOM   4268  C C   . PHE C 3 145 ? -41.104 -58.699 -5.995  1.000 143.592 ? 145 PHE CCC C   1 
ATOM   4269  O O   . PHE C 3 145 ? -40.902 -58.488 -4.787  1.000 142.612 ? 145 PHE CCC O   1 
ATOM   4270  C CB  . PHE C 3 145 ? -39.872 -60.531 -7.202  1.000 143.114 ? 145 PHE CCC CB  1 
ATOM   4271  C CG  . PHE C 3 145 ? -39.731 -61.396 -5.979  1.000 140.083 ? 145 PHE CCC CG  1 
ATOM   4272  C CD1 . PHE C 3 145 ? -38.482 -61.688 -5.448  1.000 138.143 ? 145 PHE CCC CD1 1 
ATOM   4273  C CD2 . PHE C 3 145 ? -40.856 -61.929 -5.374  1.000 140.146 ? 145 PHE CCC CD2 1 
ATOM   4274  C CE1 . PHE C 3 145 ? -38.366 -62.496 -4.329  1.000 138.032 ? 145 PHE CCC CE1 1 
ATOM   4275  C CE2 . PHE C 3 145 ? -40.740 -62.744 -4.260  1.000 140.205 ? 145 PHE CCC CE2 1 
ATOM   4276  C CZ  . PHE C 3 145 ? -39.495 -63.027 -3.742  1.000 139.307 ? 145 PHE CCC CZ  1 
ATOM   4277  N N   . TYR C 3 146 ? -42.298 -58.655 -6.588  1.000 143.959 ? 146 TYR CCC N   1 
ATOM   4278  C CA  . TYR C 3 146 ? -43.614 -58.514 -5.917  1.000 144.059 ? 146 TYR CCC CA  1 
ATOM   4279  C C   . TYR C 3 146 ? -44.651 -59.266 -6.746  1.000 145.933 ? 146 TYR CCC C   1 
ATOM   4280  O O   . TYR C 3 146 ? -44.665 -59.131 -7.967  1.000 149.840 ? 146 TYR CCC O   1 
ATOM   4281  C CB  . TYR C 3 146 ? -44.010 -57.041 -5.765  1.000 144.834 ? 146 TYR CCC CB  1 
ATOM   4282  C CG  . TYR C 3 146 ? -45.229 -56.857 -4.900  1.000 145.687 ? 146 TYR CCC CG  1 
ATOM   4283  C CD1 . TYR C 3 146 ? -45.114 -56.837 -3.521  1.000 143.959 ? 146 TYR CCC CD1 1 
ATOM   4284  C CD2 . TYR C 3 146 ? -46.502 -56.791 -5.447  1.000 148.432 ? 146 TYR CCC CD2 1 
ATOM   4285  C CE1 . TYR C 3 146 ? -46.225 -56.735 -2.703  1.000 145.005 ? 146 TYR CCC CE1 1 
ATOM   4286  C CE2 . TYR C 3 146 ? -47.624 -56.671 -4.642  1.000 149.720 ? 146 TYR CCC CE2 1 
ATOM   4287  C CZ  . TYR C 3 146 ? -47.483 -56.646 -3.264  1.000 147.802 ? 146 TYR CCC CZ  1 
ATOM   4288  O OH  . TYR C 3 146 ? -48.562 -56.556 -2.438  1.000 149.910 ? 146 TYR CCC OH  1 
ATOM   4289  N N   . PRO C 3 147 ? -45.571 -60.051 -6.142  1.000 146.841 ? 147 PRO CCC N   1 
ATOM   4290  C CA  . PRO C 3 147 ? -45.742 -60.128 -4.691  1.000 148.379 ? 147 PRO CCC CA  1 
ATOM   4291  C C   . PRO C 3 147 ? -44.804 -61.114 -3.980  1.000 148.216 ? 147 PRO CCC C   1 
ATOM   4292  O O   . PRO C 3 147 ? -43.874 -61.590 -4.603  1.000 144.681 ? 147 PRO CCC O   1 
ATOM   4293  C CB  . PRO C 3 147 ? -47.207 -60.571 -4.586  1.000 151.420 ? 147 PRO CCC CB  1 
ATOM   4294  C CG  . PRO C 3 147 ? -47.396 -61.495 -5.768  1.000 151.245 ? 147 PRO CCC CG  1 
ATOM   4295  C CD  . PRO C 3 147 ? -46.530 -60.905 -6.859  1.000 149.795 ? 147 PRO CCC CD  1 
ATOM   4296  N N   . ARG C 3 148 ? -45.073 -61.369 -2.695  1.000 151.558 ? 148 ARG CCC N   1 
ATOM   4297  C CA  . ARG C 3 148 ? -44.269 -62.246 -1.802  1.000 153.121 ? 148 ARG CCC CA  1 
ATOM   4298  C C   . ARG C 3 148 ? -44.313 -63.695 -2.295  1.000 152.365 ? 148 ARG CCC C   1 
ATOM   4299  O O   . ARG C 3 148 ? -43.242 -64.318 -2.403  1.000 148.080 ? 148 ARG CCC O   1 
ATOM   4300  C CB  . ARG C 3 148 ? -44.824 -62.173 -0.378  1.000 158.411 ? 148 ARG CCC CB  1 
ATOM   4301  C CG  . ARG C 3 148 ? -43.810 -62.474 0.719   1.000 160.551 ? 148 ARG CCC CG  1 
ATOM   4302  C CD  . ARG C 3 148 ? -44.255 -61.840 2.028   1.000 166.618 ? 148 ARG CCC CD  1 
ATOM   4303  N NE  . ARG C 3 148 ? -43.164 -61.436 2.907   1.000 169.201 ? 148 ARG CCC NE  1 
ATOM   4304  C CZ  . ARG C 3 148 ? -42.452 -62.267 3.664   1.000 171.244 ? 148 ARG CCC CZ  1 
ATOM   4305  N NH1 . ARG C 3 148 ? -42.695 -63.569 3.637   1.000 172.745 ? 148 ARG CCC NH1 1 
ATOM   4306  N NH2 . ARG C 3 148 ? -41.487 -61.792 4.438   1.000 170.824 ? 148 ARG CCC NH2 1 
ATOM   4307  N N   . GLU C 3 149 ? -45.518 -64.198 -2.577  1.000 157.311 ? 149 GLU CCC N   1 
ATOM   4308  C CA  . GLU C 3 149 ? -45.803 -65.634 -2.851  1.000 160.450 ? 149 GLU CCC CA  1 
ATOM   4309  C C   . GLU C 3 149 ? -45.043 -66.050 -4.111  1.000 155.787 ? 149 GLU CCC C   1 
ATOM   4310  O O   . GLU C 3 149 ? -45.577 -65.876 -5.225  1.000 157.240 ? 149 GLU CCC O   1 
ATOM   4311  C CB  . GLU C 3 149 ? -47.306 -65.900 -2.999  1.000 168.930 ? 149 GLU CCC CB  1 
ATOM   4312  C CG  . GLU C 3 149 ? -48.154 -65.252 -1.915  1.000 176.174 ? 149 GLU CCC CG  1 
ATOM   4313  C CD  . GLU C 3 149 ? -48.643 -63.844 -2.235  1.000 181.136 ? 149 GLU CCC CD  1 
ATOM   4314  O OE1 . GLU C 3 149 ? -49.546 -63.723 -3.098  1.000 184.665 ? 149 GLU CCC OE1 1 
ATOM   4315  O OE2 . GLU C 3 149 ? -48.107 -62.865 -1.635  1.000 181.840 ? 149 GLU CCC OE2 1 
ATOM   4316  N N   . ALA C 3 150 ? -43.822 -66.547 -3.916  1.000 150.459 ? 150 ALA CCC N   1 
ATOM   4317  C CA  . ALA C 3 150 ? -42.962 -67.153 -4.955  1.000 147.873 ? 150 ALA CCC CA  1 
ATOM   4318  C C   . ALA C 3 150 ? -42.642 -68.591 -4.539  1.000 147.243 ? 150 ALA CCC C   1 
ATOM   4319  O O   . ALA C 3 150 ? -42.160 -68.783 -3.403  1.000 148.709 ? 150 ALA CCC O   1 
ATOM   4320  C CB  . ALA C 3 150 ? -41.711 -66.331 -5.123  1.000 145.690 ? 150 ALA CCC CB  1 
ATOM   4321  N N   . LYS C 3 151 ? -42.932 -69.560 -5.413  1.000 146.000 ? 151 LYS CCC N   1 
ATOM   4322  C CA  . LYS C 3 151 ? -42.581 -70.991 -5.218  1.000 144.243 ? 151 LYS CCC CA  1 
ATOM   4323  C C   . LYS C 3 151 ? -41.158 -71.209 -5.736  1.000 139.489 ? 151 LYS CCC C   1 
ATOM   4324  O O   . LYS C 3 151 ? -40.903 -70.906 -6.914  1.000 137.763 ? 151 LYS CCC O   1 
ATOM   4325  C CB  . LYS C 3 151 ? -43.587 -71.903 -5.927  1.000 148.056 ? 151 LYS CCC CB  1 
ATOM   4326  C CG  . LYS C 3 151 ? -43.236 -73.388 -5.947  1.000 150.083 ? 151 LYS CCC CG  1 
ATOM   4327  C CD  . LYS C 3 151 ? -44.172 -74.222 -6.808  1.000 155.133 ? 151 LYS CCC CD  1 
ATOM   4328  C CE  . LYS C 3 151 ? -43.531 -75.482 -7.363  1.000 157.073 ? 151 LYS CCC CE  1 
ATOM   4329  N NZ  . LYS C 3 151 ? -44.382 -76.140 -8.386  1.000 161.185 ? 151 LYS CCC NZ  1 
ATOM   4330  N N   . VAL C 3 152 ? -40.267 -71.677 -4.862  1.000 137.317 ? 152 VAL CCC N   1 
ATOM   4331  C CA  . VAL C 3 152 ? -38.905 -72.164 -5.220  1.000 136.711 ? 152 VAL CCC CA  1 
ATOM   4332  C C   . VAL C 3 152 ? -38.895 -73.667 -4.964  1.000 140.023 ? 152 VAL CCC C   1 
ATOM   4333  O O   . VAL C 3 152 ? -39.315 -74.061 -3.856  1.000 143.198 ? 152 VAL CCC O   1 
ATOM   4334  C CB  . VAL C 3 152 ? -37.810 -71.459 -4.400  1.000 133.902 ? 152 VAL CCC CB  1 
ATOM   4335  C CG1 . VAL C 3 152 ? -36.434 -72.037 -4.680  1.000 132.189 ? 152 VAL CCC CG1 1 
ATOM   4336  C CG2 . VAL C 3 152 ? -37.818 -69.959 -4.631  1.000 133.568 ? 152 VAL CCC CG2 1 
ATOM   4337  N N   . GLN C 3 153 ? -38.462 -74.462 -5.946  1.000 142.219 ? 153 GLN CCC N   1 
ATOM   4338  C CA  . GLN C 3 153 ? -38.241 -75.920 -5.765  1.000 144.139 ? 153 GLN CCC CA  1 
ATOM   4339  C C   . GLN C 3 153 ? -36.884 -76.330 -6.345  1.000 142.318 ? 153 GLN CCC C   1 
ATOM   4340  O O   . GLN C 3 153 ? -36.507 -75.828 -7.423  1.000 140.866 ? 153 GLN CCC O   1 
ATOM   4341  C CB  . GLN C 3 153 ? -39.361 -76.756 -6.381  1.000 147.953 ? 153 GLN CCC CB  1 
ATOM   4342  C CG  . GLN C 3 153 ? -39.194 -78.235 -6.052  1.000 151.636 ? 153 GLN CCC CG  1 
ATOM   4343  C CD  . GLN C 3 153 ? -40.471 -78.929 -5.637  1.000 155.602 ? 153 GLN CCC CD  1 
ATOM   4344  O OE1 . GLN C 3 153 ? -41.563 -78.595 -6.091  1.000 157.933 ? 153 GLN CCC OE1 1 
ATOM   4345  N NE2 . GLN C 3 153 ? -40.339 -79.912 -4.758  1.000 156.644 ? 153 GLN CCC NE2 1 
ATOM   4346  N N   . TRP C 3 154 ? -36.192 -77.217 -5.626  1.000 141.080 ? 154 TRP CCC N   1 
ATOM   4347  C CA  . TRP C 3 154 ? -34.888 -77.806 -6.019  1.000 139.457 ? 154 TRP CCC CA  1 
ATOM   4348  C C   . TRP C 3 154 ? -35.120 -79.083 -6.824  1.000 142.304 ? 154 TRP CCC C   1 
ATOM   4349  O O   . TRP C 3 154 ? -35.994 -79.880 -6.429  1.000 145.234 ? 154 TRP CCC O   1 
ATOM   4350  C CB  . TRP C 3 154 ? -34.041 -78.086 -4.778  1.000 136.611 ? 154 TRP CCC CB  1 
ATOM   4351  C CG  . TRP C 3 154 ? -33.617 -76.836 -4.087  1.000 133.225 ? 154 TRP CCC CG  1 
ATOM   4352  C CD1 . TRP C 3 154 ? -34.281 -76.180 -3.096  1.000 133.351 ? 154 TRP CCC CD1 1 
ATOM   4353  C CD2 . TRP C 3 154 ? -32.436 -76.069 -4.360  1.000 131.647 ? 154 TRP CCC CD2 1 
ATOM   4354  N NE1 . TRP C 3 154 ? -33.584 -75.063 -2.725  1.000 132.742 ? 154 TRP CCC NE1 1 
ATOM   4355  C CE2 . TRP C 3 154 ? -32.448 -74.969 -3.481  1.000 131.586 ? 154 TRP CCC CE2 1 
ATOM   4356  C CE3 . TRP C 3 154 ? -31.367 -76.213 -5.246  1.000 132.591 ? 154 TRP CCC CE3 1 
ATOM   4357  C CZ2 . TRP C 3 154 ? -31.429 -74.019 -3.463  1.000 131.990 ? 154 TRP CCC CZ2 1 
ATOM   4358  C CZ3 . TRP C 3 154 ? -30.361 -75.274 -5.232  1.000 133.494 ? 154 TRP CCC CZ3 1 
ATOM   4359  C CH2 . TRP C 3 154 ? -30.391 -74.194 -4.349  1.000 133.357 ? 154 TRP CCC CH2 1 
ATOM   4360  N N   . LYS C 3 155 ? -34.367 -79.237 -7.911  1.000 142.391 ? 155 LYS CCC N   1 
ATOM   4361  C CA  . LYS C 3 155 ? -34.160 -80.517 -8.622  1.000 144.556 ? 155 LYS CCC CA  1 
ATOM   4362  C C   . LYS C 3 155 ? -32.687 -80.889 -8.466  1.000 142.197 ? 155 LYS CCC C   1 
ATOM   4363  O O   . LYS C 3 155 ? -31.830 -79.999 -8.580  1.000 140.218 ? 155 LYS CCC O   1 
ATOM   4364  C CB  . LYS C 3 155 ? -34.531 -80.374 -10.098 1.000 148.596 ? 155 LYS CCC CB  1 
ATOM   4365  C CG  . LYS C 3 155 ? -35.944 -79.876 -10.360 1.000 151.556 ? 155 LYS CCC CG  1 
ATOM   4366  C CD  . LYS C 3 155 ? -36.225 -79.605 -11.830 1.000 155.459 ? 155 LYS CCC CD  1 
ATOM   4367  C CE  . LYS C 3 155 ? -37.656 -79.187 -12.094 1.000 157.635 ? 155 LYS CCC CE  1 
ATOM   4368  N NZ  . LYS C 3 155 ? -37.987 -79.202 -13.538 1.000 160.077 ? 155 LYS CCC NZ  1 
ATOM   4369  N N   . VAL C 3 156 ? -32.416 -82.153 -8.172  1.000 141.947 ? 156 VAL CCC N   1 
ATOM   4370  C CA  . VAL C 3 156 ? -31.054 -82.750 -8.223  1.000 141.850 ? 156 VAL CCC CA  1 
ATOM   4371  C C   . VAL C 3 156 ? -31.140 -83.958 -9.155  1.000 144.457 ? 156 VAL CCC C   1 
ATOM   4372  O O   . VAL C 3 156 ? -31.765 -84.955 -8.766  1.000 147.439 ? 156 VAL CCC O   1 
ATOM   4373  C CB  . VAL C 3 156 ? -30.568 -83.106 -6.809  1.000 140.978 ? 156 VAL CCC CB  1 
ATOM   4374  C CG1 . VAL C 3 156 ? -29.298 -83.935 -6.825  1.000 141.727 ? 156 VAL CCC CG1 1 
ATOM   4375  C CG2 . VAL C 3 156 ? -30.379 -81.843 -5.986  1.000 139.242 ? 156 VAL CCC CG2 1 
ATOM   4376  N N   . ASP C 3 157 ? -30.588 -83.837 -10.362 1.000 145.321 ? 157 ASP CCC N   1 
ATOM   4377  C CA  . ASP C 3 157 ? -30.768 -84.826 -11.455 1.000 148.886 ? 157 ASP CCC CA  1 
ATOM   4378  C C   . ASP C 3 157 ? -32.267 -84.875 -11.803 1.000 150.760 ? 157 ASP CCC C   1 
ATOM   4379  O O   . ASP C 3 157 ? -32.852 -85.976 -11.770 1.000 151.740 ? 157 ASP CCC O   1 
ATOM   4380  C CB  . ASP C 3 157 ? -30.173 -86.186 -11.064 1.000 150.096 ? 157 ASP CCC CB  1 
ATOM   4381  C CG  . ASP C 3 157 ? -28.724 -86.148 -10.588 1.000 148.690 ? 157 ASP CCC CG  1 
ATOM   4382  O OD1 . ASP C 3 157 ? -28.010 -85.174 -10.918 1.000 147.081 ? 157 ASP CCC OD1 1 
ATOM   4383  O OD2 . ASP C 3 157 ? -28.312 -87.106 -9.896  1.000 149.023 ? 157 ASP CCC OD2 1 
ATOM   4384  N N   . ASN C 3 158 ? -32.854 -83.711 -12.117 1.000 151.960 ? 158 ASN CCC N   1 
ATOM   4385  C CA  . ASN C 3 158 ? -34.286 -83.525 -12.487 1.000 154.992 ? 158 ASN CCC CA  1 
ATOM   4386  C C   . ASN C 3 158 ? -35.137 -84.445 -11.611 1.000 156.978 ? 158 ASN CCC C   1 
ATOM   4387  O O   . ASN C 3 158 ? -35.921 -85.247 -12.167 1.000 160.549 ? 158 ASN CCC O   1 
ATOM   4388  C CB  . ASN C 3 158 ? -34.545 -83.749 -13.981 1.000 159.717 ? 158 ASN CCC CB  1 
ATOM   4389  C CG  . ASN C 3 158 ? -34.149 -82.574 -14.852 1.000 161.388 ? 158 ASN CCC CG  1 
ATOM   4390  O OD1 . ASN C 3 158 ? -34.173 -81.418 -14.417 1.000 157.555 ? 158 ASN CCC OD1 1 
ATOM   4391  N ND2 . ASN C 3 158 ? -33.804 -82.870 -16.097 1.000 166.019 ? 158 ASN CCC ND2 1 
ATOM   4392  N N   . ALA C 3 159 ? -34.945 -84.333 -10.292 1.000 156.318 ? 159 ALA CCC N   1 
ATOM   4393  C CA  . ALA C 3 159 ? -35.692 -85.042 -9.226  1.000 158.647 ? 159 ALA CCC CA  1 
ATOM   4394  C C   . ALA C 3 159 ? -35.828 -84.116 -8.012  1.000 156.248 ? 159 ALA CCC C   1 
ATOM   4395  O O   . ALA C 3 159 ? -34.789 -83.708 -7.456  1.000 154.246 ? 159 ALA CCC O   1 
ATOM   4396  C CB  . ALA C 3 159 ? -34.986 -86.323 -8.859  1.000 160.464 ? 159 ALA CCC CB  1 
ATOM   4397  N N   . LEU C 3 160 ? -37.061 -83.804 -7.616  1.000 157.411 ? 160 LEU CCC N   1 
ATOM   4398  C CA  . LEU C 3 160 ? -37.349 -82.738 -6.623  1.000 156.406 ? 160 LEU CCC CA  1 
ATOM   4399  C C   . LEU C 3 160 ? -36.719 -83.121 -5.287  1.000 156.419 ? 160 LEU CCC C   1 
ATOM   4400  O O   . LEU C 3 160 ? -37.020 -84.219 -4.794  1.000 159.220 ? 160 LEU CCC O   1 
ATOM   4401  C CB  . LEU C 3 160 ? -38.860 -82.543 -6.471  1.000 159.512 ? 160 LEU CCC CB  1 
ATOM   4402  C CG  . LEU C 3 160 ? -39.616 -82.208 -7.755  1.000 162.878 ? 160 LEU CCC CG  1 
ATOM   4403  C CD1 . LEU C 3 160 ? -41.115 -82.139 -7.499  1.000 166.017 ? 160 LEU CCC CD1 1 
ATOM   4404  C CD2 . LEU C 3 160 ? -39.114 -80.907 -8.371  1.000 161.278 ? 160 LEU CCC CD2 1 
ATOM   4405  N N   . GLN C 3 161 ? -35.865 -82.253 -4.747  1.000 154.728 ? 161 GLN CCC N   1 
ATOM   4406  C CA  . GLN C 3 161 ? -35.399 -82.330 -3.339  1.000 154.385 ? 161 GLN CCC CA  1 
ATOM   4407  C C   . GLN C 3 161 ? -36.368 -81.516 -2.474  1.000 154.533 ? 161 GLN CCC C   1 
ATOM   4408  O O   . GLN C 3 161 ? -36.938 -80.529 -2.983  1.000 151.474 ? 161 GLN CCC O   1 
ATOM   4409  C CB  . GLN C 3 161 ? -33.940 -81.889 -3.224  1.000 151.355 ? 161 GLN CCC CB  1 
ATOM   4410  C CG  . GLN C 3 161 ? -32.974 -82.838 -3.922  1.000 150.743 ? 161 GLN CCC CG  1 
ATOM   4411  C CD  . GLN C 3 161 ? -32.665 -84.080 -3.123  1.000 152.385 ? 161 GLN CCC CD  1 
ATOM   4412  O OE1 . GLN C 3 161 ? -33.266 -84.333 -2.083  1.000 153.835 ? 161 GLN CCC OE1 1 
ATOM   4413  N NE2 . GLN C 3 161 ? -31.728 -84.879 -3.612  1.000 152.079 ? 161 GLN CCC NE2 1 
ATOM   4414  N N   . SER C 3 162 ? -36.561 -81.956 -1.227  1.000 157.215 ? 162 SER CCC N   1 
ATOM   4415  C CA  . SER C 3 162 ? -37.694 -81.577 -0.344  1.000 158.554 ? 162 SER CCC CA  1 
ATOM   4416  C C   . SER C 3 162 ? -37.396 -81.986 1.106   1.000 158.366 ? 162 SER CCC C   1 
ATOM   4417  O O   . SER C 3 162 ? -37.409 -83.198 1.387   1.000 159.686 ? 162 SER CCC O   1 
ATOM   4418  C CB  . SER C 3 162 ? -38.962 -82.215 -0.854  1.000 162.514 ? 162 SER CCC CB  1 
ATOM   4419  O OG  . SER C 3 162 ? -40.046 -81.974 0.027   1.000 167.155 ? 162 SER CCC OG  1 
ATOM   4420  N N   . GLY C 3 163 ? -37.122 -81.007 1.979   1.000 156.148 ? 163 GLY CCC N   1 
ATOM   4421  C CA  . GLY C 3 163 ? -36.838 -81.203 3.416   1.000 157.894 ? 163 GLY CCC CA  1 
ATOM   4422  C C   . GLY C 3 163 ? -35.447 -80.727 3.811   1.000 155.702 ? 163 GLY CCC C   1 
ATOM   4423  O O   . GLY C 3 163 ? -35.216 -80.528 5.022   1.000 157.687 ? 163 GLY CCC O   1 
ATOM   4424  N N   . ASN C 3 164 ? -34.556 -80.556 2.829   1.000 153.231 ? 164 ASN CCC N   1 
ATOM   4425  C CA  . ASN C 3 164 ? -33.124 -80.203 3.018   1.000 152.759 ? 164 ASN CCC CA  1 
ATOM   4426  C C   . ASN C 3 164 ? -32.860 -78.789 2.478   1.000 149.851 ? 164 ASN CCC C   1 
ATOM   4427  O O   . ASN C 3 164 ? -31.674 -78.416 2.409   1.000 148.009 ? 164 ASN CCC O   1 
ATOM   4428  C CB  . ASN C 3 164 ? -32.207 -81.243 2.368   1.000 153.052 ? 164 ASN CCC CB  1 
ATOM   4429  C CG  . ASN C 3 164 ? -32.691 -81.692 1.006   1.000 153.012 ? 164 ASN CCC CG  1 
ATOM   4430  O OD1 . ASN C 3 164 ? -33.303 -80.926 0.266   1.000 151.413 ? 164 ASN CCC OD1 1 
ATOM   4431  N ND2 . ASN C 3 164 ? -32.418 -82.938 0.668   1.000 155.745 ? 164 ASN CCC ND2 1 
ATOM   4432  N N   . SER C 3 165 ? -33.912 -78.043 2.115   1.000 148.192 ? 165 SER CCC N   1 
ATOM   4433  C CA  . SER C 3 165 ? -33.828 -76.609 1.722   1.000 144.847 ? 165 SER CCC CA  1 
ATOM   4434  C C   . SER C 3 165 ? -34.380 -75.744 2.859   1.000 145.231 ? 165 SER CCC C   1 
ATOM   4435  O O   . SER C 3 165 ? -35.064 -76.307 3.737   1.000 147.455 ? 165 SER CCC O   1 
ATOM   4436  C CB  . SER C 3 165 ? -34.551 -76.327 0.425   1.000 143.318 ? 165 SER CCC CB  1 
ATOM   4437  O OG  . SER C 3 165 ? -35.938 -76.126 0.650   1.000 143.419 ? 165 SER CCC OG  1 
ATOM   4438  N N   . GLN C 3 166 ? -34.095 -74.438 2.824   1.000 142.825 ? 166 GLN CCC N   1 
ATOM   4439  C CA  . GLN C 3 166 ? -34.578 -73.439 3.814   1.000 143.260 ? 166 GLN CCC CA  1 
ATOM   4440  C C   . GLN C 3 166 ? -34.606 -72.055 3.165   1.000 142.539 ? 166 GLN CCC C   1 
ATOM   4441  O O   . GLN C 3 166 ? -33.536 -71.591 2.717   1.000 141.286 ? 166 GLN CCC O   1 
ATOM   4442  C CB  . GLN C 3 166 ? -33.667 -73.408 5.039   1.000 143.183 ? 166 GLN CCC CB  1 
ATOM   4443  C CG  . GLN C 3 166 ? -34.221 -74.143 6.244   1.000 144.396 ? 166 GLN CCC CG  1 
ATOM   4444  C CD  . GLN C 3 166 ? -33.198 -74.159 7.352   1.000 145.973 ? 166 GLN CCC CD  1 
ATOM   4445  O OE1 . GLN C 3 166 ? -32.486 -73.184 7.582   1.000 144.404 ? 166 GLN CCC OE1 1 
ATOM   4446  N NE2 . GLN C 3 166 ? -33.098 -75.284 8.037   1.000 149.300 ? 166 GLN CCC NE2 1 
ATOM   4447  N N   . GLU C 3 167 ? -35.780 -71.419 3.140   1.000 145.419 ? 167 GLU CCC N   1 
ATOM   4448  C CA  . GLU C 3 167 ? -35.985 -70.082 2.522   1.000 146.593 ? 167 GLU CCC CA  1 
ATOM   4449  C C   . GLU C 3 167 ? -35.782 -68.994 3.582   1.000 146.454 ? 167 GLU CCC C   1 
ATOM   4450  O O   . GLU C 3 167 ? -36.102 -69.225 4.766   1.000 147.282 ? 167 GLU CCC O   1 
ATOM   4451  C CB  . GLU C 3 167 ? -37.373 -69.978 1.878   1.000 148.786 ? 167 GLU CCC CB  1 
ATOM   4452  C CG  . GLU C 3 167 ? -37.556 -70.892 0.670   1.000 149.856 ? 167 GLU CCC CG  1 
ATOM   4453  C CD  . GLU C 3 167 ? -38.867 -70.743 -0.093  1.000 151.016 ? 167 GLU CCC CD  1 
ATOM   4454  O OE1 . GLU C 3 167 ? -39.570 -69.734 0.128   1.000 150.682 ? 167 GLU CCC OE1 1 
ATOM   4455  O OE2 . GLU C 3 167 ? -39.187 -71.643 -0.909  1.000 151.526 ? 167 GLU CCC OE2 1 
ATOM   4456  N N   . SER C 3 168 ? -35.258 -67.850 3.150   1.000 145.009 ? 168 SER CCC N   1 
ATOM   4457  C CA  . SER C 3 168 ? -35.150 -66.610 3.953   1.000 146.141 ? 168 SER CCC CA  1 
ATOM   4458  C C   . SER C 3 168 ? -35.488 -65.412 3.062   1.000 145.047 ? 168 SER CCC C   1 
ATOM   4459  O O   . SER C 3 168 ? -34.824 -65.239 2.022   1.000 143.474 ? 168 SER CCC O   1 
ATOM   4460  C CB  . SER C 3 168 ? -33.793 -66.482 4.560   1.000 148.263 ? 168 SER CCC CB  1 
ATOM   4461  O OG  . SER C 3 168 ? -33.799 -65.446 5.529   1.000 151.898 ? 168 SER CCC OG  1 
ATOM   4462  N N   . VAL C 3 169 ? -36.489 -64.630 3.472   1.000 146.141 ? 169 VAL CCC N   1 
ATOM   4463  C CA  . VAL C 3 169 ? -37.159 -63.574 2.657   1.000 144.435 ? 169 VAL CCC CA  1 
ATOM   4464  C C   . VAL C 3 169 ? -36.949 -62.217 3.329   1.000 143.452 ? 169 VAL CCC C   1 
ATOM   4465  O O   . VAL C 3 169 ? -37.347 -62.075 4.508   1.000 145.125 ? 169 VAL CCC O   1 
ATOM   4466  C CB  . VAL C 3 169 ? -38.665 -63.876 2.525   1.000 146.930 ? 169 VAL CCC CB  1 
ATOM   4467  C CG1 . VAL C 3 169 ? -39.396 -62.817 1.715   1.000 147.358 ? 169 VAL CCC CG1 1 
ATOM   4468  C CG2 . VAL C 3 169 ? -38.919 -65.261 1.952   1.000 147.746 ? 169 VAL CCC CG2 1 
ATOM   4469  N N   . THR C 3 170 ? -36.413 -61.245 2.591   1.000 140.738 ? 170 THR CCC N   1 
ATOM   4470  C CA  . THR C 3 170 ? -36.266 -59.839 3.055   1.000 143.609 ? 170 THR CCC CA  1 
ATOM   4471  C C   . THR C 3 170 ? -37.653 -59.188 3.114   1.000 144.816 ? 170 THR CCC C   1 
ATOM   4472  O O   . THR C 3 170 ? -38.473 -59.493 2.237   1.000 144.070 ? 170 THR CCC O   1 
ATOM   4473  C CB  . THR C 3 170 ? -35.323 -59.031 2.152   1.000 143.041 ? 170 THR CCC CB  1 
ATOM   4474  O OG1 . THR C 3 170 ? -36.047 -58.603 1.000   1.000 142.185 ? 170 THR CCC OG1 1 
ATOM   4475  C CG2 . THR C 3 170 ? -34.092 -59.802 1.724   1.000 141.765 ? 170 THR CCC CG2 1 
ATOM   4476  N N   . GLU C 3 171 ? -37.902 -58.326 4.107   1.000 147.713 ? 171 GLU CCC N   1 
ATOM   4477  C CA  . GLU C 3 171 ? -39.137 -57.498 4.206   1.000 147.985 ? 171 GLU CCC CA  1 
ATOM   4478  C C   . GLU C 3 171 ? -39.163 -56.520 3.029   1.000 143.806 ? 171 GLU CCC C   1 
ATOM   4479  O O   . GLU C 3 171 ? -38.127 -56.406 2.341   1.000 141.347 ? 171 GLU CCC O   1 
ATOM   4480  C CB  . GLU C 3 171 ? -39.189 -56.765 5.550   1.000 152.765 ? 171 GLU CCC CB  1 
ATOM   4481  C CG  . GLU C 3 171 ? -39.438 -57.692 6.723   1.000 155.300 ? 171 GLU CCC CG  1 
ATOM   4482  C CD  . GLU C 3 171 ? -40.671 -58.555 6.528   1.000 156.973 ? 171 GLU CCC CD  1 
ATOM   4483  O OE1 . GLU C 3 171 ? -41.792 -58.008 6.621   1.000 158.136 ? 171 GLU CCC OE1 1 
ATOM   4484  O OE2 . GLU C 3 171 ? -40.504 -59.759 6.237   1.000 158.269 ? 171 GLU CCC OE2 1 
ATOM   4485  N N   . GLN C 3 172 ? -40.298 -55.856 2.794   1.000 141.199 ? 172 GLN CCC N   1 
ATOM   4486  C CA  . GLN C 3 172 ? -40.457 -54.931 1.640   1.000 139.392 ? 172 GLN CCC CA  1 
ATOM   4487  C C   . GLN C 3 172 ? -39.297 -53.935 1.652   1.000 137.896 ? 172 GLN CCC C   1 
ATOM   4488  O O   . GLN C 3 172 ? -38.839 -53.586 2.752   1.000 137.819 ? 172 GLN CCC O   1 
ATOM   4489  C CB  . GLN C 3 172 ? -41.810 -54.221 1.661   1.000 141.103 ? 172 GLN CCC CB  1 
ATOM   4490  C CG  . GLN C 3 172 ? -42.811 -54.836 0.699   1.000 140.072 ? 172 GLN CCC CG  1 
ATOM   4491  C CD  . GLN C 3 172 ? -44.100 -54.056 0.624   1.000 142.421 ? 172 GLN CCC CD  1 
ATOM   4492  O OE1 . GLN C 3 172 ? -44.243 -52.967 1.177   1.000 144.886 ? 172 GLN CCC OE1 1 
ATOM   4493  N NE2 . GLN C 3 172 ? -45.071 -54.628 -0.061  1.000 144.098 ? 172 GLN CCC NE2 1 
ATOM   4494  N N   . ASP C 3 173 ? -38.839 -53.520 0.468   1.000 136.667 ? 173 ASP CCC N   1 
ATOM   4495  C CA  . ASP C 3 173 ? -37.588 -52.737 0.295   1.000 137.559 ? 173 ASP CCC CA  1 
ATOM   4496  C C   . ASP C 3 173 ? -37.816 -51.283 0.706   1.000 140.540 ? 173 ASP CCC C   1 
ATOM   4497  O O   . ASP C 3 173 ? -38.910 -50.737 0.439   1.000 138.041 ? 173 ASP CCC O   1 
ATOM   4498  C CB  . ASP C 3 173 ? -37.053 -52.793 -1.136  1.000 137.039 ? 173 ASP CCC CB  1 
ATOM   4499  C CG  . ASP C 3 173 ? -35.848 -51.895 -1.369  1.000 139.754 ? 173 ASP CCC CG  1 
ATOM   4500  O OD1 . ASP C 3 173 ? -34.983 -51.844 -0.478  1.000 141.911 ? 173 ASP CCC OD1 1 
ATOM   4501  O OD2 . ASP C 3 173 ? -35.798 -51.227 -2.428  1.000 141.511 ? 173 ASP CCC OD2 1 
ATOM   4502  N N   . SER C 3 174 ? -36.768 -50.702 1.303   1.000 145.673 ? 174 SER CCC N   1 
ATOM   4503  C CA  . SER C 3 174 ? -36.627 -49.290 1.744   1.000 150.520 ? 174 SER CCC CA  1 
ATOM   4504  C C   . SER C 3 174 ? -36.981 -48.318 0.603   1.000 153.574 ? 174 SER CCC C   1 
ATOM   4505  O O   . SER C 3 174 ? -37.430 -47.195 0.911   1.000 155.202 ? 174 SER CCC O   1 
ATOM   4506  C CB  . SER C 3 174 ? -35.213 -49.061 2.256   1.000 151.740 ? 174 SER CCC CB  1 
ATOM   4507  O OG  . SER C 3 174 ? -34.590 -50.286 2.658   1.000 147.349 ? 174 SER CCC OG  1 
ATOM   4508  N N   . LYS C 3 175 ? -36.781 -48.734 -0.657  1.000 154.417 ? 175 LYS CCC N   1 
ATOM   4509  C CA  . LYS C 3 175 ? -36.862 -47.883 -1.876  1.000 157.170 ? 175 LYS CCC CA  1 
ATOM   4510  C C   . LYS C 3 175 ? -38.038 -48.325 -2.757  1.000 155.847 ? 175 LYS CCC C   1 
ATOM   4511  O O   . LYS C 3 175 ? -38.967 -47.516 -2.921  1.000 160.498 ? 175 LYS CCC O   1 
ATOM   4512  C CB  . LYS C 3 175 ? -35.535 -47.939 -2.643  1.000 159.504 ? 175 LYS CCC CB  1 
ATOM   4513  C CG  . LYS C 3 175 ? -34.306 -47.554 -1.829  1.000 162.977 ? 175 LYS CCC CG  1 
ATOM   4514  C CD  . LYS C 3 175 ? -32.987 -47.893 -2.491  1.000 165.123 ? 175 LYS CCC CD  1 
ATOM   4515  C CE  . LYS C 3 175 ? -31.804 -47.684 -1.571  1.000 167.900 ? 175 LYS CCC CE  1 
ATOM   4516  N NZ  . LYS C 3 175 ? -31.783 -46.303 -1.031  1.000 172.003 ? 175 LYS CCC NZ  1 
ATOM   4517  N N   . ASP C 3 176 ? -38.016 -49.557 -3.280  1.000 153.321 ? 176 ASP CCC N   1 
ATOM   4518  C CA  . ASP C 3 176 ? -38.860 -49.988 -4.434  1.000 154.993 ? 176 ASP CCC CA  1 
ATOM   4519  C C   . ASP C 3 176 ? -40.000 -50.937 -4.018  1.000 151.634 ? 176 ASP CCC C   1 
ATOM   4520  O O   . ASP C 3 176 ? -40.699 -51.428 -4.923  1.000 149.331 ? 176 ASP CCC O   1 
ATOM   4521  C CB  . ASP C 3 176 ? -37.989 -50.628 -5.521  1.000 158.452 ? 176 ASP CCC CB  1 
ATOM   4522  C CG  . ASP C 3 176 ? -37.493 -52.034 -5.204  1.000 158.989 ? 176 ASP CCC CG  1 
ATOM   4523  O OD1 . ASP C 3 176 ? -37.914 -52.593 -4.176  1.000 158.913 ? 176 ASP CCC OD1 1 
ATOM   4524  O OD2 . ASP C 3 176 ? -36.691 -52.574 -6.000  1.000 163.431 ? 176 ASP CCC OD2 1 
ATOM   4525  N N   . SER C 3 177 ? -40.180 -51.205 -2.720  1.000 151.139 ? 177 SER CCC N   1 
ATOM   4526  C CA  . SER C 3 177 ? -41.315 -51.979 -2.143  1.000 148.908 ? 177 SER CCC CA  1 
ATOM   4527  C C   . SER C 3 177 ? -41.356 -53.413 -2.692  1.000 144.568 ? 177 SER CCC C   1 
ATOM   4528  O O   . SER C 3 177 ? -42.466 -53.965 -2.800  1.000 142.187 ? 177 SER CCC O   1 
ATOM   4529  C CB  . SER C 3 177 ? -42.624 -51.265 -2.385  1.000 151.064 ? 177 SER CCC CB  1 
ATOM   4530  O OG  . SER C 3 177 ? -42.535 -49.891 -2.029  1.000 154.336 ? 177 SER CCC OG  1 
ATOM   4531  N N   . THR C 3 178 ? -40.194 -53.998 -3.001  1.000 143.919 ? 178 THR CCC N   1 
ATOM   4532  C CA  . THR C 3 178 ? -40.039 -55.412 -3.442  1.000 143.168 ? 178 THR CCC CA  1 
ATOM   4533  C C   . THR C 3 178 ? -39.445 -56.256 -2.313  1.000 141.410 ? 178 THR CCC C   1 
ATOM   4534  O O   . THR C 3 178 ? -38.801 -55.695 -1.411  1.000 142.181 ? 178 THR CCC O   1 
ATOM   4535  C CB  . THR C 3 178 ? -39.139 -55.563 -4.678  1.000 143.100 ? 178 THR CCC CB  1 
ATOM   4536  O OG1 . THR C 3 178 ? -37.787 -55.270 -4.319  1.000 142.611 ? 178 THR CCC OG1 1 
ATOM   4537  C CG2 . THR C 3 178 ? -39.575 -54.694 -5.836  1.000 144.823 ? 178 THR CCC CG2 1 
ATOM   4538  N N   . TYR C 3 179 ? -39.660 -57.566 -2.394  1.000 139.410 ? 179 TYR CCC N   1 
ATOM   4539  C CA  . TYR C 3 179 ? -38.988 -58.598 -1.572  1.000 137.879 ? 179 TYR CCC CA  1 
ATOM   4540  C C   . TYR C 3 179 ? -37.822 -59.178 -2.382  1.000 135.858 ? 179 TYR CCC C   1 
ATOM   4541  O O   . TYR C 3 179 ? -37.739 -58.916 -3.598  1.000 136.805 ? 179 TYR CCC O   1 
ATOM   4542  C CB  . TYR C 3 179 ? -39.998 -59.675 -1.176  1.000 138.657 ? 179 TYR CCC CB  1 
ATOM   4543  C CG  . TYR C 3 179 ? -41.303 -59.168 -0.610  1.000 141.765 ? 179 TYR CCC CG  1 
ATOM   4544  C CD1 . TYR C 3 179 ? -41.392 -58.708 0.696   1.000 143.567 ? 179 TYR CCC CD1 1 
ATOM   4545  C CD2 . TYR C 3 179 ? -42.467 -59.192 -1.362  1.000 143.965 ? 179 TYR CCC CD2 1 
ATOM   4546  C CE1 . TYR C 3 179 ? -42.592 -58.271 1.238   1.000 145.890 ? 179 TYR CCC CE1 1 
ATOM   4547  C CE2 . TYR C 3 179 ? -43.676 -58.752 -0.839  1.000 147.479 ? 179 TYR CCC CE2 1 
ATOM   4548  C CZ  . TYR C 3 179 ? -43.741 -58.288 0.466   1.000 147.999 ? 179 TYR CCC CZ  1 
ATOM   4549  O OH  . TYR C 3 179 ? -44.931 -57.859 0.984   1.000 150.105 ? 179 TYR CCC OH  1 
ATOM   4550  N N   . SER C 3 180 ? -36.940 -59.921 -1.710  1.000 134.198 ? 180 SER CCC N   1 
ATOM   4551  C CA  . SER C 3 180 ? -35.905 -60.810 -2.303  1.000 132.689 ? 180 SER CCC CA  1 
ATOM   4552  C C   . SER C 3 180 ? -35.848 -62.090 -1.457  1.000 132.889 ? 180 SER CCC C   1 
ATOM   4553  O O   . SER C 3 180 ? -36.414 -62.065 -0.346  1.000 134.282 ? 180 SER CCC O   1 
ATOM   4554  C CB  . SER C 3 180 ? -34.566 -60.118 -2.389  1.000 132.267 ? 180 SER CCC CB  1 
ATOM   4555  O OG  . SER C 3 180 ? -34.691 -58.851 -3.021  1.000 131.818 ? 180 SER CCC OG  1 
ATOM   4556  N N   . LEU C 3 181 ? -35.211 -63.162 -1.941  1.000 133.130 ? 181 LEU CCC N   1 
ATOM   4557  C CA  . LEU C 3 181 ? -35.281 -64.507 -1.298  1.000 133.421 ? 181 LEU CCC CA  1 
ATOM   4558  C C   . LEU C 3 181 ? -33.957 -65.269 -1.461  1.000 132.902 ? 181 LEU CCC C   1 
ATOM   4559  O O   . LEU C 3 181 ? -33.387 -65.229 -2.562  1.000 132.249 ? 181 LEU CCC O   1 
ATOM   4560  C CB  . LEU C 3 181 ? -36.448 -65.265 -1.939  1.000 133.657 ? 181 LEU CCC CB  1 
ATOM   4561  C CG  . LEU C 3 181 ? -36.971 -66.476 -1.171  1.000 135.261 ? 181 LEU CCC CG  1 
ATOM   4562  C CD1 . LEU C 3 181 ? -38.398 -66.796 -1.593  1.000 135.587 ? 181 LEU CCC CD1 1 
ATOM   4563  C CD2 . LEU C 3 181 ? -36.072 -67.686 -1.368  1.000 135.457 ? 181 LEU CCC CD2 1 
ATOM   4564  N N   . SER C 3 182 ? -33.496 -65.943 -0.400  1.000 133.891 ? 182 SER CCC N   1 
ATOM   4565  C CA  . SER C 3 182 ? -32.363 -66.906 -0.427  1.000 135.966 ? 182 SER CCC CA  1 
ATOM   4566  C C   . SER C 3 182 ? -32.862 -68.276 0.035   1.000 137.823 ? 182 SER CCC C   1 
ATOM   4567  O O   . SER C 3 182 ? -33.066 -68.448 1.259   1.000 140.507 ? 182 SER CCC O   1 
ATOM   4568  C CB  . SER C 3 182 ? -31.201 -66.445 0.428   1.000 138.008 ? 182 SER CCC CB  1 
ATOM   4569  O OG  . SER C 3 182 ? -31.012 -67.293 1.562   1.000 138.730 ? 182 SER CCC OG  1 
ATOM   4570  N N   . SER C 3 183 ? -33.068 -69.203 -0.905  1.000 139.149 ? 183 SER CCC N   1 
ATOM   4571  C CA  . SER C 3 183 ? -33.259 -70.646 -0.609  1.000 140.907 ? 183 SER CCC CA  1 
ATOM   4572  C C   . SER C 3 183 ? -31.892 -71.330 -0.607  1.000 140.271 ? 183 SER CCC C   1 
ATOM   4573  O O   . SER C 3 183 ? -31.212 -71.327 -1.650  1.000 137.617 ? 183 SER CCC O   1 
ATOM   4574  C CB  . SER C 3 183 ? -34.195 -71.334 -1.559  1.000 141.984 ? 183 SER CCC CB  1 
ATOM   4575  O OG  . SER C 3 183 ? -34.534 -72.621 -1.051  1.000 144.693 ? 183 SER CCC OG  1 
ATOM   4576  N N   . THR C 3 184 ? -31.500 -71.860 0.547   1.000 141.797 ? 184 THR CCC N   1 
ATOM   4577  C CA  . THR C 3 184 ? -30.226 -72.585 0.736   1.000 143.030 ? 184 THR CCC CA  1 
ATOM   4578  C C   . THR C 3 184 ? -30.570 -74.074 0.821   1.000 142.634 ? 184 THR CCC C   1 
ATOM   4579  O O   . THR C 3 184 ? -31.509 -74.423 1.566   1.000 140.991 ? 184 THR CCC O   1 
ATOM   4580  C CB  . THR C 3 184 ? -29.455 -72.036 1.946   1.000 147.006 ? 184 THR CCC CB  1 
ATOM   4581  O OG1 . THR C 3 184 ? -29.471 -70.603 1.939   1.000 147.332 ? 184 THR CCC OG1 1 
ATOM   4582  C CG2 . THR C 3 184 ? -28.017 -72.509 1.971   1.000 148.518 ? 184 THR CCC CG2 1 
ATOM   4583  N N   . LEU C 3 185 ? -29.877 -74.887 0.021   1.000 143.099 ? 185 LEU CCC N   1 
ATOM   4584  C CA  . LEU C 3 185 ? -29.937 -76.371 0.020   1.000 142.593 ? 185 LEU CCC CA  1 
ATOM   4585  C C   . LEU C 3 185 ? -28.653 -76.896 0.667   1.000 145.954 ? 185 LEU CCC C   1 
ATOM   4586  O O   . LEU C 3 185 ? -27.574 -76.671 0.091   1.000 146.448 ? 185 LEU CCC O   1 
ATOM   4587  C CB  . LEU C 3 185 ? -30.059 -76.856 -1.425  1.000 139.625 ? 185 LEU CCC CB  1 
ATOM   4588  C CG  . LEU C 3 185 ? -30.163 -78.366 -1.614  1.000 139.880 ? 185 LEU CCC CG  1 
ATOM   4589  C CD1 . LEU C 3 185 ? -31.566 -78.844 -1.285  1.000 140.663 ? 185 LEU CCC CD1 1 
ATOM   4590  C CD2 . LEU C 3 185 ? -29.771 -78.762 -3.027  1.000 138.757 ? 185 LEU CCC CD2 1 
ATOM   4591  N N   . THR C 3 186 ? -28.768 -77.555 1.822   1.000 148.288 ? 186 THR CCC N   1 
ATOM   4592  C CA  . THR C 3 186 ? -27.622 -78.142 2.561   1.000 150.670 ? 186 THR CCC CA  1 
ATOM   4593  C C   . THR C 3 186 ? -27.649 -79.664 2.389   1.000 150.252 ? 186 THR CCC C   1 
ATOM   4594  O O   . THR C 3 186 ? -28.748 -80.237 2.359   1.000 147.231 ? 186 THR CCC O   1 
ATOM   4595  C CB  . THR C 3 186 ? -27.620 -77.712 4.034   1.000 154.088 ? 186 THR CCC CB  1 
ATOM   4596  O OG1 . THR C 3 186 ? -27.585 -76.284 4.100   1.000 153.357 ? 186 THR CCC OG1 1 
ATOM   4597  C CG2 . THR C 3 186 ? -26.447 -78.275 4.807   1.000 157.507 ? 186 THR CCC CG2 1 
ATOM   4598  N N   . LEU C 3 187 ? -26.467 -80.271 2.258   1.000 152.445 ? 187 LEU CCC N   1 
ATOM   4599  C CA  . LEU C 3 187 ? -26.256 -81.744 2.255   1.000 155.691 ? 187 LEU CCC CA  1 
ATOM   4600  C C   . LEU C 3 187 ? -24.775 -82.058 2.497   1.000 159.549 ? 187 LEU CCC C   1 
ATOM   4601  O O   . LEU C 3 187 ? -23.929 -81.144 2.359   1.000 161.694 ? 187 LEU CCC O   1 
ATOM   4602  C CB  . LEU C 3 187 ? -26.728 -82.334 0.924   1.000 153.468 ? 187 LEU CCC CB  1 
ATOM   4603  C CG  . LEU C 3 187 ? -25.920 -81.931 -0.309  1.000 152.935 ? 187 LEU CCC CG  1 
ATOM   4604  C CD1 . LEU C 3 187 ? -25.963 -83.030 -1.356  1.000 154.449 ? 187 LEU CCC CD1 1 
ATOM   4605  C CD2 . LEU C 3 187 ? -26.424 -80.621 -0.892  1.000 150.585 ? 187 LEU CCC CD2 1 
ATOM   4606  N N   . SER C 3 188 ? -24.484 -83.316 2.841   1.000 161.134 ? 188 SER CCC N   1 
ATOM   4607  C CA  . SER C 3 188 ? -23.117 -83.833 3.095   1.000 163.153 ? 188 SER CCC CA  1 
ATOM   4608  C C   . SER C 3 188 ? -22.313 -83.760 1.797   1.000 162.687 ? 188 SER CCC C   1 
ATOM   4609  O O   . SER C 3 188 ? -22.915 -83.998 0.732   1.000 161.557 ? 188 SER CCC O   1 
ATOM   4610  C CB  . SER C 3 188 ? -23.165 -85.238 3.620   1.000 165.345 ? 188 SER CCC CB  1 
ATOM   4611  O OG  . SER C 3 188 ? -23.760 -86.101 2.667   1.000 162.729 ? 188 SER CCC OG  1 
ATOM   4612  N N   . LYS C 3 189 ? -21.020 -83.428 1.893   1.000 165.200 ? 189 LYS CCC N   1 
ATOM   4613  C CA  . LYS C 3 189 ? -20.047 -83.502 0.766   1.000 165.205 ? 189 LYS CCC CA  1 
ATOM   4614  C C   . LYS C 3 189 ? -20.212 -84.861 0.081   1.000 164.453 ? 189 LYS CCC C   1 
ATOM   4615  O O   . LYS C 3 189 ? -20.285 -84.893 -1.166  1.000 164.038 ? 189 LYS CCC O   1 
ATOM   4616  C CB  . LYS C 3 189 ? -18.612 -83.299 1.265   1.000 169.016 ? 189 LYS CCC CB  1 
ATOM   4617  C CG  . LYS C 3 189 ? -17.521 -83.420 0.206   1.000 170.507 ? 189 LYS CCC CG  1 
ATOM   4618  C CD  . LYS C 3 189 ? -16.912 -84.805 0.091   1.000 173.518 ? 189 LYS CCC CD  1 
ATOM   4619  C CE  . LYS C 3 189 ? -15.694 -84.844 -0.810  1.000 176.211 ? 189 LYS CCC CE  1 
ATOM   4620  N NZ  . LYS C 3 189 ? -14.462 -84.435 -0.096  1.000 180.029 ? 189 LYS CCC NZ  1 
ATOM   4621  N N   . ALA C 3 190 ? -20.282 -85.928 0.880   1.000 165.175 ? 190 ALA CCC N   1 
ATOM   4622  C CA  . ALA C 3 190 ? -20.569 -87.313 0.440   1.000 166.779 ? 190 ALA CCC CA  1 
ATOM   4623  C C   . ALA C 3 190 ? -21.700 -87.311 -0.596  1.000 163.446 ? 190 ALA CCC C   1 
ATOM   4624  O O   . ALA C 3 190 ? -21.437 -87.662 -1.769  1.000 164.863 ? 190 ALA CCC O   1 
ATOM   4625  C CB  . ALA C 3 190 ? -20.928 -88.158 1.636   1.000 169.876 ? 190 ALA CCC CB  1 
ATOM   4626  N N   . ASP C 3 191 ? -22.901 -86.903 -0.176  1.000 159.704 ? 191 ASP CCC N   1 
ATOM   4627  C CA  . ASP C 3 191 ? -24.147 -86.985 -0.982  1.000 157.011 ? 191 ASP CCC CA  1 
ATOM   4628  C C   . ASP C 3 191 ? -24.082 -85.980 -2.140  1.000 154.636 ? 191 ASP CCC C   1 
ATOM   4629  O O   . ASP C 3 191 ? -24.749 -86.231 -3.167  1.000 152.562 ? 191 ASP CCC O   1 
ATOM   4630  C CB  . ASP C 3 191 ? -25.387 -86.794 -0.100  1.000 155.395 ? 191 ASP CCC CB  1 
ATOM   4631  C CG  . ASP C 3 191 ? -25.630 -87.913 0.904   1.000 158.036 ? 191 ASP CCC CG  1 
ATOM   4632  O OD1 . ASP C 3 191 ? -25.363 -89.092 0.576   1.000 158.464 ? 191 ASP CCC OD1 1 
ATOM   4633  O OD2 . ASP C 3 191 ? -26.086 -87.590 2.017   1.000 159.026 ? 191 ASP CCC OD2 1 
ATOM   4634  N N   . TYR C 3 192 ? -23.307 -84.897 -1.999  1.000 155.618 ? 192 TYR CCC N   1 
ATOM   4635  C CA  . TYR C 3 192 ? -23.151 -83.850 -3.044  1.000 156.029 ? 192 TYR CCC CA  1 
ATOM   4636  C C   . TYR C 3 192 ? -22.361 -84.412 -4.226  1.000 160.742 ? 192 TYR CCC C   1 
ATOM   4637  O O   . TYR C 3 192 ? -22.680 -84.076 -5.378  1.000 161.769 ? 192 TYR CCC O   1 
ATOM   4638  C CB  . TYR C 3 192 ? -22.464 -82.590 -2.511  1.000 154.393 ? 192 TYR CCC CB  1 
ATOM   4639  C CG  . TYR C 3 192 ? -22.184 -81.559 -3.575  1.000 152.436 ? 192 TYR CCC CG  1 
ATOM   4640  C CD1 . TYR C 3 192 ? -23.196 -80.757 -4.077  1.000 149.446 ? 192 TYR CCC CD1 1 
ATOM   4641  C CD2 . TYR C 3 192 ? -20.916 -81.403 -4.109  1.000 154.185 ? 192 TYR CCC CD2 1 
ATOM   4642  C CE1 . TYR C 3 192 ? -22.953 -79.813 -5.064  1.000 148.863 ? 192 TYR CCC CE1 1 
ATOM   4643  C CE2 . TYR C 3 192 ? -20.653 -80.457 -5.089  1.000 153.337 ? 192 TYR CCC CE2 1 
ATOM   4644  C CZ  . TYR C 3 192 ? -21.674 -79.660 -5.573  1.000 150.135 ? 192 TYR CCC CZ  1 
ATOM   4645  O OH  . TYR C 3 192 ? -21.413 -78.740 -6.545  1.000 148.118 ? 192 TYR CCC OH  1 
ATOM   4646  N N   . GLU C 3 193 ? -21.356 -85.241 -3.945  1.000 166.787 ? 193 GLU CCC N   1 
ATOM   4647  C CA  . GLU C 3 193 ? -20.480 -85.842 -4.981  1.000 172.043 ? 193 GLU CCC CA  1 
ATOM   4648  C C   . GLU C 3 193 ? -21.215 -86.990 -5.687  1.000 174.667 ? 193 GLU CCC C   1 
ATOM   4649  O O   . GLU C 3 193 ? -20.713 -87.432 -6.740  1.000 180.993 ? 193 GLU CCC O   1 
ATOM   4650  C CB  . GLU C 3 193 ? -19.159 -86.296 -4.357  1.000 177.110 ? 193 GLU CCC CB  1 
ATOM   4651  C CG  . GLU C 3 193 ? -18.233 -85.139 -4.019  1.000 180.409 ? 193 GLU CCC CG  1 
ATOM   4652  C CD  . GLU C 3 193 ? -16.755 -85.492 -3.943  1.000 188.106 ? 193 GLU CCC CD  1 
ATOM   4653  O OE1 . GLU C 3 193 ? -16.431 -86.661 -3.621  1.000 193.433 ? 193 GLU CCC OE1 1 
ATOM   4654  O OE2 . GLU C 3 193 ? -15.926 -84.593 -4.203  1.000 192.577 ? 193 GLU CCC OE2 1 
ATOM   4655  N N   . LYS C 3 194 ? -22.360 -87.443 -5.158  1.000 172.972 ? 194 LYS CCC N   1 
ATOM   4656  C CA  . LYS C 3 194 ? -23.158 -88.564 -5.738  1.000 172.119 ? 194 LYS CCC CA  1 
ATOM   4657  C C   . LYS C 3 194 ? -23.929 -88.076 -6.976  1.000 167.550 ? 194 LYS CCC C   1 
ATOM   4658  O O   . LYS C 3 194 ? -23.846 -88.748 -8.017  1.000 169.330 ? 194 LYS CCC O   1 
ATOM   4659  C CB  . LYS C 3 194 ? -24.075 -89.185 -4.673  1.000 173.691 ? 194 LYS CCC CB  1 
ATOM   4660  C CG  . LYS C 3 194 ? -23.436 -90.317 -3.873  1.000 177.715 ? 194 LYS CCC CG  1 
ATOM   4661  C CD  . LYS C 3 194 ? -24.076 -90.597 -2.515  1.000 179.560 ? 194 LYS CCC CD  1 
ATOM   4662  C CE  . LYS C 3 194 ? -25.546 -90.952 -2.593  1.000 180.258 ? 194 LYS CCC CE  1 
ATOM   4663  N NZ  . LYS C 3 194 ? -26.101 -91.285 -1.257  1.000 182.117 ? 194 LYS CCC NZ  1 
ATOM   4664  N N   . HIS C 3 195 ? -24.635 -86.948 -6.872  1.000 161.595 ? 195 HIS CCC N   1 
ATOM   4665  C CA  . HIS C 3 195 ? -25.468 -86.357 -7.957  1.000 158.574 ? 195 HIS CCC CA  1 
ATOM   4666  C C   . HIS C 3 195 ? -24.619 -85.346 -8.746  1.000 155.829 ? 195 HIS CCC C   1 
ATOM   4667  O O   . HIS C 3 195 ? -23.603 -84.904 -8.186  1.000 151.992 ? 195 HIS CCC O   1 
ATOM   4668  C CB  . HIS C 3 195 ? -26.739 -85.757 -7.337  1.000 157.378 ? 195 HIS CCC CB  1 
ATOM   4669  C CG  . HIS C 3 195 ? -27.415 -86.641 -6.335  1.000 158.522 ? 195 HIS CCC CG  1 
ATOM   4670  N ND1 . HIS C 3 195 ? -27.763 -87.952 -6.611  1.000 161.037 ? 195 HIS CCC ND1 1 
ATOM   4671  C CD2 . HIS C 3 195 ? -27.825 -86.403 -5.068  1.000 157.537 ? 195 HIS CCC CD2 1 
ATOM   4672  C CE1 . HIS C 3 195 ? -28.354 -88.481 -5.556  1.000 161.696 ? 195 HIS CCC CE1 1 
ATOM   4673  N NE2 . HIS C 3 195 ? -28.402 -87.551 -4.596  1.000 160.120 ? 195 HIS CCC NE2 1 
ATOM   4674  N N   . LYS C 3 196 ? -24.996 -85.001 -9.990  1.000 156.935 ? 196 LYS CCC N   1 
ATOM   4675  C CA  . LYS C 3 196 ? -24.189 -84.096 -10.870 1.000 157.672 ? 196 LYS CCC CA  1 
ATOM   4676  C C   . LYS C 3 196 ? -24.952 -82.822 -11.267 1.000 154.643 ? 196 LYS CCC C   1 
ATOM   4677  O O   . LYS C 3 196 ? -24.288 -81.773 -11.336 1.000 154.826 ? 196 LYS CCC O   1 
ATOM   4678  C CB  . LYS C 3 196 ? -23.642 -84.819 -12.111 1.000 161.333 ? 196 LYS CCC CB  1 
ATOM   4679  C CG  . LYS C 3 196 ? -22.121 -85.006 -12.097 1.000 164.092 ? 196 LYS CCC CG  1 
ATOM   4680  C CD  . LYS C 3 196 ? -21.591 -86.288 -12.718 1.000 166.813 ? 196 LYS CCC CD  1 
ATOM   4681  C CE  . LYS C 3 196 ? -20.192 -86.634 -12.244 1.000 168.174 ? 196 LYS CCC CE  1 
ATOM   4682  N NZ  . LYS C 3 196 ? -19.806 -88.011 -12.630 1.000 172.268 ? 196 LYS CCC NZ  1 
ATOM   4683  N N   . VAL C 3 197 ? -26.261 -82.879 -11.530 1.000 152.310 ? 197 VAL CCC N   1 
ATOM   4684  C CA  . VAL C 3 197 ? -27.053 -81.700 -12.008 1.000 150.043 ? 197 VAL CCC CA  1 
ATOM   4685  C C   . VAL C 3 197 ? -27.882 -81.086 -10.868 1.000 148.014 ? 197 VAL CCC C   1 
ATOM   4686  O O   . VAL C 3 197 ? -28.912 -81.685 -10.502 1.000 149.065 ? 197 VAL CCC O   1 
ATOM   4687  C CB  . VAL C 3 197 ? -27.967 -82.097 -13.175 1.000 150.392 ? 197 VAL CCC CB  1 
ATOM   4688  C CG1 . VAL C 3 197 ? -28.849 -80.935 -13.609 1.000 148.739 ? 197 VAL CCC CG1 1 
ATOM   4689  C CG2 . VAL C 3 197 ? -27.155 -82.647 -14.336 1.000 154.031 ? 197 VAL CCC CG2 1 
ATOM   4690  N N   . TYR C 3 198 ? -27.488 -79.901 -10.388 1.000 146.205 ? 198 TYR CCC N   1 
ATOM   4691  C CA  . TYR C 3 198 ? -28.170 -79.131 -9.311  1.000 142.679 ? 198 TYR CCC CA  1 
ATOM   4692  C C   . TYR C 3 198 ? -28.908 -77.942 -9.922  1.000 140.586 ? 198 TYR CCC C   1 
ATOM   4693  O O   . TYR C 3 198 ? -28.256 -77.147 -10.615 1.000 141.130 ? 198 TYR CCC O   1 
ATOM   4694  C CB  . TYR C 3 198 ? -27.158 -78.643 -8.272  1.000 142.236 ? 198 TYR CCC CB  1 
ATOM   4695  C CG  . TYR C 3 198 ? -26.577 -79.764 -7.464  1.000 143.718 ? 198 TYR CCC CG  1 
ATOM   4696  C CD1 . TYR C 3 198 ? -25.452 -80.448 -7.892  1.000 147.002 ? 198 TYR CCC CD1 1 
ATOM   4697  C CD2 . TYR C 3 198 ? -27.200 -80.182 -6.302  1.000 143.745 ? 198 TYR CCC CD2 1 
ATOM   4698  C CE1 . TYR C 3 198 ? -24.941 -81.510 -7.166  1.000 149.684 ? 198 TYR CCC CE1 1 
ATOM   4699  C CE2 . TYR C 3 198 ? -26.704 -81.241 -5.564  1.000 146.625 ? 198 TYR CCC CE2 1 
ATOM   4700  C CZ  . TYR C 3 198 ? -25.575 -81.909 -6.001  1.000 149.632 ? 198 TYR CCC CZ  1 
ATOM   4701  O OH  . TYR C 3 198 ? -25.082 -82.958 -5.285  1.000 153.346 ? 198 TYR CCC OH  1 
ATOM   4702  N N   . ALA C 3 199 ? -30.209 -77.819 -9.647  1.000 138.397 ? 199 ALA CCC N   1 
ATOM   4703  C CA  . ALA C 3 199 ? -31.106 -76.866 -10.333 1.000 138.808 ? 199 ALA CCC CA  1 
ATOM   4704  C C   . ALA C 3 199 ? -32.090 -76.223 -9.350  1.000 137.046 ? 199 ALA CCC C   1 
ATOM   4705  O O   . ALA C 3 199 ? -32.307 -76.765 -8.252  1.000 133.281 ? 199 ALA CCC O   1 
ATOM   4706  C CB  . ALA C 3 199 ? -31.824 -77.583 -11.446 1.000 141.946 ? 199 ALA CCC CB  1 
ATOM   4707  N N   . CYS C 3 200 ? -32.680 -75.106 -9.775  1.000 140.126 ? 200 CYS CCC N   1 
ATOM   4708  C CA  . CYS C 3 200 ? -33.539 -74.212 -8.959  1.000 140.693 ? 200 CYS CCC CA  1 
ATOM   4709  C C   . CYS C 3 200 ? -34.722 -73.722 -9.809  1.000 139.313 ? 200 CYS CCC C   1 
ATOM   4710  O O   . CYS C 3 200 ? -34.552 -72.729 -10.546 1.000 136.697 ? 200 CYS CCC O   1 
ATOM   4711  C CB  . CYS C 3 200 ? -32.704 -73.052 -8.429  1.000 143.645 ? 200 CYS CCC CB  1 
ATOM   4712  S SG  . CYS C 3 200 ? -33.555 -72.091 -7.153  1.000 149.112 ? 200 CYS CCC SG  1 
ATOM   4713  N N   . GLU C 3 201 ? -35.867 -74.408 -9.707  1.000 140.064 ? 201 GLU CCC N   1 
ATOM   4714  C CA  . GLU C 3 201 ? -37.122 -74.134 -10.467 1.000 142.616 ? 201 GLU CCC CA  1 
ATOM   4715  C C   . GLU C 3 201 ? -37.955 -73.108 -9.684  1.000 141.410 ? 201 GLU CCC C   1 
ATOM   4716  O O   . GLU C 3 201 ? -38.248 -73.377 -8.498  1.000 143.919 ? 201 GLU CCC O   1 
ATOM   4717  C CB  . GLU C 3 201 ? -37.895 -75.444 -10.689 1.000 145.796 ? 201 GLU CCC CB  1 
ATOM   4718  C CG  . GLU C 3 201 ? -38.950 -75.392 -11.791 1.000 148.583 ? 201 GLU CCC CG  1 
ATOM   4719  C CD  . GLU C 3 201 ? -39.857 -76.615 -11.894 1.000 151.773 ? 201 GLU CCC CD  1 
ATOM   4720  O OE1 . GLU C 3 201 ? -40.362 -77.072 -10.848 1.000 152.197 ? 201 GLU CCC OE1 1 
ATOM   4721  O OE2 . GLU C 3 201 ? -40.053 -77.123 -13.019 1.000 153.693 ? 201 GLU CCC OE2 1 
ATOM   4722  N N   . VAL C 3 202 ? -38.334 -71.992 -10.321 1.000 139.991 ? 202 VAL CCC N   1 
ATOM   4723  C CA  . VAL C 3 202 ? -39.004 -70.820 -9.674  1.000 137.639 ? 202 VAL CCC CA  1 
ATOM   4724  C C   . VAL C 3 202 ? -40.317 -70.493 -10.397 1.000 140.788 ? 202 VAL CCC C   1 
ATOM   4725  O O   . VAL C 3 202 ? -40.255 -70.003 -11.542 1.000 143.655 ? 202 VAL CCC O   1 
ATOM   4726  C CB  . VAL C 3 202 ? -38.081 -69.590 -9.669  1.000 134.854 ? 202 VAL CCC CB  1 
ATOM   4727  C CG1 . VAL C 3 202 ? -38.768 -68.383 -9.055  1.000 134.750 ? 202 VAL CCC CG1 1 
ATOM   4728  C CG2 . VAL C 3 202 ? -36.760 -69.875 -8.974  1.000 132.568 ? 202 VAL CCC CG2 1 
ATOM   4729  N N   . THR C 3 203 ? -41.455 -70.722 -9.734  1.000 142.325 ? 203 THR CCC N   1 
ATOM   4730  C CA  . THR C 3 203 ? -42.818 -70.366 -10.215 1.000 146.717 ? 203 THR CCC CA  1 
ATOM   4731  C C   . THR C 3 203 ? -43.302 -69.125 -9.460  1.000 148.162 ? 203 THR CCC C   1 
ATOM   4732  O O   . THR C 3 203 ? -43.845 -69.284 -8.351  1.000 149.829 ? 203 THR CCC O   1 
ATOM   4733  C CB  . THR C 3 203 ? -43.802 -71.534 -10.048 1.000 149.073 ? 203 THR CCC CB  1 
ATOM   4734  O OG1 . THR C 3 203 ? -43.477 -72.530 -11.018 1.000 150.172 ? 203 THR CCC OG1 1 
ATOM   4735  C CG2 . THR C 3 203 ? -45.254 -71.134 -10.209 1.000 151.893 ? 203 THR CCC CG2 1 
ATOM   4736  N N   . HIS C 3 204 ? -43.117 -67.938 -10.040 1.000 150.248 ? 204 HIS CCC N   1 
ATOM   4737  C CA  . HIS C 3 204 ? -43.633 -66.656 -9.492  1.000 151.751 ? 204 HIS CCC CA  1 
ATOM   4738  C C   . HIS C 3 204 ? -44.743 -66.105 -10.387 1.000 155.286 ? 204 HIS CCC C   1 
ATOM   4739  O O   . HIS C 3 204 ? -44.652 -66.280 -11.618 1.000 156.181 ? 204 HIS CCC O   1 
ATOM   4740  C CB  . HIS C 3 204 ? -42.516 -65.626 -9.329  1.000 150.796 ? 204 HIS CCC CB  1 
ATOM   4741  C CG  . HIS C 3 204 ? -42.995 -64.392 -8.647  1.000 151.252 ? 204 HIS CCC CG  1 
ATOM   4742  N ND1 . HIS C 3 204 ? -42.837 -63.134 -9.189  1.000 151.961 ? 204 HIS CCC ND1 1 
ATOM   4743  C CD2 . HIS C 3 204 ? -43.675 -64.232 -7.494  1.000 151.790 ? 204 HIS CCC CD2 1 
ATOM   4744  C CE1 . HIS C 3 204 ? -43.374 -62.246 -8.380  1.000 153.114 ? 204 HIS CCC CE1 1 
ATOM   4745  N NE2 . HIS C 3 204 ? -43.893 -62.895 -7.332  1.000 153.552 ? 204 HIS CCC NE2 1 
ATOM   4746  N N   . GLN C 3 205 ? -45.722 -65.435 -9.771  1.000 157.719 ? 205 GLN CCC N   1 
ATOM   4747  C CA  . GLN C 3 205 ? -46.891 -64.817 -10.448 1.000 163.226 ? 205 GLN CCC CA  1 
ATOM   4748  C C   . GLN C 3 205 ? -46.427 -63.941 -11.619 1.000 165.329 ? 205 GLN CCC C   1 
ATOM   4749  O O   . GLN C 3 205 ? -47.157 -63.884 -12.627 1.000 169.298 ? 205 GLN CCC O   1 
ATOM   4750  C CB  . GLN C 3 205 ? -47.698 -63.967 -9.467  1.000 163.765 ? 205 GLN CCC CB  1 
ATOM   4751  C CG  . GLN C 3 205 ? -49.014 -63.479 -10.060 1.000 168.576 ? 205 GLN CCC CG  1 
ATOM   4752  C CD  . GLN C 3 205 ? -49.200 -61.996 -9.861  1.000 169.599 ? 205 GLN CCC CD  1 
ATOM   4753  O OE1 . GLN C 3 205 ? -48.866 -61.470 -8.805  1.000 168.249 ? 205 GLN CCC OE1 1 
ATOM   4754  N NE2 . GLN C 3 205 ? -49.715 -61.316 -10.876 1.000 173.010 ? 205 GLN CCC NE2 1 
ATOM   4755  N N   . GLY C 3 206 ? -45.281 -63.268 -11.472 1.000 164.377 ? 206 GLY CCC N   1 
ATOM   4756  C CA  . GLY C 3 206 ? -44.655 -62.439 -12.522 1.000 166.097 ? 206 GLY CCC CA  1 
ATOM   4757  C C   . GLY C 3 206 ? -44.332 -63.237 -13.777 1.000 168.133 ? 206 GLY CCC C   1 
ATOM   4758  O O   . GLY C 3 206 ? -44.594 -62.734 -14.887 1.000 172.842 ? 206 GLY CCC O   1 
ATOM   4759  N N   . LEU C 3 207 ? -43.794 -64.447 -13.617 1.000 166.865 ? 207 LEU CCC N   1 
ATOM   4760  C CA  . LEU C 3 207 ? -43.265 -65.269 -14.738 1.000 169.076 ? 207 LEU CCC CA  1 
ATOM   4761  C C   . LEU C 3 207 ? -44.349 -66.202 -15.276 1.000 171.893 ? 207 LEU CCC C   1 
ATOM   4762  O O   . LEU C 3 207 ? -44.775 -67.109 -14.527 1.000 170.058 ? 207 LEU CCC O   1 
ATOM   4763  C CB  . LEU C 3 207 ? -42.057 -66.057 -14.236 1.000 168.066 ? 207 LEU CCC CB  1 
ATOM   4764  C CG  . LEU C 3 207 ? -40.806 -65.209 -14.035 1.000 168.166 ? 207 LEU CCC CG  1 
ATOM   4765  C CD1 . LEU C 3 207 ? -39.833 -65.902 -13.097 1.000 165.480 ? 207 LEU CCC CD1 1 
ATOM   4766  C CD2 . LEU C 3 207 ? -40.159 -64.876 -15.377 1.000 171.425 ? 207 LEU CCC CD2 1 
ATOM   4767  N N   . SER C 3 208 ? -44.761 -65.979 -16.529 1.000 175.431 ? 208 SER CCC N   1 
ATOM   4768  C CA  . SER C 3 208 ? -45.707 -66.837 -17.292 1.000 178.243 ? 208 SER CCC CA  1 
ATOM   4769  C C   . SER C 3 208 ? -45.319 -68.311 -17.110 1.000 175.704 ? 208 SER CCC C   1 
ATOM   4770  O O   . SER C 3 208 ? -45.999 -69.012 -16.328 1.000 173.453 ? 208 SER CCC O   1 
ATOM   4771  C CB  . SER C 3 208 ? -45.737 -66.436 -18.745 1.000 181.964 ? 208 SER CCC CB  1 
ATOM   4772  O OG  . SER C 3 208 ? -44.422 -66.194 -19.220 1.000 180.705 ? 208 SER CCC OG  1 
ATOM   4773  N N   . SER C 3 209 ? -44.239 -68.744 -17.771 1.000 173.741 ? 209 SER CCC N   1 
ATOM   4774  C CA  . SER C 3 209 ? -43.668 -70.113 -17.674 1.000 171.173 ? 209 SER CCC CA  1 
ATOM   4775  C C   . SER C 3 209 ? -42.596 -70.142 -16.586 1.000 164.026 ? 209 SER CCC C   1 
ATOM   4776  O O   . SER C 3 209 ? -41.757 -69.243 -16.531 1.000 161.829 ? 209 SER CCC O   1 
ATOM   4777  C CB  . SER C 3 209 ? -43.116 -70.558 -19.004 1.000 175.235 ? 209 SER CCC CB  1 
ATOM   4778  O OG  . SER C 3 209 ? -42.980 -71.971 -19.051 1.000 176.616 ? 209 SER CCC OG  1 
ATOM   4779  N N   . PRO C 3 210 ? -42.600 -71.155 -15.686 1.000 160.082 ? 210 PRO CCC N   1 
ATOM   4780  C CA  . PRO C 3 210 ? -41.590 -71.276 -14.631 1.000 154.435 ? 210 PRO CCC CA  1 
ATOM   4781  C C   . PRO C 3 210 ? -40.152 -71.109 -15.137 1.000 152.524 ? 210 PRO CCC C   1 
ATOM   4782  O O   . PRO C 3 210 ? -39.881 -71.483 -16.264 1.000 155.983 ? 210 PRO CCC O   1 
ATOM   4783  C CB  . PRO C 3 210 ? -41.776 -72.701 -14.092 1.000 154.217 ? 210 PRO CCC CB  1 
ATOM   4784  C CG  . PRO C 3 210 ? -43.233 -73.012 -14.367 1.000 159.164 ? 210 PRO CCC CG  1 
ATOM   4785  C CD  . PRO C 3 210 ? -43.597 -72.234 -15.618 1.000 162.526 ? 210 PRO CCC CD  1 
ATOM   4786  N N   . VAL C 3 211 ? -39.278 -70.560 -14.288 1.000 149.102 ? 211 VAL CCC N   1 
ATOM   4787  C CA  . VAL C 3 211 ? -37.850 -70.254 -14.604 1.000 148.957 ? 211 VAL CCC CA  1 
ATOM   4788  C C   . VAL C 3 211 ? -36.943 -71.207 -13.826 1.000 149.588 ? 211 VAL CCC C   1 
ATOM   4789  O O   . VAL C 3 211 ? -37.003 -71.178 -12.583 1.000 151.163 ? 211 VAL CCC O   1 
ATOM   4790  C CB  . VAL C 3 211 ? -37.497 -68.795 -14.269 1.000 145.418 ? 211 VAL CCC CB  1 
ATOM   4791  C CG1 . VAL C 3 211 ? -35.994 -68.581 -14.173 1.000 142.349 ? 211 VAL CCC CG1 1 
ATOM   4792  C CG2 . VAL C 3 211 ? -38.113 -67.839 -15.276 1.000 149.465 ? 211 VAL CCC CG2 1 
ATOM   4793  N N   . THR C 3 212 ? -36.116 -71.986 -14.533 1.000 151.866 ? 212 THR CCC N   1 
ATOM   4794  C CA  . THR C 3 212 ? -35.087 -72.879 -13.942 1.000 149.584 ? 212 THR CCC CA  1 
ATOM   4795  C C   . THR C 3 212 ? -33.702 -72.319 -14.267 1.000 149.096 ? 212 THR CCC C   1 
ATOM   4796  O O   . THR C 3 212 ? -33.427 -72.046 -15.454 1.000 150.879 ? 212 THR CCC O   1 
ATOM   4797  C CB  . THR C 3 212 ? -35.225 -74.325 -14.433 1.000 151.532 ? 212 THR CCC CB  1 
ATOM   4798  O OG1 . THR C 3 212 ? -36.590 -74.735 -14.345 1.000 153.277 ? 212 THR CCC OG1 1 
ATOM   4799  C CG2 . THR C 3 212 ? -34.365 -75.280 -13.637 1.000 149.272 ? 212 THR CCC CG2 1 
ATOM   4800  N N   . LYS C 3 213 ? -32.877 -72.148 -13.235 1.000 147.839 ? 213 LYS CCC N   1 
ATOM   4801  C CA  . LYS C 3 213 ? -31.430 -71.843 -13.355 1.000 150.932 ? 213 LYS CCC CA  1 
ATOM   4802  C C   . LYS C 3 213 ? -30.676 -72.961 -12.644 1.000 148.826 ? 213 LYS CCC C   1 
ATOM   4803  O O   . LYS C 3 213 ? -31.119 -73.341 -11.550 1.000 148.768 ? 213 LYS CCC O   1 
ATOM   4804  C CB  . LYS C 3 213 ? -31.126 -70.471 -12.753 1.000 154.525 ? 213 LYS CCC CB  1 
ATOM   4805  C CG  . LYS C 3 213 ? -31.601 -69.292 -13.593 1.000 160.528 ? 213 LYS CCC CG  1 
ATOM   4806  C CD  . LYS C 3 213 ? -30.508 -68.621 -14.421 1.000 165.600 ? 213 LYS CCC CD  1 
ATOM   4807  C CE  . LYS C 3 213 ? -29.569 -67.758 -13.598 1.000 166.863 ? 213 LYS CCC CE  1 
ATOM   4808  N NZ  . LYS C 3 213 ? -29.024 -66.622 -14.382 1.000 171.251 ? 213 LYS CCC NZ  1 
ATOM   4809  N N   . SER C 3 214 ? -29.610 -73.476 -13.262 1.000 150.187 ? 214 SER CCC N   1 
ATOM   4810  C CA  . SER C 3 214 ? -28.919 -74.726 -12.854 1.000 151.353 ? 214 SER CCC CA  1 
ATOM   4811  C C   . SER C 3 214 ? -27.445 -74.705 -13.268 1.000 153.277 ? 214 SER CCC C   1 
ATOM   4812  O O   . SER C 3 214 ? -27.065 -73.868 -14.108 1.000 154.256 ? 214 SER CCC O   1 
ATOM   4813  C CB  . SER C 3 214 ? -29.613 -75.936 -13.437 1.000 153.618 ? 214 SER CCC CB  1 
ATOM   4814  O OG  . SER C 3 214 ? -29.229 -76.147 -14.791 1.000 157.381 ? 214 SER CCC OG  1 
ATOM   4815  N N   . PHE C 3 215 ? -26.662 -75.620 -12.688 1.000 155.331 ? 215 PHE CCC N   1 
ATOM   4816  C CA  . PHE C 3 215 ? -25.270 -75.949 -13.088 1.000 160.491 ? 215 PHE CCC CA  1 
ATOM   4817  C C   . PHE C 3 215 ? -25.060 -77.461 -12.982 1.000 162.519 ? 215 PHE CCC C   1 
ATOM   4818  O O   . PHE C 3 215 ? -25.546 -78.088 -12.024 1.000 160.200 ? 215 PHE CCC O   1 
ATOM   4819  C CB  . PHE C 3 215 ? -24.253 -75.201 -12.220 1.000 161.502 ? 215 PHE CCC CB  1 
ATOM   4820  C CG  . PHE C 3 215 ? -24.245 -75.604 -10.767 1.000 159.633 ? 215 PHE CCC CG  1 
ATOM   4821  C CD1 . PHE C 3 215 ? -25.150 -75.051 -9.876  1.000 156.940 ? 215 PHE CCC CD1 1 
ATOM   4822  C CD2 . PHE C 3 215 ? -23.339 -76.541 -10.293 1.000 161.375 ? 215 PHE CCC CD2 1 
ATOM   4823  C CE1 . PHE C 3 215 ? -25.150 -75.429 -8.544  1.000 156.418 ? 215 PHE CCC CE1 1 
ATOM   4824  C CE2 . PHE C 3 215 ? -23.341 -76.916 -8.958  1.000 160.094 ? 215 PHE CCC CE2 1 
ATOM   4825  C CZ  . PHE C 3 215 ? -24.242 -76.356 -8.085  1.000 157.491 ? 215 PHE CCC CZ  1 
ATOM   4826  N N   . ASN C 3 216 ? -24.363 -78.030 -13.963 1.000 168.191 ? 216 ASN CCC N   1 
ATOM   4827  C CA  . ASN C 3 216 ? -23.720 -79.360 -13.832 1.000 173.012 ? 216 ASN CCC CA  1 
ATOM   4828  C C   . ASN C 3 216 ? -22.485 -79.151 -12.947 1.000 175.803 ? 216 ASN CCC C   1 
ATOM   4829  O O   . ASN C 3 216 ? -21.942 -78.022 -12.952 1.000 179.207 ? 216 ASN CCC O   1 
ATOM   4830  C CB  . ASN C 3 216 ? -23.413 -79.981 -15.198 1.000 177.875 ? 216 ASN CCC CB  1 
ATOM   4831  C CG  . ASN C 3 216 ? -24.624 -80.042 -16.108 1.000 179.782 ? 216 ASN CCC CG  1 
ATOM   4832  O OD1 . ASN C 3 216 ? -25.400 -79.089 -16.179 1.000 178.423 ? 216 ASN CCC OD1 1 
ATOM   4833  N ND2 . ASN C 3 216 ? -24.785 -81.147 -16.822 1.000 184.083 ? 216 ASN CCC ND2 1 
ATOM   4834  N N   . ARG C 3 217 ? -22.088 -80.178 -12.193 1.000 176.435 ? 217 ARG CCC N   1 
ATOM   4835  C CA  . ARG C 3 217 ? -20.968 -80.113 -11.217 1.000 176.914 ? 217 ARG CCC CA  1 
ATOM   4836  C C   . ARG C 3 217 ? -19.631 -79.972 -11.962 1.000 183.916 ? 217 ARG CCC C   1 
ATOM   4837  O O   . ARG C 3 217 ? -19.486 -80.541 -13.059 1.000 186.322 ? 217 ARG CCC O   1 
ATOM   4838  C CB  . ARG C 3 217 ? -20.993 -81.345 -10.310 1.000 174.558 ? 217 ARG CCC CB  1 
ATOM   4839  C CG  . ARG C 3 217 ? -20.152 -81.193 -9.051  1.000 174.138 ? 217 ARG CCC CG  1 
ATOM   4840  C CD  . ARG C 3 217 ? -20.694 -82.009 -7.905  1.000 171.784 ? 217 ARG CCC CD  1 
ATOM   4841  N NE  . ARG C 3 217 ? -20.931 -83.383 -8.323  1.000 172.047 ? 217 ARG CCC NE  1 
ATOM   4842  C CZ  . ARG C 3 217 ? -20.025 -84.356 -8.307  1.000 173.800 ? 217 ARG CCC CZ  1 
ATOM   4843  N NH1 . ARG C 3 217 ? -18.798 -84.124 -7.873  1.000 175.243 ? 217 ARG CCC NH1 1 
ATOM   4844  N NH2 . ARG C 3 217 ? -20.357 -85.569 -8.719  1.000 174.495 ? 217 ARG CCC NH2 1 
ATOM   4845  N N   . GLY C 3 218 ? -18.693 -79.229 -11.370 1.000 189.552 ? 218 GLY CCC N   1 
ATOM   4846  C CA  . GLY C 3 218 ? -17.361 -78.927 -11.932 1.000 197.737 ? 218 GLY CCC CA  1 
ATOM   4847  C C   . GLY C 3 218 ? -17.334 -77.580 -12.644 1.000 202.813 ? 218 GLY CCC C   1 
ATOM   4848  O O   . GLY C 3 218 ? -16.291 -77.248 -13.257 1.000 211.721 ? 218 GLY CCC O   1 
ATOM   4849  N N   . GLU C 3 219 ? -18.426 -76.808 -12.559 1.000 198.747 ? 219 GLU CCC N   1 
ATOM   4850  C CA  . GLU C 3 219 ? -18.626 -75.527 -13.292 1.000 195.815 ? 219 GLU CCC CA  1 
ATOM   4851  C C   . GLU C 3 219 ? -19.443 -74.589 -12.395 1.000 187.416 ? 219 GLU CCC C   1 
ATOM   4852  O O   . GLU C 3 219 ? -19.478 -73.381 -12.579 1.000 183.834 ? 219 GLU CCC O   1 
ATOM   4853  C CB  . GLU C 3 219 ? -19.317 -75.781 -14.640 1.000 196.630 ? 219 GLU CCC CB  1 
ATOM   4854  C CG  . GLU C 3 219 ? -18.508 -76.622 -15.629 1.000 200.436 ? 219 GLU CCC CG  1 
ATOM   4855  C CD  . GLU C 3 219 ? -18.761 -78.127 -15.591 1.000 198.742 ? 219 GLU CCC CD  1 
ATOM   4856  O OE1 . GLU C 3 219 ? -19.939 -78.524 -15.575 1.000 195.451 ? 219 GLU CCC OE1 1 
ATOM   4857  O OE2 . GLU C 3 219 ? -17.780 -78.902 -15.575 1.000 199.652 ? 219 GLU CCC OE2 1 
ATOM   4858  N N   . GLN D 4 1   ? -51.679 -17.390 75.846  1.000 255.980 ? 1   GLN DDD N   1 
ATOM   4859  C CA  . GLN D 4 1   ? -51.354 -18.687 76.507  1.000 255.740 ? 1   GLN DDD CA  1 
ATOM   4860  C C   . GLN D 4 1   ? -52.599 -19.246 77.205  1.000 256.955 ? 1   GLN DDD C   1 
ATOM   4861  O O   . GLN D 4 1   ? -53.426 -18.444 77.678  1.000 257.244 ? 1   GLN DDD O   1 
ATOM   4862  C CB  . GLN D 4 1   ? -50.240 -18.500 77.535  1.000 254.959 ? 1   GLN DDD CB  1 
ATOM   4863  C CG  . GLN D 4 1   ? -49.670 -19.806 78.061  1.000 253.701 ? 1   GLN DDD CG  1 
ATOM   4864  C CD  . GLN D 4 1   ? -48.801 -19.550 79.263  1.000 253.672 ? 1   GLN DDD CD  1 
ATOM   4865  O OE1 . GLN D 4 1   ? -49.209 -19.760 80.402  1.000 252.936 ? 1   GLN DDD OE1 1 
ATOM   4866  N NE2 . GLN D 4 1   ? -47.601 -19.053 79.014  1.000 254.127 ? 1   GLN DDD NE2 1 
ATOM   4867  N N   . VAL D 4 2   ? -52.703 -20.575 77.283  1.000 258.728 ? 2   VAL DDD N   1 
ATOM   4868  C CA  . VAL D 4 2   ? -53.787 -21.298 78.013  1.000 259.704 ? 2   VAL DDD CA  1 
ATOM   4869  C C   . VAL D 4 2   ? -53.489 -21.228 79.512  1.000 260.074 ? 2   VAL DDD C   1 
ATOM   4870  O O   . VAL D 4 2   ? -52.343 -21.534 79.897  1.000 260.111 ? 2   VAL DDD O   1 
ATOM   4871  C CB  . VAL D 4 2   ? -53.907 -22.760 77.543  1.000 260.295 ? 2   VAL DDD CB  1 
ATOM   4872  C CG1 . VAL D 4 2   ? -54.916 -23.534 78.379  1.000 260.731 ? 2   VAL DDD CG1 1 
ATOM   4873  C CG2 . VAL D 4 2   ? -54.244 -22.852 76.062  1.000 260.306 ? 2   VAL DDD CG2 1 
ATOM   4874  N N   . GLN D 4 3   ? -54.486 -20.849 80.316  1.000 260.622 ? 3   GLN DDD N   1 
ATOM   4875  C CA  . GLN D 4 3   ? -54.391 -20.787 81.797  1.000 262.113 ? 3   GLN DDD CA  1 
ATOM   4876  C C   . GLN D 4 3   ? -55.633 -21.428 82.413  1.000 263.333 ? 3   GLN DDD C   1 
ATOM   4877  O O   . GLN D 4 3   ? -56.750 -21.096 81.985  1.000 262.680 ? 3   GLN DDD O   1 
ATOM   4878  C CB  . GLN D 4 3   ? -54.212 -19.338 82.258  1.000 262.419 ? 3   GLN DDD CB  1 
ATOM   4879  C CG  . GLN D 4 3   ? -52.748 -18.930 82.395  1.000 262.956 ? 3   GLN DDD CG  1 
ATOM   4880  C CD  . GLN D 4 3   ? -52.359 -17.690 81.626  1.000 263.343 ? 3   GLN DDD CD  1 
ATOM   4881  O OE1 . GLN D 4 3   ? -52.985 -17.317 80.632  1.000 263.211 ? 3   GLN DDD OE1 1 
ATOM   4882  N NE2 . GLN D 4 3   ? -51.279 -17.063 82.064  1.000 263.837 ? 3   GLN DDD NE2 1 
ATOM   4883  N N   . LEU D 4 4   ? -55.414 -22.336 83.363  1.000 265.877 ? 4   LEU DDD N   1 
ATOM   4884  C CA  . LEU D 4 4   ? -56.456 -22.963 84.215  1.000 268.160 ? 4   LEU DDD CA  1 
ATOM   4885  C C   . LEU D 4 4   ? -56.460 -22.227 85.561  1.000 270.703 ? 4   LEU DDD C   1 
ATOM   4886  O O   . LEU D 4 4   ? -55.356 -21.909 86.042  1.000 271.639 ? 4   LEU DDD O   1 
ATOM   4887  C CB  . LEU D 4 4   ? -56.117 -24.451 84.372  1.000 268.396 ? 4   LEU DDD CB  1 
ATOM   4888  C CG  . LEU D 4 4   ? -55.765 -25.192 83.079  1.000 267.872 ? 4   LEU DDD CG  1 
ATOM   4889  C CD1 . LEU D 4 4   ? -55.681 -26.697 83.309  1.000 268.666 ? 4   LEU DDD CD1 1 
ATOM   4890  C CD2 . LEU D 4 4   ? -56.768 -24.883 81.980  1.000 267.216 ? 4   LEU DDD CD2 1 
ATOM   4891  N N   . VAL D 4 5   ? -57.640 -21.940 86.130  1.000 273.058 ? 5   VAL DDD N   1 
ATOM   4892  C CA  . VAL D 4 5   ? -57.795 -21.247 87.449  1.000 274.958 ? 5   VAL DDD CA  1 
ATOM   4893  C C   . VAL D 4 5   ? -58.842 -21.982 88.295  1.000 278.299 ? 5   VAL DDD C   1 
ATOM   4894  O O   . VAL D 4 5   ? -60.052 -21.770 88.053  1.000 278.072 ? 5   VAL DDD O   1 
ATOM   4895  C CB  . VAL D 4 5   ? -58.167 -19.760 87.278  1.000 273.241 ? 5   VAL DDD CB  1 
ATOM   4896  C CG1 . VAL D 4 5   ? -58.343 -19.064 88.622  1.000 273.370 ? 5   VAL DDD CG1 1 
ATOM   4897  C CG2 . VAL D 4 5   ? -57.151 -19.017 86.426  1.000 272.407 ? 5   VAL DDD CG2 1 
ATOM   4898  N N   . GLU D 4 6   ? -58.389 -22.786 89.266  1.000 282.769 ? 6   GLU DDD N   1 
ATOM   4899  C CA  . GLU D 4 6   ? -59.256 -23.484 90.256  1.000 286.729 ? 6   GLU DDD CA  1 
ATOM   4900  C C   . GLU D 4 6   ? -59.859 -22.440 91.207  1.000 287.087 ? 6   GLU DDD C   1 
ATOM   4901  O O   . GLU D 4 6   ? -59.302 -21.325 91.299  1.000 287.846 ? 6   GLU DDD O   1 
ATOM   4902  C CB  . GLU D 4 6   ? -58.477 -24.544 91.046  1.000 290.354 ? 6   GLU DDD CB  1 
ATOM   4903  C CG  . GLU D 4 6   ? -57.966 -25.706 90.206  1.000 291.999 ? 6   GLU DDD CG  1 
ATOM   4904  C CD  . GLU D 4 6   ? -56.585 -25.503 89.597  1.000 293.115 ? 6   GLU DDD CD  1 
ATOM   4905  O OE1 . GLU D 4 6   ? -56.200 -24.333 89.370  1.000 293.652 ? 6   GLU DDD OE1 1 
ATOM   4906  O OE2 . GLU D 4 6   ? -55.891 -26.517 89.351  1.000 295.343 ? 6   GLU DDD OE2 1 
ATOM   4907  N N   . SER D 4 7   ? -60.974 -22.786 91.858  1.000 286.344 ? 7   SER DDD N   1 
ATOM   4908  C CA  . SER D 4 7   ? -61.593 -22.036 92.983  1.000 284.842 ? 7   SER DDD CA  1 
ATOM   4909  C C   . SER D 4 7   ? -62.673 -22.907 93.634  1.000 284.599 ? 7   SER DDD C   1 
ATOM   4910  O O   . SER D 4 7   ? -63.026 -23.954 93.052  1.000 284.184 ? 7   SER DDD O   1 
ATOM   4911  C CB  . SER D 4 7   ? -62.148 -20.706 92.533  1.000 283.551 ? 7   SER DDD CB  1 
ATOM   4912  O OG  . SER D 4 7   ? -62.943 -20.853 91.368  1.000 283.011 ? 7   SER DDD OG  1 
ATOM   4913  N N   . GLY D 4 8   ? -63.167 -22.490 94.800  1.000 284.440 ? 8   GLY DDD N   1 
ATOM   4914  C CA  . GLY D 4 8   ? -64.210 -23.212 95.554  1.000 285.789 ? 8   GLY DDD CA  1 
ATOM   4915  C C   . GLY D 4 8   ? -63.617 -24.136 96.601  1.000 287.185 ? 8   GLY DDD C   1 
ATOM   4916  O O   . GLY D 4 8   ? -64.397 -24.876 97.236  1.000 289.767 ? 8   GLY DDD O   1 
ATOM   4917  N N   . GLY D 4 9   ? -62.291 -24.102 96.775  1.000 285.594 ? 9   GLY DDD N   1 
ATOM   4918  C CA  . GLY D 4 9   ? -61.588 -24.784 97.877  1.000 286.488 ? 9   GLY DDD CA  1 
ATOM   4919  C C   . GLY D 4 9   ? -61.896 -24.127 99.210  1.000 287.100 ? 9   GLY DDD C   1 
ATOM   4920  O O   . GLY D 4 9   ? -62.192 -22.917 99.214  1.000 285.078 ? 9   GLY DDD O   1 
ATOM   4921  N N   . GLY D 4 10  ? -61.833 -24.898 100.300 1.000 289.228 ? 10  GLY DDD N   1 
ATOM   4922  C CA  . GLY D 4 10  ? -62.043 -24.395 101.668 1.000 291.167 ? 10  GLY DDD CA  1 
ATOM   4923  C C   . GLY D 4 10  ? -62.340 -25.507 102.658 1.000 293.885 ? 10  GLY DDD C   1 
ATOM   4924  O O   . GLY D 4 10  ? -61.844 -26.641 102.468 1.000 294.535 ? 10  GLY DDD O   1 
ATOM   4925  N N   . LEU D 4 11  ? -63.149 -25.176 103.663 1.000 295.452 ? 11  LEU DDD N   1 
ATOM   4926  C CA  . LEU D 4 11  ? -63.386 -25.957 104.901 1.000 299.325 ? 11  LEU DDD CA  1 
ATOM   4927  C C   . LEU D 4 11  ? -64.750 -26.642 104.785 1.000 301.302 ? 11  LEU DDD C   1 
ATOM   4928  O O   . LEU D 4 11  ? -65.658 -25.997 104.237 1.000 300.122 ? 11  LEU DDD O   1 
ATOM   4929  C CB  . LEU D 4 11  ? -63.361 -24.943 106.049 1.000 300.159 ? 11  LEU DDD CB  1 
ATOM   4930  C CG  . LEU D 4 11  ? -62.819 -25.414 107.393 1.000 303.488 ? 11  LEU DDD CG  1 
ATOM   4931  C CD1 . LEU D 4 11  ? -61.348 -25.771 107.314 1.000 303.297 ? 11  LEU DDD CD1 1 
ATOM   4932  C CD2 . LEU D 4 11  ? -63.011 -24.319 108.417 1.000 304.944 ? 11  LEU DDD CD2 1 
ATOM   4933  N N   . MET D 4 12  ? -64.901 -27.882 105.270 1.000 305.067 ? 12  MET DDD N   1 
ATOM   4934  C CA  . MET D 4 12  ? -66.199 -28.617 105.233 1.000 307.130 ? 12  MET DDD CA  1 
ATOM   4935  C C   . MET D 4 12  ? -66.208 -29.782 106.228 1.000 310.022 ? 12  MET DDD C   1 
ATOM   4936  O O   . MET D 4 12  ? -65.386 -30.710 106.057 1.000 310.941 ? 12  MET DDD O   1 
ATOM   4937  C CB  . MET D 4 12  ? -66.482 -29.179 103.834 1.000 306.414 ? 12  MET DDD CB  1 
ATOM   4938  C CG  . MET D 4 12  ? -67.377 -28.295 102.984 1.000 304.756 ? 12  MET DDD CG  1 
ATOM   4939  S SD  . MET D 4 12  ? -68.745 -27.567 103.943 1.000 307.325 ? 12  MET DDD SD  1 
ATOM   4940  C CE  . MET D 4 12  ? -69.776 -29.006 104.208 1.000 310.820 ? 12  MET DDD CE  1 
ATOM   4941  N N   . GLN D 4 13  ? -67.139 -29.768 107.189 1.000 311.203 ? 13  GLN DDD N   1 
ATOM   4942  C CA  . GLN D 4 13  ? -67.318 -30.890 108.149 1.000 313.989 ? 13  GLN DDD CA  1 
ATOM   4943  C C   . GLN D 4 13  ? -67.713 -32.128 107.327 1.000 313.362 ? 13  GLN DDD C   1 
ATOM   4944  O O   . GLN D 4 13  ? -68.681 -32.034 106.536 1.000 312.085 ? 13  GLN DDD O   1 
ATOM   4945  C CB  . GLN D 4 13  ? -68.268 -30.510 109.292 1.000 316.171 ? 13  GLN DDD CB  1 
ATOM   4946  C CG  . GLN D 4 13  ? -69.732 -30.341 108.913 1.000 315.246 ? 13  GLN DDD CG  1 
ATOM   4947  C CD  . GLN D 4 13  ? -70.560 -29.951 110.114 1.000 317.801 ? 13  GLN DDD CD  1 
ATOM   4948  O OE1 . GLN D 4 13  ? -70.114 -30.011 111.260 1.000 319.828 ? 13  GLN DDD OE1 1 
ATOM   4949  N NE2 . GLN D 4 13  ? -71.790 -29.539 109.859 1.000 317.022 ? 13  GLN DDD NE2 1 
ATOM   4950  N N   . ALA D 4 14  ? -66.924 -33.204 107.454 1.000 313.552 ? 14  ALA DDD N   1 
ATOM   4951  C CA  . ALA D 4 14  ? -67.030 -34.476 106.695 1.000 312.670 ? 14  ALA DDD CA  1 
ATOM   4952  C C   . ALA D 4 14  ? -68.488 -34.940 106.652 1.000 314.716 ? 14  ALA DDD C   1 
ATOM   4953  O O   . ALA D 4 14  ? -69.124 -34.978 107.717 1.000 318.798 ? 14  ALA DDD O   1 
ATOM   4954  C CB  . ALA D 4 14  ? -66.144 -35.527 107.319 1.000 314.639 ? 14  ALA DDD CB  1 
ATOM   4955  N N   . GLY D 4 15  ? -68.988 -35.285 105.463 1.000 312.756 ? 15  GLY DDD N   1 
ATOM   4956  C CA  . GLY D 4 15  ? -70.404 -35.633 105.234 1.000 314.715 ? 15  GLY DDD CA  1 
ATOM   4957  C C   . GLY D 4 15  ? -71.169 -34.499 104.572 1.000 312.552 ? 15  GLY DDD C   1 
ATOM   4958  O O   . GLY D 4 15  ? -72.233 -34.787 103.995 1.000 312.886 ? 15  GLY DDD O   1 
ATOM   4959  N N   . GLY D 4 16  ? -70.668 -33.259 104.666 1.000 310.913 ? 16  GLY DDD N   1 
ATOM   4960  C CA  . GLY D 4 16  ? -71.173 -32.099 103.901 1.000 308.366 ? 16  GLY DDD CA  1 
ATOM   4961  C C   . GLY D 4 16  ? -70.883 -32.260 102.414 1.000 305.520 ? 16  GLY DDD C   1 
ATOM   4962  O O   . GLY D 4 16  ? -70.772 -33.419 101.975 1.000 306.375 ? 16  GLY DDD O   1 
ATOM   4963  N N   . SER D 4 17  ? -70.752 -31.163 101.657 1.000 302.403 ? 17  SER DDD N   1 
ATOM   4964  C CA  . SER D 4 17  ? -70.294 -31.174 100.239 1.000 299.376 ? 17  SER DDD CA  1 
ATOM   4965  C C   . SER D 4 17  ? -69.568 -29.871 99.884  1.000 296.216 ? 17  SER DDD C   1 
ATOM   4966  O O   . SER D 4 17  ? -69.822 -28.845 100.539 1.000 294.880 ? 17  SER DDD O   1 
ATOM   4967  C CB  . SER D 4 17  ? -71.432 -31.442 99.292  1.000 299.478 ? 17  SER DDD CB  1 
ATOM   4968  O OG  . SER D 4 17  ? -70.954 -31.608 97.963  1.000 297.089 ? 17  SER DDD OG  1 
ATOM   4969  N N   . LEU D 4 18  ? -68.701 -29.932 98.869  1.000 295.092 ? 18  LEU DDD N   1 
ATOM   4970  C CA  . LEU D 4 18  ? -67.969 -28.767 98.306  1.000 292.908 ? 18  LEU DDD CA  1 
ATOM   4971  C C   . LEU D 4 18  ? -67.890 -28.900 96.778  1.000 291.346 ? 18  LEU DDD C   1 
ATOM   4972  O O   . LEU D 4 18  ? -67.675 -30.031 96.279  1.000 292.256 ? 18  LEU DDD O   1 
ATOM   4973  C CB  . LEU D 4 18  ? -66.575 -28.712 98.942  1.000 292.572 ? 18  LEU DDD CB  1 
ATOM   4974  C CG  . LEU D 4 18  ? -65.859 -27.361 98.902  1.000 289.920 ? 18  LEU DDD CG  1 
ATOM   4975  C CD1 . LEU D 4 18  ? -66.836 -26.197 98.999  1.000 288.962 ? 18  LEU DDD CD1 1 
ATOM   4976  C CD2 . LEU D 4 18  ? -64.822 -27.280 100.011 1.000 291.031 ? 18  LEU DDD CD2 1 
ATOM   4977  N N   . ARG D 4 19  ? -68.068 -27.782 96.069  1.000 289.222 ? 19  ARG DDD N   1 
ATOM   4978  C CA  . ARG D 4 19  ? -67.994 -27.681 94.588  1.000 287.075 ? 19  ARG DDD CA  1 
ATOM   4979  C C   . ARG D 4 19  ? -66.678 -26.994 94.209  1.000 287.353 ? 19  ARG DDD C   1 
ATOM   4980  O O   . ARG D 4 19  ? -66.338 -25.982 94.858  1.000 287.418 ? 19  ARG DDD O   1 
ATOM   4981  C CB  . ARG D 4 19  ? -69.207 -26.898 94.085  1.000 284.378 ? 19  ARG DDD CB  1 
ATOM   4982  C CG  . ARG D 4 19  ? -69.306 -26.773 92.574  1.000 280.376 ? 19  ARG DDD CG  1 
ATOM   4983  C CD  . ARG D 4 19  ? -70.560 -26.002 92.235  1.000 279.181 ? 19  ARG DDD CD  1 
ATOM   4984  N NE  . ARG D 4 19  ? -70.791 -25.913 90.805  1.000 276.836 ? 19  ARG DDD NE  1 
ATOM   4985  C CZ  . ARG D 4 19  ? -71.896 -25.421 90.251  1.000 276.780 ? 19  ARG DDD CZ  1 
ATOM   4986  N NH1 . ARG D 4 19  ? -72.883 -24.960 91.004  1.000 277.973 ? 19  ARG DDD NH1 1 
ATOM   4987  N NH2 . ARG D 4 19  ? -72.013 -25.394 88.936  1.000 275.974 ? 19  ARG DDD NH2 1 
ATOM   4988  N N   . LEU D 4 20  ? -65.962 -27.532 93.217  1.000 288.822 ? 20  LEU DDD N   1 
ATOM   4989  C CA  . LEU D 4 20  ? -64.698 -26.950 92.686  1.000 288.137 ? 20  LEU DDD CA  1 
ATOM   4990  C C   . LEU D 4 20  ? -64.921 -26.528 91.230  1.000 287.595 ? 20  LEU DDD C   1 
ATOM   4991  O O   . LEU D 4 20  ? -65.624 -27.259 90.505  1.000 288.754 ? 20  LEU DDD O   1 
ATOM   4992  C CB  . LEU D 4 20  ? -63.567 -27.975 92.816  1.000 288.299 ? 20  LEU DDD CB  1 
ATOM   4993  C CG  . LEU D 4 20  ? -62.852 -27.979 94.166  1.000 288.950 ? 20  LEU DDD CG  1 
ATOM   4994  C CD1 . LEU D 4 20  ? -62.755 -29.383 94.721  1.000 290.567 ? 20  LEU DDD CD1 1 
ATOM   4995  C CD2 . LEU D 4 20  ? -61.473 -27.359 94.059  1.000 287.400 ? 20  LEU DDD CD2 1 
ATOM   4996  N N   . SER D 4 21  ? -64.349 -25.384 90.839  1.000 286.474 ? 21  SER DDD N   1 
ATOM   4997  C CA  . SER D 4 21  ? -64.568 -24.712 89.532  1.000 284.612 ? 21  SER DDD CA  1 
ATOM   4998  C C   . SER D 4 21  ? -63.217 -24.385 88.884  1.000 283.244 ? 21  SER DDD C   1 
ATOM   4999  O O   . SER D 4 21  ? -62.502 -23.524 89.431  1.000 283.112 ? 21  SER DDD O   1 
ATOM   5000  C CB  . SER D 4 21  ? -65.403 -23.468 89.712  1.000 284.014 ? 21  SER DDD CB  1 
ATOM   5001  O OG  . SER D 4 21  ? -66.409 -23.669 90.695  1.000 285.656 ? 21  SER DDD OG  1 
ATOM   5002  N N   . CYS D 4 22  ? -62.886 -25.050 87.770  1.000 282.557 ? 22  CYS DDD N   1 
ATOM   5003  C CA  . CYS D 4 22  ? -61.657 -24.806 86.964  1.000 280.572 ? 22  CYS DDD CA  1 
ATOM   5004  C C   . CYS D 4 22  ? -62.032 -24.076 85.665  1.000 278.924 ? 22  CYS DDD C   1 
ATOM   5005  O O   . CYS D 4 22  ? -62.625 -24.713 84.761  1.000 278.083 ? 22  CYS DDD O   1 
ATOM   5006  C CB  . CYS D 4 22  ? -60.910 -26.105 86.684  1.000 280.378 ? 22  CYS DDD CB  1 
ATOM   5007  S SG  . CYS D 4 22  ? -59.575 -25.927 85.469  1.000 278.602 ? 22  CYS DDD SG  1 
ATOM   5008  N N   . ALA D 4 23  ? -61.707 -22.782 85.600  1.000 277.364 ? 23  ALA DDD N   1 
ATOM   5009  C CA  . ALA D 4 23  ? -61.975 -21.877 84.458  1.000 275.555 ? 23  ALA DDD CA  1 
ATOM   5010  C C   . ALA D 4 23  ? -60.783 -21.915 83.494  1.000 274.616 ? 23  ALA DDD C   1 
ATOM   5011  O O   . ALA D 4 23  ? -59.632 -21.770 83.967  1.000 274.027 ? 23  ALA DDD O   1 
ATOM   5012  C CB  . ALA D 4 23  ? -62.241 -20.477 84.960  1.000 275.112 ? 23  ALA DDD CB  1 
ATOM   5013  N N   . VAL D 4 24  ? -61.062 -22.103 82.199  1.000 274.873 ? 24  VAL DDD N   1 
ATOM   5014  C CA  . VAL D 4 24  ? -60.058 -22.258 81.103  1.000 273.962 ? 24  VAL DDD CA  1 
ATOM   5015  C C   . VAL D 4 24  ? -60.160 -21.043 80.174  1.000 271.927 ? 24  VAL DDD C   1 
ATOM   5016  O O   . VAL D 4 24  ? -61.279 -20.762 79.709  1.000 272.155 ? 24  VAL DDD O   1 
ATOM   5017  C CB  . VAL D 4 24  ? -60.292 -23.563 80.313  1.000 275.294 ? 24  VAL DDD CB  1 
ATOM   5018  C CG1 . VAL D 4 24  ? -59.134 -23.867 79.375  1.000 275.076 ? 24  VAL DDD CG1 1 
ATOM   5019  C CG2 . VAL D 4 24  ? -60.571 -24.755 81.219  1.000 276.367 ? 24  VAL DDD CG2 1 
ATOM   5020  N N   . SER D 4 25  ? -59.044 -20.358 79.907  1.000 269.527 ? 25  SER DDD N   1 
ATOM   5021  C CA  . SER D 4 25  ? -58.947 -19.262 78.906  1.000 268.631 ? 25  SER DDD CA  1 
ATOM   5022  C C   . SER D 4 25  ? -57.766 -19.527 77.966  1.000 268.526 ? 25  SER DDD C   1 
ATOM   5023  O O   . SER D 4 25  ? -56.628 -19.625 78.466  1.000 268.071 ? 25  SER DDD O   1 
ATOM   5024  C CB  . SER D 4 25  ? -58.826 -17.915 79.566  1.000 268.118 ? 25  SER DDD CB  1 
ATOM   5025  O OG  . SER D 4 25  ? -57.583 -17.791 80.240  1.000 267.892 ? 25  SER DDD OG  1 
ATOM   5026  N N   . GLY D 4 26  ? -58.039 -19.622 76.659  1.000 268.659 ? 26  GLY DDD N   1 
ATOM   5027  C CA  . GLY D 4 26  ? -57.057 -19.926 75.595  1.000 267.845 ? 26  GLY DDD CA  1 
ATOM   5028  C C   . GLY D 4 26  ? -57.732 -20.541 74.379  1.000 267.210 ? 26  GLY DDD C   1 
ATOM   5029  O O   . GLY D 4 26  ? -58.933 -20.279 74.177  1.000 267.795 ? 26  GLY DDD O   1 
ATOM   5030  N N   . ARG D 4 27  ? -56.998 -21.333 73.595  1.000 266.118 ? 27  ARG DDD N   1 
ATOM   5031  C CA  . ARG D 4 27  ? -57.552 -22.095 72.444  1.000 266.679 ? 27  ARG DDD CA  1 
ATOM   5032  C C   . ARG D 4 27  ? -58.532 -23.154 72.968  1.000 267.185 ? 27  ARG DDD C   1 
ATOM   5033  O O   . ARG D 4 27  ? -58.103 -24.312 73.122  1.000 267.605 ? 27  ARG DDD O   1 
ATOM   5034  C CB  . ARG D 4 27  ? -56.430 -22.766 71.647  1.000 265.908 ? 27  ARG DDD CB  1 
ATOM   5035  C CG  . ARG D 4 27  ? -55.499 -21.796 70.940  1.000 265.884 ? 27  ARG DDD CG  1 
ATOM   5036  C CD  . ARG D 4 27  ? -54.667 -22.524 69.907  1.000 265.731 ? 27  ARG DDD CD  1 
ATOM   5037  N NE  . ARG D 4 27  ? -53.623 -21.679 69.348  1.000 265.940 ? 27  ARG DDD NE  1 
ATOM   5038  C CZ  . ARG D 4 27  ? -52.999 -21.898 68.193  1.000 266.426 ? 27  ARG DDD CZ  1 
ATOM   5039  N NH1 . ARG D 4 27  ? -53.315 -22.943 67.444  1.000 266.763 ? 27  ARG DDD NH1 1 
ATOM   5040  N NH2 . ARG D 4 27  ? -52.061 -21.062 67.782  1.000 266.959 ? 27  ARG DDD NH2 1 
ATOM   5041  N N   . THR D 4 28  ? -59.790 -22.768 73.234  1.000 267.523 ? 28  THR DDD N   1 
ATOM   5042  C CA  . THR D 4 28  ? -60.879 -23.648 73.756  1.000 267.120 ? 28  THR DDD CA  1 
ATOM   5043  C C   . THR D 4 28  ? -61.200 -24.774 72.766  1.000 268.262 ? 28  THR DDD C   1 
ATOM   5044  O O   . THR D 4 28  ? -61.541 -25.883 73.231  1.000 268.140 ? 28  THR DDD O   1 
ATOM   5045  C CB  . THR D 4 28  ? -62.188 -22.886 74.004  1.000 266.717 ? 28  THR DDD CB  1 
ATOM   5046  O OG1 . THR D 4 28  ? -61.996 -21.988 75.097  1.000 265.842 ? 28  THR DDD OG1 1 
ATOM   5047  C CG2 . THR D 4 28  ? -63.361 -23.798 74.299  1.000 266.587 ? 28  THR DDD CG2 1 
ATOM   5048  N N   . PHE D 4 29  ? -61.135 -24.476 71.462  1.000 269.150 ? 29  PHE DDD N   1 
ATOM   5049  C CA  . PHE D 4 29  ? -61.569 -25.359 70.344  1.000 269.705 ? 29  PHE DDD CA  1 
ATOM   5050  C C   . PHE D 4 29  ? -60.850 -26.712 70.422  1.000 270.531 ? 29  PHE DDD C   1 
ATOM   5051  O O   . PHE D 4 29  ? -61.474 -27.744 70.109  1.000 271.016 ? 29  PHE DDD O   1 
ATOM   5052  C CB  . PHE D 4 29  ? -61.327 -24.678 68.991  1.000 268.806 ? 29  PHE DDD CB  1 
ATOM   5053  C CG  . PHE D 4 29  ? -59.904 -24.706 68.485  1.000 266.782 ? 29  PHE DDD CG  1 
ATOM   5054  C CD1 . PHE D 4 29  ? -59.421 -25.801 67.781  1.000 266.222 ? 29  PHE DDD CD1 1 
ATOM   5055  C CD2 . PHE D 4 29  ? -59.053 -23.628 68.686  1.000 265.152 ? 29  PHE DDD CD2 1 
ATOM   5056  C CE1 . PHE D 4 29  ? -58.118 -25.826 67.307  1.000 265.211 ? 29  PHE DDD CE1 1 
ATOM   5057  C CE2 . PHE D 4 29  ? -57.752 -23.656 68.209  1.000 264.557 ? 29  PHE DDD CE2 1 
ATOM   5058  C CZ  . PHE D 4 29  ? -57.286 -24.754 67.523  1.000 264.629 ? 29  PHE DDD CZ  1 
ATOM   5059  N N   . SER D 4 30  ? -59.581 -26.696 70.839  1.000 270.952 ? 30  SER DDD N   1 
ATOM   5060  C CA  . SER D 4 30  ? -58.640 -27.844 70.774  1.000 270.933 ? 30  SER DDD CA  1 
ATOM   5061  C C   . SER D 4 30  ? -58.725 -28.721 72.036  1.000 270.419 ? 30  SER DDD C   1 
ATOM   5062  O O   . SER D 4 30  ? -57.996 -29.732 72.078  1.000 270.534 ? 30  SER DDD O   1 
ATOM   5063  C CB  . SER D 4 30  ? -57.234 -27.343 70.509  1.000 270.719 ? 30  SER DDD CB  1 
ATOM   5064  O OG  . SER D 4 30  ? -57.025 -26.050 71.070  1.000 270.540 ? 30  SER DDD OG  1 
ATOM   5065  N N   . THR D 4 31  ? -59.587 -28.390 73.010  1.000 270.099 ? 31  THR DDD N   1 
ATOM   5066  C CA  . THR D 4 31  ? -59.749 -29.149 74.284  1.000 269.485 ? 31  THR DDD CA  1 
ATOM   5067  C C   . THR D 4 31  ? -60.361 -30.525 73.999  1.000 269.828 ? 31  THR DDD C   1 
ATOM   5068  O O   . THR D 4 31  ? -61.498 -30.567 73.492  1.000 270.067 ? 31  THR DDD O   1 
ATOM   5069  C CB  . THR D 4 31  ? -60.636 -28.417 75.300  1.000 269.505 ? 31  THR DDD CB  1 
ATOM   5070  O OG1 . THR D 4 31  ? -60.135 -27.092 75.468  1.000 269.128 ? 31  THR DDD OG1 1 
ATOM   5071  C CG2 . THR D 4 31  ? -60.687 -29.111 76.644  1.000 269.061 ? 31  THR DDD CG2 1 
ATOM   5072  N N   . ALA D 4 32  ? -59.637 -31.598 74.334  1.000 269.364 ? 32  ALA DDD N   1 
ATOM   5073  C CA  . ALA D 4 32  ? -60.101 -33.001 74.238  1.000 270.179 ? 32  ALA DDD CA  1 
ATOM   5074  C C   . ALA D 4 32  ? -60.889 -33.348 75.506  1.000 270.952 ? 32  ALA DDD C   1 
ATOM   5075  O O   . ALA D 4 32  ? -62.091 -33.673 75.394  1.000 271.714 ? 32  ALA DDD O   1 
ATOM   5076  C CB  . ALA D 4 32  ? -58.921 -33.927 74.036  1.000 269.639 ? 32  ALA DDD CB  1 
ATOM   5077  N N   . ALA D 4 33  ? -60.223 -33.247 76.662  1.000 270.876 ? 33  ALA DDD N   1 
ATOM   5078  C CA  . ALA D 4 33  ? -60.712 -33.685 77.990  1.000 272.410 ? 33  ALA DDD CA  1 
ATOM   5079  C C   . ALA D 4 33  ? -60.151 -32.769 79.083  1.000 273.266 ? 33  ALA DDD C   1 
ATOM   5080  O O   . ALA D 4 33  ? -59.052 -32.209 78.883  1.000 272.689 ? 33  ALA DDD O   1 
ATOM   5081  C CB  . ALA D 4 33  ? -60.307 -35.121 78.223  1.000 272.344 ? 33  ALA DDD CB  1 
ATOM   5082  N N   . MET D 4 34  ? -60.887 -32.634 80.194  1.000 276.234 ? 34  MET DDD N   1 
ATOM   5083  C CA  . MET D 4 34  ? -60.433 -32.002 81.465  1.000 277.007 ? 34  MET DDD CA  1 
ATOM   5084  C C   . MET D 4 34  ? -60.361 -33.082 82.549  1.000 277.757 ? 34  MET DDD C   1 
ATOM   5085  O O   . MET D 4 34  ? -61.246 -33.958 82.558  1.000 278.137 ? 34  MET DDD O   1 
ATOM   5086  C CB  . MET D 4 34  ? -61.405 -30.915 81.933  1.000 278.342 ? 34  MET DDD CB  1 
ATOM   5087  C CG  . MET D 4 34  ? -61.561 -29.756 80.967  1.000 278.346 ? 34  MET DDD CG  1 
ATOM   5088  S SD  . MET D 4 34  ? -60.060 -28.760 80.778  1.000 278.162 ? 34  MET DDD SD  1 
ATOM   5089  C CE  . MET D 4 34  ? -59.902 -28.059 82.418  1.000 277.636 ? 34  MET DDD CE  1 
ATOM   5090  N N   . GLY D 4 35  ? -59.360 -33.010 83.431  1.000 277.975 ? 35  GLY DDD N   1 
ATOM   5091  C CA  . GLY D 4 35  ? -59.163 -33.966 84.538  1.000 280.030 ? 35  GLY DDD CA  1 
ATOM   5092  C C   . GLY D 4 35  ? -58.922 -33.259 85.861  1.000 280.935 ? 35  GLY DDD C   1 
ATOM   5093  O O   . GLY D 4 35  ? -58.288 -32.190 85.851  1.000 281.032 ? 35  GLY DDD O   1 
ATOM   5094  N N   . TRP D 4 36  ? -59.420 -33.830 86.960  1.000 282.058 ? 36  TRP DDD N   1 
ATOM   5095  C CA  . TRP D 4 36  ? -59.086 -33.407 88.344  1.000 282.303 ? 36  TRP DDD CA  1 
ATOM   5096  C C   . TRP D 4 36  ? -58.043 -34.378 88.914  1.000 283.331 ? 36  TRP DDD C   1 
ATOM   5097  O O   . TRP D 4 36  ? -58.218 -35.603 88.742  1.000 284.256 ? 36  TRP DDD O   1 
ATOM   5098  C CB  . TRP D 4 36  ? -60.360 -33.315 89.194  1.000 283.248 ? 36  TRP DDD CB  1 
ATOM   5099  C CG  . TRP D 4 36  ? -61.192 -32.110 88.875  1.000 281.821 ? 36  TRP DDD CG  1 
ATOM   5100  C CD1 . TRP D 4 36  ? -62.298 -32.058 88.079  1.000 280.929 ? 36  TRP DDD CD1 1 
ATOM   5101  C CD2 . TRP D 4 36  ? -60.972 -30.764 89.333  1.000 281.273 ? 36  TRP DDD CD2 1 
ATOM   5102  N NE1 . TRP D 4 36  ? -62.782 -30.779 88.014  1.000 279.932 ? 36  TRP DDD NE1 1 
ATOM   5103  C CE2 . TRP D 4 36  ? -61.990 -29.962 88.775  1.000 280.223 ? 36  TRP DDD CE2 1 
ATOM   5104  C CE3 . TRP D 4 36  ? -60.019 -30.160 90.162  1.000 281.696 ? 36  TRP DDD CE3 1 
ATOM   5105  C CZ2 . TRP D 4 36  ? -62.082 -28.592 89.023  1.000 279.863 ? 36  TRP DDD CZ2 1 
ATOM   5106  C CZ3 . TRP D 4 36  ? -60.110 -28.807 90.409  1.000 280.978 ? 36  TRP DDD CZ3 1 
ATOM   5107  C CH2 . TRP D 4 36  ? -61.125 -28.035 89.841  1.000 280.141 ? 36  TRP DDD CH2 1 
ATOM   5108  N N   . PHE D 4 37  ? -56.967 -33.842 89.500  1.000 283.044 ? 37  PHE DDD N   1 
ATOM   5109  C CA  . PHE D 4 37  ? -55.950 -34.587 90.290  1.000 283.790 ? 37  PHE DDD CA  1 
ATOM   5110  C C   . PHE D 4 37  ? -55.864 -33.958 91.683  1.000 286.243 ? 37  PHE DDD C   1 
ATOM   5111  O O   . PHE D 4 37  ? -56.049 -32.725 91.792  1.000 286.635 ? 37  PHE DDD O   1 
ATOM   5112  C CB  . PHE D 4 37  ? -54.570 -34.542 89.627  1.000 280.569 ? 37  PHE DDD CB  1 
ATOM   5113  C CG  . PHE D 4 37  ? -54.454 -35.320 88.342  1.000 277.385 ? 37  PHE DDD CG  1 
ATOM   5114  C CD1 . PHE D 4 37  ? -55.052 -34.855 87.184  1.000 274.649 ? 37  PHE DDD CD1 1 
ATOM   5115  C CD2 . PHE D 4 37  ? -53.732 -36.504 88.282  1.000 276.546 ? 37  PHE DDD CD2 1 
ATOM   5116  C CE1 . PHE D 4 37  ? -54.947 -35.564 86.000  1.000 272.688 ? 37  PHE DDD CE1 1 
ATOM   5117  C CE2 . PHE D 4 37  ? -53.630 -37.214 87.096  1.000 274.164 ? 37  PHE DDD CE2 1 
ATOM   5118  C CZ  . PHE D 4 37  ? -54.238 -36.742 85.957  1.000 272.648 ? 37  PHE DDD CZ  1 
ATOM   5119  N N   . ARG D 4 38  ? -55.594 -34.770 92.709  1.000 287.955 ? 38  ARG DDD N   1 
ATOM   5120  C CA  . ARG D 4 38  ? -55.363 -34.289 94.097  1.000 288.098 ? 38  ARG DDD CA  1 
ATOM   5121  C C   . ARG D 4 38  ? -54.042 -34.873 94.601  1.000 289.760 ? 38  ARG DDD C   1 
ATOM   5122  O O   . ARG D 4 38  ? -53.717 -36.031 94.246  1.000 291.186 ? 38  ARG DDD O   1 
ATOM   5123  C CB  . ARG D 4 38  ? -56.542 -34.646 95.010  1.000 288.171 ? 38  ARG DDD CB  1 
ATOM   5124  C CG  . ARG D 4 38  ? -56.650 -36.123 95.357  1.000 288.684 ? 38  ARG DDD CG  1 
ATOM   5125  C CD  . ARG D 4 38  ? -57.957 -36.436 96.054  1.000 289.354 ? 38  ARG DDD CD  1 
ATOM   5126  N NE  . ARG D 4 38  ? -58.110 -37.858 96.310  1.000 290.506 ? 38  ARG DDD NE  1 
ATOM   5127  C CZ  . ARG D 4 38  ? -59.180 -38.416 96.859  1.000 292.235 ? 38  ARG DDD CZ  1 
ATOM   5128  N NH1 . ARG D 4 38  ? -60.210 -37.668 97.222  1.000 292.491 ? 38  ARG DDD NH1 1 
ATOM   5129  N NH2 . ARG D 4 38  ? -59.210 -39.725 97.048  1.000 294.062 ? 38  ARG DDD NH2 1 
ATOM   5130  N N   . GLN D 4 39  ? -53.309 -34.070 95.372  1.000 289.983 ? 39  GLN DDD N   1 
ATOM   5131  C CA  . GLN D 4 39  ? -52.132 -34.500 96.162  1.000 291.663 ? 39  GLN DDD CA  1 
ATOM   5132  C C   . GLN D 4 39  ? -52.469 -34.315 97.642  1.000 294.852 ? 39  GLN DDD C   1 
ATOM   5133  O O   . GLN D 4 39  ? -52.615 -33.153 98.066  1.000 295.948 ? 39  GLN DDD O   1 
ATOM   5134  C CB  . GLN D 4 39  ? -50.903 -33.678 95.789  1.000 290.019 ? 39  GLN DDD CB  1 
ATOM   5135  C CG  . GLN D 4 39  ? -49.695 -33.984 96.657  1.000 292.135 ? 39  GLN DDD CG  1 
ATOM   5136  C CD  . GLN D 4 39  ? -48.427 -33.944 95.841  1.000 290.527 ? 39  GLN DDD CD  1 
ATOM   5137  O OE1 . GLN D 4 39  ? -48.171 -32.997 95.102  1.000 288.658 ? 39  GLN DDD OE1 1 
ATOM   5138  N NE2 . GLN D 4 39  ? -47.633 -34.996 95.945  1.000 291.273 ? 39  GLN DDD NE2 1 
ATOM   5139  N N   . ALA D 4 40  ? -52.613 -35.421 98.378  1.000 296.959 ? 40  ALA DDD N   1 
ATOM   5140  C CA  . ALA D 4 40  ? -52.834 -35.443 99.843  1.000 299.400 ? 40  ALA DDD CA  1 
ATOM   5141  C C   . ALA D 4 40  ? -51.513 -35.123 100.534 1.000 299.923 ? 40  ALA DDD C   1 
ATOM   5142  O O   . ALA D 4 40  ? -50.459 -35.148 99.900  1.000 298.618 ? 40  ALA DDD O   1 
ATOM   5143  C CB  . ALA D 4 40  ? -53.369 -36.791 100.267 1.000 301.733 ? 40  ALA DDD CB  1 
ATOM   5144  N N   . PRO D 4 41  ? -51.514 -34.804 101.846 1.000 301.645 ? 41  PRO DDD N   1 
ATOM   5145  C CA  . PRO D 4 41  ? -50.259 -34.658 102.579 1.000 303.280 ? 41  PRO DDD CA  1 
ATOM   5146  C C   . PRO D 4 41  ? -49.526 -36.008 102.605 1.000 304.236 ? 41  PRO DDD C   1 
ATOM   5147  O O   . PRO D 4 41  ? -50.168 -37.002 102.884 1.000 305.359 ? 41  PRO DDD O   1 
ATOM   5148  C CB  . PRO D 4 41  ? -50.715 -34.197 103.972 1.000 306.523 ? 41  PRO DDD CB  1 
ATOM   5149  C CG  . PRO D 4 41  ? -52.122 -34.740 104.089 1.000 307.063 ? 41  PRO DDD CG  1 
ATOM   5150  C CD  . PRO D 4 41  ? -52.695 -34.587 102.696 1.000 303.190 ? 41  PRO DDD CD  1 
ATOM   5151  N N   . GLY D 4 42  ? -48.239 -36.018 102.240 1.000 303.544 ? 42  GLY DDD N   1 
ATOM   5152  C CA  . GLY D 4 42  ? -47.342 -37.186 102.349 1.000 305.246 ? 42  GLY DDD CA  1 
ATOM   5153  C C   . GLY D 4 42  ? -47.426 -38.145 101.168 1.000 302.839 ? 42  GLY DDD C   1 
ATOM   5154  O O   . GLY D 4 42  ? -46.543 -39.018 101.072 1.000 303.293 ? 42  GLY DDD O   1 
ATOM   5155  N N   . LYS D 4 43  ? -48.435 -37.992 100.300 1.000 273.798 ? 43  LYS DDD N   1 
ATOM   5156  C CA  . LYS D 4 43  ? -48.789 -38.947 99.210  1.000 271.854 ? 43  LYS DDD CA  1 
ATOM   5157  C C   . LYS D 4 43  ? -48.479 -38.339 97.840  1.000 270.164 ? 43  LYS DDD C   1 
ATOM   5158  O O   . LYS D 4 43  ? -48.622 -37.109 97.701  1.000 270.035 ? 43  LYS DDD O   1 
ATOM   5159  C CB  . LYS D 4 43  ? -50.281 -39.292 99.270  1.000 271.916 ? 43  LYS DDD CB  1 
ATOM   5160  C CG  . LYS D 4 43  ? -50.626 -40.576 100.009 1.000 271.945 ? 43  LYS DDD CG  1 
ATOM   5161  C CD  . LYS D 4 43  ? -52.113 -40.849 100.040 1.000 271.879 ? 43  LYS DDD CD  1 
ATOM   5162  C CE  . LYS D 4 43  ? -52.458 -42.243 100.514 1.000 271.759 ? 43  LYS DDD CE  1 
ATOM   5163  N NZ  . LYS D 4 43  ? -52.565 -43.192 99.381  1.000 269.671 ? 43  LYS DDD NZ  1 
ATOM   5164  N N   . GLU D 4 44  ? -48.151 -39.183 96.855  1.000 268.995 ? 44  GLU DDD N   1 
ATOM   5165  C CA  . GLU D 4 44  ? -47.967 -38.793 95.430  1.000 267.858 ? 44  GLU DDD CA  1 
ATOM   5166  C C   . GLU D 4 44  ? -49.331 -38.377 94.864  1.000 267.862 ? 44  GLU DDD C   1 
ATOM   5167  O O   . GLU D 4 44  ? -50.335 -38.988 95.278  1.000 268.538 ? 44  GLU DDD O   1 
ATOM   5168  C CB  . GLU D 4 44  ? -47.357 -39.954 94.635  1.000 266.481 ? 44  GLU DDD CB  1 
ATOM   5169  C CG  . GLU D 4 44  ? -46.117 -40.567 95.275  1.000 267.396 ? 44  GLU DDD CG  1 
ATOM   5170  C CD  . GLU D 4 44  ? -44.958 -39.617 95.521  1.000 268.569 ? 44  GLU DDD CD  1 
ATOM   5171  O OE1 . GLU D 4 44  ? -44.436 -39.059 94.530  1.000 268.644 ? 44  GLU DDD OE1 1 
ATOM   5172  O OE2 . GLU D 4 44  ? -44.564 -39.457 96.702  1.000 269.929 ? 44  GLU DDD OE2 1 
ATOM   5173  N N   . ARG D 4 45  ? -49.374 -37.377 93.972  1.000 267.203 ? 45  ARG DDD N   1 
ATOM   5174  C CA  . ARG D 4 45  ? -50.647 -36.815 93.431  1.000 266.943 ? 45  ARG DDD CA  1 
ATOM   5175  C C   . ARG D 4 45  ? -51.245 -37.859 92.479  1.000 266.199 ? 45  ARG DDD C   1 
ATOM   5176  O O   . ARG D 4 45  ? -50.531 -38.320 91.570  1.000 264.982 ? 45  ARG DDD O   1 
ATOM   5177  C CB  . ARG D 4 45  ? -50.459 -35.406 92.840  1.000 265.293 ? 45  ARG DDD CB  1 
ATOM   5178  C CG  . ARG D 4 45  ? -50.483 -35.256 91.323  1.000 261.942 ? 45  ARG DDD CG  1 
ATOM   5179  C CD  . ARG D 4 45  ? -49.223 -35.730 90.624  1.000 259.398 ? 45  ARG DDD CD  1 
ATOM   5180  N NE  . ARG D 4 45  ? -49.513 -36.901 89.809  1.000 257.396 ? 45  ARG DDD NE  1 
ATOM   5181  C CZ  . ARG D 4 45  ? -49.611 -36.918 88.481  1.000 255.481 ? 45  ARG DDD CZ  1 
ATOM   5182  N NH1 . ARG D 4 45  ? -49.409 -35.821 87.772  1.000 255.021 ? 45  ARG DDD NH1 1 
ATOM   5183  N NH2 . ARG D 4 45  ? -49.891 -38.051 87.859  1.000 254.273 ? 45  ARG DDD NH2 1 
ATOM   5184  N N   . GLU D 4 46  ? -52.495 -38.250 92.734  1.000 267.256 ? 46  GLU DDD N   1 
ATOM   5185  C CA  . GLU D 4 46  ? -53.174 -39.406 92.089  1.000 266.413 ? 46  GLU DDD CA  1 
ATOM   5186  C C   . GLU D 4 46  ? -54.329 -38.888 91.231  1.000 267.710 ? 46  GLU DDD C   1 
ATOM   5187  O O   . GLU D 4 46  ? -54.775 -37.743 91.456  1.000 269.097 ? 46  GLU DDD O   1 
ATOM   5188  C CB  . GLU D 4 46  ? -53.685 -40.393 93.142  1.000 266.487 ? 46  GLU DDD CB  1 
ATOM   5189  C CG  . GLU D 4 46  ? -54.759 -39.812 94.049  1.000 267.530 ? 46  GLU DDD CG  1 
ATOM   5190  C CD  . GLU D 4 46  ? -54.794 -40.321 95.486  1.000 268.401 ? 46  GLU DDD CD  1 
ATOM   5191  O OE1 . GLU D 4 46  ? -55.909 -40.433 96.028  1.000 268.905 ? 46  GLU DDD OE1 1 
ATOM   5192  O OE2 . GLU D 4 46  ? -53.720 -40.575 96.076  1.000 267.432 ? 46  GLU DDD OE2 1 
ATOM   5193  N N   . PHE D 4 47  ? -54.777 -39.705 90.277  1.000 268.211 ? 47  PHE DDD N   1 
ATOM   5194  C CA  . PHE D 4 47  ? -55.942 -39.432 89.399  1.000 268.532 ? 47  PHE DDD CA  1 
ATOM   5195  C C   . PHE D 4 47  ? -57.207 -39.341 90.263  1.000 270.367 ? 47  PHE DDD C   1 
ATOM   5196  O O   . PHE D 4 47  ? -57.273 -40.065 91.272  1.000 271.498 ? 47  PHE DDD O   1 
ATOM   5197  C CB  . PHE D 4 47  ? -56.067 -40.538 88.350  1.000 267.296 ? 47  PHE DDD CB  1 
ATOM   5198  C CG  . PHE D 4 47  ? -57.280 -40.413 87.469  1.000 267.712 ? 47  PHE DDD CG  1 
ATOM   5199  C CD1 . PHE D 4 47  ? -57.468 -39.282 86.690  1.000 267.771 ? 47  PHE DDD CD1 1 
ATOM   5200  C CD2 . PHE D 4 47  ? -58.230 -41.421 87.418  1.000 268.310 ? 47  PHE DDD CD2 1 
ATOM   5201  C CE1 . PHE D 4 47  ? -58.584 -39.165 85.876  1.000 267.848 ? 47  PHE DDD CE1 1 
ATOM   5202  C CE2 . PHE D 4 47  ? -59.345 -41.302 86.602  1.000 268.268 ? 47  PHE DDD CE2 1 
ATOM   5203  C CZ  . PHE D 4 47  ? -59.522 -40.172 85.835  1.000 267.997 ? 47  PHE DDD CZ  1 
ATOM   5204  N N   . VAL D 4 48  ? -58.158 -38.477 89.887  1.000 270.550 ? 48  VAL DDD N   1 
ATOM   5205  C CA  . VAL D 4 48  ? -59.476 -38.301 90.574  1.000 271.663 ? 48  VAL DDD CA  1 
ATOM   5206  C C   . VAL D 4 48  ? -60.590 -38.650 89.583  1.000 269.902 ? 48  VAL DDD C   1 
ATOM   5207  O O   . VAL D 4 48  ? -61.293 -39.654 89.793  1.000 269.052 ? 48  VAL DDD O   1 
ATOM   5208  C CB  . VAL D 4 48  ? -59.657 -36.867 91.112  1.000 273.627 ? 48  VAL DDD CB  1 
ATOM   5209  C CG1 . VAL D 4 48  ? -61.052 -36.631 91.683  1.000 275.380 ? 48  VAL DDD CG1 1 
ATOM   5210  C CG2 . VAL D 4 48  ? -58.586 -36.500 92.130  1.000 275.251 ? 48  VAL DDD CG2 1 
ATOM   5211  N N   . ALA D 4 49  ? -60.759 -37.818 88.558  1.000 268.729 ? 49  ALA DDD N   1 
ATOM   5212  C CA  . ALA D 4 49  ? -61.822 -37.940 87.537  1.000 267.866 ? 49  ALA DDD CA  1 
ATOM   5213  C C   . ALA D 4 49  ? -61.381 -37.204 86.269  1.000 266.123 ? 49  ALA DDD C   1 
ATOM   5214  O O   . ALA D 4 49  ? -60.582 -36.249 86.392  1.000 268.174 ? 49  ALA DDD O   1 
ATOM   5215  C CB  . ALA D 4 49  ? -63.117 -37.386 88.083  1.000 269.120 ? 49  ALA DDD CB  1 
ATOM   5216  N N   . ALA D 4 50  ? -61.866 -37.652 85.106  1.000 262.206 ? 50  ALA DDD N   1 
ATOM   5217  C CA  . ALA D 4 50  ? -61.737 -36.959 83.803  1.000 258.310 ? 50  ALA DDD CA  1 
ATOM   5218  C C   . ALA D 4 50  ? -63.103 -36.944 83.110  1.000 256.027 ? 50  ALA DDD C   1 
ATOM   5219  O O   . ALA D 4 50  ? -63.928 -37.821 83.426  1.000 254.462 ? 50  ALA DDD O   1 
ATOM   5220  C CB  . ALA D 4 50  ? -60.682 -37.637 82.964  1.000 256.955 ? 50  ALA DDD CB  1 
ATOM   5221  N N   . ILE D 4 51  ? -63.325 -35.971 82.221  1.000 254.581 ? 51  ILE DDD N   1 
ATOM   5222  C CA  . ILE D 4 51  ? -64.575 -35.808 81.418  1.000 253.917 ? 51  ILE DDD CA  1 
ATOM   5223  C C   . ILE D 4 51  ? -64.203 -35.429 79.980  1.000 251.546 ? 51  ILE DDD C   1 
ATOM   5224  O O   . ILE D 4 51  ? -63.408 -34.486 79.814  1.000 252.351 ? 51  ILE DDD O   1 
ATOM   5225  C CB  . ILE D 4 51  ? -65.502 -34.746 82.042  1.000 255.567 ? 51  ILE DDD CB  1 
ATOM   5226  C CG1 . ILE D 4 51  ? -66.851 -34.695 81.320  1.000 255.255 ? 51  ILE DDD CG1 1 
ATOM   5227  C CG2 . ILE D 4 51  ? -64.829 -33.380 82.067  1.000 256.283 ? 51  ILE DDD CG2 1 
ATOM   5228  C CD1 . ILE D 4 51  ? -67.938 -33.986 82.098  1.000 257.186 ? 51  ILE DDD CD1 1 
ATOM   5229  N N   . ARG D 4 52  ? -64.778 -36.114 78.984  1.000 248.233 ? 52  ARG DDD N   1 
ATOM   5230  C CA  . ARG D 4 52  ? -64.598 -35.770 77.548  1.000 244.621 ? 52  ARG DDD CA  1 
ATOM   5231  C C   . ARG D 4 52  ? -65.389 -34.491 77.249  1.000 245.206 ? 52  ARG DDD C   1 
ATOM   5232  O O   . ARG D 4 52  ? -66.580 -34.430 77.614  1.000 246.290 ? 52  ARG DDD O   1 
ATOM   5233  C CB  . ARG D 4 52  ? -65.032 -36.910 76.623  1.000 241.199 ? 52  ARG DDD CB  1 
ATOM   5234  C CG  . ARG D 4 52  ? -64.461 -36.780 75.220  1.000 237.563 ? 52  ARG DDD CG  1 
ATOM   5235  C CD  . ARG D 4 52  ? -65.022 -37.805 74.262  1.000 234.981 ? 52  ARG DDD CD  1 
ATOM   5236  N NE  . ARG D 4 52  ? -64.651 -39.169 74.604  1.000 233.649 ? 52  ARG DDD NE  1 
ATOM   5237  C CZ  . ARG D 4 52  ? -63.423 -39.676 74.508  1.000 232.648 ? 52  ARG DDD CZ  1 
ATOM   5238  N NH1 . ARG D 4 52  ? -62.409 -38.926 74.106  1.000 232.129 ? 52  ARG DDD NH1 1 
ATOM   5239  N NH2 . ARG D 4 52  ? -63.208 -40.941 74.828  1.000 232.560 ? 52  ARG DDD NH2 1 
ATOM   5240  N N   . TRP D 4 53  ? -64.738 -33.507 76.623  1.000 244.737 ? 53  TRP DDD N   1 
ATOM   5241  C CA  . TRP D 4 53  ? -65.347 -32.205 76.240  1.000 245.060 ? 53  TRP DDD CA  1 
ATOM   5242  C C   . TRP D 4 53  ? -66.586 -32.460 75.375  1.000 244.145 ? 53  TRP DDD C   1 
ATOM   5243  O O   . TRP D 4 53  ? -67.639 -31.867 75.670  1.000 245.563 ? 53  TRP DDD O   1 
ATOM   5244  C CB  . TRP D 4 53  ? -64.324 -31.316 75.516  1.000 244.364 ? 53  TRP DDD CB  1 
ATOM   5245  C CG  . TRP D 4 53  ? -64.482 -29.847 75.774  1.000 245.022 ? 53  TRP DDD CG  1 
ATOM   5246  C CD1 . TRP D 4 53  ? -64.675 -28.857 74.854  1.000 244.466 ? 53  TRP DDD CD1 1 
ATOM   5247  C CD2 . TRP D 4 53  ? -64.445 -29.196 77.054  1.000 246.226 ? 53  TRP DDD CD2 1 
ATOM   5248  N NE1 . TRP D 4 53  ? -64.762 -27.638 75.472  1.000 245.364 ? 53  TRP DDD NE1 1 
ATOM   5249  C CE2 . TRP D 4 53  ? -64.626 -27.816 76.822  1.000 246.808 ? 53  TRP DDD CE2 1 
ATOM   5250  C CE3 . TRP D 4 53  ? -64.278 -29.648 78.367  1.000 247.150 ? 53  TRP DDD CE3 1 
ATOM   5251  C CZ2 . TRP D 4 53  ? -64.646 -26.885 77.860  1.000 248.901 ? 53  TRP DDD CZ2 1 
ATOM   5252  C CZ3 . TRP D 4 53  ? -64.298 -28.729 79.391  1.000 249.109 ? 53  TRP DDD CZ3 1 
ATOM   5253  C CH2 . TRP D 4 53  ? -64.485 -27.368 79.140  1.000 250.034 ? 53  TRP DDD CH2 1 
ATOM   5254  N N   . SER D 4 54  ? -66.462 -33.330 74.368  1.000 241.088 ? 54  SER DDD N   1 
ATOM   5255  C CA  . SER D 4 54  ? -67.497 -33.593 73.335  1.000 239.520 ? 54  SER DDD CA  1 
ATOM   5256  C C   . SER D 4 54  ? -68.316 -34.837 73.702  1.000 239.235 ? 54  SER DDD C   1 
ATOM   5257  O O   . SER D 4 54  ? -68.297 -35.802 72.916  1.000 238.449 ? 54  SER DDD O   1 
ATOM   5258  C CB  . SER D 4 54  ? -66.849 -33.714 71.971  1.000 237.425 ? 54  SER DDD CB  1 
ATOM   5259  O OG  . SER D 4 54  ? -67.701 -34.340 71.020  1.000 236.308 ? 54  SER DDD OG  1 
ATOM   5260  N N   . GLY D 4 55  ? -69.018 -34.819 74.842  1.000 240.210 ? 55  GLY DDD N   1 
ATOM   5261  C CA  . GLY D 4 55  ? -69.995 -35.871 75.198  1.000 240.035 ? 55  GLY DDD CA  1 
ATOM   5262  C C   . GLY D 4 55  ? -70.320 -35.957 76.682  1.000 241.693 ? 55  GLY DDD C   1 
ATOM   5263  O O   . GLY D 4 55  ? -71.376 -36.531 76.997  1.000 241.881 ? 55  GLY DDD O   1 
ATOM   5264  N N   . GLY D 4 56  ? -69.454 -35.443 77.562  1.000 242.990 ? 56  GLY DDD N   1 
ATOM   5265  C CA  . GLY D 4 56  ? -69.696 -35.359 79.016  1.000 244.930 ? 56  GLY DDD CA  1 
ATOM   5266  C C   . GLY D 4 56  ? -69.698 -36.719 79.697  1.000 244.772 ? 56  GLY DDD C   1 
ATOM   5267  O O   . GLY D 4 56  ? -70.079 -36.773 80.881  1.000 245.753 ? 56  GLY DDD O   1 
ATOM   5268  N N   . SER D 4 57  ? -69.301 -37.784 78.993  1.000 243.145 ? 57  SER DDD N   1 
ATOM   5269  C CA  . SER D 4 57  ? -69.028 -39.116 79.593  1.000 242.977 ? 57  SER DDD CA  1 
ATOM   5270  C C   . SER D 4 57  ? -67.784 -38.987 80.483  1.000 244.090 ? 57  SER DDD C   1 
ATOM   5271  O O   . SER D 4 57  ? -66.725 -38.608 79.947  1.000 243.915 ? 57  SER DDD O   1 
ATOM   5272  C CB  . SER D 4 57  ? -68.878 -40.191 78.535  1.000 240.247 ? 57  SER DDD CB  1 
ATOM   5273  O OG  . SER D 4 57  ? -68.781 -39.622 77.238  1.000 237.793 ? 57  SER DDD OG  1 
ATOM   5274  N N   . ALA D 4 58  ? -67.926 -39.227 81.793  1.000 245.722 ? 58  ALA DDD N   1 
ATOM   5275  C CA  . ALA D 4 58  ? -66.855 -39.075 82.809  1.000 246.689 ? 58  ALA DDD CA  1 
ATOM   5276  C C   . ALA D 4 58  ? -66.246 -40.441 83.139  1.000 246.266 ? 58  ALA DDD C   1 
ATOM   5277  O O   . ALA D 4 58  ? -66.936 -41.460 82.931  1.000 245.353 ? 58  ALA DDD O   1 
ATOM   5278  C CB  . ALA D 4 58  ? -67.406 -38.426 84.054  1.000 249.338 ? 58  ALA DDD CB  1 
ATOM   5279  N N   . TYR D 4 59  ? -65.006 -40.449 83.646  1.000 246.833 ? 59  TYR DDD N   1 
ATOM   5280  C CA  . TYR D 4 59  ? -64.338 -41.653 84.205  1.000 247.843 ? 59  TYR DDD CA  1 
ATOM   5281  C C   . TYR D 4 59  ? -63.935 -41.393 85.652  1.000 252.363 ? 59  TYR DDD C   1 
ATOM   5282  O O   . TYR D 4 59  ? -62.768 -41.026 85.925  1.000 253.414 ? 59  TYR DDD O   1 
ATOM   5283  C CB  . TYR D 4 59  ? -63.106 -42.077 83.408  1.000 245.005 ? 59  TYR DDD CB  1 
ATOM   5284  C CG  . TYR D 4 59  ? -62.541 -43.414 83.822  1.000 243.910 ? 59  TYR DDD CG  1 
ATOM   5285  C CD1 . TYR D 4 59  ? -63.367 -44.441 84.260  1.000 244.095 ? 59  TYR DDD CD1 1 
ATOM   5286  C CD2 . TYR D 4 59  ? -61.178 -43.658 83.759  1.000 242.906 ? 59  TYR DDD CD2 1 
ATOM   5287  C CE1 . TYR D 4 59  ? -62.854 -45.673 84.625  1.000 244.143 ? 59  TYR DDD CE1 1 
ATOM   5288  C CE2 . TYR D 4 59  ? -60.648 -44.885 84.119  1.000 242.819 ? 59  TYR DDD CE2 1 
ATOM   5289  C CZ  . TYR D 4 59  ? -61.491 -45.896 84.547  1.000 243.565 ? 59  TYR DDD CZ  1 
ATOM   5290  O OH  . TYR D 4 59  ? -60.978 -47.109 84.901  1.000 243.686 ? 59  TYR DDD OH  1 
ATOM   5291  N N   . TYR D 4 60  ? -64.896 -41.603 86.547  1.000 256.466 ? 60  TYR DDD N   1 
ATOM   5292  C CA  . TYR D 4 60  ? -64.715 -41.527 88.012  1.000 259.560 ? 60  TYR DDD CA  1 
ATOM   5293  C C   . TYR D 4 60  ? -63.665 -42.560 88.432  1.000 258.405 ? 60  TYR DDD C   1 
ATOM   5294  O O   . TYR D 4 60  ? -63.710 -43.718 87.951  1.000 255.520 ? 60  TYR DDD O   1 
ATOM   5295  C CB  . TYR D 4 60  ? -66.090 -41.613 88.672  1.000 263.112 ? 60  TYR DDD CB  1 
ATOM   5296  C CG  . TYR D 4 60  ? -66.676 -40.241 88.810  1.000 266.169 ? 60  TYR DDD CG  1 
ATOM   5297  C CD1 . TYR D 4 60  ? -67.145 -39.547 87.706  1.000 265.700 ? 60  TYR DDD CD1 1 
ATOM   5298  C CD2 . TYR D 4 60  ? -66.634 -39.601 90.032  1.000 270.246 ? 60  TYR DDD CD2 1 
ATOM   5299  C CE1 . TYR D 4 60  ? -67.637 -38.265 87.833  1.000 268.172 ? 60  TYR DDD CE1 1 
ATOM   5300  C CE2 . TYR D 4 60  ? -67.114 -38.318 90.175  1.000 272.837 ? 60  TYR DDD CE2 1 
ATOM   5301  C CZ  . TYR D 4 60  ? -67.610 -37.657 89.072  1.000 272.182 ? 60  TYR DDD CZ  1 
ATOM   5302  O OH  . TYR D 4 60  ? -68.082 -36.395 89.200  1.000 276.011 ? 60  TYR DDD OH  1 
ATOM   5303  N N   . ALA D 4 61  ? -62.698 -42.113 89.244  1.000 259.387 ? 61  ALA DDD N   1 
ATOM   5304  C CA  . ALA D 4 61  ? -61.642 -42.957 89.844  1.000 259.850 ? 61  ALA DDD CA  1 
ATOM   5305  C C   . ALA D 4 61  ? -62.252 -43.780 90.981  1.000 262.052 ? 61  ALA DDD C   1 
ATOM   5306  O O   . ALA D 4 61  ? -63.321 -43.399 91.499  1.000 264.729 ? 61  ALA DDD O   1 
ATOM   5307  C CB  . ALA D 4 61  ? -60.491 -42.119 90.338  1.000 260.129 ? 61  ALA DDD CB  1 
ATOM   5308  N N   . ASP D 4 62  ? -61.545 -44.831 91.385  1.000 261.435 ? 62  ASP DDD N   1 
ATOM   5309  C CA  . ASP D 4 62  ? -62.084 -45.994 92.136  1.000 261.785 ? 62  ASP DDD CA  1 
ATOM   5310  C C   . ASP D 4 62  ? -62.524 -45.567 93.546  1.000 264.868 ? 62  ASP DDD C   1 
ATOM   5311  O O   . ASP D 4 62  ? -63.535 -46.111 94.029  1.000 266.323 ? 62  ASP DDD O   1 
ATOM   5312  C CB  . ASP D 4 62  ? -61.052 -47.123 92.191  1.000 259.943 ? 62  ASP DDD CB  1 
ATOM   5313  C CG  . ASP D 4 62  ? -60.089 -47.146 91.013  1.000 256.836 ? 62  ASP DDD CG  1 
ATOM   5314  O OD1 . ASP D 4 62  ? -59.438 -46.113 90.752  1.000 255.204 ? 62  ASP DDD OD1 1 
ATOM   5315  O OD2 . ASP D 4 62  ? -60.005 -48.193 90.362  1.000 255.044 ? 62  ASP DDD OD2 1 
ATOM   5316  N N   . SER D 4 63  ? -61.793 -44.645 94.183  1.000 265.871 ? 63  SER DDD N   1 
ATOM   5317  C CA  . SER D 4 63  ? -61.980 -44.266 95.611  1.000 267.898 ? 63  SER DDD CA  1 
ATOM   5318  C C   . SER D 4 63  ? -63.013 -43.140 95.759  1.000 269.999 ? 63  SER DDD C   1 
ATOM   5319  O O   . SER D 4 63  ? -63.371 -42.836 96.920  1.000 271.904 ? 63  SER DDD O   1 
ATOM   5320  C CB  . SER D 4 63  ? -60.668 -43.898 96.257  1.000 267.320 ? 63  SER DDD CB  1 
ATOM   5321  O OG  . SER D 4 63  ? -59.868 -43.117 95.385  1.000 264.863 ? 63  SER DDD OG  1 
ATOM   5322  N N   . VAL D 4 64  ? -63.474 -42.546 94.650  1.000 270.135 ? 64  VAL DDD N   1 
ATOM   5323  C CA  . VAL D 4 64  ? -64.503 -41.455 94.644  1.000 271.353 ? 64  VAL DDD CA  1 
ATOM   5324  C C   . VAL D 4 64  ? -65.793 -41.932 93.953  1.000 269.619 ? 64  VAL DDD C   1 
ATOM   5325  O O   . VAL D 4 64  ? -66.836 -41.269 94.148  1.000 270.076 ? 64  VAL DDD O   1 
ATOM   5326  C CB  . VAL D 4 64  ? -63.962 -40.156 94.006  1.000 271.903 ? 64  VAL DDD CB  1 
ATOM   5327  C CG1 . VAL D 4 64  ? -62.736 -39.635 94.747  1.000 272.646 ? 64  VAL DDD CG1 1 
ATOM   5328  C CG2 . VAL D 4 64  ? -63.659 -40.319 92.521  1.000 269.953 ? 64  VAL DDD CG2 1 
ATOM   5329  N N   . LYS D 4 65  ? -65.736 -43.014 93.167  1.000 266.613 ? 65  LYS DDD N   1 
ATOM   5330  C CA  . LYS D 4 65  ? -66.923 -43.588 92.476  1.000 264.764 ? 65  LYS DDD CA  1 
ATOM   5331  C C   . LYS D 4 65  ? -68.065 -43.647 93.498  1.000 266.852 ? 65  LYS DDD C   1 
ATOM   5332  O O   . LYS D 4 65  ? -67.905 -44.354 94.504  1.000 267.495 ? 65  LYS DDD O   1 
ATOM   5333  C CB  . LYS D 4 65  ? -66.593 -44.966 91.882  1.000 261.889 ? 65  LYS DDD CB  1 
ATOM   5334  C CG  . LYS D 4 65  ? -67.066 -45.203 90.451  1.000 258.482 ? 65  LYS DDD CG  1 
ATOM   5335  C CD  . LYS D 4 65  ? -66.182 -46.167 89.674  1.000 255.441 ? 65  LYS DDD CD  1 
ATOM   5336  C CE  . LYS D 4 65  ? -66.330 -46.047 88.170  1.000 252.275 ? 65  LYS DDD CE  1 
ATOM   5337  N NZ  . LYS D 4 65  ? -65.039 -46.226 87.461  1.000 249.986 ? 65  LYS DDD NZ  1 
ATOM   5338  N N   . GLY D 4 66  ? -69.128 -42.864 93.285  1.000 267.889 ? 66  GLY DDD N   1 
ATOM   5339  C CA  . GLY D 4 66  ? -70.364 -42.890 94.092  1.000 270.570 ? 66  GLY DDD CA  1 
ATOM   5340  C C   . GLY D 4 66  ? -70.473 -41.717 95.051  1.000 274.109 ? 66  GLY DDD C   1 
ATOM   5341  O O   . GLY D 4 66  ? -71.457 -41.689 95.807  1.000 275.077 ? 66  GLY DDD O   1 
ATOM   5342  N N   . ARG D 4 67  ? -69.512 -40.785 95.025  1.000 277.008 ? 67  ARG DDD N   1 
ATOM   5343  C CA  . ARG D 4 67  ? -69.480 -39.595 95.922  1.000 281.933 ? 67  ARG DDD CA  1 
ATOM   5344  C C   . ARG D 4 67  ? -69.359 -38.313 95.081  1.000 282.365 ? 67  ARG DDD C   1 
ATOM   5345  O O   . ARG D 4 67  ? -70.249 -37.450 95.198  1.000 283.667 ? 67  ARG DDD O   1 
ATOM   5346  C CB  . ARG D 4 67  ? -68.361 -39.744 96.962  1.000 284.272 ? 67  ARG DDD CB  1 
ATOM   5347  C CG  . ARG D 4 67  ? -68.423 -41.052 97.742  1.000 286.058 ? 67  ARG DDD CG  1 
ATOM   5348  C CD  . ARG D 4 67  ? -67.534 -41.122 98.975  1.000 288.227 ? 67  ARG DDD CD  1 
ATOM   5349  N NE  . ARG D 4 67  ? -66.139 -40.837 98.661  1.000 287.655 ? 67  ARG DDD NE  1 
ATOM   5350  C CZ  . ARG D 4 67  ? -65.454 -39.777 99.082  1.000 289.417 ? 67  ARG DDD CZ  1 
ATOM   5351  N NH1 . ARG D 4 67  ? -66.013 -38.881 99.883  1.000 292.160 ? 67  ARG DDD NH1 1 
ATOM   5352  N NH2 . ARG D 4 67  ? -64.193 -39.630 98.713  1.000 288.315 ? 67  ARG DDD NH2 1 
ATOM   5353  N N   . PHE D 4 68  ? -68.323 -38.197 94.246  1.000 281.711 ? 68  PHE DDD N   1 
ATOM   5354  C CA  . PHE D 4 68  ? -68.003 -36.963 93.475  1.000 281.795 ? 68  PHE DDD CA  1 
ATOM   5355  C C   . PHE D 4 68  ? -68.926 -36.884 92.240  1.000 281.291 ? 68  PHE DDD C   1 
ATOM   5356  O O   . PHE D 4 68  ? -69.631 -37.881 91.981  1.000 280.567 ? 68  PHE DDD O   1 
ATOM   5357  C CB  . PHE D 4 68  ? -66.494 -36.943 93.192  1.000 280.708 ? 68  PHE DDD CB  1 
ATOM   5358  C CG  . PHE D 4 68  ? -65.611 -36.728 94.400  1.000 282.273 ? 68  PHE DDD CG  1 
ATOM   5359  C CD1 . PHE D 4 68  ? -66.123 -36.804 95.689  1.000 284.352 ? 68  PHE DDD CD1 1 
ATOM   5360  C CD2 . PHE D 4 68  ? -64.251 -36.483 94.251  1.000 281.471 ? 68  PHE DDD CD2 1 
ATOM   5361  C CE1 . PHE D 4 68  ? -65.309 -36.608 96.792  1.000 285.426 ? 68  PHE DDD CE1 1 
ATOM   5362  C CE2 . PHE D 4 68  ? -63.438 -36.290 95.358  1.000 282.654 ? 68  PHE DDD CE2 1 
ATOM   5363  C CZ  . PHE D 4 68  ? -63.969 -36.355 96.624  1.000 284.726 ? 68  PHE DDD CZ  1 
ATOM   5364  N N   . THR D 4 69  ? -68.971 -35.734 91.535  1.000 282.012 ? 69  THR DDD N   1 
ATOM   5365  C CA  . THR D 4 69  ? -69.556 -35.573 90.161  1.000 281.042 ? 69  THR DDD CA  1 
ATOM   5366  C C   . THR D 4 69  ? -68.782 -34.507 89.351  1.000 280.365 ? 69  THR DDD C   1 
ATOM   5367  O O   . THR D 4 69  ? -68.949 -33.301 89.651  1.000 281.397 ? 69  THR DDD O   1 
ATOM   5368  C CB  . THR D 4 69  ? -71.058 -35.251 90.148  1.000 281.843 ? 69  THR DDD CB  1 
ATOM   5369  O OG1 . THR D 4 69  ? -71.749 -36.120 91.047  1.000 282.777 ? 69  THR DDD OG1 1 
ATOM   5370  C CG2 . THR D 4 69  ? -71.649 -35.394 88.759  1.000 280.095 ? 69  THR DDD CG2 1 
ATOM   5371  N N   . ILE D 4 70  ? -67.989 -34.943 88.351  1.000 278.019 ? 70  ILE DDD N   1 
ATOM   5372  C CA  . ILE D 4 70  ? -67.312 -34.090 87.329  1.000 275.700 ? 70  ILE DDD CA  1 
ATOM   5373  C C   . ILE D 4 70  ? -68.336 -33.805 86.231  1.000 272.921 ? 70  ILE DDD C   1 
ATOM   5374  O O   . ILE D 4 70  ? -69.063 -34.731 85.815  1.000 271.129 ? 70  ILE DDD O   1 
ATOM   5375  C CB  . ILE D 4 70  ? -66.013 -34.715 86.763  1.000 275.229 ? 70  ILE DDD CB  1 
ATOM   5376  C CG1 . ILE D 4 70  ? -65.167 -33.666 86.034  1.000 275.677 ? 70  ILE DDD CG1 1 
ATOM   5377  C CG2 . ILE D 4 70  ? -66.296 -35.905 85.858  1.000 273.809 ? 70  ILE DDD CG2 1 
ATOM   5378  C CD1 . ILE D 4 70  ? -63.823 -34.176 85.540  1.000 274.946 ? 70  ILE DDD CD1 1 
ATOM   5379  N N   . SER D 4 71  ? -68.393 -32.544 85.819  1.000 271.519 ? 71  SER DDD N   1 
ATOM   5380  C CA  . SER D 4 71  ? -69.322 -32.000 84.804  1.000 270.031 ? 71  SER DDD CA  1 
ATOM   5381  C C   . SER D 4 71  ? -68.665 -30.755 84.215  1.000 268.388 ? 71  SER DDD C   1 
ATOM   5382  O O   . SER D 4 71  ? -67.820 -30.164 84.912  1.000 269.230 ? 71  SER DDD O   1 
ATOM   5383  C CB  . SER D 4 71  ? -70.651 -31.683 85.422  1.000 272.224 ? 71  SER DDD CB  1 
ATOM   5384  O OG  . SER D 4 71  ? -70.497 -30.737 86.472  1.000 274.590 ? 71  SER DDD OG  1 
ATOM   5385  N N   . ARG D 4 72  ? -69.024 -30.381 82.990  1.000 266.023 ? 72  ARG DDD N   1 
ATOM   5386  C CA  . ARG D 4 72  ? -68.426 -29.208 82.307  1.000 265.301 ? 72  ARG DDD CA  1 
ATOM   5387  C C   . ARG D 4 72  ? -69.539 -28.402 81.639  1.000 264.612 ? 72  ARG DDD C   1 
ATOM   5388  O O   . ARG D 4 72  ? -70.564 -28.997 81.261  1.000 262.814 ? 72  ARG DDD O   1 
ATOM   5389  C CB  . ARG D 4 72  ? -67.331 -29.659 81.332  1.000 264.058 ? 72  ARG DDD CB  1 
ATOM   5390  C CG  . ARG D 4 72  ? -67.790 -30.640 80.262  1.000 262.753 ? 72  ARG DDD CG  1 
ATOM   5391  C CD  . ARG D 4 72  ? -68.118 -29.940 78.957  1.000 261.954 ? 72  ARG DDD CD  1 
ATOM   5392  N NE  . ARG D 4 72  ? -68.611 -30.838 77.920  1.000 260.227 ? 72  ARG DDD NE  1 
ATOM   5393  C CZ  . ARG D 4 72  ? -69.863 -31.287 77.830  1.000 260.570 ? 72  ARG DDD CZ  1 
ATOM   5394  N NH1 . ARG D 4 72  ? -70.771 -30.951 78.732  1.000 262.453 ? 72  ARG DDD NH1 1 
ATOM   5395  N NH2 . ARG D 4 72  ? -70.206 -32.086 76.837  1.000 259.186 ? 72  ARG DDD NH2 1 
ATOM   5396  N N   . ASP D 4 73  ? -69.334 -27.088 81.550  1.000 265.322 ? 73  ASP DDD N   1 
ATOM   5397  C CA  . ASP D 4 73  ? -70.207 -26.122 80.836  1.000 266.251 ? 73  ASP DDD CA  1 
ATOM   5398  C C   . ASP D 4 73  ? -69.395 -25.536 79.673  1.000 265.589 ? 73  ASP DDD C   1 
ATOM   5399  O O   . ASP D 4 73  ? -68.535 -24.676 79.936  1.000 267.294 ? 73  ASP DDD O   1 
ATOM   5400  C CB  . ASP D 4 73  ? -70.716 -25.057 81.809  1.000 268.417 ? 73  ASP DDD CB  1 
ATOM   5401  C CG  . ASP D 4 73  ? -71.648 -24.034 81.189  1.000 268.867 ? 73  ASP DDD CG  1 
ATOM   5402  O OD1 . ASP D 4 73  ? -71.926 -24.146 79.976  1.000 266.836 ? 73  ASP DDD OD1 1 
ATOM   5403  O OD2 . ASP D 4 73  ? -72.086 -23.133 81.930  1.000 271.015 ? 73  ASP DDD OD2 1 
ATOM   5404  N N   . LYS D 4 74  ? -69.646 -26.004 78.444  1.000 263.868 ? 74  LYS DDD N   1 
ATOM   5405  C CA  . LYS D 4 74  ? -68.810 -25.710 77.242  1.000 261.630 ? 74  LYS DDD CA  1 
ATOM   5406  C C   . LYS D 4 74  ? -68.835 -24.207 76.931  1.000 262.742 ? 74  LYS DDD C   1 
ATOM   5407  O O   . LYS D 4 74  ? -67.786 -23.676 76.516  1.000 262.855 ? 74  LYS DDD O   1 
ATOM   5408  C CB  . LYS D 4 74  ? -69.281 -26.510 76.022  1.000 258.562 ? 74  LYS DDD CB  1 
ATOM   5409  C CG  . LYS D 4 74  ? -68.904 -27.985 76.027  1.000 256.094 ? 74  LYS DDD CG  1 
ATOM   5410  C CD  . LYS D 4 74  ? -69.286 -28.714 74.753  1.000 253.038 ? 74  LYS DDD CD  1 
ATOM   5411  C CE  . LYS D 4 74  ? -68.266 -28.570 73.645  1.000 250.467 ? 74  LYS DDD CE  1 
ATOM   5412  N NZ  . LYS D 4 74  ? -68.552 -29.482 72.512  1.000 248.121 ? 74  LYS DDD NZ  1 
ATOM   5413  N N   . ALA D 4 75  ? -69.987 -23.556 77.121  1.000 263.592 ? 75  ALA DDD N   1 
ATOM   5414  C CA  . ALA D 4 75  ? -70.200 -22.112 76.861  1.000 264.010 ? 75  ALA DDD CA  1 
ATOM   5415  C C   . ALA D 4 75  ? -69.395 -21.260 77.852  1.000 265.377 ? 75  ALA DDD C   1 
ATOM   5416  O O   . ALA D 4 75  ? -69.018 -20.136 77.472  1.000 264.922 ? 75  ALA DDD O   1 
ATOM   5417  C CB  . ALA D 4 75  ? -71.671 -21.791 76.936  1.000 264.985 ? 75  ALA DDD CB  1 
ATOM   5418  N N   . LYS D 4 76  ? -69.159 -21.768 79.071  1.000 266.772 ? 76  LYS DDD N   1 
ATOM   5419  C CA  . LYS D 4 76  ? -68.418 -21.072 80.164  1.000 268.693 ? 76  LYS DDD CA  1 
ATOM   5420  C C   . LYS D 4 76  ? -66.953 -21.545 80.216  1.000 268.111 ? 76  LYS DDD C   1 
ATOM   5421  O O   . LYS D 4 76  ? -66.191 -20.974 81.019  1.000 269.479 ? 76  LYS DDD O   1 
ATOM   5422  C CB  . LYS D 4 76  ? -69.101 -21.285 81.526  1.000 270.180 ? 76  LYS DDD CB  1 
ATOM   5423  C CG  . LYS D 4 76  ? -70.284 -20.370 81.829  1.000 271.663 ? 76  LYS DDD CG  1 
ATOM   5424  C CD  . LYS D 4 76  ? -70.770 -20.422 83.271  1.000 273.046 ? 76  LYS DDD CD  1 
ATOM   5425  C CE  . LYS D 4 76  ? -71.683 -19.270 83.644  1.000 275.219 ? 76  LYS DDD CE  1 
ATOM   5426  N NZ  . LYS D 4 76  ? -72.688 -18.983 82.593  1.000 275.172 ? 76  LYS DDD NZ  1 
ATOM   5427  N N   . ASN D 4 77  ? -66.565 -22.540 79.407  1.000 266.754 ? 77  ASN DDD N   1 
ATOM   5428  C CA  . ASN D 4 77  ? -65.188 -23.112 79.379  1.000 266.115 ? 77  ASN DDD CA  1 
ATOM   5429  C C   . ASN D 4 77  ? -64.762 -23.480 80.805  1.000 268.777 ? 77  ASN DDD C   1 
ATOM   5430  O O   . ASN D 4 77  ? -63.586 -23.264 81.160  1.000 270.087 ? 77  ASN DDD O   1 
ATOM   5431  C CB  . ASN D 4 77  ? -64.192 -22.143 78.742  1.000 264.818 ? 77  ASN DDD CB  1 
ATOM   5432  C CG  . ASN D 4 77  ? -64.433 -21.971 77.260  1.000 262.818 ? 77  ASN DDD CG  1 
ATOM   5433  O OD1 . ASN D 4 77  ? -64.800 -22.924 76.575  1.000 260.899 ? 77  ASN DDD OD1 1 
ATOM   5434  N ND2 . ASN D 4 77  ? -64.216 -20.770 76.752  1.000 262.720 ? 77  ASN DDD ND2 1 
ATOM   5435  N N   . THR D 4 78  ? -65.701 -24.013 81.587  1.000 270.538 ? 78  THR DDD N   1 
ATOM   5436  C CA  . THR D 4 78  ? -65.516 -24.377 83.011  1.000 271.935 ? 78  THR DDD CA  1 
ATOM   5437  C C   . THR D 4 78  ? -65.736 -25.881 83.159  1.000 271.074 ? 78  THR DDD C   1 
ATOM   5438  O O   . THR D 4 78  ? -66.638 -26.412 82.487  1.000 269.092 ? 78  THR DDD O   1 
ATOM   5439  C CB  . THR D 4 78  ? -66.484 -23.595 83.906  1.000 274.940 ? 78  THR DDD CB  1 
ATOM   5440  O OG1 . THR D 4 78  ? -66.504 -22.238 83.462  1.000 275.751 ? 78  THR DDD OG1 1 
ATOM   5441  C CG2 . THR D 4 78  ? -66.112 -23.663 85.371  1.000 277.060 ? 78  THR DDD CG2 1 
ATOM   5442  N N   . VAL D 4 79  ? -64.922 -26.529 83.990  1.000 272.682 ? 79  VAL DDD N   1 
ATOM   5443  C CA  . VAL D 4 79  ? -65.168 -27.913 84.485  1.000 274.621 ? 79  VAL DDD CA  1 
ATOM   5444  C C   . VAL D 4 79  ? -65.376 -27.820 86.001  1.000 278.436 ? 79  VAL DDD C   1 
ATOM   5445  O O   . VAL D 4 79  ? -64.690 -26.995 86.641  1.000 281.288 ? 79  VAL DDD O   1 
ATOM   5446  C CB  . VAL D 4 79  ? -64.032 -28.878 84.093  1.000 273.383 ? 79  VAL DDD CB  1 
ATOM   5447  C CG1 . VAL D 4 79  ? -62.684 -28.450 84.646  1.000 273.607 ? 79  VAL DDD CG1 1 
ATOM   5448  C CG2 . VAL D 4 79  ? -64.343 -30.309 84.508  1.000 273.662 ? 79  VAL DDD CG2 1 
ATOM   5449  N N   . TYR D 4 80  ? -66.316 -28.607 86.534  1.000 279.560 ? 80  TYR DDD N   1 
ATOM   5450  C CA  . TYR D 4 80  ? -66.735 -28.607 87.962  1.000 281.286 ? 80  TYR DDD CA  1 
ATOM   5451  C C   . TYR D 4 80  ? -66.456 -29.983 88.580  1.000 282.684 ? 80  TYR DDD C   1 
ATOM   5452  O O   . TYR D 4 80  ? -66.663 -30.996 87.878  1.000 280.942 ? 80  TYR DDD O   1 
ATOM   5453  C CB  . TYR D 4 80  ? -68.222 -28.258 88.088  1.000 280.786 ? 80  TYR DDD CB  1 
ATOM   5454  C CG  . TYR D 4 80  ? -68.638 -26.953 87.453  1.000 279.192 ? 80  TYR DDD CG  1 
ATOM   5455  C CD1 . TYR D 4 80  ? -68.322 -25.733 88.032  1.000 279.532 ? 80  TYR DDD CD1 1 
ATOM   5456  C CD2 . TYR D 4 80  ? -69.362 -26.932 86.271  1.000 276.665 ? 80  TYR DDD CD2 1 
ATOM   5457  C CE1 . TYR D 4 80  ? -68.705 -24.533 87.449  1.000 278.745 ? 80  TYR DDD CE1 1 
ATOM   5458  C CE2 . TYR D 4 80  ? -69.754 -25.743 85.677  1.000 275.644 ? 80  TYR DDD CE2 1 
ATOM   5459  C CZ  . TYR D 4 80  ? -69.424 -24.536 86.264  1.000 276.756 ? 80  TYR DDD CZ  1 
ATOM   5460  O OH  . TYR D 4 80  ? -69.821 -23.376 85.660  1.000 275.155 ? 80  TYR DDD OH  1 
ATOM   5461  N N   . LEU D 4 81  ? -65.993 -30.014 89.838  1.000 286.062 ? 81  LEU DDD N   1 
ATOM   5462  C CA  . LEU D 4 81  ? -65.962 -31.235 90.690  1.000 287.299 ? 81  LEU DDD CA  1 
ATOM   5463  C C   . LEU D 4 81  ? -66.923 -31.032 91.870  1.000 291.019 ? 81  LEU DDD C   1 
ATOM   5464  O O   . LEU D 4 81  ? -66.618 -30.195 92.752  1.000 293.994 ? 81  LEU DDD O   1 
ATOM   5465  C CB  . LEU D 4 81  ? -64.533 -31.519 91.170  1.000 285.947 ? 81  LEU DDD CB  1 
ATOM   5466  C CG  . LEU D 4 81  ? -64.326 -32.876 91.844  1.000 284.901 ? 81  LEU DDD CG  1 
ATOM   5467  C CD1 . LEU D 4 81  ? -64.543 -34.017 90.862  1.000 282.926 ? 81  LEU DDD CD1 1 
ATOM   5468  C CD2 . LEU D 4 81  ? -62.940 -32.976 92.459  1.000 284.095 ? 81  LEU DDD CD2 1 
ATOM   5469  N N   . GLN D 4 82  ? -68.062 -31.737 91.855  1.000 291.511 ? 82  GLN DDD N   1 
ATOM   5470  C CA  . GLN D 4 82  ? -69.008 -31.831 93.000  1.000 293.365 ? 82  GLN DDD CA  1 
ATOM   5471  C C   . GLN D 4 82  ? -68.486 -32.921 93.938  1.000 295.351 ? 82  GLN DDD C   1 
ATOM   5472  O O   . GLN D 4 82  ? -68.296 -34.053 93.462  1.000 293.840 ? 82  GLN DDD O   1 
ATOM   5473  C CB  . GLN D 4 82  ? -70.430 -32.143 92.524  1.000 291.457 ? 82  GLN DDD CB  1 
ATOM   5474  C CG  . GLN D 4 82  ? -71.490 -31.867 93.580  1.000 292.099 ? 82  GLN DDD CG  1 
ATOM   5475  C CD  . GLN D 4 82  ? -71.420 -30.440 94.067  1.000 292.131 ? 82  GLN DDD CD  1 
ATOM   5476  O OE1 . GLN D 4 82  ? -71.525 -29.490 93.295  1.000 289.907 ? 82  GLN DDD OE1 1 
ATOM   5477  N NE2 . GLN D 4 82  ? -71.207 -30.276 95.361  1.000 293.154 ? 82  GLN DDD NE2 1 
ATOM   5478  N N   . MET D 4 83  ? -68.229 -32.581 95.202  1.000 298.927 ? 83  MET DDD N   1 
ATOM   5479  C CA  . MET D 4 83  ? -67.626 -33.509 96.192  1.000 300.866 ? 83  MET DDD CA  1 
ATOM   5480  C C   . MET D 4 83  ? -68.634 -33.760 97.317  1.000 304.088 ? 83  MET DDD C   1 
ATOM   5481  O O   . MET D 4 83  ? -68.573 -33.060 98.346  1.000 306.441 ? 83  MET DDD O   1 
ATOM   5482  C CB  . MET D 4 83  ? -66.323 -32.936 96.754  1.000 302.126 ? 83  MET DDD CB  1 
ATOM   5483  C CG  . MET D 4 83  ? -65.291 -32.658 95.680  1.000 300.656 ? 83  MET DDD CG  1 
ATOM   5484  S SD  . MET D 4 83  ? -63.869 -31.721 96.296  1.000 302.110 ? 83  MET DDD SD  1 
ATOM   5485  C CE  . MET D 4 83  ? -63.054 -32.948 97.315  1.000 302.742 ? 83  MET DDD CE  1 
ATOM   5486  N N   . ASN D 4 84  ? -69.537 -34.721 97.102  1.000 304.999 ? 84  ASN DDD N   1 
ATOM   5487  C CA  . ASN D 4 84  ? -70.553 -35.161 98.095  1.000 307.125 ? 84  ASN DDD CA  1 
ATOM   5488  C C   . ASN D 4 84  ? -69.865 -36.097 99.099  1.000 306.766 ? 84  ASN DDD C   1 
ATOM   5489  O O   . ASN D 4 84  ? -68.801 -36.655 98.749  1.000 306.647 ? 84  ASN DDD O   1 
ATOM   5490  C CB  . ASN D 4 84  ? -71.758 -35.835 97.421  1.000 307.122 ? 84  ASN DDD CB  1 
ATOM   5491  C CG  . ASN D 4 84  ? -72.330 -35.047 96.259  1.000 306.187 ? 84  ASN DDD CG  1 
ATOM   5492  O OD1 . ASN D 4 84  ? -72.563 -33.845 96.375  1.000 307.589 ? 84  ASN DDD OD1 1 
ATOM   5493  N ND2 . ASN D 4 84  ? -72.574 -35.709 95.137  1.000 303.739 ? 84  ASN DDD ND2 1 
ATOM   5494  N N   . SER D 4 85  ? -70.437 -36.241 100.300 1.000 306.467 ? 85  SER DDD N   1 
ATOM   5495  C CA  . SER D 4 85  ? -70.054 -37.236 101.341 1.000 305.773 ? 85  SER DDD CA  1 
ATOM   5496  C C   . SER D 4 85  ? -68.555 -37.162 101.673 1.000 304.770 ? 85  SER DDD C   1 
ATOM   5497  O O   . SER D 4 85  ? -67.946 -38.244 101.826 1.000 304.654 ? 85  SER DDD O   1 
ATOM   5498  C CB  . SER D 4 85  ? -70.422 -38.634 100.902 1.000 303.601 ? 85  SER DDD CB  1 
ATOM   5499  O OG  . SER D 4 85  ? -71.800 -38.727 100.577 1.000 302.807 ? 85  SER DDD OG  1 
ATOM   5500  N N   . LEU D 4 86  ? -67.982 -35.957 101.806 1.000 303.659 ? 86  LEU DDD N   1 
ATOM   5501  C CA  . LEU D 4 86  ? -66.504 -35.785 101.941 1.000 300.873 ? 86  LEU DDD CA  1 
ATOM   5502  C C   . LEU D 4 86  ? -65.997 -36.710 103.063 1.000 301.106 ? 86  LEU DDD C   1 
ATOM   5503  O O   . LEU D 4 86  ? -66.608 -36.718 104.159 1.000 305.010 ? 86  LEU DDD O   1 
ATOM   5504  C CB  . LEU D 4 86  ? -66.097 -34.329 102.227 1.000 300.657 ? 86  LEU DDD CB  1 
ATOM   5505  C CG  . LEU D 4 86  ? -66.658 -33.237 101.315 1.000 298.729 ? 86  LEU DDD CG  1 
ATOM   5506  C CD1 . LEU D 4 86  ? -67.984 -32.734 101.843 1.000 300.705 ? 86  LEU DDD CD1 1 
ATOM   5507  C CD2 . LEU D 4 86  ? -65.686 -32.072 101.186 1.000 297.427 ? 86  LEU DDD CD2 1 
ATOM   5508  N N   . LYS D 4 87  ? -64.937 -37.474 102.774 1.000 296.332 ? 87  LYS DDD N   1 
ATOM   5509  C CA  . LYS D 4 87  ? -64.164 -38.310 103.735 1.000 294.207 ? 87  LYS DDD CA  1 
ATOM   5510  C C   . LYS D 4 87  ? -62.982 -37.481 104.257 1.000 294.120 ? 87  LYS DDD C   1 
ATOM   5511  O O   . LYS D 4 87  ? -62.711 -36.431 103.649 1.000 294.285 ? 87  LYS DDD O   1 
ATOM   5512  C CB  . LYS D 4 87  ? -63.633 -39.572 103.044 1.000 289.787 ? 87  LYS DDD CB  1 
ATOM   5513  C CG  . LYS D 4 87  ? -64.614 -40.722 102.861 1.000 287.639 ? 87  LYS DDD CG  1 
ATOM   5514  C CD  . LYS D 4 87  ? -63.900 -42.041 102.674 1.000 285.029 ? 87  LYS DDD CD  1 
ATOM   5515  C CE  . LYS D 4 87  ? -64.606 -42.992 101.735 1.000 282.906 ? 87  LYS DDD CE  1 
ATOM   5516  N NZ  . LYS D 4 87  ? -63.670 -44.029 101.249 1.000 280.881 ? 87  LYS DDD NZ  1 
ATOM   5517  N N   . TYR D 4 88  ? -62.293 -37.941 105.312 1.000 293.617 ? 88  TYR DDD N   1 
ATOM   5518  C CA  . TYR D 4 88  ? -61.068 -37.300 105.869 1.000 292.268 ? 88  TYR DDD CA  1 
ATOM   5519  C C   . TYR D 4 88  ? -59.892 -37.448 104.888 1.000 291.918 ? 88  TYR DDD C   1 
ATOM   5520  O O   . TYR D 4 88  ? -58.990 -36.584 104.916 1.000 292.261 ? 88  TYR DDD O   1 
ATOM   5521  C CB  . TYR D 4 88  ? -60.712 -37.870 107.247 1.000 290.586 ? 88  TYR DDD CB  1 
ATOM   5522  C CG  . TYR D 4 88  ? -61.412 -37.227 108.418 1.000 290.073 ? 88  TYR DDD CG  1 
ATOM   5523  C CD1 . TYR D 4 88  ? -61.520 -35.850 108.529 1.000 289.239 ? 88  TYR DDD CD1 1 
ATOM   5524  C CD2 . TYR D 4 88  ? -61.935 -38.001 109.440 1.000 290.317 ? 88  TYR DDD CD2 1 
ATOM   5525  C CE1 . TYR D 4 88  ? -62.151 -35.262 109.612 1.000 291.139 ? 88  TYR DDD CE1 1 
ATOM   5526  C CE2 . TYR D 4 88  ? -62.565 -37.429 110.531 1.000 292.232 ? 88  TYR DDD CE2 1 
ATOM   5527  C CZ  . TYR D 4 88  ? -62.672 -36.056 110.617 1.000 292.782 ? 88  TYR DDD CZ  1 
ATOM   5528  O OH  . TYR D 4 88  ? -63.296 -35.514 111.701 1.000 295.141 ? 88  TYR DDD OH  1 
ATOM   5529  N N   . GLU D 4 89  ? -59.895 -38.502 104.055 1.000 291.817 ? 89  GLU DDD N   1 
ATOM   5530  C CA  . GLU D 4 89  ? -58.844 -38.789 103.032 1.000 290.057 ? 89  GLU DDD CA  1 
ATOM   5531  C C   . GLU D 4 89  ? -58.934 -37.803 101.863 1.000 290.721 ? 89  GLU DDD C   1 
ATOM   5532  O O   . GLU D 4 89  ? -57.982 -37.775 101.062 1.000 288.931 ? 89  GLU DDD O   1 
ATOM   5533  C CB  . GLU D 4 89  ? -58.967 -40.216 102.489 1.000 287.291 ? 89  GLU DDD CB  1 
ATOM   5534  C CG  . GLU D 4 89  ? -58.061 -41.224 103.178 1.000 286.740 ? 89  GLU DDD CG  1 
ATOM   5535  C CD  . GLU D 4 89  ? -58.110 -41.237 104.697 1.000 289.247 ? 89  GLU DDD CD  1 
ATOM   5536  O OE1 . GLU D 4 89  ? -57.092 -41.615 105.313 1.000 289.621 ? 89  GLU DDD OE1 1 
ATOM   5537  O OE2 . GLU D 4 89  ? -59.164 -40.882 105.264 1.000 290.996 ? 89  GLU DDD OE2 1 
ATOM   5538  N N   . ASP D 4 90  ? -60.037 -37.054 101.753 1.000 294.057 ? 90  ASP DDD N   1 
ATOM   5539  C CA  . ASP D 4 90  ? -60.265 -36.046 100.680 1.000 293.844 ? 90  ASP DDD CA  1 
ATOM   5540  C C   . ASP D 4 90  ? -59.473 -34.761 100.958 1.000 293.854 ? 90  ASP DDD C   1 
ATOM   5541  O O   . ASP D 4 90  ? -59.414 -33.927 100.042 1.000 292.836 ? 90  ASP DDD O   1 
ATOM   5542  C CB  . ASP D 4 90  ? -61.750 -35.702 100.526 1.000 295.900 ? 90  ASP DDD CB  1 
ATOM   5543  C CG  . ASP D 4 90  ? -62.609 -36.858 100.051 1.000 296.381 ? 90  ASP DDD CG  1 
ATOM   5544  O OD1 . ASP D 4 90  ? -62.036 -37.893 99.646  1.000 296.247 ? 90  ASP DDD OD1 1 
ATOM   5545  O OD2 . ASP D 4 90  ? -63.847 -36.715 100.090 1.000 298.453 ? 90  ASP DDD OD2 1 
ATOM   5546  N N   . THR D 4 91  ? -58.908 -34.588 102.162 1.000 294.550 ? 91  THR DDD N   1 
ATOM   5547  C CA  . THR D 4 91  ? -58.037 -33.429 102.503 1.000 294.292 ? 91  THR DDD CA  1 
ATOM   5548  C C   . THR D 4 91  ? -56.791 -33.469 101.614 1.000 292.380 ? 91  THR DDD C   1 
ATOM   5549  O O   . THR D 4 91  ? -55.957 -34.372 101.817 1.000 291.445 ? 91  THR DDD O   1 
ATOM   5550  C CB  . THR D 4 91  ? -57.592 -33.407 103.971 1.000 295.228 ? 91  THR DDD CB  1 
ATOM   5551  O OG1 . THR D 4 91  ? -58.716 -33.124 104.804 1.000 296.623 ? 91  THR DDD OG1 1 
ATOM   5552  C CG2 . THR D 4 91  ? -56.531 -32.362 104.243 1.000 295.036 ? 91  THR DDD CG2 1 
ATOM   5553  N N   . ALA D 4 92  ? -56.664 -32.516 100.689 1.000 291.824 ? 92  ALA DDD N   1 
ATOM   5554  C CA  . ALA D 4 92  ? -55.586 -32.474 99.674  1.000 290.464 ? 92  ALA DDD CA  1 
ATOM   5555  C C   . ALA D 4 92  ? -55.591 -31.121 98.958  1.000 290.817 ? 92  ALA DDD C   1 
ATOM   5556  O O   . ALA D 4 92  ? -56.459 -30.276 99.276  1.000 292.147 ? 92  ALA DDD O   1 
ATOM   5557  C CB  . ALA D 4 92  ? -55.780 -33.603 98.688  1.000 288.600 ? 92  ALA DDD CB  1 
ATOM   5558  N N   . VAL D 4 93  ? -54.647 -30.936 98.029  1.000 289.952 ? 93  VAL DDD N   1 
ATOM   5559  C CA  . VAL D 4 93  ? -54.672 -29.845 97.012  1.000 288.790 ? 93  VAL DDD CA  1 
ATOM   5560  C C   . VAL D 4 93  ? -55.190 -30.434 95.699  1.000 286.802 ? 93  VAL DDD C   1 
ATOM   5561  O O   . VAL D 4 93  ? -54.521 -31.332 95.151  1.000 283.955 ? 93  VAL DDD O   1 
ATOM   5562  C CB  . VAL D 4 93  ? -53.291 -29.200 96.817  1.000 287.535 ? 93  VAL DDD CB  1 
ATOM   5563  C CG1 . VAL D 4 93  ? -53.330 -28.134 95.735  1.000 285.627 ? 93  VAL DDD CG1 1 
ATOM   5564  C CG2 . VAL D 4 93  ? -52.748 -28.627 98.116  1.000 289.553 ? 93  VAL DDD CG2 1 
ATOM   5565  N N   . TYR D 4 94  ? -56.328 -29.925 95.220  1.000 287.714 ? 94  TYR DDD N   1 
ATOM   5566  C CA  . TYR D 4 94  ? -57.016 -30.387 93.988  1.000 286.530 ? 94  TYR DDD CA  1 
ATOM   5567  C C   . TYR D 4 94  ? -56.520 -29.550 92.804  1.000 285.027 ? 94  TYR DDD C   1 
ATOM   5568  O O   . TYR D 4 94  ? -56.670 -28.308 92.823  1.000 286.257 ? 94  TYR DDD O   1 
ATOM   5569  C CB  . TYR D 4 94  ? -58.534 -30.370 94.198  1.000 287.857 ? 94  TYR DDD CB  1 
ATOM   5570  C CG  . TYR D 4 94  ? -58.997 -31.496 95.085  1.000 288.667 ? 94  TYR DDD CG  1 
ATOM   5571  C CD1 . TYR D 4 94  ? -58.722 -31.489 96.442  1.000 290.794 ? 94  TYR DDD CD1 1 
ATOM   5572  C CD2 . TYR D 4 94  ? -59.645 -32.602 94.561  1.000 287.614 ? 94  TYR DDD CD2 1 
ATOM   5573  C CE1 . TYR D 4 94  ? -59.107 -32.537 97.262  1.000 292.090 ? 94  TYR DDD CE1 1 
ATOM   5574  C CE2 . TYR D 4 94  ? -60.040 -33.658 95.368  1.000 288.385 ? 94  TYR DDD CE2 1 
ATOM   5575  C CZ  . TYR D 4 94  ? -59.770 -33.626 96.723  1.000 290.787 ? 94  TYR DDD CZ  1 
ATOM   5576  O OH  . TYR D 4 94  ? -60.155 -34.666 97.520  1.000 292.447 ? 94  TYR DDD OH  1 
ATOM   5577  N N   . TYR D 4 95  ? -55.914 -30.233 91.826  1.000 282.213 ? 95  TYR DDD N   1 
ATOM   5578  C CA  . TYR D 4 95  ? -55.377 -29.673 90.559  1.000 279.446 ? 95  TYR DDD CA  1 
ATOM   5579  C C   . TYR D 4 95  ? -56.259 -30.113 89.387  1.000 277.357 ? 95  TYR DDD C   1 
ATOM   5580  O O   . TYR D 4 95  ? -56.381 -31.336 89.154  1.000 275.536 ? 95  TYR DDD O   1 
ATOM   5581  C CB  . TYR D 4 95  ? -53.953 -30.172 90.295  1.000 277.700 ? 95  TYR DDD CB  1 
ATOM   5582  C CG  . TYR D 4 95  ? -52.927 -29.825 91.345  1.000 278.480 ? 95  TYR DDD CG  1 
ATOM   5583  C CD1 . TYR D 4 95  ? -52.224 -28.632 91.292  1.000 277.997 ? 95  TYR DDD CD1 1 
ATOM   5584  C CD2 . TYR D 4 95  ? -52.635 -30.701 92.378  1.000 278.958 ? 95  TYR DDD CD2 1 
ATOM   5585  C CE1 . TYR D 4 95  ? -51.270 -28.314 92.246  1.000 278.259 ? 95  TYR DDD CE1 1 
ATOM   5586  C CE2 . TYR D 4 95  ? -51.687 -30.397 93.341  1.000 278.795 ? 95  TYR DDD CE2 1 
ATOM   5587  C CZ  . TYR D 4 95  ? -51.004 -29.197 93.277  1.000 278.503 ? 95  TYR DDD CZ  1 
ATOM   5588  O OH  . TYR D 4 95  ? -50.066 -28.892 94.217  1.000 278.116 ? 95  TYR DDD OH  1 
ATOM   5589  N N   . CYS D 4 96  ? -56.843 -29.154 88.663  1.000 276.855 ? 96  CYS DDD N   1 
ATOM   5590  C CA  . CYS D 4 96  ? -57.480 -29.392 87.342  1.000 274.814 ? 96  CYS DDD CA  1 
ATOM   5591  C C   . CYS D 4 96  ? -56.381 -29.370 86.273  1.000 273.673 ? 96  CYS DDD C   1 
ATOM   5592  O O   . CYS D 4 96  ? -55.401 -28.601 86.427  1.000 273.574 ? 96  CYS DDD O   1 
ATOM   5593  C CB  . CYS D 4 96  ? -58.579 -28.383 87.027  1.000 274.712 ? 96  CYS DDD CB  1 
ATOM   5594  S SG  . CYS D 4 96  ? -57.959 -26.839 86.309  1.000 273.898 ? 96  CYS DDD SG  1 
ATOM   5595  N N   . ALA D 4 97  ? -56.543 -30.204 85.245  1.000 272.642 ? 97  ALA DDD N   1 
ATOM   5596  C CA  . ALA D 4 97  ? -55.570 -30.442 84.155  1.000 269.816 ? 97  ALA DDD CA  1 
ATOM   5597  C C   . ALA D 4 97  ? -56.330 -30.516 82.823  1.000 266.980 ? 97  ALA DDD C   1 
ATOM   5598  O O   . ALA D 4 97  ? -57.485 -30.997 82.817  1.000 266.502 ? 97  ALA DDD O   1 
ATOM   5599  C CB  . ALA D 4 97  ? -54.788 -31.705 84.440  1.000 269.418 ? 97  ALA DDD CB  1 
ATOM   5600  N N   . ARG D 4 98  ? -55.709 -30.034 81.745  1.000 263.955 ? 98  ARG DDD N   1 
ATOM   5601  C CA  . ARG D 4 98  ? -56.296 -29.984 80.381  1.000 261.037 ? 98  ARG DDD CA  1 
ATOM   5602  C C   . ARG D 4 98  ? -55.353 -30.707 79.419  1.000 258.056 ? 98  ARG DDD C   1 
ATOM   5603  O O   . ARG D 4 98  ? -54.135 -30.483 79.525  1.000 258.284 ? 98  ARG DDD O   1 
ATOM   5604  C CB  . ARG D 4 98  ? -56.498 -28.528 79.950  1.000 261.096 ? 98  ARG DDD CB  1 
ATOM   5605  C CG  . ARG D 4 98  ? -57.027 -28.355 78.534  1.000 259.561 ? 98  ARG DDD CG  1 
ATOM   5606  C CD  . ARG D 4 98  ? -57.397 -26.911 78.249  1.000 260.234 ? 98  ARG DDD CD  1 
ATOM   5607  N NE  . ARG D 4 98  ? -57.799 -26.689 76.865  1.000 259.138 ? 98  ARG DDD NE  1 
ATOM   5608  C CZ  . ARG D 4 98  ? -56.964 -26.534 75.837  1.000 258.130 ? 98  ARG DDD CZ  1 
ATOM   5609  N NH1 . ARG D 4 98  ? -55.656 -26.598 76.011  1.000 257.758 ? 98  ARG DDD NH1 1 
ATOM   5610  N NH2 . ARG D 4 98  ? -57.445 -26.329 74.623  1.000 257.513 ? 98  ARG DDD NH2 1 
ATOM   5611  N N   . THR D 4 99  ? -55.897 -31.534 78.524  1.000 255.508 ? 99  THR DDD N   1 
ATOM   5612  C CA  . THR D 4 99  ? -55.145 -32.199 77.426  1.000 252.256 ? 99  THR DDD CA  1 
ATOM   5613  C C   . THR D 4 99  ? -55.864 -31.924 76.103  1.000 249.284 ? 99  THR DDD C   1 
ATOM   5614  O O   . THR D 4 99  ? -57.110 -31.910 76.096  1.000 250.498 ? 99  THR DDD O   1 
ATOM   5615  C CB  . THR D 4 99  ? -54.946 -33.696 77.697  1.000 251.840 ? 99  THR DDD CB  1 
ATOM   5616  O OG1 . THR D 4 99  ? -54.140 -34.203 76.635  1.000 249.777 ? 99  THR DDD OG1 1 
ATOM   5617  C CG2 . THR D 4 99  ? -56.241 -34.474 77.803  1.000 252.377 ? 99  THR DDD CG2 1 
ATOM   5618  N N   . GLU D 4 100 ? -55.096 -31.691 75.039  1.000 244.812 ? 100 GLU DDD N   1 
ATOM   5619  C CA  . GLU D 4 100 ? -55.629 -31.502 73.667  1.000 241.926 ? 100 GLU DDD CA  1 
ATOM   5620  C C   . GLU D 4 100 ? -55.666 -32.862 72.955  1.000 238.228 ? 100 GLU DDD C   1 
ATOM   5621  O O   . GLU D 4 100 ? -56.187 -32.911 71.831  1.000 237.282 ? 100 GLU DDD O   1 
ATOM   5622  C CB  . GLU D 4 100 ? -54.789 -30.464 72.917  1.000 242.168 ? 100 GLU DDD CB  1 
ATOM   5623  C CG  . GLU D 4 100 ? -54.871 -29.060 73.511  1.000 244.025 ? 100 GLU DDD CG  1 
ATOM   5624  C CD  . GLU D 4 100 ? -54.278 -27.934 72.669  1.000 244.107 ? 100 GLU DDD CD  1 
ATOM   5625  O OE1 . GLU D 4 100 ? -53.880 -28.194 71.516  1.000 242.919 ? 100 GLU DDD OE1 1 
ATOM   5626  O OE2 . GLU D 4 100 ? -54.229 -26.785 73.161  1.000 245.270 ? 100 GLU DDD OE2 1 
ATOM   5627  N N   . ASN D 4 101 ? -55.155 -33.924 73.593  1.000 235.595 ? 101 ASN DDD N   1 
ATOM   5628  C CA  . ASN D 4 101 ? -55.047 -35.295 73.023  1.000 233.043 ? 101 ASN DDD CA  1 
ATOM   5629  C C   . ASN D 4 101 ? -56.413 -35.987 73.090  1.000 232.658 ? 101 ASN DDD C   1 
ATOM   5630  O O   . ASN D 4 101 ? -56.839 -36.344 74.195  1.000 232.854 ? 101 ASN DDD O   1 
ATOM   5631  C CB  . ASN D 4 101 ? -53.963 -36.110 73.738  1.000 232.344 ? 101 ASN DDD CB  1 
ATOM   5632  C CG  . ASN D 4 101 ? -53.669 -37.454 73.103  1.000 230.365 ? 101 ASN DDD CG  1 
ATOM   5633  O OD1 . ASN D 4 101 ? -54.381 -37.900 72.211  1.000 229.324 ? 101 ASN DDD OD1 1 
ATOM   5634  N ND2 . ASN D 4 101 ? -52.616 -38.112 73.558  1.000 229.473 ? 101 ASN DDD ND2 1 
ATOM   5635  N N   . VAL D 4 102 ? -57.059 -36.176 71.937  1.000 231.743 ? 102 VAL DDD N   1 
ATOM   5636  C CA  . VAL D 4 102 ? -58.344 -36.923 71.789  1.000 231.397 ? 102 VAL DDD CA  1 
ATOM   5637  C C   . VAL D 4 102 ? -58.043 -38.423 71.806  1.000 230.181 ? 102 VAL DDD C   1 
ATOM   5638  O O   . VAL D 4 102 ? -57.362 -38.883 70.871  1.000 229.748 ? 102 VAL DDD O   1 
ATOM   5639  C CB  . VAL D 4 102 ? -59.058 -36.544 70.479  1.000 230.731 ? 102 VAL DDD CB  1 
ATOM   5640  C CG1 . VAL D 4 102 ? -60.317 -37.372 70.269  1.000 230.826 ? 102 VAL DDD CG1 1 
ATOM   5641  C CG2 . VAL D 4 102 ? -59.367 -35.058 70.412  1.000 231.458 ? 102 VAL DDD CG2 1 
ATOM   5642  N N   . ARG D 4 103 ? -58.569 -39.157 72.789  1.000 229.712 ? 103 ARG DDD N   1 
ATOM   5643  C CA  . ARG D 4 103 ? -58.318 -40.613 72.959  1.000 228.789 ? 103 ARG DDD CA  1 
ATOM   5644  C C   . ARG D 4 103 ? -59.657 -41.351 72.911  1.000 230.358 ? 103 ARG DDD C   1 
ATOM   5645  O O   . ARG D 4 103 ? -60.533 -41.017 73.722  1.000 230.868 ? 103 ARG DDD O   1 
ATOM   5646  C CB  . ARG D 4 103 ? -57.572 -40.857 74.271  1.000 228.035 ? 103 ARG DDD CB  1 
ATOM   5647  C CG  . ARG D 4 103 ? -56.254 -40.104 74.368  1.000 227.185 ? 103 ARG DDD CG  1 
ATOM   5648  C CD  . ARG D 4 103 ? -55.195 -40.751 73.504  1.000 225.288 ? 103 ARG DDD CD  1 
ATOM   5649  N NE  . ARG D 4 103 ? -55.034 -42.146 73.880  1.000 224.678 ? 103 ARG DDD NE  1 
ATOM   5650  C CZ  . ARG D 4 103 ? -54.751 -43.146 73.048  1.000 223.537 ? 103 ARG DDD CZ  1 
ATOM   5651  N NH1 . ARG D 4 103 ? -54.596 -42.932 71.754  1.000 222.448 ? 103 ARG DDD NH1 1 
ATOM   5652  N NH2 . ARG D 4 103 ? -54.605 -44.378 73.522  1.000 224.014 ? 103 ARG DDD NH2 1 
ATOM   5653  N N   . SER D 4 104 ? -59.804 -42.299 71.981  1.000 210.325 ? 104 SER DDD N   1 
ATOM   5654  C CA  . SER D 4 104 ? -61.053 -43.071 71.735  1.000 213.392 ? 104 SER DDD CA  1 
ATOM   5655  C C   . SER D 4 104 ? -61.487 -43.756 73.029  1.000 214.921 ? 104 SER DDD C   1 
ATOM   5656  O O   . SER D 4 104 ? -62.620 -43.508 73.490  1.000 216.069 ? 104 SER DDD O   1 
ATOM   5657  C CB  . SER D 4 104 ? -60.876 -44.084 70.631  1.000 213.928 ? 104 SER DDD CB  1 
ATOM   5658  O OG  . SER D 4 104 ? -61.896 -45.073 70.684  1.000 214.270 ? 104 SER DDD OG  1 
ATOM   5659  N N   . LEU D 4 105 ? -60.615 -44.609 73.565  1.000 216.456 ? 105 LEU DDD N   1 
ATOM   5660  C CA  . LEU D 4 105 ? -60.793 -45.241 74.893  1.000 218.033 ? 105 LEU DDD CA  1 
ATOM   5661  C C   . LEU D 4 105 ? -60.813 -44.124 75.941  1.000 220.483 ? 105 LEU DDD C   1 
ATOM   5662  O O   . LEU D 4 105 ? -59.798 -43.410 76.030  1.000 222.732 ? 105 LEU DDD O   1 
ATOM   5663  C CB  . LEU D 4 105 ? -59.629 -46.206 75.130  1.000 217.079 ? 105 LEU DDD CB  1 
ATOM   5664  C CG  . LEU D 4 105 ? -59.699 -46.996 76.432  1.000 216.337 ? 105 LEU DDD CG  1 
ATOM   5665  C CD1 . LEU D 4 105 ? -60.859 -47.977 76.396  1.000 216.309 ? 105 LEU DDD CD1 1 
ATOM   5666  C CD2 . LEU D 4 105 ? -58.388 -47.718 76.700  1.000 215.469 ? 105 LEU DDD CD2 1 
ATOM   5667  N N   . LEU D 4 106 ? -61.920 -43.962 76.680  1.000 221.321 ? 106 LEU DDD N   1 
ATOM   5668  C CA  . LEU D 4 106 ? -62.083 -42.901 77.720  1.000 220.616 ? 106 LEU DDD CA  1 
ATOM   5669  C C   . LEU D 4 106 ? -61.141 -43.188 78.901  1.000 218.876 ? 106 LEU DDD C   1 
ATOM   5670  O O   . LEU D 4 106 ? -60.454 -42.245 79.359  1.000 217.715 ? 106 LEU DDD O   1 
ATOM   5671  C CB  . LEU D 4 106 ? -63.549 -42.841 78.171  1.000 221.351 ? 106 LEU DDD CB  1 
ATOM   5672  C CG  . LEU D 4 106 ? -63.863 -41.880 79.322  1.000 221.538 ? 106 LEU DDD CG  1 
ATOM   5673  C CD1 . LEU D 4 106 ? -63.230 -40.513 79.108  1.000 221.312 ? 106 LEU DDD CD1 1 
ATOM   5674  C CD2 . LEU D 4 106 ? -65.368 -41.729 79.525  1.000 222.582 ? 106 LEU DDD CD2 1 
ATOM   5675  N N   . SER D 4 107 ? -61.085 -44.451 79.344  1.000 217.396 ? 107 SER DDD N   1 
ATOM   5676  C CA  . SER D 4 107 ? -60.352 -44.914 80.553  1.000 216.851 ? 107 SER DDD CA  1 
ATOM   5677  C C   . SER D 4 107 ? -58.890 -44.446 80.518  1.000 218.255 ? 107 SER DDD C   1 
ATOM   5678  O O   . SER D 4 107 ? -58.288 -44.324 81.601  1.000 219.111 ? 107 SER DDD O   1 
ATOM   5679  C CB  . SER D 4 107 ? -60.463 -46.412 80.725  1.000 214.748 ? 107 SER DDD CB  1 
ATOM   5680  O OG  . SER D 4 107 ? -59.702 -47.109 79.754  1.000 212.559 ? 107 SER DDD OG  1 
ATOM   5681  N N   . ASP D 4 108 ? -58.356 -44.177 79.322  1.000 220.285 ? 108 ASP DDD N   1 
ATOM   5682  C CA  . ASP D 4 108 ? -56.971 -43.688 79.082  1.000 221.713 ? 108 ASP DDD CA  1 
ATOM   5683  C C   . ASP D 4 108 ? -56.659 -42.410 79.863  1.000 221.993 ? 108 ASP DDD C   1 
ATOM   5684  O O   . ASP D 4 108 ? -55.460 -42.142 80.059  1.000 222.727 ? 108 ASP DDD O   1 
ATOM   5685  C CB  . ASP D 4 108 ? -56.732 -43.355 77.609  1.000 223.565 ? 108 ASP DDD CB  1 
ATOM   5686  C CG  . ASP D 4 108 ? -56.218 -44.515 76.781  1.000 224.394 ? 108 ASP DDD CG  1 
ATOM   5687  O OD1 . ASP D 4 108 ? -55.881 -45.559 77.375  1.000 224.415 ? 108 ASP DDD OD1 1 
ATOM   5688  O OD2 . ASP D 4 108 ? -56.156 -44.355 75.546  1.000 226.340 ? 108 ASP DDD OD2 1 
ATOM   5689  N N   . TYR D 4 109 ? -57.662 -41.625 80.258  1.000 221.888 ? 109 TYR DDD N   1 
ATOM   5690  C CA  . TYR D 4 109 ? -57.440 -40.274 80.837  1.000 221.836 ? 109 TYR DDD CA  1 
ATOM   5691  C C   . TYR D 4 109 ? -57.025 -40.365 82.316  1.000 220.186 ? 109 TYR DDD C   1 
ATOM   5692  O O   . TYR D 4 109 ? -57.015 -39.327 82.999  1.000 219.279 ? 109 TYR DDD O   1 
ATOM   5693  C CB  . TYR D 4 109 ? -58.664 -39.390 80.577  1.000 223.277 ? 109 TYR DDD CB  1 
ATOM   5694  C CG  . TYR D 4 109 ? -58.743 -38.858 79.170  1.000 223.880 ? 109 TYR DDD CG  1 
ATOM   5695  C CD1 . TYR D 4 109 ? -57.673 -38.189 78.599  1.000 224.824 ? 109 TYR DDD CD1 1 
ATOM   5696  C CD2 . TYR D 4 109 ? -59.887 -39.012 78.407  1.000 224.879 ? 109 TYR DDD CD2 1 
ATOM   5697  C CE1 . TYR D 4 109 ? -57.731 -37.702 77.303  1.000 227.032 ? 109 TYR DDD CE1 1 
ATOM   5698  C CE2 . TYR D 4 109 ? -59.964 -38.529 77.110  1.000 227.432 ? 109 TYR DDD CE2 1 
ATOM   5699  C CZ  . TYR D 4 109 ? -58.881 -37.872 76.551  1.000 228.337 ? 109 TYR DDD CZ  1 
ATOM   5700  O OH  . TYR D 4 109 ? -58.948 -37.397 75.268  1.000 229.702 ? 109 TYR DDD OH  1 
ATOM   5701  N N   . ALA D 4 110 ? -56.666 -41.556 82.799  1.000 218.699 ? 110 ALA DDD N   1 
ATOM   5702  C CA  . ALA D 4 110 ? -55.875 -41.746 84.035  1.000 218.342 ? 110 ALA DDD CA  1 
ATOM   5703  C C   . ALA D 4 110 ? -54.408 -41.966 83.638  1.000 218.087 ? 110 ALA DDD C   1 
ATOM   5704  O O   . ALA D 4 110 ? -53.587 -41.082 83.950  1.000 217.991 ? 110 ALA DDD O   1 
ATOM   5705  C CB  . ALA D 4 110 ? -56.436 -42.889 84.840  1.000 217.754 ? 110 ALA DDD CB  1 
ATOM   5706  N N   . THR D 4 111 ? -54.116 -43.072 82.935  1.000 218.859 ? 111 THR DDD N   1 
ATOM   5707  C CA  . THR D 4 111 ? -52.773 -43.464 82.407  1.000 219.808 ? 111 THR DDD CA  1 
ATOM   5708  C C   . THR D 4 111 ? -52.040 -42.238 81.848  1.000 220.704 ? 111 THR DDD C   1 
ATOM   5709  O O   . THR D 4 111 ? -50.892 -41.993 82.268  1.000 220.439 ? 111 THR DDD O   1 
ATOM   5710  C CB  . THR D 4 111 ? -52.878 -44.532 81.303  1.000 219.340 ? 111 THR DDD CB  1 
ATOM   5711  O OG1 . THR D 4 111 ? -53.253 -45.771 81.902  1.000 219.772 ? 111 THR DDD OG1 1 
ATOM   5712  C CG2 . THR D 4 111 ? -51.597 -44.743 80.519  1.000 218.003 ? 111 THR DDD CG2 1 
ATOM   5713  N N   . TRP D 4 112 ? -52.695 -41.509 80.940  1.000 221.311 ? 112 TRP DDD N   1 
ATOM   5714  C CA  . TRP D 4 112 ? -52.062 -40.542 80.004  1.000 220.822 ? 112 TRP DDD CA  1 
ATOM   5715  C C   . TRP D 4 112 ? -51.759 -39.218 80.698  1.000 220.469 ? 112 TRP DDD C   1 
ATOM   5716  O O   . TRP D 4 112 ? -52.359 -38.887 81.722  1.000 219.894 ? 112 TRP DDD O   1 
ATOM   5717  C CB  . TRP D 4 112 ? -52.938 -40.349 78.763  1.000 221.328 ? 112 TRP DDD CB  1 
ATOM   5718  C CG  . TRP D 4 112 ? -52.732 -41.436 77.757  1.000 221.851 ? 112 TRP DDD CG  1 
ATOM   5719  C CD1 . TRP D 4 112 ? -53.097 -42.744 77.891  1.000 221.390 ? 112 TRP DDD CD1 1 
ATOM   5720  C CD2 . TRP D 4 112 ? -52.093 -41.324 76.472  1.000 223.120 ? 112 TRP DDD CD2 1 
ATOM   5721  N NE1 . TRP D 4 112 ? -52.734 -43.454 76.781  1.000 222.227 ? 112 TRP DDD NE1 1 
ATOM   5722  C CE2 . TRP D 4 112 ? -52.122 -42.611 75.890  1.000 223.168 ? 112 TRP DDD CE2 1 
ATOM   5723  C CE3 . TRP D 4 112 ? -51.508 -40.274 75.751  1.000 223.444 ? 112 TRP DDD CE3 1 
ATOM   5724  C CZ2 . TRP D 4 112 ? -51.593 -42.868 74.624  1.000 223.404 ? 112 TRP DDD CZ2 1 
ATOM   5725  C CZ3 . TRP D 4 112 ? -50.988 -40.530 74.499  1.000 223.616 ? 112 TRP DDD CZ3 1 
ATOM   5726  C CH2 . TRP D 4 112 ? -51.032 -41.810 73.945  1.000 223.669 ? 112 TRP DDD CH2 1 
ATOM   5727  N N   . PRO D 4 113 ? -50.835 -38.415 80.122  1.000 219.749 ? 113 PRO DDD N   1 
ATOM   5728  C CA  . PRO D 4 113 ? -50.350 -37.193 80.749  1.000 220.442 ? 113 PRO DDD CA  1 
ATOM   5729  C C   . PRO D 4 113 ? -51.181 -36.003 80.258  1.000 222.407 ? 113 PRO DDD C   1 
ATOM   5730  O O   . PRO D 4 113 ? -51.854 -36.140 79.252  1.000 221.947 ? 113 PRO DDD O   1 
ATOM   5731  C CB  . PRO D 4 113 ? -48.924 -37.154 80.198  1.000 219.239 ? 113 PRO DDD CB  1 
ATOM   5732  C CG  . PRO D 4 113 ? -49.114 -37.574 78.754  1.000 219.039 ? 113 PRO DDD CG  1 
ATOM   5733  C CD  . PRO D 4 113 ? -50.243 -38.589 78.784  1.000 219.105 ? 113 PRO DDD CD  1 
ATOM   5734  N N   . TYR D 4 114 ? -51.098 -34.873 80.958  1.000 225.483 ? 114 TYR DDD N   1 
ATOM   5735  C CA  . TYR D 4 114 ? -51.840 -33.627 80.635  1.000 228.290 ? 114 TYR DDD CA  1 
ATOM   5736  C C   . TYR D 4 114 ? -50.830 -32.512 80.331  1.000 230.420 ? 114 TYR DDD C   1 
ATOM   5737  O O   . TYR D 4 114 ? -49.822 -32.405 81.056  1.000 230.770 ? 114 TYR DDD O   1 
ATOM   5738  C CB  . TYR D 4 114 ? -52.803 -33.303 81.779  1.000 229.088 ? 114 TYR DDD CB  1 
ATOM   5739  C CG  . TYR D 4 114 ? -53.967 -34.255 81.898  1.000 229.015 ? 114 TYR DDD CG  1 
ATOM   5740  C CD1 . TYR D 4 114 ? -53.793 -35.558 82.346  1.000 228.285 ? 114 TYR DDD CD1 1 
ATOM   5741  C CD2 . TYR D 4 114 ? -55.247 -33.849 81.555  1.000 229.810 ? 114 TYR DDD CD2 1 
ATOM   5742  C CE1 . TYR D 4 114 ? -54.860 -36.435 82.448  1.000 228.144 ? 114 TYR DDD CE1 1 
ATOM   5743  C CE2 . TYR D 4 114 ? -56.325 -34.711 81.659  1.000 230.101 ? 114 TYR DDD CE2 1 
ATOM   5744  C CZ  . TYR D 4 114 ? -56.132 -36.006 82.108  1.000 229.287 ? 114 TYR DDD CZ  1 
ATOM   5745  O OH  . TYR D 4 114 ? -57.196 -36.851 82.213  1.000 229.653 ? 114 TYR DDD OH  1 
ATOM   5746  N N   . ASP D 4 115 ? -51.089 -31.720 79.282  1.000 232.891 ? 115 ASP DDD N   1 
ATOM   5747  C CA  . ASP D 4 115 ? -50.150 -30.698 78.741  1.000 234.821 ? 115 ASP DDD CA  1 
ATOM   5748  C C   . ASP D 4 115 ? -50.156 -29.445 79.645  1.000 237.432 ? 115 ASP DDD C   1 
ATOM   5749  O O   . ASP D 4 115 ? -49.067 -28.871 79.855  1.000 237.789 ? 115 ASP DDD O   1 
ATOM   5750  C CB  . ASP D 4 115 ? -50.474 -30.357 77.278  1.000 234.729 ? 115 ASP DDD CB  1 
ATOM   5751  C CG  . ASP D 4 115 ? -50.212 -31.441 76.242  1.000 233.756 ? 115 ASP DDD CG  1 
ATOM   5752  O OD1 . ASP D 4 115 ? -49.032 -31.791 76.029  1.000 233.454 ? 115 ASP DDD OD1 1 
ATOM   5753  O OD2 . ASP D 4 115 ? -51.192 -31.889 75.614  1.000 232.267 ? 115 ASP DDD OD2 1 
ATOM   5754  N N   . TYR D 4 116 ? -51.320 -29.041 80.177  1.000 240.059 ? 116 TYR DDD N   1 
ATOM   5755  C CA  . TYR D 4 116 ? -51.518 -27.797 80.975  1.000 241.911 ? 116 TYR DDD CA  1 
ATOM   5756  C C   . TYR D 4 116 ? -52.043 -28.150 82.378  1.000 243.361 ? 116 TYR DDD C   1 
ATOM   5757  O O   . TYR D 4 116 ? -52.913 -29.039 82.485  1.000 245.803 ? 116 TYR DDD O   1 
ATOM   5758  C CB  . TYR D 4 116 ? -52.480 -26.848 80.249  1.000 242.571 ? 116 TYR DDD CB  1 
ATOM   5759  C CG  . TYR D 4 116 ? -52.235 -26.684 78.767  1.000 242.664 ? 116 TYR DDD CG  1 
ATOM   5760  C CD1 . TYR D 4 116 ? -52.749 -27.590 77.850  1.000 242.247 ? 116 TYR DDD CD1 1 
ATOM   5761  C CD2 . TYR D 4 116 ? -51.507 -25.612 78.268  1.000 243.045 ? 116 TYR DDD CD2 1 
ATOM   5762  C CE1 . TYR D 4 116 ? -52.530 -27.448 76.487  1.000 241.688 ? 116 TYR DDD CE1 1 
ATOM   5763  C CE2 . TYR D 4 116 ? -51.278 -25.458 76.907  1.000 242.746 ? 116 TYR DDD CE2 1 
ATOM   5764  C CZ  . TYR D 4 116 ? -51.790 -26.379 76.011  1.000 241.803 ? 116 TYR DDD CZ  1 
ATOM   5765  O OH  . TYR D 4 116 ? -51.569 -26.222 74.673  1.000 240.055 ? 116 TYR DDD OH  1 
ATOM   5766  N N   . TRP D 4 117 ? -51.544 -27.467 83.419  1.000 243.672 ? 117 TRP DDD N   1 
ATOM   5767  C CA  . TRP D 4 117 ? -51.940 -27.667 84.844  1.000 243.533 ? 117 TRP DDD CA  1 
ATOM   5768  C C   . TRP D 4 117 ? -52.278 -26.324 85.502  1.000 245.559 ? 117 TRP DDD C   1 
ATOM   5769  O O   . TRP D 4 117 ? -51.598 -25.327 85.186  1.000 247.474 ? 117 TRP DDD O   1 
ATOM   5770  C CB  . TRP D 4 117 ? -50.827 -28.384 85.617  1.000 241.648 ? 117 TRP DDD CB  1 
ATOM   5771  C CG  . TRP D 4 117 ? -50.645 -29.812 85.213  1.000 239.352 ? 117 TRP DDD CG  1 
ATOM   5772  C CD1 . TRP D 4 117 ? -49.953 -30.275 84.133  1.000 237.384 ? 117 TRP DDD CD1 1 
ATOM   5773  C CD2 . TRP D 4 117 ? -51.176 -30.971 85.882  1.000 238.980 ? 117 TRP DDD CD2 1 
ATOM   5774  N NE1 . TRP D 4 117 ? -50.013 -31.641 84.083  1.000 236.499 ? 117 TRP DDD NE1 1 
ATOM   5775  C CE2 . TRP D 4 117 ? -50.756 -32.097 85.141  1.000 237.579 ? 117 TRP DDD CE2 1 
ATOM   5776  C CE3 . TRP D 4 117 ? -51.954 -31.170 87.031  1.000 239.504 ? 117 TRP DDD CE3 1 
ATOM   5777  C CZ2 . TRP D 4 117 ? -51.094 -33.398 85.512  1.000 237.399 ? 117 TRP DDD CZ2 1 
ATOM   5778  C CZ3 . TRP D 4 117 ? -52.287 -32.457 87.397  1.000 238.948 ? 117 TRP DDD CZ3 1 
ATOM   5779  C CH2 . TRP D 4 117 ? -51.862 -33.555 86.645  1.000 238.141 ? 117 TRP DDD CH2 1 
ATOM   5780  N N   . GLY D 4 118 ? -53.279 -26.312 86.389  1.000 245.877 ? 118 GLY DDD N   1 
ATOM   5781  C CA  . GLY D 4 118 ? -53.621 -25.154 87.240  1.000 247.213 ? 118 GLY DDD CA  1 
ATOM   5782  C C   . GLY D 4 118 ? -52.759 -25.136 88.491  1.000 247.948 ? 118 GLY DDD C   1 
ATOM   5783  O O   . GLY D 4 118 ? -52.156 -26.188 88.800  1.000 247.610 ? 118 GLY DDD O   1 
ATOM   5784  N N   . GLN D 4 119 ? -52.694 -23.996 89.190  1.000 248.587 ? 119 GLN DDD N   1 
ATOM   5785  C CA  . GLN D 4 119 ? -51.856 -23.824 90.411  1.000 248.166 ? 119 GLN DDD CA  1 
ATOM   5786  C C   . GLN D 4 119 ? -52.422 -24.701 91.544  1.000 249.128 ? 119 GLN DDD C   1 
ATOM   5787  O O   . GLN D 4 119 ? -51.651 -25.035 92.462  1.000 248.844 ? 119 GLN DDD O   1 
ATOM   5788  C CB  . GLN D 4 119 ? -51.688 -22.338 90.763  1.000 247.528 ? 119 GLN DDD CB  1 
ATOM   5789  C CG  . GLN D 4 119 ? -52.939 -21.625 91.262  1.000 247.430 ? 119 GLN DDD CG  1 
ATOM   5790  C CD  . GLN D 4 119 ? -52.701 -20.146 91.452  1.000 247.355 ? 119 GLN DDD CD  1 
ATOM   5791  O OE1 . GLN D 4 119 ? -51.684 -19.593 91.034  1.000 245.966 ? 119 GLN DDD OE1 1 
ATOM   5792  N NE2 . GLN D 4 119 ? -53.653 -19.484 92.084  1.000 248.233 ? 119 GLN DDD NE2 1 
ATOM   5793  N N   . GLY D 4 120 ? -53.696 -25.107 91.453  1.000 249.997 ? 120 GLY DDD N   1 
ATOM   5794  C CA  . GLY D 4 120 ? -54.365 -26.013 92.409  1.000 250.635 ? 120 GLY DDD CA  1 
ATOM   5795  C C   . GLY D 4 120 ? -55.083 -25.229 93.495  1.000 252.903 ? 120 GLY DDD C   1 
ATOM   5796  O O   . GLY D 4 120 ? -54.910 -23.995 93.530  1.000 254.277 ? 120 GLY DDD O   1 
ATOM   5797  N N   . THR D 4 121 ? -55.861 -25.902 94.350  1.000 253.776 ? 121 THR DDD N   1 
ATOM   5798  C CA  . THR D 4 121 ? -56.607 -25.260 95.468  1.000 256.350 ? 121 THR DDD CA  1 
ATOM   5799  C C   . THR D 4 121 ? -56.815 -26.257 96.614  1.000 258.178 ? 121 THR DDD C   1 
ATOM   5800  O O   . THR D 4 121 ? -57.017 -27.451 96.331  1.000 258.395 ? 121 THR DDD O   1 
ATOM   5801  C CB  . THR D 4 121 ? -57.932 -24.671 94.968  1.000 256.275 ? 121 THR DDD CB  1 
ATOM   5802  O OG1 . THR D 4 121 ? -58.204 -23.498 95.733  1.000 258.521 ? 121 THR DDD OG1 1 
ATOM   5803  C CG2 . THR D 4 121 ? -59.097 -25.626 95.077  1.000 255.506 ? 121 THR DDD CG2 1 
ATOM   5804  N N   . GLN D 4 122 ? -56.794 -25.767 97.856  1.000 260.289 ? 122 GLN DDD N   1 
ATOM   5805  C CA  . GLN D 4 122 ? -56.842 -26.602 99.085  1.000 261.470 ? 122 GLN DDD CA  1 
ATOM   5806  C C   . GLN D 4 122 ? -58.303 -26.918 99.427  1.000 264.709 ? 122 GLN DDD C   1 
ATOM   5807  O O   . GLN D 4 122 ? -59.119 -25.985 99.412  1.000 265.016 ? 122 GLN DDD O   1 
ATOM   5808  C CB  . GLN D 4 122 ? -56.120 -25.880 100.228 1.000 261.286 ? 122 GLN DDD CB  1 
ATOM   5809  C CG  . GLN D 4 122 ? -56.001 -26.694 101.512 1.000 260.689 ? 122 GLN DDD CG  1 
ATOM   5810  C CD  . GLN D 4 122 ? -55.050 -27.864 101.414 1.000 258.513 ? 122 GLN DDD CD  1 
ATOM   5811  O OE1 . GLN D 4 122 ? -53.937 -27.748 100.903 1.000 255.736 ? 122 GLN DDD OE1 1 
ATOM   5812  N NE2 . GLN D 4 122 ? -55.475 -29.007 101.933 1.000 258.605 ? 122 GLN DDD NE2 1 
ATOM   5813  N N   . VAL D 4 123 ? -58.606 -28.198 99.686  1.000 267.794 ? 123 VAL DDD N   1 
ATOM   5814  C CA  . VAL D 4 123 ? -59.847 -28.686 100.365 1.000 270.900 ? 123 VAL DDD CA  1 
ATOM   5815  C C   . VAL D 4 123 ? -59.421 -29.364 101.671 1.000 274.178 ? 123 VAL DDD C   1 
ATOM   5816  O O   . VAL D 4 123 ? -58.595 -30.305 101.601 1.000 275.527 ? 123 VAL DDD O   1 
ATOM   5817  C CB  . VAL D 4 123 ? -60.657 -29.664 99.491  1.000 269.278 ? 123 VAL DDD CB  1 
ATOM   5818  C CG1 . VAL D 4 123 ? -61.905 -30.169 100.208 1.000 269.039 ? 123 VAL DDD CG1 1 
ATOM   5819  C CG2 . VAL D 4 123 ? -61.018 -29.053 98.146  1.000 269.028 ? 123 VAL DDD CG2 1 
ATOM   5820  N N   . THR D 4 124 ? -59.961 -28.906 102.806 1.000 276.950 ? 124 THR DDD N   1 
ATOM   5821  C CA  . THR D 4 124 ? -59.660 -29.432 104.165 1.000 277.746 ? 124 THR DDD CA  1 
ATOM   5822  C C   . THR D 4 124 ? -60.975 -29.897 104.813 1.000 279.926 ? 124 THR DDD C   1 
ATOM   5823  O O   . THR D 4 124 ? -61.841 -29.028 105.052 1.000 282.951 ? 124 THR DDD O   1 
ATOM   5824  C CB  . THR D 4 124 ? -58.920 -28.371 104.993 1.000 277.601 ? 124 THR DDD CB  1 
ATOM   5825  O OG1 . THR D 4 124 ? -59.783 -27.247 105.140 1.000 278.319 ? 124 THR DDD OG1 1 
ATOM   5826  C CG2 . THR D 4 124 ? -57.634 -27.884 104.364 1.000 275.009 ? 124 THR DDD CG2 1 
ATOM   5827  N N   . VAL D 4 125 ? -61.122 -31.205 105.078 1.000 279.151 ? 125 VAL DDD N   1 
ATOM   5828  C CA  . VAL D 4 125 ? -62.335 -31.821 105.712 1.000 279.254 ? 125 VAL DDD CA  1 
ATOM   5829  C C   . VAL D 4 125 ? -62.148 -31.822 107.236 1.000 279.561 ? 125 VAL DDD C   1 
ATOM   5830  O O   . VAL D 4 125 ? -61.139 -32.391 107.694 1.000 278.414 ? 125 VAL DDD O   1 
ATOM   5831  C CB  . VAL D 4 125 ? -62.641 -33.248 105.207 1.000 278.283 ? 125 VAL DDD CB  1 
ATOM   5832  C CG1 . VAL D 4 125 ? -63.888 -33.292 104.337 1.000 277.776 ? 125 VAL DDD CG1 1 
ATOM   5833  C CG2 . VAL D 4 125 ? -61.464 -33.903 104.494 1.000 276.328 ? 125 VAL DDD CG2 1 
ATOM   5834  N N   . SER D 4 126 ? -63.117 -31.271 107.983 1.000 280.091 ? 126 SER DDD N   1 
ATOM   5835  C CA  . SER D 4 126 ? -63.007 -30.903 109.425 1.000 281.125 ? 126 SER DDD CA  1 
ATOM   5836  C C   . SER D 4 126 ? -64.065 -31.624 110.289 1.000 279.889 ? 126 SER DDD C   1 
ATOM   5837  O O   . SER D 4 126 ? -64.402 -32.780 109.966 1.000 280.568 ? 126 SER DDD O   1 
ATOM   5838  C CB  . SER D 4 126 ? -63.102 -29.404 109.573 1.000 283.051 ? 126 SER DDD CB  1 
ATOM   5839  O OG  . SER D 4 126 ? -64.455 -28.972 109.503 1.000 284.634 ? 126 SER DDD OG  1 
ATOM   5840  N N   . SER D 4 127 ? -64.533 -30.981 111.373 1.000 276.960 ? 127 SER DDD N   1 
ATOM   5841  C CA  . SER D 4 127 ? -65.590 -31.478 112.299 1.000 274.423 ? 127 SER DDD CA  1 
ATOM   5842  C C   . SER D 4 127 ? -66.414 -30.308 112.855 1.000 274.533 ? 127 SER DDD C   1 
ATOM   5843  O O   . SER D 4 127 ? -67.648 -30.346 112.969 1.000 272.713 ? 127 SER DDD O   1 
ATOM   5844  C CB  . SER D 4 127 ? -64.977 -32.283 113.413 1.000 273.666 ? 127 SER DDD CB  1 
ATOM   5845  O OG  . SER D 4 127 ? -64.432 -33.491 112.917 1.000 270.951 ? 127 SER DDD OG  1 
ATOM   5846  N N   . ASN E 1 5   ? -61.939 -19.215 9.654   1.000 187.157 ? 334 ASN EEE N   1 
ATOM   5847  C CA  . ASN E 1 5   ? -60.654 -18.499 9.389   1.000 180.472 ? 334 ASN EEE CA  1 
ATOM   5848  C C   . ASN E 1 5   ? -59.495 -19.505 9.488   1.000 175.418 ? 334 ASN EEE C   1 
ATOM   5849  O O   . ASN E 1 5   ? -58.757 -19.449 10.484  1.000 173.920 ? 334 ASN EEE O   1 
ATOM   5850  C CB  . ASN E 1 5   ? -60.488 -17.268 10.293  1.000 181.464 ? 334 ASN EEE CB  1 
ATOM   5851  C CG  . ASN E 1 5   ? -61.238 -17.345 11.609  1.000 187.571 ? 334 ASN EEE CG  1 
ATOM   5852  O OD1 . ASN E 1 5   ? -61.238 -18.377 12.277  1.000 186.400 ? 334 ASN EEE OD1 1 
ATOM   5853  N ND2 . ASN E 1 5   ? -61.884 -16.254 11.991  1.000 193.675 ? 334 ASN EEE ND2 1 
ATOM   5854  N N   . LEU E 1 6   ? -59.344 -20.382 8.485   1.000 174.930 ? 335 LEU EEE N   1 
ATOM   5855  C CA  . LEU E 1 6   ? -58.281 -21.429 8.395   1.000 170.858 ? 335 LEU EEE CA  1 
ATOM   5856  C C   . LEU E 1 6   ? -57.304 -21.074 7.264   1.000 166.262 ? 335 LEU EEE C   1 
ATOM   5857  O O   . LEU E 1 6   ? -57.771 -20.920 6.123   1.000 167.430 ? 335 LEU EEE O   1 
ATOM   5858  C CB  . LEU E 1 6   ? -58.955 -22.786 8.148   1.000 173.801 ? 335 LEU EEE CB  1 
ATOM   5859  C CG  . LEU E 1 6   ? -58.064 -23.905 7.608   1.000 169.669 ? 335 LEU EEE CG  1 
ATOM   5860  C CD1 . LEU E 1 6   ? -56.866 -24.159 8.515   1.000 165.085 ? 335 LEU EEE CD1 1 
ATOM   5861  C CD2 . LEU E 1 6   ? -58.876 -25.180 7.430   1.000 173.631 ? 335 LEU EEE CD2 1 
ATOM   5862  N N   . CYS E 1 7   ? -56.001 -20.973 7.563   1.000 162.609 ? 336 CYS EEE N   1 
ATOM   5863  C CA  . CYS E 1 7   ? -54.947 -20.464 6.637   1.000 159.187 ? 336 CYS EEE CA  1 
ATOM   5864  C C   . CYS E 1 7   ? -55.001 -21.230 5.319   1.000 158.448 ? 336 CYS EEE C   1 
ATOM   5865  O O   . CYS E 1 7   ? -54.742 -22.433 5.280   1.000 156.305 ? 336 CYS EEE O   1 
ATOM   5866  C CB  . CYS E 1 7   ? -53.542 -20.561 7.224   1.000 154.928 ? 336 CYS EEE CB  1 
ATOM   5867  S SG  . CYS E 1 7   ? -53.219 -19.455 8.631   1.000 157.488 ? 336 CYS EEE SG  1 
ATOM   5868  N N   . PRO E 1 8   ? -55.342 -20.547 4.204   1.000 161.171 ? 337 PRO EEE N   1 
ATOM   5869  C CA  . PRO E 1 8   ? -55.477 -21.199 2.907   1.000 161.037 ? 337 PRO EEE CA  1 
ATOM   5870  C C   . PRO E 1 8   ? -54.113 -21.361 2.231   1.000 154.727 ? 337 PRO EEE C   1 
ATOM   5871  O O   . PRO E 1 8   ? -53.777 -20.568 1.375   1.000 153.680 ? 337 PRO EEE O   1 
ATOM   5872  C CB  . PRO E 1 8   ? -56.376 -20.226 2.134   1.000 165.717 ? 337 PRO EEE CB  1 
ATOM   5873  C CG  . PRO E 1 8   ? -55.974 -18.865 2.668   1.000 165.186 ? 337 PRO EEE CG  1 
ATOM   5874  C CD  . PRO E 1 8   ? -55.613 -19.102 4.122   1.000 163.974 ? 337 PRO EEE CD  1 
ATOM   5875  N N   . PHE E 1 9   ? -53.356 -22.368 2.659   1.000 150.913 ? 338 PHE EEE N   1 
ATOM   5876  C CA  . PHE E 1 9   ? -52.184 -22.894 1.919   1.000 146.775 ? 338 PHE EEE CA  1 
ATOM   5877  C C   . PHE E 1 9   ? -52.699 -23.700 0.723   1.000 148.235 ? 338 PHE EEE C   1 
ATOM   5878  O O   . PHE E 1 9   ? -51.949 -23.868 -0.259  1.000 144.919 ? 338 PHE EEE O   1 
ATOM   5879  C CB  . PHE E 1 9   ? -51.300 -23.716 2.854   1.000 145.332 ? 338 PHE EEE CB  1 
ATOM   5880  C CG  . PHE E 1 9   ? -50.683 -22.922 3.975   1.000 145.062 ? 338 PHE EEE CG  1 
ATOM   5881  C CD1 . PHE E 1 9   ? -49.980 -21.754 3.716   1.000 142.567 ? 338 PHE EEE CD1 1 
ATOM   5882  C CD2 . PHE E 1 9   ? -50.797 -23.352 5.287   1.000 147.079 ? 338 PHE EEE CD2 1 
ATOM   5883  C CE1 . PHE E 1 9   ? -49.408 -21.027 4.748   1.000 141.837 ? 338 PHE EEE CE1 1 
ATOM   5884  C CE2 . PHE E 1 9   ? -50.217 -22.627 6.315   1.000 147.185 ? 338 PHE EEE CE2 1 
ATOM   5885  C CZ  . PHE E 1 9   ? -49.523 -21.469 6.045   1.000 144.424 ? 338 PHE EEE CZ  1 
ATOM   5886  N N   . GLY E 1 10  ? -53.955 -24.159 0.813   1.000 153.762 ? 339 GLY EEE N   1 
ATOM   5887  C CA  . GLY E 1 10  ? -54.690 -24.864 -0.255  1.000 158.049 ? 339 GLY EEE CA  1 
ATOM   5888  C C   . GLY E 1 10  ? -54.520 -24.198 -1.609  1.000 159.377 ? 339 GLY EEE C   1 
ATOM   5889  O O   . GLY E 1 10  ? -54.240 -24.924 -2.574  1.000 164.001 ? 339 GLY EEE O   1 
ATOM   5890  N N   . GLU E 1 11  ? -54.654 -22.869 -1.682  1.000 159.335 ? 340 GLU EEE N   1 
ATOM   5891  C CA  . GLU E 1 11  ? -54.600 -22.090 -2.955  1.000 158.748 ? 340 GLU EEE CA  1 
ATOM   5892  C C   . GLU E 1 11  ? -53.185 -21.530 -3.181  1.000 148.569 ? 340 GLU EEE C   1 
ATOM   5893  O O   . GLU E 1 11  ? -53.057 -20.498 -3.871  1.000 146.813 ? 340 GLU EEE O   1 
ATOM   5894  C CB  . GLU E 1 11  ? -55.672 -20.993 -2.950  1.000 167.771 ? 340 GLU EEE CB  1 
ATOM   5895  C CG  . GLU E 1 11  ? -55.474 -19.917 -1.888  1.000 171.137 ? 340 GLU EEE CG  1 
ATOM   5896  C CD  . GLU E 1 11  ? -56.627 -18.932 -1.753  1.000 179.253 ? 340 GLU EEE CD  1 
ATOM   5897  O OE1 . GLU E 1 11  ? -57.314 -18.958 -0.704  1.000 184.007 ? 340 GLU EEE OE1 1 
ATOM   5898  O OE2 . GLU E 1 11  ? -56.834 -18.132 -2.694  1.000 182.909 ? 340 GLU EEE OE2 1 
ATOM   5899  N N   . VAL E 1 12  ? -52.159 -22.194 -2.640  1.000 141.200 ? 341 VAL EEE N   1 
ATOM   5900  C CA  . VAL E 1 12  ? -50.721 -21.859 -2.865  1.000 136.046 ? 341 VAL EEE CA  1 
ATOM   5901  C C   . VAL E 1 12  ? -50.017 -23.112 -3.391  1.000 131.901 ? 341 VAL EEE C   1 
ATOM   5902  O O   . VAL E 1 12  ? -49.475 -23.062 -4.509  1.000 131.851 ? 341 VAL EEE O   1 
ATOM   5903  C CB  . VAL E 1 12  ? -50.040 -21.333 -1.586  1.000 134.209 ? 341 VAL EEE CB  1 
ATOM   5904  C CG1 . VAL E 1 12  ? -48.563 -21.052 -1.808  1.000 130.489 ? 341 VAL EEE CG1 1 
ATOM   5905  C CG2 . VAL E 1 12  ? -50.731 -20.093 -1.045  1.000 136.616 ? 341 VAL EEE CG2 1 
ATOM   5906  N N   . PHE E 1 13  ? -50.035 -24.189 -2.604  1.000 128.106 ? 342 PHE EEE N   1 
ATOM   5907  C CA  . PHE E 1 13  ? -49.378 -25.482 -2.918  1.000 126.482 ? 342 PHE EEE CA  1 
ATOM   5908  C C   . PHE E 1 13  ? -50.125 -26.167 -4.061  1.000 131.232 ? 342 PHE EEE C   1 
ATOM   5909  O O   . PHE E 1 13  ? -49.509 -26.467 -5.097  1.000 129.307 ? 342 PHE EEE O   1 
ATOM   5910  C CB  . PHE E 1 13  ? -49.356 -26.381 -1.682  1.000 125.524 ? 342 PHE EEE CB  1 
ATOM   5911  C CG  . PHE E 1 13  ? -48.421 -25.910 -0.602  1.000 120.765 ? 342 PHE EEE CG  1 
ATOM   5912  C CD1 . PHE E 1 13  ? -48.788 -24.891 0.259   1.000 120.610 ? 342 PHE EEE CD1 1 
ATOM   5913  C CD2 . PHE E 1 13  ? -47.166 -26.478 -0.463  1.000 117.952 ? 342 PHE EEE CD2 1 
ATOM   5914  C CE1 . PHE E 1 13  ? -47.922 -24.457 1.248   1.000 118.917 ? 342 PHE EEE CE1 1 
ATOM   5915  C CE2 . PHE E 1 13  ? -46.295 -26.032 0.516   1.000 115.509 ? 342 PHE EEE CE2 1 
ATOM   5916  C CZ  . PHE E 1 13  ? -46.675 -25.021 1.367   1.000 116.229 ? 342 PHE EEE CZ  1 
ATOM   5917  N N   . ASN E 1 14  ? -51.422 -26.402 -3.859  1.000 139.758 ? 343 ASN EEE N   1 
ATOM   5918  C CA  . ASN E 1 14  ? -52.317 -27.093 -4.825  1.000 148.443 ? 343 ASN EEE CA  1 
ATOM   5919  C C   . ASN E 1 14  ? -52.703 -26.134 -5.958  1.000 149.883 ? 343 ASN EEE C   1 
ATOM   5920  O O   . ASN E 1 14  ? -53.397 -26.592 -6.886  1.000 153.477 ? 343 ASN EEE O   1 
ATOM   5921  C CB  . ASN E 1 14  ? -53.563 -27.664 -4.138  1.000 156.844 ? 343 ASN EEE CB  1 
ATOM   5922  C CG  . ASN E 1 14  ? -53.302 -28.978 -3.439  1.000 161.731 ? 343 ASN EEE CG  1 
ATOM   5923  O OD1 . ASN E 1 14  ? -53.021 -29.981 -4.087  1.000 162.251 ? 343 ASN EEE OD1 1 
ATOM   5924  N ND2 . ASN E 1 14  ? -53.394 -28.988 -2.122  1.000 172.383 ? 343 ASN EEE ND2 1 
ATOM   5925  N N   . ALA E 1 15  ? -52.279 -24.865 -5.894  1.000 148.527 ? 344 ALA EEE N   1 
ATOM   5926  C CA  . ALA E 1 15  ? -52.556 -23.829 -6.920  1.000 150.782 ? 344 ALA EEE CA  1 
ATOM   5927  C C   . ALA E 1 15  ? -52.251 -24.400 -8.311  1.000 150.122 ? 344 ALA EEE C   1 
ATOM   5928  O O   . ALA E 1 15  ? -51.158 -24.983 -8.481  1.000 147.578 ? 344 ALA EEE O   1 
ATOM   5929  C CB  . ALA E 1 15  ? -51.750 -22.584 -6.636  1.000 148.928 ? 344 ALA EEE CB  1 
ATOM   5930  N N   . THR E 1 16  ? -53.189 -24.244 -9.256  1.000 151.292 ? 345 THR EEE N   1 
ATOM   5931  C CA  . THR E 1 16  ? -53.172 -24.864 -10.612 1.000 150.809 ? 345 THR EEE CA  1 
ATOM   5932  C C   . THR E 1 16  ? -51.896 -24.461 -11.363 1.000 146.897 ? 345 THR EEE C   1 
ATOM   5933  O O   . THR E 1 16  ? -51.150 -25.358 -11.762 1.000 142.935 ? 345 THR EEE O   1 
ATOM   5934  C CB  . THR E 1 16  ? -54.442 -24.512 -11.398 1.000 155.535 ? 345 THR EEE CB  1 
ATOM   5935  O OG1 . THR E 1 16  ? -54.813 -23.168 -11.085 1.000 157.264 ? 345 THR EEE OG1 1 
ATOM   5936  C CG2 . THR E 1 16  ? -55.602 -25.431 -11.085 1.000 159.250 ? 345 THR EEE CG2 1 
ATOM   5937  N N   . ARG E 1 17  ? -51.648 -23.163 -11.537 1.000 148.842 ? 346 ARG EEE N   1 
ATOM   5938  C CA  . ARG E 1 17  ? -50.436 -22.633 -12.221 1.000 149.728 ? 346 ARG EEE CA  1 
ATOM   5939  C C   . ARG E 1 17  ? -49.478 -22.030 -11.186 1.000 144.787 ? 346 ARG EEE C   1 
ATOM   5940  O O   . ARG E 1 17  ? -49.966 -21.508 -10.164 1.000 146.377 ? 346 ARG EEE O   1 
ATOM   5941  C CB  . ARG E 1 17  ? -50.851 -21.581 -13.251 1.000 156.564 ? 346 ARG EEE CB  1 
ATOM   5942  C CG  . ARG E 1 17  ? -49.792 -21.266 -14.299 1.000 159.650 ? 346 ARG EEE CG  1 
ATOM   5943  C CD  . ARG E 1 17  ? -50.334 -20.390 -15.416 1.000 165.523 ? 346 ARG EEE CD  1 
ATOM   5944  N NE  . ARG E 1 17  ? -51.299 -21.114 -16.242 1.000 170.682 ? 346 ARG EEE NE  1 
ATOM   5945  C CZ  . ARG E 1 17  ? -52.610 -20.870 -16.319 1.000 175.200 ? 346 ARG EEE CZ  1 
ATOM   5946  N NH1 . ARG E 1 17  ? -53.171 -19.889 -15.626 1.000 175.844 ? 346 ARG EEE NH1 1 
ATOM   5947  N NH2 . ARG E 1 17  ? -53.361 -21.621 -17.106 1.000 179.610 ? 346 ARG EEE NH2 1 
ATOM   5948  N N   . PHE E 1 18  ? -48.167 -22.105 -11.444 1.000 140.260 ? 347 PHE EEE N   1 
ATOM   5949  C CA  . PHE E 1 18  ? -47.103 -21.471 -10.621 1.000 136.023 ? 347 PHE EEE CA  1 
ATOM   5950  C C   . PHE E 1 18  ? -46.435 -20.350 -11.418 1.000 135.283 ? 347 PHE EEE C   1 
ATOM   5951  O O   . PHE E 1 18  ? -46.693 -20.243 -12.622 1.000 138.690 ? 347 PHE EEE O   1 
ATOM   5952  C CB  . PHE E 1 18  ? -46.063 -22.500 -10.183 1.000 134.727 ? 347 PHE EEE CB  1 
ATOM   5953  C CG  . PHE E 1 18  ? -46.256 -23.024 -8.784  1.000 134.104 ? 347 PHE EEE CG  1 
ATOM   5954  C CD1 . PHE E 1 18  ? -47.370 -23.779 -8.459  1.000 136.258 ? 347 PHE EEE CD1 1 
ATOM   5955  C CD2 . PHE E 1 18  ? -45.312 -22.785 -7.798  1.000 131.639 ? 347 PHE EEE CD2 1 
ATOM   5956  C CE1 . PHE E 1 18  ? -47.544 -24.270 -7.174  1.000 135.740 ? 347 PHE EEE CE1 1 
ATOM   5957  C CE2 . PHE E 1 18  ? -45.483 -23.282 -6.517  1.000 130.017 ? 347 PHE EEE CE2 1 
ATOM   5958  C CZ  . PHE E 1 18  ? -46.600 -24.022 -6.207  1.000 132.656 ? 347 PHE EEE CZ  1 
ATOM   5959  N N   . ALA E 1 19  ? -45.591 -19.556 -10.756 1.000 133.043 ? 348 ALA EEE N   1 
ATOM   5960  C CA  . ALA E 1 19  ? -44.906 -18.373 -11.333 1.000 134.120 ? 348 ALA EEE CA  1 
ATOM   5961  C C   . ALA E 1 19  ? -43.519 -18.772 -11.844 1.000 132.085 ? 348 ALA EEE C   1 
ATOM   5962  O O   . ALA E 1 19  ? -43.033 -19.841 -11.444 1.000 128.469 ? 348 ALA EEE O   1 
ATOM   5963  C CB  . ALA E 1 19  ? -44.818 -17.277 -10.299 1.000 134.682 ? 348 ALA EEE CB  1 
ATOM   5964  N N   . SER E 1 20  ? -42.930 -17.951 -12.721 1.000 134.902 ? 349 SER EEE N   1 
ATOM   5965  C CA  . SER E 1 20  ? -41.522 -18.061 -13.194 1.000 134.590 ? 349 SER EEE CA  1 
ATOM   5966  C C   . SER E 1 20  ? -40.618 -17.530 -12.083 1.000 128.828 ? 349 SER EEE C   1 
ATOM   5967  O O   . SER E 1 20  ? -41.007 -16.541 -11.433 1.000 126.070 ? 349 SER EEE O   1 
ATOM   5968  C CB  . SER E 1 20  ? -41.288 -17.299 -14.485 1.000 140.783 ? 349 SER EEE CB  1 
ATOM   5969  O OG  . SER E 1 20  ? -42.032 -17.836 -15.570 1.000 145.844 ? 349 SER EEE OG  1 
ATOM   5970  N N   . VAL E 1 21  ? -39.458 -18.151 -11.886 1.000 125.469 ? 350 VAL EEE N   1 
ATOM   5971  C CA  . VAL E 1 21  ? -38.603 -17.932 -10.684 1.000 122.863 ? 350 VAL EEE CA  1 
ATOM   5972  C C   . VAL E 1 21  ? -38.380 -16.432 -10.451 1.000 122.774 ? 350 VAL EEE C   1 
ATOM   5973  O O   . VAL E 1 21  ? -38.671 -15.985 -9.337  1.000 125.541 ? 350 VAL EEE O   1 
ATOM   5974  C CB  . VAL E 1 21  ? -37.270 -18.690 -10.782 1.000 123.920 ? 350 VAL EEE CB  1 
ATOM   5975  C CG1 . VAL E 1 21  ? -36.438 -18.259 -11.980 1.000 128.069 ? 350 VAL EEE CG1 1 
ATOM   5976  C CG2 . VAL E 1 21  ? -36.472 -18.546 -9.499  1.000 122.995 ? 350 VAL EEE CG2 1 
ATOM   5977  N N   . TYR E 1 22  ? -37.893 -15.688 -11.449 1.000 123.216 ? 351 TYR EEE N   1 
ATOM   5978  C CA  . TYR E 1 22  ? -37.507 -14.255 -11.327 1.000 124.598 ? 351 TYR EEE CA  1 
ATOM   5979  C C   . TYR E 1 22  ? -38.719 -13.387 -10.988 1.000 122.939 ? 351 TYR EEE C   1 
ATOM   5980  O O   . TYR E 1 22  ? -38.479 -12.272 -10.472 1.000 122.633 ? 351 TYR EEE O   1 
ATOM   5981  C CB  . TYR E 1 22  ? -36.913 -13.711 -12.626 1.000 129.626 ? 351 TYR EEE CB  1 
ATOM   5982  C CG  . TYR E 1 22  ? -37.925 -13.488 -13.721 1.000 130.521 ? 351 TYR EEE CG  1 
ATOM   5983  C CD1 . TYR E 1 22  ? -38.484 -14.558 -14.400 1.000 130.430 ? 351 TYR EEE CD1 1 
ATOM   5984  C CD2 . TYR E 1 22  ? -38.339 -12.215 -14.071 1.000 131.341 ? 351 TYR EEE CD2 1 
ATOM   5985  C CE1 . TYR E 1 22  ? -39.421 -14.371 -15.400 1.000 131.549 ? 351 TYR EEE CE1 1 
ATOM   5986  C CE2 . TYR E 1 22  ? -39.275 -12.013 -15.070 1.000 132.985 ? 351 TYR EEE CE2 1 
ATOM   5987  C CZ  . TYR E 1 22  ? -39.818 -13.094 -15.739 1.000 133.047 ? 351 TYR EEE CZ  1 
ATOM   5988  O OH  . TYR E 1 22  ? -40.742 -12.915 -16.724 1.000 135.319 ? 351 TYR EEE OH  1 
ATOM   5989  N N   . ALA E 1 23  ? -39.927 -13.870 -11.325 1.000 122.124 ? 352 ALA EEE N   1 
ATOM   5990  C CA  . ALA E 1 23  ? -41.240 -13.204 -11.139 1.000 124.920 ? 352 ALA EEE CA  1 
ATOM   5991  C C   . ALA E 1 23  ? -42.052 -13.897 -10.035 1.000 125.027 ? 352 ALA EEE C   1 
ATOM   5992  O O   . ALA E 1 23  ? -43.291 -13.985 -10.174 1.000 127.711 ? 352 ALA EEE O   1 
ATOM   5993  C CB  . ALA E 1 23  ? -41.990 -13.221 -12.445 1.000 127.079 ? 352 ALA EEE CB  1 
ATOM   5994  N N   . TRP E 1 24  ? -41.371 -14.346 -8.976  1.000 123.877 ? 353 TRP EEE N   1 
ATOM   5995  C CA  . TRP E 1 24  ? -41.929 -15.177 -7.874  1.000 121.790 ? 353 TRP EEE CA  1 
ATOM   5996  C C   . TRP E 1 24  ? -43.143 -14.496 -7.230  1.000 126.164 ? 353 TRP EEE C   1 
ATOM   5997  O O   . TRP E 1 24  ? -43.175 -13.249 -7.167  1.000 129.415 ? 353 TRP EEE O   1 
ATOM   5998  C CB  . TRP E 1 24  ? -40.850 -15.512 -6.837  1.000 118.293 ? 353 TRP EEE CB  1 
ATOM   5999  C CG  . TRP E 1 24  ? -40.057 -14.345 -6.343  1.000 117.694 ? 353 TRP EEE CG  1 
ATOM   6000  C CD1 . TRP E 1 24  ? -38.956 -13.786 -6.921  1.000 118.805 ? 353 TRP EEE CD1 1 
ATOM   6001  C CD2 . TRP E 1 24  ? -40.284 -13.618 -5.129  1.000 119.113 ? 353 TRP EEE CD2 1 
ATOM   6002  N NE1 . TRP E 1 24  ? -38.497 -12.747 -6.163  1.000 120.655 ? 353 TRP EEE NE1 1 
ATOM   6003  C CE2 . TRP E 1 24  ? -39.291 -12.618 -5.057  1.000 120.947 ? 353 TRP EEE CE2 1 
ATOM   6004  C CE3 . TRP E 1 24  ? -41.235 -13.708 -4.108  1.000 119.610 ? 353 TRP EEE CE3 1 
ATOM   6005  C CZ2 . TRP E 1 24  ? -39.215 -11.719 -3.996  1.000 122.568 ? 353 TRP EEE CZ2 1 
ATOM   6006  C CZ3 . TRP E 1 24  ? -41.165 -12.814 -3.063  1.000 121.713 ? 353 TRP EEE CZ3 1 
ATOM   6007  C CH2 . TRP E 1 24  ? -40.170 -11.834 -3.012  1.000 123.026 ? 353 TRP EEE CH2 1 
ATOM   6008  N N   . ASN E 1 25  ? -44.087 -15.313 -6.755  1.000 128.126 ? 354 ASN EEE N   1 
ATOM   6009  C CA  . ASN E 1 25  ? -45.437 -14.893 -6.300  1.000 130.573 ? 354 ASN EEE CA  1 
ATOM   6010  C C   . ASN E 1 25  ? -45.491 -14.964 -4.769  1.000 127.190 ? 354 ASN EEE C   1 
ATOM   6011  O O   . ASN E 1 25  ? -45.330 -16.071 -4.220  1.000 123.579 ? 354 ASN EEE O   1 
ATOM   6012  C CB  . ASN E 1 25  ? -46.514 -15.748 -6.979  1.000 134.325 ? 354 ASN EEE CB  1 
ATOM   6013  C CG  . ASN E 1 25  ? -47.593 -14.910 -7.635  1.000 141.166 ? 354 ASN EEE CG  1 
ATOM   6014  O OD1 . ASN E 1 25  ? -47.974 -13.864 -7.111  1.000 146.452 ? 354 ASN EEE OD1 1 
ATOM   6015  N ND2 . ASN E 1 25  ? -48.077 -15.340 -8.791  1.000 144.547 ? 354 ASN EEE ND2 1 
ATOM   6016  N N   . ARG E 1 26  ? -45.705 -13.821 -4.114  1.000 128.231 ? 355 ARG EEE N   1 
ATOM   6017  C CA  . ARG E 1 26  ? -45.840 -13.730 -2.636  1.000 129.362 ? 355 ARG EEE CA  1 
ATOM   6018  C C   . ARG E 1 26  ? -47.319 -13.758 -2.244  1.000 131.271 ? 355 ARG EEE C   1 
ATOM   6019  O O   . ARG E 1 26  ? -48.105 -13.046 -2.883  1.000 133.401 ? 355 ARG EEE O   1 
ATOM   6020  C CB  . ARG E 1 26  ? -45.193 -12.448 -2.104  1.000 131.713 ? 355 ARG EEE CB  1 
ATOM   6021  C CG  . ARG E 1 26  ? -45.428 -12.218 -0.617  1.000 132.809 ? 355 ARG EEE CG  1 
ATOM   6022  C CD  . ARG E 1 26  ? -44.347 -11.392 0.054   1.000 134.257 ? 355 ARG EEE CD  1 
ATOM   6023  N NE  . ARG E 1 26  ? -43.091 -12.121 0.168   1.000 132.092 ? 355 ARG EEE NE  1 
ATOM   6024  C CZ  . ARG E 1 26  ? -42.064 -11.775 0.945   1.000 134.160 ? 355 ARG EEE CZ  1 
ATOM   6025  N NH1 . ARG E 1 26  ? -42.114 -10.694 1.711   1.000 137.210 ? 355 ARG EEE NH1 1 
ATOM   6026  N NH2 . ARG E 1 26  ? -40.980 -12.531 0.958   1.000 133.440 ? 355 ARG EEE NH2 1 
ATOM   6027  N N   . LYS E 1 27  ? -47.657 -14.542 -1.218  1.000 131.476 ? 356 LYS EEE N   1 
ATOM   6028  C CA  . LYS E 1 27  ? -49.005 -14.609 -0.589  1.000 135.322 ? 356 LYS EEE CA  1 
ATOM   6029  C C   . LYS E 1 27  ? -48.873 -14.225 0.885   1.000 135.049 ? 356 LYS EEE C   1 
ATOM   6030  O O   . LYS E 1 27  ? -48.099 -14.882 1.602   1.000 132.623 ? 356 LYS EEE O   1 
ATOM   6031  C CB  . LYS E 1 27  ? -49.579 -16.023 -0.698  1.000 137.128 ? 356 LYS EEE CB  1 
ATOM   6032  C CG  . LYS E 1 27  ? -51.075 -16.154 -0.442  1.000 142.607 ? 356 LYS EEE CG  1 
ATOM   6033  C CD  . LYS E 1 27  ? -51.917 -15.951 -1.684  1.000 148.321 ? 356 LYS EEE CD  1 
ATOM   6034  C CE  . LYS E 1 27  ? -53.212 -16.741 -1.684  1.000 153.438 ? 356 LYS EEE CE  1 
ATOM   6035  N NZ  . LYS E 1 27  ? -54.206 -16.174 -0.741  1.000 158.755 ? 356 LYS EEE NZ  1 
ATOM   6036  N N   . ARG E 1 28  ? -49.600 -13.200 1.318   1.000 138.757 ? 357 ARG EEE N   1 
ATOM   6037  C CA  . ARG E 1 28  ? -49.556 -12.698 2.714   1.000 140.659 ? 357 ARG EEE CA  1 
ATOM   6038  C C   . ARG E 1 28  ? -50.593 -13.458 3.537   1.000 140.360 ? 357 ARG EEE C   1 
ATOM   6039  O O   . ARG E 1 28  ? -51.779 -13.113 3.455   1.000 146.590 ? 357 ARG EEE O   1 
ATOM   6040  C CB  . ARG E 1 28  ? -49.820 -11.193 2.748   1.000 147.608 ? 357 ARG EEE CB  1 
ATOM   6041  C CG  . ARG E 1 28  ? -49.655 -10.557 4.121   1.000 151.423 ? 357 ARG EEE CG  1 
ATOM   6042  C CD  . ARG E 1 28  ? -49.271 -9.101  3.967   1.000 156.060 ? 357 ARG EEE CD  1 
ATOM   6043  N NE  . ARG E 1 28  ? -48.673 -8.507  5.151   1.000 157.995 ? 357 ARG EEE NE  1 
ATOM   6044  C CZ  . ARG E 1 28  ? -49.348 -8.100  6.218   1.000 163.770 ? 357 ARG EEE CZ  1 
ATOM   6045  N NH1 . ARG E 1 28  ? -50.662 -8.258  6.280   1.000 167.022 ? 357 ARG EEE NH1 1 
ATOM   6046  N NH2 . ARG E 1 28  ? -48.700 -7.551  7.232   1.000 166.156 ? 357 ARG EEE NH2 1 
ATOM   6047  N N   . ILE E 1 29  ? -50.153 -14.459 4.295   1.000 136.269 ? 358 ILE EEE N   1 
ATOM   6048  C CA  . ILE E 1 29  ? -51.029 -15.225 5.226   1.000 138.517 ? 358 ILE EEE CA  1 
ATOM   6049  C C   . ILE E 1 29  ? -51.157 -14.415 6.521   1.000 140.110 ? 358 ILE EEE C   1 
ATOM   6050  O O   . ILE E 1 29  ? -50.111 -14.070 7.110   1.000 136.385 ? 358 ILE EEE O   1 
ATOM   6051  C CB  . ILE E 1 29  ? -50.477 -16.642 5.470   1.000 138.075 ? 358 ILE EEE CB  1 
ATOM   6052  C CG1 . ILE E 1 29  ? -50.166 -17.389 4.168   1.000 137.565 ? 358 ILE EEE CG1 1 
ATOM   6053  C CG2 . ILE E 1 29  ? -51.431 -17.437 6.341   1.000 141.749 ? 358 ILE EEE CG2 1 
ATOM   6054  C CD1 . ILE E 1 29  ? -51.395 -17.823 3.391   1.000 140.965 ? 358 ILE EEE CD1 1 
ATOM   6055  N N   . SER E 1 30  ? -52.394 -14.102 6.919   1.000 144.982 ? 359 SER EEE N   1 
ATOM   6056  C CA  . SER E 1 30  ? -52.736 -13.303 8.128   1.000 149.331 ? 359 SER EEE CA  1 
ATOM   6057  C C   . SER E 1 30  ? -54.137 -13.674 8.624   1.000 154.933 ? 359 SER EEE C   1 
ATOM   6058  O O   . SER E 1 30  ? -54.933 -14.188 7.813   1.000 156.021 ? 359 SER EEE O   1 
ATOM   6059  C CB  . SER E 1 30  ? -52.640 -11.830 7.849   1.000 151.134 ? 359 SER EEE CB  1 
ATOM   6060  O OG  . SER E 1 30  ? -51.342 -11.491 7.397   1.000 146.714 ? 359 SER EEE OG  1 
ATOM   6061  N N   . ASN E 1 31  ? -54.406 -13.406 9.906   1.000 159.483 ? 360 ASN EEE N   1 
ATOM   6062  C CA  . ASN E 1 31  ? -55.701 -13.641 10.603  1.000 167.303 ? 360 ASN EEE CA  1 
ATOM   6063  C C   . ASN E 1 31  ? -56.282 -14.994 10.184  1.000 166.803 ? 360 ASN EEE C   1 
ATOM   6064  O O   . ASN E 1 31  ? -57.370 -15.030 9.577   1.000 170.062 ? 360 ASN EEE O   1 
ATOM   6065  C CB  . ASN E 1 31  ? -56.669 -12.478 10.388  1.000 175.269 ? 360 ASN EEE CB  1 
ATOM   6066  C CG  . ASN E 1 31  ? -56.123 -11.191 10.963  1.000 178.199 ? 360 ASN EEE CG  1 
ATOM   6067  O OD1 . ASN E 1 31  ? -54.986 -10.824 10.677  1.000 175.979 ? 360 ASN EEE OD1 1 
ATOM   6068  N ND2 . ASN E 1 31  ? -56.914 -10.519 11.786  1.000 184.360 ? 360 ASN EEE ND2 1 
ATOM   6069  N N   . CYS E 1 32  ? -55.564 -16.062 10.528  1.000 163.985 ? 361 CYS EEE N   1 
ATOM   6070  C CA  . CYS E 1 32  ? -55.971 -17.475 10.333  1.000 164.516 ? 361 CYS EEE CA  1 
ATOM   6071  C C   . CYS E 1 32  ? -55.108 -18.383 11.215  1.000 161.045 ? 361 CYS EEE C   1 
ATOM   6072  O O   . CYS E 1 32  ? -53.986 -17.976 11.567  1.000 157.853 ? 361 CYS EEE O   1 
ATOM   6073  C CB  . CYS E 1 32  ? -55.834 -17.873 8.871   1.000 162.749 ? 361 CYS EEE CB  1 
ATOM   6074  S SG  . CYS E 1 32  ? -54.151 -17.669 8.238   1.000 158.235 ? 361 CYS EEE SG  1 
ATOM   6075  N N   . VAL E 1 33  ? -55.625 -19.564 11.555  1.000 161.621 ? 362 VAL EEE N   1 
ATOM   6076  C CA  . VAL E 1 33  ? -54.861 -20.651 12.226  1.000 160.095 ? 362 VAL EEE CA  1 
ATOM   6077  C C   . VAL E 1 33  ? -54.459 -21.666 11.158  1.000 157.154 ? 362 VAL EEE C   1 
ATOM   6078  O O   . VAL E 1 33  ? -55.315 -22.013 10.315  1.000 158.289 ? 362 VAL EEE O   1 
ATOM   6079  C CB  . VAL E 1 33  ? -55.673 -21.320 13.347  1.000 166.174 ? 362 VAL EEE CB  1 
ATOM   6080  C CG1 . VAL E 1 33  ? -54.972 -22.554 13.903  1.000 164.656 ? 362 VAL EEE CG1 1 
ATOM   6081  C CG2 . VAL E 1 33  ? -55.984 -20.339 14.463  1.000 171.323 ? 362 VAL EEE CG2 1 
ATOM   6082  N N   . ALA E 1 34  ? -53.206 -22.117 11.213  1.000 154.149 ? 363 ALA EEE N   1 
ATOM   6083  C CA  . ALA E 1 34  ? -52.637 -23.157 10.331  1.000 152.918 ? 363 ALA EEE CA  1 
ATOM   6084  C C   . ALA E 1 34  ? -52.159 -24.325 11.194  1.000 155.381 ? 363 ALA EEE C   1 
ATOM   6085  O O   . ALA E 1 34  ? -51.303 -24.087 12.066  1.000 157.420 ? 363 ALA EEE O   1 
ATOM   6086  C CB  . ALA E 1 34  ? -51.498 -22.572 9.542   1.000 148.158 ? 363 ALA EEE CB  1 
ATOM   6087  N N   . ASP E 1 35  ? -52.696 -25.531 10.988  1.000 158.257 ? 364 ASP EEE N   1 
ATOM   6088  C CA  . ASP E 1 35  ? -52.019 -26.767 11.460  1.000 156.939 ? 364 ASP EEE CA  1 
ATOM   6089  C C   . ASP E 1 35  ? -50.918 -27.030 10.438  1.000 146.691 ? 364 ASP EEE C   1 
ATOM   6090  O O   . ASP E 1 35  ? -51.234 -27.514 9.343   1.000 145.140 ? 364 ASP EEE O   1 
ATOM   6091  C CB  . ASP E 1 35  ? -52.960 -27.959 11.659  1.000 166.304 ? 364 ASP EEE CB  1 
ATOM   6092  C CG  . ASP E 1 35  ? -52.387 -29.048 12.562  1.000 171.165 ? 364 ASP EEE CG  1 
ATOM   6093  O OD1 . ASP E 1 35  ? -51.147 -29.110 12.702  1.000 168.975 ? 364 ASP EEE OD1 1 
ATOM   6094  O OD2 . ASP E 1 35  ? -53.190 -29.815 13.146  1.000 180.681 ? 364 ASP EEE OD2 1 
ATOM   6095  N N   . TYR E 1 36  ? -49.692 -26.627 10.771  1.000 138.680 ? 365 TYR EEE N   1 
ATOM   6096  C CA  . TYR E 1 36  ? -48.504 -26.782 9.903   1.000 131.124 ? 365 TYR EEE CA  1 
ATOM   6097  C C   . TYR E 1 36  ? -48.192 -28.281 9.811   1.000 128.720 ? 365 TYR EEE C   1 
ATOM   6098  O O   . TYR E 1 36  ? -47.626 -28.704 8.797   1.000 123.576 ? 365 TYR EEE O   1 
ATOM   6099  C CB  . TYR E 1 36  ? -47.338 -25.934 10.422  1.000 128.849 ? 365 TYR EEE CB  1 
ATOM   6100  C CG  . TYR E 1 36  ? -47.573 -24.441 10.518  1.000 131.124 ? 365 TYR EEE CG  1 
ATOM   6101  C CD1 . TYR E 1 36  ? -47.396 -23.589 9.432   1.000 129.238 ? 365 TYR EEE CD1 1 
ATOM   6102  C CD2 . TYR E 1 36  ? -47.941 -23.863 11.723  1.000 135.878 ? 365 TYR EEE CD2 1 
ATOM   6103  C CE1 . TYR E 1 36  ? -47.583 -22.217 9.541   1.000 129.935 ? 365 TYR EEE CE1 1 
ATOM   6104  C CE2 . TYR E 1 36  ? -48.129 -22.492 11.851  1.000 136.874 ? 365 TYR EEE CE2 1 
ATOM   6105  C CZ  . TYR E 1 36  ? -47.954 -21.664 10.758  1.000 133.542 ? 365 TYR EEE CZ  1 
ATOM   6106  O OH  . TYR E 1 36  ? -48.148 -20.321 10.915  1.000 132.502 ? 365 TYR EEE OH  1 
ATOM   6107  N N   . SER E 1 37  ? -48.597 -29.068 10.815  1.000 132.374 ? 366 SER EEE N   1 
ATOM   6108  C CA  . SER E 1 37  ? -48.495 -30.556 10.809  1.000 134.393 ? 366 SER EEE CA  1 
ATOM   6109  C C   . SER E 1 37  ? -49.030 -31.097 9.475   1.000 134.293 ? 366 SER EEE C   1 
ATOM   6110  O O   . SER E 1 37  ? -48.419 -32.041 8.937   1.000 134.562 ? 366 SER EEE O   1 
ATOM   6111  C CB  . SER E 1 37  ? -49.182 -31.196 12.010  1.000 138.071 ? 366 SER EEE CB  1 
ATOM   6112  O OG  . SER E 1 37  ? -50.551 -31.479 11.752  1.000 140.106 ? 366 SER EEE OG  1 
ATOM   6113  N N   . VAL E 1 38  ? -50.091 -30.488 8.938   1.000 134.361 ? 367 VAL EEE N   1 
ATOM   6114  C CA  . VAL E 1 38  ? -50.679 -30.819 7.604   1.000 134.292 ? 367 VAL EEE CA  1 
ATOM   6115  C C   . VAL E 1 38  ? -49.558 -31.003 6.580   1.000 127.980 ? 367 VAL EEE C   1 
ATOM   6116  O O   . VAL E 1 38  ? -49.661 -31.941 5.783   1.000 128.609 ? 367 VAL EEE O   1 
ATOM   6117  C CB  . VAL E 1 38  ? -51.656 -29.728 7.127   1.000 139.146 ? 367 VAL EEE CB  1 
ATOM   6118  C CG1 . VAL E 1 38  ? -52.013 -29.876 5.651   1.000 139.297 ? 367 VAL EEE CG1 1 
ATOM   6119  C CG2 . VAL E 1 38  ? -52.915 -29.689 7.980   1.000 145.870 ? 367 VAL EEE CG2 1 
ATOM   6120  N N   . LEU E 1 39  ? -48.558 -30.116 6.590   1.000 122.809 ? 368 LEU EEE N   1 
ATOM   6121  C CA  . LEU E 1 39  ? -47.493 -30.037 5.552   1.000 119.143 ? 368 LEU EEE CA  1 
ATOM   6122  C C   . LEU E 1 39  ? -46.394 -31.067 5.842   1.000 118.726 ? 368 LEU EEE C   1 
ATOM   6123  O O   . LEU E 1 39  ? -46.124 -31.881 4.940   1.000 117.915 ? 368 LEU EEE O   1 
ATOM   6124  C CB  . LEU E 1 39  ? -46.925 -28.614 5.497   1.000 116.048 ? 368 LEU EEE CB  1 
ATOM   6125  C CG  . LEU E 1 39  ? -47.772 -27.587 4.745   1.000 117.101 ? 368 LEU EEE CG  1 
ATOM   6126  C CD1 . LEU E 1 39  ? -49.153 -27.441 5.368   1.000 121.791 ? 368 LEU EEE CD1 1 
ATOM   6127  C CD2 . LEU E 1 39  ? -47.081 -26.232 4.691   1.000 114.903 ? 368 LEU EEE CD2 1 
ATOM   6128  N N   . TYR E 1 40  ? -45.777 -31.032 7.035   1.000 119.801 ? 369 TYR EEE N   1 
ATOM   6129  C CA  . TYR E 1 40  ? -44.555 -31.823 7.356   1.000 118.751 ? 369 TYR EEE CA  1 
ATOM   6130  C C   . TYR E 1 40  ? -44.914 -33.305 7.529   1.000 118.433 ? 369 TYR EEE C   1 
ATOM   6131  O O   . TYR E 1 40  ? -44.104 -34.153 7.115   1.000 116.090 ? 369 TYR EEE O   1 
ATOM   6132  C CB  . TYR E 1 40  ? -43.740 -31.244 8.524   1.000 120.492 ? 369 TYR EEE CB  1 
ATOM   6133  C CG  . TYR E 1 40  ? -44.408 -31.017 9.862   1.000 125.718 ? 369 TYR EEE CG  1 
ATOM   6134  C CD1 . TYR E 1 40  ? -44.513 -32.022 10.815  1.000 129.677 ? 369 TYR EEE CD1 1 
ATOM   6135  C CD2 . TYR E 1 40  ? -44.840 -29.751 10.224  1.000 127.906 ? 369 TYR EEE CD2 1 
ATOM   6136  C CE1 . TYR E 1 40  ? -45.091 -31.790 12.058  1.000 132.846 ? 369 TYR EEE CE1 1 
ATOM   6137  C CE2 . TYR E 1 40  ? -45.414 -29.498 11.463  1.000 131.598 ? 369 TYR EEE CE2 1 
ATOM   6138  C CZ  . TYR E 1 40  ? -45.538 -30.519 12.389  1.000 133.409 ? 369 TYR EEE CZ  1 
ATOM   6139  O OH  . TYR E 1 40  ? -46.121 -30.247 13.596  1.000 135.072 ? 369 TYR EEE OH  1 
ATOM   6140  N N   . ASN E 1 41  ? -46.099 -33.621 8.050   1.000 120.958 ? 370 ASN EEE N   1 
ATOM   6141  C CA  . ASN E 1 41  ? -46.520 -35.031 8.267   1.000 127.020 ? 370 ASN EEE CA  1 
ATOM   6142  C C   . ASN E 1 41  ? -46.858 -35.678 6.907   1.000 129.998 ? 370 ASN EEE C   1 
ATOM   6143  O O   . ASN E 1 41  ? -47.030 -36.913 6.894   1.000 133.866 ? 370 ASN EEE O   1 
ATOM   6144  C CB  . ASN E 1 41  ? -47.633 -35.144 9.323   1.000 131.007 ? 370 ASN EEE CB  1 
ATOM   6145  C CG  . ASN E 1 41  ? -47.148 -35.077 10.766  1.000 131.323 ? 370 ASN EEE CG  1 
ATOM   6146  O OD1 . ASN E 1 41  ? -46.093 -35.601 11.110  1.000 131.137 ? 370 ASN EEE OD1 1 
ATOM   6147  N ND2 . ASN E 1 41  ? -47.923 -34.459 11.645  1.000 131.599 ? 370 ASN EEE ND2 1 
ATOM   6148  N N   . SER E 1 42  ? -46.910 -34.905 5.806   1.000 131.609 ? 371 SER EEE N   1 
ATOM   6149  C CA  . SER E 1 42  ? -47.161 -35.396 4.416   1.000 135.318 ? 371 SER EEE CA  1 
ATOM   6150  C C   . SER E 1 42  ? -45.851 -35.775 3.719   1.000 134.179 ? 371 SER EEE C   1 
ATOM   6151  O O   . SER E 1 42  ? -44.974 -34.899 3.593   1.000 130.592 ? 371 SER EEE O   1 
ATOM   6152  C CB  . SER E 1 42  ? -47.900 -34.390 3.567   1.000 136.515 ? 371 SER EEE CB  1 
ATOM   6153  O OG  . SER E 1 42  ? -47.757 -34.692 2.186   1.000 136.070 ? 371 SER EEE OG  1 
ATOM   6154  N N   . ALA E 1 43  ? -45.787 -37.003 3.194   1.000 137.708 ? 372 ALA EEE N   1 
ATOM   6155  C CA  . ALA E 1 43  ? -44.566 -37.642 2.646   1.000 138.788 ? 372 ALA EEE CA  1 
ATOM   6156  C C   . ALA E 1 43  ? -44.165 -37.021 1.297   1.000 136.163 ? 372 ALA EEE C   1 
ATOM   6157  O O   . ALA E 1 43  ? -42.983 -37.174 0.927   1.000 136.312 ? 372 ALA EEE O   1 
ATOM   6158  C CB  . ALA E 1 43  ? -44.776 -39.138 2.531   1.000 142.995 ? 372 ALA EEE CB  1 
ATOM   6159  N N   . SER E 1 44  ? -45.082 -36.338 0.601   1.000 134.041 ? 373 SER EEE N   1 
ATOM   6160  C CA  . SER E 1 44  ? -44.951 -35.962 -0.837  1.000 132.285 ? 373 SER EEE CA  1 
ATOM   6161  C C   . SER E 1 44  ? -44.354 -34.551 -1.020  1.000 126.174 ? 373 SER EEE C   1 
ATOM   6162  O O   . SER E 1 44  ? -45.009 -33.699 -1.642  1.000 125.361 ? 373 SER EEE O   1 
ATOM   6163  C CB  . SER E 1 44  ? -46.288 -36.112 -1.517  1.000 135.838 ? 373 SER EEE CB  1 
ATOM   6164  O OG  . SER E 1 44  ? -47.336 -35.899 -0.583  1.000 138.590 ? 373 SER EEE OG  1 
ATOM   6165  N N   . PHE E 1 45  ? -43.144 -34.320 -0.505  1.000 121.587 ? 374 PHE EEE N   1 
ATOM   6166  C CA  . PHE E 1 45  ? -42.281 -33.136 -0.767  1.000 117.850 ? 374 PHE EEE CA  1 
ATOM   6167  C C   . PHE E 1 45  ? -40.821 -33.603 -0.778  1.000 118.799 ? 374 PHE EEE C   1 
ATOM   6168  O O   . PHE E 1 45  ? -40.422 -34.285 0.183   1.000 120.122 ? 374 PHE EEE O   1 
ATOM   6169  C CB  . PHE E 1 45  ? -42.418 -32.064 0.319   1.000 115.913 ? 374 PHE EEE CB  1 
ATOM   6170  C CG  . PHE E 1 45  ? -43.750 -31.364 0.428   1.000 117.229 ? 374 PHE EEE CG  1 
ATOM   6171  C CD1 . PHE E 1 45  ? -44.299 -30.713 -0.666  1.000 119.243 ? 374 PHE EEE CD1 1 
ATOM   6172  C CD2 . PHE E 1 45  ? -44.427 -31.303 1.640   1.000 117.613 ? 374 PHE EEE CD2 1 
ATOM   6173  C CE1 . PHE E 1 45  ? -45.511 -30.043 -0.567  1.000 119.598 ? 374 PHE EEE CE1 1 
ATOM   6174  C CE2 . PHE E 1 45  ? -45.638 -30.634 1.744   1.000 118.571 ? 374 PHE EEE CE2 1 
ATOM   6175  C CZ  . PHE E 1 45  ? -46.173 -30.000 0.640   1.000 119.548 ? 374 PHE EEE CZ  1 
ATOM   6176  N N   . SER E 1 46  ? -40.043 -33.251 -1.807  1.000 120.816 ? 375 SER EEE N   1 
ATOM   6177  C CA  . SER E 1 46  ? -38.614 -33.656 -1.960  1.000 122.440 ? 375 SER EEE CA  1 
ATOM   6178  C C   . SER E 1 46  ? -37.774 -33.043 -0.835  1.000 120.082 ? 375 SER EEE C   1 
ATOM   6179  O O   . SER E 1 46  ? -36.990 -33.768 -0.197  1.000 119.161 ? 375 SER EEE O   1 
ATOM   6180  C CB  . SER E 1 46  ? -38.050 -33.269 -3.317  1.000 123.645 ? 375 SER EEE CB  1 
ATOM   6181  O OG  . SER E 1 46  ? -38.444 -34.200 -4.317  1.000 127.930 ? 375 SER EEE OG  1 
ATOM   6182  N N   . THR E 1 47  ? -37.963 -31.745 -0.614  1.000 119.401 ? 376 THR EEE N   1 
ATOM   6183  C CA  . THR E 1 47  ? -37.090 -30.856 0.186   1.000 119.001 ? 376 THR EEE CA  1 
ATOM   6184  C C   . THR E 1 47  ? -37.983 -30.047 1.133   1.000 117.090 ? 376 THR EEE C   1 
ATOM   6185  O O   . THR E 1 47  ? -38.753 -29.196 0.647   1.000 116.198 ? 376 THR EEE O   1 
ATOM   6186  C CB  . THR E 1 47  ? -36.263 -29.976 -0.765  1.000 121.534 ? 376 THR EEE CB  1 
ATOM   6187  O OG1 . THR E 1 47  ? -35.543 -30.834 -1.656  1.000 125.579 ? 376 THR EEE OG1 1 
ATOM   6188  C CG2 . THR E 1 47  ? -35.293 -29.041 -0.072  1.000 120.763 ? 376 THR EEE CG2 1 
ATOM   6189  N N   . PHE E 1 48  ? -37.903 -30.330 2.432   1.000 117.257 ? 377 PHE EEE N   1 
ATOM   6190  C CA  . PHE E 1 48  ? -38.511 -29.512 3.510   1.000 116.127 ? 377 PHE EEE CA  1 
ATOM   6191  C C   . PHE E 1 48  ? -37.384 -29.020 4.422   1.000 119.836 ? 377 PHE EEE C   1 
ATOM   6192  O O   . PHE E 1 48  ? -37.294 -29.441 5.605   1.000 124.058 ? 377 PHE EEE O   1 
ATOM   6193  C CB  . PHE E 1 48  ? -39.572 -30.328 4.247   1.000 114.998 ? 377 PHE EEE CB  1 
ATOM   6194  C CG  . PHE E 1 48  ? -40.719 -29.517 4.792   1.000 113.246 ? 377 PHE EEE CG  1 
ATOM   6195  C CD1 . PHE E 1 48  ? -40.511 -28.542 5.752   1.000 112.008 ? 377 PHE EEE CD1 1 
ATOM   6196  C CD2 . PHE E 1 48  ? -42.014 -29.739 4.352   1.000 114.058 ? 377 PHE EEE CD2 1 
ATOM   6197  C CE1 . PHE E 1 48  ? -41.571 -27.808 6.259   1.000 110.801 ? 377 PHE EEE CE1 1 
ATOM   6198  C CE2 . PHE E 1 48  ? -43.072 -29.010 4.866   1.000 112.887 ? 377 PHE EEE CE2 1 
ATOM   6199  C CZ  . PHE E 1 48  ? -42.850 -28.050 5.820   1.000 111.505 ? 377 PHE EEE CZ  1 
ATOM   6200  N N   . LYS E 1 49  ? -36.512 -28.177 3.863   1.000 121.470 ? 378 LYS EEE N   1 
ATOM   6201  C CA  . LYS E 1 49  ? -35.397 -27.539 4.608   1.000 123.371 ? 378 LYS EEE CA  1 
ATOM   6202  C C   . LYS E 1 49  ? -35.960 -26.328 5.347   1.000 121.211 ? 378 LYS EEE C   1 
ATOM   6203  O O   . LYS E 1 49  ? -36.514 -25.426 4.684   1.000 117.194 ? 378 LYS EEE O   1 
ATOM   6204  C CB  . LYS E 1 49  ? -34.245 -27.130 3.686   1.000 126.877 ? 378 LYS EEE CB  1 
ATOM   6205  C CG  . LYS E 1 49  ? -33.289 -28.255 3.301   1.000 130.956 ? 378 LYS EEE CG  1 
ATOM   6206  C CD  . LYS E 1 49  ? -32.188 -27.838 2.345   1.000 135.581 ? 378 LYS EEE CD  1 
ATOM   6207  C CE  . LYS E 1 49  ? -32.714 -27.019 1.180   1.000 139.637 ? 378 LYS EEE CE  1 
ATOM   6208  N NZ  . LYS E 1 49  ? -32.018 -27.327 -0.090  1.000 144.540 ? 378 LYS EEE NZ  1 
ATOM   6209  N N   . CYS E 1 50  ? -35.847 -26.346 6.673   1.000 121.976 ? 379 CYS EEE N   1 
ATOM   6210  C CA  . CYS E 1 50  ? -36.267 -25.241 7.566   1.000 123.645 ? 379 CYS EEE CA  1 
ATOM   6211  C C   . CYS E 1 50  ? -35.026 -24.519 8.082   1.000 126.159 ? 379 CYS EEE C   1 
ATOM   6212  O O   . CYS E 1 50  ? -34.100 -25.206 8.526   1.000 133.223 ? 379 CYS EEE O   1 
ATOM   6213  C CB  . CYS E 1 50  ? -37.111 -25.782 8.709   1.000 123.959 ? 379 CYS EEE CB  1 
ATOM   6214  S SG  . CYS E 1 50  ? -38.816 -26.083 8.190   1.000 124.009 ? 379 CYS EEE SG  1 
ATOM   6215  N N   . TYR E 1 51  ? -35.011 -23.192 7.998   1.000 125.303 ? 380 TYR EEE N   1 
ATOM   6216  C CA  . TYR E 1 51  ? -33.864 -22.343 8.405   1.000 126.641 ? 380 TYR EEE CA  1 
ATOM   6217  C C   . TYR E 1 51  ? -34.319 -21.412 9.533   1.000 126.280 ? 380 TYR EEE C   1 
ATOM   6218  O O   . TYR E 1 51  ? -35.191 -20.555 9.287   1.000 128.152 ? 380 TYR EEE O   1 
ATOM   6219  C CB  . TYR E 1 51  ? -33.326 -21.573 7.195   1.000 128.002 ? 380 TYR EEE CB  1 
ATOM   6220  C CG  . TYR E 1 51  ? -32.770 -22.426 6.079   1.000 127.370 ? 380 TYR EEE CG  1 
ATOM   6221  C CD1 . TYR E 1 51  ? -33.574 -22.905 5.056   1.000 125.265 ? 380 TYR EEE CD1 1 
ATOM   6222  C CD2 . TYR E 1 51  ? -31.420 -22.733 6.027   1.000 130.042 ? 380 TYR EEE CD2 1 
ATOM   6223  C CE1 . TYR E 1 51  ? -33.055 -23.678 4.026   1.000 125.571 ? 380 TYR EEE CE1 1 
ATOM   6224  C CE2 . TYR E 1 51  ? -30.884 -23.498 5.004   1.000 130.630 ? 380 TYR EEE CE2 1 
ATOM   6225  C CZ  . TYR E 1 51  ? -31.702 -23.981 3.998   1.000 128.341 ? 380 TYR EEE CZ  1 
ATOM   6226  O OH  . TYR E 1 51  ? -31.145 -24.733 2.998   1.000 128.010 ? 380 TYR EEE OH  1 
ATOM   6227  N N   . GLY E 1 52  ? -33.771 -21.601 10.738  1.000 124.276 ? 381 GLY EEE N   1 
ATOM   6228  C CA  . GLY E 1 52  ? -33.924 -20.677 11.879  1.000 121.924 ? 381 GLY EEE CA  1 
ATOM   6229  C C   . GLY E 1 52  ? -35.310 -20.718 12.499  1.000 117.779 ? 381 GLY EEE C   1 
ATOM   6230  O O   . GLY E 1 52  ? -35.686 -19.717 13.113  1.000 117.273 ? 381 GLY EEE O   1 
ATOM   6231  N N   . VAL E 1 53  ? -36.051 -21.820 12.357  1.000 114.353 ? 382 VAL EEE N   1 
ATOM   6232  C CA  . VAL E 1 53  ? -37.336 -22.014 13.088  1.000 115.694 ? 382 VAL EEE CA  1 
ATOM   6233  C C   . VAL E 1 53  ? -37.766 -23.480 13.011  1.000 113.015 ? 382 VAL EEE C   1 
ATOM   6234  O O   . VAL E 1 53  ? -37.832 -24.025 11.896  1.000 108.611 ? 382 VAL EEE O   1 
ATOM   6235  C CB  . VAL E 1 53  ? -38.441 -21.062 12.590  1.000 116.375 ? 382 VAL EEE CB  1 
ATOM   6236  C CG1 . VAL E 1 53  ? -38.869 -21.356 11.165  1.000 112.453 ? 382 VAL EEE CG1 1 
ATOM   6237  C CG2 . VAL E 1 53  ? -39.639 -21.084 13.532  1.000 121.006 ? 382 VAL EEE CG2 1 
ATOM   6238  N N   . SER E 1 54  ? -38.050 -24.071 14.174  1.000 114.922 ? 383 SER EEE N   1 
ATOM   6239  C CA  . SER E 1 54  ? -38.602 -25.439 14.311  1.000 117.592 ? 383 SER EEE CA  1 
ATOM   6240  C C   . SER E 1 54  ? -40.057 -25.398 13.871  1.000 119.882 ? 383 SER EEE C   1 
ATOM   6241  O O   . SER E 1 54  ? -40.863 -24.760 14.536  1.000 127.158 ? 383 SER EEE O   1 
ATOM   6242  C CB  . SER E 1 54  ? -38.458 -25.975 15.722  1.000 121.027 ? 383 SER EEE CB  1 
ATOM   6243  O OG  . SER E 1 54  ? -37.221 -26.671 15.891  1.000 120.877 ? 383 SER EEE OG  1 
ATOM   6244  N N   . PRO E 1 55  ? -40.430 -26.030 12.735  1.000 121.063 ? 384 PRO EEE N   1 
ATOM   6245  C CA  . PRO E 1 55  ? -41.822 -26.083 12.285  1.000 123.071 ? 384 PRO EEE CA  1 
ATOM   6246  C C   . PRO E 1 55  ? -42.688 -27.023 13.138  1.000 126.548 ? 384 PRO EEE C   1 
ATOM   6247  O O   . PRO E 1 55  ? -43.886 -26.815 13.233  1.000 128.779 ? 384 PRO EEE O   1 
ATOM   6248  C CB  . PRO E 1 55  ? -41.701 -26.644 10.866  1.000 121.163 ? 384 PRO EEE CB  1 
ATOM   6249  C CG  . PRO E 1 55  ? -40.504 -27.551 10.968  1.000 122.298 ? 384 PRO EEE CG  1 
ATOM   6250  C CD  . PRO E 1 55  ? -39.540 -26.758 11.823  1.000 121.870 ? 384 PRO EEE CD  1 
ATOM   6251  N N   . THR E 1 56  ? -42.060 -28.031 13.743  1.000 126.931 ? 385 THR EEE N   1 
ATOM   6252  C CA  . THR E 1 56  ? -42.711 -28.965 14.693  1.000 131.806 ? 385 THR EEE CA  1 
ATOM   6253  C C   . THR E 1 56  ? -43.250 -28.175 15.892  1.000 134.485 ? 385 THR EEE C   1 
ATOM   6254  O O   . THR E 1 56  ? -44.202 -28.663 16.535  1.000 139.333 ? 385 THR EEE O   1 
ATOM   6255  C CB  . THR E 1 56  ? -41.726 -30.043 15.158  1.000 133.711 ? 385 THR EEE CB  1 
ATOM   6256  O OG1 . THR E 1 56  ? -40.617 -29.390 15.778  1.000 133.435 ? 385 THR EEE OG1 1 
ATOM   6257  C CG2 . THR E 1 56  ? -41.248 -30.924 14.024  1.000 132.800 ? 385 THR EEE CG2 1 
ATOM   6258  N N   . LYS E 1 57  ? -42.669 -27.004 16.171  1.000 132.566 ? 386 LYS EEE N   1 
ATOM   6259  C CA  . LYS E 1 57  ? -42.879 -26.249 17.429  1.000 136.146 ? 386 LYS EEE CA  1 
ATOM   6260  C C   . LYS E 1 57  ? -43.754 -25.008 17.194  1.000 137.617 ? 386 LYS EEE C   1 
ATOM   6261  O O   . LYS E 1 57  ? -44.420 -24.598 18.161  1.000 139.807 ? 386 LYS EEE O   1 
ATOM   6262  C CB  . LYS E 1 57  ? -41.509 -25.932 18.038  1.000 137.291 ? 386 LYS EEE CB  1 
ATOM   6263  C CG  . LYS E 1 57  ? -40.782 -27.134 18.638  1.000 139.794 ? 386 LYS EEE CG  1 
ATOM   6264  C CD  . LYS E 1 57  ? -39.374 -26.842 19.159  1.000 139.525 ? 386 LYS EEE CD  1 
ATOM   6265  C CE  . LYS E 1 57  ? -39.332 -25.921 20.366  1.000 141.643 ? 386 LYS EEE CE  1 
ATOM   6266  N NZ  . LYS E 1 57  ? -40.071 -26.473 21.528  1.000 145.374 ? 386 LYS EEE NZ  1 
ATOM   6267  N N   . LEU E 1 58  ? -43.813 -24.458 15.974  1.000 157.451 ? 387 LEU EEE N   1 
ATOM   6268  C CA  . LEU E 1 58  ? -44.564 -23.195 15.701  1.000 161.014 ? 387 LEU EEE CA  1 
ATOM   6269  C C   . LEU E 1 58  ? -46.074 -23.455 15.574  1.000 169.165 ? 387 LEU EEE C   1 
ATOM   6270  O O   . LEU E 1 58  ? -46.810 -22.495 15.229  1.000 170.827 ? 387 LEU EEE O   1 
ATOM   6271  C CB  . LEU E 1 58  ? -44.015 -22.466 14.461  1.000 154.221 ? 387 LEU EEE CB  1 
ATOM   6272  C CG  . LEU E 1 58  ? -43.920 -23.226 13.134  1.000 148.025 ? 387 LEU EEE CG  1 
ATOM   6273  C CD1 . LEU E 1 58  ? -45.153 -24.058 12.829  1.000 148.822 ? 387 LEU EEE CD1 1 
ATOM   6274  C CD2 . LEU E 1 58  ? -43.678 -22.255 11.998  1.000 142.759 ? 387 LEU EEE CD2 1 
ATOM   6275  N N   . ASN E 1 59  ? -46.531 -24.686 15.836  1.000 177.023 ? 388 ASN EEE N   1 
ATOM   6276  C CA  . ASN E 1 59  ? -47.975 -24.989 16.015  1.000 182.761 ? 388 ASN EEE CA  1 
ATOM   6277  C C   . ASN E 1 59  ? -48.342 -24.748 17.488  1.000 188.428 ? 388 ASN EEE C   1 
ATOM   6278  O O   . ASN E 1 59  ? -49.396 -25.261 17.897  1.000 197.869 ? 388 ASN EEE O   1 
ATOM   6279  C CB  . ASN E 1 59  ? -48.366 -26.375 15.466  1.000 185.972 ? 388 ASN EEE CB  1 
ATOM   6280  C CG  . ASN E 1 59  ? -47.707 -27.565 16.138  1.000 190.188 ? 388 ASN EEE CG  1 
ATOM   6281  O OD1 . ASN E 1 59  ? -47.998 -27.885 17.292  1.000 196.490 ? 388 ASN EEE OD1 1 
ATOM   6282  N ND2 . ASN E 1 59  ? -46.868 -28.273 15.396  1.000 187.068 ? 388 ASN EEE ND2 1 
ATOM   6283  N N   . ASP E 1 60  ? -47.512 -24.007 18.248  1.000 185.430 ? 389 ASP EEE N   1 
ATOM   6284  C CA  . ASP E 1 60  ? -47.861 -23.462 19.594  1.000 189.028 ? 389 ASP EEE CA  1 
ATOM   6285  C C   . ASP E 1 60  ? -47.070 -22.166 19.861  1.000 183.019 ? 389 ASP EEE C   1 
ATOM   6286  O O   . ASP E 1 60  ? -46.635 -21.958 21.011  1.000 186.634 ? 389 ASP EEE O   1 
ATOM   6287  C CB  . ASP E 1 60  ? -47.718 -24.532 20.690  1.000 195.631 ? 389 ASP EEE CB  1 
ATOM   6288  C CG  . ASP E 1 60  ? -46.402 -25.300 20.728  1.000 194.713 ? 389 ASP EEE CG  1 
ATOM   6289  O OD1 . ASP E 1 60  ? -45.338 -24.652 20.829  1.000 192.807 ? 389 ASP EEE OD1 1 
ATOM   6290  O OD2 . ASP E 1 60  ? -46.452 -26.553 20.698  1.000 195.605 ? 389 ASP EEE OD2 1 
ATOM   6291  N N   . LEU E 1 61  ? -46.923 -21.315 18.839  1.000 174.019 ? 390 LEU EEE N   1 
ATOM   6292  C CA  . LEU E 1 61  ? -46.378 -19.930 18.938  1.000 170.735 ? 390 LEU EEE CA  1 
ATOM   6293  C C   . LEU E 1 61  ? -46.963 -19.072 17.808  1.000 168.848 ? 390 LEU EEE C   1 
ATOM   6294  O O   . LEU E 1 61  ? -47.030 -19.567 16.660  1.000 169.493 ? 390 LEU EEE O   1 
ATOM   6295  C CB  . LEU E 1 61  ? -44.849 -19.961 18.848  1.000 165.733 ? 390 LEU EEE CB  1 
ATOM   6296  C CG  . LEU E 1 61  ? -44.200 -18.636 18.433  1.000 161.627 ? 390 LEU EEE CG  1 
ATOM   6297  C CD1 . LEU E 1 61  ? -44.230 -17.634 19.577  1.000 165.510 ? 390 LEU EEE CD1 1 
ATOM   6298  C CD2 . LEU E 1 61  ? -42.778 -18.845 17.936  1.000 157.689 ? 390 LEU EEE CD2 1 
ATOM   6299  N N   . CYS E 1 62  ? -47.304 -17.813 18.105  1.000 169.619 ? 391 CYS EEE N   1 
ATOM   6300  C CA  . CYS E 1 62  ? -48.052 -16.884 17.211  1.000 167.401 ? 391 CYS EEE CA  1 
ATOM   6301  C C   . CYS E 1 62  ? -47.111 -15.878 16.532  1.000 162.213 ? 391 CYS EEE C   1 
ATOM   6302  O O   . CYS E 1 62  ? -46.493 -15.071 17.254  1.000 164.405 ? 391 CYS EEE O   1 
ATOM   6303  C CB  . CYS E 1 62  ? -49.126 -16.151 18.002  1.000 173.075 ? 391 CYS EEE CB  1 
ATOM   6304  S SG  . CYS E 1 62  ? -50.474 -17.241 18.527  1.000 179.597 ? 391 CYS EEE SG  1 
ATOM   6305  N N   . PHE E 1 63  ? -47.045 -15.917 15.193  1.000 156.442 ? 392 PHE EEE N   1 
ATOM   6306  C CA  . PHE E 1 63  ? -46.294 -14.970 14.325  1.000 151.064 ? 392 PHE EEE CA  1 
ATOM   6307  C C   . PHE E 1 63  ? -47.246 -13.935 13.722  1.000 150.976 ? 392 PHE EEE C   1 
ATOM   6308  O O   . PHE E 1 63  ? -48.400 -14.299 13.407  1.000 152.801 ? 392 PHE EEE O   1 
ATOM   6309  C CB  . PHE E 1 63  ? -45.610 -15.711 13.179  1.000 146.648 ? 392 PHE EEE CB  1 
ATOM   6310  C CG  . PHE E 1 63  ? -44.423 -16.530 13.599  1.000 147.133 ? 392 PHE EEE CG  1 
ATOM   6311  C CD1 . PHE E 1 63  ? -43.192 -15.924 13.807  1.000 146.883 ? 392 PHE EEE CD1 1 
ATOM   6312  C CD2 . PHE E 1 63  ? -44.539 -17.899 13.782  1.000 148.627 ? 392 PHE EEE CD2 1 
ATOM   6313  C CE1 . PHE E 1 63  ? -42.091 -16.674 14.186  1.000 147.389 ? 392 PHE EEE CE1 1 
ATOM   6314  C CE2 . PHE E 1 63  ? -43.437 -18.647 14.167  1.000 149.771 ? 392 PHE EEE CE2 1 
ATOM   6315  C CZ  . PHE E 1 63  ? -42.215 -18.035 14.361  1.000 149.314 ? 392 PHE EEE CZ  1 
ATOM   6316  N N   . THR E 1 64  ? -46.760 -12.701 13.540  1.000 148.484 ? 393 THR EEE N   1 
ATOM   6317  C CA  . THR E 1 64  ? -47.535 -11.546 13.008  1.000 149.050 ? 393 THR EEE CA  1 
ATOM   6318  C C   . THR E 1 64  ? -47.944 -11.830 11.562  1.000 146.481 ? 393 THR EEE C   1 
ATOM   6319  O O   . THR E 1 64  ? -49.118 -11.591 11.233  1.000 149.226 ? 393 THR EEE O   1 
ATOM   6320  C CB  . THR E 1 64  ? -46.753 -10.231 13.124  1.000 147.726 ? 393 THR EEE CB  1 
ATOM   6321  O OG1 . THR E 1 64  ? -45.375 -10.533 12.926  1.000 143.785 ? 393 THR EEE OG1 1 
ATOM   6322  C CG2 . THR E 1 64  ? -46.929 -9.547  14.461  1.000 152.478 ? 393 THR EEE CG2 1 
ATOM   6323  N N   . ASN E 1 65  ? -47.018 -12.330 10.741  1.000 144.245 ? 394 ASN EEE N   1 
ATOM   6324  C CA  . ASN E 1 65  ? -47.256 -12.611 9.299   1.000 142.192 ? 394 ASN EEE CA  1 
ATOM   6325  C C   . ASN E 1 65  ? -46.440 -13.818 8.835   1.000 135.656 ? 394 ASN EEE C   1 
ATOM   6326  O O   . ASN E 1 65  ? -45.244 -13.937 9.200   1.000 132.279 ? 394 ASN EEE O   1 
ATOM   6327  C CB  . ASN E 1 65  ? -46.921 -11.410 8.416   1.000 143.980 ? 394 ASN EEE CB  1 
ATOM   6328  C CG  . ASN E 1 65  ? -47.918 -10.287 8.584   1.000 150.363 ? 394 ASN EEE CG  1 
ATOM   6329  O OD1 . ASN E 1 65  ? -49.070 -10.423 8.177   1.000 153.733 ? 394 ASN EEE OD1 1 
ATOM   6330  N ND2 . ASN E 1 65  ? -47.495 -9.192  9.201   1.000 153.546 ? 394 ASN EEE ND2 1 
ATOM   6331  N N   . VAL E 1 66  ? -47.087 -14.665 8.041   1.000 131.823 ? 395 VAL EEE N   1 
ATOM   6332  C CA  . VAL E 1 66  ? -46.435 -15.738 7.251   1.000 128.024 ? 395 VAL EEE CA  1 
ATOM   6333  C C   . VAL E 1 66  ? -46.519 -15.327 5.785   1.000 126.380 ? 395 VAL EEE C   1 
ATOM   6334  O O   . VAL E 1 66  ? -47.640 -15.143 5.282   1.000 128.135 ? 395 VAL EEE O   1 
ATOM   6335  C CB  . VAL E 1 66  ? -47.099 -17.098 7.503   1.000 129.209 ? 395 VAL EEE CB  1 
ATOM   6336  C CG1 . VAL E 1 66  ? -46.447 -18.199 6.687   1.000 127.501 ? 395 VAL EEE CG1 1 
ATOM   6337  C CG2 . VAL E 1 66  ? -47.081 -17.440 8.979   1.000 132.379 ? 395 VAL EEE CG2 1 
ATOM   6338  N N   . TYR E 1 67  ? -45.362 -15.144 5.157   1.000 123.922 ? 396 TYR EEE N   1 
ATOM   6339  C CA  . TYR E 1 67  ? -45.225 -14.889 3.706   1.000 123.417 ? 396 TYR EEE CA  1 
ATOM   6340  C C   . TYR E 1 67  ? -44.954 -16.232 3.018   1.000 123.938 ? 396 TYR EEE C   1 
ATOM   6341  O O   . TYR E 1 67  ? -44.113 -17.002 3.517   1.000 125.006 ? 396 TYR EEE O   1 
ATOM   6342  C CB  . TYR E 1 67  ? -44.153 -13.821 3.474   1.000 121.305 ? 396 TYR EEE CB  1 
ATOM   6343  C CG  . TYR E 1 67  ? -44.487 -12.470 4.058   1.000 124.023 ? 396 TYR EEE CG  1 
ATOM   6344  C CD1 . TYR E 1 67  ? -45.775 -11.952 3.994   1.000 126.676 ? 396 TYR EEE CD1 1 
ATOM   6345  C CD2 . TYR E 1 67  ? -43.513 -11.691 4.661   1.000 125.216 ? 396 TYR EEE CD2 1 
ATOM   6346  C CE1 . TYR E 1 67  ? -46.090 -10.711 4.524   1.000 128.765 ? 396 TYR EEE CE1 1 
ATOM   6347  C CE2 . TYR E 1 67  ? -43.812 -10.441 5.189   1.000 128.651 ? 396 TYR EEE CE2 1 
ATOM   6348  C CZ  . TYR E 1 67  ? -45.107 -9.948  5.124   1.000 129.699 ? 396 TYR EEE CZ  1 
ATOM   6349  O OH  . TYR E 1 67  ? -45.434 -8.725  5.638   1.000 130.377 ? 396 TYR EEE OH  1 
ATOM   6350  N N   . ALA E 1 68  ? -45.688 -16.515 1.936   1.000 124.784 ? 397 ALA EEE N   1 
ATOM   6351  C CA  . ALA E 1 68  ? -45.579 -17.740 1.111   1.000 123.301 ? 397 ALA EEE CA  1 
ATOM   6352  C C   . ALA E 1 68  ? -45.209 -17.362 -0.330  1.000 123.007 ? 397 ALA EEE C   1 
ATOM   6353  O O   . ALA E 1 68  ? -46.097 -16.964 -1.109  1.000 124.700 ? 397 ALA EEE O   1 
ATOM   6354  C CB  . ALA E 1 68  ? -46.872 -18.512 1.170   1.000 125.550 ? 397 ALA EEE CB  1 
ATOM   6355  N N   . ASP E 1 69  ? -43.925 -17.481 -0.662  1.000 121.979 ? 398 ASP EEE N   1 
ATOM   6356  C CA  . ASP E 1 69  ? -43.370 -17.192 -2.008  1.000 122.506 ? 398 ASP EEE CA  1 
ATOM   6357  C C   . ASP E 1 69  ? -43.371 -18.508 -2.794  1.000 122.983 ? 398 ASP EEE C   1 
ATOM   6358  O O   . ASP E 1 69  ? -42.780 -19.486 -2.298  1.000 125.149 ? 398 ASP EEE O   1 
ATOM   6359  C CB  . ASP E 1 69  ? -41.985 -16.551 -1.879  1.000 122.043 ? 398 ASP EEE CB  1 
ATOM   6360  C CG  . ASP E 1 69  ? -41.934 -15.395 -0.887  1.000 121.199 ? 398 ASP EEE CG  1 
ATOM   6361  O OD1 . ASP E 1 69  ? -42.946 -14.672 -0.791  1.000 120.829 ? 398 ASP EEE OD1 1 
ATOM   6362  O OD2 . ASP E 1 69  ? -40.887 -15.228 -0.210  1.000 118.736 ? 398 ASP EEE OD2 1 
ATOM   6363  N N   . SER E 1 70  ? -44.047 -18.550 -3.944  1.000 122.727 ? 399 SER EEE N   1 
ATOM   6364  C CA  . SER E 1 70  ? -44.176 -19.761 -4.799  1.000 123.139 ? 399 SER EEE CA  1 
ATOM   6365  C C   . SER E 1 70  ? -43.576 -19.496 -6.186  1.000 120.308 ? 399 SER EEE C   1 
ATOM   6366  O O   . SER E 1 70  ? -43.793 -18.386 -6.716  1.000 121.591 ? 399 SER EEE O   1 
ATOM   6367  C CB  . SER E 1 70  ? -45.621 -20.209 -4.889  1.000 127.698 ? 399 SER EEE CB  1 
ATOM   6368  O OG  . SER E 1 70  ? -46.486 -19.126 -5.206  1.000 132.261 ? 399 SER EEE OG  1 
ATOM   6369  N N   . PHE E 1 71  ? -42.860 -20.477 -6.753  1.000 116.826 ? 400 PHE EEE N   1 
ATOM   6370  C CA  . PHE E 1 71  ? -42.277 -20.412 -8.121  1.000 116.868 ? 400 PHE EEE CA  1 
ATOM   6371  C C   . PHE E 1 71  ? -41.704 -21.768 -8.550  1.000 115.676 ? 400 PHE EEE C   1 
ATOM   6372  O O   . PHE E 1 71  ? -41.673 -22.689 -7.730  1.000 114.481 ? 400 PHE EEE O   1 
ATOM   6373  C CB  . PHE E 1 71  ? -41.177 -19.356 -8.172  1.000 117.930 ? 400 PHE EEE CB  1 
ATOM   6374  C CG  . PHE E 1 71  ? -40.077 -19.591 -7.176  1.000 119.239 ? 400 PHE EEE CG  1 
ATOM   6375  C CD1 . PHE E 1 71  ? -39.056 -20.485 -7.449  1.000 121.405 ? 400 PHE EEE CD1 1 
ATOM   6376  C CD2 . PHE E 1 71  ? -40.075 -18.926 -5.959  1.000 121.999 ? 400 PHE EEE CD2 1 
ATOM   6377  C CE1 . PHE E 1 71  ? -38.047 -20.704 -6.524  1.000 123.350 ? 400 PHE EEE CE1 1 
ATOM   6378  C CE2 . PHE E 1 71  ? -39.063 -19.140 -5.038  1.000 123.767 ? 400 PHE EEE CE2 1 
ATOM   6379  C CZ  . PHE E 1 71  ? -38.054 -20.033 -5.321  1.000 124.629 ? 400 PHE EEE CZ  1 
ATOM   6380  N N   . VAL E 1 72  ? -41.241 -21.860 -9.801  1.000 118.011 ? 401 VAL EEE N   1 
ATOM   6381  C CA  . VAL E 1 72  ? -40.714 -23.100 -10.449 1.000 119.875 ? 401 VAL EEE CA  1 
ATOM   6382  C C   . VAL E 1 72  ? -39.270 -22.869 -10.895 1.000 120.589 ? 401 VAL EEE C   1 
ATOM   6383  O O   . VAL E 1 72  ? -38.997 -21.840 -11.555 1.000 124.034 ? 401 VAL EEE O   1 
ATOM   6384  C CB  . VAL E 1 72  ? -41.565 -23.515 -11.663 1.000 122.666 ? 401 VAL EEE CB  1 
ATOM   6385  C CG1 . VAL E 1 72  ? -40.831 -24.491 -12.570 1.000 124.337 ? 401 VAL EEE CG1 1 
ATOM   6386  C CG2 . VAL E 1 72  ? -42.902 -24.088 -11.240 1.000 124.801 ? 401 VAL EEE CG2 1 
ATOM   6387  N N   . ILE E 1 73  ? -38.410 -23.844 -10.606 1.000 120.352 ? 402 ILE EEE N   1 
ATOM   6388  C CA  . ILE E 1 73  ? -37.001 -23.933 -11.089 1.000 122.584 ? 402 ILE EEE CA  1 
ATOM   6389  C C   . ILE E 1 73  ? -36.724 -25.402 -11.402 1.000 125.643 ? 402 ILE EEE C   1 
ATOM   6390  O O   . ILE E 1 73  ? -37.543 -26.248 -10.997 1.000 126.366 ? 402 ILE EEE O   1 
ATOM   6391  C CB  . ILE E 1 73  ? -36.018 -23.386 -10.035 1.000 121.552 ? 402 ILE EEE CB  1 
ATOM   6392  C CG1 . ILE E 1 73  ? -36.333 -23.927 -8.637  1.000 121.216 ? 402 ILE EEE CG1 1 
ATOM   6393  C CG2 . ILE E 1 73  ? -35.998 -21.868 -10.055 1.000 120.450 ? 402 ILE EEE CG2 1 
ATOM   6394  C CD1 . ILE E 1 73  ? -35.191 -23.837 -7.667  1.000 121.517 ? 402 ILE EEE CD1 1 
ATOM   6395  N N   . ARG E 1 74  ? -35.616 -25.700 -12.079 1.000 128.861 ? 403 ARG EEE N   1 
ATOM   6396  C CA  . ARG E 1 74  ? -35.215 -27.107 -12.339 1.000 134.569 ? 403 ARG EEE CA  1 
ATOM   6397  C C   . ARG E 1 74  ? -34.605 -27.667 -11.050 1.000 134.477 ? 403 ARG EEE C   1 
ATOM   6398  O O   . ARG E 1 74  ? -33.920 -26.906 -10.349 1.000 135.971 ? 403 ARG EEE O   1 
ATOM   6399  C CB  . ARG E 1 74  ? -34.315 -27.208 -13.576 1.000 140.284 ? 403 ARG EEE CB  1 
ATOM   6400  C CG  . ARG E 1 74  ? -32.910 -26.641 -13.442 1.000 142.477 ? 403 ARG EEE CG  1 
ATOM   6401  C CD  . ARG E 1 74  ? -32.254 -26.512 -14.812 1.000 146.667 ? 403 ARG EEE CD  1 
ATOM   6402  N NE  . ARG E 1 74  ? -30.866 -26.072 -14.751 1.000 148.099 ? 403 ARG EEE NE  1 
ATOM   6403  C CZ  . ARG E 1 74  ? -29.831 -26.853 -14.450 1.000 151.683 ? 403 ARG EEE CZ  1 
ATOM   6404  N NH1 . ARG E 1 74  ? -30.010 -28.132 -14.171 1.000 152.272 ? 403 ARG EEE NH1 1 
ATOM   6405  N NH2 . ARG E 1 74  ? -28.613 -26.344 -14.419 1.000 155.471 ? 403 ARG EEE NH2 1 
ATOM   6406  N N   . GLY E 1 75  ? -34.884 -28.937 -10.744 1.000 136.015 ? 404 GLY EEE N   1 
ATOM   6407  C CA  . GLY E 1 75  ? -34.506 -29.633 -9.496  1.000 138.196 ? 404 GLY EEE CA  1 
ATOM   6408  C C   . GLY E 1 75  ? -33.078 -29.358 -9.037  1.000 139.977 ? 404 GLY EEE C   1 
ATOM   6409  O O   . GLY E 1 75  ? -32.862 -29.270 -7.810  1.000 144.034 ? 404 GLY EEE O   1 
ATOM   6410  N N   . ASP E 1 76  ? -32.130 -29.243 -9.969  1.000 141.213 ? 405 ASP EEE N   1 
ATOM   6411  C CA  . ASP E 1 76  ? -30.692 -29.000 -9.676  1.000 143.134 ? 405 ASP EEE CA  1 
ATOM   6412  C C   . ASP E 1 76  ? -30.517 -27.786 -8.760  1.000 138.573 ? 405 ASP EEE C   1 
ATOM   6413  O O   . ASP E 1 76  ? -29.624 -27.821 -7.902  1.000 139.005 ? 405 ASP EEE O   1 
ATOM   6414  C CB  . ASP E 1 76  ? -29.900 -28.761 -10.961 1.000 148.695 ? 405 ASP EEE CB  1 
ATOM   6415  C CG  . ASP E 1 76  ? -29.453 -30.044 -11.633 1.000 156.707 ? 405 ASP EEE CG  1 
ATOM   6416  O OD1 . ASP E 1 76  ? -29.691 -31.121 -11.046 1.000 160.835 ? 405 ASP EEE OD1 1 
ATOM   6417  O OD2 . ASP E 1 76  ? -28.857 -29.954 -12.730 1.000 161.629 ? 405 ASP EEE OD2 1 
ATOM   6418  N N   . GLU E 1 77  ? -31.334 -26.753 -8.959  1.000 135.928 ? 406 GLU EEE N   1 
ATOM   6419  C CA  . GLU E 1 77  ? -31.156 -25.406 -8.358  1.000 135.883 ? 406 GLU EEE CA  1 
ATOM   6420  C C   . GLU E 1 77  ? -31.888 -25.314 -7.008  1.000 133.119 ? 406 GLU EEE C   1 
ATOM   6421  O O   . GLU E 1 77  ? -31.707 -24.289 -6.321  1.000 134.983 ? 406 GLU EEE O   1 
ATOM   6422  C CB  . GLU E 1 77  ? -31.646 -24.342 -9.347  1.000 138.547 ? 406 GLU EEE CB  1 
ATOM   6423  C CG  . GLU E 1 77  ? -30.925 -24.355 -10.699 1.000 144.005 ? 406 GLU EEE CG  1 
ATOM   6424  C CD  . GLU E 1 77  ? -31.629 -23.662 -11.865 1.000 144.465 ? 406 GLU EEE CD  1 
ATOM   6425  O OE1 . GLU E 1 77  ? -32.876 -23.555 -11.832 1.000 142.266 ? 406 GLU EEE OE1 1 
ATOM   6426  O OE2 . GLU E 1 77  ? -30.931 -23.246 -12.828 1.000 147.046 ? 406 GLU EEE OE2 1 
ATOM   6427  N N   . VAL E 1 78  ? -32.674 -26.325 -6.623  1.000 131.157 ? 407 VAL EEE N   1 
ATOM   6428  C CA  . VAL E 1 78  ? -33.389 -26.367 -5.308  1.000 127.610 ? 407 VAL EEE CA  1 
ATOM   6429  C C   . VAL E 1 78  ? -32.420 -25.996 -4.182  1.000 127.065 ? 407 VAL EEE C   1 
ATOM   6430  O O   . VAL E 1 78  ? -32.774 -25.125 -3.372  1.000 121.269 ? 407 VAL EEE O   1 
ATOM   6431  C CB  . VAL E 1 78  ? -34.026 -27.745 -5.067  1.000 130.158 ? 407 VAL EEE CB  1 
ATOM   6432  C CG1 . VAL E 1 78  ? -34.012 -28.159 -3.601  1.000 131.453 ? 407 VAL EEE CG1 1 
ATOM   6433  C CG2 . VAL E 1 78  ? -35.433 -27.781 -5.638  1.000 129.038 ? 407 VAL EEE CG2 1 
ATOM   6434  N N   . ARG E 1 79  ? -31.255 -26.651 -4.139  1.000 131.020 ? 408 ARG EEE N   1 
ATOM   6435  C CA  . ARG E 1 79  ? -30.161 -26.397 -3.164  1.000 134.574 ? 408 ARG EEE CA  1 
ATOM   6436  C C   . ARG E 1 79  ? -29.967 -24.892 -2.955  1.000 130.452 ? 408 ARG EEE C   1 
ATOM   6437  O O   . ARG E 1 79  ? -29.732 -24.475 -1.811  1.000 130.475 ? 408 ARG EEE O   1 
ATOM   6438  C CB  . ARG E 1 79  ? -28.815 -26.917 -3.673  1.000 144.668 ? 408 ARG EEE CB  1 
ATOM   6439  C CG  . ARG E 1 79  ? -28.691 -28.426 -3.824  1.000 155.462 ? 408 ARG EEE CG  1 
ATOM   6440  C CD  . ARG E 1 79  ? -27.230 -28.835 -3.950  1.000 169.551 ? 408 ARG EEE CD  1 
ATOM   6441  N NE  . ARG E 1 79  ? -26.354 -27.880 -4.644  1.000 178.274 ? 408 ARG EEE NE  1 
ATOM   6442  C CZ  . ARG E 1 79  ? -25.385 -27.135 -4.081  1.000 183.166 ? 408 ARG EEE CZ  1 
ATOM   6443  N NH1 . ARG E 1 79  ? -25.115 -27.214 -2.785  1.000 185.377 ? 408 ARG EEE NH1 1 
ATOM   6444  N NH2 . ARG E 1 79  ? -24.664 -26.316 -4.832  1.000 183.650 ? 408 ARG EEE NH2 1 
ATOM   6445  N N   . GLN E 1 80  ? -30.014 -24.115 -4.039  1.000 130.312 ? 409 GLN EEE N   1 
ATOM   6446  C CA  . GLN E 1 80  ? -29.632 -22.676 -4.071  1.000 131.018 ? 409 GLN EEE CA  1 
ATOM   6447  C C   . GLN E 1 80  ? -30.682 -21.815 -3.362  1.000 126.280 ? 409 GLN EEE C   1 
ATOM   6448  O O   . GLN E 1 80  ? -30.376 -20.630 -3.120  1.000 127.302 ? 409 GLN EEE O   1 
ATOM   6449  C CB  . GLN E 1 80  ? -29.439 -22.178 -5.507  1.000 134.723 ? 409 GLN EEE CB  1 
ATOM   6450  C CG  . GLN E 1 80  ? -28.138 -22.636 -6.158  1.000 140.762 ? 409 GLN EEE CG  1 
ATOM   6451  C CD  . GLN E 1 80  ? -27.543 -21.589 -7.072  1.000 145.609 ? 409 GLN EEE CD  1 
ATOM   6452  O OE1 . GLN E 1 80  ? -28.254 -20.791 -7.690  1.000 145.933 ? 409 GLN EEE OE1 1 
ATOM   6453  N NE2 . GLN E 1 80  ? -26.222 -21.588 -7.169  1.000 152.466 ? 409 GLN EEE NE2 1 
ATOM   6454  N N   . ILE E 1 81  ? -31.867 -22.361 -3.057  1.000 122.490 ? 410 ILE EEE N   1 
ATOM   6455  C CA  . ILE E 1 81  ? -32.923 -21.657 -2.261  1.000 118.332 ? 410 ILE EEE CA  1 
ATOM   6456  C C   . ILE E 1 81  ? -32.623 -21.853 -0.767  1.000 115.431 ? 410 ILE EEE C   1 
ATOM   6457  O O   . ILE E 1 81  ? -33.172 -22.784 -0.125  1.000 111.048 ? 410 ILE EEE O   1 
ATOM   6458  C CB  . ILE E 1 81  ? -34.346 -22.104 -2.649  1.000 118.771 ? 410 ILE EEE CB  1 
ATOM   6459  C CG1 . ILE E 1 81  ? -34.531 -22.203 -4.167  1.000 119.097 ? 410 ILE EEE CG1 1 
ATOM   6460  C CG2 . ILE E 1 81  ? -35.381 -21.185 -2.013  1.000 116.245 ? 410 ILE EEE CG2 1 
ATOM   6461  C CD1 . ILE E 1 81  ? -34.098 -20.974 -4.926  1.000 118.341 ? 410 ILE EEE CD1 1 
ATOM   6462  N N   . ALA E 1 82  ? -31.760 -20.982 -0.254  1.000 114.681 ? 411 ALA EEE N   1 
ATOM   6463  C CA  . ALA E 1 82  ? -31.149 -21.062 1.083   1.000 116.684 ? 411 ALA EEE CA  1 
ATOM   6464  C C   . ALA E 1 82  ? -30.289 -19.820 1.280   1.000 116.241 ? 411 ALA EEE C   1 
ATOM   6465  O O   . ALA E 1 82  ? -29.642 -19.342 0.349   1.000 114.463 ? 411 ALA EEE O   1 
ATOM   6466  C CB  . ALA E 1 82  ? -30.328 -22.326 1.205   1.000 120.618 ? 411 ALA EEE CB  1 
ATOM   6467  N N   . PRO E 1 83  ? -30.230 -19.283 2.511   1.000 116.677 ? 412 PRO EEE N   1 
ATOM   6468  C CA  . PRO E 1 83  ? -29.336 -18.171 2.814   1.000 118.780 ? 412 PRO EEE CA  1 
ATOM   6469  C C   . PRO E 1 83  ? -27.867 -18.506 2.539   1.000 121.479 ? 412 PRO EEE C   1 
ATOM   6470  O O   . PRO E 1 83  ? -27.492 -19.650 2.756   1.000 121.473 ? 412 PRO EEE O   1 
ATOM   6471  C CB  . PRO E 1 83  ? -29.544 -17.961 4.316   1.000 120.240 ? 412 PRO EEE CB  1 
ATOM   6472  C CG  . PRO E 1 83  ? -30.080 -19.282 4.804   1.000 120.036 ? 412 PRO EEE CG  1 
ATOM   6473  C CD  . PRO E 1 83  ? -30.973 -19.757 3.684   1.000 116.610 ? 412 PRO EEE CD  1 
ATOM   6474  N N   . GLY E 1 84  ? -27.102 -17.519 2.055   1.000 124.033 ? 413 GLY EEE N   1 
ATOM   6475  C CA  . GLY E 1 84  ? -25.635 -17.598 1.884   1.000 129.912 ? 413 GLY EEE CA  1 
ATOM   6476  C C   . GLY E 1 84  ? -25.212 -18.290 0.594   1.000 131.342 ? 413 GLY EEE C   1 
ATOM   6477  O O   . GLY E 1 84  ? -24.002 -18.244 0.277   1.000 132.897 ? 413 GLY EEE O   1 
ATOM   6478  N N   . GLN E 1 85  ? -26.162 -18.914 -0.116  1.000 130.106 ? 414 GLN EEE N   1 
ATOM   6479  C CA  . GLN E 1 85  ? -25.955 -19.528 -1.452  1.000 131.710 ? 414 GLN EEE CA  1 
ATOM   6480  C C   . GLN E 1 85  ? -25.689 -18.412 -2.464  1.000 131.636 ? 414 GLN EEE C   1 
ATOM   6481  O O   . GLN E 1 85  ? -26.210 -17.290 -2.257  1.000 127.521 ? 414 GLN EEE O   1 
ATOM   6482  C CB  . GLN E 1 85  ? -27.172 -20.353 -1.877  1.000 130.676 ? 414 GLN EEE CB  1 
ATOM   6483  C CG  . GLN E 1 85  ? -27.364 -21.616 -1.047  1.000 133.483 ? 414 GLN EEE CG  1 
ATOM   6484  C CD  . GLN E 1 85  ? -26.435 -22.743 -1.426  1.000 139.747 ? 414 GLN EEE CD  1 
ATOM   6485  O OE1 . GLN E 1 85  ? -26.004 -22.863 -2.573  1.000 144.250 ? 414 GLN EEE OE1 1 
ATOM   6486  N NE2 . GLN E 1 85  ? -26.130 -23.589 -0.455  1.000 144.120 ? 414 GLN EEE NE2 1 
ATOM   6487  N N   . THR E 1 86  ? -24.919 -18.726 -3.513  1.000 135.240 ? 415 THR EEE N   1 
ATOM   6488  C CA  . THR E 1 86  ? -24.600 -17.815 -4.646  1.000 136.994 ? 415 THR EEE CA  1 
ATOM   6489  C C   . THR E 1 86  ? -24.580 -18.605 -5.957  1.000 136.584 ? 415 THR EEE C   1 
ATOM   6490  O O   . THR E 1 86  ? -24.306 -19.826 -5.921  1.000 136.635 ? 415 THR EEE O   1 
ATOM   6491  C CB  . THR E 1 86  ? -23.266 -17.081 -4.446  1.000 141.977 ? 415 THR EEE CB  1 
ATOM   6492  O OG1 . THR E 1 86  ? -22.290 -18.068 -4.117  1.000 145.793 ? 415 THR EEE OG1 1 
ATOM   6493  C CG2 . THR E 1 86  ? -23.313 -16.017 -3.369  1.000 141.789 ? 415 THR EEE CG2 1 
ATOM   6494  N N   . GLY E 1 87  ? -24.843 -17.906 -7.063  1.000 135.439 ? 416 GLY EEE N   1 
ATOM   6495  C CA  . GLY E 1 87  ? -24.968 -18.479 -8.413  1.000 136.001 ? 416 GLY EEE CA  1 
ATOM   6496  C C   . GLY E 1 87  ? -26.006 -17.716 -9.198  1.000 132.494 ? 416 GLY EEE C   1 
ATOM   6497  O O   . GLY E 1 87  ? -26.229 -16.539 -8.872  1.000 129.087 ? 416 GLY EEE O   1 
ATOM   6498  N N   . LYS E 1 88  ? -26.632 -18.371 -10.176 1.000 134.387 ? 417 LYS EEE N   1 
ATOM   6499  C CA  . LYS E 1 88  ? -27.606 -17.728 -11.096 1.000 137.224 ? 417 LYS EEE CA  1 
ATOM   6500  C C   . LYS E 1 88  ? -28.883 -17.430 -10.312 1.000 131.208 ? 417 LYS EEE C   1 
ATOM   6501  O O   . LYS E 1 88  ? -29.262 -16.250 -10.207 1.000 129.573 ? 417 LYS EEE O   1 
ATOM   6502  C CB  . LYS E 1 88  ? -27.886 -18.601 -12.327 1.000 142.748 ? 417 LYS EEE CB  1 
ATOM   6503  C CG  . LYS E 1 88  ? -26.656 -19.029 -13.124 1.000 152.189 ? 417 LYS EEE CG  1 
ATOM   6504  C CD  . LYS E 1 88  ? -25.684 -17.892 -13.466 1.000 158.660 ? 417 LYS EEE CD  1 
ATOM   6505  C CE  . LYS E 1 88  ? -24.273 -18.104 -12.940 1.000 163.504 ? 417 LYS EEE CE  1 
ATOM   6506  N NZ  . LYS E 1 88  ? -23.673 -16.859 -12.392 1.000 164.131 ? 417 LYS EEE NZ  1 
ATOM   6507  N N   . ILE E 1 89  ? -29.494 -18.469 -9.753  1.000 129.220 ? 418 ILE EEE N   1 
ATOM   6508  C CA  . ILE E 1 89  ? -30.815 -18.381 -9.068  1.000 126.994 ? 418 ILE EEE CA  1 
ATOM   6509  C C   . ILE E 1 89  ? -30.636 -17.555 -7.792  1.000 126.412 ? 418 ILE EEE C   1 
ATOM   6510  O O   . ILE E 1 89  ? -31.420 -16.600 -7.572  1.000 123.355 ? 418 ILE EEE O   1 
ATOM   6511  C CB  . ILE E 1 89  ? -31.372 -19.788 -8.777  1.000 126.397 ? 418 ILE EEE CB  1 
ATOM   6512  C CG1 . ILE E 1 89  ? -31.428 -20.664 -10.033 1.000 128.246 ? 418 ILE EEE CG1 1 
ATOM   6513  C CG2 . ILE E 1 89  ? -32.732 -19.701 -8.112  1.000 124.588 ? 418 ILE EEE CG2 1 
ATOM   6514  C CD1 . ILE E 1 89  ? -32.115 -20.019 -11.216 1.000 128.072 ? 418 ILE EEE CD1 1 
ATOM   6515  N N   . ALA E 1 90  ? -29.631 -17.916 -6.995  1.000 128.766 ? 419 ALA EEE N   1 
ATOM   6516  C CA  . ALA E 1 90  ? -29.296 -17.269 -5.709  1.000 129.235 ? 419 ALA EEE CA  1 
ATOM   6517  C C   . ALA E 1 90  ? -29.264 -15.752 -5.891  1.000 129.863 ? 419 ALA EEE C   1 
ATOM   6518  O O   . ALA E 1 90  ? -30.058 -15.070 -5.221  1.000 128.040 ? 419 ALA EEE O   1 
ATOM   6519  C CB  . ALA E 1 90  ? -27.966 -17.778 -5.216  1.000 132.385 ? 419 ALA EEE CB  1 
ATOM   6520  N N   . ASP E 1 91  ? -28.417 -15.263 -6.799  1.000 134.152 ? 420 ASP EEE N   1 
ATOM   6521  C CA  . ASP E 1 91  ? -27.967 -13.847 -6.815  1.000 137.767 ? 420 ASP EEE CA  1 
ATOM   6522  C C   . ASP E 1 91  ? -28.761 -13.003 -7.820  1.000 135.289 ? 420 ASP EEE C   1 
ATOM   6523  O O   . ASP E 1 91  ? -28.721 -11.766 -7.658  1.000 138.890 ? 420 ASP EEE O   1 
ATOM   6524  C CB  . ASP E 1 91  ? -26.463 -13.746 -7.088  1.000 146.538 ? 420 ASP EEE CB  1 
ATOM   6525  C CG  . ASP E 1 91  ? -25.600 -14.113 -5.893  1.000 151.221 ? 420 ASP EEE CG  1 
ATOM   6526  O OD1 . ASP E 1 91  ? -26.002 -13.777 -4.752  1.000 150.878 ? 420 ASP EEE OD1 1 
ATOM   6527  O OD2 . ASP E 1 91  ? -24.528 -14.725 -6.111  1.000 158.588 ? 420 ASP EEE OD2 1 
ATOM   6528  N N   . TYR E 1 92  ? -29.431 -13.601 -8.817  1.000 131.056 ? 421 TYR EEE N   1 
ATOM   6529  C CA  . TYR E 1 92  ? -30.074 -12.838 -9.924  1.000 131.008 ? 421 TYR EEE CA  1 
ATOM   6530  C C   . TYR E 1 92  ? -31.599 -13.063 -9.987  1.000 128.718 ? 421 TYR EEE C   1 
ATOM   6531  O O   . TYR E 1 92  ? -32.248 -12.356 -10.790 1.000 130.065 ? 421 TYR EEE O   1 
ATOM   6532  C CB  . TYR E 1 92  ? -29.412 -13.159 -11.272 1.000 132.396 ? 421 TYR EEE CB  1 
ATOM   6533  C CG  . TYR E 1 92  ? -27.941 -12.821 -11.395 1.000 133.999 ? 421 TYR EEE CG  1 
ATOM   6534  C CD1 . TYR E 1 92  ? -27.445 -11.580 -11.030 1.000 134.989 ? 421 TYR EEE CD1 1 
ATOM   6535  C CD2 . TYR E 1 92  ? -27.037 -13.740 -11.909 1.000 135.979 ? 421 TYR EEE CD2 1 
ATOM   6536  C CE1 . TYR E 1 92  ? -26.100 -11.267 -11.166 1.000 139.519 ? 421 TYR EEE CE1 1 
ATOM   6537  C CE2 . TYR E 1 92  ? -25.687 -13.454 -12.033 1.000 139.369 ? 421 TYR EEE CE2 1 
ATOM   6538  C CZ  . TYR E 1 92  ? -25.215 -12.213 -11.656 1.000 141.499 ? 421 TYR EEE CZ  1 
ATOM   6539  O OH  . TYR E 1 92  ? -23.885 -11.936 -11.785 1.000 147.375 ? 421 TYR EEE OH  1 
ATOM   6540  N N   . ASN E 1 93  ? -32.187 -13.956 -9.176  1.000 125.289 ? 422 ASN EEE N   1 
ATOM   6541  C CA  . ASN E 1 93  ? -33.616 -14.357 -9.342  1.000 122.980 ? 422 ASN EEE CA  1 
ATOM   6542  C C   . ASN E 1 93  ? -34.408 -14.245 -8.037  1.000 121.885 ? 422 ASN EEE C   1 
ATOM   6543  O O   . ASN E 1 93  ? -35.357 -13.419 -8.013  1.000 123.811 ? 422 ASN EEE O   1 
ATOM   6544  C CB  . ASN E 1 93  ? -33.727 -15.760 -9.930  1.000 121.342 ? 422 ASN EEE CB  1 
ATOM   6545  C CG  . ASN E 1 93  ? -33.155 -15.803 -11.327 1.000 122.586 ? 422 ASN EEE CG  1 
ATOM   6546  O OD1 . ASN E 1 93  ? -33.895 -15.729 -12.298 1.000 122.018 ? 422 ASN EEE OD1 1 
ATOM   6547  N ND2 . ASN E 1 93  ? -31.837 -15.859 -11.434 1.000 122.556 ? 422 ASN EEE ND2 1 
ATOM   6548  N N   . TYR E 1 94  ? -34.055 -15.051 -7.025  1.000 120.493 ? 423 TYR EEE N   1 
ATOM   6549  C CA  . TYR E 1 94  ? -34.700 -15.088 -5.681  1.000 117.987 ? 423 TYR EEE CA  1 
ATOM   6550  C C   . TYR E 1 94  ? -33.628 -15.221 -4.592  1.000 116.387 ? 423 TYR EEE C   1 
ATOM   6551  O O   . TYR E 1 94  ? -33.145 -16.344 -4.358  1.000 112.954 ? 423 TYR EEE O   1 
ATOM   6552  C CB  . TYR E 1 94  ? -35.715 -16.232 -5.622  1.000 117.368 ? 423 TYR EEE CB  1 
ATOM   6553  C CG  . TYR E 1 94  ? -36.529 -16.300 -4.355  1.000 117.533 ? 423 TYR EEE CG  1 
ATOM   6554  C CD1 . TYR E 1 94  ? -37.479 -15.337 -4.068  1.000 119.353 ? 423 TYR EEE CD1 1 
ATOM   6555  C CD2 . TYR E 1 94  ? -36.363 -17.328 -3.442  1.000 116.834 ? 423 TYR EEE CD2 1 
ATOM   6556  C CE1 . TYR E 1 94  ? -38.239 -15.386 -2.909  1.000 118.862 ? 423 TYR EEE CE1 1 
ATOM   6557  C CE2 . TYR E 1 94  ? -37.114 -17.395 -2.279  1.000 115.341 ? 423 TYR EEE CE2 1 
ATOM   6558  C CZ  . TYR E 1 94  ? -38.057 -16.421 -2.009  1.000 116.970 ? 423 TYR EEE CZ  1 
ATOM   6559  O OH  . TYR E 1 94  ? -38.790 -16.465 -0.858  1.000 118.443 ? 423 TYR EEE OH  1 
ATOM   6560  N N   . LYS E 1 95  ? -33.254 -14.103 -3.962  1.000 119.418 ? 424 LYS EEE N   1 
ATOM   6561  C CA  . LYS E 1 95  ? -32.245 -14.081 -2.870  1.000 123.082 ? 424 LYS EEE CA  1 
ATOM   6562  C C   . LYS E 1 95  ? -32.986 -14.274 -1.553  1.000 121.291 ? 424 LYS EEE C   1 
ATOM   6563  O O   . LYS E 1 95  ? -34.118 -13.778 -1.457  1.000 121.310 ? 424 LYS EEE O   1 
ATOM   6564  C CB  . LYS E 1 95  ? -31.449 -12.770 -2.833  1.000 129.500 ? 424 LYS EEE CB  1 
ATOM   6565  C CG  . LYS E 1 95  ? -30.175 -12.798 -1.987  1.000 134.513 ? 424 LYS EEE CG  1 
ATOM   6566  C CD  . LYS E 1 95  ? -28.873 -12.934 -2.787  1.000 138.689 ? 424 LYS EEE CD  1 
ATOM   6567  C CE  . LYS E 1 95  ? -27.615 -12.997 -1.933  1.000 143.571 ? 424 LYS EEE CE  1 
ATOM   6568  N NZ  . LYS E 1 95  ? -27.291 -14.375 -1.477  1.000 144.130 ? 424 LYS EEE NZ  1 
ATOM   6569  N N   . LEU E 1 96  ? -32.369 -14.983 -0.606  1.000 121.548 ? 425 LEU EEE N   1 
ATOM   6570  C CA  . LEU E 1 96  ? -32.828 -15.094 0.805   1.000 124.240 ? 425 LEU EEE CA  1 
ATOM   6571  C C   . LEU E 1 96  ? -31.781 -14.451 1.706   1.000 127.138 ? 425 LEU EEE C   1 
ATOM   6572  O O   . LEU E 1 96  ? -30.583 -14.581 1.456   1.000 129.743 ? 425 LEU EEE O   1 
ATOM   6573  C CB  . LEU E 1 96  ? -33.048 -16.563 1.189   1.000 123.893 ? 425 LEU EEE CB  1 
ATOM   6574  C CG  . LEU E 1 96  ? -34.361 -17.193 0.715   1.000 123.592 ? 425 LEU EEE CG  1 
ATOM   6575  C CD1 . LEU E 1 96  ? -34.463 -18.651 1.134   1.000 123.088 ? 425 LEU EEE CD1 1 
ATOM   6576  C CD2 . LEU E 1 96  ? -35.570 -16.418 1.210   1.000 123.937 ? 425 LEU EEE CD2 1 
ATOM   6577  N N   . PRO E 1 97  ? -32.203 -13.747 2.780   1.000 128.653 ? 426 PRO EEE N   1 
ATOM   6578  C CA  . PRO E 1 97  ? -31.271 -13.093 3.696   1.000 132.983 ? 426 PRO EEE CA  1 
ATOM   6579  C C   . PRO E 1 97  ? -30.604 -14.090 4.644   1.000 134.789 ? 426 PRO EEE C   1 
ATOM   6580  O O   . PRO E 1 97  ? -31.170 -15.129 4.855   1.000 131.729 ? 426 PRO EEE O   1 
ATOM   6581  C CB  . PRO E 1 97  ? -32.170 -12.146 4.495   1.000 134.890 ? 426 PRO EEE CB  1 
ATOM   6582  C CG  . PRO E 1 97  ? -33.498 -12.867 4.526   1.000 132.048 ? 426 PRO EEE CG  1 
ATOM   6583  C CD  . PRO E 1 97  ? -33.605 -13.551 3.178   1.000 127.876 ? 426 PRO EEE CD  1 
ATOM   6584  N N   . ASP E 1 98  ? -29.452 -13.722 5.207   1.000 141.213 ? 427 ASP EEE N   1 
ATOM   6585  C CA  . ASP E 1 98  ? -28.610 -14.608 6.058   1.000 145.748 ? 427 ASP EEE CA  1 
ATOM   6586  C C   . ASP E 1 98  ? -29.397 -14.977 7.332   1.000 147.293 ? 427 ASP EEE C   1 
ATOM   6587  O O   . ASP E 1 98  ? -29.309 -16.135 7.801   1.000 152.439 ? 427 ASP EEE O   1 
ATOM   6588  C CB  . ASP E 1 98  ? -27.257 -13.944 6.342   1.000 151.420 ? 427 ASP EEE CB  1 
ATOM   6589  C CG  . ASP E 1 98  ? -26.644 -13.245 5.137   1.000 154.426 ? 427 ASP EEE CG  1 
ATOM   6590  O OD1 . ASP E 1 98  ? -26.660 -13.839 4.029   1.000 154.846 ? 427 ASP EEE OD1 1 
ATOM   6591  O OD2 . ASP E 1 98  ? -26.174 -12.101 5.308   1.000 159.323 ? 427 ASP EEE OD2 1 
ATOM   6592  N N   . ASP E 1 99  ? -30.161 -14.028 7.871   1.000 145.250 ? 428 ASP EEE N   1 
ATOM   6593  C CA  . ASP E 1 99  ? -31.038 -14.206 9.059   1.000 141.776 ? 428 ASP EEE CA  1 
ATOM   6594  C C   . ASP E 1 99  ? -32.434 -14.591 8.567   1.000 134.006 ? 428 ASP EEE C   1 
ATOM   6595  O O   . ASP E 1 99  ? -33.413 -13.985 9.013   1.000 135.023 ? 428 ASP EEE O   1 
ATOM   6596  C CB  . ASP E 1 99  ? -31.054 -12.945 9.929   1.000 147.982 ? 428 ASP EEE CB  1 
ATOM   6597  C CG  . ASP E 1 99  ? -31.422 -11.670 9.182   1.000 152.000 ? 428 ASP EEE CG  1 
ATOM   6598  O OD1 . ASP E 1 99  ? -32.144 -11.768 8.152   1.000 149.318 ? 428 ASP EEE OD1 1 
ATOM   6599  O OD2 . ASP E 1 99  ? -30.971 -10.581 9.624   1.000 158.923 ? 428 ASP EEE OD2 1 
ATOM   6600  N N   . PHE E 1 100 ? -32.517 -15.563 7.663   1.000 126.576 ? 429 PHE EEE N   1 
ATOM   6601  C CA  . PHE E 1 100 ? -33.804 -16.101 7.154   1.000 122.511 ? 429 PHE EEE CA  1 
ATOM   6602  C C   . PHE E 1 100 ? -34.401 -16.985 8.243   1.000 120.526 ? 429 PHE EEE C   1 
ATOM   6603  O O   . PHE E 1 100 ? -33.650 -17.795 8.823   1.000 119.350 ? 429 PHE EEE O   1 
ATOM   6604  C CB  . PHE E 1 100 ? -33.613 -16.884 5.855   1.000 120.234 ? 429 PHE EEE CB  1 
ATOM   6605  C CG  . PHE E 1 100 ? -34.855 -17.575 5.347   1.000 116.401 ? 429 PHE EEE CG  1 
ATOM   6606  C CD1 . PHE E 1 100 ? -36.034 -16.870 5.174   1.000 115.469 ? 429 PHE EEE CD1 1 
ATOM   6607  C CD2 . PHE E 1 100 ? -34.845 -18.927 5.035   1.000 113.592 ? 429 PHE EEE CD2 1 
ATOM   6608  C CE1 . PHE E 1 100 ? -37.170 -17.503 4.693   1.000 113.395 ? 429 PHE EEE CE1 1 
ATOM   6609  C CE2 . PHE E 1 100 ? -35.986 -19.559 4.563   1.000 110.598 ? 429 PHE EEE CE2 1 
ATOM   6610  C CZ  . PHE E 1 100 ? -37.144 -18.843 4.387   1.000 110.779 ? 429 PHE EEE CZ  1 
ATOM   6611  N N   . THR E 1 101 ? -35.693 -16.809 8.516   1.000 119.170 ? 430 THR EEE N   1 
ATOM   6612  C CA  . THR E 1 101 ? -36.453 -17.575 9.532   1.000 121.462 ? 430 THR EEE CA  1 
ATOM   6613  C C   . THR E 1 101 ? -37.707 -18.137 8.871   1.000 120.444 ? 430 THR EEE C   1 
ATOM   6614  O O   . THR E 1 101 ? -38.804 -17.607 9.118   1.000 122.586 ? 430 THR EEE O   1 
ATOM   6615  C CB  . THR E 1 101 ? -36.780 -16.697 10.743  1.000 126.138 ? 430 THR EEE CB  1 
ATOM   6616  O OG1 . THR E 1 101 ? -37.607 -15.623 10.301  1.000 128.720 ? 430 THR EEE OG1 1 
ATOM   6617  C CG2 . THR E 1 101 ? -35.544 -16.136 11.409  1.000 129.799 ? 430 THR EEE CG2 1 
ATOM   6618  N N   . GLY E 1 102 ? -37.529 -19.168 8.052   1.000 119.592 ? 431 GLY EEE N   1 
ATOM   6619  C CA  . GLY E 1 102 ? -38.617 -19.820 7.302   1.000 120.074 ? 431 GLY EEE CA  1 
ATOM   6620  C C   . GLY E 1 102 ? -38.194 -21.181 6.784   1.000 119.821 ? 431 GLY EEE C   1 
ATOM   6621  O O   . GLY E 1 102 ? -37.152 -21.694 7.246   1.000 121.075 ? 431 GLY EEE O   1 
ATOM   6622  N N   . CYS E 1 103 ? -38.973 -21.758 5.870   1.000 119.537 ? 432 CYS EEE N   1 
ATOM   6623  C CA  . CYS E 1 103 ? -38.694 -23.087 5.271   1.000 118.368 ? 432 CYS EEE CA  1 
ATOM   6624  C C   . CYS E 1 103 ? -38.896 -23.037 3.759   1.000 116.563 ? 432 CYS EEE C   1 
ATOM   6625  O O   . CYS E 1 103 ? -39.736 -22.257 3.269   1.000 117.944 ? 432 CYS EEE O   1 
ATOM   6626  C CB  . CYS E 1 103 ? -39.568 -24.177 5.873   1.000 119.862 ? 432 CYS EEE CB  1 
ATOM   6627  S SG  . CYS E 1 103 ? -39.483 -24.220 7.681   1.000 125.362 ? 432 CYS EEE SG  1 
ATOM   6628  N N   . VAL E 1 104 ? -38.107 -23.851 3.073   1.000 114.075 ? 433 VAL EEE N   1 
ATOM   6629  C CA  . VAL E 1 104 ? -38.117 -24.040 1.603   1.000 112.305 ? 433 VAL EEE CA  1 
ATOM   6630  C C   . VAL E 1 104 ? -38.757 -25.403 1.371   1.000 111.772 ? 433 VAL EEE C   1 
ATOM   6631  O O   . VAL E 1 104 ? -38.241 -26.394 1.925   1.000 112.899 ? 433 VAL EEE O   1 
ATOM   6632  C CB  . VAL E 1 104 ? -36.675 -23.957 1.078   1.000 114.666 ? 433 VAL EEE CB  1 
ATOM   6633  C CG1 . VAL E 1 104 ? -36.519 -24.497 -0.330  1.000 115.461 ? 433 VAL EEE CG1 1 
ATOM   6634  C CG2 . VAL E 1 104 ? -36.143 -22.540 1.191   1.000 115.486 ? 433 VAL EEE CG2 1 
ATOM   6635  N N   . ILE E 1 105 ? -39.876 -25.431 0.649   1.000 111.410 ? 434 ILE EEE N   1 
ATOM   6636  C CA  . ILE E 1 105 ? -40.665 -26.671 0.385   1.000 112.946 ? 434 ILE EEE CA  1 
ATOM   6637  C C   . ILE E 1 105 ? -40.741 -26.874 -1.130  1.000 111.750 ? 434 ILE EEE C   1 
ATOM   6638  O O   . ILE E 1 105 ? -41.278 -25.982 -1.816  1.000 112.131 ? 434 ILE EEE O   1 
ATOM   6639  C CB  . ILE E 1 105 ? -42.057 -26.593 1.043   1.000 114.201 ? 434 ILE EEE CB  1 
ATOM   6640  C CG1 . ILE E 1 105 ? -41.958 -26.100 2.489   1.000 115.509 ? 434 ILE EEE CG1 1 
ATOM   6641  C CG2 . ILE E 1 105 ? -42.781 -27.931 0.952   1.000 113.980 ? 434 ILE EEE CG2 1 
ATOM   6642  C CD1 . ILE E 1 105 ? -43.212 -25.450 3.000   1.000 117.741 ? 434 ILE EEE CD1 1 
ATOM   6643  N N   . ALA E 1 106 ? -40.221 -28.002 -1.620  1.000 111.335 ? 435 ALA EEE N   1 
ATOM   6644  C CA  . ALA E 1 106 ? -40.025 -28.276 -3.061  1.000 112.600 ? 435 ALA EEE CA  1 
ATOM   6645  C C   . ALA E 1 106 ? -40.418 -29.714 -3.396  1.000 114.234 ? 435 ALA EEE C   1 
ATOM   6646  O O   . ALA E 1 106 ? -39.906 -30.631 -2.721  1.000 116.741 ? 435 ALA EEE O   1 
ATOM   6647  C CB  . ALA E 1 106 ? -38.588 -28.022 -3.429  1.000 113.102 ? 435 ALA EEE CB  1 
ATOM   6648  N N   . TRP E 1 107 ? -41.259 -29.895 -4.418  1.000 115.331 ? 436 TRP EEE N   1 
ATOM   6649  C CA  . TRP E 1 107 ? -41.638 -31.228 -4.952  1.000 118.081 ? 436 TRP EEE CA  1 
ATOM   6650  C C   . TRP E 1 107 ? -41.430 -31.263 -6.467  1.000 117.432 ? 436 TRP EEE C   1 
ATOM   6651  O O   . TRP E 1 107 ? -41.586 -30.207 -7.111  1.000 117.023 ? 436 TRP EEE O   1 
ATOM   6652  C CB  . TRP E 1 107 ? -43.079 -31.572 -4.571  1.000 121.441 ? 436 TRP EEE CB  1 
ATOM   6653  C CG  . TRP E 1 107 ? -44.122 -30.669 -5.152  1.000 122.784 ? 436 TRP EEE CG  1 
ATOM   6654  C CD1 . TRP E 1 107 ? -44.818 -30.853 -6.310  1.000 125.656 ? 436 TRP EEE CD1 1 
ATOM   6655  C CD2 . TRP E 1 107 ? -44.632 -29.459 -4.572  1.000 123.027 ? 436 TRP EEE CD2 1 
ATOM   6656  N NE1 . TRP E 1 107 ? -45.710 -29.834 -6.499  1.000 126.687 ? 436 TRP EEE NE1 1 
ATOM   6657  C CE2 . TRP E 1 107 ? -45.621 -28.966 -5.449  1.000 124.836 ? 436 TRP EEE CE2 1 
ATOM   6658  C CE3 . TRP E 1 107 ? -44.341 -28.742 -3.412  1.000 123.541 ? 436 TRP EEE CE3 1 
ATOM   6659  C CZ2 . TRP E 1 107 ? -46.320 -27.790 -5.202  1.000 125.943 ? 436 TRP EEE CZ2 1 
ATOM   6660  C CZ3 . TRP E 1 107 ? -45.036 -27.583 -3.163  1.000 124.789 ? 436 TRP EEE CZ3 1 
ATOM   6661  C CH2 . TRP E 1 107 ? -46.012 -27.117 -4.046  1.000 126.151 ? 436 TRP EEE CH2 1 
ATOM   6662  N N   . ASN E 1 108 ? -41.081 -32.440 -6.996  1.000 118.299 ? 437 ASN EEE N   1 
ATOM   6663  C CA  . ASN E 1 108 ? -40.923 -32.686 -8.453  1.000 119.092 ? 437 ASN EEE CA  1 
ATOM   6664  C C   . ASN E 1 108 ? -42.284 -32.491 -9.120  1.000 117.684 ? 437 ASN EEE C   1 
ATOM   6665  O O   . ASN E 1 108 ? -43.282 -32.976 -8.565  1.000 117.868 ? 437 ASN EEE O   1 
ATOM   6666  C CB  . ASN E 1 108 ? -40.348 -34.076 -8.735  1.000 122.392 ? 437 ASN EEE CB  1 
ATOM   6667  C CG  . ASN E 1 108 ? -39.973 -34.276 -10.189 1.000 124.120 ? 437 ASN EEE CG  1 
ATOM   6668  O OD1 . ASN E 1 108 ? -40.825 -34.204 -11.075 1.000 124.782 ? 437 ASN EEE OD1 1 
ATOM   6669  N ND2 . ASN E 1 108 ? -38.701 -34.539 -10.442 1.000 125.470 ? 437 ASN EEE ND2 1 
ATOM   6670  N N   . SER E 1 109 ? -42.309 -31.798 -10.258 1.000 116.711 ? 438 SER EEE N   1 
ATOM   6671  C CA  . SER E 1 109 ? -43.542 -31.440 -11.005 1.000 119.170 ? 438 SER EEE CA  1 
ATOM   6672  C C   . SER E 1 109 ? -43.317 -31.575 -12.520 1.000 124.375 ? 438 SER EEE C   1 
ATOM   6673  O O   . SER E 1 109 ? -43.821 -30.710 -13.279 1.000 127.058 ? 438 SER EEE O   1 
ATOM   6674  C CB  . SER E 1 109 ? -43.986 -30.055 -10.628 1.000 116.343 ? 438 SER EEE CB  1 
ATOM   6675  O OG  . SER E 1 109 ? -42.948 -29.112 -10.850 1.000 112.944 ? 438 SER EEE OG  1 
ATOM   6676  N N   . ASN E 1 110 ? -42.590 -32.617 -12.947 1.000 127.610 ? 439 ASN EEE N   1 
ATOM   6677  C CA  . ASN E 1 110 ? -42.489 -33.033 -14.375 1.000 129.129 ? 439 ASN EEE CA  1 
ATOM   6678  C C   . ASN E 1 110 ? -43.923 -33.232 -14.881 1.000 131.128 ? 439 ASN EEE C   1 
ATOM   6679  O O   . ASN E 1 110 ? -44.278 -32.608 -15.891 1.000 130.921 ? 439 ASN EEE O   1 
ATOM   6680  C CB  . ASN E 1 110 ? -41.621 -34.289 -14.536 1.000 131.275 ? 439 ASN EEE CB  1 
ATOM   6681  C CG  . ASN E 1 110 ? -40.894 -34.393 -15.864 1.000 132.947 ? 439 ASN EEE CG  1 
ATOM   6682  O OD1 . ASN E 1 110 ? -40.593 -33.393 -16.516 1.000 130.082 ? 439 ASN EEE OD1 1 
ATOM   6683  N ND2 . ASN E 1 110 ? -40.580 -35.616 -16.262 1.000 136.476 ? 439 ASN EEE ND2 1 
ATOM   6684  N N   . ASN E 1 111 ? -44.727 -33.990 -14.121 1.000 133.722 ? 440 ASN EEE N   1 
ATOM   6685  C CA  . ASN E 1 111 ? -46.134 -34.389 -14.419 1.000 135.986 ? 440 ASN EEE CA  1 
ATOM   6686  C C   . ASN E 1 111 ? -47.003 -33.181 -14.811 1.000 131.239 ? 440 ASN EEE C   1 
ATOM   6687  O O   . ASN E 1 111 ? -48.033 -33.417 -15.460 1.000 132.487 ? 440 ASN EEE O   1 
ATOM   6688  C CB  . ASN E 1 111 ? -46.767 -35.185 -13.259 1.000 141.095 ? 440 ASN EEE CB  1 
ATOM   6689  C CG  . ASN E 1 111 ? -46.818 -34.477 -11.911 1.000 140.996 ? 440 ASN EEE CG  1 
ATOM   6690  O OD1 . ASN E 1 111 ? -45.782 -34.151 -11.321 1.000 141.390 ? 440 ASN EEE OD1 1 
ATOM   6691  N ND2 . ASN E 1 111 ? -48.019 -34.284 -11.377 1.000 140.015 ? 440 ASN EEE ND2 1 
ATOM   6692  N N   . LEU E 1 112 ? -46.622 -31.949 -14.447 1.000 126.132 ? 441 LEU EEE N   1 
ATOM   6693  C CA  . LEU E 1 112 ? -47.486 -30.741 -14.578 1.000 126.152 ? 441 LEU EEE CA  1 
ATOM   6694  C C   . LEU E 1 112 ? -46.858 -29.677 -15.489 1.000 124.052 ? 441 LEU EEE C   1 
ATOM   6695  O O   . LEU E 1 112 ? -47.635 -28.977 -16.175 1.000 125.896 ? 441 LEU EEE O   1 
ATOM   6696  C CB  . LEU E 1 112 ? -47.744 -30.162 -13.183 1.000 125.804 ? 441 LEU EEE CB  1 
ATOM   6697  C CG  . LEU E 1 112 ? -48.508 -31.076 -12.227 1.000 129.095 ? 441 LEU EEE CG  1 
ATOM   6698  C CD1 . LEU E 1 112 ? -48.384 -30.597 -10.786 1.000 128.213 ? 441 LEU EEE CD1 1 
ATOM   6699  C CD2 . LEU E 1 112 ? -49.967 -31.186 -12.640 1.000 131.861 ? 441 LEU EEE CD2 1 
ATOM   6700  N N   . ASP E 1 113 ? -45.527 -29.536 -15.499 1.000 121.398 ? 442 ASP EEE N   1 
ATOM   6701  C CA  . ASP E 1 113 ? -44.834 -28.343 -16.062 1.000 120.478 ? 442 ASP EEE CA  1 
ATOM   6702  C C   . ASP E 1 113 ? -43.925 -28.724 -17.251 1.000 121.926 ? 442 ASP EEE C   1 
ATOM   6703  O O   . ASP E 1 113 ? -43.049 -27.910 -17.579 1.000 120.953 ? 442 ASP EEE O   1 
ATOM   6704  C CB  . ASP E 1 113 ? -44.068 -27.620 -14.946 1.000 117.591 ? 442 ASP EEE CB  1 
ATOM   6705  C CG  . ASP E 1 113 ? -44.922 -27.134 -13.776 1.000 115.812 ? 442 ASP EEE CG  1 
ATOM   6706  O OD1 . ASP E 1 113 ? -45.898 -26.424 -14.028 1.000 117.758 ? 442 ASP EEE OD1 1 
ATOM   6707  O OD2 . ASP E 1 113 ? -44.600 -27.461 -12.612 1.000 112.297 ? 442 ASP EEE OD2 1 
ATOM   6708  N N   . SER E 1 114 ? -44.142 -29.877 -17.905 1.000 124.771 ? 443 SER EEE N   1 
ATOM   6709  C CA  . SER E 1 114 ? -43.293 -30.426 -19.003 1.000 125.886 ? 443 SER EEE CA  1 
ATOM   6710  C C   . SER E 1 114 ? -44.142 -30.878 -20.200 1.000 130.314 ? 443 SER EEE C   1 
ATOM   6711  O O   . SER E 1 114 ? -44.965 -31.804 -20.040 1.000 129.617 ? 443 SER EEE O   1 
ATOM   6712  C CB  . SER E 1 114 ? -42.440 -31.571 -18.513 1.000 125.640 ? 443 SER EEE CB  1 
ATOM   6713  O OG  . SER E 1 114 ? -41.616 -31.176 -17.429 1.000 121.666 ? 443 SER EEE OG  1 
ATOM   6714  N N   . LYS E 1 115 ? -43.897 -30.289 -21.373 1.000 135.537 ? 444 LYS EEE N   1 
ATOM   6715  C CA  . LYS E 1 115 ? -44.547 -30.660 -22.659 1.000 144.266 ? 444 LYS EEE CA  1 
ATOM   6716  C C   . LYS E 1 115 ? -43.578 -31.485 -23.503 1.000 145.288 ? 444 LYS EEE C   1 
ATOM   6717  O O   . LYS E 1 115 ? -42.357 -31.327 -23.323 1.000 142.076 ? 444 LYS EEE O   1 
ATOM   6718  C CB  . LYS E 1 115 ? -44.976 -29.414 -23.437 1.000 150.001 ? 444 LYS EEE CB  1 
ATOM   6719  C CG  . LYS E 1 115 ? -45.890 -28.481 -22.654 1.000 154.238 ? 444 LYS EEE CG  1 
ATOM   6720  C CD  . LYS E 1 115 ? -46.318 -27.227 -23.386 1.000 158.868 ? 444 LYS EEE CD  1 
ATOM   6721  C CE  . LYS E 1 115 ? -46.857 -26.174 -22.435 1.000 159.122 ? 444 LYS EEE CE  1 
ATOM   6722  N NZ  . LYS E 1 115 ? -47.690 -25.163 -23.130 1.000 162.894 ? 444 LYS EEE NZ  1 
ATOM   6723  N N   . VAL E 1 116 ? -44.115 -32.314 -24.402 1.000 149.398 ? 445 VAL EEE N   1 
ATOM   6724  C CA  . VAL E 1 116 ? -43.314 -33.110 -25.377 1.000 153.398 ? 445 VAL EEE CA  1 
ATOM   6725  C C   . VAL E 1 116 ? -42.446 -32.130 -26.184 1.000 152.314 ? 445 VAL EEE C   1 
ATOM   6726  O O   . VAL E 1 116 ? -41.227 -32.380 -26.293 1.000 152.789 ? 445 VAL EEE O   1 
ATOM   6727  C CB  . VAL E 1 116 ? -44.202 -34.010 -26.267 1.000 159.686 ? 445 VAL EEE CB  1 
ATOM   6728  C CG1 . VAL E 1 116 ? -44.930 -35.071 -25.447 1.000 159.790 ? 445 VAL EEE CG1 1 
ATOM   6729  C CG2 . VAL E 1 116 ? -45.191 -33.221 -27.121 1.000 162.155 ? 445 VAL EEE CG2 1 
ATOM   6730  N N   . GLY E 1 117 ? -43.027 -31.017 -26.654 1.000 150.475 ? 446 GLY EEE N   1 
ATOM   6731  C CA  . GLY E 1 117 ? -42.326 -29.977 -27.434 1.000 150.748 ? 446 GLY EEE CA  1 
ATOM   6732  C C   . GLY E 1 117 ? -41.368 -29.152 -26.586 1.000 147.795 ? 446 GLY EEE C   1 
ATOM   6733  O O   . GLY E 1 117 ? -40.565 -28.398 -27.183 1.000 146.549 ? 446 GLY EEE O   1 
ATOM   6734  N N   . GLY E 1 118 ? -41.466 -29.276 -25.252 1.000 147.189 ? 447 GLY EEE N   1 
ATOM   6735  C CA  . GLY E 1 118 ? -40.664 -28.549 -24.245 1.000 144.089 ? 447 GLY EEE CA  1 
ATOM   6736  C C   . GLY E 1 118 ? -41.394 -27.312 -23.732 1.000 141.671 ? 447 GLY EEE C   1 
ATOM   6737  O O   . GLY E 1 118 ? -41.639 -26.416 -24.552 1.000 143.841 ? 447 GLY EEE O   1 
ATOM   6738  N N   . ASN E 1 119 ? -41.744 -27.257 -22.438 1.000 139.545 ? 448 ASN EEE N   1 
ATOM   6739  C CA  . ASN E 1 119 ? -42.477 -26.114 -21.813 1.000 138.431 ? 448 ASN EEE CA  1 
ATOM   6740  C C   . ASN E 1 119 ? -41.496 -24.953 -21.593 1.000 137.953 ? 448 ASN EEE C   1 
ATOM   6741  O O   . ASN E 1 119 ? -40.836 -24.910 -20.521 1.000 137.199 ? 448 ASN EEE O   1 
ATOM   6742  C CB  . ASN E 1 119 ? -43.194 -26.494 -20.507 1.000 135.883 ? 448 ASN EEE CB  1 
ATOM   6743  C CG  . ASN E 1 119 ? -44.169 -25.442 -20.009 1.000 132.137 ? 448 ASN EEE CG  1 
ATOM   6744  O OD1 . ASN E 1 119 ? -44.095 -24.280 -20.396 1.000 128.897 ? 448 ASN EEE OD1 1 
ATOM   6745  N ND2 . ASN E 1 119 ? -45.094 -25.836 -19.147 1.000 130.868 ? 448 ASN EEE ND2 1 
ATOM   6746  N N   . TYR E 1 120 ? -41.434 -24.034 -22.563 1.000 138.874 ? 449 TYR EEE N   1 
ATOM   6747  C CA  . TYR E 1 120 ? -40.493 -22.881 -22.595 1.000 135.990 ? 449 TYR EEE CA  1 
ATOM   6748  C C   . TYR E 1 120 ? -41.083 -21.694 -21.804 1.000 131.856 ? 449 TYR EEE C   1 
ATOM   6749  O O   . TYR E 1 120 ? -40.380 -20.681 -21.668 1.000 126.670 ? 449 TYR EEE O   1 
ATOM   6750  C CB  . TYR E 1 120 ? -40.136 -22.523 -24.051 1.000 138.098 ? 449 TYR EEE CB  1 
ATOM   6751  C CG  . TYR E 1 120 ? -39.399 -23.583 -24.849 1.000 139.178 ? 449 TYR EEE CG  1 
ATOM   6752  C CD1 . TYR E 1 120 ? -38.105 -23.973 -24.520 1.000 138.746 ? 449 TYR EEE CD1 1 
ATOM   6753  C CD2 . TYR E 1 120 ? -39.980 -24.184 -25.957 1.000 141.412 ? 449 TYR EEE CD2 1 
ATOM   6754  C CE1 . TYR E 1 120 ? -37.426 -24.942 -25.246 1.000 139.704 ? 449 TYR EEE CE1 1 
ATOM   6755  C CE2 . TYR E 1 120 ? -39.316 -25.155 -26.693 1.000 143.822 ? 449 TYR EEE CE2 1 
ATOM   6756  C CZ  . TYR E 1 120 ? -38.034 -25.535 -26.335 1.000 142.642 ? 449 TYR EEE CZ  1 
ATOM   6757  O OH  . TYR E 1 120 ? -37.371 -26.488 -27.046 1.000 146.667 ? 449 TYR EEE OH  1 
ATOM   6758  N N   . ASN E 1 121 ? -42.304 -21.826 -21.263 1.000 132.440 ? 450 ASN EEE N   1 
ATOM   6759  C CA  . ASN E 1 121 ? -43.094 -20.723 -20.644 1.000 132.680 ? 450 ASN EEE CA  1 
ATOM   6760  C C   . ASN E 1 121 ? -42.613 -20.416 -19.215 1.000 130.191 ? 450 ASN EEE C   1 
ATOM   6761  O O   . ASN E 1 121 ? -43.091 -19.406 -18.653 1.000 131.239 ? 450 ASN EEE O   1 
ATOM   6762  C CB  . ASN E 1 121 ? -44.595 -21.037 -20.610 1.000 134.800 ? 450 ASN EEE CB  1 
ATOM   6763  C CG  . ASN E 1 121 ? -45.226 -21.146 -21.981 1.000 138.652 ? 450 ASN EEE CG  1 
ATOM   6764  O OD1 . ASN E 1 121 ? -45.410 -22.242 -22.507 1.000 140.848 ? 450 ASN EEE OD1 1 
ATOM   6765  N ND2 . ASN E 1 121 ? -45.582 -20.011 -22.555 1.000 141.797 ? 450 ASN EEE ND2 1 
ATOM   6766  N N   . TYR E 1 122 ? -41.749 -21.254 -18.628 1.000 127.894 ? 451 TYR EEE N   1 
ATOM   6767  C CA  . TYR E 1 122 ? -41.077 -20.988 -17.327 1.000 124.708 ? 451 TYR EEE CA  1 
ATOM   6768  C C   . TYR E 1 122 ? -39.684 -20.440 -17.623 1.000 121.869 ? 451 TYR EEE C   1 
ATOM   6769  O O   . TYR E 1 122 ? -38.965 -21.056 -18.443 1.000 122.941 ? 451 TYR EEE O   1 
ATOM   6770  C CB  . TYR E 1 122 ? -41.014 -22.241 -16.451 1.000 126.569 ? 451 TYR EEE CB  1 
ATOM   6771  C CG  . TYR E 1 122 ? -42.314 -22.575 -15.770 1.000 129.288 ? 451 TYR EEE CG  1 
ATOM   6772  C CD1 . TYR E 1 122 ? -42.691 -21.928 -14.609 1.000 130.230 ? 451 TYR EEE CD1 1 
ATOM   6773  C CD2 . TYR E 1 122 ? -43.181 -23.519 -16.297 1.000 134.014 ? 451 TYR EEE CD2 1 
ATOM   6774  C CE1 . TYR E 1 122 ? -43.897 -22.214 -13.985 1.000 134.347 ? 451 TYR EEE CE1 1 
ATOM   6775  C CE2 . TYR E 1 122 ? -44.387 -23.824 -15.683 1.000 136.879 ? 451 TYR EEE CE2 1 
ATOM   6776  C CZ  . TYR E 1 122 ? -44.749 -23.165 -14.521 1.000 137.144 ? 451 TYR EEE CZ  1 
ATOM   6777  O OH  . TYR E 1 122 ? -45.935 -23.449 -13.899 1.000 140.265 ? 451 TYR EEE OH  1 
ATOM   6778  N N   . LEU E 1 123 ? -39.329 -19.329 -16.970 1.000 118.497 ? 452 LEU EEE N   1 
ATOM   6779  C CA  . LEU E 1 123 ? -38.157 -18.487 -17.321 1.000 117.444 ? 452 LEU EEE CA  1 
ATOM   6780  C C   . LEU E 1 123 ? -37.268 -18.289 -16.099 1.000 114.589 ? 452 LEU EEE C   1 
ATOM   6781  O O   . LEU E 1 123 ? -37.685 -18.700 -14.992 1.000 112.154 ? 452 LEU EEE O   1 
ATOM   6782  C CB  . LEU E 1 123 ? -38.653 -17.134 -17.824 1.000 119.743 ? 452 LEU EEE CB  1 
ATOM   6783  C CG  . LEU E 1 123 ? -39.782 -17.200 -18.844 1.000 123.918 ? 452 LEU EEE CG  1 
ATOM   6784  C CD1 . LEU E 1 123 ? -40.347 -15.823 -19.133 1.000 125.510 ? 452 LEU EEE CD1 1 
ATOM   6785  C CD2 . LEU E 1 123 ? -39.300 -17.854 -20.127 1.000 127.252 ? 452 LEU EEE CD2 1 
ATOM   6786  N N   . TYR E 1 124 ? -36.113 -17.654 -16.319 1.000 114.034 ? 453 TYR EEE N   1 
ATOM   6787  C CA  . TYR E 1 124 ? -35.069 -17.375 -15.302 1.000 114.021 ? 453 TYR EEE CA  1 
ATOM   6788  C C   . TYR E 1 124 ? -34.107 -16.308 -15.833 1.000 114.734 ? 453 TYR EEE C   1 
ATOM   6789  O O   . TYR E 1 124 ? -33.755 -16.356 -17.018 1.000 116.560 ? 453 TYR EEE O   1 
ATOM   6790  C CB  . TYR E 1 124 ? -34.346 -18.671 -14.917 1.000 116.475 ? 453 TYR EEE CB  1 
ATOM   6791  C CG  . TYR E 1 124 ? -33.294 -19.172 -15.877 1.000 119.975 ? 453 TYR EEE CG  1 
ATOM   6792  C CD1 . TYR E 1 124 ? -33.642 -19.836 -17.040 1.000 122.840 ? 453 TYR EEE CD1 1 
ATOM   6793  C CD2 . TYR E 1 124 ? -31.942 -19.022 -15.603 1.000 122.549 ? 453 TYR EEE CD2 1 
ATOM   6794  C CE1 . TYR E 1 124 ? -32.676 -20.296 -17.925 1.000 126.575 ? 453 TYR EEE CE1 1 
ATOM   6795  C CE2 . TYR E 1 124 ? -30.966 -19.475 -16.475 1.000 125.491 ? 453 TYR EEE CE2 1 
ATOM   6796  C CZ  . TYR E 1 124 ? -31.332 -20.112 -17.648 1.000 127.327 ? 453 TYR EEE CZ  1 
ATOM   6797  O OH  . TYR E 1 124 ? -30.386 -20.575 -18.521 1.000 129.800 ? 453 TYR EEE OH  1 
ATOM   6798  N N   . ARG E 1 125 ? -33.698 -15.375 -14.968 1.000 116.553 ? 454 ARG EEE N   1 
ATOM   6799  C CA  . ARG E 1 125 ? -32.705 -14.309 -15.276 1.000 120.748 ? 454 ARG EEE CA  1 
ATOM   6800  C C   . ARG E 1 125 ? -31.300 -14.915 -15.263 1.000 124.701 ? 454 ARG EEE C   1 
ATOM   6801  O O   . ARG E 1 125 ? -31.099 -15.925 -14.571 1.000 128.632 ? 454 ARG EEE O   1 
ATOM   6802  C CB  . ARG E 1 125 ? -32.808 -13.152 -14.277 1.000 120.900 ? 454 ARG EEE CB  1 
ATOM   6803  C CG  . ARG E 1 125 ? -31.950 -11.940 -14.619 1.000 123.129 ? 454 ARG EEE CG  1 
ATOM   6804  C CD  . ARG E 1 125 ? -32.192 -10.773 -13.681 1.000 123.743 ? 454 ARG EEE CD  1 
ATOM   6805  N NE  . ARG E 1 125 ? -33.561 -10.289 -13.791 1.000 122.970 ? 454 ARG EEE NE  1 
ATOM   6806  C CZ  . ARG E 1 125 ? -33.983 -9.417  -14.697 1.000 122.782 ? 454 ARG EEE CZ  1 
ATOM   6807  N NH1 . ARG E 1 125 ? -33.139 -8.900  -15.574 1.000 123.156 ? 454 ARG EEE NH1 1 
ATOM   6808  N NH2 . ARG E 1 125 ? -35.253 -9.061  -14.713 1.000 122.278 ? 454 ARG EEE NH2 1 
ATOM   6809  N N   . LEU E 1 126 ? -30.368 -14.304 -15.996 1.000 128.959 ? 455 LEU EEE N   1 
ATOM   6810  C CA  . LEU E 1 126 ? -29.025 -14.870 -16.289 1.000 130.757 ? 455 LEU EEE CA  1 
ATOM   6811  C C   . LEU E 1 126 ? -27.905 -13.896 -15.907 1.000 132.626 ? 455 LEU EEE C   1 
ATOM   6812  O O   . LEU E 1 126 ? -26.841 -14.387 -15.465 1.000 132.604 ? 455 LEU EEE O   1 
ATOM   6813  C CB  . LEU E 1 126 ? -28.987 -15.185 -17.783 1.000 133.644 ? 455 LEU EEE CB  1 
ATOM   6814  C CG  . LEU E 1 126 ? -27.995 -16.260 -18.197 1.000 137.629 ? 455 LEU EEE CG  1 
ATOM   6815  C CD1 . LEU E 1 126 ? -28.170 -17.514 -17.349 1.000 136.853 ? 455 LEU EEE CD1 1 
ATOM   6816  C CD2 . LEU E 1 126 ? -28.161 -16.571 -19.679 1.000 139.614 ? 455 LEU EEE CD2 1 
ATOM   6817  N N   . PHE E 1 127 ? -28.124 -12.588 -16.108 1.000 133.916 ? 456 PHE EEE N   1 
ATOM   6818  C CA  . PHE E 1 127 ? -27.172 -11.491 -15.780 1.000 135.572 ? 456 PHE EEE CA  1 
ATOM   6819  C C   . PHE E 1 127 ? -27.867 -10.370 -15.006 1.000 132.237 ? 456 PHE EEE C   1 
ATOM   6820  O O   . PHE E 1 127 ? -29.119 -10.313 -14.961 1.000 127.983 ? 456 PHE EEE O   1 
ATOM   6821  C CB  . PHE E 1 127 ? -26.591 -10.869 -17.049 1.000 140.070 ? 456 PHE EEE CB  1 
ATOM   6822  C CG  . PHE E 1 127 ? -26.201 -11.861 -18.109 1.000 140.810 ? 456 PHE EEE CG  1 
ATOM   6823  C CD1 . PHE E 1 127 ? -25.174 -12.761 -17.879 1.000 141.625 ? 456 PHE EEE CD1 1 
ATOM   6824  C CD2 . PHE E 1 127 ? -26.865 -11.897 -19.321 1.000 140.991 ? 456 PHE EEE CD2 1 
ATOM   6825  C CE1 . PHE E 1 127 ? -24.817 -13.683 -18.846 1.000 142.267 ? 456 PHE EEE CE1 1 
ATOM   6826  C CE2 . PHE E 1 127 ? -26.503 -12.819 -20.287 1.000 142.437 ? 456 PHE EEE CE2 1 
ATOM   6827  C CZ  . PHE E 1 127 ? -25.483 -13.709 -20.048 1.000 143.352 ? 456 PHE EEE CZ  1 
ATOM   6828  N N   . ARG E 1 128 ? -27.058 -9.456  -14.469 1.000 132.025 ? 457 ARG EEE N   1 
ATOM   6829  C CA  . ARG E 1 128 ? -27.539 -8.293  -13.690 1.000 133.300 ? 457 ARG EEE CA  1 
ATOM   6830  C C   . ARG E 1 128 ? -26.335 -7.457  -13.262 1.000 135.024 ? 457 ARG EEE C   1 
ATOM   6831  O O   . ARG E 1 128 ? -25.303 -8.067  -12.914 1.000 131.730 ? 457 ARG EEE O   1 
ATOM   6832  C CB  . ARG E 1 128 ? -28.333 -8.785  -12.477 1.000 133.731 ? 457 ARG EEE CB  1 
ATOM   6833  C CG  . ARG E 1 128 ? -29.519 -7.911  -12.101 1.000 134.572 ? 457 ARG EEE CG  1 
ATOM   6834  C CD  . ARG E 1 128 ? -30.421 -8.590  -11.085 1.000 131.775 ? 457 ARG EEE CD  1 
ATOM   6835  N NE  . ARG E 1 128 ? -31.297 -7.618  -10.450 1.000 132.471 ? 457 ARG EEE NE  1 
ATOM   6836  C CZ  . ARG E 1 128 ? -30.938 -6.794  -9.466  1.000 135.100 ? 457 ARG EEE CZ  1 
ATOM   6837  N NH1 . ARG E 1 128 ? -29.710 -6.823  -8.980  1.000 136.615 ? 457 ARG EEE NH1 1 
ATOM   6838  N NH2 . ARG E 1 128 ? -31.815 -5.936  -8.970  1.000 136.513 ? 457 ARG EEE NH2 1 
ATOM   6839  N N   . LYS E 1 129 ? -26.483 -6.125  -13.294 1.000 139.404 ? 458 LYS EEE N   1 
ATOM   6840  C CA  . LYS E 1 129 ? -25.450 -5.126  -12.900 1.000 145.526 ? 458 LYS EEE CA  1 
ATOM   6841  C C   . LYS E 1 129 ? -24.858 -5.543  -11.549 1.000 146.336 ? 458 LYS EEE C   1 
ATOM   6842  O O   . LYS E 1 129 ? -23.625 -5.520  -11.400 1.000 151.606 ? 458 LYS EEE O   1 
ATOM   6843  C CB  . LYS E 1 129 ? -26.038 -3.710  -12.783 1.000 148.202 ? 458 LYS EEE CB  1 
ATOM   6844  C CG  . LYS E 1 129 ? -26.563 -3.082  -14.071 1.000 150.390 ? 458 LYS EEE CG  1 
ATOM   6845  C CD  . LYS E 1 129 ? -25.511 -2.378  -14.913 1.000 156.454 ? 458 LYS EEE CD  1 
ATOM   6846  C CE  . LYS E 1 129 ? -25.822 -2.396  -16.402 1.000 158.052 ? 458 LYS EEE CE  1 
ATOM   6847  N NZ  . LYS E 1 129 ? -24.716 -1.831  -17.212 1.000 161.630 ? 458 LYS EEE NZ  1 
ATOM   6848  N N   . SER E 1 130 ? -25.726 -5.914  -10.608 1.000 143.456 ? 459 SER EEE N   1 
ATOM   6849  C CA  . SER E 1 130 ? -25.367 -6.312  -9.222  1.000 142.917 ? 459 SER EEE CA  1 
ATOM   6850  C C   . SER E 1 130 ? -26.227 -7.501  -8.788  1.000 137.329 ? 459 SER EEE C   1 
ATOM   6851  O O   . SER E 1 130 ? -27.088 -7.936  -9.573  1.000 133.943 ? 459 SER EEE O   1 
ATOM   6852  C CB  . SER E 1 130 ? -25.530 -5.155  -8.274  1.000 146.400 ? 459 SER EEE CB  1 
ATOM   6853  O OG  . SER E 1 130 ? -26.890 -5.011  -7.889  1.000 146.243 ? 459 SER EEE OG  1 
ATOM   6854  N N   . ASN E 1 131 ? -26.003 -7.990  -7.568  1.000 135.762 ? 460 ASN EEE N   1 
ATOM   6855  C CA  . ASN E 1 131 ? -26.785 -9.097  -6.959  1.000 132.419 ? 460 ASN EEE CA  1 
ATOM   6856  C C   . ASN E 1 131 ? -28.091 -8.513  -6.404  1.000 130.800 ? 460 ASN EEE C   1 
ATOM   6857  O O   . ASN E 1 131 ? -28.097 -7.314  -6.043  1.000 131.231 ? 460 ASN EEE O   1 
ATOM   6858  C CB  . ASN E 1 131 ? -25.962 -9.840  -5.901  1.000 133.051 ? 460 ASN EEE CB  1 
ATOM   6859  C CG  . ASN E 1 131 ? -24.648 -10.359 -6.445  1.000 133.597 ? 460 ASN EEE CG  1 
ATOM   6860  O OD1 . ASN E 1 131 ? -24.632 -11.122 -7.405  1.000 130.218 ? 460 ASN EEE OD1 1 
ATOM   6861  N ND2 . ASN E 1 131 ? -23.541 -9.921  -5.865  1.000 138.727 ? 460 ASN EEE ND2 1 
ATOM   6862  N N   . LEU E 1 132 ? -29.153 -9.327  -6.362  1.000 127.804 ? 461 LEU EEE N   1 
ATOM   6863  C CA  . LEU E 1 132 ? -30.469 -8.965  -5.769  1.000 126.920 ? 461 LEU EEE CA  1 
ATOM   6864  C C   . LEU E 1 132 ? -30.288 -8.688  -4.279  1.000 129.379 ? 461 LEU EEE C   1 
ATOM   6865  O O   . LEU E 1 132 ? -29.515 -9.427  -3.636  1.000 130.016 ? 461 LEU EEE O   1 
ATOM   6866  C CB  . LEU E 1 132 ? -31.459 -10.122 -5.944  1.000 124.029 ? 461 LEU EEE CB  1 
ATOM   6867  C CG  . LEU E 1 132 ? -32.085 -10.288 -7.325  1.000 123.642 ? 461 LEU EEE CG  1 
ATOM   6868  C CD1 . LEU E 1 132 ? -33.003 -11.501 -7.358  1.000 120.999 ? 461 LEU EEE CD1 1 
ATOM   6869  C CD2 . LEU E 1 132 ? -32.850 -9.039  -7.728  1.000 126.175 ? 461 LEU EEE CD2 1 
ATOM   6870  N N   . LYS E 1 133 ? -31.000 -7.691  -3.753  1.000 132.629 ? 462 LYS EEE N   1 
ATOM   6871  C CA  . LYS E 1 133 ? -31.217 -7.534  -2.291  1.000 135.652 ? 462 LYS EEE CA  1 
ATOM   6872  C C   . LYS E 1 133 ? -32.114 -8.684  -1.840  1.000 132.746 ? 462 LYS EEE C   1 
ATOM   6873  O O   . LYS E 1 133 ? -32.869 -9.237  -2.640  1.000 132.048 ? 462 LYS EEE O   1 
ATOM   6874  C CB  . LYS E 1 133 ? -31.818 -6.168  -1.950  1.000 140.727 ? 462 LYS EEE CB  1 
ATOM   6875  C CG  . LYS E 1 133 ? -30.804 -5.104  -1.554  1.000 147.965 ? 462 LYS EEE CG  1 
ATOM   6876  C CD  . LYS E 1 133 ? -31.436 -3.770  -1.220  1.000 154.561 ? 462 LYS EEE CD  1 
ATOM   6877  C CE  . LYS E 1 133 ? -30.448 -2.705  -0.777  1.000 161.493 ? 462 LYS EEE CE  1 
ATOM   6878  N NZ  . LYS E 1 133 ? -29.777 -2.045  -1.927  1.000 164.105 ? 462 LYS EEE NZ  1 
ATOM   6879  N N   . PRO E 1 134 ? -32.043 -9.109  -0.559  1.000 131.598 ? 463 PRO EEE N   1 
ATOM   6880  C CA  . PRO E 1 134 ? -32.902 -10.189 -0.071  1.000 128.675 ? 463 PRO EEE CA  1 
ATOM   6881  C C   . PRO E 1 134 ? -34.390 -9.912  -0.349  1.000 127.739 ? 463 PRO EEE C   1 
ATOM   6882  O O   . PRO E 1 134 ? -34.821 -8.796  -0.147  1.000 130.262 ? 463 PRO EEE O   1 
ATOM   6883  C CB  . PRO E 1 134 ? -32.628 -10.195 1.436   1.000 131.300 ? 463 PRO EEE CB  1 
ATOM   6884  C CG  . PRO E 1 134 ? -31.237 -9.598  1.578   1.000 133.846 ? 463 PRO EEE CG  1 
ATOM   6885  C CD  . PRO E 1 134 ? -31.126 -8.582  0.464   1.000 133.971 ? 463 PRO EEE CD  1 
ATOM   6886  N N   . PHE E 1 135 ? -35.125 -10.917 -0.828  1.000 125.028 ? 464 PHE EEE N   1 
ATOM   6887  C CA  . PHE E 1 135 ? -36.575 -10.834 -1.146  1.000 125.223 ? 464 PHE EEE CA  1 
ATOM   6888  C C   . PHE E 1 135 ? -36.821 -9.748  -2.193  1.000 127.430 ? 464 PHE EEE C   1 
ATOM   6889  O O   . PHE E 1 135 ? -37.872 -9.082  -2.125  1.000 127.761 ? 464 PHE EEE O   1 
ATOM   6890  C CB  . PHE E 1 135 ? -37.410 -10.522 0.103   1.000 126.606 ? 464 PHE EEE CB  1 
ATOM   6891  C CG  . PHE E 1 135 ? -37.420 -11.596 1.161   1.000 125.789 ? 464 PHE EEE CG  1 
ATOM   6892  C CD1 . PHE E 1 135 ? -37.730 -12.915 0.839   1.000 123.339 ? 464 PHE EEE CD1 1 
ATOM   6893  C CD2 . PHE E 1 135 ? -37.158 -11.283 2.484   1.000 128.194 ? 464 PHE EEE CD2 1 
ATOM   6894  C CE1 . PHE E 1 135 ? -37.744 -13.903 1.810   1.000 121.291 ? 464 PHE EEE CE1 1 
ATOM   6895  C CE2 . PHE E 1 135 ? -37.169 -12.273 3.453   1.000 128.874 ? 464 PHE EEE CE2 1 
ATOM   6896  C CZ  . PHE E 1 135 ? -37.461 -13.578 3.114   1.000 125.500 ? 464 PHE EEE CZ  1 
ATOM   6897  N N   . GLU E 1 136 ? -35.887 -9.551  -3.122  1.000 130.710 ? 465 GLU EEE N   1 
ATOM   6898  C CA  . GLU E 1 136 ? -36.106 -8.610  -4.249  1.000 135.095 ? 465 GLU EEE CA  1 
ATOM   6899  C C   . GLU E 1 136 ? -36.716 -9.413  -5.395  1.000 135.271 ? 465 GLU EEE C   1 
ATOM   6900  O O   . GLU E 1 136 ? -36.426 -10.628 -5.480  1.000 136.956 ? 465 GLU EEE O   1 
ATOM   6901  C CB  . GLU E 1 136 ? -34.830 -7.883  -4.679  1.000 137.805 ? 465 GLU EEE CB  1 
ATOM   6902  C CG  . GLU E 1 136 ? -35.084 -6.832  -5.755  1.000 139.837 ? 465 GLU EEE CG  1 
ATOM   6903  C CD  . GLU E 1 136 ? -33.975 -5.820  -6.010  1.000 144.039 ? 465 GLU EEE CD  1 
ATOM   6904  O OE1 . GLU E 1 136 ? -32.892 -5.951  -5.390  1.000 145.985 ? 465 GLU EEE OE1 1 
ATOM   6905  O OE2 . GLU E 1 136 ? -34.199 -4.898  -6.837  1.000 145.969 ? 465 GLU EEE OE2 1 
ATOM   6906  N N   . ARG E 1 137 ? -37.537 -8.744  -6.209  1.000 136.297 ? 466 ARG EEE N   1 
ATOM   6907  C CA  . ARG E 1 137 ? -38.339 -9.337  -7.307  1.000 134.921 ? 466 ARG EEE CA  1 
ATOM   6908  C C   . ARG E 1 137 ? -38.140 -8.483  -8.562  1.000 134.570 ? 466 ARG EEE C   1 
ATOM   6909  O O   . ARG E 1 137 ? -38.989 -7.597  -8.830  1.000 132.521 ? 466 ARG EEE O   1 
ATOM   6910  C CB  . ARG E 1 137 ? -39.807 -9.398  -6.876  1.000 137.586 ? 466 ARG EEE CB  1 
ATOM   6911  C CG  . ARG E 1 137 ? -40.719 -10.137 -7.841  1.000 137.412 ? 466 ARG EEE CG  1 
ATOM   6912  C CD  . ARG E 1 137 ? -42.154 -10.178 -7.343  1.000 139.240 ? 466 ARG EEE CD  1 
ATOM   6913  N NE  . ARG E 1 137 ? -43.071 -10.753 -8.320  1.000 138.485 ? 466 ARG EEE NE  1 
ATOM   6914  C CZ  . ARG E 1 137 ? -43.478 -10.154 -9.442  1.000 138.539 ? 466 ARG EEE CZ  1 
ATOM   6915  N NH1 . ARG E 1 137 ? -43.045 -8.944  -9.774  1.000 138.449 ? 466 ARG EEE NH1 1 
ATOM   6916  N NH2 . ARG E 1 137 ? -44.314 -10.791 -10.244 1.000 138.111 ? 466 ARG EEE NH2 1 
ATOM   6917  N N   . ASP E 1 138 ? -37.048 -8.741  -9.290  1.000 134.038 ? 467 ASP EEE N   1 
ATOM   6918  C CA  . ASP E 1 138 ? -36.649 -7.966  -10.493 1.000 135.120 ? 467 ASP EEE CA  1 
ATOM   6919  C C   . ASP E 1 138 ? -37.238 -8.635  -11.732 1.000 132.418 ? 467 ASP EEE C   1 
ATOM   6920  O O   . ASP E 1 138 ? -36.981 -9.854  -11.912 1.000 130.042 ? 467 ASP EEE O   1 
ATOM   6921  C CB  . ASP E 1 138 ? -35.133 -7.854  -10.648 1.000 136.805 ? 467 ASP EEE CB  1 
ATOM   6922  C CG  . ASP E 1 138 ? -34.711 -6.823  -11.680 1.000 137.974 ? 467 ASP EEE CG  1 
ATOM   6923  O OD1 . ASP E 1 138 ? -35.592 -6.325  -12.399 1.000 137.136 ? 467 ASP EEE OD1 1 
ATOM   6924  O OD2 . ASP E 1 138 ? -33.505 -6.523  -11.755 1.000 138.887 ? 467 ASP EEE OD2 1 
ATOM   6925  N N   . ILE E 1 139 ? -37.965 -7.845  -12.536 1.000 131.594 ? 468 ILE EEE N   1 
ATOM   6926  C CA  . ILE E 1 139 ? -38.668 -8.278  -13.780 1.000 130.265 ? 468 ILE EEE CA  1 
ATOM   6927  C C   . ILE E 1 139 ? -38.298 -7.371  -14.967 1.000 133.286 ? 468 ILE EEE C   1 
ATOM   6928  O O   . ILE E 1 139 ? -38.907 -7.552  -16.032 1.000 134.878 ? 468 ILE EEE O   1 
ATOM   6929  C CB  . ILE E 1 139 ? -40.192 -8.328  -13.546 1.000 128.407 ? 468 ILE EEE CB  1 
ATOM   6930  C CG1 . ILE E 1 139 ? -40.826 -6.938  -13.465 1.000 131.533 ? 468 ILE EEE CG1 1 
ATOM   6931  C CG2 . ILE E 1 139 ? -40.509 -9.158  -12.313 1.000 127.117 ? 468 ILE EEE CG2 1 
ATOM   6932  C CD1 . ILE E 1 139 ? -42.333 -6.960  -13.331 1.000 132.705 ? 468 ILE EEE CD1 1 
ATOM   6933  N N   . SER E 1 140 ? -37.338 -6.450  -14.818 1.000 135.407 ? 469 SER EEE N   1 
ATOM   6934  C CA  . SER E 1 140 ? -36.896 -5.531  -15.903 1.000 138.534 ? 469 SER EEE CA  1 
ATOM   6935  C C   . SER E 1 140 ? -36.182 -6.341  -16.992 1.000 136.556 ? 469 SER EEE C   1 
ATOM   6936  O O   . SER E 1 140 ? -35.525 -7.333  -16.643 1.000 133.566 ? 469 SER EEE O   1 
ATOM   6937  C CB  . SER E 1 140 ? -36.020 -4.416  -15.371 1.000 142.352 ? 469 SER EEE CB  1 
ATOM   6938  O OG  . SER E 1 140 ? -34.699 -4.870  -15.107 1.000 142.928 ? 469 SER EEE OG  1 
ATOM   6939  N N   . THR E 1 141 ? -36.328 -5.939  -18.259 1.000 136.158 ? 470 THR EEE N   1 
ATOM   6940  C CA  . THR E 1 141 ? -35.668 -6.560  -19.437 1.000 134.747 ? 470 THR EEE CA  1 
ATOM   6941  C C   . THR E 1 141 ? -34.664 -5.564  -20.029 1.000 137.575 ? 470 THR EEE C   1 
ATOM   6942  O O   . THR E 1 141 ? -34.662 -5.368  -21.266 1.000 139.096 ? 470 THR EEE O   1 
ATOM   6943  C CB  . THR E 1 141 ? -36.707 -7.031  -20.458 1.000 135.338 ? 470 THR EEE CB  1 
ATOM   6944  O OG1 . THR E 1 141 ? -37.199 -5.894  -21.172 1.000 142.287 ? 470 THR EEE OG1 1 
ATOM   6945  C CG2 . THR E 1 141 ? -37.853 -7.785  -19.819 1.000 132.465 ? 470 THR EEE CG2 1 
ATOM   6946  N N   . GLU E 1 142 ? -33.843 -4.961  -19.165 1.000 139.863 ? 471 GLU EEE N   1 
ATOM   6947  C CA  . GLU E 1 142 ? -32.741 -4.039  -19.548 1.000 144.998 ? 471 GLU EEE CA  1 
ATOM   6948  C C   . GLU E 1 142 ? -31.698 -4.844  -20.333 1.000 142.145 ? 471 GLU EEE C   1 
ATOM   6949  O O   . GLU E 1 142 ? -31.253 -5.891  -19.826 1.000 139.703 ? 471 GLU EEE O   1 
ATOM   6950  C CB  . GLU E 1 142 ? -32.133 -3.391  -18.295 1.000 148.536 ? 471 GLU EEE CB  1 
ATOM   6951  C CG  . GLU E 1 142 ? -31.320 -2.129  -18.564 1.000 153.617 ? 471 GLU EEE CG  1 
ATOM   6952  C CD  . GLU E 1 142 ? -30.430 -1.673  -17.414 1.000 154.348 ? 471 GLU EEE CD  1 
ATOM   6953  O OE1 . GLU E 1 142 ? -30.794 -1.920  -16.242 1.000 151.776 ? 471 GLU EEE OE1 1 
ATOM   6954  O OE2 . GLU E 1 142 ? -29.366 -1.077  -17.693 1.000 156.491 ? 471 GLU EEE OE2 1 
ATOM   6955  N N   . ILE E 1 143 ? -31.329 -4.382  -21.526 1.000 141.942 ? 472 ILE EEE N   1 
ATOM   6956  C CA  . ILE E 1 143 ? -30.303 -5.059  -22.371 1.000 144.831 ? 472 ILE EEE CA  1 
ATOM   6957  C C   . ILE E 1 143 ? -28.969 -4.982  -21.621 1.000 144.393 ? 472 ILE EEE C   1 
ATOM   6958  O O   . ILE E 1 143 ? -28.431 -3.862  -21.498 1.000 146.697 ? 472 ILE EEE O   1 
ATOM   6959  C CB  . ILE E 1 143 ? -30.246 -4.435  -23.782 1.000 151.233 ? 472 ILE EEE CB  1 
ATOM   6960  C CG1 . ILE E 1 143 ? -31.644 -4.315  -24.405 1.000 152.853 ? 472 ILE EEE CG1 1 
ATOM   6961  C CG2 . ILE E 1 143 ? -29.288 -5.199  -24.690 1.000 152.429 ? 472 ILE EEE CG2 1 
ATOM   6962  C CD1 . ILE E 1 143 ? -32.521 -5.546  -24.225 1.000 150.481 ? 472 ILE EEE CD1 1 
ATOM   6963  N N   . TYR E 1 144 ? -28.477 -6.124  -21.123 1.000 142.477 ? 473 TYR EEE N   1 
ATOM   6964  C CA  . TYR E 1 144 ? -27.351 -6.211  -20.153 1.000 143.411 ? 473 TYR EEE CA  1 
ATOM   6965  C C   . TYR E 1 144 ? -25.995 -5.925  -20.821 1.000 145.188 ? 473 TYR EEE C   1 
ATOM   6966  O O   . TYR E 1 144 ? -25.531 -6.743  -21.643 1.000 143.683 ? 473 TYR EEE O   1 
ATOM   6967  C CB  . TYR E 1 144 ? -27.281 -7.581  -19.473 1.000 141.695 ? 473 TYR EEE CB  1 
ATOM   6968  C CG  . TYR E 1 144 ? -26.060 -7.721  -18.600 1.000 144.796 ? 473 TYR EEE CG  1 
ATOM   6969  C CD1 . TYR E 1 144 ? -25.860 -6.874  -17.516 1.000 146.856 ? 473 TYR EEE CD1 1 
ATOM   6970  C CD2 . TYR E 1 144 ? -25.072 -8.649  -18.889 1.000 145.409 ? 473 TYR EEE CD2 1 
ATOM   6971  C CE1 . TYR E 1 144 ? -24.727 -6.971  -16.725 1.000 147.921 ? 473 TYR EEE CE1 1 
ATOM   6972  C CE2 . TYR E 1 144 ? -23.942 -8.769  -18.095 1.000 147.290 ? 473 TYR EEE CE2 1 
ATOM   6973  C CZ  . TYR E 1 144 ? -23.767 -7.927  -17.011 1.000 148.341 ? 473 TYR EEE CZ  1 
ATOM   6974  O OH  . TYR E 1 144 ? -22.648 -8.027  -16.237 1.000 149.499 ? 473 TYR EEE OH  1 
ATOM   6975  N N   . GLN E 1 145 ? -25.354 -4.823  -20.409 1.000 146.727 ? 474 GLN EEE N   1 
ATOM   6976  C CA  . GLN E 1 145 ? -23.998 -4.401  -20.851 1.000 149.712 ? 474 GLN EEE CA  1 
ATOM   6977  C C   . GLN E 1 145 ? -22.948 -5.206  -20.079 1.000 150.159 ? 474 GLN EEE C   1 
ATOM   6978  O O   . GLN E 1 145 ? -22.713 -4.878  -18.888 1.000 150.630 ? 474 GLN EEE O   1 
ATOM   6979  C CB  . GLN E 1 145 ? -23.826 -2.897  -20.623 1.000 151.635 ? 474 GLN EEE CB  1 
ATOM   6980  C CG  . GLN E 1 145 ? -22.440 -2.363  -20.963 1.000 155.061 ? 474 GLN EEE CG  1 
ATOM   6981  C CD  . GLN E 1 145 ? -22.333 -0.879  -20.717 1.000 157.818 ? 474 GLN EEE CD  1 
ATOM   6982  O OE1 . GLN E 1 145 ? -23.204 -0.259  -20.115 1.000 157.120 ? 474 GLN EEE OE1 1 
ATOM   6983  N NE2 . GLN E 1 145 ? -21.250 -0.290  -21.194 1.000 161.897 ? 474 GLN EEE NE2 1 
ATOM   6984  N N   . ALA E 1 146 ? -22.345 -6.205  -20.733 1.000 150.666 ? 475 ALA EEE N   1 
ATOM   6985  C CA  . ALA E 1 146 ? -21.230 -7.024  -20.196 1.000 152.348 ? 475 ALA EEE CA  1 
ATOM   6986  C C   . ALA E 1 146 ? -19.906 -6.258  -20.347 1.000 158.551 ? 475 ALA EEE C   1 
ATOM   6987  O O   . ALA E 1 146 ? -19.348 -5.811  -19.316 1.000 161.469 ? 475 ALA EEE O   1 
ATOM   6988  C CB  . ALA E 1 146 ? -21.186 -8.367  -20.891 1.000 150.414 ? 475 ALA EEE CB  1 
ATOM   6989  N N   . GLY E 1 147 ? -19.445 -6.079  -21.588 1.000 160.752 ? 476 GLY EEE N   1 
ATOM   6990  C CA  . GLY E 1 147 ? -18.132 -5.496  -21.921 1.000 165.717 ? 476 GLY EEE CA  1 
ATOM   6991  C C   . GLY E 1 147 ? -18.127 -3.983  -21.763 1.000 168.621 ? 476 GLY EEE C   1 
ATOM   6992  O O   . GLY E 1 147 ? -18.936 -3.461  -20.967 1.000 164.735 ? 476 GLY EEE O   1 
ATOM   6993  N N   . SER E 1 148 ? -17.259 -3.307  -22.523 1.000 175.489 ? 477 SER EEE N   1 
ATOM   6994  C CA  . SER E 1 148 ? -17.053 -1.833  -22.530 1.000 180.550 ? 477 SER EEE CA  1 
ATOM   6995  C C   . SER E 1 148 ? -18.294 -1.118  -23.083 1.000 180.197 ? 477 SER EEE C   1 
ATOM   6996  O O   . SER E 1 148 ? -18.946 -0.397  -22.300 1.000 179.492 ? 477 SER EEE O   1 
ATOM   6997  C CB  . SER E 1 148 ? -15.825 -1.454  -23.335 1.000 186.966 ? 477 SER EEE CB  1 
ATOM   6998  O OG  . SER E 1 148 ? -14.806 -2.439  -23.233 1.000 189.127 ? 477 SER EEE OG  1 
ATOM   6999  N N   . THR E 1 149 ? -18.590 -1.317  -24.376 1.000 180.789 ? 478 THR EEE N   1 
ATOM   7000  C CA  . THR E 1 149 ? -19.525 -0.499  -25.203 1.000 180.181 ? 478 THR EEE CA  1 
ATOM   7001  C C   . THR E 1 149 ? -20.855 -0.329  -24.475 1.000 176.964 ? 478 THR EEE C   1 
ATOM   7002  O O   . THR E 1 149 ? -21.432 -1.309  -24.014 1.000 172.479 ? 478 THR EEE O   1 
ATOM   7003  C CB  . THR E 1 149 ? -19.738 -1.127  -26.585 1.000 178.734 ? 478 THR EEE CB  1 
ATOM   7004  O OG1 . THR E 1 149 ? -18.457 -1.562  -27.035 1.000 181.626 ? 478 THR EEE OG1 1 
ATOM   7005  C CG2 . THR E 1 149 ? -20.370 -0.179  -27.581 1.000 180.562 ? 478 THR EEE CG2 1 
ATOM   7006  N N   . PRO E 1 150 ? -21.377 0.914   -24.330 1.000 179.644 ? 479 PRO EEE N   1 
ATOM   7007  C CA  . PRO E 1 150 ? -22.653 1.142   -23.661 1.000 175.794 ? 479 PRO EEE CA  1 
ATOM   7008  C C   . PRO E 1 150 ? -23.805 0.872   -24.634 1.000 172.917 ? 479 PRO EEE C   1 
ATOM   7009  O O   . PRO E 1 150 ? -23.763 1.367   -25.746 1.000 173.456 ? 479 PRO EEE O   1 
ATOM   7010  C CB  . PRO E 1 150 ? -22.606 2.609   -23.210 1.000 179.929 ? 479 PRO EEE CB  1 
ATOM   7011  C CG  . PRO E 1 150 ? -21.471 3.255   -24.003 1.000 185.856 ? 479 PRO EEE CG  1 
ATOM   7012  C CD  . PRO E 1 150 ? -20.778 2.169   -24.807 1.000 185.870 ? 479 PRO EEE CD  1 
ATOM   7013  N N   . CYS E 1 151 ? -24.778 0.070   -24.201 1.000 169.413 ? 480 CYS EEE N   1 
ATOM   7014  C CA  . CYS E 1 151 ? -25.909 -0.376  -25.050 1.000 168.144 ? 480 CYS EEE CA  1 
ATOM   7015  C C   . CYS E 1 151 ? -27.116 0.521   -24.834 1.000 169.541 ? 480 CYS EEE C   1 
ATOM   7016  O O   . CYS E 1 151 ? -27.482 0.765   -23.675 1.000 169.290 ? 480 CYS EEE O   1 
ATOM   7017  C CB  . CYS E 1 151 ? -26.254 -1.830  -24.798 1.000 162.932 ? 480 CYS EEE CB  1 
ATOM   7018  S SG  . CYS E 1 151 ? -24.998 -2.859  -25.580 1.000 164.248 ? 480 CYS EEE SG  1 
ATOM   7019  N N   . ASN E 1 152 ? -27.706 0.952   -25.945 1.000 171.863 ? 481 ASN EEE N   1 
ATOM   7020  C CA  . ASN E 1 152 ? -28.875 1.861   -26.003 1.000 173.858 ? 481 ASN EEE CA  1 
ATOM   7021  C C   . ASN E 1 152 ? -30.093 1.005   -26.371 1.000 168.533 ? 481 ASN EEE C   1 
ATOM   7022  O O   . ASN E 1 152 ? -30.823 1.373   -27.312 1.000 171.713 ? 481 ASN EEE O   1 
ATOM   7023  C CB  . ASN E 1 152 ? -28.583 3.028   -26.954 1.000 182.023 ? 481 ASN EEE CB  1 
ATOM   7024  C CG  . ASN E 1 152 ? -27.668 2.652   -28.108 1.000 187.656 ? 481 ASN EEE CG  1 
ATOM   7025  O OD1 . ASN E 1 152 ? -26.866 1.726   -27.994 1.000 188.947 ? 481 ASN EEE OD1 1 
ATOM   7026  N ND2 . ASN E 1 152 ? -27.767 3.362   -29.223 1.000 192.215 ? 481 ASN EEE ND2 1 
ATOM   7027  N N   . GLY E 1 153 ? -30.279 -0.116  -25.665 1.000 161.445 ? 482 GLY EEE N   1 
ATOM   7028  C CA  . GLY E 1 153 ? -31.317 -1.124  -25.955 1.000 157.921 ? 482 GLY EEE CA  1 
ATOM   7029  C C   . GLY E 1 153 ? -30.990 -1.941  -27.195 1.000 158.167 ? 482 GLY EEE C   1 
ATOM   7030  O O   . GLY E 1 153 ? -31.860 -2.713  -27.642 1.000 158.178 ? 482 GLY EEE O   1 
ATOM   7031  N N   . VAL E 1 154 ? -29.787 -1.770  -27.746 1.000 159.039 ? 483 VAL EEE N   1 
ATOM   7032  C CA  . VAL E 1 154 ? -29.292 -2.524  -28.932 1.000 158.074 ? 483 VAL EEE CA  1 
ATOM   7033  C C   . VAL E 1 154 ? -28.578 -3.769  -28.411 1.000 154.696 ? 483 VAL EEE C   1 
ATOM   7034  O O   . VAL E 1 154 ? -27.760 -3.624  -27.485 1.000 157.347 ? 483 VAL EEE O   1 
ATOM   7035  C CB  . VAL E 1 154 ? -28.354 -1.650  -29.780 1.000 162.826 ? 483 VAL EEE CB  1 
ATOM   7036  C CG1 . VAL E 1 154 ? -27.791 -2.411  -30.969 1.000 165.478 ? 483 VAL EEE CG1 1 
ATOM   7037  C CG2 . VAL E 1 154 ? -29.049 -0.375  -30.230 1.000 165.492 ? 483 VAL EEE CG2 1 
ATOM   7038  N N   . GLU E 1 155 ? -28.883 -4.939  -28.969 1.000 150.557 ? 484 GLU EEE N   1 
ATOM   7039  C CA  . GLU E 1 155 ? -28.281 -6.222  -28.530 1.000 148.630 ? 484 GLU EEE CA  1 
ATOM   7040  C C   . GLU E 1 155 ? -27.054 -6.523  -29.392 1.000 151.831 ? 484 GLU EEE C   1 
ATOM   7041  O O   . GLU E 1 155 ? -26.885 -5.840  -30.412 1.000 155.416 ? 484 GLU EEE O   1 
ATOM   7042  C CB  . GLU E 1 155 ? -29.317 -7.336  -28.617 1.000 145.923 ? 484 GLU EEE CB  1 
ATOM   7043  C CG  . GLU E 1 155 ? -30.171 -7.422  -27.375 1.000 142.959 ? 484 GLU EEE CG  1 
ATOM   7044  C CD  . GLU E 1 155 ? -31.076 -8.633  -27.348 1.000 140.997 ? 484 GLU EEE CD  1 
ATOM   7045  O OE1 . GLU E 1 155 ? -30.530 -9.753  -27.402 1.000 140.730 ? 484 GLU EEE OE1 1 
ATOM   7046  O OE2 . GLU E 1 155 ? -32.318 -8.451  -27.294 1.000 140.088 ? 484 GLU EEE OE2 1 
ATOM   7047  N N   . GLY E 1 156 ? -26.229 -7.493  -28.979 1.000 152.642 ? 485 GLY EEE N   1 
ATOM   7048  C CA  . GLY E 1 156 ? -25.161 -8.086  -29.808 1.000 156.580 ? 485 GLY EEE CA  1 
ATOM   7049  C C   . GLY E 1 156 ? -23.886 -8.391  -29.033 1.000 157.590 ? 485 GLY EEE C   1 
ATOM   7050  O O   . GLY E 1 156 ? -23.951 -9.072  -27.974 1.000 155.030 ? 485 GLY EEE O   1 
ATOM   7051  N N   . PHE E 1 157 ? -22.751 -7.936  -29.568 1.000 161.458 ? 486 PHE EEE N   1 
ATOM   7052  C CA  . PHE E 1 157 ? -21.390 -8.199  -29.037 1.000 164.509 ? 486 PHE EEE CA  1 
ATOM   7053  C C   . PHE E 1 157 ? -21.286 -7.593  -27.636 1.000 161.758 ? 486 PHE EEE C   1 
ATOM   7054  O O   . PHE E 1 157 ? -21.318 -6.368  -27.542 1.000 163.610 ? 486 PHE EEE O   1 
ATOM   7055  C CB  . PHE E 1 157 ? -20.342 -7.623  -29.993 1.000 173.153 ? 486 PHE EEE CB  1 
ATOM   7056  C CG  . PHE E 1 157 ? -18.918 -8.019  -29.693 1.000 179.920 ? 486 PHE EEE CG  1 
ATOM   7057  C CD1 . PHE E 1 157 ? -18.162 -7.311  -28.767 1.000 182.878 ? 486 PHE EEE CD1 1 
ATOM   7058  C CD2 . PHE E 1 157 ? -18.327 -9.091  -30.348 1.000 184.126 ? 486 PHE EEE CD2 1 
ATOM   7059  C CE1 . PHE E 1 157 ? -16.849 -7.673  -28.497 1.000 187.078 ? 486 PHE EEE CE1 1 
ATOM   7060  C CE2 . PHE E 1 157 ? -17.016 -9.452  -30.073 1.000 188.458 ? 486 PHE EEE CE2 1 
ATOM   7061  C CZ  . PHE E 1 157 ? -16.278 -8.742  -29.151 1.000 189.655 ? 486 PHE EEE CZ  1 
ATOM   7062  N N   . ASN E 1 158 ? -21.202 -8.428  -26.595 1.000 158.740 ? 487 ASN EEE N   1 
ATOM   7063  C CA  . ASN E 1 158 ? -21.084 -8.016  -25.166 1.000 156.322 ? 487 ASN EEE CA  1 
ATOM   7064  C C   . ASN E 1 158 ? -22.369 -7.321  -24.707 1.000 151.921 ? 487 ASN EEE C   1 
ATOM   7065  O O   . ASN E 1 158 ? -22.297 -6.538  -23.720 1.000 150.070 ? 487 ASN EEE O   1 
ATOM   7066  C CB  . ASN E 1 158 ? -19.880 -7.109  -24.897 1.000 161.284 ? 487 ASN EEE CB  1 
ATOM   7067  C CG  . ASN E 1 158 ? -18.596 -7.608  -25.524 1.000 166.923 ? 487 ASN EEE CG  1 
ATOM   7068  O OD1 . ASN E 1 158 ? -18.514 -8.760  -25.943 1.000 168.173 ? 487 ASN EEE OD1 1 
ATOM   7069  N ND2 . ASN E 1 158 ? -17.585 -6.752  -25.587 1.000 171.547 ? 487 ASN EEE ND2 1 
ATOM   7070  N N   . CYS E 1 159 ? -23.494 -7.573  -25.389 1.000 150.357 ? 488 CYS EEE N   1 
ATOM   7071  C CA  . CYS E 1 159 ? -24.845 -7.101  -24.976 1.000 148.111 ? 488 CYS EEE CA  1 
ATOM   7072  C C   . CYS E 1 159 ? -25.927 -8.142  -25.254 1.000 145.416 ? 488 CYS EEE C   1 
ATOM   7073  O O   . CYS E 1 159 ? -26.115 -8.525  -26.423 1.000 144.946 ? 488 CYS EEE O   1 
ATOM   7074  C CB  . CYS E 1 159 ? -25.220 -5.772  -25.604 1.000 150.246 ? 488 CYS EEE CB  1 
ATOM   7075  S SG  . CYS E 1 159 ? -24.955 -4.456  -24.398 1.000 151.738 ? 488 CYS EEE SG  1 
ATOM   7076  N N   . TYR E 1 160 ? -26.630 -8.528  -24.187 1.000 143.478 ? 489 TYR EEE N   1 
ATOM   7077  C CA  . TYR E 1 160 ? -27.521 -9.710  -24.117 1.000 141.111 ? 489 TYR EEE CA  1 
ATOM   7078  C C   . TYR E 1 160 ? -28.821 -9.304  -23.426 1.000 136.685 ? 489 TYR EEE C   1 
ATOM   7079  O O   . TYR E 1 160 ? -28.791 -8.416  -22.550 1.000 136.538 ? 489 TYR EEE O   1 
ATOM   7080  C CB  . TYR E 1 160 ? -26.821 -10.851 -23.374 1.000 141.998 ? 489 TYR EEE CB  1 
ATOM   7081  C CG  . TYR E 1 160 ? -25.357 -10.991 -23.710 1.000 147.740 ? 489 TYR EEE CG  1 
ATOM   7082  C CD1 . TYR E 1 160 ? -24.957 -11.398 -24.973 1.000 152.718 ? 489 TYR EEE CD1 1 
ATOM   7083  C CD2 . TYR E 1 160 ? -24.370 -10.666 -22.790 1.000 149.668 ? 489 TYR EEE CD2 1 
ATOM   7084  C CE1 . TYR E 1 160 ? -23.617 -11.498 -25.310 1.000 157.367 ? 489 TYR EEE CE1 1 
ATOM   7085  C CE2 . TYR E 1 160 ? -23.025 -10.761 -23.108 1.000 153.884 ? 489 TYR EEE CE2 1 
ATOM   7086  C CZ  . TYR E 1 160 ? -22.649 -11.193 -24.368 1.000 158.061 ? 489 TYR EEE CZ  1 
ATOM   7087  O OH  . TYR E 1 160 ? -21.326 -11.297 -24.691 1.000 163.918 ? 489 TYR EEE OH  1 
ATOM   7088  N N   . PHE E 1 161 ? -29.920 -9.937  -23.841 1.000 134.127 ? 490 PHE EEE N   1 
ATOM   7089  C CA  . PHE E 1 161 ? -31.236 -9.941  -23.154 1.000 130.658 ? 490 PHE EEE CA  1 
ATOM   7090  C C   . PHE E 1 161 ? -31.096 -10.791 -21.896 1.000 127.738 ? 490 PHE EEE C   1 
ATOM   7091  O O   . PHE E 1 161 ? -30.601 -11.912 -21.974 1.000 126.509 ? 490 PHE EEE O   1 
ATOM   7092  C CB  . PHE E 1 161 ? -32.306 -10.491 -24.098 1.000 130.752 ? 490 PHE EEE CB  1 
ATOM   7093  C CG  . PHE E 1 161 ? -33.731 -10.384 -23.616 1.000 128.393 ? 490 PHE EEE CG  1 
ATOM   7094  C CD1 . PHE E 1 161 ? -34.399 -9.173  -23.652 1.000 129.810 ? 490 PHE EEE CD1 1 
ATOM   7095  C CD2 . PHE E 1 161 ? -34.421 -11.503 -23.172 1.000 126.176 ? 490 PHE EEE CD2 1 
ATOM   7096  C CE1 . PHE E 1 161 ? -35.720 -9.083  -23.240 1.000 129.375 ? 490 PHE EEE CE1 1 
ATOM   7097  C CE2 . PHE E 1 161 ? -35.739 -11.410 -22.755 1.000 125.154 ? 490 PHE EEE CE2 1 
ATOM   7098  C CZ  . PHE E 1 161 ? -36.387 -10.200 -22.789 1.000 126.661 ? 490 PHE EEE CZ  1 
ATOM   7099  N N   . PRO E 1 162 ? -31.510 -10.293 -20.706 1.000 126.675 ? 491 PRO EEE N   1 
ATOM   7100  C CA  . PRO E 1 162 ? -31.092 -10.893 -19.438 1.000 124.580 ? 491 PRO EEE CA  1 
ATOM   7101  C C   . PRO E 1 162 ? -31.854 -12.155 -19.002 1.000 122.216 ? 491 PRO EEE C   1 
ATOM   7102  O O   . PRO E 1 162 ? -31.387 -12.789 -18.074 1.000 121.811 ? 491 PRO EEE O   1 
ATOM   7103  C CB  . PRO E 1 162 ? -31.332 -9.759  -18.433 1.000 124.782 ? 491 PRO EEE CB  1 
ATOM   7104  C CG  . PRO E 1 162 ? -32.497 -8.986  -19.013 1.000 125.600 ? 491 PRO EEE CG  1 
ATOM   7105  C CD  . PRO E 1 162 ? -32.380 -9.120  -20.517 1.000 127.401 ? 491 PRO EEE CD  1 
ATOM   7106  N N   . LEU E 1 163 ? -32.969 -12.491 -19.662 1.000 122.207 ? 492 LEU EEE N   1 
ATOM   7107  C CA  . LEU E 1 163 ? -33.809 -13.673 -19.327 1.000 121.688 ? 492 LEU EEE CA  1 
ATOM   7108  C C   . LEU E 1 163 ? -33.590 -14.793 -20.341 1.000 121.534 ? 492 LEU EEE C   1 
ATOM   7109  O O   . LEU E 1 163 ? -33.122 -14.507 -21.460 1.000 124.086 ? 492 LEU EEE O   1 
ATOM   7110  C CB  . LEU E 1 163 ? -35.286 -13.273 -19.324 1.000 123.851 ? 492 LEU EEE CB  1 
ATOM   7111  C CG  . LEU E 1 163 ? -35.704 -12.215 -18.306 1.000 126.913 ? 492 LEU EEE CG  1 
ATOM   7112  C CD1 . LEU E 1 163 ? -37.210 -12.256 -18.100 1.000 127.072 ? 492 LEU EEE CD1 1 
ATOM   7113  C CD2 . LEU E 1 163 ? -34.994 -12.395 -16.971 1.000 127.574 ? 492 LEU EEE CD2 1 
ATOM   7114  N N   . GLN E 1 164 ? -33.959 -16.014 -19.950 1.000 120.342 ? 493 GLN EEE N   1 
ATOM   7115  C CA  . GLN E 1 164 ? -33.939 -17.218 -20.818 1.000 122.122 ? 493 GLN EEE CA  1 
ATOM   7116  C C   . GLN E 1 164 ? -35.068 -18.160 -20.391 1.000 120.955 ? 493 GLN EEE C   1 
ATOM   7117  O O   . GLN E 1 164 ? -35.650 -17.935 -19.304 1.000 120.273 ? 493 GLN EEE O   1 
ATOM   7118  C CB  . GLN E 1 164 ? -32.573 -17.896 -20.718 1.000 122.641 ? 493 GLN EEE CB  1 
ATOM   7119  C CG  . GLN E 1 164 ? -32.198 -18.721 -21.938 1.000 123.781 ? 493 GLN EEE CG  1 
ATOM   7120  C CD  . GLN E 1 164 ? -30.707 -18.959 -21.978 1.000 124.588 ? 493 GLN EEE CD  1 
ATOM   7121  O OE1 . GLN E 1 164 ? -30.033 -18.709 -22.986 1.000 125.836 ? 493 GLN EEE OE1 1 
ATOM   7122  N NE2 . GLN E 1 164 ? -30.183 -19.426 -20.851 1.000 123.878 ? 493 GLN EEE NE2 1 
ATOM   7123  N N   . SER E 1 165 ? -35.367 -19.165 -21.218 1.000 121.451 ? 494 SER EEE N   1 
ATOM   7124  C CA  . SER E 1 165 ? -36.378 -20.218 -20.936 1.000 120.644 ? 494 SER EEE CA  1 
ATOM   7125  C C   . SER E 1 165 ? -35.697 -21.445 -20.329 1.000 119.321 ? 494 SER EEE C   1 
ATOM   7126  O O   . SER E 1 165 ? -34.449 -21.516 -20.355 1.000 117.584 ? 494 SER EEE O   1 
ATOM   7127  C CB  . SER E 1 165 ? -37.158 -20.585 -22.168 1.000 122.741 ? 494 SER EEE CB  1 
ATOM   7128  O OG  . SER E 1 165 ? -38.165 -19.621 -22.436 1.000 121.924 ? 494 SER EEE OG  1 
ATOM   7129  N N   . TYR E 1 166 ? -36.505 -22.378 -19.829 1.000 118.853 ? 495 TYR EEE N   1 
ATOM   7130  C CA  . TYR E 1 166 ? -36.037 -23.587 -19.113 1.000 120.470 ? 495 TYR EEE CA  1 
ATOM   7131  C C   . TYR E 1 166 ? -36.090 -24.810 -20.029 1.000 123.431 ? 495 TYR EEE C   1 
ATOM   7132  O O   . TYR E 1 166 ? -35.134 -25.624 -19.982 1.000 125.277 ? 495 TYR EEE O   1 
ATOM   7133  C CB  . TYR E 1 166 ? -36.855 -23.801 -17.840 1.000 119.734 ? 495 TYR EEE CB  1 
ATOM   7134  C CG  . TYR E 1 166 ? -36.194 -23.254 -16.603 1.000 118.125 ? 495 TYR EEE CG  1 
ATOM   7135  C CD1 . TYR E 1 166 ? -34.896 -23.608 -16.282 1.000 118.551 ? 495 TYR EEE CD1 1 
ATOM   7136  C CD2 . TYR E 1 166 ? -36.863 -22.394 -15.751 1.000 118.909 ? 495 TYR EEE CD2 1 
ATOM   7137  C CE1 . TYR E 1 166 ? -34.270 -23.118 -15.153 1.000 119.396 ? 495 TYR EEE CE1 1 
ATOM   7138  C CE2 . TYR E 1 166 ? -36.259 -21.899 -14.609 1.000 119.068 ? 495 TYR EEE CE2 1 
ATOM   7139  C CZ  . TYR E 1 166 ? -34.957 -22.263 -14.313 1.000 120.895 ? 495 TYR EEE CZ  1 
ATOM   7140  O OH  . TYR E 1 166 ? -34.340 -21.784 -13.195 1.000 125.945 ? 495 TYR EEE OH  1 
ATOM   7141  N N   . GLY E 1 167 ? -37.169 -24.950 -20.804 1.000 124.226 ? 496 GLY EEE N   1 
ATOM   7142  C CA  . GLY E 1 167 ? -37.352 -26.083 -21.730 1.000 127.747 ? 496 GLY EEE CA  1 
ATOM   7143  C C   . GLY E 1 167 ? -37.408 -27.396 -20.971 1.000 126.370 ? 496 GLY EEE C   1 
ATOM   7144  O O   . GLY E 1 167 ? -36.474 -28.212 -21.091 1.000 127.668 ? 496 GLY EEE O   1 
ATOM   7145  N N   . PHE E 1 168 ? -38.460 -27.569 -20.180 1.000 125.189 ? 497 PHE EEE N   1 
ATOM   7146  C CA  . PHE E 1 168 ? -38.737 -28.810 -19.421 1.000 127.010 ? 497 PHE EEE CA  1 
ATOM   7147  C C   . PHE E 1 168 ? -39.393 -29.810 -20.371 1.000 130.853 ? 497 PHE EEE C   1 
ATOM   7148  O O   . PHE E 1 168 ? -40.476 -29.500 -20.903 1.000 130.775 ? 497 PHE EEE O   1 
ATOM   7149  C CB  . PHE E 1 168 ? -39.626 -28.509 -18.215 1.000 125.428 ? 497 PHE EEE CB  1 
ATOM   7150  C CG  . PHE E 1 168 ? -39.018 -27.563 -17.214 1.000 122.418 ? 497 PHE EEE CG  1 
ATOM   7151  C CD1 . PHE E 1 168 ? -37.898 -27.933 -16.491 1.000 122.437 ? 497 PHE EEE CD1 1 
ATOM   7152  C CD2 . PHE E 1 168 ? -39.564 -26.309 -16.991 1.000 120.967 ? 497 PHE EEE CD2 1 
ATOM   7153  C CE1 . PHE E 1 168 ? -37.337 -27.069 -15.566 1.000 120.703 ? 497 PHE EEE CE1 1 
ATOM   7154  C CE2 . PHE E 1 168 ? -39.002 -25.447 -16.063 1.000 119.729 ? 497 PHE EEE CE2 1 
ATOM   7155  C CZ  . PHE E 1 168 ? -37.887 -25.826 -15.355 1.000 118.881 ? 497 PHE EEE CZ  1 
ATOM   7156  N N   . GLN E 1 169 ? -38.729 -30.946 -20.593 1.000 134.571 ? 498 GLN EEE N   1 
ATOM   7157  C CA  . GLN E 1 169 ? -39.258 -32.093 -21.376 1.000 138.722 ? 498 GLN EEE CA  1 
ATOM   7158  C C   . GLN E 1 169 ? -39.507 -33.242 -20.398 1.000 140.126 ? 498 GLN EEE C   1 
ATOM   7159  O O   . GLN E 1 169 ? -38.768 -33.403 -19.428 1.000 139.083 ? 498 GLN EEE O   1 
ATOM   7160  C CB  . GLN E 1 169 ? -38.300 -32.432 -22.521 1.000 141.355 ? 498 GLN EEE CB  1 
ATOM   7161  C CG  . GLN E 1 169 ? -37.790 -31.196 -23.257 1.000 141.660 ? 498 GLN EEE CG  1 
ATOM   7162  C CD  . GLN E 1 169 ? -37.765 -31.341 -24.758 1.000 147.302 ? 498 GLN EEE CD  1 
ATOM   7163  O OE1 . GLN E 1 169 ? -37.310 -32.344 -25.296 1.000 152.020 ? 498 GLN EEE OE1 1 
ATOM   7164  N NE2 . GLN E 1 169 ? -38.258 -30.328 -25.453 1.000 148.247 ? 498 GLN EEE NE2 1 
ATOM   7165  N N   . PRO E 1 170 ? -40.595 -34.029 -20.572 1.000 142.249 ? 499 PRO EEE N   1 
ATOM   7166  C CA  . PRO E 1 170 ? -40.844 -35.204 -19.737 1.000 142.965 ? 499 PRO EEE CA  1 
ATOM   7167  C C   . PRO E 1 170 ? -39.683 -36.211 -19.730 1.000 145.573 ? 499 PRO EEE C   1 
ATOM   7168  O O   . PRO E 1 170 ? -39.568 -36.947 -18.772 1.000 144.898 ? 499 PRO EEE O   1 
ATOM   7169  C CB  . PRO E 1 170 ? -42.079 -35.860 -20.374 1.000 147.164 ? 499 PRO EEE CB  1 
ATOM   7170  C CG  . PRO E 1 170 ? -42.776 -34.738 -21.110 1.000 147.251 ? 499 PRO EEE CG  1 
ATOM   7171  C CD  . PRO E 1 170 ? -41.671 -33.796 -21.545 1.000 145.120 ? 499 PRO EEE CD  1 
ATOM   7172  N N   . THR E 1 171 ? -38.879 -36.224 -20.800 1.000 149.605 ? 500 THR EEE N   1 
ATOM   7173  C CA  . THR E 1 171 ? -37.740 -37.158 -21.021 1.000 153.298 ? 500 THR EEE CA  1 
ATOM   7174  C C   . THR E 1 171 ? -36.449 -36.584 -20.420 1.000 150.156 ? 500 THR EEE C   1 
ATOM   7175  O O   . THR E 1 171 ? -35.475 -37.345 -20.336 1.000 149.891 ? 500 THR EEE O   1 
ATOM   7176  C CB  . THR E 1 171 ? -37.557 -37.457 -22.516 1.000 159.686 ? 500 THR EEE CB  1 
ATOM   7177  O OG1 . THR E 1 171 ? -37.521 -36.203 -23.197 1.000 161.121 ? 500 THR EEE OG1 1 
ATOM   7178  C CG2 . THR E 1 171 ? -38.654 -38.319 -23.105 1.000 163.754 ? 500 THR EEE CG2 1 
ATOM   7179  N N   . ASN E 1 172 ? -36.437 -35.305 -20.026 1.000 148.876 ? 501 ASN EEE N   1 
ATOM   7180  C CA  . ASN E 1 172 ? -35.296 -34.659 -19.316 1.000 149.507 ? 501 ASN EEE CA  1 
ATOM   7181  C C   . ASN E 1 172 ? -34.901 -35.485 -18.087 1.000 150.195 ? 501 ASN EEE C   1 
ATOM   7182  O O   . ASN E 1 172 ? -35.795 -36.093 -17.471 1.000 151.319 ? 501 ASN EEE O   1 
ATOM   7183  C CB  . ASN E 1 172 ? -35.614 -33.233 -18.854 1.000 147.392 ? 501 ASN EEE CB  1 
ATOM   7184  C CG  . ASN E 1 172 ? -35.008 -32.168 -19.740 1.000 150.799 ? 501 ASN EEE CG  1 
ATOM   7185  O OD1 . ASN E 1 172 ? -35.725 -31.294 -20.228 1.000 156.031 ? 501 ASN EEE OD1 1 
ATOM   7186  N ND2 . ASN E 1 172 ? -33.695 -32.221 -19.935 1.000 151.257 ? 501 ASN EEE ND2 1 
ATOM   7187  N N   . GLY E 1 173 ? -33.610 -35.475 -17.738 1.000 151.271 ? 502 GLY EEE N   1 
ATOM   7188  C CA  . GLY E 1 173 ? -33.072 -36.077 -16.501 1.000 150.133 ? 502 GLY EEE CA  1 
ATOM   7189  C C   . GLY E 1 173 ? -33.637 -35.397 -15.266 1.000 144.559 ? 502 GLY EEE C   1 
ATOM   7190  O O   . GLY E 1 173 ? -33.971 -34.193 -15.357 1.000 141.761 ? 502 GLY EEE O   1 
ATOM   7191  N N   . VAL E 1 174 ? -33.713 -36.127 -14.147 1.000 142.335 ? 503 VAL EEE N   1 
ATOM   7192  C CA  . VAL E 1 174 ? -34.487 -35.734 -12.927 1.000 136.398 ? 503 VAL EEE CA  1 
ATOM   7193  C C   . VAL E 1 174 ? -34.057 -34.327 -12.498 1.000 129.286 ? 503 VAL EEE C   1 
ATOM   7194  O O   . VAL E 1 174 ? -34.910 -33.600 -11.973 1.000 124.045 ? 503 VAL EEE O   1 
ATOM   7195  C CB  . VAL E 1 174 ? -34.325 -36.730 -11.758 1.000 138.163 ? 503 VAL EEE CB  1 
ATOM   7196  C CG1 . VAL E 1 174 ? -35.248 -36.363 -10.603 1.000 134.708 ? 503 VAL EEE CG1 1 
ATOM   7197  C CG2 . VAL E 1 174 ? -34.544 -38.184 -12.170 1.000 143.392 ? 503 VAL EEE CG2 1 
ATOM   7198  N N   . GLY E 1 175 ? -32.787 -33.974 -12.716 1.000 128.352 ? 504 GLY EEE N   1 
ATOM   7199  C CA  . GLY E 1 175 ? -32.215 -32.657 -12.374 1.000 127.308 ? 504 GLY EEE CA  1 
ATOM   7200  C C   . GLY E 1 175 ? -32.788 -31.529 -13.219 1.000 126.327 ? 504 GLY EEE C   1 
ATOM   7201  O O   . GLY E 1 175 ? -33.019 -30.435 -12.664 1.000 121.971 ? 504 GLY EEE O   1 
ATOM   7202  N N   . TYR E 1 176 ? -32.984 -31.764 -14.521 1.000 130.645 ? 505 TYR EEE N   1 
ATOM   7203  C CA  . TYR E 1 176 ? -33.506 -30.761 -15.486 1.000 132.402 ? 505 TYR EEE CA  1 
ATOM   7204  C C   . TYR E 1 176 ? -35.018 -30.947 -15.653 1.000 130.086 ? 505 TYR EEE C   1 
ATOM   7205  O O   . TYR E 1 176 ? -35.576 -30.436 -16.650 1.000 128.866 ? 505 TYR EEE O   1 
ATOM   7206  C CB  . TYR E 1 176 ? -32.751 -30.854 -16.812 1.000 140.231 ? 505 TYR EEE CB  1 
ATOM   7207  C CG  . TYR E 1 176 ? -31.265 -30.614 -16.707 1.000 144.946 ? 505 TYR EEE CG  1 
ATOM   7208  C CD1 . TYR E 1 176 ? -30.397 -31.649 -16.389 1.000 148.922 ? 505 TYR EEE CD1 1 
ATOM   7209  C CD2 . TYR E 1 176 ? -30.721 -29.356 -16.926 1.000 144.294 ? 505 TYR EEE CD2 1 
ATOM   7210  C CE1 . TYR E 1 176 ? -29.028 -31.444 -16.295 1.000 150.743 ? 505 TYR EEE CE1 1 
ATOM   7211  C CE2 . TYR E 1 176 ? -29.355 -29.133 -16.839 1.000 145.526 ? 505 TYR EEE CE2 1 
ATOM   7212  C CZ  . TYR E 1 176 ? -28.506 -30.180 -16.517 1.000 150.003 ? 505 TYR EEE CZ  1 
ATOM   7213  O OH  . TYR E 1 176 ? -27.161 -29.967 -16.424 1.000 154.901 ? 505 TYR EEE OH  1 
ATOM   7214  N N   . GLN E 1 177 ? -35.650 -31.662 -14.711 1.000 128.035 ? 506 GLN EEE N   1 
ATOM   7215  C CA  . GLN E 1 177 ? -37.124 -31.676 -14.497 1.000 125.265 ? 506 GLN EEE CA  1 
ATOM   7216  C C   . GLN E 1 177 ? -37.489 -30.479 -13.619 1.000 121.577 ? 506 GLN EEE C   1 
ATOM   7217  O O   . GLN E 1 177 ? -36.687 -30.046 -12.797 1.000 122.375 ? 506 GLN EEE O   1 
ATOM   7218  C CB  . GLN E 1 177 ? -37.586 -32.990 -13.858 1.000 125.118 ? 506 GLN EEE CB  1 
ATOM   7219  C CG  . GLN E 1 177 ? -37.531 -34.181 -14.807 1.000 128.536 ? 506 GLN EEE CG  1 
ATOM   7220  C CD  . GLN E 1 177 ? -38.098 -35.450 -14.217 1.000 129.351 ? 506 GLN EEE CD  1 
ATOM   7221  O OE1 . GLN E 1 177 ? -38.855 -35.434 -13.250 1.000 127.840 ? 506 GLN EEE OE1 1 
ATOM   7222  N NE2 . GLN E 1 177 ? -37.738 -36.578 -14.805 1.000 131.849 ? 506 GLN EEE NE2 1 
ATOM   7223  N N   . PRO E 1 178 ? -38.702 -29.904 -13.758 1.000 119.601 ? 507 PRO EEE N   1 
ATOM   7224  C CA  . PRO E 1 178 ? -39.100 -28.736 -12.978 1.000 117.819 ? 507 PRO EEE CA  1 
ATOM   7225  C C   . PRO E 1 178 ? -39.634 -29.096 -11.582 1.000 118.785 ? 507 PRO EEE C   1 
ATOM   7226  O O   . PRO E 1 178 ? -40.535 -29.906 -11.486 1.000 120.000 ? 507 PRO EEE O   1 
ATOM   7227  C CB  . PRO E 1 178 ? -40.220 -28.133 -13.831 1.000 118.242 ? 507 PRO EEE CB  1 
ATOM   7228  C CG  . PRO E 1 178 ? -40.860 -29.326 -14.508 1.000 121.220 ? 507 PRO EEE CG  1 
ATOM   7229  C CD  . PRO E 1 178 ? -39.758 -30.352 -14.674 1.000 122.526 ? 507 PRO EEE CD  1 
ATOM   7230  N N   . TYR E 1 179 ? -39.073 -28.485 -10.536 1.000 118.729 ? 508 TYR EEE N   1 
ATOM   7231  C CA  . TYR E 1 179 ? -39.586 -28.582 -9.146  1.000 118.868 ? 508 TYR EEE CA  1 
ATOM   7232  C C   . TYR E 1 179 ? -40.329 -27.291 -8.793  1.000 116.842 ? 508 TYR EEE C   1 
ATOM   7233  O O   . TYR E 1 179 ? -39.861 -26.186 -9.121  1.000 113.348 ? 508 TYR EEE O   1 
ATOM   7234  C CB  . TYR E 1 179 ? -38.454 -28.865 -8.159  1.000 119.653 ? 508 TYR EEE CB  1 
ATOM   7235  C CG  . TYR E 1 179 ? -37.969 -30.291 -8.147  1.000 122.571 ? 508 TYR EEE CG  1 
ATOM   7236  C CD1 . TYR E 1 179 ? -37.431 -30.879 -9.281  1.000 125.269 ? 508 TYR EEE CD1 1 
ATOM   7237  C CD2 . TYR E 1 179 ? -38.012 -31.051 -6.989  1.000 124.623 ? 508 TYR EEE CD2 1 
ATOM   7238  C CE1 . TYR E 1 179 ? -36.960 -32.184 -9.267  1.000 128.641 ? 508 TYR EEE CE1 1 
ATOM   7239  C CE2 . TYR E 1 179 ? -37.544 -32.358 -6.958  1.000 128.063 ? 508 TYR EEE CE2 1 
ATOM   7240  C CZ  . TYR E 1 179 ? -37.014 -32.931 -8.102  1.000 128.983 ? 508 TYR EEE CZ  1 
ATOM   7241  O OH  . TYR E 1 179 ? -36.552 -34.218 -8.072  1.000 129.193 ? 508 TYR EEE OH  1 
ATOM   7242  N N   . ARG E 1 180 ? -41.484 -27.450 -8.154  1.000 118.664 ? 509 ARG EEE N   1 
ATOM   7243  C CA  . ARG E 1 180 ? -42.299 -26.338 -7.610  1.000 120.308 ? 509 ARG EEE CA  1 
ATOM   7244  C C   . ARG E 1 180 ? -41.857 -26.085 -6.169  1.000 120.178 ? 509 ARG EEE C   1 
ATOM   7245  O O   . ARG E 1 180 ? -41.852 -27.045 -5.369  1.000 124.470 ? 509 ARG EEE O   1 
ATOM   7246  C CB  . ARG E 1 180 ? -43.789 -26.680 -7.687  1.000 122.889 ? 509 ARG EEE CB  1 
ATOM   7247  C CG  . ARG E 1 180 ? -44.320 -26.680 -9.111  1.000 123.883 ? 509 ARG EEE CG  1 
ATOM   7248  C CD  . ARG E 1 180 ? -45.796 -26.990 -9.187  1.000 125.151 ? 509 ARG EEE CD  1 
ATOM   7249  N NE  . ARG E 1 180 ? -46.289 -26.634 -10.506 1.000 126.333 ? 509 ARG EEE NE  1 
ATOM   7250  C CZ  . ARG E 1 180 ? -47.564 -26.438 -10.805 1.000 130.034 ? 509 ARG EEE CZ  1 
ATOM   7251  N NH1 . ARG E 1 180 ? -48.499 -26.559 -9.875  1.000 130.679 ? 509 ARG EEE NH1 1 
ATOM   7252  N NH2 . ARG E 1 180 ? -47.898 -26.092 -12.034 1.000 133.708 ? 509 ARG EEE NH2 1 
ATOM   7253  N N   . VAL E 1 181 ? -41.541 -24.828 -5.864  1.000 116.719 ? 510 VAL EEE N   1 
ATOM   7254  C CA  . VAL E 1 181 ? -40.939 -24.381 -4.579  1.000 113.172 ? 510 VAL EEE CA  1 
ATOM   7255  C C   . VAL E 1 181 ? -41.881 -23.369 -3.914  1.000 116.090 ? 510 VAL EEE C   1 
ATOM   7256  O O   . VAL E 1 181 ? -42.187 -22.333 -4.552  1.000 119.819 ? 510 VAL EEE O   1 
ATOM   7257  C CB  . VAL E 1 181 ? -39.550 -23.783 -4.851  1.000 110.391 ? 510 VAL EEE CB  1 
ATOM   7258  C CG1 . VAL E 1 181 ? -38.873 -23.298 -3.581  1.000 109.459 ? 510 VAL EEE CG1 1 
ATOM   7259  C CG2 . VAL E 1 181 ? -38.669 -24.774 -5.601  1.000 110.959 ? 510 VAL EEE CG2 1 
ATOM   7260  N N   . VAL E 1 182 ? -42.333 -23.666 -2.689  1.000 115.993 ? 511 VAL EEE N   1 
ATOM   7261  C CA  . VAL E 1 182 ? -42.979 -22.690 -1.759  1.000 114.044 ? 511 VAL EEE CA  1 
ATOM   7262  C C   . VAL E 1 182 ? -41.966 -22.315 -0.673  1.000 112.719 ? 511 VAL EEE C   1 
ATOM   7263  O O   . VAL E 1 182 ? -41.252 -23.220 -0.190  1.000 112.933 ? 511 VAL EEE O   1 
ATOM   7264  C CB  . VAL E 1 182 ? -44.256 -23.265 -1.128  1.000 114.774 ? 511 VAL EEE CB  1 
ATOM   7265  C CG1 . VAL E 1 182 ? -44.889 -22.271 -0.173  1.000 117.173 ? 511 VAL EEE CG1 1 
ATOM   7266  C CG2 . VAL E 1 182 ? -45.252 -23.704 -2.181  1.000 115.590 ? 511 VAL EEE CG2 1 
ATOM   7267  N N   . VAL E 1 183 ? -41.907 -21.036 -0.301  1.000 111.715 ? 512 VAL EEE N   1 
ATOM   7268  C CA  . VAL E 1 183 ? -40.990 -20.546 0.767   1.000 113.479 ? 512 VAL EEE CA  1 
ATOM   7269  C C   . VAL E 1 183 ? -41.813 -19.800 1.810   1.000 115.185 ? 512 VAL EEE C   1 
ATOM   7270  O O   . VAL E 1 183 ? -42.235 -18.654 1.541   1.000 116.239 ? 512 VAL EEE O   1 
ATOM   7271  C CB  . VAL E 1 183 ? -39.863 -19.669 0.202   1.000 115.693 ? 512 VAL EEE CB  1 
ATOM   7272  C CG1 . VAL E 1 183 ? -39.075 -18.978 1.305   1.000 118.332 ? 512 VAL EEE CG1 1 
ATOM   7273  C CG2 . VAL E 1 183 ? -38.947 -20.488 -0.686  1.000 116.040 ? 512 VAL EEE CG2 1 
ATOM   7274  N N   . LEU E 1 184 ? -42.015 -20.449 2.954   1.000 115.479 ? 513 LEU EEE N   1 
ATOM   7275  C CA  . LEU E 1 184 ? -42.769 -19.903 4.105   1.000 117.463 ? 513 LEU EEE CA  1 
ATOM   7276  C C   . LEU E 1 184 ? -41.793 -19.118 4.986   1.000 118.602 ? 513 LEU EEE C   1 
ATOM   7277  O O   . LEU E 1 184 ? -41.087 -19.760 5.772   1.000 118.342 ? 513 LEU EEE O   1 
ATOM   7278  C CB  . LEU E 1 184 ? -43.425 -21.070 4.851   1.000 117.657 ? 513 LEU EEE CB  1 
ATOM   7279  C CG  . LEU E 1 184 ? -44.417 -21.903 4.032   1.000 117.087 ? 513 LEU EEE CG  1 
ATOM   7280  C CD1 . LEU E 1 184 ? -45.074 -22.974 4.891   1.000 118.582 ? 513 LEU EEE CD1 1 
ATOM   7281  C CD2 . LEU E 1 184 ? -45.488 -21.032 3.394   1.000 117.977 ? 513 LEU EEE CD2 1 
ATOM   7282  N N   . SER E 1 185 ? -41.717 -17.796 4.794   1.000 120.942 ? 514 SER EEE N   1 
ATOM   7283  C CA  . SER E 1 185 ? -41.037 -16.827 5.697   1.000 122.462 ? 514 SER EEE CA  1 
ATOM   7284  C C   . SER E 1 185 ? -42.003 -16.439 6.820   1.000 123.570 ? 514 SER EEE C   1 
ATOM   7285  O O   . SER E 1 185 ? -43.199 -16.258 6.532   1.000 123.047 ? 514 SER EEE O   1 
ATOM   7286  C CB  . SER E 1 185 ? -40.531 -15.602 4.957   1.000 124.006 ? 514 SER EEE CB  1 
ATOM   7287  O OG  . SER E 1 185 ? -41.134 -15.479 3.677   1.000 124.182 ? 514 SER EEE OG  1 
ATOM   7288  N N   . PHE E 1 186 ? -41.494 -16.341 8.051   1.000 124.442 ? 515 PHE EEE N   1 
ATOM   7289  C CA  . PHE E 1 186 ? -42.235 -15.910 9.266   1.000 126.558 ? 515 PHE EEE CA  1 
ATOM   7290  C C   . PHE E 1 186 ? -41.629 -14.618 9.801   1.000 127.452 ? 515 PHE EEE C   1 
ATOM   7291  O O   . PHE E 1 186 ? -40.407 -14.598 9.998   1.000 129.518 ? 515 PHE EEE O   1 
ATOM   7292  C CB  . PHE E 1 186 ? -42.125 -16.960 10.369  1.000 127.930 ? 515 PHE EEE CB  1 
ATOM   7293  C CG  . PHE E 1 186 ? -42.711 -18.292 9.995   1.000 128.216 ? 515 PHE EEE CG  1 
ATOM   7294  C CD1 . PHE E 1 186 ? -44.080 -18.494 10.047  1.000 131.463 ? 515 PHE EEE CD1 1 
ATOM   7295  C CD2 . PHE E 1 186 ? -41.901 -19.331 9.569   1.000 126.292 ? 515 PHE EEE CD2 1 
ATOM   7296  C CE1 . PHE E 1 186 ? -44.631 -19.714 9.683   1.000 130.370 ? 515 PHE EEE CE1 1 
ATOM   7297  C CE2 . PHE E 1 186 ? -42.454 -20.550 9.207   1.000 125.798 ? 515 PHE EEE CE2 1 
ATOM   7298  C CZ  . PHE E 1 186 ? -43.818 -20.739 9.259   1.000 126.914 ? 515 PHE EEE CZ  1 
ATOM   7299  N N   . GLU E 1 187 ? -42.441 -13.589 10.038  1.000 159.891 ? 516 GLU EEE N   1 
ATOM   7300  C CA  . GLU E 1 187 ? -41.972 -12.350 10.708  1.000 159.670 ? 516 GLU EEE CA  1 
ATOM   7301  C C   . GLU E 1 187 ? -42.738 -12.196 12.023  1.000 158.869 ? 516 GLU EEE C   1 
ATOM   7302  O O   . GLU E 1 187 ? -43.884 -12.678 12.104  1.000 158.428 ? 516 GLU EEE O   1 
ATOM   7303  C CB  . GLU E 1 187 ? -42.100 -11.133 9.791   1.000 160.866 ? 516 GLU EEE CB  1 
ATOM   7304  C CG  . GLU E 1 187 ? -43.505 -10.868 9.282   1.000 160.224 ? 516 GLU EEE CG  1 
ATOM   7305  C CD  . GLU E 1 187 ? -43.691 -9.503  8.632   1.000 162.161 ? 516 GLU EEE CD  1 
ATOM   7306  O OE1 . GLU E 1 187 ? -42.756 -9.043  7.942   1.000 165.288 ? 516 GLU EEE OE1 1 
ATOM   7307  O OE2 . GLU E 1 187 ? -44.766 -8.893  8.822   1.000 162.119 ? 516 GLU EEE OE2 1 
ATOM   7308  N N   . LEU E 1 188 ? -42.087 -11.586 13.013  1.000 160.058 ? 517 LEU EEE N   1 
ATOM   7309  C CA  . LEU E 1 188 ? -42.644 -11.293 14.356  1.000 160.436 ? 517 LEU EEE CA  1 
ATOM   7310  C C   . LEU E 1 188 ? -42.318 -9.832  14.674  1.000 163.473 ? 517 LEU EEE C   1 
ATOM   7311  O O   . LEU E 1 188 ? -41.175 -9.568  15.060  1.000 165.379 ? 517 LEU EEE O   1 
ATOM   7312  C CB  . LEU E 1 188 ? -42.032 -12.263 15.373  1.000 160.953 ? 517 LEU EEE CB  1 
ATOM   7313  C CG  . LEU E 1 188 ? -42.874 -12.520 16.621  1.000 163.100 ? 517 LEU EEE CG  1 
ATOM   7314  C CD1 . LEU E 1 188 ? -42.460 -13.825 17.289  1.000 162.625 ? 517 LEU EEE CD1 1 
ATOM   7315  C CD2 . LEU E 1 188 ? -42.786 -11.354 17.606  1.000 166.982 ? 517 LEU EEE CD2 1 
ATOM   7316  N N   . LEU E 1 189 ? -43.280 -8.927  14.469  1.000 166.153 ? 518 LEU EEE N   1 
ATOM   7317  C CA  . LEU E 1 189 ? -43.113 -7.457  14.653  1.000 172.161 ? 518 LEU EEE CA  1 
ATOM   7318  C C   . LEU E 1 189 ? -43.259 -7.105  16.145  1.000 177.425 ? 518 LEU EEE C   1 
ATOM   7319  O O   . LEU E 1 189 ? -42.866 -7.938  16.996  1.000 179.137 ? 518 LEU EEE O   1 
ATOM   7320  C CB  . LEU E 1 189 ? -44.145 -6.721  13.782  1.000 171.931 ? 518 LEU EEE CB  1 
ATOM   7321  C CG  . LEU E 1 189 ? -44.193 -7.101  12.300  1.000 168.184 ? 518 LEU EEE CG  1 
ATOM   7322  C CD1 . LEU E 1 189 ? -45.172 -6.217  11.537  1.000 167.657 ? 518 LEU EEE CD1 1 
ATOM   7323  C CD2 . LEU E 1 189 ? -42.810 -7.030  11.672  1.000 168.752 ? 518 LEU EEE CD2 1 
ATOM   7324  N N   . HIS E 1 190 ? -43.759 -5.902  16.453  1.000 181.481 ? 519 HIS EEE N   1 
ATOM   7325  C CA  . HIS E 1 190 ? -44.252 -5.492  17.795  1.000 186.516 ? 519 HIS EEE CA  1 
ATOM   7326  C C   . HIS E 1 190 ? -45.766 -5.235  17.720  1.000 187.921 ? 519 HIS EEE C   1 
ATOM   7327  O O   . HIS E 1 190 ? -46.283 -4.489  18.574  1.000 193.828 ? 519 HIS EEE O   1 
ATOM   7328  C CB  . HIS E 1 190 ? -43.428 -4.298  18.303  1.000 192.674 ? 519 HIS EEE CB  1 
ATOM   7329  C CG  . HIS E 1 190 ? -42.469 -4.625  19.403  1.000 195.422 ? 519 HIS EEE CG  1 
ATOM   7330  N ND1 . HIS E 1 190 ? -42.677 -4.187  20.701  1.000 200.599 ? 519 HIS EEE ND1 1 
ATOM   7331  C CD2 . HIS E 1 190 ? -41.300 -5.305  19.416  1.000 193.807 ? 519 HIS EEE CD2 1 
ATOM   7332  C CE1 . HIS E 1 190 ? -41.686 -4.592  21.467  1.000 202.225 ? 519 HIS EEE CE1 1 
ATOM   7333  N NE2 . HIS E 1 190 ? -40.827 -5.282  20.702  1.000 198.054 ? 519 HIS EEE NE2 1 
ATOM   7334  N N   . ALA E 1 191 ? -46.445 -5.849  16.742  1.000 185.038 ? 520 ALA EEE N   1 
ATOM   7335  C CA  . ALA E 1 191 ? -47.910 -5.791  16.527  1.000 187.430 ? 520 ALA EEE CA  1 
ATOM   7336  C C   . ALA E 1 191 ? -48.533 -7.094  17.023  1.000 186.429 ? 520 ALA EEE C   1 
ATOM   7337  O O   . ALA E 1 191 ? -47.883 -8.138  16.968  1.000 182.935 ? 520 ALA EEE O   1 
ATOM   7338  C CB  . ALA E 1 191 ? -48.205 -5.557  15.061  1.000 185.262 ? 520 ALA EEE CB  1 
ATOM   7339  N N   . PRO E 1 192 ? -49.800 -7.088  17.512  1.000 190.583 ? 521 PRO EEE N   1 
ATOM   7340  C CA  . PRO E 1 192 ? -50.490 -8.325  17.893  1.000 190.133 ? 521 PRO EEE CA  1 
ATOM   7341  C C   . PRO E 1 192 ? -50.498 -9.380  16.771  1.000 184.880 ? 521 PRO EEE C   1 
ATOM   7342  O O   . PRO E 1 192 ? -51.031 -9.104  15.705  1.000 183.781 ? 521 PRO EEE O   1 
ATOM   7343  C CB  . PRO E 1 192 ? -51.923 -7.866  18.223  1.000 195.435 ? 521 PRO EEE CB  1 
ATOM   7344  C CG  . PRO E 1 192 ? -51.779 -6.401  18.595  1.000 200.015 ? 521 PRO EEE CG  1 
ATOM   7345  C CD  . PRO E 1 192 ? -50.623 -5.891  17.758  1.000 196.106 ? 521 PRO EEE CD  1 
ATOM   7346  N N   . ALA E 1 193 ? -49.915 -10.556 17.046  1.000 181.833 ? 522 ALA EEE N   1 
ATOM   7347  C CA  . ALA E 1 193 ? -49.704 -11.676 16.094  1.000 177.633 ? 522 ALA EEE CA  1 
ATOM   7348  C C   . ALA E 1 193 ? -51.051 -12.221 15.602  1.000 178.962 ? 522 ALA EEE C   1 
ATOM   7349  O O   . ALA E 1 193 ? -52.065 -11.963 16.278  1.000 183.180 ? 522 ALA EEE O   1 
ATOM   7350  C CB  . ALA E 1 193 ? -48.884 -12.748 16.760  1.000 176.260 ? 522 ALA EEE CB  1 
ATOM   7351  N N   . THR E 1 194 ? -51.069 -12.933 14.466  1.000 176.910 ? 523 THR EEE N   1 
ATOM   7352  C CA  . THR E 1 194 ? -52.318 -13.400 13.797  1.000 179.471 ? 523 THR EEE CA  1 
ATOM   7353  C C   . THR E 1 194 ? -52.115 -14.660 12.932  1.000 178.334 ? 523 THR EEE C   1 
ATOM   7354  O O   . THR E 1 194 ? -52.957 -14.868 12.036  1.000 180.774 ? 523 THR EEE O   1 
ATOM   7355  C CB  . THR E 1 194 ? -52.920 -12.290 12.919  1.000 179.685 ? 523 THR EEE CB  1 
ATOM   7356  O OG1 . THR E 1 194 ? -52.084 -12.110 11.775  1.000 176.327 ? 523 THR EEE OG1 1 
ATOM   7357  C CG2 . THR E 1 194 ? -53.087 -10.962 13.626  1.000 181.519 ? 523 THR EEE CG2 1 
ATOM   7358  N N   . VAL E 1 195 ? -51.085 -15.485 13.159  1.000 176.284 ? 524 VAL EEE N   1 
ATOM   7359  C CA  . VAL E 1 195 ? -50.914 -16.766 12.405  1.000 177.996 ? 524 VAL EEE CA  1 
ATOM   7360  C C   . VAL E 1 195 ? -50.299 -17.835 13.316  1.000 181.415 ? 524 VAL EEE C   1 
ATOM   7361  O O   . VAL E 1 195 ? -49.062 -18.059 13.244  1.000 181.482 ? 524 VAL EEE O   1 
ATOM   7362  C CB  . VAL E 1 195 ? -50.092 -16.601 11.112  1.000 174.838 ? 524 VAL EEE CB  1 
ATOM   7363  C CG1 . VAL E 1 195 ? -50.245 -17.830 10.228  1.000 176.836 ? 524 VAL EEE CG1 1 
ATOM   7364  C CG2 . VAL E 1 195 ? -50.463 -15.347 10.336  1.000 173.683 ? 524 VAL EEE CG2 1 
ATOM   7365  N N   . CYS E 1 196 ? -51.156 -18.506 14.094  1.000 186.166 ? 525 CYS EEE N   1 
ATOM   7366  C CA  . CYS E 1 196 ? -50.793 -19.561 15.077  1.000 188.127 ? 525 CYS EEE CA  1 
ATOM   7367  C C   . CYS E 1 196 ? -51.242 -20.928 14.546  1.000 191.542 ? 525 CYS EEE C   1 
ATOM   7368  O O   . CYS E 1 196 ? -51.904 -20.964 13.491  1.000 192.356 ? 525 CYS EEE O   1 
ATOM   7369  C CB  . CYS E 1 196 ? -51.431 -19.273 16.434  1.000 191.543 ? 525 CYS EEE CB  1 
ATOM   7370  S SG  . CYS E 1 196 ? -51.550 -17.506 16.827  1.000 192.155 ? 525 CYS EEE SG  1 
ATOM   7371  N N   . GLY E 1 197 ? -50.869 -22.001 15.252  1.000 194.841 ? 526 GLY EEE N   1 
ATOM   7372  C CA  . GLY E 1 197 ? -51.335 -23.383 15.015  1.000 202.683 ? 526 GLY EEE CA  1 
ATOM   7373  C C   . GLY E 1 197 ? -52.188 -23.899 16.175  1.000 211.271 ? 526 GLY EEE C   1 
ATOM   7374  O O   . GLY E 1 197 ? -52.592 -23.120 17.038  1.000 213.615 ? 526 GLY EEE O   1 
ATOM   7375  N N   . PRO E 1 198 ? -52.513 -25.216 16.216  1.000 219.452 ? 527 PRO EEE N   1 
ATOM   7376  C CA  . PRO E 1 198 ? -53.345 -25.791 17.284  1.000 226.833 ? 527 PRO EEE CA  1 
ATOM   7377  C C   . PRO E 1 198 ? -52.747 -25.770 18.711  1.000 227.550 ? 527 PRO EEE C   1 
ATOM   7378  O O   . PRO E 1 198 ? -53.113 -24.864 19.454  1.000 229.716 ? 527 PRO EEE O   1 
ATOM   7379  C CB  . PRO E 1 198 ? -53.624 -27.230 16.803  1.000 231.706 ? 527 PRO EEE CB  1 
ATOM   7380  C CG  . PRO E 1 198 ? -52.519 -27.535 15.814  1.000 227.387 ? 527 PRO EEE CG  1 
ATOM   7381  C CD  . PRO E 1 198 ? -52.163 -26.204 15.184  1.000 220.992 ? 527 PRO EEE CD  1 
ATOM   7382  N N   . LYS E 1 199 ? -51.877 -26.735 19.067  1.000 227.068 ? 528 LYS EEE N   1 
ATOM   7383  C CA  . LYS E 1 199 ? -51.343 -26.988 20.446  1.000 224.237 ? 528 LYS EEE CA  1 
ATOM   7384  C C   . LYS E 1 199 ? -51.257 -25.679 21.249  1.000 221.009 ? 528 LYS EEE C   1 
ATOM   7385  O O   . LYS E 1 199 ? -50.678 -25.593 22.335  1.000 218.225 ? 528 LYS EEE O   1 
ATOM   7386  C CB  . LYS E 1 199 ? -49.962 -27.660 20.385  1.000 218.143 ? 528 LYS EEE CB  1 
ATOM   7387  C CG  . LYS E 1 199 ? -49.963 -29.167 20.148  1.000 220.271 ? 528 LYS EEE CG  1 
ATOM   7388  C CD  . LYS E 1 199 ? -50.317 -29.981 21.370  1.000 222.489 ? 528 LYS EEE CD  1 
ATOM   7389  C CE  . LYS E 1 199 ? -49.931 -31.435 21.236  1.000 224.721 ? 528 LYS EEE CE  1 
ATOM   7390  N NZ  . LYS E 1 199 ? -50.103 -32.152 22.519  1.000 227.643 ? 528 LYS EEE NZ  1 
ATOM   7391  N N   . GLN F 4 1   ? -55.504 -23.182 -32.215 1.000 197.516 ? 1   GLN FFF N   1 
ATOM   7392  C CA  . GLN F 4 1   ? -54.134 -23.489 -32.724 1.000 192.042 ? 1   GLN FFF CA  1 
ATOM   7393  C C   . GLN F 4 1   ? -53.462 -22.206 -33.225 1.000 183.080 ? 1   GLN FFF C   1 
ATOM   7394  O O   . GLN F 4 1   ? -54.189 -21.317 -33.709 1.000 184.628 ? 1   GLN FFF O   1 
ATOM   7395  C CB  . GLN F 4 1   ? -54.214 -24.500 -33.864 1.000 196.018 ? 1   GLN FFF CB  1 
ATOM   7396  C CG  . GLN F 4 1   ? -52.863 -25.058 -34.284 1.000 194.358 ? 1   GLN FFF CG  1 
ATOM   7397  C CD  . GLN F 4 1   ? -52.999 -25.804 -35.584 1.000 197.478 ? 1   GLN FFF CD  1 
ATOM   7398  O OE1 . GLN F 4 1   ? -52.647 -25.295 -36.647 1.000 195.804 ? 1   GLN FFF OE1 1 
ATOM   7399  N NE2 . GLN F 4 1   ? -53.561 -27.002 -35.510 1.000 204.341 ? 1   GLN FFF NE2 1 
ATOM   7400  N N   . VAL F 4 2   ? -52.129 -22.135 -33.137 1.000 173.338 ? 2   VAL FFF N   1 
ATOM   7401  C CA  . VAL F 4 2   ? -51.311 -21.010 -33.680 1.000 163.398 ? 2   VAL FFF CA  1 
ATOM   7402  C C   . VAL F 4 2   ? -51.202 -21.184 -35.195 1.000 159.666 ? 2   VAL FFF C   1 
ATOM   7403  O O   . VAL F 4 2   ? -50.860 -22.293 -35.632 1.000 158.224 ? 2   VAL FFF O   1 
ATOM   7404  C CB  . VAL F 4 2   ? -49.921 -20.941 -33.028 1.000 158.424 ? 2   VAL FFF CB  1 
ATOM   7405  C CG1 . VAL F 4 2   ? -49.049 -19.878 -33.674 1.000 152.598 ? 2   VAL FFF CG1 1 
ATOM   7406  C CG2 . VAL F 4 2   ? -50.020 -20.704 -31.531 1.000 161.275 ? 2   VAL FFF CG2 1 
ATOM   7407  N N   . GLN F 4 3   ? -51.484 -20.119 -35.947 1.000 158.292 ? 3   GLN FFF N   1 
ATOM   7408  C CA  . GLN F 4 3   ? -51.347 -20.076 -37.423 1.000 157.540 ? 3   GLN FFF CA  1 
ATOM   7409  C C   . GLN F 4 3   ? -50.617 -18.790 -37.813 1.000 154.161 ? 3   GLN FFF C   1 
ATOM   7410  O O   . GLN F 4 3   ? -51.007 -17.703 -37.336 1.000 155.037 ? 3   GLN FFF O   1 
ATOM   7411  C CB  . GLN F 4 3   ? -52.709 -20.181 -38.103 1.000 162.136 ? 3   GLN FFF CB  1 
ATOM   7412  C CG  . GLN F 4 3   ? -53.077 -21.612 -38.452 1.000 166.292 ? 3   GLN FFF CG  1 
ATOM   7413  C CD  . GLN F 4 3   ? -54.565 -21.779 -38.639 1.000 172.822 ? 3   GLN FFF CD  1 
ATOM   7414  O OE1 . GLN F 4 3   ? -55.178 -21.095 -39.457 1.000 173.501 ? 3   GLN FFF OE1 1 
ATOM   7415  N NE2 . GLN F 4 3   ? -55.158 -22.697 -37.886 1.000 177.759 ? 3   GLN FFF NE2 1 
ATOM   7416  N N   . LEU F 4 4   ? -49.578 -18.943 -38.630 1.000 152.002 ? 4   LEU FFF N   1 
ATOM   7417  C CA  . LEU F 4 4   ? -48.837 -17.838 -39.281 1.000 150.782 ? 4   LEU FFF CA  1 
ATOM   7418  C C   . LEU F 4 4   ? -49.370 -17.700 -40.712 1.000 153.367 ? 4   LEU FFF C   1 
ATOM   7419  O O   . LEU F 4 4   ? -49.636 -18.751 -41.334 1.000 155.504 ? 4   LEU FFF O   1 
ATOM   7420  C CB  . LEU F 4 4   ? -47.345 -18.181 -39.247 1.000 148.840 ? 4   LEU FFF CB  1 
ATOM   7421  C CG  . LEU F 4 4   ? -46.796 -18.647 -37.897 1.000 149.363 ? 4   LEU FFF CG  1 
ATOM   7422  C CD1 . LEU F 4 4   ? -45.276 -18.709 -37.921 1.000 146.839 ? 4   LEU FFF CD1 1 
ATOM   7423  C CD2 . LEU F 4 4   ? -47.264 -17.737 -36.774 1.000 150.269 ? 4   LEU FFF CD2 1 
ATOM   7424  N N   . VAL F 4 5   ? -49.566 -16.465 -41.193 1.000 154.078 ? 5   VAL FFF N   1 
ATOM   7425  C CA  . VAL F 4 5   ? -50.078 -16.170 -42.567 1.000 156.453 ? 5   VAL FFF CA  1 
ATOM   7426  C C   . VAL F 4 5   ? -49.225 -15.064 -43.201 1.000 152.891 ? 5   VAL FFF C   1 
ATOM   7427  O O   . VAL F 4 5   ? -49.459 -13.880 -42.881 1.000 152.888 ? 5   VAL FFF O   1 
ATOM   7428  C CB  . VAL F 4 5   ? -51.573 -15.786 -42.551 1.000 162.160 ? 5   VAL FFF CB  1 
ATOM   7429  C CG1 . VAL F 4 5   ? -52.090 -15.459 -43.948 1.000 165.011 ? 5   VAL FFF CG1 1 
ATOM   7430  C CG2 . VAL F 4 5   ? -52.431 -16.868 -41.909 1.000 165.536 ? 5   VAL FFF CG2 1 
ATOM   7431  N N   . GLU F 4 6   ? -48.304 -15.441 -44.095 1.000 149.408 ? 6   GLU FFF N   1 
ATOM   7432  C CA  . GLU F 4 6   ? -47.478 -14.499 -44.900 1.000 147.193 ? 6   GLU FFF CA  1 
ATOM   7433  C C   . GLU F 4 6   ? -48.387 -13.795 -45.919 1.000 150.617 ? 6   GLU FFF C   1 
ATOM   7434  O O   . GLU F 4 6   ? -49.482 -14.320 -46.205 1.000 153.426 ? 6   GLU FFF O   1 
ATOM   7435  C CB  . GLU F 4 6   ? -46.330 -15.224 -45.614 1.000 144.134 ? 6   GLU FFF CB  1 
ATOM   7436  C CG  . GLU F 4 6   ? -45.301 -15.841 -44.681 1.000 141.958 ? 6   GLU FFF CG  1 
ATOM   7437  C CD  . GLU F 4 6   ? -45.594 -17.263 -44.232 1.000 143.876 ? 6   GLU FFF CD  1 
ATOM   7438  O OE1 . GLU F 4 6   ? -46.787 -17.645 -44.208 1.000 145.737 ? 6   GLU FFF OE1 1 
ATOM   7439  O OE2 . GLU F 4 6   ? -44.627 -17.992 -43.913 1.000 142.125 ? 6   GLU FFF OE2 1 
ATOM   7440  N N   . SER F 4 7   ? -47.954 -12.633 -46.415 1.000 151.704 ? 7   SER FFF N   1 
ATOM   7441  C CA  . SER F 4 7   ? -48.537 -11.907 -47.578 1.000 153.573 ? 7   SER FFF CA  1 
ATOM   7442  C C   . SER F 4 7   ? -47.579 -10.786 -47.998 1.000 151.091 ? 7   SER FFF C   1 
ATOM   7443  O O   . SER F 4 7   ? -46.619 -10.514 -47.256 1.000 147.866 ? 7   SER FFF O   1 
ATOM   7444  C CB  . SER F 4 7   ? -49.915 -11.378 -47.272 1.000 158.064 ? 7   SER FFF CB  1 
ATOM   7445  O OG  . SER F 4 7   ? -49.929 -10.694 -46.028 1.000 160.041 ? 7   SER FFF OG  1 
ATOM   7446  N N   . GLY F 4 8   ? -47.824 -10.171 -49.154 1.000 152.907 ? 8   GLY FFF N   1 
ATOM   7447  C CA  . GLY F 4 8   ? -46.987 -9.083  -49.695 1.000 153.020 ? 8   GLY FFF CA  1 
ATOM   7448  C C   . GLY F 4 8   ? -45.935 -9.600  -50.662 1.000 150.868 ? 8   GLY FFF C   1 
ATOM   7449  O O   . GLY F 4 8   ? -45.087 -8.797  -51.097 1.000 151.297 ? 8   GLY FFF O   1 
ATOM   7450  N N   . GLY F 4 9   ? -45.978 -10.897 -50.979 1.000 149.259 ? 9   GLY FFF N   1 
ATOM   7451  C CA  . GLY F 4 9   ? -45.164 -11.512 -52.044 1.000 146.766 ? 9   GLY FFF CA  1 
ATOM   7452  C C   . GLY F 4 9   ? -45.611 -11.045 -53.418 1.000 146.460 ? 9   GLY FFF C   1 
ATOM   7453  O O   . GLY F 4 9   ? -46.793 -10.650 -53.570 1.000 147.304 ? 9   GLY FFF O   1 
ATOM   7454  N N   . GLY F 4 10  ? -44.695 -11.072 -54.386 1.000 143.584 ? 10  GLY FFF N   1 
ATOM   7455  C CA  . GLY F 4 10  ? -45.002 -10.755 -55.791 1.000 144.607 ? 10  GLY FFF CA  1 
ATOM   7456  C C   . GLY F 4 10  ? -43.766 -10.404 -56.590 1.000 141.847 ? 10  GLY FFF C   1 
ATOM   7457  O O   . GLY F 4 10  ? -42.680 -10.933 -56.295 1.000 136.402 ? 10  GLY FFF O   1 
ATOM   7458  N N   . LEU F 4 11  ? -43.952 -9.502  -57.551 1.000 144.021 ? 11  LEU FFF N   1 
ATOM   7459  C CA  . LEU F 4 11  ? -42.994 -9.139  -58.620 1.000 145.589 ? 11  LEU FFF CA  1 
ATOM   7460  C C   . LEU F 4 11  ? -42.326 -7.819  -58.225 1.000 147.971 ? 11  LEU FFF C   1 
ATOM   7461  O O   . LEU F 4 11  ? -43.039 -6.968  -57.672 1.000 151.267 ? 11  LEU FFF O   1 
ATOM   7462  C CB  . LEU F 4 11  ? -43.821 -8.999  -59.900 1.000 149.756 ? 11  LEU FFF CB  1 
ATOM   7463  C CG  . LEU F 4 11  ? -43.137 -9.373  -61.211 1.000 151.294 ? 11  LEU FFF CG  1 
ATOM   7464  C CD1 . LEU F 4 11  ? -42.874 -10.871 -61.274 1.000 148.581 ? 11  LEU FFF CD1 1 
ATOM   7465  C CD2 . LEU F 4 11  ? -43.983 -8.908  -62.400 1.000 156.424 ? 11  LEU FFF CD2 1 
ATOM   7466  N N   . MET F 4 12  ? -41.024 -7.653  -58.476 1.000 149.847 ? 12  MET FFF N   1 
ATOM   7467  C CA  . MET F 4 12  ? -40.320 -6.359  -58.248 1.000 153.842 ? 12  MET FFF CA  1 
ATOM   7468  C C   . MET F 4 12  ? -39.039 -6.271  -59.074 1.000 153.943 ? 12  MET FFF C   1 
ATOM   7469  O O   . MET F 4 12  ? -38.151 -7.110  -58.872 1.000 150.208 ? 12  MET FFF O   1 
ATOM   7470  C CB  . MET F 4 12  ? -39.960 -6.164  -56.775 1.000 154.659 ? 12  MET FFF CB  1 
ATOM   7471  C CG  . MET F 4 12  ? -40.975 -5.325  -56.034 1.000 159.730 ? 12  MET FFF CG  1 
ATOM   7472  S SD  . MET F 4 12  ? -41.554 -3.887  -56.995 1.000 169.770 ? 12  MET FFF SD  1 
ATOM   7473  C CE  . MET F 4 12  ? -40.105 -2.838  -56.933 1.000 171.811 ? 12  MET FFF CE  1 
ATOM   7474  N N   . GLN F 4 13  ? -38.940 -5.252  -59.931 1.000 157.782 ? 13  GLN FFF N   1 
ATOM   7475  C CA  . GLN F 4 13  ? -37.706 -4.991  -60.708 1.000 158.848 ? 13  GLN FFF CA  1 
ATOM   7476  C C   . GLN F 4 13  ? -36.591 -4.689  -59.697 1.000 152.697 ? 13  GLN FFF C   1 
ATOM   7477  O O   . GLN F 4 13  ? -36.783 -3.809  -58.842 1.000 151.425 ? 13  GLN FFF O   1 
ATOM   7478  C CB  . GLN F 4 13  ? -37.956 -3.939  -61.794 1.000 166.715 ? 13  GLN FFF CB  1 
ATOM   7479  C CG  . GLN F 4 13  ? -38.159 -2.515  -61.308 1.000 171.363 ? 13  GLN FFF CG  1 
ATOM   7480  C CD  . GLN F 4 13  ? -37.802 -1.583  -62.439 1.000 180.336 ? 13  GLN FFF CD  1 
ATOM   7481  O OE1 . GLN F 4 13  ? -38.078 -1.862  -63.612 1.000 184.171 ? 13  GLN FFF OE1 1 
ATOM   7482  N NE2 . GLN F 4 13  ? -37.115 -0.508  -62.095 1.000 186.195 ? 13  GLN FFF NE2 1 
ATOM   7483  N N   . ALA F 4 14  ? -35.508 -5.469  -59.760 1.000 147.605 ? 14  ALA FFF N   1 
ATOM   7484  C CA  . ALA F 4 14  ? -34.334 -5.425  -58.861 1.000 145.894 ? 14  ALA FFF CA  1 
ATOM   7485  C C   . ALA F 4 14  ? -33.886 -3.975  -58.650 1.000 151.529 ? 14  ALA FFF C   1 
ATOM   7486  O O   . ALA F 4 14  ? -33.732 -3.249  -59.646 1.000 154.679 ? 14  ALA FFF O   1 
ATOM   7487  C CB  . ALA F 4 14  ? -33.219 -6.255  -59.443 1.000 144.309 ? 14  ALA FFF CB  1 
ATOM   7488  N N   . GLY F 4 15  ? -33.676 -3.580  -57.392 1.000 154.657 ? 15  GLY FFF N   1 
ATOM   7489  C CA  . GLY F 4 15  ? -33.362 -2.194  -56.997 1.000 161.211 ? 15  GLY FFF CA  1 
ATOM   7490  C C   . GLY F 4 15  ? -34.575 -1.488  -56.410 1.000 165.262 ? 15  GLY FFF C   1 
ATOM   7491  O O   . GLY F 4 15  ? -34.367 -0.497  -55.680 1.000 167.423 ? 15  GLY FFF O   1 
ATOM   7492  N N   . GLY F 4 16  ? -35.793 -1.954  -56.729 1.000 167.132 ? 16  GLY FFF N   1 
ATOM   7493  C CA  . GLY F 4 16  ? -37.051 -1.527  -56.082 1.000 168.020 ? 16  GLY FFF CA  1 
ATOM   7494  C C   . GLY F 4 16  ? -37.086 -2.005  -54.642 1.000 165.139 ? 16  GLY FFF C   1 
ATOM   7495  O O   . GLY F 4 16  ? -35.993 -2.182  -54.066 1.000 165.584 ? 16  GLY FFF O   1 
ATOM   7496  N N   . SER F 4 17  ? -38.274 -2.206  -54.059 1.000 163.289 ? 17  SER FFF N   1 
ATOM   7497  C CA  . SER F 4 17  ? -38.447 -2.784  -52.697 1.000 157.870 ? 17  SER FFF CA  1 
ATOM   7498  C C   . SER F 4 17  ? -39.785 -3.519  -52.581 1.000 155.108 ? 17  SER FFF C   1 
ATOM   7499  O O   . SER F 4 17  ? -40.721 -3.183  -53.330 1.000 158.405 ? 17  SER FFF O   1 
ATOM   7500  C CB  . SER F 4 17  ? -38.310 -1.734  -51.625 1.000 159.023 ? 17  SER FFF CB  1 
ATOM   7501  O OG  . SER F 4 17  ? -38.325 -2.319  -50.334 1.000 155.120 ? 17  SER FFF OG  1 
ATOM   7502  N N   . LEU F 4 18  ? -39.855 -4.484  -51.662 1.000 151.095 ? 18  LEU FFF N   1 
ATOM   7503  C CA  . LEU F 4 18  ? -41.089 -5.241  -51.329 1.000 151.562 ? 18  LEU FFF CA  1 
ATOM   7504  C C   . LEU F 4 18  ? -41.169 -5.452  -49.811 1.000 152.251 ? 18  LEU FFF C   1 
ATOM   7505  O O   . LEU F 4 18  ? -40.120 -5.713  -49.190 1.000 152.484 ? 18  LEU FFF O   1 
ATOM   7506  C CB  . LEU F 4 18  ? -41.066 -6.571  -52.090 1.000 149.330 ? 18  LEU FFF CB  1 
ATOM   7507  C CG  . LEU F 4 18  ? -42.419 -7.250  -52.311 1.000 150.331 ? 18  LEU FFF CG  1 
ATOM   7508  C CD1 . LEU F 4 18  ? -43.553 -6.239  -52.460 1.000 154.496 ? 18  LEU FFF CD1 1 
ATOM   7509  C CD2 . LEU F 4 18  ? -42.367 -8.171  -53.524 1.000 148.733 ? 18  LEU FFF CD2 1 
ATOM   7510  N N   . ARG F 4 19  ? -42.371 -5.313  -49.245 1.000 153.177 ? 19  ARG FFF N   1 
ATOM   7511  C CA  . ARG F 4 19  ? -42.669 -5.510  -47.802 1.000 150.655 ? 19  ARG FFF CA  1 
ATOM   7512  C C   . ARG F 4 19  ? -43.425 -6.829  -47.643 1.000 147.964 ? 19  ARG FFF C   1 
ATOM   7513  O O   . ARG F 4 19  ? -44.343 -7.081  -48.442 1.000 149.491 ? 19  ARG FFF O   1 
ATOM   7514  C CB  . ARG F 4 19  ? -43.499 -4.332  -47.290 1.000 155.394 ? 19  ARG FFF CB  1 
ATOM   7515  C CG  . ARG F 4 19  ? -43.833 -4.366  -45.809 1.000 154.828 ? 19  ARG FFF CG  1 
ATOM   7516  C CD  . ARG F 4 19  ? -44.630 -3.122  -45.485 1.000 160.525 ? 19  ARG FFF CD  1 
ATOM   7517  N NE  . ARG F 4 19  ? -44.906 -2.994  -44.067 1.000 163.327 ? 19  ARG FFF NE  1 
ATOM   7518  C CZ  . ARG F 4 19  ? -45.411 -1.911  -43.482 1.000 169.989 ? 19  ARG FFF CZ  1 
ATOM   7519  N NH1 . ARG F 4 19  ? -45.698 -0.831  -44.192 1.000 176.295 ? 19  ARG FFF NH1 1 
ATOM   7520  N NH2 . ARG F 4 19  ? -45.629 -1.910  -42.179 1.000 170.359 ? 19  ARG FFF NH2 1 
ATOM   7521  N N   . LEU F 4 20  ? -43.036 -7.642  -46.662 1.000 145.174 ? 20  LEU FFF N   1 
ATOM   7522  C CA  . LEU F 4 20  ? -43.693 -8.935  -46.336 1.000 144.232 ? 20  LEU FFF CA  1 
ATOM   7523  C C   . LEU F 4 20  ? -44.301 -8.840  -44.937 1.000 143.975 ? 20  LEU FFF C   1 
ATOM   7524  O O   . LEU F 4 20  ? -43.675 -8.214  -44.066 1.000 142.569 ? 20  LEU FFF O   1 
ATOM   7525  C CB  . LEU F 4 20  ? -42.667 -10.066 -46.431 1.000 141.233 ? 20  LEU FFF CB  1 
ATOM   7526  C CG  . LEU F 4 20  ? -42.500 -10.661 -47.824 1.000 140.851 ? 20  LEU FFF CG  1 
ATOM   7527  C CD1 . LEU F 4 20  ? -41.037 -10.719 -48.214 1.000 140.763 ? 20  LEU FFF CD1 1 
ATOM   7528  C CD2 . LEU F 4 20  ? -43.130 -12.037 -47.906 1.000 140.192 ? 20  LEU FFF CD2 1 
ATOM   7529  N N   . SER F 4 21  ? -45.482 -9.435  -44.757 1.000 143.971 ? 21  SER FFF N   1 
ATOM   7530  C CA  . SER F 4 21  ? -46.336 -9.297  -43.552 1.000 145.094 ? 21  SER FFF CA  1 
ATOM   7531  C C   . SER F 4 21  ? -46.762 -10.684 -43.074 1.000 141.317 ? 21  SER FFF C   1 
ATOM   7532  O O   . SER F 4 21  ? -47.536 -11.337 -43.796 1.000 141.523 ? 21  SER FFF O   1 
ATOM   7533  C CB  . SER F 4 21  ? -47.533 -8.422  -43.847 1.000 152.380 ? 21  SER FFF CB  1 
ATOM   7534  O OG  . SER F 4 21  ? -47.184 -7.345  -44.714 1.000 156.392 ? 21  SER FFF OG  1 
ATOM   7535  N N   . CYS F 4 22  ? -46.268 -11.109 -41.908 1.000 138.542 ? 22  CYS FFF N   1 
ATOM   7536  C CA  . CYS F 4 22  ? -46.620 -12.404 -41.265 1.000 138.726 ? 22  CYS FFF CA  1 
ATOM   7537  C C   . CYS F 4 22  ? -47.509 -12.135 -40.047 1.000 139.773 ? 22  CYS FFF C   1 
ATOM   7538  O O   . CYS F 4 22  ? -46.998 -11.642 -39.018 1.000 136.131 ? 22  CYS FFF O   1 
ATOM   7539  C CB  . CYS F 4 22  ? -45.382 -13.210 -40.884 1.000 137.016 ? 22  CYS FFF CB  1 
ATOM   7540  S SG  . CYS F 4 22  ? -45.749 -14.662 -39.863 1.000 138.542 ? 22  CYS FFF SG  1 
ATOM   7541  N N   . ALA F 4 23  ? -48.798 -12.451 -40.186 1.000 144.208 ? 23  ALA FFF N   1 
ATOM   7542  C CA  . ALA F 4 23  ? -49.843 -12.296 -39.151 1.000 149.487 ? 23  ALA FFF CA  1 
ATOM   7543  C C   . ALA F 4 23  ? -49.919 -13.576 -38.308 1.000 149.885 ? 23  ALA FFF C   1 
ATOM   7544  O O   . ALA F 4 23  ? -49.989 -14.678 -38.897 1.000 150.546 ? 23  ALA FFF O   1 
ATOM   7545  C CB  . ALA F 4 23  ? -51.165 -11.978 -39.810 1.000 154.797 ? 23  ALA FFF CB  1 
ATOM   7546  N N   . VAL F 4 24  ? -49.913 -13.416 -36.979 1.000 148.583 ? 24  VAL FFF N   1 
ATOM   7547  C CA  . VAL F 4 24  ? -49.921 -14.514 -35.966 1.000 147.224 ? 24  VAL FFF CA  1 
ATOM   7548  C C   . VAL F 4 24  ? -51.259 -14.471 -35.224 1.000 150.837 ? 24  VAL FFF C   1 
ATOM   7549  O O   . VAL F 4 24  ? -51.597 -13.391 -34.710 1.000 152.326 ? 24  VAL FFF O   1 
ATOM   7550  C CB  . VAL F 4 24  ? -48.752 -14.355 -34.974 1.000 144.770 ? 24  VAL FFF CB  1 
ATOM   7551  C CG1 . VAL F 4 24  ? -48.586 -15.588 -34.104 1.000 145.372 ? 24  VAL FFF CG1 1 
ATOM   7552  C CG2 . VAL F 4 24  ? -47.441 -14.013 -35.670 1.000 141.830 ? 24  VAL FFF CG2 1 
ATOM   7553  N N   . SER F 4 25  ? -51.982 -15.592 -35.164 1.000 154.620 ? 25  SER FFF N   1 
ATOM   7554  C CA  . SER F 4 25  ? -53.198 -15.757 -34.322 1.000 162.786 ? 25  SER FFF CA  1 
ATOM   7555  C C   . SER F 4 25  ? -53.055 -17.018 -33.464 1.000 167.168 ? 25  SER FFF C   1 
ATOM   7556  O O   . SER F 4 25  ? -52.883 -18.109 -34.043 1.000 167.373 ? 25  SER FFF O   1 
ATOM   7557  C CB  . SER F 4 25  ? -54.457 -15.795 -35.147 1.000 166.630 ? 25  SER FFF CB  1 
ATOM   7558  O OG  . SER F 4 25  ? -54.510 -16.972 -35.937 1.000 167.549 ? 25  SER FFF OG  1 
ATOM   7559  N N   . GLY F 4 26  ? -53.122 -16.851 -32.139 1.000 173.024 ? 26  GLY FFF N   1 
ATOM   7560  C CA  . GLY F 4 26  ? -52.944 -17.918 -31.136 1.000 178.572 ? 26  GLY FFF CA  1 
ATOM   7561  C C   . GLY F 4 26  ? -52.497 -17.354 -29.798 1.000 182.161 ? 26  GLY FFF C   1 
ATOM   7562  O O   . GLY F 4 26  ? -52.805 -16.176 -29.521 1.000 183.450 ? 26  GLY FFF O   1 
ATOM   7563  N N   . ARG F 4 27  ? -51.807 -18.161 -28.987 1.000 185.664 ? 27  ARG FFF N   1 
ATOM   7564  C CA  . ARG F 4 27  ? -51.241 -17.728 -27.682 1.000 188.272 ? 27  ARG FFF CA  1 
ATOM   7565  C C   . ARG F 4 27  ? -50.137 -16.698 -27.940 1.000 185.487 ? 27  ARG FFF C   1 
ATOM   7566  O O   . ARG F 4 27  ? -48.966 -17.114 -27.968 1.000 183.657 ? 27  ARG FFF O   1 
ATOM   7567  C CB  . ARG F 4 27  ? -50.666 -18.925 -26.920 1.000 190.027 ? 27  ARG FFF CB  1 
ATOM   7568  C CG  . ARG F 4 27  ? -51.701 -19.931 -26.451 1.000 196.991 ? 27  ARG FFF CG  1 
ATOM   7569  C CD  . ARG F 4 27  ? -51.064 -20.862 -25.443 1.000 200.437 ? 27  ARG FFF CD  1 
ATOM   7570  N NE  . ARG F 4 27  ? -51.965 -21.928 -25.037 1.000 207.670 ? 27  ARG FFF NE  1 
ATOM   7571  C CZ  . ARG F 4 27  ? -51.842 -22.649 -23.925 1.000 211.892 ? 27  ARG FFF CZ  1 
ATOM   7572  N NH1 . ARG F 4 27  ? -50.847 -22.425 -23.081 1.000 209.652 ? 27  ARG FFF NH1 1 
ATOM   7573  N NH2 . ARG F 4 27  ? -52.728 -23.595 -23.660 1.000 218.232 ? 27  ARG FFF NH2 1 
ATOM   7574  N N   . THR F 4 28  ? -50.500 -15.420 -28.129 1.000 187.195 ? 28  THR FFF N   1 
ATOM   7575  C CA  . THR F 4 28  ? -49.575 -14.281 -28.414 1.000 185.297 ? 28  THR FFF CA  1 
ATOM   7576  C C   . THR F 4 28  ? -48.585 -14.074 -27.261 1.000 189.539 ? 28  THR FFF C   1 
ATOM   7577  O O   . THR F 4 28  ? -47.420 -13.700 -27.539 1.000 189.573 ? 28  THR FFF O   1 
ATOM   7578  C CB  . THR F 4 28  ? -50.315 -12.946 -28.583 1.000 184.016 ? 28  THR FFF CB  1 
ATOM   7579  O OG1 . THR F 4 28  ? -51.130 -13.002 -29.750 1.000 183.340 ? 28  THR FFF OG1 1 
ATOM   7580  C CG2 . THR F 4 28  ? -49.370 -11.767 -28.674 1.000 180.519 ? 28  THR FFF CG2 1 
ATOM   7581  N N   . PHE F 4 29  ? -49.055 -14.266 -26.022 1.000 194.653 ? 29  PHE FFF N   1 
ATOM   7582  C CA  . PHE F 4 29  ? -48.339 -13.946 -24.759 1.000 194.333 ? 29  PHE FFF CA  1 
ATOM   7583  C C   . PHE F 4 29  ? -46.985 -14.662 -24.721 1.000 185.122 ? 29  PHE FFF C   1 
ATOM   7584  O O   . PHE F 4 29  ? -46.011 -14.079 -24.215 1.000 182.907 ? 29  PHE FFF O   1 
ATOM   7585  C CB  . PHE F 4 29  ? -49.206 -14.320 -23.551 1.000 205.967 ? 29  PHE FFF CB  1 
ATOM   7586  C CG  . PHE F 4 29  ? -49.239 -15.788 -23.187 1.000 214.282 ? 29  PHE FFF CG  1 
ATOM   7587  C CD1 . PHE F 4 29  ? -48.250 -16.343 -22.382 1.000 216.446 ? 29  PHE FFF CD1 1 
ATOM   7588  C CD2 . PHE F 4 29  ? -50.271 -16.613 -23.617 1.000 218.475 ? 29  PHE FFF CD2 1 
ATOM   7589  C CE1 . PHE F 4 29  ? -48.283 -17.686 -22.032 1.000 218.217 ? 29  PHE FFF CE1 1 
ATOM   7590  C CE2 . PHE F 4 29  ? -50.303 -17.956 -23.264 1.000 220.896 ? 29  PHE FFF CE2 1 
ATOM   7591  C CZ  . PHE F 4 29  ? -49.310 -18.491 -22.473 1.000 220.409 ? 29  PHE FFF CZ  1 
ATOM   7592  N N   . SER F 4 30  ? -46.935 -15.884 -25.255 1.000 178.828 ? 30  SER FFF N   1 
ATOM   7593  C CA  . SER F 4 30  ? -45.801 -16.832 -25.122 1.000 175.608 ? 30  SER FFF CA  1 
ATOM   7594  C C   . SER F 4 30  ? -44.762 -16.638 -26.240 1.000 166.825 ? 30  SER FFF C   1 
ATOM   7595  O O   . SER F 4 30  ? -43.761 -17.375 -26.218 1.000 168.296 ? 30  SER FFF O   1 
ATOM   7596  C CB  . SER F 4 30  ? -46.327 -18.255 -25.062 1.000 181.034 ? 30  SER FFF CB  1 
ATOM   7597  O OG  . SER F 4 30  ? -47.527 -18.404 -25.814 1.000 183.369 ? 30  SER FFF OG  1 
ATOM   7598  N N   . THR F 4 31  ? -44.958 -15.686 -27.163 1.000 158.055 ? 31  THR FFF N   1 
ATOM   7599  C CA  . THR F 4 31  ? -44.038 -15.433 -28.311 1.000 150.287 ? 31  THR FFF CA  1 
ATOM   7600  C C   . THR F 4 31  ? -42.704 -14.872 -27.804 1.000 146.725 ? 31  THR FFF C   1 
ATOM   7601  O O   . THR F 4 31  ? -42.719 -13.784 -27.207 1.000 147.039 ? 31  THR FFF O   1 
ATOM   7602  C CB  . THR F 4 31  ? -44.628 -14.459 -29.338 1.000 147.892 ? 31  THR FFF CB  1 
ATOM   7603  O OG1 . THR F 4 31  ? -45.922 -14.928 -29.716 1.000 148.357 ? 31  THR FFF OG1 1 
ATOM   7604  C CG2 . THR F 4 31  ? -43.758 -14.313 -30.569 1.000 144.694 ? 31  THR FFF CG2 1 
ATOM   7605  N N   . ALA F 4 32  ? -41.601 -15.583 -28.058 1.000 143.807 ? 32  ALA FFF N   1 
ATOM   7606  C CA  . ALA F 4 32  ? -40.218 -15.150 -27.751 1.000 141.162 ? 32  ALA FFF CA  1 
ATOM   7607  C C   . ALA F 4 32  ? -39.704 -14.269 -28.896 1.000 137.095 ? 32  ALA FFF C   1 
ATOM   7608  O O   . ALA F 4 32  ? -39.386 -13.090 -28.639 1.000 135.617 ? 32  ALA FFF O   1 
ATOM   7609  C CB  . ALA F 4 32  ? -39.328 -16.353 -27.531 1.000 141.068 ? 32  ALA FFF CB  1 
ATOM   7610  N N   . ALA F 4 33  ? -39.660 -14.831 -30.110 1.000 134.453 ? 33  ALA FFF N   1 
ATOM   7611  C CA  . ALA F 4 33  ? -39.034 -14.249 -31.322 1.000 129.922 ? 33  ALA FFF CA  1 
ATOM   7612  C C   . ALA F 4 33  ? -39.785 -14.711 -32.578 1.000 128.355 ? 33  ALA FFF C   1 
ATOM   7613  O O   . ALA F 4 33  ? -40.375 -15.809 -32.543 1.000 128.932 ? 33  ALA FFF O   1 
ATOM   7614  C CB  . ALA F 4 33  ? -37.581 -14.658 -31.378 1.000 128.038 ? 33  ALA FFF CB  1 
ATOM   7615  N N   . MET F 4 34  ? -39.769 -13.885 -33.631 1.000 126.642 ? 34  MET FFF N   1 
ATOM   7616  C CA  . MET F 4 34  ? -40.238 -14.219 -35.002 1.000 126.384 ? 34  MET FFF CA  1 
ATOM   7617  C C   . MET F 4 34  ? -39.032 -14.203 -35.942 1.000 125.343 ? 34  MET FFF C   1 
ATOM   7618  O O   . MET F 4 34  ? -38.164 -13.323 -35.771 1.000 126.138 ? 34  MET FFF O   1 
ATOM   7619  C CB  . MET F 4 34  ? -41.247 -13.192 -35.520 1.000 128.491 ? 34  MET FFF CB  1 
ATOM   7620  C CG  . MET F 4 34  ? -42.517 -13.097 -34.708 1.000 132.477 ? 34  MET FFF CG  1 
ATOM   7621  S SD  . MET F 4 34  ? -43.529 -14.590 -34.796 1.000 137.222 ? 34  MET FFF SD  1 
ATOM   7622  C CE  . MET F 4 34  ? -44.020 -14.597 -36.519 1.000 137.033 ? 34  MET FFF CE  1 
ATOM   7623  N N   . GLY F 4 35  ? -38.999 -15.122 -36.908 1.000 125.622 ? 35  GLY FFF N   1 
ATOM   7624  C CA  . GLY F 4 35  ? -37.902 -15.243 -37.885 1.000 126.051 ? 35  GLY FFF CA  1 
ATOM   7625  C C   . GLY F 4 35  ? -38.430 -15.367 -39.301 1.000 127.258 ? 35  GLY FFF C   1 
ATOM   7626  O O   . GLY F 4 35  ? -39.492 -15.983 -39.483 1.000 131.507 ? 35  GLY FFF O   1 
ATOM   7627  N N   . TRP F 4 36  ? -37.718 -14.791 -40.268 1.000 126.393 ? 36  TRP FFF N   1 
ATOM   7628  C CA  . TRP F 4 36  ? -37.958 -15.002 -41.717 1.000 125.915 ? 36  TRP FFF CA  1 
ATOM   7629  C C   . TRP F 4 36  ? -36.915 -15.990 -42.249 1.000 126.287 ? 36  TRP FFF C   1 
ATOM   7630  O O   . TRP F 4 36  ? -35.731 -15.839 -41.908 1.000 129.745 ? 36  TRP FFF O   1 
ATOM   7631  C CB  . TRP F 4 36  ? -37.935 -13.662 -42.455 1.000 126.666 ? 36  TRP FFF CB  1 
ATOM   7632  C CG  . TRP F 4 36  ? -39.164 -12.843 -42.218 1.000 127.867 ? 36  TRP FFF CG  1 
ATOM   7633  C CD1 . TRP F 4 36  ? -39.315 -11.811 -41.341 1.000 129.388 ? 36  TRP FFF CD1 1 
ATOM   7634  C CD2 . TRP F 4 36  ? -40.436 -13.003 -42.866 1.000 129.226 ? 36  TRP FFF CD2 1 
ATOM   7635  N NE1 . TRP F 4 36  ? -40.584 -11.308 -41.412 1.000 130.733 ? 36  TRP FFF NE1 1 
ATOM   7636  C CE2 . TRP F 4 36  ? -41.296 -12.021 -42.336 1.000 130.841 ? 36  TRP FFF CE2 1 
ATOM   7637  C CE3 . TRP F 4 36  ? -40.927 -13.870 -43.846 1.000 131.333 ? 36  TRP FFF CE3 1 
ATOM   7638  C CZ2 . TRP F 4 36  ? -42.619 -11.892 -42.750 1.000 133.996 ? 36  TRP FFF CZ2 1 
ATOM   7639  C CZ3 . TRP F 4 36  ? -42.234 -13.740 -44.259 1.000 133.598 ? 36  TRP FFF CZ3 1 
ATOM   7640  C CH2 . TRP F 4 36  ? -43.068 -12.761 -43.719 1.000 134.912 ? 36  TRP FFF CH2 1 
ATOM   7641  N N   . PHE F 4 37  ? -37.359 -17.005 -42.992 1.000 125.911 ? 37  PHE FFF N   1 
ATOM   7642  C CA  . PHE F 4 37  ? -36.506 -17.957 -43.751 1.000 125.888 ? 37  PHE FFF CA  1 
ATOM   7643  C C   . PHE F 4 37  ? -36.939 -17.920 -45.218 1.000 127.426 ? 37  PHE FFF C   1 
ATOM   7644  O O   . PHE F 4 37  ? -38.137 -17.697 -45.476 1.000 129.326 ? 37  PHE FFF O   1 
ATOM   7645  C CB  . PHE F 4 37  ? -36.639 -19.382 -43.214 1.000 126.381 ? 37  PHE FFF CB  1 
ATOM   7646  C CG  . PHE F 4 37  ? -36.061 -19.603 -41.841 1.000 127.427 ? 37  PHE FFF CG  1 
ATOM   7647  C CD1 . PHE F 4 37  ? -36.689 -19.099 -40.712 1.000 127.066 ? 37  PHE FFF CD1 1 
ATOM   7648  C CD2 . PHE F 4 37  ? -34.895 -20.329 -41.671 1.000 130.017 ? 37  PHE FFF CD2 1 
ATOM   7649  C CE1 . PHE F 4 37  ? -36.160 -19.312 -39.446 1.000 127.327 ? 37  PHE FFF CE1 1 
ATOM   7650  C CE2 . PHE F 4 37  ? -34.369 -20.545 -40.404 1.000 130.975 ? 37  PHE FFF CE2 1 
ATOM   7651  C CZ  . PHE F 4 37  ? -35.002 -20.036 -39.293 1.000 128.799 ? 37  PHE FFF CZ  1 
ATOM   7652  N N   . ARG F 4 38  ? -35.995 -18.119 -46.140 1.000 126.225 ? 38  ARG FFF N   1 
ATOM   7653  C CA  . ARG F 4 38  ? -36.272 -18.205 -47.596 1.000 124.054 ? 38  ARG FFF CA  1 
ATOM   7654  C C   . ARG F 4 38  ? -35.630 -19.477 -48.142 1.000 122.539 ? 38  ARG FFF C   1 
ATOM   7655  O O   . ARG F 4 38  ? -34.554 -19.854 -47.658 1.000 120.288 ? 38  ARG FFF O   1 
ATOM   7656  C CB  . ARG F 4 38  ? -35.771 -16.962 -48.340 1.000 124.705 ? 38  ARG FFF CB  1 
ATOM   7657  C CG  . ARG F 4 38  ? -34.255 -16.853 -48.467 1.000 124.896 ? 38  ARG FFF CG  1 
ATOM   7658  C CD  . ARG F 4 38  ? -33.840 -15.508 -49.034 1.000 124.230 ? 38  ARG FFF CD  1 
ATOM   7659  N NE  . ARG F 4 38  ? -32.394 -15.352 -49.099 1.000 124.103 ? 38  ARG FFF NE  1 
ATOM   7660  C CZ  . ARG F 4 38  ? -31.778 -14.233 -49.467 1.000 126.171 ? 38  ARG FFF CZ  1 
ATOM   7661  N NH1 . ARG F 4 38  ? -32.482 -13.166 -49.814 1.000 126.238 ? 38  ARG FFF NH1 1 
ATOM   7662  N NH2 . ARG F 4 38  ? -30.456 -14.179 -49.487 1.000 128.432 ? 38  ARG FFF NH2 1 
ATOM   7663  N N   . GLN F 4 39  ? -36.308 -20.115 -49.092 1.000 124.161 ? 39  GLN FFF N   1 
ATOM   7664  C CA  . GLN F 4 39  ? -35.776 -21.214 -49.931 1.000 127.974 ? 39  GLN FFF CA  1 
ATOM   7665  C C   . GLN F 4 39  ? -35.767 -20.742 -51.381 1.000 128.749 ? 39  GLN FFF C   1 
ATOM   7666  O O   . GLN F 4 39  ? -36.863 -20.532 -51.929 1.000 128.660 ? 39  GLN FFF O   1 
ATOM   7667  C CB  . GLN F 4 39  ? -36.660 -22.448 -49.792 1.000 132.029 ? 39  GLN FFF CB  1 
ATOM   7668  C CG  . GLN F 4 39  ? -36.271 -23.572 -50.732 1.000 135.895 ? 39  GLN FFF CG  1 
ATOM   7669  C CD  . GLN F 4 39  ? -36.437 -24.906 -50.056 1.000 141.638 ? 39  GLN FFF CD  1 
ATOM   7670  O OE1 . GLN F 4 39  ? -37.487 -25.204 -49.484 1.000 144.771 ? 39  GLN FFF OE1 1 
ATOM   7671  N NE2 . GLN F 4 39  ? -35.384 -25.707 -50.104 1.000 146.749 ? 39  GLN FFF NE2 1 
ATOM   7672  N N   . ALA F 4 40  ? -34.581 -20.562 -51.965 1.000 131.532 ? 40  ALA FFF N   1 
ATOM   7673  C CA  . ALA F 4 40  ? -34.387 -20.204 -53.393 1.000 133.872 ? 40  ALA FFF CA  1 
ATOM   7674  C C   . ALA F 4 40  ? -34.657 -21.438 -54.247 1.000 136.029 ? 40  ALA FFF C   1 
ATOM   7675  O O   . ALA F 4 40  ? -34.725 -22.548 -53.729 1.000 142.387 ? 40  ALA FFF O   1 
ATOM   7676  C CB  . ALA F 4 40  ? -32.990 -19.663 -53.615 1.000 135.093 ? 40  ALA FFF CB  1 
ATOM   7677  N N   . PRO F 4 41  ? -34.822 -21.302 -55.577 1.000 133.994 ? 41  PRO FFF N   1 
ATOM   7678  C CA  . PRO F 4 41  ? -34.876 -22.475 -56.443 1.000 136.219 ? 41  PRO FFF CA  1 
ATOM   7679  C C   . PRO F 4 41  ? -33.528 -23.214 -56.379 1.000 136.132 ? 41  PRO FFF C   1 
ATOM   7680  O O   . PRO F 4 41  ? -32.503 -22.568 -56.454 1.000 133.256 ? 41  PRO FFF O   1 
ATOM   7681  C CB  . PRO F 4 41  ? -35.166 -21.873 -57.826 1.000 138.535 ? 41  PRO FFF CB  1 
ATOM   7682  C CG  . PRO F 4 41  ? -34.594 -20.473 -57.729 1.000 137.242 ? 41  PRO FFF CG  1 
ATOM   7683  C CD  . PRO F 4 41  ? -34.928 -20.040 -56.319 1.000 133.685 ? 41  PRO FFF CD  1 
ATOM   7684  N N   . GLY F 4 42  ? -33.561 -24.532 -56.181 1.000 139.202 ? 42  GLY FFF N   1 
ATOM   7685  C CA  . GLY F 4 42  ? -32.369 -25.404 -56.231 1.000 142.862 ? 42  GLY FFF CA  1 
ATOM   7686  C C   . GLY F 4 42  ? -31.692 -25.564 -54.880 1.000 143.860 ? 42  GLY FFF C   1 
ATOM   7687  O O   . GLY F 4 42  ? -31.097 -26.644 -54.668 1.000 144.025 ? 42  GLY FFF O   1 
ATOM   7688  N N   . LYS F 4 43  ? -31.860 -24.579 -53.983 1.000 144.075 ? 43  LYS FFF N   1 
ATOM   7689  C CA  . LYS F 4 43  ? -31.045 -24.339 -52.760 1.000 145.683 ? 43  LYS FFF CA  1 
ATOM   7690  C C   . LYS F 4 43  ? -31.829 -24.699 -51.492 1.000 145.802 ? 43  LYS FFF C   1 
ATOM   7691  O O   . LYS F 4 43  ? -33.058 -24.538 -51.484 1.000 143.006 ? 43  LYS FFF O   1 
ATOM   7692  C CB  . LYS F 4 43  ? -30.674 -22.857 -52.658 1.000 146.678 ? 43  LYS FFF CB  1 
ATOM   7693  C CG  . LYS F 4 43  ? -29.319 -22.458 -53.226 1.000 150.845 ? 43  LYS FFF CG  1 
ATOM   7694  C CD  . LYS F 4 43  ? -29.007 -20.986 -53.024 1.000 152.294 ? 43  LYS FFF CD  1 
ATOM   7695  C CE  . LYS F 4 43  ? -27.543 -20.650 -53.237 1.000 156.239 ? 43  LYS FFF CE  1 
ATOM   7696  N NZ  . LYS F 4 43  ? -26.757 -20.714 -51.979 1.000 157.608 ? 43  LYS FFF NZ  1 
ATOM   7697  N N   . GLU F 4 44  ? -31.116 -25.110 -50.441 1.000 150.184 ? 44  GLU FFF N   1 
ATOM   7698  C CA  . GLU F 4 44  ? -31.710 -25.481 -49.127 1.000 153.526 ? 44  GLU FFF CA  1 
ATOM   7699  C C   . GLU F 4 44  ? -32.156 -24.182 -48.438 1.000 149.056 ? 44  GLU FFF C   1 
ATOM   7700  O O   . GLU F 4 44  ? -31.492 -23.148 -48.669 1.000 148.288 ? 44  GLU FFF O   1 
ATOM   7701  C CB  . GLU F 4 44  ? -30.718 -26.297 -48.293 1.000 159.843 ? 44  GLU FFF CB  1 
ATOM   7702  C CG  . GLU F 4 44  ? -30.035 -27.442 -49.043 1.000 166.819 ? 44  GLU FFF CG  1 
ATOM   7703  C CD  . GLU F 4 44  ? -30.929 -28.457 -49.748 1.000 172.414 ? 44  GLU FFF CD  1 
ATOM   7704  O OE1 . GLU F 4 44  ? -31.729 -29.127 -49.061 1.000 176.316 ? 44  GLU FFF OE1 1 
ATOM   7705  O OE2 . GLU F 4 44  ? -30.811 -28.589 -50.990 1.000 174.542 ? 44  GLU FFF OE2 1 
ATOM   7706  N N   . ARG F 4 45  ? -33.254 -24.212 -47.668 1.000 147.769 ? 45  ARG FFF N   1 
ATOM   7707  C CA  . ARG F 4 45  ? -33.869 -22.985 -47.078 1.000 145.803 ? 45  ARG FFF CA  1 
ATOM   7708  C C   . ARG F 4 45  ? -32.952 -22.491 -45.954 1.000 142.417 ? 45  ARG FFF C   1 
ATOM   7709  O O   . ARG F 4 45  ? -32.625 -23.287 -45.068 1.000 146.699 ? 45  ARG FFF O   1 
ATOM   7710  C CB  . ARG F 4 45  ? -35.345 -23.211 -46.698 1.000 148.070 ? 45  ARG FFF CB  1 
ATOM   7711  C CG  . ARG F 4 45  ? -35.707 -23.249 -45.217 1.000 148.109 ? 45  ARG FFF CG  1 
ATOM   7712  C CD  . ARG F 4 45  ? -35.360 -24.556 -44.544 1.000 151.331 ? 45  ARG FFF CD  1 
ATOM   7713  N NE  . ARG F 4 45  ? -34.295 -24.357 -43.567 1.000 152.338 ? 45  ARG FFF NE  1 
ATOM   7714  C CZ  . ARG F 4 45  ? -34.437 -24.377 -42.246 1.000 151.165 ? 45  ARG FFF CZ  1 
ATOM   7715  N NH1 . ARG F 4 45  ? -35.623 -24.602 -41.702 1.000 152.065 ? 45  ARG FFF NH1 1 
ATOM   7716  N NH2 . ARG F 4 45  ? -33.380 -24.177 -41.472 1.000 149.866 ? 45  ARG FFF NH2 1 
ATOM   7717  N N   . GLU F 4 46  ? -32.534 -21.226 -46.027 1.000 138.131 ? 46  GLU FFF N   1 
ATOM   7718  C CA  . GLU F 4 46  ? -31.493 -20.619 -45.156 1.000 137.604 ? 46  GLU FFF CA  1 
ATOM   7719  C C   . GLU F 4 46  ? -32.139 -19.564 -44.255 1.000 132.653 ? 46  GLU FFF C   1 
ATOM   7720  O O   . GLU F 4 46  ? -33.246 -19.094 -44.582 1.000 129.722 ? 46  GLU FFF O   1 
ATOM   7721  C CB  . GLU F 4 46  ? -30.387 -20.002 -46.015 1.000 141.199 ? 46  GLU FFF CB  1 
ATOM   7722  C CG  . GLU F 4 46  ? -30.858 -18.812 -46.845 1.000 141.936 ? 46  GLU FFF CG  1 
ATOM   7723  C CD  . GLU F 4 46  ? -30.165 -18.594 -48.176 1.000 143.929 ? 46  GLU FFF CD  1 
ATOM   7724  O OE1 . GLU F 4 46  ? -29.774 -17.433 -48.436 1.000 141.992 ? 46  GLU FFF OE1 1 
ATOM   7725  O OE2 . GLU F 4 46  ? -30.049 -19.577 -48.958 1.000 146.019 ? 46  GLU FFF OE2 1 
ATOM   7726  N N   . PHE F 4 47  ? -31.455 -19.208 -43.169 1.000 129.449 ? 47  PHE FFF N   1 
ATOM   7727  C CA  . PHE F 4 47  ? -31.854 -18.124 -42.237 1.000 126.463 ? 47  PHE FFF CA  1 
ATOM   7728  C C   . PHE F 4 47  ? -31.838 -16.794 -42.991 1.000 122.518 ? 47  PHE FFF C   1 
ATOM   7729  O O   . PHE F 4 47  ? -30.982 -16.649 -43.868 1.000 123.189 ? 47  PHE FFF O   1 
ATOM   7730  C CB  . PHE F 4 47  ? -30.905 -18.100 -41.040 1.000 128.191 ? 47  PHE FFF CB  1 
ATOM   7731  C CG  . PHE F 4 47  ? -31.149 -16.965 -40.084 1.000 127.290 ? 47  PHE FFF CG  1 
ATOM   7732  C CD1 . PHE F 4 47  ? -32.371 -16.833 -39.449 1.000 125.667 ? 47  PHE FFF CD1 1 
ATOM   7733  C CD2 . PHE F 4 47  ? -30.159 -16.029 -39.828 1.000 129.107 ? 47  PHE FFF CD2 1 
ATOM   7734  C CE1 . PHE F 4 47  ? -32.595 -15.788 -38.572 1.000 126.558 ? 47  PHE FFF CE1 1 
ATOM   7735  C CE2 . PHE F 4 47  ? -30.381 -14.989 -38.943 1.000 129.331 ? 47  PHE FFF CE2 1 
ATOM   7736  C CZ  . PHE F 4 47  ? -31.598 -14.873 -38.318 1.000 128.397 ? 47  PHE FFF CZ  1 
ATOM   7737  N N   . VAL F 4 48  ? -32.743 -15.871 -42.657 1.000 120.178 ? 48  VAL FFF N   1 
ATOM   7738  C CA  . VAL F 4 48  ? -32.808 -14.496 -43.245 1.000 120.090 ? 48  VAL FFF CA  1 
ATOM   7739  C C   . VAL F 4 48  ? -32.591 -13.471 -42.128 1.000 121.745 ? 48  VAL FFF C   1 
ATOM   7740  O O   . VAL F 4 48  ? -31.562 -12.770 -42.145 1.000 126.395 ? 48  VAL FFF O   1 
ATOM   7741  C CB  . VAL F 4 48  ? -34.147 -14.234 -43.961 1.000 118.683 ? 48  VAL FFF CB  1 
ATOM   7742  C CG1 . VAL F 4 48  ? -34.258 -12.803 -44.461 1.000 118.478 ? 48  VAL FFF CG1 1 
ATOM   7743  C CG2 . VAL F 4 48  ? -34.376 -15.208 -45.095 1.000 118.644 ? 48  VAL FFF CG2 1 
ATOM   7744  N N   . ALA F 4 49  ? -33.556 -13.372 -41.216 1.000 119.498 ? 49  ALA FFF N   1 
ATOM   7745  C CA  . ALA F 4 49  ? -33.561 -12.405 -40.100 1.000 118.740 ? 49  ALA FFF CA  1 
ATOM   7746  C C   . ALA F 4 49  ? -34.465 -12.938 -38.986 1.000 117.812 ? 49  ALA FFF C   1 
ATOM   7747  O O   . ALA F 4 49  ? -35.401 -13.697 -39.299 1.000 116.200 ? 49  ALA FFF O   1 
ATOM   7748  C CB  . ALA F 4 49  ? -34.021 -11.059 -40.600 1.000 118.877 ? 49  ALA FFF CB  1 
ATOM   7749  N N   . ALA F 4 50  ? -34.166 -12.565 -37.739 1.000 117.607 ? 50  ALA FFF N   1 
ATOM   7750  C CA  . ALA F 4 50  ? -35.022 -12.787 -36.553 1.000 116.396 ? 50  ALA FFF CA  1 
ATOM   7751  C C   . ALA F 4 50  ? -35.103 -11.485 -35.759 1.000 116.612 ? 50  ALA FFF C   1 
ATOM   7752  O O   . ALA F 4 50  ? -34.168 -10.661 -35.872 1.000 115.834 ? 50  ALA FFF O   1 
ATOM   7753  C CB  . ALA F 4 50  ? -34.474 -13.913 -35.720 1.000 116.783 ? 50  ALA FFF CB  1 
ATOM   7754  N N   . ILE F 4 51  ? -36.186 -11.319 -34.997 1.000 117.849 ? 51  ILE FFF N   1 
ATOM   7755  C CA  . ILE F 4 51  ? -36.428 -10.146 -34.108 1.000 122.040 ? 51  ILE FFF CA  1 
ATOM   7756  C C   . ILE F 4 51  ? -36.993 -10.640 -32.777 1.000 125.186 ? 51  ILE FFF C   1 
ATOM   7757  O O   . ILE F 4 51  ? -37.959 -11.430 -32.812 1.000 126.134 ? 51  ILE FFF O   1 
ATOM   7758  C CB  . ILE F 4 51  ? -37.392 -9.151  -34.772 1.000 124.422 ? 51  ILE FFF CB  1 
ATOM   7759  C CG1 . ILE F 4 51  ? -37.505 -7.865  -33.949 1.000 129.421 ? 51  ILE FFF CG1 1 
ATOM   7760  C CG2 . ILE F 4 51  ? -38.752 -9.791  -35.031 1.000 123.981 ? 51  ILE FFF CG2 1 
ATOM   7761  C CD1 . ILE F 4 51  ? -38.116 -6.698  -34.695 1.000 131.777 ? 51  ILE FFF CD1 1 
ATOM   7762  N N   . ARG F 4 52  ? -36.438 -10.172 -31.655 1.000 129.280 ? 52  ARG FFF N   1 
ATOM   7763  C CA  . ARG F 4 52  ? -36.983 -10.464 -30.301 1.000 133.258 ? 52  ARG FFF CA  1 
ATOM   7764  C C   . ARG F 4 52  ? -38.288 -9.679  -30.114 1.000 137.410 ? 52  ARG FFF C   1 
ATOM   7765  O O   . ARG F 4 52  ? -38.289 -8.458  -30.375 1.000 138.594 ? 52  ARG FFF O   1 
ATOM   7766  C CB  . ARG F 4 52  ? -35.980 -10.126 -29.194 1.000 133.173 ? 52  ARG FFF CB  1 
ATOM   7767  C CG  . ARG F 4 52  ? -36.306 -10.812 -27.877 1.000 132.473 ? 52  ARG FFF CG  1 
ATOM   7768  C CD  . ARG F 4 52  ? -35.439 -10.336 -26.737 1.000 132.302 ? 52  ARG FFF CD  1 
ATOM   7769  N NE  . ARG F 4 52  ? -34.046 -10.705 -26.922 1.000 129.805 ? 52  ARG FFF NE  1 
ATOM   7770  C CZ  . ARG F 4 52  ? -33.566 -11.942 -26.856 1.000 127.656 ? 52  ARG FFF CZ  1 
ATOM   7771  N NH1 . ARG F 4 52  ? -34.367 -12.966 -26.619 1.000 127.053 ? 52  ARG FFF NH1 1 
ATOM   7772  N NH2 . ARG F 4 52  ? -32.273 -12.149 -27.024 1.000 127.715 ? 52  ARG FFF NH2 1 
ATOM   7773  N N   . TRP F 4 53  ? -39.354 -10.365 -29.689 1.000 141.100 ? 53  TRP FFF N   1 
ATOM   7774  C CA  . TRP F 4 53  ? -40.687 -9.767  -29.416 1.000 144.871 ? 53  TRP FFF CA  1 
ATOM   7775  C C   . TRP F 4 53  ? -40.525 -8.623  -28.407 1.000 150.835 ? 53  TRP FFF C   1 
ATOM   7776  O O   . TRP F 4 53  ? -41.057 -7.526  -28.673 1.000 156.411 ? 53  TRP FFF O   1 
ATOM   7777  C CB  . TRP F 4 53  ? -41.673 -10.831 -28.909 1.000 144.662 ? 53  TRP FFF CB  1 
ATOM   7778  C CG  . TRP F 4 53  ? -43.093 -10.619 -29.334 1.000 144.266 ? 53  TRP FFF CG  1 
ATOM   7779  C CD1 . TRP F 4 53  ? -44.193 -10.478 -28.537 1.000 148.199 ? 53  TRP FFF CD1 1 
ATOM   7780  C CD2 . TRP F 4 53  ? -43.572 -10.542 -30.684 1.000 141.714 ? 53  TRP FFF CD2 1 
ATOM   7781  N NE1 . TRP F 4 53  ? -45.322 -10.315 -29.296 1.000 147.770 ? 53  TRP FFF NE1 1 
ATOM   7782  C CE2 . TRP F 4 53  ? -44.969 -10.347 -30.617 1.000 144.659 ? 53  TRP FFF CE2 1 
ATOM   7783  C CE3 . TRP F 4 53  ? -42.953 -10.606 -31.936 1.000 139.170 ? 53  TRP FFF CE3 1 
ATOM   7784  C CZ2 . TRP F 4 53  ? -45.753 -10.220 -31.760 1.000 145.144 ? 53  TRP FFF CZ2 1 
ATOM   7785  C CZ3 . TRP F 4 53  ? -43.729 -10.475 -33.065 1.000 139.201 ? 53  TRP FFF CZ3 1 
ATOM   7786  C CH2 . TRP F 4 53  ? -45.110 -10.292 -32.975 1.000 142.760 ? 53  TRP FFF CH2 1 
ATOM   7787  N N   . SER F 4 54  ? -39.801 -8.862  -27.307 1.000 151.363 ? 54  SER FFF N   1 
ATOM   7788  C CA  . SER F 4 54  ? -39.677 -7.917  -26.168 1.000 154.011 ? 54  SER FFF CA  1 
ATOM   7789  C C   . SER F 4 54  ? -38.383 -7.101  -26.278 1.000 153.630 ? 54  SER FFF C   1 
ATOM   7790  O O   . SER F 4 54  ? -37.581 -7.163  -25.333 1.000 158.541 ? 54  SER FFF O   1 
ATOM   7791  C CB  . SER F 4 54  ? -39.769 -8.646  -24.852 1.000 156.696 ? 54  SER FFF CB  1 
ATOM   7792  O OG  . SER F 4 54  ? -39.481 -7.765  -23.775 1.000 160.084 ? 54  SER FFF OG  1 
ATOM   7793  N N   . GLY F 4 55  ? -38.207 -6.333  -27.360 1.000 150.458 ? 55  GLY FFF N   1 
ATOM   7794  C CA  . GLY F 4 55  ? -37.097 -5.366  -27.485 1.000 149.480 ? 55  GLY FFF CA  1 
ATOM   7795  C C   . GLY F 4 55  ? -36.875 -4.856  -28.896 1.000 146.494 ? 55  GLY FFF C   1 
ATOM   7796  O O   . GLY F 4 55  ? -36.284 -3.769  -29.029 1.000 148.020 ? 55  GLY FFF O   1 
ATOM   7797  N N   . GLY F 4 56  ? -37.272 -5.623  -29.916 1.000 143.411 ? 56  GLY FFF N   1 
ATOM   7798  C CA  . GLY F 4 56  ? -37.166 -5.234  -31.337 1.000 141.677 ? 56  GLY FFF CA  1 
ATOM   7799  C C   . GLY F 4 56  ? -35.725 -5.195  -31.823 1.000 140.267 ? 56  GLY FFF C   1 
ATOM   7800  O O   . GLY F 4 56  ? -35.497 -4.713  -32.944 1.000 139.581 ? 56  GLY FFF O   1 
ATOM   7801  N N   . SER F 4 57  ? -34.779 -5.680  -31.016 1.000 140.315 ? 57  SER FFF N   1 
ATOM   7802  C CA  . SER F 4 57  ? -33.377 -5.928  -31.432 1.000 139.795 ? 57  SER FFF CA  1 
ATOM   7803  C C   . SER F 4 57  ? -33.390 -7.080  -32.444 1.000 135.788 ? 57  SER FFF C   1 
ATOM   7804  O O   . SER F 4 57  ? -33.856 -8.175  -32.075 1.000 134.100 ? 57  SER FFF O   1 
ATOM   7805  C CB  . SER F 4 57  ? -32.490 -6.204  -30.231 1.000 141.630 ? 57  SER FFF CB  1 
ATOM   7806  O OG  . SER F 4 57  ? -33.258 -6.468  -29.059 1.000 141.215 ? 57  SER FFF OG  1 
ATOM   7807  N N   . ALA F 4 58  ? -32.948 -6.830  -33.680 1.000 134.253 ? 58  ALA FFF N   1 
ATOM   7808  C CA  . ALA F 4 58  ? -32.976 -7.810  -34.793 1.000 132.546 ? 58  ALA FFF CA  1 
ATOM   7809  C C   . ALA F 4 58  ? -31.590 -8.429  -34.984 1.000 131.282 ? 58  ALA FFF C   1 
ATOM   7810  O O   . ALA F 4 58  ? -30.597 -7.783  -34.583 1.000 132.173 ? 58  ALA FFF O   1 
ATOM   7811  C CB  . ALA F 4 58  ? -33.444 -7.145  -36.064 1.000 133.949 ? 58  ALA FFF CB  1 
ATOM   7812  N N   . TYR F 4 59  ? -31.537 -9.631  -35.573 1.000 128.132 ? 59  TYR FFF N   1 
ATOM   7813  C CA  . TYR F 4 59  ? -30.288 -10.276 -36.052 1.000 128.881 ? 59  TYR FFF CA  1 
ATOM   7814  C C   . TYR F 4 59  ? -30.387 -10.549 -37.550 1.000 130.879 ? 59  TYR FFF C   1 
ATOM   7815  O O   . TYR F 4 59  ? -30.731 -11.665 -37.965 1.000 130.020 ? 59  TYR FFF O   1 
ATOM   7816  C CB  . TYR F 4 59  ? -29.977 -11.575 -35.317 1.000 126.284 ? 59  TYR FFF CB  1 
ATOM   7817  C CG  . TYR F 4 59  ? -28.612 -12.143 -35.627 1.000 125.142 ? 59  TYR FFF CG  1 
ATOM   7818  C CD1 . TYR F 4 59  ? -27.524 -11.317 -35.865 1.000 125.617 ? 59  TYR FFF CD1 1 
ATOM   7819  C CD2 . TYR F 4 59  ? -28.403 -13.511 -35.660 1.000 122.938 ? 59  TYR FFF CD2 1 
ATOM   7820  C CE1 . TYR F 4 59  ? -26.268 -11.835 -36.125 1.000 126.244 ? 59  TYR FFF CE1 1 
ATOM   7821  C CE2 . TYR F 4 59  ? -27.153 -14.047 -35.910 1.000 122.964 ? 59  TYR FFF CE2 1 
ATOM   7822  C CZ  . TYR F 4 59  ? -26.085 -13.206 -36.142 1.000 125.887 ? 59  TYR FFF CZ  1 
ATOM   7823  O OH  . TYR F 4 59  ? -24.864 -13.753 -36.392 1.000 131.444 ? 59  TYR FFF OH  1 
ATOM   7824  N N   . TYR F 4 60  ? -30.063 -9.524  -38.327 1.000 135.105 ? 60  TYR FFF N   1 
ATOM   7825  C CA  . TYR F 4 60  ? -29.942 -9.572  -39.799 1.000 134.800 ? 60  TYR FFF CA  1 
ATOM   7826  C C   . TYR F 4 60  ? -28.873 -10.607 -40.175 1.000 132.850 ? 60  TYR FFF C   1 
ATOM   7827  O O   . TYR F 4 60  ? -27.786 -10.642 -39.544 1.000 132.400 ? 60  TYR FFF O   1 
ATOM   7828  C CB  . TYR F 4 60  ? -29.727 -8.141  -40.287 1.000 141.311 ? 60  TYR FFF CB  1 
ATOM   7829  C CG  . TYR F 4 60  ? -31.051 -7.493  -40.547 1.000 144.611 ? 60  TYR FFF CG  1 
ATOM   7830  C CD1 . TYR F 4 60  ? -31.876 -7.094  -39.508 1.000 145.193 ? 60  TYR FFF CD1 1 
ATOM   7831  C CD2 . TYR F 4 60  ? -31.517 -7.413  -41.843 1.000 150.335 ? 60  TYR FFF CD2 1 
ATOM   7832  C CE1 . TYR F 4 60  ? -33.120 -6.551  -39.761 1.000 149.578 ? 60  TYR FFF CE1 1 
ATOM   7833  C CE2 . TYR F 4 60  ? -32.758 -6.880  -42.114 1.000 154.213 ? 60  TYR FFF CE2 1 
ATOM   7834  C CZ  . TYR F 4 60  ? -33.553 -6.455  -41.068 1.000 155.212 ? 60  TYR FFF CZ  1 
ATOM   7835  O OH  . TYR F 4 60  ? -34.782 -5.951  -41.328 1.000 161.074 ? 60  TYR FFF OH  1 
ATOM   7836  N N   . ALA F 4 61  ? -29.206 -11.474 -41.136 1.000 129.619 ? 61  ALA FFF N   1 
ATOM   7837  C CA  . ALA F 4 61  ? -28.290 -12.479 -41.726 1.000 130.201 ? 61  ALA FFF CA  1 
ATOM   7838  C C   . ALA F 4 61  ? -27.323 -11.783 -42.683 1.000 134.172 ? 61  ALA FFF C   1 
ATOM   7839  O O   . ALA F 4 61  ? -27.617 -10.673 -43.133 1.000 135.898 ? 61  ALA FFF O   1 
ATOM   7840  C CB  . ALA F 4 61  ? -29.048 -13.562 -42.438 1.000 126.839 ? 61  ALA FFF CB  1 
ATOM   7841  N N   . ASP F 4 62  ? -26.222 -12.449 -43.014 1.000 138.598 ? 62  ASP FFF N   1 
ATOM   7842  C CA  . ASP F 4 62  ? -24.976 -11.793 -43.495 1.000 143.410 ? 62  ASP FFF CA  1 
ATOM   7843  C C   . ASP F 4 62  ? -25.167 -11.283 -44.923 1.000 140.265 ? 62  ASP FFF C   1 
ATOM   7844  O O   . ASP F 4 62  ? -24.565 -10.251 -45.250 1.000 142.554 ? 62  ASP FFF O   1 
ATOM   7845  C CB  . ASP F 4 62  ? -23.786 -12.744 -43.369 1.000 150.682 ? 62  ASP FFF CB  1 
ATOM   7846  C CG  . ASP F 4 62  ? -23.852 -13.590 -42.104 1.000 155.441 ? 62  ASP FFF CG  1 
ATOM   7847  O OD1 . ASP F 4 62  ? -24.834 -14.367 -41.974 1.000 157.060 ? 62  ASP FFF OD1 1 
ATOM   7848  O OD2 . ASP F 4 62  ? -22.955 -13.433 -41.233 1.000 159.470 ? 62  ASP FFF OD2 1 
ATOM   7849  N N   . SER F 4 63  ? -25.985 -11.963 -45.728 1.000 136.161 ? 63  SER FFF N   1 
ATOM   7850  C CA  . SER F 4 63  ? -26.180 -11.665 -47.172 1.000 136.497 ? 63  SER FFF CA  1 
ATOM   7851  C C   . SER F 4 63  ? -27.252 -10.589 -47.382 1.000 135.761 ? 63  SER FFF C   1 
ATOM   7852  O O   . SER F 4 63  ? -27.368 -10.119 -48.532 1.000 137.789 ? 63  SER FFF O   1 
ATOM   7853  C CB  . SER F 4 63  ? -26.506 -12.913 -47.949 1.000 134.863 ? 63  SER FFF CB  1 
ATOM   7854  O OG  . SER F 4 63  ? -27.404 -13.742 -47.226 1.000 131.496 ? 63  SER FFF OG  1 
ATOM   7855  N N   . VAL F 4 64  ? -27.996 -10.216 -46.331 1.000 133.639 ? 64  VAL FFF N   1 
ATOM   7856  C CA  . VAL F 4 64  ? -29.074 -9.180  -46.388 1.000 133.657 ? 64  VAL FFF CA  1 
ATOM   7857  C C   . VAL F 4 64  ? -28.700 -7.967  -45.521 1.000 133.840 ? 64  VAL FFF C   1 
ATOM   7858  O O   . VAL F 4 64  ? -29.326 -6.895  -45.704 1.000 132.827 ? 64  VAL FFF O   1 
ATOM   7859  C CB  . VAL F 4 64  ? -30.446 -9.758  -45.984 1.000 132.150 ? 64  VAL FFF CB  1 
ATOM   7860  C CG1 . VAL F 4 64  ? -30.854 -10.917 -46.874 1.000 131.197 ? 64  VAL FFF CG1 1 
ATOM   7861  C CG2 . VAL F 4 64  ? -30.512 -10.172 -44.522 1.000 132.666 ? 64  VAL FFF CG2 1 
ATOM   7862  N N   . LYS F 4 65  ? -27.738 -8.115  -44.606 1.000 133.255 ? 65  LYS FFF N   1 
ATOM   7863  C CA  . LYS F 4 65  ? -27.248 -7.004  -43.754 1.000 135.631 ? 65  LYS FFF CA  1 
ATOM   7864  C C   . LYS F 4 65  ? -27.027 -5.805  -44.679 1.000 138.415 ? 65  LYS FFF C   1 
ATOM   7865  O O   . LYS F 4 65  ? -26.206 -5.924  -45.610 1.000 140.166 ? 65  LYS FFF O   1 
ATOM   7866  C CB  . LYS F 4 65  ? -25.977 -7.415  -43.002 1.000 138.650 ? 65  LYS FFF CB  1 
ATOM   7867  C CG  . LYS F 4 65  ? -25.934 -7.030  -41.528 1.000 141.146 ? 65  LYS FFF CG  1 
ATOM   7868  C CD  . LYS F 4 65  ? -25.142 -8.006  -40.669 1.000 144.149 ? 65  LYS FFF CD  1 
ATOM   7869  C CE  . LYS F 4 65  ? -25.524 -7.962  -39.199 1.000 145.811 ? 65  LYS FFF CE  1 
ATOM   7870  N NZ  . LYS F 4 65  ? -25.440 -9.294  -38.547 1.000 143.782 ? 65  LYS FFF NZ  1 
ATOM   7871  N N   . GLY F 4 66  ? -27.800 -4.734  -44.479 1.000 140.184 ? 66  GLY FFF N   1 
ATOM   7872  C CA  . GLY F 4 66  ? -27.633 -3.443  -45.174 1.000 143.214 ? 66  GLY FFF CA  1 
ATOM   7873  C C   . GLY F 4 66  ? -28.713 -3.196  -46.208 1.000 141.401 ? 66  GLY FFF C   1 
ATOM   7874  O O   . GLY F 4 66  ? -28.658 -2.125  -46.844 1.000 145.353 ? 66  GLY FFF O   1 
ATOM   7875  N N   . ARG F 4 67  ? -29.651 -4.136  -46.381 1.000 137.285 ? 67  ARG FFF N   1 
ATOM   7876  C CA  . ARG F 4 67  ? -30.715 -4.058  -47.419 1.000 138.515 ? 67  ARG FFF CA  1 
ATOM   7877  C C   . ARG F 4 67  ? -32.093 -4.237  -46.769 1.000 137.498 ? 67  ARG FFF C   1 
ATOM   7878  O O   . ARG F 4 67  ? -32.925 -3.327  -46.910 1.000 140.026 ? 67  ARG FFF O   1 
ATOM   7879  C CB  . ARG F 4 67  ? -30.430 -5.067  -48.539 1.000 137.674 ? 67  ARG FFF CB  1 
ATOM   7880  C CG  . ARG F 4 67  ? -29.033 -4.932  -49.138 1.000 139.654 ? 67  ARG FFF CG  1 
ATOM   7881  C CD  . ARG F 4 67  ? -28.768 -5.733  -50.402 1.000 137.769 ? 67  ARG FFF CD  1 
ATOM   7882  N NE  . ARG F 4 67  ? -29.093 -7.147  -50.248 1.000 133.071 ? 67  ARG FFF NE  1 
ATOM   7883  C CZ  . ARG F 4 67  ? -30.080 -7.784  -50.873 1.000 129.967 ? 67  ARG FFF CZ  1 
ATOM   7884  N NH1 . ARG F 4 67  ? -30.862 -7.144  -51.729 1.000 131.561 ? 67  ARG FFF NH1 1 
ATOM   7885  N NH2 . ARG F 4 67  ? -30.279 -9.070  -50.640 1.000 125.874 ? 67  ARG FFF NH2 1 
ATOM   7886  N N   . PHE F 4 68  ? -32.323 -5.343  -46.061 1.000 140.524 ? 68  PHE FFF N   1 
ATOM   7887  C CA  . PHE F 4 68  ? -33.647 -5.711  -45.488 1.000 140.917 ? 68  PHE FFF CA  1 
ATOM   7888  C C   . PHE F 4 68  ? -33.886 -4.894  -44.198 1.000 145.046 ? 68  PHE FFF C   1 
ATOM   7889  O O   . PHE F 4 68  ? -32.926 -4.225  -43.746 1.000 149.946 ? 68  PHE FFF O   1 
ATOM   7890  C CB  . PHE F 4 68  ? -33.704 -7.238  -45.341 1.000 138.090 ? 68  PHE FFF CB  1 
ATOM   7891  C CG  . PHE F 4 68  ? -33.758 -8.012  -46.640 1.000 138.306 ? 68  PHE FFF CG  1 
ATOM   7892  C CD1 . PHE F 4 68  ? -33.491 -7.393  -47.853 1.000 141.648 ? 68  PHE FFF CD1 1 
ATOM   7893  C CD2 . PHE F 4 68  ? -34.043 -9.373  -46.654 1.000 134.832 ? 68  PHE FFF CD2 1 
ATOM   7894  C CE1 . PHE F 4 68  ? -33.533 -8.104  -49.042 1.000 141.255 ? 68  PHE FFF CE1 1 
ATOM   7895  C CE2 . PHE F 4 68  ? -34.081 -10.085 -47.843 1.000 133.477 ? 68  PHE FFF CE2 1 
ATOM   7896  C CZ  . PHE F 4 68  ? -33.825 -9.449  -49.035 1.000 137.499 ? 68  PHE FFF CZ  1 
ATOM   7897  N N   . THR F 4 69  ? -35.120 -4.890  -43.656 1.000 145.866 ? 69  THR FFF N   1 
ATOM   7898  C CA  . THR F 4 69  ? -35.471 -4.411  -42.276 1.000 146.982 ? 69  THR FFF CA  1 
ATOM   7899  C C   . THR F 4 69  ? -36.640 -5.242  -41.692 1.000 142.475 ? 69  THR FFF C   1 
ATOM   7900  O O   . THR F 4 69  ? -37.793 -5.051  -42.136 1.000 139.480 ? 69  THR FFF O   1 
ATOM   7901  C CB  . THR F 4 69  ? -35.774 -2.905  -42.186 1.000 152.305 ? 69  THR FFF CB  1 
ATOM   7902  O OG1 . THR F 4 69  ? -34.765 -2.153  -42.870 1.000 154.062 ? 69  THR FFF OG1 1 
ATOM   7903  C CG2 . THR F 4 69  ? -35.853 -2.435  -40.745 1.000 154.253 ? 69  THR FFF CG2 1 
ATOM   7904  N N   . ILE F 4 70  ? -36.348 -6.124  -40.719 1.000 139.357 ? 70  ILE FFF N   1 
ATOM   7905  C CA  . ILE F 4 70  ? -37.335 -6.877  -39.890 1.000 135.076 ? 70  ILE FFF CA  1 
ATOM   7906  C C   . ILE F 4 70  ? -37.762 -5.954  -38.749 1.000 136.413 ? 70  ILE FFF C   1 
ATOM   7907  O O   . ILE F 4 70  ? -36.899 -5.277  -38.148 1.000 136.293 ? 70  ILE FFF O   1 
ATOM   7908  C CB  . ILE F 4 70  ? -36.799 -8.231  -39.370 1.000 131.020 ? 70  ILE FFF CB  1 
ATOM   7909  C CG1 . ILE F 4 70  ? -37.946 -9.119  -38.876 1.000 128.963 ? 70  ILE FFF CG1 1 
ATOM   7910  C CG2 . ILE F 4 70  ? -35.740 -8.052  -38.292 1.000 132.547 ? 70  ILE FFF CG2 1 
ATOM   7911  C CD1 . ILE F 4 70  ? -37.526 -10.505 -38.448 1.000 127.608 ? 70  ILE FFF CD1 1 
ATOM   7912  N N   . SER F 4 71  ? -39.065 -5.916  -38.508 1.000 137.351 ? 71  SER FFF N   1 
ATOM   7913  C CA  . SER F 4 71  ? -39.735 -5.065  -37.503 1.000 142.244 ? 71  SER FFF CA  1 
ATOM   7914  C C   . SER F 4 71  ? -41.046 -5.756  -37.141 1.000 144.490 ? 71  SER FFF C   1 
ATOM   7915  O O   . SER F 4 71  ? -41.541 -6.535  -37.983 1.000 143.426 ? 71  SER FFF O   1 
ATOM   7916  C CB  . SER F 4 71  ? -39.965 -3.685  -38.048 1.000 146.858 ? 71  SER FFF CB  1 
ATOM   7917  O OG  . SER F 4 71  ? -40.768 -3.739  -39.221 1.000 148.129 ? 71  SER FFF OG  1 
ATOM   7918  N N   . ARG F 4 72  ? -41.578 -5.495  -35.948 1.000 148.583 ? 72  ARG FFF N   1 
ATOM   7919  C CA  . ARG F 4 72  ? -42.828 -6.140  -35.472 1.000 150.586 ? 72  ARG FFF CA  1 
ATOM   7920  C C   . ARG F 4 72  ? -43.718 -5.084  -34.817 1.000 153.363 ? 72  ARG FFF C   1 
ATOM   7921  O O   . ARG F 4 72  ? -43.176 -4.099  -34.283 1.000 154.498 ? 72  ARG FFF O   1 
ATOM   7922  C CB  . ARG F 4 72  ? -42.501 -7.312  -34.542 1.000 151.388 ? 72  ARG FFF CB  1 
ATOM   7923  C CG  . ARG F 4 72  ? -41.663 -6.948  -33.323 1.000 154.527 ? 72  ARG FFF CG  1 
ATOM   7924  C CD  . ARG F 4 72  ? -42.520 -6.723  -32.096 1.000 160.180 ? 72  ARG FFF CD  1 
ATOM   7925  N NE  . ARG F 4 72  ? -41.761 -6.318  -30.918 1.000 162.120 ? 72  ARG FFF NE  1 
ATOM   7926  C CZ  . ARG F 4 72  ? -41.338 -5.084  -30.653 1.000 164.711 ? 72  ARG FFF CZ  1 
ATOM   7927  N NH1 . ARG F 4 72  ? -41.579 -4.096  -31.497 1.000 168.682 ? 72  ARG FFF NH1 1 
ATOM   7928  N NH2 . ARG F 4 72  ? -40.670 -4.846  -29.536 1.000 164.470 ? 72  ARG FFF NH2 1 
ATOM   7929  N N   . ASP F 4 73  ? -45.034 -5.287  -34.907 1.000 156.250 ? 73  ASP FFF N   1 
ATOM   7930  C CA  . ASP F 4 73  ? -46.083 -4.471  -34.242 1.000 161.094 ? 73  ASP FFF CA  1 
ATOM   7931  C C   . ASP F 4 73  ? -46.815 -5.386  -33.253 1.000 159.969 ? 73  ASP FFF C   1 
ATOM   7932  O O   . ASP F 4 73  ? -47.635 -6.212  -33.709 1.000 159.213 ? 73  ASP FFF O   1 
ATOM   7933  C CB  . ASP F 4 73  ? -47.016 -3.844  -35.283 1.000 166.006 ? 73  ASP FFF CB  1 
ATOM   7934  C CG  . ASP F 4 73  ? -48.110 -2.969  -34.693 1.000 171.873 ? 73  ASP FFF CG  1 
ATOM   7935  O OD1 . ASP F 4 73  ? -48.138 -2.821  -33.453 1.000 173.025 ? 73  ASP FFF OD1 1 
ATOM   7936  O OD2 . ASP F 4 73  ? -48.924 -2.437  -35.479 1.000 176.977 ? 73  ASP FFF OD2 1 
ATOM   7937  N N   . LYS F 4 74  ? -46.514 -5.253  -31.956 1.000 159.223 ? 74  LYS FFF N   1 
ATOM   7938  C CA  . LYS F 4 74  ? -46.957 -6.196  -30.891 1.000 159.997 ? 74  LYS FFF CA  1 
ATOM   7939  C C   . LYS F 4 74  ? -48.488 -6.199  -30.786 1.000 163.069 ? 74  LYS FFF C   1 
ATOM   7940  O O   . LYS F 4 74  ? -49.061 -7.282  -30.552 1.000 164.116 ? 74  LYS FFF O   1 
ATOM   7941  C CB  . LYS F 4 74  ? -46.329 -5.824  -29.546 1.000 162.033 ? 74  LYS FFF CB  1 
ATOM   7942  C CG  . LYS F 4 74  ? -44.851 -6.159  -29.403 1.000 160.531 ? 74  LYS FFF CG  1 
ATOM   7943  C CD  . LYS F 4 74  ? -44.295 -5.893  -28.016 1.000 164.284 ? 74  LYS FFF CD  1 
ATOM   7944  C CE  . LYS F 4 74  ? -44.569 -7.010  -27.028 1.000 166.327 ? 74  LYS FFF CE  1 
ATOM   7945  N NZ  . LYS F 4 74  ? -43.952 -6.737  -25.707 1.000 168.068 ? 74  LYS FFF NZ  1 
ATOM   7946  N N   . ALA F 4 75  ? -49.117 -5.032  -30.945 1.000 165.822 ? 75  ALA FFF N   1 
ATOM   7947  C CA  . ALA F 4 75  ? -50.582 -4.829  -30.849 1.000 170.516 ? 75  ALA FFF CA  1 
ATOM   7948  C C   . ALA F 4 75  ? -51.295 -5.522  -32.017 1.000 170.700 ? 75  ALA FFF C   1 
ATOM   7949  O O   . ALA F 4 75  ? -52.459 -5.926  -31.824 1.000 173.403 ? 75  ALA FFF O   1 
ATOM   7950  C CB  . ALA F 4 75  ? -50.898 -3.354  -30.816 1.000 174.439 ? 75  ALA FFF CB  1 
ATOM   7951  N N   . LYS F 4 76  ? -50.631 -5.637  -33.176 1.000 169.216 ? 76  LYS FFF N   1 
ATOM   7952  C CA  . LYS F 4 76  ? -51.178 -6.255  -34.420 1.000 169.801 ? 76  LYS FFF CA  1 
ATOM   7953  C C   . LYS F 4 76  ? -50.701 -7.714  -34.553 1.000 164.056 ? 76  LYS FFF C   1 
ATOM   7954  O O   . LYS F 4 76  ? -51.167 -8.389  -35.490 1.000 163.308 ? 76  LYS FFF O   1 
ATOM   7955  C CB  . LYS F 4 76  ? -50.788 -5.440  -35.664 1.000 171.198 ? 76  LYS FFF CB  1 
ATOM   7956  C CG  . LYS F 4 76  ? -51.654 -4.218  -35.973 1.000 176.763 ? 76  LYS FFF CG  1 
ATOM   7957  C CD  . LYS F 4 76  ? -51.388 -3.593  -37.348 1.000 176.239 ? 76  LYS FFF CD  1 
ATOM   7958  C CE  . LYS F 4 76  ? -52.490 -2.672  -37.835 1.000 181.991 ? 76  LYS FFF CE  1 
ATOM   7959  N NZ  . LYS F 4 76  ? -52.974 -1.768  -36.764 1.000 187.715 ? 76  LYS FFF NZ  1 
ATOM   7960  N N   . ASN F 4 77  ? -49.820 -8.194  -33.666 1.000 159.743 ? 77  ASN FFF N   1 
ATOM   7961  C CA  . ASN F 4 77  ? -49.271 -9.580  -33.697 1.000 155.977 ? 77  ASN FFF CA  1 
ATOM   7962  C C   . ASN F 4 77  ? -48.722 -9.875  -35.093 1.000 152.781 ? 77  ASN FFF C   1 
ATOM   7963  O O   . ASN F 4 77  ? -48.900 -11.005 -35.585 1.000 150.596 ? 77  ASN FFF O   1 
ATOM   7964  C CB  . ASN F 4 77  ? -50.319 -10.617 -33.297 1.000 158.857 ? 77  ASN FFF CB  1 
ATOM   7965  C CG  . ASN F 4 77  ? -50.683 -10.518 -31.835 1.000 164.062 ? 77  ASN FFF CG  1 
ATOM   7966  O OD1 . ASN F 4 77  ? -49.820 -10.243 -31.005 1.000 165.312 ? 77  ASN FFF OD1 1 
ATOM   7967  N ND2 . ASN F 4 77  ? -51.951 -10.728 -31.521 1.000 171.319 ? 77  ASN FFF ND2 1 
ATOM   7968  N N   . THR F 4 78  ? -48.084 -8.877  -35.698 1.000 152.419 ? 78  THR FFF N   1 
ATOM   7969  C CA  . THR F 4 78  ? -47.538 -8.926  -37.073 1.000 151.071 ? 78  THR FFF CA  1 
ATOM   7970  C C   . THR F 4 78  ? -46.028 -8.717  -36.993 1.000 147.119 ? 78  THR FFF C   1 
ATOM   7971  O O   . THR F 4 78  ? -45.585 -7.881  -36.173 1.000 147.997 ? 78  THR FFF O   1 
ATOM   7972  C CB  . THR F 4 78  ? -48.184 -7.859  -37.965 1.000 156.167 ? 78  THR FFF CB  1 
ATOM   7973  O OG1 . THR F 4 78  ? -49.588 -7.857  -37.703 1.000 159.739 ? 78  THR FFF OG1 1 
ATOM   7974  C CG2 . THR F 4 78  ? -47.921 -8.090  -39.438 1.000 156.566 ? 78  THR FFF CG2 1 
ATOM   7975  N N   . VAL F 4 79  ? -45.283 -9.455  -37.811 1.000 142.013 ? 79  VAL FFF N   1 
ATOM   7976  C CA  . VAL F 4 79  ? -43.848 -9.178  -38.098 1.000 137.977 ? 79  VAL FFF CA  1 
ATOM   7977  C C   . VAL F 4 79  ? -43.745 -8.836  -39.585 1.000 136.001 ? 79  VAL FFF C   1 
ATOM   7978  O O   . VAL F 4 79  ? -44.482 -9.449  -40.384 1.000 134.583 ? 79  VAL FFF O   1 
ATOM   7979  C CB  . VAL F 4 79  ? -42.948 -10.356 -37.687 1.000 136.140 ? 79  VAL FFF CB  1 
ATOM   7980  C CG1 . VAL F 4 79  ? -43.318 -11.644 -38.408 1.000 136.997 ? 79  VAL FFF CG1 1 
ATOM   7981  C CG2 . VAL F 4 79  ? -41.476 -10.030 -37.877 1.000 134.585 ? 79  VAL FFF CG2 1 
ATOM   7982  N N   . TYR F 4 80  ? -42.891 -7.864  -39.921 1.000 136.149 ? 80  TYR FFF N   1 
ATOM   7983  C CA  . TYR F 4 80  ? -42.692 -7.328  -41.292 1.000 136.725 ? 80  TYR FFF CA  1 
ATOM   7984  C C   . TYR F 4 80  ? -41.246 -7.580  -41.739 1.000 134.950 ? 80  TYR FFF C   1 
ATOM   7985  O O   . TYR F 4 80  ? -40.334 -7.442  -40.899 1.000 137.173 ? 80  TYR FFF O   1 
ATOM   7986  C CB  . TYR F 4 80  ? -43.012 -5.830  -41.329 1.000 139.143 ? 80  TYR FFF CB  1 
ATOM   7987  C CG  . TYR F 4 80  ? -44.389 -5.455  -40.842 1.000 142.250 ? 80  TYR FFF CG  1 
ATOM   7988  C CD1 . TYR F 4 80  ? -45.514 -5.694  -41.617 1.000 144.528 ? 80  TYR FFF CD1 1 
ATOM   7989  C CD2 . TYR F 4 80  ? -44.574 -4.837  -39.615 1.000 145.540 ? 80  TYR FFF CD2 1 
ATOM   7990  C CE1 . TYR F 4 80  ? -46.784 -5.342  -41.183 1.000 148.563 ? 80  TYR FFF CE1 1 
ATOM   7991  C CE2 . TYR F 4 80  ? -45.838 -4.478  -39.163 1.000 149.446 ? 80  TYR FFF CE2 1 
ATOM   7992  C CZ  . TYR F 4 80  ? -46.950 -4.730  -39.949 1.000 150.937 ? 80  TYR FFF CZ  1 
ATOM   7993  O OH  . TYR F 4 80  ? -48.195 -4.376  -39.499 1.000 152.364 ? 80  TYR FFF OH  1 
ATOM   7994  N N   . LEU F 4 81  ? -41.048 -7.941  -43.014 1.000 131.580 ? 81  LEU FFF N   1 
ATOM   7995  C CA  . LEU F 4 81  ? -39.724 -7.918  -43.692 1.000 128.880 ? 81  LEU FFF CA  1 
ATOM   7996  C C   . LEU F 4 81  ? -39.752 -6.858  -44.800 1.000 132.290 ? 81  LEU FFF C   1 
ATOM   7997  O O   . LEU F 4 81  ? -40.459 -7.066  -45.802 1.000 131.978 ? 81  LEU FFF O   1 
ATOM   7998  C CB  . LEU F 4 81  ? -39.400 -9.305  -44.252 1.000 124.401 ? 81  LEU FFF CB  1 
ATOM   7999  C CG  . LEU F 4 81  ? -37.965 -9.475  -44.743 1.000 124.695 ? 81  LEU FFF CG  1 
ATOM   8000  C CD1 . LEU F 4 81  ? -36.976 -9.351  -43.593 1.000 125.235 ? 81  LEU FFF CD1 1 
ATOM   8001  C CD2 . LEU F 4 81  ? -37.783 -10.798 -45.469 1.000 123.227 ? 81  LEU FFF CD2 1 
ATOM   8002  N N   . GLN F 4 82  ? -39.041 -5.747  -44.589 1.000 136.351 ? 82  GLN FFF N   1 
ATOM   8003  C CA  . GLN F 4 82  ? -38.792 -4.702  -45.615 1.000 139.289 ? 82  GLN FFF CA  1 
ATOM   8004  C C   . GLN F 4 82  ? -37.580 -5.149  -46.430 1.000 135.964 ? 82  GLN FFF C   1 
ATOM   8005  O O   . GLN F 4 82  ? -36.530 -5.401  -45.828 1.000 132.946 ? 82  GLN FFF O   1 
ATOM   8006  C CB  . GLN F 4 82  ? -38.553 -3.335  -44.965 1.000 145.903 ? 82  GLN FFF CB  1 
ATOM   8007  C CG  . GLN F 4 82  ? -38.660 -2.174  -45.940 1.000 150.841 ? 82  GLN FFF CG  1 
ATOM   8008  C CD  . GLN F 4 82  ? -40.010 -2.177  -46.609 1.000 152.461 ? 82  GLN FFF CD  1 
ATOM   8009  O OE1 . GLN F 4 82  ? -41.048 -2.117  -45.951 1.000 154.071 ? 82  GLN FFF OE1 1 
ATOM   8010  N NE2 . GLN F 4 82  ? -40.002 -2.276  -47.929 1.000 154.019 ? 82  GLN FFF NE2 1 
ATOM   8011  N N   . MET F 4 83  ? -37.738 -5.281  -47.743 1.000 135.868 ? 83  MET FFF N   1 
ATOM   8012  C CA  . MET F 4 83  ? -36.679 -5.799  -48.646 1.000 136.416 ? 83  MET FFF CA  1 
ATOM   8013  C C   . MET F 4 83  ? -36.274 -4.697  -49.626 1.000 139.617 ? 83  MET FFF C   1 
ATOM   8014  O O   . MET F 4 83  ? -36.825 -4.658  -50.734 1.000 142.186 ? 83  MET FFF O   1 
ATOM   8015  C CB  . MET F 4 83  ? -37.177 -7.036  -49.397 1.000 134.942 ? 83  MET FFF CB  1 
ATOM   8016  C CG  . MET F 4 83  ? -37.600 -8.152  -48.466 1.000 133.455 ? 83  MET FFF CG  1 
ATOM   8017  S SD  . MET F 4 83  ? -38.482 -9.473  -49.310 1.000 134.923 ? 83  MET FFF SD  1 
ATOM   8018  C CE  . MET F 4 83  ? -37.146 -10.255 -50.207 1.000 136.062 ? 83  MET FFF CE  1 
ATOM   8019  N N   . ASN F 4 84  ? -35.356 -3.824  -49.208 1.000 141.971 ? 84  ASN FFF N   1 
ATOM   8020  C CA  . ASN F 4 84  ? -34.784 -2.738  -50.049 1.000 146.550 ? 84  ASN FFF CA  1 
ATOM   8021  C C   . ASN F 4 84  ? -33.716 -3.353  -50.966 1.000 144.852 ? 84  ASN FFF C   1 
ATOM   8022  O O   . ASN F 4 84  ? -33.232 -4.453  -50.653 1.000 138.892 ? 84  ASN FFF O   1 
ATOM   8023  C CB  . ASN F 4 84  ? -34.208 -1.595  -49.200 1.000 153.038 ? 84  ASN FFF CB  1 
ATOM   8024  C CG  . ASN F 4 84  ? -35.131 -1.112  -48.096 1.000 155.306 ? 84  ASN FFF CG  1 
ATOM   8025  O OD1 . ASN F 4 84  ? -36.315 -0.875  -48.331 1.000 158.730 ? 84  ASN FFF OD1 1 
ATOM   8026  N ND2 . ASN F 4 84  ? -34.597 -0.944  -46.893 1.000 154.465 ? 84  ASN FFF ND2 1 
ATOM   8027  N N   . SER F 4 85  ? -33.394 -2.674  -52.071 1.000 149.285 ? 85  SER FFF N   1 
ATOM   8028  C CA  . SER F 4 85  ? -32.263 -2.972  -52.994 1.000 152.052 ? 85  SER FFF CA  1 
ATOM   8029  C C   . SER F 4 85  ? -32.313 -4.422  -53.486 1.000 149.289 ? 85  SER FFF C   1 
ATOM   8030  O O   . SER F 4 85  ? -31.223 -5.034  -53.560 1.000 151.045 ? 85  SER FFF O   1 
ATOM   8031  C CB  . SER F 4 85  ? -30.926 -2.712  -52.326 1.000 153.824 ? 85  SER FFF CB  1 
ATOM   8032  O OG  . SER F 4 85  ? -30.836 -1.393  -51.821 1.000 158.494 ? 85  SER FFF OG  1 
ATOM   8033  N N   . LEU F 4 86  ? -33.493 -4.958  -53.828 1.000 146.332 ? 86  LEU FFF N   1 
ATOM   8034  C CA  . LEU F 4 86  ? -33.643 -6.414  -54.119 1.000 143.473 ? 86  LEU FFF CA  1 
ATOM   8035  C C   . LEU F 4 86  ? -32.580 -6.820  -55.153 1.000 145.378 ? 86  LEU FFF C   1 
ATOM   8036  O O   . LEU F 4 86  ? -32.405 -6.100  -56.157 1.000 146.982 ? 86  LEU FFF O   1 
ATOM   8037  C CB  . LEU F 4 86  ? -35.045 -6.793  -54.619 1.000 141.133 ? 86  LEU FFF CB  1 
ATOM   8038  C CG  . LEU F 4 86  ? -36.245 -6.308  -53.811 1.000 139.396 ? 86  LEU FFF CG  1 
ATOM   8039  C CD1 . LEU F 4 86  ? -36.686 -4.941  -54.307 1.000 142.394 ? 86  LEU FFF CD1 1 
ATOM   8040  C CD2 . LEU F 4 86  ? -37.401 -7.300  -53.897 1.000 135.820 ? 86  LEU FFF CD2 1 
ATOM   8041  N N   . LYS F 4 87  ? -31.876 -7.918  -54.873 1.000 145.503 ? 87  LYS FFF N   1 
ATOM   8042  C CA  . LYS F 4 87  ? -30.931 -8.607  -55.789 1.000 149.362 ? 87  LYS FFF CA  1 
ATOM   8043  C C   . LYS F 4 87  ? -31.697 -9.725  -56.509 1.000 147.601 ? 87  LYS FFF C   1 
ATOM   8044  O O   . LYS F 4 87  ? -32.812 -10.034 -56.062 1.000 142.641 ? 87  LYS FFF O   1 
ATOM   8045  C CB  . LYS F 4 87  ? -29.761 -9.191  -54.992 1.000 152.144 ? 87  LYS FFF CB  1 
ATOM   8046  C CG  . LYS F 4 87  ? -28.664 -8.212  -54.591 1.000 156.904 ? 87  LYS FFF CG  1 
ATOM   8047  C CD  . LYS F 4 87  ? -27.364 -8.932  -54.273 1.000 160.250 ? 87  LYS FFF CD  1 
ATOM   8048  C CE  . LYS F 4 87  ? -26.568 -8.317  -53.142 1.000 163.681 ? 87  LYS FFF CE  1 
ATOM   8049  N NZ  . LYS F 4 87  ? -25.884 -9.356  -52.332 1.000 164.735 ? 87  LYS FFF NZ  1 
ATOM   8050  N N   . TYR F 4 88  ? -31.113 -10.320 -57.559 1.000 150.447 ? 88  TYR FFF N   1 
ATOM   8051  C CA  . TYR F 4 88  ? -31.681 -11.480 -58.305 1.000 148.283 ? 88  TYR FFF CA  1 
ATOM   8052  C C   . TYR F 4 88  ? -31.655 -12.740 -57.421 1.000 144.292 ? 88  TYR FFF C   1 
ATOM   8053  O O   . TYR F 4 88  ? -32.498 -13.630 -57.634 1.000 141.029 ? 88  TYR FFF O   1 
ATOM   8054  C CB  . TYR F 4 88  ? -30.935 -11.720 -59.625 1.000 152.178 ? 88  TYR FFF CB  1 
ATOM   8055  C CG  . TYR F 4 88  ? -31.406 -10.899 -60.801 1.000 154.507 ? 88  TYR FFF CG  1 
ATOM   8056  C CD1 . TYR F 4 88  ? -32.755 -10.770 -61.090 1.000 153.239 ? 88  TYR FFF CD1 1 
ATOM   8057  C CD2 . TYR F 4 88  ? -30.503 -10.274 -61.650 1.000 158.168 ? 88  TYR FFF CD2 1 
ATOM   8058  C CE1 . TYR F 4 88  ? -33.195 -10.022 -62.170 1.000 156.171 ? 88  TYR FFF CE1 1 
ATOM   8059  C CE2 . TYR F 4 88  ? -30.925 -9.530  -62.739 1.000 159.671 ? 88  TYR FFF CE2 1 
ATOM   8060  C CZ  . TYR F 4 88  ? -32.276 -9.402  -63.003 1.000 158.939 ? 88  TYR FFF CZ  1 
ATOM   8061  O OH  . TYR F 4 88  ? -32.680 -8.658  -64.076 1.000 160.668 ? 88  TYR FFF OH  1 
ATOM   8062  N N   . GLU F 4 89  ? -30.727 -12.801 -56.457 1.000 144.525 ? 89  GLU FFF N   1 
ATOM   8063  C CA  . GLU F 4 89  ? -30.533 -13.920 -55.489 1.000 141.768 ? 89  GLU FFF CA  1 
ATOM   8064  C C   . GLU F 4 89  ? -31.682 -13.971 -54.483 1.000 132.560 ? 89  GLU FFF C   1 
ATOM   8065  O O   . GLU F 4 89  ? -31.800 -14.990 -53.804 1.000 125.224 ? 89  GLU FFF O   1 
ATOM   8066  C CB  . GLU F 4 89  ? -29.219 -13.765 -54.714 1.000 148.374 ? 89  GLU FFF CB  1 
ATOM   8067  C CG  . GLU F 4 89  ? -28.053 -14.514 -55.338 1.000 158.123 ? 89  GLU FFF CG  1 
ATOM   8068  C CD  . GLU F 4 89  ? -27.786 -14.238 -56.816 1.000 166.070 ? 89  GLU FFF CD  1 
ATOM   8069  O OE1 . GLU F 4 89  ? -27.238 -15.134 -57.506 1.000 169.423 ? 89  GLU FFF OE1 1 
ATOM   8070  O OE2 . GLU F 4 89  ? -28.119 -13.125 -57.280 1.000 172.652 ? 89  GLU FFF OE2 1 
ATOM   8071  N N   . ASP F 4 90  ? -32.455 -12.891 -54.372 1.000 132.487 ? 90  ASP FFF N   1 
ATOM   8072  C CA  . ASP F 4 90  ? -33.583 -12.752 -53.416 1.000 132.810 ? 90  ASP FFF CA  1 
ATOM   8073  C C   . ASP F 4 90  ? -34.822 -13.494 -53.931 1.000 132.287 ? 90  ASP FFF C   1 
ATOM   8074  O O   . ASP F 4 90  ? -35.784 -13.606 -53.148 1.000 130.809 ? 90  ASP FFF O   1 
ATOM   8075  C CB  . ASP F 4 90  ? -33.931 -11.283 -53.170 1.000 135.448 ? 90  ASP FFF CB  1 
ATOM   8076  C CG  . ASP F 4 90  ? -32.833 -10.491 -52.480 1.000 138.192 ? 90  ASP FFF CG  1 
ATOM   8077  O OD1 . ASP F 4 90  ? -31.857 -11.114 -52.001 1.000 138.228 ? 90  ASP FFF OD1 1 
ATOM   8078  O OD2 . ASP F 4 90  ? -32.967 -9.252  -52.420 1.000 142.072 ? 90  ASP FFF OD2 1 
ATOM   8079  N N   . THR F 4 91  ? -34.837 -13.948 -55.192 1.000 133.960 ? 91  THR FFF N   1 
ATOM   8080  C CA  . THR F 4 91  ? -35.963 -14.744 -55.759 1.000 134.544 ? 91  THR FFF CA  1 
ATOM   8081  C C   . THR F 4 91  ? -36.062 -16.063 -54.996 1.000 132.998 ? 91  THR FFF C   1 
ATOM   8082  O O   . THR F 4 91  ? -35.144 -16.884 -55.154 1.000 136.902 ? 91  THR FFF O   1 
ATOM   8083  C CB  . THR F 4 91  ? -35.793 -15.070 -57.248 1.000 138.542 ? 91  THR FFF CB  1 
ATOM   8084  O OG1 . THR F 4 91  ? -35.940 -13.880 -58.016 1.000 144.910 ? 91  THR FFF OG1 1 
ATOM   8085  C CG2 . THR F 4 91  ? -36.809 -16.069 -57.758 1.000 138.582 ? 91  THR FFF CG2 1 
ATOM   8086  N N   . ALA F 4 92  ? -37.130 -16.256 -54.217 1.000 130.551 ? 92  ALA FFF N   1 
ATOM   8087  C CA  . ALA F 4 92  ? -37.308 -17.424 -53.322 1.000 128.579 ? 92  ALA FFF CA  1 
ATOM   8088  C C   . ALA F 4 92  ? -38.742 -17.478 -52.792 1.000 126.789 ? 92  ALA FFF C   1 
ATOM   8089  O O   . ALA F 4 92  ? -39.535 -16.590 -53.141 1.000 128.235 ? 92  ALA FFF O   1 
ATOM   8090  C CB  . ALA F 4 92  ? -36.323 -17.341 -52.185 1.000 127.833 ? 92  ALA FFF CB  1 
ATOM   8091  N N   . VAL F 4 93  ? -39.046 -18.498 -51.988 1.000 124.599 ? 93  VAL FFF N   1 
ATOM   8092  C CA  . VAL F 4 93  ? -40.263 -18.562 -51.132 1.000 125.368 ? 93  VAL FFF CA  1 
ATOM   8093  C C   . VAL F 4 93  ? -39.860 -18.170 -49.710 1.000 125.481 ? 93  VAL FFF C   1 
ATOM   8094  O O   . VAL F 4 93  ? -39.050 -18.897 -49.104 1.000 126.930 ? 93  VAL FFF O   1 
ATOM   8095  C CB  . VAL F 4 93  ? -40.910 -19.955 -51.149 1.000 127.090 ? 93  VAL FFF CB  1 
ATOM   8096  C CG1 . VAL F 4 93  ? -42.114 -20.009 -50.215 1.000 130.251 ? 93  VAL FFF CG1 1 
ATOM   8097  C CG2 . VAL F 4 93  ? -41.297 -20.367 -52.558 1.000 128.476 ? 93  VAL FFF CG2 1 
ATOM   8098  N N   . TYR F 4 94  ? -40.428 -17.077 -49.201 1.000 125.588 ? 94  TYR FFF N   1 
ATOM   8099  C CA  . TYR F 4 94  ? -40.138 -16.513 -47.859 1.000 123.978 ? 94  TYR FFF CA  1 
ATOM   8100  C C   . TYR F 4 94  ? -41.137 -17.099 -46.856 1.000 123.797 ? 94  TYR FFF C   1 
ATOM   8101  O O   . TYR F 4 94  ? -42.364 -16.927 -47.027 1.000 123.533 ? 94  TYR FFF O   1 
ATOM   8102  C CB  . TYR F 4 94  ? -40.116 -14.984 -47.933 1.000 124.823 ? 94  TYR FFF CB  1 
ATOM   8103  C CG  . TYR F 4 94  ? -38.875 -14.467 -48.611 1.000 124.664 ? 94  TYR FFF CG  1 
ATOM   8104  C CD1 . TYR F 4 94  ? -38.706 -14.610 -49.977 1.000 126.008 ? 94  TYR FFF CD1 1 
ATOM   8105  C CD2 . TYR F 4 94  ? -37.843 -13.895 -47.887 1.000 124.529 ? 94  TYR FFF CD2 1 
ATOM   8106  C CE1 . TYR F 4 94  ? -37.559 -14.169 -50.616 1.000 127.023 ? 94  TYR FFF CE1 1 
ATOM   8107  C CE2 . TYR F 4 94  ? -36.689 -13.447 -48.509 1.000 126.375 ? 94  TYR FFF CE2 1 
ATOM   8108  C CZ  . TYR F 4 94  ? -36.542 -13.590 -49.879 1.000 127.243 ? 94  TYR FFF CZ  1 
ATOM   8109  O OH  . TYR F 4 94  ? -35.406 -13.161 -50.508 1.000 127.075 ? 94  TYR FFF OH  1 
ATOM   8110  N N   . TYR F 4 95  ? -40.600 -17.799 -45.854 1.000 123.673 ? 95  TYR FFF N   1 
ATOM   8111  C CA  . TYR F 4 95  ? -41.336 -18.432 -44.732 1.000 125.216 ? 95  TYR FFF CA  1 
ATOM   8112  C C   . TYR F 4 95  ? -41.062 -17.675 -43.429 1.000 123.699 ? 95  TYR FFF C   1 
ATOM   8113  O O   . TYR F 4 95  ? -39.886 -17.587 -43.023 1.000 120.839 ? 95  TYR FFF O   1 
ATOM   8114  C CB  . TYR F 4 95  ? -40.879 -19.878 -44.533 1.000 127.356 ? 95  TYR FFF CB  1 
ATOM   8115  C CG  . TYR F 4 95  ? -41.082 -20.805 -45.704 1.000 129.042 ? 95  TYR FFF CG  1 
ATOM   8116  C CD1 . TYR F 4 95  ? -42.267 -21.502 -45.870 1.000 129.990 ? 95  TYR FFF CD1 1 
ATOM   8117  C CD2 . TYR F 4 95  ? -40.065 -21.027 -46.617 1.000 130.064 ? 95  TYR FFF CD2 1 
ATOM   8118  C CE1 . TYR F 4 95  ? -42.447 -22.377 -46.928 1.000 130.585 ? 95  TYR FFF CE1 1 
ATOM   8119  C CE2 . TYR F 4 95  ? -40.226 -21.901 -47.680 1.000 130.564 ? 95  TYR FFF CE2 1 
ATOM   8120  C CZ  . TYR F 4 95  ? -41.420 -22.582 -47.833 1.000 130.611 ? 95  TYR FFF CZ  1 
ATOM   8121  O OH  . TYR F 4 95  ? -41.566 -23.433 -48.889 1.000 130.127 ? 95  TYR FFF OH  1 
ATOM   8122  N N   . CYS F 4 96  ? -42.112 -17.157 -42.789 1.000 124.991 ? 96  CYS FFF N   1 
ATOM   8123  C CA  . CYS F 4 96  ? -42.056 -16.641 -41.397 1.000 126.146 ? 96  CYS FFF CA  1 
ATOM   8124  C C   . CYS F 4 96  ? -42.230 -17.822 -40.439 1.000 125.470 ? 96  CYS FFF C   1 
ATOM   8125  O O   . CYS F 4 96  ? -42.969 -18.767 -40.775 1.000 123.552 ? 96  CYS FFF O   1 
ATOM   8126  C CB  . CYS F 4 96  ? -43.094 -15.557 -41.124 1.000 128.157 ? 96  CYS FFF CB  1 
ATOM   8127  S SG  . CYS F 4 96  ? -44.717 -16.217 -40.675 1.000 130.909 ? 96  CYS FFF SG  1 
ATOM   8128  N N   . ALA F 4 97  ? -41.550 -17.751 -39.297 1.000 126.845 ? 97  ALA FFF N   1 
ATOM   8129  C CA  . ALA F 4 97  ? -41.467 -18.805 -38.265 1.000 129.818 ? 97  ALA FFF CA  1 
ATOM   8130  C C   . ALA F 4 97  ? -41.567 -18.155 -36.881 1.000 130.264 ? 97  ALA FFF C   1 
ATOM   8131  O O   . ALA F 4 97  ? -41.082 -17.015 -36.718 1.000 130.353 ? 97  ALA FFF O   1 
ATOM   8132  C CB  . ALA F 4 97  ? -40.174 -19.565 -38.434 1.000 130.952 ? 97  ALA FFF CB  1 
ATOM   8133  N N   . ARG F 4 98  ? -42.182 -18.857 -35.928 1.000 130.757 ? 98  ARG FFF N   1 
ATOM   8134  C CA  . ARG F 4 98  ? -42.404 -18.381 -34.540 1.000 132.079 ? 98  ARG FFF CA  1 
ATOM   8135  C C   . ARG F 4 98  ? -41.821 -19.408 -33.568 1.000 132.604 ? 98  ARG FFF C   1 
ATOM   8136  O O   . ARG F 4 98  ? -42.029 -20.615 -33.814 1.000 137.902 ? 98  ARG FFF O   1 
ATOM   8137  C CB  . ARG F 4 98  ? -43.902 -18.196 -34.289 1.000 135.594 ? 98  ARG FFF CB  1 
ATOM   8138  C CG  . ARG F 4 98  ? -44.251 -17.772 -32.869 1.000 138.139 ? 98  ARG FFF CG  1 
ATOM   8139  C CD  . ARG F 4 98  ? -45.714 -17.397 -32.731 1.000 141.450 ? 98  ARG FFF CD  1 
ATOM   8140  N NE  . ARG F 4 98  ? -46.116 -17.129 -31.355 1.000 143.250 ? 98  ARG FFF NE  1 
ATOM   8141  C CZ  . ARG F 4 98  ? -46.401 -18.057 -30.438 1.000 146.108 ? 98  ARG FFF CZ  1 
ATOM   8142  N NH1 . ARG F 4 98  ? -46.330 -19.350 -30.728 1.000 148.492 ? 98  ARG FFF NH1 1 
ATOM   8143  N NH2 . ARG F 4 98  ? -46.762 -17.684 -29.224 1.000 146.951 ? 98  ARG FFF NH2 1 
ATOM   8144  N N   . THR F 4 99  ? -41.126 -18.950 -32.518 1.000 129.295 ? 99  THR FFF N   1 
ATOM   8145  C CA  . THR F 4 99  ? -40.622 -19.802 -31.405 1.000 127.534 ? 99  THR FFF CA  1 
ATOM   8146  C C   . THR F 4 99  ? -41.066 -19.189 -30.078 1.000 126.050 ? 99  THR FFF C   1 
ATOM   8147  O O   . THR F 4 99  ? -41.074 -17.959 -29.974 1.000 122.204 ? 99  THR FFF O   1 
ATOM   8148  C CB  . THR F 4 99  ? -39.102 -20.012 -31.479 1.000 126.074 ? 99  THR FFF CB  1 
ATOM   8149  O OG1 . THR F 4 99  ? -38.758 -20.919 -30.429 1.000 126.377 ? 99  THR FFF OG1 1 
ATOM   8150  C CG2 . THR F 4 99  ? -38.300 -18.731 -31.371 1.000 124.410 ? 99  THR FFF CG2 1 
ATOM   8151  N N   . GLU F 4 100 ? -41.437 -20.032 -29.117 1.000 129.500 ? 100 GLU FFF N   1 
ATOM   8152  C CA  . GLU F 4 100 ? -41.803 -19.614 -27.741 1.000 133.286 ? 100 GLU FFF CA  1 
ATOM   8153  C C   . GLU F 4 100 ? -40.552 -19.643 -26.849 1.000 131.822 ? 100 GLU FFF C   1 
ATOM   8154  O O   . GLU F 4 100 ? -40.650 -19.212 -25.697 1.000 131.583 ? 100 GLU FFF O   1 
ATOM   8155  C CB  . GLU F 4 100 ? -42.924 -20.511 -27.205 1.000 139.300 ? 100 GLU FFF CB  1 
ATOM   8156  C CG  . GLU F 4 100 ? -44.231 -20.384 -27.980 1.000 142.825 ? 100 GLU FFF CG  1 
ATOM   8157  C CD  . GLU F 4 100 ? -45.458 -21.039 -27.354 1.000 149.335 ? 100 GLU FFF CD  1 
ATOM   8158  O OE1 . GLU F 4 100 ? -45.356 -21.542 -26.209 1.000 152.141 ? 100 GLU FFF OE1 1 
ATOM   8159  O OE2 . GLU F 4 100 ? -46.532 -21.036 -28.006 1.000 153.258 ? 100 GLU FFF OE2 1 
ATOM   8160  N N   . ASN F 4 101 ? -39.418 -20.119 -27.373 1.000 131.467 ? 101 ASN FFF N   1 
ATOM   8161  C CA  . ASN F 4 101 ? -38.143 -20.308 -26.625 1.000 130.818 ? 101 ASN FFF CA  1 
ATOM   8162  C C   . ASN F 4 101 ? -37.435 -18.954 -26.496 1.000 128.633 ? 101 ASN FFF C   1 
ATOM   8163  O O   . ASN F 4 101 ? -36.928 -18.456 -27.504 1.000 126.266 ? 101 ASN FFF O   1 
ATOM   8164  C CB  . ASN F 4 101 ? -37.253 -21.359 -27.302 1.000 130.671 ? 101 ASN FFF CB  1 
ATOM   8165  C CG  . ASN F 4 101 ? -36.005 -21.717 -26.523 1.000 131.007 ? 101 ASN FFF CG  1 
ATOM   8166  O OD1 . ASN F 4 101 ? -35.676 -21.081 -25.526 1.000 131.161 ? 101 ASN FFF OD1 1 
ATOM   8167  N ND2 . ASN F 4 101 ? -35.301 -22.743 -26.974 1.000 131.933 ? 101 ASN FFF ND2 1 
ATOM   8168  N N   . VAL F 4 102 ? -37.399 -18.393 -25.290 1.000 131.648 ? 102 VAL FFF N   1 
ATOM   8169  C CA  . VAL F 4 102 ? -36.663 -17.135 -24.965 1.000 134.343 ? 102 VAL FFF CA  1 
ATOM   8170  C C   . VAL F 4 102 ? -35.181 -17.464 -24.787 1.000 135.688 ? 102 VAL FFF C   1 
ATOM   8171  O O   . VAL F 4 102 ? -34.863 -18.212 -23.849 1.000 140.606 ? 102 VAL FFF O   1 
ATOM   8172  C CB  . VAL F 4 102 ? -37.200 -16.479 -23.684 1.000 139.152 ? 102 VAL FFF CB  1 
ATOM   8173  C CG1 . VAL F 4 102 ? -36.393 -15.243 -23.315 1.000 140.172 ? 102 VAL FFF CG1 1 
ATOM   8174  C CG2 . VAL F 4 102 ? -38.681 -16.158 -23.791 1.000 141.674 ? 102 VAL FFF CG2 1 
ATOM   8175  N N   . ARG F 4 103 ? -34.312 -16.883 -25.616 1.000 133.917 ? 103 ARG FFF N   1 
ATOM   8176  C CA  . ARG F 4 103 ? -32.849 -17.143 -25.602 1.000 134.175 ? 103 ARG FFF CA  1 
ATOM   8177  C C   . ARG F 4 103 ? -32.120 -15.827 -25.339 1.000 133.044 ? 103 ARG FFF C   1 
ATOM   8178  O O   . ARG F 4 103 ? -32.339 -14.883 -26.106 1.000 132.167 ? 103 ARG FFF O   1 
ATOM   8179  C CB  . ARG F 4 103 ? -32.444 -17.781 -26.931 1.000 133.726 ? 103 ARG FFF CB  1 
ATOM   8180  C CG  . ARG F 4 103 ? -33.186 -19.078 -27.232 1.000 135.032 ? 103 ARG FFF CG  1 
ATOM   8181  C CD  . ARG F 4 103 ? -32.674 -20.224 -26.384 1.000 137.973 ? 103 ARG FFF CD  1 
ATOM   8182  N NE  . ARG F 4 103 ? -31.239 -20.355 -26.584 1.000 139.256 ? 103 ARG FFF NE  1 
ATOM   8183  C CZ  . ARG F 4 103 ? -30.361 -20.721 -25.659 1.000 142.625 ? 103 ARG FFF CZ  1 
ATOM   8184  N NH1 . ARG F 4 103 ? -30.749 -21.005 -24.427 1.000 144.028 ? 103 ARG FFF NH1 1 
ATOM   8185  N NH2 . ARG F 4 103 ? -29.082 -20.795 -25.975 1.000 145.973 ? 103 ARG FFF NH2 1 
ATOM   8186  N N   . SER F 4 104 ? -31.315 -15.765 -24.277 1.000 134.655 ? 104 SER FFF N   1 
ATOM   8187  C CA  . SER F 4 104 ? -30.595 -14.541 -23.833 1.000 136.411 ? 104 SER FFF CA  1 
ATOM   8188  C C   . SER F 4 104 ? -29.729 -14.007 -24.978 1.000 134.602 ? 104 SER FFF C   1 
ATOM   8189  O O   . SER F 4 104 ? -29.914 -12.841 -25.377 1.000 132.248 ? 104 SER FFF O   1 
ATOM   8190  C CB  . SER F 4 104 ? -29.762 -14.805 -22.609 1.000 140.408 ? 104 SER FFF CB  1 
ATOM   8191  O OG  . SER F 4 104 ? -28.804 -13.772 -22.427 1.000 143.431 ? 104 SER FFF OG  1 
ATOM   8192  N N   . LEU F 4 105 ? -28.805 -14.837 -25.458 1.000 135.260 ? 105 LEU FFF N   1 
ATOM   8193  C CA  . LEU F 4 105 ? -27.993 -14.560 -26.667 1.000 136.537 ? 105 LEU FFF CA  1 
ATOM   8194  C C   . LEU F 4 105 ? -28.951 -14.434 -27.856 1.000 133.761 ? 105 LEU FFF C   1 
ATOM   8195  O O   . LEU F 4 105 ? -29.652 -15.428 -28.126 1.000 136.458 ? 105 LEU FFF O   1 
ATOM   8196  C CB  . LEU F 4 105 ? -27.012 -15.715 -26.874 1.000 140.570 ? 105 LEU FFF CB  1 
ATOM   8197  C CG  . LEU F 4 105 ? -26.059 -15.538 -28.055 1.000 146.107 ? 105 LEU FFF CG  1 
ATOM   8198  C CD1 . LEU F 4 105 ? -25.079 -14.404 -27.793 1.000 149.073 ? 105 LEU FFF CD1 1 
ATOM   8199  C CD2 . LEU F 4 105 ? -25.325 -16.835 -28.367 1.000 150.345 ? 105 LEU FFF CD2 1 
ATOM   8200  N N   . LEU F 4 106 ? -29.006 -13.269 -28.517 1.000 130.501 ? 106 LEU FFF N   1 
ATOM   8201  C CA  . LEU F 4 106 ? -29.921 -13.016 -29.670 1.000 125.362 ? 106 LEU FFF CA  1 
ATOM   8202  C C   . LEU F 4 106 ? -29.491 -13.860 -30.879 1.000 121.829 ? 106 LEU FFF C   1 
ATOM   8203  O O   . LEU F 4 106 ? -30.366 -14.489 -31.510 1.000 115.406 ? 106 LEU FFF O   1 
ATOM   8204  C CB  . LEU F 4 106 ? -29.921 -11.520 -30.008 1.000 126.394 ? 106 LEU FFF CB  1 
ATOM   8205  C CG  . LEU F 4 106 ? -30.737 -11.113 -31.236 1.000 125.017 ? 106 LEU FFF CG  1 
ATOM   8206  C CD1 . LEU F 4 106 ? -32.124 -11.732 -31.212 1.000 122.495 ? 106 LEU FFF CD1 1 
ATOM   8207  C CD2 . LEU F 4 106 ? -30.834 -9.602  -31.338 1.000 126.612 ? 106 LEU FFF CD2 1 
ATOM   8208  N N   . SER F 4 107 ? -28.185 -13.892 -31.162 1.000 123.928 ? 107 SER FFF N   1 
ATOM   8209  C CA  . SER F 4 107 ? -27.572 -14.521 -32.363 1.000 125.168 ? 107 SER FFF CA  1 
ATOM   8210  C C   . SER F 4 107 ? -28.033 -15.978 -32.498 1.000 125.119 ? 107 SER FFF C   1 
ATOM   8211  O O   . SER F 4 107 ? -28.008 -16.498 -33.627 1.000 128.212 ? 107 SER FFF O   1 
ATOM   8212  C CB  . SER F 4 107 ? -26.062 -14.405 -32.337 1.000 127.680 ? 107 SER FFF CB  1 
ATOM   8213  O OG  . SER F 4 107 ? -25.493 -15.239 -31.337 1.000 128.036 ? 107 SER FFF OG  1 
ATOM   8214  N N   . ASP F 4 108 ? -28.467 -16.598 -31.401 1.000 125.526 ? 108 ASP FFF N   1 
ATOM   8215  C CA  . ASP F 4 108 ? -29.002 -17.986 -31.355 1.000 127.678 ? 108 ASP FFF CA  1 
ATOM   8216  C C   . ASP F 4 108 ? -30.156 -18.206 -32.336 1.000 124.579 ? 108 ASP FFF C   1 
ATOM   8217  O O   . ASP F 4 108 ? -30.406 -19.369 -32.676 1.000 127.108 ? 108 ASP FFF O   1 
ATOM   8218  C CB  . ASP F 4 108 ? -29.546 -18.341 -29.971 1.000 131.225 ? 108 ASP FFF CB  1 
ATOM   8219  C CG  . ASP F 4 108 ? -28.510 -18.942 -29.042 1.000 137.212 ? 108 ASP FFF CG  1 
ATOM   8220  O OD1 . ASP F 4 108 ? -27.388 -19.234 -29.515 1.000 141.500 ? 108 ASP FFF OD1 1 
ATOM   8221  O OD2 . ASP F 4 108 ? -28.835 -19.115 -27.853 1.000 141.778 ? 108 ASP FFF OD2 1 
ATOM   8222  N N   . TYR F 4 109 ? -30.871 -17.162 -32.744 1.000 121.069 ? 109 TYR FFF N   1 
ATOM   8223  C CA  . TYR F 4 109 ? -32.133 -17.319 -33.510 1.000 119.918 ? 109 TYR FFF CA  1 
ATOM   8224  C C   . TYR F 4 109 ? -31.855 -17.588 -34.999 1.000 120.686 ? 109 TYR FFF C   1 
ATOM   8225  O O   . TYR F 4 109 ? -32.803 -17.545 -35.804 1.000 120.339 ? 109 TYR FFF O   1 
ATOM   8226  C CB  . TYR F 4 109 ? -33.042 -16.122 -33.246 1.000 119.055 ? 109 TYR FFF CB  1 
ATOM   8227  C CG  . TYR F 4 109 ? -33.751 -16.178 -31.917 1.000 119.264 ? 109 TYR FFF CG  1 
ATOM   8228  C CD1 . TYR F 4 109 ? -34.492 -17.289 -31.543 1.000 118.853 ? 109 TYR FFF CD1 1 
ATOM   8229  C CD2 . TYR F 4 109 ? -33.705 -15.108 -31.041 1.000 120.153 ? 109 TYR FFF CD2 1 
ATOM   8230  C CE1 . TYR F 4 109 ? -35.161 -17.337 -30.331 1.000 119.849 ? 109 TYR FFF CE1 1 
ATOM   8231  C CE2 . TYR F 4 109 ? -34.371 -15.138 -29.828 1.000 120.899 ? 109 TYR FFF CE2 1 
ATOM   8232  C CZ  . TYR F 4 109 ? -35.097 -16.258 -29.467 1.000 120.860 ? 109 TYR FFF CZ  1 
ATOM   8233  O OH  . TYR F 4 109 ? -35.735 -16.282 -28.259 1.000 122.848 ? 109 TYR FFF OH  1 
ATOM   8234  N N   . ALA F 4 110 ? -30.612 -17.911 -35.359 1.000 123.347 ? 110 ALA FFF N   1 
ATOM   8235  C CA  . ALA F 4 110 ? -30.272 -18.601 -36.622 1.000 125.670 ? 110 ALA FFF CA  1 
ATOM   8236  C C   . ALA F 4 110 ? -30.126 -20.102 -36.342 1.000 131.177 ? 110 ALA FFF C   1 
ATOM   8237  O O   . ALA F 4 110 ? -30.972 -20.876 -36.834 1.000 130.219 ? 110 ALA FFF O   1 
ATOM   8238  C CB  . ALA F 4 110 ? -29.027 -17.995 -37.210 1.000 126.436 ? 110 ALA FFF CB  1 
ATOM   8239  N N   . THR F 4 111 ? -29.122 -20.474 -35.535 1.000 139.739 ? 111 THR FFF N   1 
ATOM   8240  C CA  . THR F 4 111 ? -28.812 -21.864 -35.083 1.000 146.949 ? 111 THR FFF CA  1 
ATOM   8241  C C   . THR F 4 111 ? -30.104 -22.612 -34.741 1.000 148.373 ? 111 THR FFF C   1 
ATOM   8242  O O   . THR F 4 111 ? -30.298 -23.716 -35.288 1.000 153.791 ? 111 THR FFF O   1 
ATOM   8243  C CB  . THR F 4 111 ? -27.893 -21.871 -33.847 1.000 152.024 ? 111 THR FFF CB  1 
ATOM   8244  O OG1 . THR F 4 111 ? -26.590 -21.448 -34.252 1.000 156.653 ? 111 THR FFF OG1 1 
ATOM   8245  C CG2 . THR F 4 111 ? -27.792 -23.218 -33.155 1.000 154.021 ? 111 THR FFF CG2 1 
ATOM   8246  N N   . TRP F 4 112 ? -30.938 -22.019 -33.875 1.000 146.725 ? 112 TRP FFF N   1 
ATOM   8247  C CA  . TRP F 4 112 ? -32.016 -22.710 -33.116 1.000 145.629 ? 112 TRP FFF CA  1 
ATOM   8248  C C   . TRP F 4 112 ? -33.242 -22.937 -33.988 1.000 143.464 ? 112 TRP FFF C   1 
ATOM   8249  O O   . TRP F 4 112 ? -33.435 -22.251 -34.993 1.000 144.540 ? 112 TRP FFF O   1 
ATOM   8250  C CB  . TRP F 4 112 ? -32.368 -21.940 -31.839 1.000 145.865 ? 112 TRP FFF CB  1 
ATOM   8251  C CG  . TRP F 4 112 ? -31.428 -22.255 -30.719 1.000 150.925 ? 112 TRP FFF CG  1 
ATOM   8252  C CD1 . TRP F 4 112 ? -30.106 -21.927 -30.655 1.000 153.129 ? 112 TRP FFF CD1 1 
ATOM   8253  C CD2 . TRP F 4 112 ? -31.713 -23.009 -29.524 1.000 155.566 ? 112 TRP FFF CD2 1 
ATOM   8254  N NE1 . TRP F 4 112 ? -29.553 -22.396 -29.495 1.000 155.460 ? 112 TRP FFF NE1 1 
ATOM   8255  C CE2 . TRP F 4 112 ? -30.513 -23.064 -28.780 1.000 157.372 ? 112 TRP FFF CE2 1 
ATOM   8256  C CE3 . TRP F 4 112 ? -32.858 -23.626 -29.000 1.000 157.220 ? 112 TRP FFF CE3 1 
ATOM   8257  C CZ2 . TRP F 4 112 ? -30.430 -23.714 -27.548 1.000 159.972 ? 112 TRP FFF CZ2 1 
ATOM   8258  C CZ3 . TRP F 4 112 ? -32.772 -24.272 -27.784 1.000 159.906 ? 112 TRP FFF CZ3 1 
ATOM   8259  C CH2 . TRP F 4 112 ? -31.574 -24.313 -27.068 1.000 160.707 ? 112 TRP FFF CH2 1 
ATOM   8260  N N   . PRO F 4 113 ? -34.108 -23.904 -33.600 1.000 141.131 ? 113 PRO FFF N   1 
ATOM   8261  C CA  . PRO F 4 113 ? -35.226 -24.338 -34.427 1.000 138.204 ? 113 PRO FFF CA  1 
ATOM   8262  C C   . PRO F 4 113 ? -36.480 -23.551 -34.034 1.000 134.012 ? 113 PRO FFF C   1 
ATOM   8263  O O   . PRO F 4 113 ? -36.497 -22.980 -32.963 1.000 133.844 ? 113 PRO FFF O   1 
ATOM   8264  C CB  . PRO F 4 113 ? -35.312 -25.807 -34.008 1.000 141.002 ? 113 PRO FFF CB  1 
ATOM   8265  C CG  . PRO F 4 113 ? -35.103 -25.740 -32.509 1.000 142.621 ? 113 PRO FFF CG  1 
ATOM   8266  C CD  . PRO F 4 113 ? -34.111 -24.611 -32.309 1.000 142.150 ? 113 PRO FFF CD  1 
ATOM   8267  N N   . TYR F 4 114 ? -37.492 -23.561 -34.896 1.000 131.411 ? 114 TYR FFF N   1 
ATOM   8268  C CA  . TYR F 4 114 ? -38.776 -22.843 -34.696 1.000 129.986 ? 114 TYR FFF CA  1 
ATOM   8269  C C   . TYR F 4 114 ? -39.916 -23.871 -34.651 1.000 133.423 ? 114 TYR FFF C   1 
ATOM   8270  O O   . TYR F 4 114 ? -39.919 -24.815 -35.455 1.000 137.173 ? 114 TYR FFF O   1 
ATOM   8271  C CB  . TYR F 4 114 ? -38.938 -21.774 -35.779 1.000 124.644 ? 114 TYR FFF CB  1 
ATOM   8272  C CG  . TYR F 4 114 ? -37.988 -20.611 -35.646 1.000 118.916 ? 114 TYR FFF CG  1 
ATOM   8273  C CD1 . TYR F 4 114 ? -36.640 -20.754 -35.922 1.000 117.820 ? 114 TYR FFF CD1 1 
ATOM   8274  C CD2 . TYR F 4 114 ? -38.436 -19.366 -35.247 1.000 115.654 ? 114 TYR FFF CD2 1 
ATOM   8275  C CE1 . TYR F 4 114 ? -35.764 -19.690 -35.810 1.000 116.814 ? 114 TYR FFF CE1 1 
ATOM   8276  C CE2 . TYR F 4 114 ? -37.575 -18.292 -35.123 1.000 114.672 ? 114 TYR FFF CE2 1 
ATOM   8277  C CZ  . TYR F 4 114 ? -36.233 -18.455 -35.406 1.000 115.296 ? 114 TYR FFF CZ  1 
ATOM   8278  O OH  . TYR F 4 114 ? -35.377 -17.401 -35.299 1.000 116.262 ? 114 TYR FFF OH  1 
ATOM   8279  N N   . ASP F 4 115 ? -40.854 -23.693 -33.720 1.000 135.250 ? 115 ASP FFF N   1 
ATOM   8280  C CA  . ASP F 4 115 ? -41.925 -24.677 -33.410 1.000 138.577 ? 115 ASP FFF CA  1 
ATOM   8281  C C   . ASP F 4 115 ? -43.050 -24.560 -34.455 1.000 137.633 ? 115 ASP FFF C   1 
ATOM   8282  O O   . ASP F 4 115 ? -43.597 -25.611 -34.833 1.000 140.115 ? 115 ASP FFF O   1 
ATOM   8283  C CB  . ASP F 4 115 ? -42.392 -24.518 -31.955 1.000 142.174 ? 115 ASP FFF CB  1 
ATOM   8284  C CG  . ASP F 4 115 ? -41.396 -25.012 -30.900 1.000 143.088 ? 115 ASP FFF CG  1 
ATOM   8285  O OD1 . ASP F 4 115 ? -41.139 -26.241 -30.849 1.000 144.016 ? 115 ASP FFF OD1 1 
ATOM   8286  O OD2 . ASP F 4 115 ? -40.893 -24.168 -30.112 1.000 141.870 ? 115 ASP FFF OD2 1 
ATOM   8287  N N   . TYR F 4 116 ? -43.370 -23.346 -34.921 1.000 135.321 ? 116 TYR FFF N   1 
ATOM   8288  C CA  . TYR F 4 116 ? -44.502 -23.055 -35.845 1.000 137.870 ? 116 TYR FFF CA  1 
ATOM   8289  C C   . TYR F 4 116 ? -43.981 -22.407 -37.137 1.000 135.842 ? 116 TYR FFF C   1 
ATOM   8290  O O   . TYR F 4 116 ? -43.094 -21.544 -37.046 1.000 134.107 ? 116 TYR FFF O   1 
ATOM   8291  C CB  . TYR F 4 116 ? -45.525 -22.145 -35.157 1.000 140.620 ? 116 TYR FFF CB  1 
ATOM   8292  C CG  . TYR F 4 116 ? -45.874 -22.524 -33.737 1.000 144.806 ? 116 TYR FFF CG  1 
ATOM   8293  C CD1 . TYR F 4 116 ? -45.088 -22.113 -32.670 1.000 144.331 ? 116 TYR FFF CD1 1 
ATOM   8294  C CD2 . TYR F 4 116 ? -46.999 -23.284 -33.450 1.000 150.334 ? 116 TYR FFF CD2 1 
ATOM   8295  C CE1 . TYR F 4 116 ? -45.402 -22.450 -31.361 1.000 147.863 ? 116 TYR FFF CE1 1 
ATOM   8296  C CE2 . TYR F 4 116 ? -47.333 -23.627 -32.148 1.000 152.964 ? 116 TYR FFF CE2 1 
ATOM   8297  C CZ  . TYR F 4 116 ? -46.532 -23.209 -31.096 1.000 152.173 ? 116 TYR FFF CZ  1 
ATOM   8298  O OH  . TYR F 4 116 ? -46.855 -23.555 -29.811 1.000 155.181 ? 116 TYR FFF OH  1 
ATOM   8299  N N   . TRP F 4 117 ? -44.528 -22.799 -38.296 1.000 136.563 ? 117 TRP FFF N   1 
ATOM   8300  C CA  . TRP F 4 117 ? -44.136 -22.297 -39.643 1.000 133.976 ? 117 TRP FFF CA  1 
ATOM   8301  C C   . TRP F 4 117 ? -45.377 -21.897 -40.446 1.000 135.220 ? 117 TRP FFF C   1 
ATOM   8302  O O   . TRP F 4 117 ? -46.409 -22.588 -40.326 1.000 137.140 ? 117 TRP FFF O   1 
ATOM   8303  C CB  . TRP F 4 117 ? -43.319 -23.349 -40.401 1.000 133.891 ? 117 TRP FFF CB  1 
ATOM   8304  C CG  . TRP F 4 117 ? -41.957 -23.576 -39.827 1.000 132.675 ? 117 TRP FFF CG  1 
ATOM   8305  C CD1 . TRP F 4 117 ? -41.646 -24.367 -38.761 1.000 133.911 ? 117 TRP FFF CD1 1 
ATOM   8306  C CD2 . TRP F 4 117 ? -40.717 -23.006 -40.282 1.000 131.255 ? 117 TRP FFF CD2 1 
ATOM   8307  N NE1 . TRP F 4 117 ? -40.299 -24.332 -38.526 1.000 133.465 ? 117 TRP FFF NE1 1 
ATOM   8308  C CE2 . TRP F 4 117 ? -39.702 -23.506 -39.440 1.000 131.280 ? 117 TRP FFF CE2 1 
ATOM   8309  C CE3 . TRP F 4 117 ? -40.361 -22.133 -41.318 1.000 130.715 ? 117 TRP FFF CE3 1 
ATOM   8310  C CZ2 . TRP F 4 117 ? -38.361 -23.158 -39.599 1.000 130.818 ? 117 TRP FFF CZ2 1 
ATOM   8311  C CZ3 . TRP F 4 117 ? -39.036 -21.790 -41.477 1.000 129.891 ? 117 TRP FFF CZ3 1 
ATOM   8312  C CH2 . TRP F 4 117 ? -38.053 -22.295 -40.625 1.000 130.423 ? 117 TRP FFF CH2 1 
ATOM   8313  N N   . GLY F 4 118 ? -45.260 -20.834 -41.247 1.000 134.783 ? 118 GLY FFF N   1 
ATOM   8314  C CA  . GLY F 4 118 ? -46.284 -20.406 -42.220 1.000 138.302 ? 118 GLY FFF CA  1 
ATOM   8315  C C   . GLY F 4 118 ? -46.138 -21.158 -43.529 1.000 140.527 ? 118 GLY FFF C   1 
ATOM   8316  O O   . GLY F 4 118 ? -45.057 -21.746 -43.739 1.000 140.463 ? 118 GLY FFF O   1 
ATOM   8317  N N   . GLN F 4 119 ? -47.166 -21.138 -44.389 1.000 144.405 ? 119 GLN FFF N   1 
ATOM   8318  C CA  . GLN F 4 119 ? -47.160 -21.872 -45.686 1.000 145.553 ? 119 GLN FFF CA  1 
ATOM   8319  C C   . GLN F 4 119 ? -46.124 -21.229 -46.629 1.000 139.121 ? 119 GLN FFF C   1 
ATOM   8320  O O   . GLN F 4 119 ? -45.668 -21.922 -47.551 1.000 136.906 ? 119 GLN FFF O   1 
ATOM   8321  C CB  . GLN F 4 119 ? -48.581 -21.992 -46.261 1.000 152.941 ? 119 GLN FFF CB  1 
ATOM   8322  C CG  . GLN F 4 119 ? -49.206 -20.701 -46.788 1.000 157.759 ? 119 GLN FFF CG  1 
ATOM   8323  C CD  . GLN F 4 119 ? -50.436 -20.991 -47.621 1.000 165.566 ? 119 GLN FFF CD  1 
ATOM   8324  O OE1 . GLN F 4 119 ? -51.126 -21.987 -47.398 1.000 171.476 ? 119 GLN FFF OE1 1 
ATOM   8325  N NE2 . GLN F 4 119 ? -50.720 -20.134 -48.598 1.000 168.167 ? 119 GLN FFF NE2 1 
ATOM   8326  N N   . GLY F 4 120 ? -45.728 -19.977 -46.372 1.000 135.291 ? 120 GLY FFF N   1 
ATOM   8327  C CA  . GLY F 4 120 ? -44.692 -19.242 -47.128 1.000 131.303 ? 120 GLY FFF CA  1 
ATOM   8328  C C   . GLY F 4 120 ? -45.314 -18.418 -48.243 1.000 130.060 ? 120 GLY FFF C   1 
ATOM   8329  O O   . GLY F 4 120 ? -46.531 -18.572 -48.463 1.000 131.333 ? 120 GLY FFF O   1 
ATOM   8330  N N   . THR F 4 121 ? -44.531 -17.571 -48.922 1.000 126.086 ? 121 THR FFF N   1 
ATOM   8331  C CA  . THR F 4 121 ? -45.012 -16.729 -50.052 1.000 125.590 ? 121 THR FFF CA  1 
ATOM   8332  C C   . THR F 4 121 ? -43.873 -16.444 -51.036 1.000 122.330 ? 121 THR FFF C   1 
ATOM   8333  O O   . THR F 4 121 ? -42.729 -16.278 -50.582 1.000 120.240 ? 121 THR FFF O   1 
ATOM   8334  C CB  . THR F 4 121 ? -45.654 -15.446 -49.519 1.000 127.511 ? 121 THR FFF CB  1 
ATOM   8335  O OG1 . THR F 4 121 ? -46.719 -15.102 -50.404 1.000 132.536 ? 121 THR FFF OG1 1 
ATOM   8336  C CG2 . THR F 4 121 ? -44.690 -14.287 -49.411 1.000 127.541 ? 121 THR FFF CG2 1 
ATOM   8337  N N   . GLN F 4 122 ? -44.194 -16.355 -52.329 1.000 122.376 ? 122 GLN FFF N   1 
ATOM   8338  C CA  . GLN F 4 122 ? -43.199 -16.203 -53.420 1.000 123.844 ? 122 GLN FFF CA  1 
ATOM   8339  C C   . GLN F 4 122 ? -42.848 -14.719 -53.586 1.000 123.293 ? 122 GLN FFF C   1 
ATOM   8340  O O   . GLN F 4 122 ? -43.777 -13.896 -53.618 1.000 123.647 ? 122 GLN FFF O   1 
ATOM   8341  C CB  . GLN F 4 122 ? -43.747 -16.817 -54.710 1.000 127.240 ? 122 GLN FFF CB  1 
ATOM   8342  C CG  . GLN F 4 122 ? -42.756 -16.820 -55.872 1.000 129.473 ? 122 GLN FFF CG  1 
ATOM   8343  C CD  . GLN F 4 122 ? -41.604 -17.789 -55.713 1.000 129.569 ? 122 GLN FFF CD  1 
ATOM   8344  O OE1 . GLN F 4 122 ? -41.777 -18.948 -55.339 1.000 130.393 ? 122 GLN FFF OE1 1 
ATOM   8345  N NE2 . GLN F 4 122 ? -40.404 -17.336 -56.034 1.000 129.148 ? 122 GLN FFF NE2 1 
ATOM   8346  N N   . VAL F 4 123 ? -41.548 -14.410 -53.645 1.000 123.664 ? 123 VAL FFF N   1 
ATOM   8347  C CA  . VAL F 4 123 ? -40.970 -13.125 -54.143 1.000 126.291 ? 123 VAL FFF CA  1 
ATOM   8348  C C   . VAL F 4 123 ? -40.118 -13.446 -55.375 1.000 126.155 ? 123 VAL FFF C   1 
ATOM   8349  O O   . VAL F 4 123 ? -39.195 -14.268 -55.248 1.000 126.012 ? 123 VAL FFF O   1 
ATOM   8350  C CB  . VAL F 4 123 ? -40.116 -12.422 -53.070 1.000 128.123 ? 123 VAL FFF CB  1 
ATOM   8351  C CG1 . VAL F 4 123 ? -39.505 -11.123 -53.589 1.000 131.224 ? 123 VAL FFF CG1 1 
ATOM   8352  C CG2 . VAL F 4 123 ? -40.902 -12.173 -51.793 1.000 128.572 ? 123 VAL FFF CG2 1 
ATOM   8353  N N   . THR F 4 124 ? -40.408 -12.808 -56.510 1.000 126.341 ? 124 THR FFF N   1 
ATOM   8354  C CA  . THR F 4 124 ? -39.682 -12.982 -57.797 1.000 127.874 ? 124 THR FFF CA  1 
ATOM   8355  C C   . THR F 4 124 ? -39.136 -11.617 -58.246 1.000 130.433 ? 124 THR FFF C   1 
ATOM   8356  O O   . THR F 4 124 ? -39.961 -10.731 -58.528 1.000 135.846 ? 124 THR FFF O   1 
ATOM   8357  C CB  . THR F 4 124 ? -40.609 -13.629 -58.837 1.000 128.495 ? 124 THR FFF CB  1 
ATOM   8358  O OG1 . THR F 4 124 ? -41.700 -12.739 -59.061 1.000 132.157 ? 124 THR FFF OG1 1 
ATOM   8359  C CG2 . THR F 4 124 ? -41.181 -14.961 -58.408 1.000 127.522 ? 124 THR FFF CG2 1 
ATOM   8360  N N   . VAL F 4 125 ? -37.807 -11.450 -58.307 1.000 129.790 ? 125 VAL FFF N   1 
ATOM   8361  C CA  . VAL F 4 125 ? -37.118 -10.187 -58.732 1.000 131.679 ? 125 VAL FFF CA  1 
ATOM   8362  C C   . VAL F 4 125 ? -36.913 -10.224 -60.252 1.000 130.868 ? 125 VAL FFF C   1 
ATOM   8363  O O   . VAL F 4 125 ? -36.294 -11.186 -60.729 1.000 128.142 ? 125 VAL FFF O   1 
ATOM   8364  C CB  . VAL F 4 125 ? -35.769 -9.943  -58.019 1.000 134.682 ? 125 VAL FFF CB  1 
ATOM   8365  C CG1 . VAL F 4 125 ? -35.831 -8.790  -57.036 1.000 136.307 ? 125 VAL FFF CG1 1 
ATOM   8366  C CG2 . VAL F 4 125 ? -35.214 -11.177 -57.335 1.000 134.201 ? 125 VAL FFF CG2 1 
ATOM   8367  N N   . SER F 4 126 ? -37.357 -9.177  -60.960 1.000 132.986 ? 126 SER FFF N   1 
ATOM   8368  C CA  . SER F 4 126 ? -37.535 -9.135  -62.440 1.000 135.937 ? 126 SER FFF CA  1 
ATOM   8369  C C   . SER F 4 126 ? -36.722 -7.995  -63.089 1.000 138.089 ? 126 SER FFF C   1 
ATOM   8370  O O   . SER F 4 126 ? -35.620 -7.704  -62.587 1.000 139.538 ? 126 SER FFF O   1 
ATOM   8371  C CB  . SER F 4 126 ? -39.003 -9.016  -62.758 1.000 138.243 ? 126 SER FFF CB  1 
ATOM   8372  O OG  . SER F 4 126 ? -39.451 -7.678  -62.573 1.000 141.354 ? 126 SER FFF OG  1 
ATOM   8373  N N   . SER F 4 127 ? -37.226 -7.409  -64.193 1.000 138.463 ? 127 SER FFF N   1 
ATOM   8374  C CA  . SER F 4 127 ? -36.659 -6.233  -64.914 1.000 139.155 ? 127 SER FFF CA  1 
ATOM   8375  C C   . SER F 4 127 ? -37.786 -5.396  -65.546 1.000 139.529 ? 127 SER FFF C   1 
ATOM   8376  O O   . SER F 4 127 ? -37.854 -4.160  -65.545 1.000 136.624 ? 127 SER FFF O   1 
ATOM   8377  C CB  . SER F 4 127 ? -35.668 -6.688  -65.945 1.000 140.009 ? 127 SER FFF CB  1 
ATOM   8378  O OG  . SER F 4 127 ? -34.509 -7.214  -65.317 1.000 137.534 ? 127 SER FFF OG  1 
ATOM   8379  N N   . THR G 2 1   ? -44.946 -38.840 21.391  1.000 135.266 ? 0   THR HHH N   1 
ATOM   8380  C CA  . THR G 2 1   ? -44.126 -37.657 20.993  1.000 134.582 ? 0   THR HHH CA  1 
ATOM   8381  C C   . THR G 2 1   ? -43.974 -37.617 19.473  1.000 131.178 ? 0   THR HHH C   1 
ATOM   8382  O O   . THR G 2 1   ? -44.376 -38.595 18.820  1.000 129.050 ? 0   THR HHH O   1 
ATOM   8383  C CB  . THR G 2 1   ? -42.730 -37.653 21.633  1.000 133.721 ? 0   THR HHH CB  1 
ATOM   8384  O OG1 . THR G 2 1   ? -42.005 -36.537 21.102  1.000 133.853 ? 0   THR HHH OG1 1 
ATOM   8385  C CG2 . THR G 2 1   ? -41.955 -38.928 21.381  1.000 130.627 ? 0   THR HHH CG2 1 
ATOM   8386  N N   . GLN G 2 2   ? -43.390 -36.525 18.963  1.000 129.648 ? 1   GLN HHH N   1 
ATOM   8387  C CA  . GLN G 2 2   ? -43.224 -36.241 17.515  1.000 129.314 ? 1   GLN HHH CA  1 
ATOM   8388  C C   . GLN G 2 2   ? -42.158 -37.177 16.952  1.000 127.333 ? 1   GLN HHH C   1 
ATOM   8389  O O   . GLN G 2 2   ? -42.468 -37.906 15.977  1.000 129.373 ? 1   GLN HHH O   1 
ATOM   8390  C CB  . GLN G 2 2   ? -42.827 -34.780 17.284  1.000 129.652 ? 1   GLN HHH CB  1 
ATOM   8391  C CG  . GLN G 2 2   ? -42.625 -34.408 15.815  1.000 128.892 ? 1   GLN HHH CG  1 
ATOM   8392  C CD  . GLN G 2 2   ? -43.909 -34.138 15.067  1.000 132.223 ? 1   GLN HHH CD  1 
ATOM   8393  O OE1 . GLN G 2 2   ? -44.781 -33.406 15.540  1.000 134.641 ? 1   GLN HHH OE1 1 
ATOM   8394  N NE2 . GLN G 2 2   ? -44.022 -34.708 13.877  1.000 131.419 ? 1   GLN HHH NE2 1 
ATOM   8395  N N   . MET G 2 3   ? -40.960 -37.136 17.549  1.000 125.371 ? 2   MET HHH N   1 
ATOM   8396  C CA  . MET G 2 3   ? -39.718 -37.770 17.022  1.000 123.112 ? 2   MET HHH CA  1 
ATOM   8397  C C   . MET G 2 3   ? -38.906 -38.342 18.184  1.000 119.158 ? 2   MET HHH C   1 
ATOM   8398  O O   . MET G 2 3   ? -38.751 -37.625 19.174  1.000 122.472 ? 2   MET HHH O   1 
ATOM   8399  C CB  . MET G 2 3   ? -38.855 -36.740 16.283  1.000 123.025 ? 2   MET HHH CB  1 
ATOM   8400  C CG  . MET G 2 3   ? -37.683 -37.323 15.504  1.000 121.859 ? 2   MET HHH CG  1 
ATOM   8401  S SD  . MET G 2 3   ? -38.137 -38.678 14.379  1.000 127.159 ? 2   MET HHH SD  1 
ATOM   8402  C CE  . MET G 2 3   ? -39.589 -38.027 13.545  1.000 129.773 ? 2   MET HHH CE  1 
ATOM   8403  N N   . GLN G 2 4   ? -38.418 -39.577 18.044  1.000 114.208 ? 3   GLN HHH N   1 
ATOM   8404  C CA  . GLN G 2 4   ? -37.535 -40.277 19.017  1.000 111.814 ? 3   GLN HHH CA  1 
ATOM   8405  C C   . GLN G 2 4   ? -36.341 -40.824 18.238  1.000 110.354 ? 3   GLN HHH C   1 
ATOM   8406  O O   . GLN G 2 4   ? -36.561 -41.309 17.118  1.000 113.940 ? 3   GLN HHH O   1 
ATOM   8407  C CB  . GLN G 2 4   ? -38.311 -41.405 19.696  1.000 112.406 ? 3   GLN HHH CB  1 
ATOM   8408  C CG  . GLN G 2 4   ? -37.564 -42.120 20.811  1.000 110.551 ? 3   GLN HHH CG  1 
ATOM   8409  C CD  . GLN G 2 4   ? -38.339 -43.334 21.258  1.000 111.602 ? 3   GLN HHH CD  1 
ATOM   8410  O OE1 . GLN G 2 4   ? -39.496 -43.531 20.891  1.000 112.934 ? 3   GLN HHH OE1 1 
ATOM   8411  N NE2 . GLN G 2 4   ? -37.701 -44.164 22.064  1.000 111.002 ? 3   GLN HHH NE2 1 
ATOM   8412  N N   . LEU G 2 5   ? -35.129 -40.730 18.778  1.000 107.831 ? 4   LEU HHH N   1 
ATOM   8413  C CA  . LEU G 2 5   ? -33.919 -41.200 18.061  1.000 106.857 ? 4   LEU HHH CA  1 
ATOM   8414  C C   . LEU G 2 5   ? -33.372 -42.428 18.774  1.000 108.777 ? 4   LEU HHH C   1 
ATOM   8415  O O   . LEU G 2 5   ? -33.094 -42.345 19.992  1.000 111.752 ? 4   LEU HHH O   1 
ATOM   8416  C CB  . LEU G 2 5   ? -32.886 -40.077 17.989  1.000 105.823 ? 4   LEU HHH CB  1 
ATOM   8417  C CG  . LEU G 2 5   ? -33.374 -38.822 17.274  1.000 107.878 ? 4   LEU HHH CG  1 
ATOM   8418  C CD1 . LEU G 2 5   ? -32.273 -37.781 17.163  1.000 107.172 ? 4   LEU HHH CD1 1 
ATOM   8419  C CD2 . LEU G 2 5   ? -33.918 -39.158 15.896  1.000 109.715 ? 4   LEU HHH CD2 1 
ATOM   8420  N N   . VAL G 2 6   ? -33.259 -43.525 18.031  1.000 109.966 ? 5   VAL HHH N   1 
ATOM   8421  C CA  . VAL G 2 6   ? -32.643 -44.794 18.505  1.000 111.712 ? 5   VAL HHH CA  1 
ATOM   8422  C C   . VAL G 2 6   ? -31.230 -44.816 17.936  1.000 111.595 ? 5   VAL HHH C   1 
ATOM   8423  O O   . VAL G 2 6   ? -31.038 -44.313 16.808  1.000 112.011 ? 5   VAL HHH O   1 
ATOM   8424  C CB  . VAL G 2 6   ? -33.459 -46.027 18.075  1.000 114.844 ? 5   VAL HHH CB  1 
ATOM   8425  C CG1 . VAL G 2 6   ? -34.947 -45.713 17.999  1.000 115.898 ? 5   VAL HHH CG1 1 
ATOM   8426  C CG2 . VAL G 2 6   ? -32.976 -46.616 16.757  1.000 118.060 ? 5   VAL HHH CG2 1 
ATOM   8427  N N   . GLN G 2 7   ? -30.285 -45.363 18.694  1.000 113.498 ? 6   GLN HHH N   1 
ATOM   8428  C CA  . GLN G 2 7   ? -28.860 -45.404 18.289  1.000 115.048 ? 6   GLN HHH CA  1 
ATOM   8429  C C   . GLN G 2 7   ? -28.370 -46.844 18.342  1.000 116.455 ? 6   GLN HHH C   1 
ATOM   8430  O O   . GLN G 2 7   ? -28.893 -47.617 19.170  1.000 113.728 ? 6   GLN HHH O   1 
ATOM   8431  C CB  . GLN G 2 7   ? -28.020 -44.501 19.188  1.000 114.399 ? 6   GLN HHH CB  1 
ATOM   8432  C CG  . GLN G 2 7   ? -28.393 -43.034 19.055  1.000 113.329 ? 6   GLN HHH CG  1 
ATOM   8433  C CD  . GLN G 2 7   ? -27.220 -42.131 19.320  1.000 111.763 ? 6   GLN HHH CD  1 
ATOM   8434  O OE1 . GLN G 2 7   ? -27.329 -41.148 20.047  1.000 109.289 ? 6   GLN HHH OE1 1 
ATOM   8435  N NE2 . GLN G 2 7   ? -26.087 -42.471 18.722  1.000 111.768 ? 6   GLN HHH NE2 1 
ATOM   8436  N N   . SER G 2 8   ? -27.406 -47.168 17.477  1.000 119.761 ? 7   SER HHH N   1 
ATOM   8437  C CA  . SER G 2 8   ? -26.707 -48.476 17.454  1.000 121.773 ? 7   SER HHH CA  1 
ATOM   8438  C C   . SER G 2 8   ? -26.199 -48.782 18.864  1.000 121.636 ? 7   SER HHH C   1 
ATOM   8439  O O   . SER G 2 8   ? -25.998 -47.826 19.654  1.000 120.810 ? 7   SER HHH O   1 
ATOM   8440  C CB  . SER G 2 8   ? -25.588 -48.502 16.443  1.000 121.937 ? 7   SER HHH CB  1 
ATOM   8441  O OG  . SER G 2 8   ? -24.590 -47.543 16.756  1.000 120.541 ? 7   SER HHH OG  1 
ATOM   8442  N N   . GLY G 2 9   ? -26.016 -50.069 19.158  1.000 123.563 ? 8   GLY HHH N   1 
ATOM   8443  C CA  . GLY G 2 9   ? -25.520 -50.558 20.455  1.000 124.992 ? 8   GLY HHH CA  1 
ATOM   8444  C C   . GLY G 2 9   ? -24.097 -50.102 20.738  1.000 124.456 ? 8   GLY HHH C   1 
ATOM   8445  O O   . GLY G 2 9   ? -23.543 -49.300 19.956  1.000 124.008 ? 8   GLY HHH O   1 
ATOM   8446  N N   . THR G 2 10  ? -23.527 -50.610 21.829  1.000 124.141 ? 9   THR HHH N   1 
ATOM   8447  C CA  . THR G 2 10  ? -22.169 -50.280 22.318  1.000 123.069 ? 9   THR HHH CA  1 
ATOM   8448  C C   . THR G 2 10  ? -21.142 -51.029 21.475  1.000 122.852 ? 9   THR HHH C   1 
ATOM   8449  O O   . THR G 2 10  ? -21.360 -52.227 21.202  1.000 119.665 ? 9   THR HHH O   1 
ATOM   8450  C CB  . THR G 2 10  ? -22.031 -50.648 23.795  1.000 126.665 ? 9   THR HHH CB  1 
ATOM   8451  O OG1 . THR G 2 10  ? -23.181 -50.116 24.451  1.000 129.556 ? 9   THR HHH OG1 1 
ATOM   8452  C CG2 . THR G 2 10  ? -20.764 -50.117 24.425  1.000 128.414 ? 9   THR HHH CG2 1 
ATOM   8453  N N   . GLU G 2 11  ? -20.057 -50.338 21.119  1.000 125.500 ? 10  GLU HHH N   1 
ATOM   8454  C CA  . GLU G 2 11  ? -18.985 -50.832 20.215  1.000 130.920 ? 10  GLU HHH CA  1 
ATOM   8455  C C   . GLU G 2 11  ? -17.661 -50.892 20.990  1.000 131.903 ? 10  GLU HHH C   1 
ATOM   8456  O O   . GLU G 2 11  ? -17.153 -49.822 21.377  1.000 130.825 ? 10  GLU HHH O   1 
ATOM   8457  C CB  . GLU G 2 11  ? -18.874 -49.920 18.987  1.000 132.593 ? 10  GLU HHH CB  1 
ATOM   8458  C CG  . GLU G 2 11  ? -20.171 -49.783 18.200  1.000 133.597 ? 10  GLU HHH CG  1 
ATOM   8459  C CD  . GLU G 2 11  ? -20.493 -50.917 17.236  1.000 136.771 ? 10  GLU HHH CD  1 
ATOM   8460  O OE1 . GLU G 2 11  ? -19.845 -51.990 17.329  1.000 137.960 ? 10  GLU HHH OE1 1 
ATOM   8461  O OE2 . GLU G 2 11  ? -21.396 -50.719 16.387  1.000 137.822 ? 10  GLU HHH OE2 1 
ATOM   8462  N N   . VAL G 2 12  ? -17.142 -52.106 21.216  1.000 132.947 ? 11  VAL HHH N   1 
ATOM   8463  C CA  . VAL G 2 12  ? -15.735 -52.368 21.648  1.000 132.897 ? 11  VAL HHH CA  1 
ATOM   8464  C C   . VAL G 2 12  ? -14.925 -52.689 20.388  1.000 134.587 ? 11  VAL HHH C   1 
ATOM   8465  O O   . VAL G 2 12  ? -15.134 -53.773 19.807  1.000 138.141 ? 11  VAL HHH O   1 
ATOM   8466  C CB  . VAL G 2 12  ? -15.624 -53.508 22.679  1.000 133.011 ? 11  VAL HHH CB  1 
ATOM   8467  C CG1 . VAL G 2 12  ? -14.228 -53.555 23.287  1.000 133.245 ? 11  VAL HHH CG1 1 
ATOM   8468  C CG2 . VAL G 2 12  ? -16.688 -53.413 23.765  1.000 130.780 ? 11  VAL HHH CG2 1 
ATOM   8469  N N   . LYS G 2 13  ? -14.038 -51.779 19.984  1.000 133.703 ? 12  LYS HHH N   1 
ATOM   8470  C CA  . LYS G 2 13  ? -13.243 -51.920 18.741  1.000 136.501 ? 12  LYS HHH CA  1 
ATOM   8471  C C   . LYS G 2 13  ? -11.754 -51.811 19.069  1.000 138.186 ? 12  LYS HHH C   1 
ATOM   8472  O O   . LYS G 2 13  ? -11.404 -51.264 20.137  1.000 138.424 ? 12  LYS HHH O   1 
ATOM   8473  C CB  . LYS G 2 13  ? -13.687 -50.880 17.712  1.000 136.382 ? 12  LYS HHH CB  1 
ATOM   8474  C CG  . LYS G 2 13  ? -15.141 -51.001 17.269  1.000 136.448 ? 12  LYS HHH CG  1 
ATOM   8475  C CD  . LYS G 2 13  ? -15.423 -52.205 16.393  1.000 140.079 ? 12  LYS HHH CD  1 
ATOM   8476  C CE  . LYS G 2 13  ? -15.058 -51.963 14.943  1.000 144.593 ? 12  LYS HHH CE  1 
ATOM   8477  N NZ  . LYS G 2 13  ? -14.842 -53.221 14.185  1.000 149.268 ? 12  LYS HHH NZ  1 
ATOM   8478  N N   . LYS G 2 14  ? -10.926 -52.367 18.184  1.000 138.840 ? 13  LYS HHH N   1 
ATOM   8479  C CA  . LYS G 2 14  ? -9.444  -52.348 18.275  1.000 139.602 ? 13  LYS HHH CA  1 
ATOM   8480  C C   . LYS G 2 14  ? -8.942  -51.143 17.486  1.000 137.816 ? 13  LYS HHH C   1 
ATOM   8481  O O   . LYS G 2 14  ? -9.512  -50.790 16.456  1.000 134.384 ? 13  LYS HHH O   1 
ATOM   8482  C CB  . LYS G 2 14  ? -8.860  -53.667 17.760  1.000 144.328 ? 13  LYS HHH CB  1 
ATOM   8483  C CG  . LYS G 2 14  ? -9.177  -54.897 18.606  1.000 145.051 ? 13  LYS HHH CG  1 
ATOM   8484  C CD  . LYS G 2 14  ? -8.303  -55.031 19.832  1.000 146.474 ? 13  LYS HHH CD  1 
ATOM   8485  C CE  . LYS G 2 14  ? -6.984  -55.709 19.527  1.000 151.644 ? 13  LYS HHH CE  1 
ATOM   8486  N NZ  . LYS G 2 14  ? -7.112  -57.183 19.558  1.000 154.044 ? 13  LYS HHH NZ  1 
ATOM   8487  N N   . PRO G 2 15  ? -7.890  -50.450 17.973  1.000 138.512 ? 14  PRO HHH N   1 
ATOM   8488  C CA  . PRO G 2 15  ? -7.310  -49.319 17.251  1.000 140.048 ? 14  PRO HHH CA  1 
ATOM   8489  C C   . PRO G 2 15  ? -6.987  -49.667 15.790  1.000 143.901 ? 14  PRO HHH C   1 
ATOM   8490  O O   . PRO G 2 15  ? -6.281  -50.635 15.557  1.000 148.993 ? 14  PRO HHH O   1 
ATOM   8491  C CB  . PRO G 2 15  ? -6.020  -49.020 18.030  1.000 141.955 ? 14  PRO HHH CB  1 
ATOM   8492  C CG  . PRO G 2 15  ? -6.279  -49.544 19.430  1.000 139.939 ? 14  PRO HHH CG  1 
ATOM   8493  C CD  . PRO G 2 15  ? -7.228  -50.710 19.262  1.000 138.955 ? 14  PRO HHH CD  1 
ATOM   8494  N N   . GLY G 2 16  ? -7.514  -48.884 14.848  1.000 142.777 ? 15  GLY HHH N   1 
ATOM   8495  C CA  . GLY G 2 16  ? -7.252  -49.055 13.407  1.000 146.875 ? 15  GLY HHH CA  1 
ATOM   8496  C C   . GLY G 2 16  ? -8.493  -49.514 12.666  1.000 146.483 ? 15  GLY HHH C   1 
ATOM   8497  O O   . GLY G 2 16  ? -8.697  -49.062 11.516  1.000 152.525 ? 15  GLY HHH O   1 
ATOM   8498  N N   . GLU G 2 17  ? -9.297  -50.379 13.292  1.000 142.343 ? 16  GLU HHH N   1 
ATOM   8499  C CA  . GLU G 2 17  ? -10.552 -50.908 12.695  1.000 141.061 ? 16  GLU HHH CA  1 
ATOM   8500  C C   . GLU G 2 17  ? -11.454 -49.728 12.319  1.000 134.509 ? 16  GLU HHH C   1 
ATOM   8501  O O   . GLU G 2 17  ? -11.247 -48.624 12.854  1.000 132.846 ? 16  GLU HHH O   1 
ATOM   8502  C CB  . GLU G 2 17  ? -11.252 -51.877 13.651  1.000 142.751 ? 16  GLU HHH CB  1 
ATOM   8503  C CG  . GLU G 2 17  ? -10.650 -53.276 13.650  1.000 149.277 ? 16  GLU HHH CG  1 
ATOM   8504  C CD  . GLU G 2 17  ? -11.168 -54.233 14.718  1.000 150.379 ? 16  GLU HHH CD  1 
ATOM   8505  O OE1 . GLU G 2 17  ? -11.909 -53.781 15.624  1.000 148.192 ? 16  GLU HHH OE1 1 
ATOM   8506  O OE2 . GLU G 2 17  ? -10.819 -55.438 14.653  1.000 155.652 ? 16  GLU HHH OE2 1 
ATOM   8507  N N   . SER G 2 18  ? -12.390 -49.961 11.402  1.000 131.535 ? 17  SER HHH N   1 
ATOM   8508  C CA  . SER G 2 18  ? -13.379 -48.975 10.901  1.000 129.196 ? 17  SER HHH CA  1 
ATOM   8509  C C   . SER G 2 18  ? -14.749 -49.294 11.503  1.000 125.848 ? 17  SER HHH C   1 
ATOM   8510  O O   . SER G 2 18  ? -14.965 -50.458 11.863  1.000 127.388 ? 17  SER HHH O   1 
ATOM   8511  C CB  . SER G 2 18  ? -13.410 -49.018 9.416   1.000 133.189 ? 17  SER HHH CB  1 
ATOM   8512  O OG  . SER G 2 18  ? -13.217 -50.357 8.978   1.000 139.247 ? 17  SER HHH OG  1 
ATOM   8513  N N   . LEU G 2 19  ? -15.644 -48.308 11.584  1.000 123.360 ? 18  LEU HHH N   1 
ATOM   8514  C CA  . LEU G 2 19  ? -16.883 -48.392 12.401  1.000 122.235 ? 18  LEU HHH CA  1 
ATOM   8515  C C   . LEU G 2 19  ? -17.946 -47.421 11.883  1.000 120.714 ? 18  LEU HHH C   1 
ATOM   8516  O O   . LEU G 2 19  ? -17.619 -46.232 11.761  1.000 118.990 ? 18  LEU HHH O   1 
ATOM   8517  C CB  . LEU G 2 19  ? -16.507 -48.032 13.839  1.000 123.166 ? 18  LEU HHH CB  1 
ATOM   8518  C CG  . LEU G 2 19  ? -17.683 -47.900 14.803  1.000 123.319 ? 18  LEU HHH CG  1 
ATOM   8519  C CD1 . LEU G 2 19  ? -18.268 -49.266 15.107  1.000 125.573 ? 18  LEU HHH CD1 1 
ATOM   8520  C CD2 . LEU G 2 19  ? -17.274 -47.204 16.093  1.000 122.404 ? 18  LEU HHH CD2 1 
ATOM   8521  N N   . LYS G 2 20  ? -19.178 -47.896 11.662  1.000 122.030 ? 19  LYS HHH N   1 
ATOM   8522  C CA  . LYS G 2 20  ? -20.331 -47.066 11.205  1.000 122.185 ? 19  LYS HHH CA  1 
ATOM   8523  C C   . LYS G 2 20  ? -21.486 -47.220 12.195  1.000 120.034 ? 19  LYS HHH C   1 
ATOM   8524  O O   . LYS G 2 20  ? -22.210 -48.250 12.117  1.000 122.236 ? 19  LYS HHH O   1 
ATOM   8525  C CB  . LYS G 2 20  ? -20.801 -47.457 9.798   1.000 126.472 ? 19  LYS HHH CB  1 
ATOM   8526  C CG  . LYS G 2 20  ? -22.017 -46.685 9.285   1.000 126.885 ? 19  LYS HHH CG  1 
ATOM   8527  C CD  . LYS G 2 20  ? -22.266 -46.797 7.790   1.000 130.137 ? 19  LYS HHH CD  1 
ATOM   8528  C CE  . LYS G 2 20  ? -22.935 -48.099 7.389   1.000 133.832 ? 19  LYS HHH CE  1 
ATOM   8529  N NZ  . LYS G 2 20  ? -23.453 -48.067 5.999   1.000 136.136 ? 19  LYS HHH NZ  1 
ATOM   8530  N N   . ILE G 2 21  ? -21.659 -46.231 13.076  1.000 117.024 ? 20  ILE HHH N   1 
ATOM   8531  C CA  . ILE G 2 21  ? -22.758 -46.219 14.083  1.000 116.104 ? 20  ILE HHH CA  1 
ATOM   8532  C C   . ILE G 2 21  ? -23.992 -45.567 13.458  1.000 114.372 ? 20  ILE HHH C   1 
ATOM   8533  O O   . ILE G 2 21  ? -23.849 -44.624 12.661  1.000 110.509 ? 20  ILE HHH O   1 
ATOM   8534  C CB  . ILE G 2 21  ? -22.336 -45.569 15.414  1.000 115.377 ? 20  ILE HHH CB  1 
ATOM   8535  C CG1 . ILE G 2 21  ? -22.006 -44.080 15.286  1.000 115.162 ? 20  ILE HHH CG1 1 
ATOM   8536  C CG2 . ILE G 2 21  ? -21.185 -46.353 16.022  1.000 116.379 ? 20  ILE HHH CG2 1 
ATOM   8537  C CD1 . ILE G 2 21  ? -21.944 -43.359 16.613  1.000 114.194 ? 20  ILE HHH CD1 1 
ATOM   8538  N N   . SER G 2 22  ? -25.157 -46.115 13.794  1.000 115.766 ? 21  SER HHH N   1 
ATOM   8539  C CA  . SER G 2 22  ? -26.472 -45.747 13.226  1.000 115.787 ? 21  SER HHH CA  1 
ATOM   8540  C C   . SER G 2 22  ? -27.157 -44.770 14.174  1.000 110.354 ? 21  SER HHH C   1 
ATOM   8541  O O   . SER G 2 22  ? -26.700 -44.606 15.335  1.000 105.619 ? 21  SER HHH O   1 
ATOM   8542  C CB  . SER G 2 22  ? -27.335 -46.969 12.973  1.000 120.794 ? 21  SER HHH CB  1 
ATOM   8543  O OG  . SER G 2 22  ? -28.299 -47.160 14.012  1.000 121.913 ? 21  SER HHH OG  1 
ATOM   8544  N N   . CYS G 2 23  ? -28.203 -44.144 13.651  1.000 107.170 ? 22  CYS HHH N   1 
ATOM   8545  C CA  . CYS G 2 23  ? -29.150 -43.288 14.389  1.000 105.713 ? 22  CYS HHH CA  1 
ATOM   8546  C C   . CYS G 2 23  ? -30.418 -43.231 13.552  1.000 104.934 ? 22  CYS HHH C   1 
ATOM   8547  O O   . CYS G 2 23  ? -30.374 -42.606 12.486  1.000 104.071 ? 22  CYS HHH O   1 
ATOM   8548  C CB  . CYS G 2 23  ? -28.567 -41.901 14.617  1.000 106.228 ? 22  CYS HHH CB  1 
ATOM   8549  S SG  . CYS G 2 23  ? -29.800 -40.655 15.077  1.000 108.129 ? 22  CYS HHH SG  1 
ATOM   8550  N N   . LYS G 2 24  ? -31.467 -43.917 13.997  1.000 106.652 ? 23  LYS HHH N   1 
ATOM   8551  C CA  . LYS G 2 24  ? -32.746 -44.029 13.257  1.000 109.502 ? 23  LYS HHH CA  1 
ATOM   8552  C C   . LYS G 2 24  ? -33.800 -43.105 13.875  1.000 108.911 ? 23  LYS HHH C   1 
ATOM   8553  O O   . LYS G 2 24  ? -33.835 -42.988 15.106  1.000 109.097 ? 23  LYS HHH O   1 
ATOM   8554  C CB  . LYS G 2 24  ? -33.226 -45.478 13.264  1.000 114.091 ? 23  LYS HHH CB  1 
ATOM   8555  C CG  . LYS G 2 24  ? -34.338 -45.745 12.265  1.000 120.058 ? 23  LYS HHH CG  1 
ATOM   8556  C CD  . LYS G 2 24  ? -34.705 -47.199 12.105  1.000 124.997 ? 23  LYS HHH CD  1 
ATOM   8557  C CE  . LYS G 2 24  ? -35.567 -47.431 10.882  1.000 127.940 ? 23  LYS HHH CE  1 
ATOM   8558  N NZ  . LYS G 2 24  ? -36.103 -48.810 10.870  1.000 131.727 ? 23  LYS HHH NZ  1 
ATOM   8559  N N   . GLY G 2 25  ? -34.637 -42.495 13.035  1.000 109.930 ? 24  GLY HHH N   1 
ATOM   8560  C CA  . GLY G 2 25  ? -35.712 -41.568 13.436  1.000 111.613 ? 24  GLY HHH CA  1 
ATOM   8561  C C   . GLY G 2 25  ? -37.071 -42.251 13.496  1.000 115.874 ? 24  GLY HHH C   1 
ATOM   8562  O O   . GLY G 2 25  ? -37.724 -42.359 12.437  1.000 117.795 ? 24  GLY HHH O   1 
ATOM   8563  N N   . SER G 2 26  ? -37.494 -42.671 14.694  1.000 118.269 ? 25  SER HHH N   1 
ATOM   8564  C CA  . SER G 2 26  ? -38.851 -43.205 14.994  1.000 121.638 ? 25  SER HHH CA  1 
ATOM   8565  C C   . SER G 2 26  ? -39.889 -42.085 14.896  1.000 121.768 ? 25  SER HHH C   1 
ATOM   8566  O O   . SER G 2 26  ? -39.871 -41.186 15.758  1.000 117.671 ? 25  SER HHH O   1 
ATOM   8567  C CB  . SER G 2 26  ? -38.909 -43.860 16.359  1.000 123.995 ? 25  SER HHH CB  1 
ATOM   8568  O OG  . SER G 2 26  ? -40.200 -43.712 16.948  1.000 126.727 ? 25  SER HHH OG  1 
ATOM   8569  N N   . GLY G 2 27  ? -40.772 -42.159 13.897  1.000 125.156 ? 26  GLY HHH N   1 
ATOM   8570  C CA  . GLY G 2 27  ? -41.978 -41.315 13.834  1.000 128.145 ? 26  GLY HHH CA  1 
ATOM   8571  C C   . GLY G 2 27  ? -42.109 -40.553 12.533  1.000 127.241 ? 26  GLY HHH C   1 
ATOM   8572  O O   . GLY G 2 27  ? -41.410 -40.884 11.550  1.000 127.319 ? 26  GLY HHH O   1 
ATOM   8573  N N   . TYR G 2 28  ? -42.996 -39.562 12.541  1.000 126.942 ? 27  TYR HHH N   1 
ATOM   8574  C CA  . TYR G 2 28  ? -43.476 -38.867 11.328  1.000 129.818 ? 27  TYR HHH CA  1 
ATOM   8575  C C   . TYR G 2 28  ? -42.869 -37.477 11.256  1.000 127.522 ? 27  TYR HHH C   1 
ATOM   8576  O O   . TYR G 2 28  ? -42.498 -36.932 12.315  1.000 128.968 ? 27  TYR HHH O   1 
ATOM   8577  C CB  . TYR G 2 28  ? -45.001 -38.809 11.329  1.000 135.485 ? 27  TYR HHH CB  1 
ATOM   8578  C CG  . TYR G 2 28  ? -45.605 -40.147 11.008  1.000 140.239 ? 27  TYR HHH CG  1 
ATOM   8579  C CD1 . TYR G 2 28  ? -45.694 -40.589 9.699   1.000 141.971 ? 27  TYR HHH CD1 1 
ATOM   8580  C CD2 . TYR G 2 28  ? -46.003 -41.005 12.017  1.000 143.397 ? 27  TYR HHH CD2 1 
ATOM   8581  C CE1 . TYR G 2 28  ? -46.209 -41.837 9.397   1.000 145.208 ? 27  TYR HHH CE1 1 
ATOM   8582  C CE2 . TYR G 2 28  ? -46.523 -42.255 11.732  1.000 146.386 ? 27  TYR HHH CE2 1 
ATOM   8583  C CZ  . TYR G 2 28  ? -46.627 -42.672 10.417  1.000 146.803 ? 27  TYR HHH CZ  1 
ATOM   8584  O OH  . TYR G 2 28  ? -47.136 -43.902 10.132  1.000 150.202 ? 27  TYR HHH OH  1 
ATOM   8585  N N   . GLY G 2 29  ? -42.815 -36.942 10.031  1.000 125.112 ? 28  GLY HHH N   1 
ATOM   8586  C CA  . GLY G 2 29  ? -42.296 -35.602 9.713   1.000 122.243 ? 28  GLY HHH CA  1 
ATOM   8587  C C   . GLY G 2 29  ? -40.788 -35.554 9.831   1.000 118.841 ? 28  GLY HHH C   1 
ATOM   8588  O O   . GLY G 2 29  ? -40.234 -34.446 9.957   1.000 115.461 ? 28  GLY HHH O   1 
ATOM   8589  N N   . PHE G 2 30  ? -40.136 -36.716 9.785   1.000 118.840 ? 29  PHE HHH N   1 
ATOM   8590  C CA  . PHE G 2 30  ? -38.659 -36.831 9.820   1.000 118.258 ? 29  PHE HHH CA  1 
ATOM   8591  C C   . PHE G 2 30  ? -38.064 -35.938 8.724   1.000 117.142 ? 29  PHE HHH C   1 
ATOM   8592  O O   . PHE G 2 30  ? -36.900 -35.516 8.829   1.000 117.056 ? 29  PHE HHH O   1 
ATOM   8593  C CB  . PHE G 2 30  ? -38.240 -38.291 9.646   1.000 119.572 ? 29  PHE HHH CB  1 
ATOM   8594  C CG  . PHE G 2 30  ? -36.750 -38.501 9.701   1.000 119.587 ? 29  PHE HHH CG  1 
ATOM   8595  C CD1 . PHE G 2 30  ? -36.101 -38.673 10.918  1.000 120.545 ? 29  PHE HHH CD1 1 
ATOM   8596  C CD2 . PHE G 2 30  ? -35.995 -38.504 8.539   1.000 119.037 ? 29  PHE HHH CD2 1 
ATOM   8597  C CE1 . PHE G 2 30  ? -34.730 -38.872 10.966  1.000 119.942 ? 29  PHE HHH CE1 1 
ATOM   8598  C CE2 . PHE G 2 30  ? -34.623 -38.693 8.588   1.000 119.151 ? 29  PHE HHH CE2 1 
ATOM   8599  C CZ  . PHE G 2 30  ? -33.992 -38.872 9.800   1.000 119.378 ? 29  PHE HHH CZ  1 
ATOM   8600  N N   . ILE G 2 31  ? -38.853 -35.648 7.691   1.000 118.387 ? 30  ILE HHH N   1 
ATOM   8601  C CA  . ILE G 2 31  ? -38.381 -34.956 6.457   1.000 116.991 ? 30  ILE HHH CA  1 
ATOM   8602  C C   . ILE G 2 31  ? -37.807 -33.585 6.818   1.000 114.566 ? 30  ILE HHH C   1 
ATOM   8603  O O   . ILE G 2 31  ? -36.859 -33.172 6.143   1.000 112.824 ? 30  ILE HHH O   1 
ATOM   8604  C CB  . ILE G 2 31  ? -39.499 -34.863 5.398   1.000 118.338 ? 30  ILE HHH CB  1 
ATOM   8605  C CG1 . ILE G 2 31  ? -38.960 -34.337 4.066   1.000 118.666 ? 30  ILE HHH CG1 1 
ATOM   8606  C CG2 . ILE G 2 31  ? -40.673 -34.040 5.896   1.000 119.184 ? 30  ILE HHH CG2 1 
ATOM   8607  C CD1 . ILE G 2 31  ? -37.877 -35.202 3.461   1.000 119.374 ? 30  ILE HHH CD1 1 
ATOM   8608  N N   . THR G 2 32  ? -38.352 -32.918 7.837   1.000 114.524 ? 31  THR HHH N   1 
ATOM   8609  C CA  . THR G 2 32  ? -37.955 -31.540 8.232   1.000 116.349 ? 31  THR HHH CA  1 
ATOM   8610  C C   . THR G 2 32  ? -36.717 -31.575 9.121   1.000 118.465 ? 31  THR HHH C   1 
ATOM   8611  O O   . THR G 2 32  ? -36.135 -30.481 9.303   1.000 121.465 ? 31  THR HHH O   1 
ATOM   8612  C CB  . THR G 2 32  ? -39.024 -30.805 9.044   1.000 117.011 ? 31  THR HHH CB  1 
ATOM   8613  O OG1 . THR G 2 32  ? -39.003 -31.323 10.375  1.000 115.315 ? 31  THR HHH OG1 1 
ATOM   8614  C CG2 . THR G 2 32  ? -40.409 -30.932 8.453   1.000 120.052 ? 31  THR HHH CG2 1 
ATOM   8615  N N   . TYR G 2 33  ? -36.385 -32.756 9.675   1.000 118.226 ? 32  TYR HHH N   1 
ATOM   8616  C CA  . TYR G 2 33  ? -35.379 -32.963 10.756  1.000 115.630 ? 32  TYR HHH CA  1 
ATOM   8617  C C   . TYR G 2 33  ? -33.967 -33.011 10.177  1.000 111.022 ? 32  TYR HHH C   1 
ATOM   8618  O O   . TYR G 2 33  ? -33.774 -33.649 9.128   1.000 110.662 ? 32  TYR HHH O   1 
ATOM   8619  C CB  . TYR G 2 33  ? -35.639 -34.240 11.568  1.000 118.211 ? 32  TYR HHH CB  1 
ATOM   8620  C CG  . TYR G 2 33  ? -36.598 -34.042 12.711  1.000 121.638 ? 32  TYR HHH CG  1 
ATOM   8621  C CD1 . TYR G 2 33  ? -37.967 -34.069 12.501  1.000 124.583 ? 32  TYR HHH CD1 1 
ATOM   8622  C CD2 . TYR G 2 33  ? -36.136 -33.759 13.987  1.000 122.494 ? 32  TYR HHH CD2 1 
ATOM   8623  C CE1 . TYR G 2 33  ? -38.860 -33.839 13.533  1.000 126.958 ? 32  TYR HHH CE1 1 
ATOM   8624  C CE2 . TYR G 2 33  ? -37.016 -33.532 15.032  1.000 125.355 ? 32  TYR HHH CE2 1 
ATOM   8625  C CZ  . TYR G 2 33  ? -38.381 -33.569 14.803  1.000 127.893 ? 32  TYR HHH CZ  1 
ATOM   8626  O OH  . TYR G 2 33  ? -39.258 -33.341 15.822  1.000 132.092 ? 32  TYR HHH OH  1 
ATOM   8627  N N   . TRP G 2 34  ? -33.036 -32.342 10.861  1.000 108.528 ? 33  TRP HHH N   1 
ATOM   8628  C CA  . TRP G 2 34  ? -31.573 -32.363 10.593  1.000 108.427 ? 33  TRP HHH CA  1 
ATOM   8629  C C   . TRP G 2 34  ? -30.880 -33.074 11.761  1.000 105.596 ? 33  TRP HHH C   1 
ATOM   8630  O O   . TRP G 2 34  ? -30.934 -32.542 12.890  1.000 108.159 ? 33  TRP HHH O   1 
ATOM   8631  C CB  . TRP G 2 34  ? -31.015 -30.942 10.435  1.000 109.898 ? 33  TRP HHH CB  1 
ATOM   8632  C CG  . TRP G 2 34  ? -31.538 -30.120 9.297   1.000 110.979 ? 33  TRP HHH CG  1 
ATOM   8633  C CD1 . TRP G 2 34  ? -32.836 -29.829 8.996   1.000 113.739 ? 33  TRP HHH CD1 1 
ATOM   8634  C CD2 . TRP G 2 34  ? -30.743 -29.394 8.349   1.000 111.862 ? 33  TRP HHH CD2 1 
ATOM   8635  N NE1 . TRP G 2 34  ? -32.905 -29.006 7.905   1.000 115.295 ? 33  TRP HHH NE1 1 
ATOM   8636  C CE2 . TRP G 2 34  ? -31.634 -28.718 7.492   1.000 114.189 ? 33  TRP HHH CE2 1 
ATOM   8637  C CE3 . TRP G 2 34  ? -29.369 -29.263 8.136   1.000 113.554 ? 33  TRP HHH CE3 1 
ATOM   8638  C CZ2 . TRP G 2 34  ? -31.193 -27.928 6.435   1.000 117.133 ? 33  TRP HHH CZ2 1 
ATOM   8639  C CZ3 . TRP G 2 34  ? -28.932 -28.478 7.094   1.000 116.784 ? 33  TRP HHH CZ3 1 
ATOM   8640  C CH2 . TRP G 2 34  ? -29.834 -27.820 6.257   1.000 118.389 ? 33  TRP HHH CH2 1 
ATOM   8641  N N   . ILE G 2 35  ? -30.246 -34.219 11.514  1.000 101.870 ? 34  ILE HHH N   1 
ATOM   8642  C CA  . ILE G 2 35  ? -29.589 -35.008 12.590  1.000 100.514 ? 34  ILE HHH CA  1 
ATOM   8643  C C   . ILE G 2 35  ? -28.127 -34.589 12.682  1.000 100.126 ? 34  ILE HHH C   1 
ATOM   8644  O O   . ILE G 2 35  ? -27.388 -34.804 11.693  1.000 95.841  ? 34  ILE HHH O   1 
ATOM   8645  C CB  . ILE G 2 35  ? -29.719 -36.521 12.374  1.000 103.044 ? 34  ILE HHH CB  1 
ATOM   8646  C CG1 . ILE G 2 35  ? -31.149 -37.007 12.597  1.000 105.272 ? 34  ILE HHH CG1 1 
ATOM   8647  C CG2 . ILE G 2 35  ? -28.749 -37.263 13.274  1.000 104.722 ? 34  ILE HHH CG2 1 
ATOM   8648  C CD1 . ILE G 2 35  ? -32.035 -36.810 11.403  1.000 108.358 ? 34  ILE HHH CD1 1 
ATOM   8649  N N   . GLY G 2 36  ? -27.758 -34.036 13.845  1.000 103.032 ? 35  GLY HHH N   1 
ATOM   8650  C CA  . GLY G 2 36  ? -26.375 -33.737 14.262  1.000 103.525 ? 35  GLY HHH CA  1 
ATOM   8651  C C   . GLY G 2 36  ? -25.763 -34.878 15.056  1.000 103.311 ? 35  GLY HHH C   1 
ATOM   8652  O O   . GLY G 2 36  ? -26.508 -35.758 15.519  1.000 103.022 ? 35  GLY HHH O   1 
ATOM   8653  N N   . TRP G 2 37  ? -24.438 -34.869 15.190  1.000 104.326 ? 36  TRP HHH N   1 
ATOM   8654  C CA  . TRP G 2 37  ? -23.658 -35.808 16.036  1.000 105.316 ? 36  TRP HHH CA  1 
ATOM   8655  C C   . TRP G 2 37  ? -22.817 -35.010 17.040  1.000 107.293 ? 36  TRP HHH C   1 
ATOM   8656  O O   . TRP G 2 37  ? -22.204 -33.998 16.649  1.000 109.019 ? 36  TRP HHH O   1 
ATOM   8657  C CB  . TRP G 2 37  ? -22.781 -36.713 15.169  1.000 105.436 ? 36  TRP HHH CB  1 
ATOM   8658  C CG  . TRP G 2 37  ? -23.547 -37.707 14.360  1.000 104.085 ? 36  TRP HHH CG  1 
ATOM   8659  C CD1 . TRP G 2 37  ? -23.967 -37.564 13.074  1.000 105.323 ? 36  TRP HHH CD1 1 
ATOM   8660  C CD2 . TRP G 2 37  ? -23.979 -39.009 14.778  1.000 104.153 ? 36  TRP HHH CD2 1 
ATOM   8661  N NE1 . TRP G 2 37  ? -24.627 -38.687 12.660  1.000 106.037 ? 36  TRP HHH NE1 1 
ATOM   8662  C CE2 . TRP G 2 37  ? -24.650 -39.591 13.683  1.000 105.685 ? 36  TRP HHH CE2 1 
ATOM   8663  C CE3 . TRP G 2 37  ? -23.870 -39.738 15.965  1.000 105.650 ? 36  TRP HHH CE3 1 
ATOM   8664  C CZ2 . TRP G 2 37  ? -25.208 -40.867 13.741  1.000 108.173 ? 36  TRP HHH CZ2 1 
ATOM   8665  C CZ3 . TRP G 2 37  ? -24.416 -41.003 16.024  1.000 107.195 ? 36  TRP HHH CZ3 1 
ATOM   8666  C CH2 . TRP G 2 37  ? -25.080 -41.556 14.927  1.000 108.688 ? 36  TRP HHH CH2 1 
ATOM   8667  N N   . VAL G 2 38  ? -22.777 -35.464 18.291  1.000 107.617 ? 37  VAL HHH N   1 
ATOM   8668  C CA  . VAL G 2 38  ? -22.027 -34.802 19.394  1.000 107.397 ? 37  VAL HHH CA  1 
ATOM   8669  C C   . VAL G 2 38  ? -21.135 -35.844 20.067  1.000 108.684 ? 37  VAL HHH C   1 
ATOM   8670  O O   . VAL G 2 38  ? -21.620 -36.962 20.325  1.000 109.205 ? 37  VAL HHH O   1 
ATOM   8671  C CB  . VAL G 2 38  ? -23.000 -34.150 20.387  1.000 106.337 ? 37  VAL HHH CB  1 
ATOM   8672  C CG1 . VAL G 2 38  ? -22.263 -33.496 21.542  1.000 109.124 ? 37  VAL HHH CG1 1 
ATOM   8673  C CG2 . VAL G 2 38  ? -23.902 -33.146 19.689  1.000 106.270 ? 37  VAL HHH CG2 1 
ATOM   8674  N N   . ARG G 2 39  ? -19.876 -35.486 20.319  1.000 111.219 ? 38  ARG HHH N   1 
ATOM   8675  C CA  . ARG G 2 39  ? -18.904 -36.324 21.062  1.000 113.645 ? 38  ARG HHH CA  1 
ATOM   8676  C C   . ARG G 2 39  ? -18.776 -35.776 22.483  1.000 114.218 ? 38  ARG HHH C   1 
ATOM   8677  O O   . ARG G 2 39  ? -18.443 -34.589 22.647  1.000 115.851 ? 38  ARG HHH O   1 
ATOM   8678  C CB  . ARG G 2 39  ? -17.539 -36.341 20.368  1.000 117.618 ? 38  ARG HHH CB  1 
ATOM   8679  C CG  . ARG G 2 39  ? -16.510 -37.216 21.068  1.000 121.312 ? 38  ARG HHH CG  1 
ATOM   8680  C CD  . ARG G 2 39  ? -15.213 -37.346 20.301  1.000 125.185 ? 38  ARG HHH CD  1 
ATOM   8681  N NE  . ARG G 2 39  ? -14.387 -36.154 20.369  1.000 129.500 ? 38  ARG HHH NE  1 
ATOM   8682  C CZ  . ARG G 2 39  ? -13.155 -36.070 19.875  1.000 139.212 ? 38  ARG HHH CZ  1 
ATOM   8683  N NH1 . ARG G 2 39  ? -12.609 -37.114 19.269  1.000 143.242 ? 38  ARG HHH NH1 1 
ATOM   8684  N NH2 . ARG G 2 39  ? -12.469 -34.943 19.981  1.000 144.323 ? 38  ARG HHH NH2 1 
ATOM   8685  N N   . GLN G 2 40  ? -19.054 -36.616 23.472  1.000 113.730 ? 39  GLN HHH N   1 
ATOM   8686  C CA  . GLN G 2 40  ? -18.679 -36.366 24.880  1.000 115.353 ? 39  GLN HHH CA  1 
ATOM   8687  C C   . GLN G 2 40  ? -17.576 -37.364 25.211  1.000 116.109 ? 39  GLN HHH C   1 
ATOM   8688  O O   . GLN G 2 40  ? -17.874 -38.575 25.256  1.000 112.946 ? 39  GLN HHH O   1 
ATOM   8689  C CB  . GLN G 2 40  ? -19.902 -36.512 25.782  1.000 115.088 ? 39  GLN HHH CB  1 
ATOM   8690  C CG  . GLN G 2 40  ? -19.598 -36.318 27.256  1.000 116.886 ? 39  GLN HHH CG  1 
ATOM   8691  C CD  . GLN G 2 40  ? -20.813 -35.872 28.024  1.000 118.265 ? 39  GLN HHH CD  1 
ATOM   8692  O OE1 . GLN G 2 40  ? -21.728 -36.654 28.283  1.000 119.636 ? 39  GLN HHH OE1 1 
ATOM   8693  N NE2 . GLN G 2 40  ? -20.818 -34.603 28.399  1.000 118.988 ? 39  GLN HHH NE2 1 
ATOM   8694  N N   . MET G 2 41  ? -16.344 -36.885 25.375  1.000 119.010 ? 40  MET HHH N   1 
ATOM   8695  C CA  . MET G 2 41  ? -15.206 -37.764 25.742  1.000 123.785 ? 40  MET HHH CA  1 
ATOM   8696  C C   . MET G 2 41  ? -15.299 -38.138 27.224  1.000 128.506 ? 40  MET HHH C   1 
ATOM   8697  O O   . MET G 2 41  ? -15.995 -37.473 27.990  1.000 134.770 ? 40  MET HHH O   1 
ATOM   8698  C CB  . MET G 2 41  ? -13.881 -37.071 25.431  1.000 124.452 ? 40  MET HHH CB  1 
ATOM   8699  C CG  . MET G 2 41  ? -13.329 -37.448 24.093  1.000 123.323 ? 40  MET HHH CG  1 
ATOM   8700  S SD  . MET G 2 41  ? -12.026 -36.316 23.632  1.000 126.521 ? 40  MET HHH SD  1 
ATOM   8701  C CE  . MET G 2 41  ? -10.884 -37.462 22.864  1.000 130.146 ? 40  MET HHH CE  1 
ATOM   8702  N N   . PRO G 2 42  ? -14.611 -39.212 27.682  1.000 128.735 ? 41  PRO HHH N   1 
ATOM   8703  C CA  . PRO G 2 42  ? -14.651 -39.615 29.085  1.000 128.876 ? 41  PRO HHH CA  1 
ATOM   8704  C C   . PRO G 2 42  ? -14.499 -38.434 30.056  1.000 131.060 ? 41  PRO HHH C   1 
ATOM   8705  O O   . PRO G 2 42  ? -13.400 -37.918 30.185  1.000 128.439 ? 41  PRO HHH O   1 
ATOM   8706  C CB  . PRO G 2 42  ? -13.444 -40.556 29.207  1.000 131.148 ? 41  PRO HHH CB  1 
ATOM   8707  C CG  . PRO G 2 42  ? -13.317 -41.169 27.839  1.000 130.230 ? 41  PRO HHH CG  1 
ATOM   8708  C CD  . PRO G 2 42  ? -13.716 -40.065 26.886  1.000 130.047 ? 41  PRO HHH CD  1 
ATOM   8709  N N   . GLY G 2 43  ? -15.609 -38.035 30.689  1.000 133.409 ? 42  GLY HHH N   1 
ATOM   8710  C CA  . GLY G 2 43  ? -15.652 -37.018 31.758  1.000 137.706 ? 42  GLY HHH CA  1 
ATOM   8711  C C   . GLY G 2 43  ? -15.287 -35.642 31.239  1.000 138.233 ? 42  GLY HHH C   1 
ATOM   8712  O O   . GLY G 2 43  ? -14.584 -34.897 31.957  1.000 143.652 ? 42  GLY HHH O   1 
ATOM   8713  N N   . LYS G 2 44  ? -15.756 -35.320 30.034  1.000 133.768 ? 43  LYS HHH N   1 
ATOM   8714  C CA  . LYS G 2 44  ? -15.453 -34.053 29.329  1.000 134.215 ? 43  LYS HHH CA  1 
ATOM   8715  C C   . LYS G 2 44  ? -16.761 -33.412 28.874  1.000 131.919 ? 43  LYS HHH C   1 
ATOM   8716  O O   . LYS G 2 44  ? -17.828 -34.036 29.049  1.000 127.400 ? 43  LYS HHH O   1 
ATOM   8717  C CB  . LYS G 2 44  ? -14.591 -34.311 28.094  1.000 135.528 ? 43  LYS HHH CB  1 
ATOM   8718  C CG  . LYS G 2 44  ? -13.389 -35.211 28.316  1.000 137.065 ? 43  LYS HHH CG  1 
ATOM   8719  C CD  . LYS G 2 44  ? -12.213 -34.539 28.959  1.000 140.011 ? 43  LYS HHH CD  1 
ATOM   8720  C CE  . LYS G 2 44  ? -10.927 -35.248 28.588  1.000 141.577 ? 43  LYS HHH CE  1 
ATOM   8721  N NZ  . LYS G 2 44  ? -9.859  -35.005 29.583  1.000 146.771 ? 43  LYS HHH NZ  1 
ATOM   8722  N N   . GLY G 2 45  ? -16.648 -32.227 28.273  1.000 133.081 ? 44  GLY HHH N   1 
ATOM   8723  C CA  . GLY G 2 45  ? -17.780 -31.454 27.735  1.000 130.589 ? 44  GLY HHH CA  1 
ATOM   8724  C C   . GLY G 2 45  ? -18.261 -31.991 26.404  1.000 124.451 ? 44  GLY HHH C   1 
ATOM   8725  O O   . GLY G 2 45  ? -17.688 -32.988 25.903  1.000 122.209 ? 44  GLY HHH O   1 
ATOM   8726  N N   . LEU G 2 46  ? -19.288 -31.338 25.862  1.000 121.286 ? 45  LEU HHH N   1 
ATOM   8727  C CA  . LEU G 2 46  ? -19.971 -31.734 24.608  1.000 120.311 ? 45  LEU HHH CA  1 
ATOM   8728  C C   . LEU G 2 46  ? -19.304 -31.023 23.434  1.000 121.924 ? 45  LEU HHH C   1 
ATOM   8729  O O   . LEU G 2 46  ? -19.268 -29.788 23.452  1.000 126.843 ? 45  LEU HHH O   1 
ATOM   8730  C CB  . LEU G 2 46  ? -21.444 -31.336 24.701  1.000 119.628 ? 45  LEU HHH CB  1 
ATOM   8731  C CG  . LEU G 2 46  ? -22.215 -31.927 25.876  1.000 120.084 ? 45  LEU HHH CG  1 
ATOM   8732  C CD1 . LEU G 2 46  ? -23.613 -31.332 25.947  1.000 120.817 ? 45  LEU HHH CD1 1 
ATOM   8733  C CD2 . LEU G 2 46  ? -22.278 -33.445 25.784  1.000 117.296 ? 45  LEU HHH CD2 1 
ATOM   8734  N N   . GLU G 2 47  ? -18.810 -31.779 22.452  1.000 121.114 ? 46  GLU HHH N   1 
ATOM   8735  C CA  . GLU G 2 47  ? -18.231 -31.238 21.196  1.000 122.008 ? 46  GLU HHH CA  1 
ATOM   8736  C C   . GLU G 2 47  ? -19.225 -31.530 20.072  1.000 118.263 ? 46  GLU HHH C   1 
ATOM   8737  O O   . GLU G 2 47  ? -19.576 -32.706 19.884  1.000 116.222 ? 46  GLU HHH O   1 
ATOM   8738  C CB  . GLU G 2 47  ? -16.866 -31.868 20.898  1.000 126.825 ? 46  GLU HHH CB  1 
ATOM   8739  C CG  . GLU G 2 47  ? -15.944 -31.957 22.105  1.000 132.176 ? 46  GLU HHH CG  1 
ATOM   8740  C CD  . GLU G 2 47  ? -14.763 -32.897 21.938  1.000 134.095 ? 46  GLU HHH CD  1 
ATOM   8741  O OE1 . GLU G 2 47  ? -13.890 -32.587 21.099  1.000 136.376 ? 46  GLU HHH OE1 1 
ATOM   8742  O OE2 . GLU G 2 47  ? -14.727 -33.944 22.644  1.000 134.910 ? 46  GLU HHH OE2 1 
ATOM   8743  N N   . TRP G 2 48  ? -19.680 -30.500 19.365  1.000 117.910 ? 47  TRP HHH N   1 
ATOM   8744  C CA  . TRP G 2 48  ? -20.517 -30.667 18.152  1.000 116.653 ? 47  TRP HHH CA  1 
ATOM   8745  C C   . TRP G 2 48  ? -19.613 -31.070 16.989  1.000 113.580 ? 47  TRP HHH C   1 
ATOM   8746  O O   . TRP G 2 48  ? -18.661 -30.335 16.708  1.000 112.411 ? 47  TRP HHH O   1 
ATOM   8747  C CB  . TRP G 2 48  ? -21.285 -29.383 17.847  1.000 121.552 ? 47  TRP HHH CB  1 
ATOM   8748  C CG  . TRP G 2 48  ? -22.230 -29.520 16.695  1.000 123.823 ? 47  TRP HHH CG  1 
ATOM   8749  C CD1 . TRP G 2 48  ? -23.490 -30.037 16.721  1.000 124.607 ? 47  TRP HHH CD1 1 
ATOM   8750  C CD2 . TRP G 2 48  ? -21.991 -29.130 15.335  1.000 125.774 ? 47  TRP HHH CD2 1 
ATOM   8751  N NE1 . TRP G 2 48  ? -24.052 -29.995 15.473  1.000 124.276 ? 47  TRP HHH NE1 1 
ATOM   8752  C CE2 . TRP G 2 48  ? -23.156 -29.440 14.604  1.000 124.929 ? 47  TRP HHH CE2 1 
ATOM   8753  C CE3 . TRP G 2 48  ? -20.912 -28.543 14.671  1.000 129.932 ? 47  TRP HHH CE3 1 
ATOM   8754  C CZ2 . TRP G 2 48  ? -23.269 -29.182 13.242  1.000 126.743 ? 47  TRP HHH CZ2 1 
ATOM   8755  C CZ3 . TRP G 2 48  ? -21.025 -28.284 13.323  1.000 131.656 ? 47  TRP HHH CZ3 1 
ATOM   8756  C CH2 . TRP G 2 48  ? -22.188 -28.602 12.621  1.000 130.015 ? 47  TRP HHH CH2 1 
ATOM   8757  N N   . MET G 2 49  ? -19.903 -32.202 16.354  1.000 112.008 ? 48  MET HHH N   1 
ATOM   8758  C CA  . MET G 2 49  ? -19.047 -32.801 15.296  1.000 114.561 ? 48  MET HHH CA  1 
ATOM   8759  C C   . MET G 2 49  ? -19.482 -32.279 13.920  1.000 114.596 ? 48  MET HHH C   1 
ATOM   8760  O O   . MET G 2 49  ? -18.621 -31.755 13.183  1.000 114.818 ? 48  MET HHH O   1 
ATOM   8761  C CB  . MET G 2 49  ? -19.157 -34.330 15.306  1.000 114.339 ? 48  MET HHH CB  1 
ATOM   8762  C CG  . MET G 2 49  ? -18.760 -34.977 16.621  1.000 113.436 ? 48  MET HHH CG  1 
ATOM   8763  S SD  . MET G 2 49  ? -18.802 -36.788 16.537  1.000 111.462 ? 48  MET HHH SD  1 
ATOM   8764  C CE  . MET G 2 49  ? -17.295 -37.113 15.624  1.000 112.834 ? 48  MET HHH CE  1 
ATOM   8765  N N   . GLY G 2 50  ? -20.769 -32.444 13.598  1.000 113.768 ? 49  GLY HHH N   1 
ATOM   8766  C CA  . GLY G 2 50  ? -21.363 -32.129 12.286  1.000 113.854 ? 49  GLY HHH CA  1 
ATOM   8767  C C   . GLY G 2 50  ? -22.858 -32.420 12.240  1.000 112.540 ? 49  GLY HHH C   1 
ATOM   8768  O O   . GLY G 2 50  ? -23.347 -33.179 13.094  1.000 110.661 ? 49  GLY HHH O   1 
ATOM   8769  N N   . ILE G 2 51  ? -23.560 -31.835 11.267  1.000 113.310 ? 50  ILE HHH N   1 
ATOM   8770  C CA  . ILE G 2 51  ? -25.011 -32.060 11.007  1.000 113.457 ? 50  ILE HHH CA  1 
ATOM   8771  C C   . ILE G 2 51  ? -25.181 -32.461 9.544   1.000 113.139 ? 50  ILE HHH C   1 
ATOM   8772  O O   . ILE G 2 51  ? -24.371 -32.016 8.703   1.000 111.910 ? 50  ILE HHH O   1 
ATOM   8773  C CB  . ILE G 2 51  ? -25.846 -30.811 11.354  1.000 116.145 ? 50  ILE HHH CB  1 
ATOM   8774  C CG1 . ILE G 2 51  ? -27.348 -31.109 11.408  1.000 120.643 ? 50  ILE HHH CG1 1 
ATOM   8775  C CG2 . ILE G 2 51  ? -25.544 -29.669 10.403  1.000 115.813 ? 50  ILE HHH CG2 1 
ATOM   8776  C CD1 . ILE G 2 51  ? -28.087 -30.375 12.535  1.000 124.638 ? 50  ILE HHH CD1 1 
ATOM   8777  N N   . ILE G 2 52  ? -26.205 -33.269 9.268   1.000 112.973 ? 51  ILE HHH N   1 
ATOM   8778  C CA  . ILE G 2 52  ? -26.636 -33.624 7.887   1.000 113.218 ? 51  ILE HHH CA  1 
ATOM   8779  C C   . ILE G 2 52  ? -28.149 -33.457 7.781   1.000 113.110 ? 51  ILE HHH C   1 
ATOM   8780  O O   . ILE G 2 52  ? -28.850 -33.749 8.772   1.000 114.235 ? 51  ILE HHH O   1 
ATOM   8781  C CB  . ILE G 2 52  ? -26.226 -35.055 7.521   1.000 113.144 ? 51  ILE HHH CB  1 
ATOM   8782  C CG1 . ILE G 2 52  ? -26.404 -35.302 6.024   1.000 114.438 ? 51  ILE HHH CG1 1 
ATOM   8783  C CG2 . ILE G 2 52  ? -26.993 -36.066 8.361   1.000 113.283 ? 51  ILE HHH CG2 1 
ATOM   8784  C CD1 . ILE G 2 52  ? -25.731 -36.565 5.543   1.000 117.585 ? 51  ILE HHH CD1 1 
ATOM   8785  N N   . TYR G 2 53  ? -28.610 -33.011 6.613   1.000 112.951 ? 52  TYR HHH N   1 
ATOM   8786  C CA  . TYR G 2 53  ? -30.039 -33.002 6.224   1.000 111.540 ? 52  TYR HHH CA  1 
ATOM   8787  C C   . TYR G 2 53  ? -30.278 -34.208 5.325   1.000 109.716 ? 52  TYR HHH C   1 
ATOM   8788  O O   . TYR G 2 53  ? -29.954 -34.170 4.143   1.000 110.322 ? 52  TYR HHH O   1 
ATOM   8789  C CB  . TYR G 2 53  ? -30.439 -31.685 5.552   1.000 112.179 ? 52  TYR HHH CB  1 
ATOM   8790  C CG  . TYR G 2 53  ? -31.869 -31.694 5.074   1.000 112.960 ? 52  TYR HHH CG  1 
ATOM   8791  C CD1 . TYR G 2 53  ? -32.899 -32.039 5.935   1.000 113.691 ? 52  TYR HHH CD1 1 
ATOM   8792  C CD2 . TYR G 2 53  ? -32.195 -31.421 3.759   1.000 113.793 ? 52  TYR HHH CD2 1 
ATOM   8793  C CE1 . TYR G 2 53  ? -34.216 -32.091 5.512   1.000 112.802 ? 52  TYR HHH CE1 1 
ATOM   8794  C CE2 . TYR G 2 53  ? -33.508 -31.471 3.320   1.000 114.955 ? 52  TYR HHH CE2 1 
ATOM   8795  C CZ  . TYR G 2 53  ? -34.525 -31.804 4.197   1.000 113.347 ? 52  TYR HHH CZ  1 
ATOM   8796  O OH  . TYR G 2 53  ? -35.820 -31.856 3.773   1.000 113.210 ? 52  TYR HHH OH  1 
ATOM   8797  N N   . PRO G 2 54  ? -30.854 -35.306 5.859   1.000 107.570 ? 53  PRO HHH N   1 
ATOM   8798  C CA  . PRO G 2 54  ? -31.060 -36.530 5.090   1.000 110.116 ? 53  PRO HHH CA  1 
ATOM   8799  C C   . PRO G 2 54  ? -31.666 -36.289 3.701   1.000 115.467 ? 53  PRO HHH C   1 
ATOM   8800  O O   . PRO G 2 54  ? -31.320 -37.024 2.780   1.000 118.062 ? 53  PRO HHH O   1 
ATOM   8801  C CB  . PRO G 2 54  ? -32.068 -37.311 5.938   1.000 109.007 ? 53  PRO HHH CB  1 
ATOM   8802  C CG  . PRO G 2 54  ? -31.834 -36.843 7.347   1.000 107.366 ? 53  PRO HHH CG  1 
ATOM   8803  C CD  . PRO G 2 54  ? -31.376 -35.409 7.226   1.000 106.190 ? 53  PRO HHH CD  1 
ATOM   8804  N N   . GLY G 2 55  ? -32.554 -35.289 3.604   1.000 117.780 ? 54  GLY HHH N   1 
ATOM   8805  C CA  . GLY G 2 55  ? -33.284 -34.909 2.379   1.000 121.451 ? 54  GLY HHH CA  1 
ATOM   8806  C C   . GLY G 2 55  ? -32.372 -34.868 1.170   1.000 125.323 ? 54  GLY HHH C   1 
ATOM   8807  O O   . GLY G 2 55  ? -32.468 -35.783 0.343   1.000 130.538 ? 54  GLY HHH O   1 
ATOM   8808  N N   . ASP G 2 56  ? -31.507 -33.854 1.077   1.000 127.371 ? 55  ASP HHH N   1 
ATOM   8809  C CA  . ASP G 2 56  ? -30.530 -33.699 -0.035  1.000 131.550 ? 55  ASP HHH CA  1 
ATOM   8810  C C   . ASP G 2 56  ? -29.122 -33.983 0.497   1.000 129.595 ? 55  ASP HHH C   1 
ATOM   8811  O O   . ASP G 2 56  ? -28.153 -33.542 -0.149  1.000 135.786 ? 55  ASP HHH O   1 
ATOM   8812  C CB  . ASP G 2 56  ? -30.632 -32.323 -0.708  1.000 135.375 ? 55  ASP HHH CB  1 
ATOM   8813  C CG  . ASP G 2 56  ? -30.424 -31.117 0.203   1.000 137.067 ? 55  ASP HHH CG  1 
ATOM   8814  O OD1 . ASP G 2 56  ? -30.005 -31.301 1.364   1.000 138.255 ? 55  ASP HHH OD1 1 
ATOM   8815  O OD2 . ASP G 2 56  ? -30.680 -29.996 -0.263  1.000 141.476 ? 55  ASP HHH OD2 1 
ATOM   8816  N N   . SER G 2 57  ? -29.016 -34.687 1.627   1.000 123.807 ? 56  SER HHH N   1 
ATOM   8817  C CA  . SER G 2 57  ? -27.729 -35.073 2.258   1.000 122.337 ? 56  SER HHH CA  1 
ATOM   8818  C C   . SER G 2 57  ? -26.760 -33.877 2.274   1.000 120.897 ? 56  SER HHH C   1 
ATOM   8819  O O   . SER G 2 57  ? -25.561 -34.080 2.011   1.000 120.497 ? 56  SER HHH O   1 
ATOM   8820  C CB  . SER G 2 57  ? -27.159 -36.282 1.558   1.000 124.296 ? 56  SER HHH CB  1 
ATOM   8821  O OG  . SER G 2 57  ? -28.094 -37.359 1.573   1.000 124.501 ? 56  SER HHH OG  1 
ATOM   8822  N N   . GLU G 2 58  ? -27.276 -32.677 2.579   1.000 120.943 ? 57  GLU HHH N   1 
ATOM   8823  C CA  . GLU G 2 58  ? -26.502 -31.416 2.784   1.000 121.986 ? 57  GLU HHH CA  1 
ATOM   8824  C C   . GLU G 2 58  ? -25.770 -31.531 4.121   1.000 121.110 ? 57  GLU HHH C   1 
ATOM   8825  O O   . GLU G 2 58  ? -26.438 -31.470 5.165   1.000 123.654 ? 57  GLU HHH O   1 
ATOM   8826  C CB  . GLU G 2 58  ? -27.426 -30.190 2.774   1.000 122.164 ? 57  GLU HHH CB  1 
ATOM   8827  C CG  . GLU G 2 58  ? -26.782 -28.888 3.246   1.000 121.328 ? 57  GLU HHH CG  1 
ATOM   8828  C CD  . GLU G 2 58  ? -27.670 -27.652 3.129   1.000 122.627 ? 57  GLU HHH CD  1 
ATOM   8829  O OE1 . GLU G 2 58  ? -28.917 -27.805 3.002   1.000 120.849 ? 57  GLU HHH OE1 1 
ATOM   8830  O OE2 . GLU G 2 58  ? -27.122 -26.528 3.171   1.000 124.147 ? 57  GLU HHH OE2 1 
ATOM   8831  N N   . THR G 2 59  ? -24.452 -31.702 4.080   1.000 121.872 ? 58  THR HHH N   1 
ATOM   8832  C CA  . THR G 2 59  ? -23.616 -32.090 5.244   1.000 121.741 ? 58  THR HHH CA  1 
ATOM   8833  C C   . THR G 2 59  ? -22.703 -30.920 5.620   1.000 120.976 ? 58  THR HHH C   1 
ATOM   8834  O O   . THR G 2 59  ? -22.100 -30.338 4.687   1.000 125.146 ? 58  THR HHH O   1 
ATOM   8835  C CB  . THR G 2 59  ? -22.807 -33.347 4.900   1.000 125.946 ? 58  THR HHH CB  1 
ATOM   8836  O OG1 . THR G 2 59  ? -23.640 -34.213 4.125   1.000 126.179 ? 58  THR HHH OG1 1 
ATOM   8837  C CG2 . THR G 2 59  ? -22.293 -34.073 6.124   1.000 127.157 ? 58  THR HHH CG2 1 
ATOM   8838  N N   . ARG G 2 60  ? -22.607 -30.592 6.914   1.000 116.580 ? 59  ARG HHH N   1 
ATOM   8839  C CA  . ARG G 2 60  ? -21.641 -29.592 7.451   1.000 117.925 ? 59  ARG HHH CA  1 
ATOM   8840  C C   . ARG G 2 60  ? -20.835 -30.232 8.576   1.000 117.204 ? 59  ARG HHH C   1 
ATOM   8841  O O   . ARG G 2 60  ? -21.432 -31.001 9.330   1.000 117.878 ? 59  ARG HHH O   1 
ATOM   8842  C CB  . ARG G 2 60  ? -22.364 -28.346 7.960   1.000 116.911 ? 59  ARG HHH CB  1 
ATOM   8843  C CG  . ARG G 2 60  ? -23.345 -27.780 6.949   1.000 118.803 ? 59  ARG HHH CG  1 
ATOM   8844  C CD  . ARG G 2 60  ? -23.929 -26.442 7.346   1.000 119.800 ? 59  ARG HHH CD  1 
ATOM   8845  N NE  . ARG G 2 60  ? -25.047 -26.128 6.474   1.000 121.306 ? 59  ARG HHH NE  1 
ATOM   8846  C CZ  . ARG G 2 60  ? -25.912 -25.144 6.672   1.000 124.768 ? 59  ARG HHH CZ  1 
ATOM   8847  N NH1 . ARG G 2 60  ? -25.798 -24.352 7.725   1.000 126.150 ? 59  ARG HHH NH1 1 
ATOM   8848  N NH2 . ARG G 2 60  ? -26.894 -24.956 5.807   1.000 127.861 ? 59  ARG HHH NH2 1 
ATOM   8849  N N   . TYR G 2 61  ? -19.540 -29.928 8.668   1.000 119.228 ? 60  TYR HHH N   1 
ATOM   8850  C CA  . TYR G 2 61  ? -18.623 -30.482 9.696   1.000 119.941 ? 60  TYR HHH CA  1 
ATOM   8851  C C   . TYR G 2 61  ? -18.076 -29.342 10.553  1.000 118.605 ? 60  TYR HHH C   1 
ATOM   8852  O O   . TYR G 2 61  ? -17.966 -28.209 10.067  1.000 117.235 ? 60  TYR HHH O   1 
ATOM   8853  C CB  . TYR G 2 61  ? -17.483 -31.274 9.049   1.000 125.414 ? 60  TYR HHH CB  1 
ATOM   8854  C CG  . TYR G 2 61  ? -17.911 -32.516 8.308   1.000 127.773 ? 60  TYR HHH CG  1 
ATOM   8855  C CD1 . TYR G 2 61  ? -18.378 -33.626 8.990   1.000 127.018 ? 60  TYR HHH CD1 1 
ATOM   8856  C CD2 . TYR G 2 61  ? -17.837 -32.592 6.925   1.000 132.673 ? 60  TYR HHH CD2 1 
ATOM   8857  C CE1 . TYR G 2 61  ? -18.774 -34.772 8.321   1.000 128.755 ? 60  TYR HHH CE1 1 
ATOM   8858  C CE2 . TYR G 2 61  ? -18.230 -33.732 6.241   1.000 133.957 ? 60  TYR HHH CE2 1 
ATOM   8859  C CZ  . TYR G 2 61  ? -18.705 -34.825 6.942   1.000 131.998 ? 60  TYR HHH CZ  1 
ATOM   8860  O OH  . TYR G 2 61  ? -19.103 -35.953 6.284   1.000 135.660 ? 60  TYR HHH OH  1 
ATOM   8861  N N   . SER G 2 62  ? -17.753 -29.648 11.806  1.000 119.224 ? 61  SER HHH N   1 
ATOM   8862  C CA  . SER G 2 62  ? -16.859 -28.824 12.653  1.000 124.534 ? 61  SER HHH CA  1 
ATOM   8863  C C   . SER G 2 62  ? -15.474 -28.874 12.026  1.000 128.363 ? 61  SER HHH C   1 
ATOM   8864  O O   . SER G 2 62  ? -15.066 -29.934 11.550  1.000 133.747 ? 61  SER HHH O   1 
ATOM   8865  C CB  . SER G 2 62  ? -16.816 -29.326 14.074  1.000 126.445 ? 61  SER HHH CB  1 
ATOM   8866  O OG  . SER G 2 62  ? -15.762 -28.708 14.807  1.000 130.507 ? 61  SER HHH OG  1 
ATOM   8867  N N   . PRO G 2 63  ? -14.717 -27.754 12.005  1.000 128.934 ? 62  PRO HHH N   1 
ATOM   8868  C CA  . PRO G 2 63  ? -13.326 -27.779 11.547  1.000 131.242 ? 62  PRO HHH CA  1 
ATOM   8869  C C   . PRO G 2 63  ? -12.501 -28.872 12.248  1.000 130.832 ? 62  PRO HHH C   1 
ATOM   8870  O O   . PRO G 2 63  ? -11.586 -29.404 11.647  1.000 131.897 ? 62  PRO HHH O   1 
ATOM   8871  C CB  . PRO G 2 63  ? -12.802 -26.383 11.915  1.000 134.008 ? 62  PRO HHH CB  1 
ATOM   8872  C CG  . PRO G 2 63  ? -14.040 -25.510 11.943  1.000 132.443 ? 62  PRO HHH CG  1 
ATOM   8873  C CD  . PRO G 2 63  ? -15.159 -26.413 12.416  1.000 128.526 ? 62  PRO HHH CD  1 
ATOM   8874  N N   . SER G 2 64  ? -12.876 -29.191 13.490  1.000 129.876 ? 63  SER HHH N   1 
ATOM   8875  C CA  . SER G 2 64  ? -12.221 -30.190 14.374  1.000 131.729 ? 63  SER HHH CA  1 
ATOM   8876  C C   . SER G 2 64  ? -12.579 -31.626 13.967  1.000 130.190 ? 63  SER HHH C   1 
ATOM   8877  O O   . SER G 2 64  ? -12.227 -32.548 14.745  1.000 133.711 ? 63  SER HHH O   1 
ATOM   8878  C CB  . SER G 2 64  ? -12.607 -29.944 15.809  1.000 132.252 ? 63  SER HHH CB  1 
ATOM   8879  O OG  . SER G 2 64  ? -12.567 -28.561 16.114  1.000 135.445 ? 63  SER HHH OG  1 
ATOM   8880  N N   . PHE G 2 65  ? -13.266 -31.823 12.834  1.000 127.107 ? 64  PHE HHH N   1 
ATOM   8881  C CA  . PHE G 2 65  ? -13.676 -33.167 12.344  1.000 123.887 ? 64  PHE HHH CA  1 
ATOM   8882  C C   . PHE G 2 65  ? -13.595 -33.277 10.811  1.000 125.710 ? 64  PHE HHH C   1 
ATOM   8883  O O   . PHE G 2 65  ? -13.353 -34.411 10.342  1.000 126.335 ? 64  PHE HHH O   1 
ATOM   8884  C CB  . PHE G 2 65  ? -15.045 -33.521 12.931  1.000 118.293 ? 64  PHE HHH CB  1 
ATOM   8885  C CG  . PHE G 2 65  ? -15.020 -33.726 14.426  1.000 116.447 ? 64  PHE HHH CG  1 
ATOM   8886  C CD1 . PHE G 2 65  ? -14.455 -34.867 14.979  1.000 116.245 ? 64  PHE HHH CD1 1 
ATOM   8887  C CD2 . PHE G 2 65  ? -15.516 -32.759 15.287  1.000 116.015 ? 64  PHE HHH CD2 1 
ATOM   8888  C CE1 . PHE G 2 65  ? -14.415 -35.053 16.352  1.000 115.270 ? 64  PHE HHH CE1 1 
ATOM   8889  C CE2 . PHE G 2 65  ? -15.484 -32.952 16.662  1.000 115.385 ? 64  PHE HHH CE2 1 
ATOM   8890  C CZ  . PHE G 2 65  ? -14.934 -34.097 17.193  1.000 114.615 ? 64  PHE HHH CZ  1 
ATOM   8891  N N   . GLN G 2 66  ? -13.737 -32.177 10.059  1.000 126.355 ? 65  GLN HHH N   1 
ATOM   8892  C CA  . GLN G 2 66  ? -13.779 -32.178 8.569   1.000 128.932 ? 65  GLN HHH CA  1 
ATOM   8893  C C   . GLN G 2 66  ? -13.209 -33.504 8.043   1.000 129.577 ? 65  GLN HHH C   1 
ATOM   8894  O O   . GLN G 2 66  ? -14.002 -34.335 7.549   1.000 127.848 ? 65  GLN HHH O   1 
ATOM   8895  C CB  . GLN G 2 66  ? -13.028 -30.965 8.008   1.000 134.446 ? 65  GLN HHH CB  1 
ATOM   8896  C CG  . GLN G 2 66  ? -13.002 -30.864 6.478   1.000 139.120 ? 65  GLN HHH CG  1 
ATOM   8897  C CD  . GLN G 2 66  ? -14.346 -30.686 5.801   1.000 138.897 ? 65  GLN HHH CD  1 
ATOM   8898  O OE1 . GLN G 2 66  ? -15.184 -29.873 6.202   1.000 139.268 ? 65  GLN HHH OE1 1 
ATOM   8899  N NE2 . GLN G 2 66  ? -14.556 -31.420 4.717   1.000 139.324 ? 65  GLN HHH NE2 1 
ATOM   8900  N N   . GLY G 2 67  ? -11.897 -33.710 8.194   1.000 132.655 ? 66  GLY HHH N   1 
ATOM   8901  C CA  . GLY G 2 67  ? -11.130 -34.765 7.502   1.000 137.805 ? 66  GLY HHH CA  1 
ATOM   8902  C C   . GLY G 2 67  ? -10.843 -35.971 8.372   1.000 138.762 ? 66  GLY HHH C   1 
ATOM   8903  O O   . GLY G 2 67  ? -9.857  -36.686 8.096   1.000 141.624 ? 66  GLY HHH O   1 
ATOM   8904  N N   . GLN G 2 68  ? -11.670 -36.198 9.387   1.000 138.100 ? 67  GLN HHH N   1 
ATOM   8905  C CA  . GLN G 2 68  ? -11.622 -37.420 10.226  1.000 141.356 ? 67  GLN HHH CA  1 
ATOM   8906  C C   . GLN G 2 68  ? -12.736 -38.360 9.752   1.000 141.123 ? 67  GLN HHH C   1 
ATOM   8907  O O   . GLN G 2 68  ? -12.432 -39.459 9.208   1.000 145.081 ? 67  GLN HHH O   1 
ATOM   8908  C CB  . GLN G 2 68  ? -11.764 -37.029 11.698  1.000 139.685 ? 67  GLN HHH CB  1 
ATOM   8909  C CG  . GLN G 2 68  ? -10.705 -36.036 12.161  1.000 141.571 ? 67  GLN HHH CG  1 
ATOM   8910  C CD  . GLN G 2 68  ? -9.387  -36.712 12.438  1.000 143.510 ? 67  GLN HHH CD  1 
ATOM   8911  O OE1 . GLN G 2 68  ? -9.268  -37.500 13.378  1.000 141.632 ? 67  GLN HHH OE1 1 
ATOM   8912  N NE2 . GLN G 2 68  ? -8.393  -36.407 11.615  1.000 145.399 ? 67  GLN HHH NE2 1 
ATOM   8913  N N   . VAL G 2 69  ? -13.978 -37.886 9.880   1.000 136.221 ? 68  VAL HHH N   1 
ATOM   8914  C CA  . VAL G 2 69  ? -15.207 -38.729 9.924   1.000 130.617 ? 68  VAL HHH CA  1 
ATOM   8915  C C   . VAL G 2 69  ? -16.181 -38.315 8.817   1.000 129.102 ? 68  VAL HHH C   1 
ATOM   8916  O O   . VAL G 2 69  ? -16.207 -37.118 8.449   1.000 129.311 ? 68  VAL HHH O   1 
ATOM   8917  C CB  . VAL G 2 69  ? -15.847 -38.626 11.316  1.000 124.508 ? 68  VAL HHH CB  1 
ATOM   8918  C CG1 . VAL G 2 69  ? -14.833 -38.976 12.389  1.000 125.127 ? 68  VAL HHH CG1 1 
ATOM   8919  C CG2 . VAL G 2 69  ? -16.448 -37.252 11.569  1.000 121.625 ? 68  VAL HHH CG2 1 
ATOM   8920  N N   . THR G 2 70  ? -16.946 -39.291 8.320   1.000 127.008 ? 69  THR HHH N   1 
ATOM   8921  C CA  . THR G 2 70  ? -18.018 -39.131 7.305   1.000 125.837 ? 69  THR HHH CA  1 
ATOM   8922  C C   . THR G 2 70  ? -19.373 -39.309 8.003   1.000 123.112 ? 69  THR HHH C   1 
ATOM   8923  O O   . THR G 2 70  ? -19.594 -40.365 8.653   1.000 121.714 ? 69  THR HHH O   1 
ATOM   8924  C CB  . THR G 2 70  ? -17.822 -40.092 6.121   1.000 128.459 ? 69  THR HHH CB  1 
ATOM   8925  O OG1 . THR G 2 70  ? -16.653 -39.710 5.399   1.000 131.731 ? 69  THR HHH OG1 1 
ATOM   8926  C CG2 . THR G 2 70  ? -18.973 -40.095 5.140   1.000 128.312 ? 69  THR HHH CG2 1 
ATOM   8927  N N   . ILE G 2 71  ? -20.226 -38.288 7.891   1.000 120.871 ? 70  ILE HHH N   1 
ATOM   8928  C CA  . ILE G 2 71  ? -21.662 -38.335 8.280   1.000 118.564 ? 70  ILE HHH CA  1 
ATOM   8929  C C   . ILE G 2 71  ? -22.468 -38.602 7.008   1.000 120.121 ? 70  ILE HHH C   1 
ATOM   8930  O O   . ILE G 2 71  ? -22.440 -37.737 6.115   1.000 119.037 ? 70  ILE HHH O   1 
ATOM   8931  C CB  . ILE G 2 71  ? -22.077 -37.019 8.959   1.000 117.194 ? 70  ILE HHH CB  1 
ATOM   8932  C CG1 . ILE G 2 71  ? -21.315 -36.802 10.269  1.000 117.386 ? 70  ILE HHH CG1 1 
ATOM   8933  C CG2 . ILE G 2 71  ? -23.582 -36.972 9.169   1.000 116.926 ? 70  ILE HHH CG2 1 
ATOM   8934  C CD1 . ILE G 2 71  ? -21.441 -35.406 10.847  1.000 116.959 ? 70  ILE HHH CD1 1 
ATOM   8935  N N   . SER G 2 72  ? -23.119 -39.767 6.924   1.000 122.774 ? 71  SER HHH N   1 
ATOM   8936  C CA  . SER G 2 72  ? -24.001 -40.184 5.799   1.000 125.047 ? 71  SER HHH CA  1 
ATOM   8937  C C   . SER G 2 72  ? -25.459 -40.184 6.270   1.000 120.676 ? 71  SER HHH C   1 
ATOM   8938  O O   . SER G 2 72  ? -25.702 -40.035 7.480   1.000 117.489 ? 71  SER HHH O   1 
ATOM   8939  C CB  . SER G 2 72  ? -23.580 -41.535 5.229   1.000 130.411 ? 71  SER HHH CB  1 
ATOM   8940  O OG  . SER G 2 72  ? -22.941 -42.350 6.208   1.000 130.579 ? 71  SER HHH OG  1 
ATOM   8941  N N   . ALA G 2 73  ? -26.397 -40.341 5.341   1.000 121.067 ? 72  ALA HHH N   1 
ATOM   8942  C CA  . ALA G 2 73  ? -27.841 -40.403 5.643   1.000 121.124 ? 72  ALA HHH CA  1 
ATOM   8943  C C   . ALA G 2 73  ? -28.563 -41.195 4.554   1.000 124.226 ? 72  ALA HHH C   1 
ATOM   8944  O O   . ALA G 2 73  ? -28.590 -40.729 3.391   1.000 126.944 ? 72  ALA HHH O   1 
ATOM   8945  C CB  . ALA G 2 73  ? -28.393 -39.009 5.776   1.000 120.394 ? 72  ALA HHH CB  1 
ATOM   8946  N N   . ASP G 2 74  ? -29.099 -42.355 4.934   1.000 124.245 ? 73  ASP HHH N   1 
ATOM   8947  C CA  . ASP G 2 74  ? -30.010 -43.177 4.101   1.000 127.391 ? 73  ASP HHH CA  1 
ATOM   8948  C C   . ASP G 2 74  ? -31.437 -42.741 4.432   1.000 124.108 ? 73  ASP HHH C   1 
ATOM   8949  O O   . ASP G 2 74  ? -32.067 -43.372 5.297   1.000 122.886 ? 73  ASP HHH O   1 
ATOM   8950  C CB  . ASP G 2 74  ? -29.762 -44.670 4.341   1.000 132.087 ? 73  ASP HHH CB  1 
ATOM   8951  C CG  . ASP G 2 74  ? -30.320 -45.596 3.269   1.000 136.738 ? 73  ASP HHH CG  1 
ATOM   8952  O OD1 . ASP G 2 74  ? -30.956 -45.088 2.313   1.000 137.581 ? 73  ASP HHH OD1 1 
ATOM   8953  O OD2 . ASP G 2 74  ? -30.103 -46.826 3.393   1.000 138.571 ? 73  ASP HHH OD2 1 
ATOM   8954  N N   . LYS G 2 75  ? -31.910 -41.681 3.776   1.000 123.783 ? 74  LYS HHH N   1 
ATOM   8955  C CA  . LYS G 2 75  ? -33.203 -41.020 4.085   1.000 123.811 ? 74  LYS HHH CA  1 
ATOM   8956  C C   . LYS G 2 75  ? -34.367 -42.008 3.939   1.000 123.026 ? 74  LYS HHH C   1 
ATOM   8957  O O   . LYS G 2 75  ? -35.412 -41.757 4.556   1.000 121.266 ? 74  LYS HHH O   1 
ATOM   8958  C CB  . LYS G 2 75  ? -33.390 -39.805 3.176   1.000 127.021 ? 74  LYS HHH CB  1 
ATOM   8959  C CG  . LYS G 2 75  ? -33.586 -40.109 1.700   1.000 132.638 ? 74  LYS HHH CG  1 
ATOM   8960  C CD  . LYS G 2 75  ? -33.963 -38.867 0.927   1.000 136.479 ? 74  LYS HHH CD  1 
ATOM   8961  C CE  . LYS G 2 75  ? -34.640 -39.151 -0.397  1.000 143.228 ? 74  LYS HHH CE  1 
ATOM   8962  N NZ  . LYS G 2 75  ? -35.215 -37.911 -0.975  1.000 145.669 ? 74  LYS HHH NZ  1 
ATOM   8963  N N   . SER G 2 76  ? -34.182 -43.084 3.166   1.000 124.322 ? 75  SER HHH N   1 
ATOM   8964  C CA  . SER G 2 76  ? -35.209 -44.116 2.848   1.000 126.766 ? 75  SER HHH CA  1 
ATOM   8965  C C   . SER G 2 76  ? -35.527 -44.992 4.063   1.000 124.940 ? 75  SER HHH C   1 
ATOM   8966  O O   . SER G 2 76  ? -36.445 -45.826 3.933   1.000 126.741 ? 75  SER HHH O   1 
ATOM   8967  C CB  . SER G 2 76  ? -34.781 -44.992 1.696   1.000 131.634 ? 75  SER HHH CB  1 
ATOM   8968  O OG  . SER G 2 76  ? -34.069 -46.134 2.160   1.000 131.727 ? 75  SER HHH OG  1 
ATOM   8969  N N   . ILE G 2 77  ? -34.768 -44.874 5.160   1.000 121.648 ? 76  ILE HHH N   1 
ATOM   8970  C CA  . ILE G 2 77  ? -35.094 -45.536 6.462   1.000 121.138 ? 76  ILE HHH CA  1 
ATOM   8971  C C   . ILE G 2 77  ? -34.928 -44.533 7.610   1.000 115.434 ? 76  ILE HHH C   1 
ATOM   8972  O O   . ILE G 2 77  ? -34.735 -44.968 8.758   1.000 111.885 ? 76  ILE HHH O   1 
ATOM   8973  C CB  . ILE G 2 77  ? -34.259 -46.817 6.670   1.000 124.757 ? 76  ILE HHH CB  1 
ATOM   8974  C CG1 . ILE G 2 77  ? -32.766 -46.597 6.410   1.000 126.314 ? 76  ILE HHH CG1 1 
ATOM   8975  C CG2 . ILE G 2 77  ? -34.809 -47.949 5.819   1.000 128.710 ? 76  ILE HHH CG2 1 
ATOM   8976  C CD1 . ILE G 2 77  ? -31.870 -47.664 7.029   1.000 127.631 ? 76  ILE HHH CD1 1 
ATOM   8977  N N   . ASN G 2 78  ? -35.050 -43.238 7.317   1.000 114.701 ? 77  ASN HHH N   1 
ATOM   8978  C CA  . ASN G 2 78  ? -34.937 -42.158 8.326   1.000 114.494 ? 77  ASN HHH CA  1 
ATOM   8979  C C   . ASN G 2 78  ? -33.711 -42.433 9.201   1.000 113.443 ? 77  ASN HHH C   1 
ATOM   8980  O O   . ASN G 2 78  ? -33.800 -42.224 10.422  1.000 115.422 ? 77  ASN HHH O   1 
ATOM   8981  C CB  . ASN G 2 78  ? -36.201 -42.059 9.184   1.000 116.561 ? 77  ASN HHH CB  1 
ATOM   8982  C CG  . ASN G 2 78  ? -37.395 -41.480 8.456   1.000 120.521 ? 77  ASN HHH CG  1 
ATOM   8983  O OD1 . ASN G 2 78  ? -37.256 -40.956 7.352   1.000 123.845 ? 77  ASN HHH OD1 1 
ATOM   8984  N ND2 . ASN G 2 78  ? -38.571 -41.555 9.072   1.000 121.531 ? 77  ASN HHH ND2 1 
ATOM   8985  N N   . THR G 2 79  ? -32.611 -42.897 8.610   1.000 111.819 ? 78  THR HHH N   1 
ATOM   8986  C CA  . THR G 2 79  ? -31.389 -43.281 9.353   1.000 109.445 ? 78  THR HHH CA  1 
ATOM   8987  C C   . THR G 2 79  ? -30.232 -42.383 8.928   1.000 107.581 ? 78  THR HHH C   1 
ATOM   8988  O O   . THR G 2 79  ? -29.804 -42.478 7.769   1.000 108.073 ? 78  THR HHH O   1 
ATOM   8989  C CB  . THR G 2 79  ? -31.048 -44.760 9.151   1.000 112.620 ? 78  THR HHH CB  1 
ATOM   8990  O OG1 . THR G 2 79  ? -32.189 -45.534 9.525   1.000 113.638 ? 78  THR HHH OG1 1 
ATOM   8991  C CG2 . THR G 2 79  ? -29.851 -45.190 9.968   1.000 114.143 ? 78  THR HHH CG2 1 
ATOM   8992  N N   . ALA G 2 80  ? -29.753 -41.552 9.847   1.000 107.158 ? 79  ALA HHH N   1 
ATOM   8993  C CA  . ALA G 2 80  ? -28.445 -40.873 9.745   1.000 109.070 ? 79  ALA HHH CA  1 
ATOM   8994  C C   . ALA G 2 80  ? -27.361 -41.780 10.349  1.000 111.222 ? 79  ALA HHH C   1 
ATOM   8995  O O   . ALA G 2 80  ? -27.644 -42.515 11.329  1.000 108.771 ? 79  ALA HHH O   1 
ATOM   8996  C CB  . ALA G 2 80  ? -28.508 -39.528 10.413  1.000 107.867 ? 79  ALA HHH CB  1 
ATOM   8997  N N   . TYR G 2 81  ? -26.176 -41.759 9.739   1.000 113.907 ? 80  TYR HHH N   1 
ATOM   8998  C CA  . TYR G 2 81  ? -24.989 -42.553 10.134  1.000 114.566 ? 80  TYR HHH CA  1 
ATOM   8999  C C   . TYR G 2 81  ? -23.820 -41.612 10.415  1.000 116.179 ? 80  TYR HHH C   1 
ATOM   9000  O O   . TYR G 2 81  ? -23.811 -40.462 9.944   1.000 115.241 ? 80  TYR HHH O   1 
ATOM   9001  C CB  . TYR G 2 81  ? -24.550 -43.509 9.025   1.000 117.051 ? 80  TYR HHH CB  1 
ATOM   9002  C CG  . TYR G 2 81  ? -25.582 -44.517 8.593   1.000 119.620 ? 80  TYR HHH CG  1 
ATOM   9003  C CD1 . TYR G 2 81  ? -26.018 -45.510 9.455   1.000 121.161 ? 80  TYR HHH CD1 1 
ATOM   9004  C CD2 . TYR G 2 81  ? -26.110 -44.491 7.310   1.000 122.058 ? 80  TYR HHH CD2 1 
ATOM   9005  C CE1 . TYR G 2 81  ? -26.956 -46.450 9.051   1.000 123.431 ? 80  TYR HHH CE1 1 
ATOM   9006  C CE2 . TYR G 2 81  ? -27.054 -45.415 6.894   1.000 123.229 ? 80  TYR HHH CE2 1 
ATOM   9007  C CZ  . TYR G 2 81  ? -27.473 -46.404 7.765   1.000 123.527 ? 80  TYR HHH CZ  1 
ATOM   9008  O OH  . TYR G 2 81  ? -28.402 -47.310 7.345   1.000 124.584 ? 80  TYR HHH OH  1 
ATOM   9009  N N   . LEU G 2 82  ? -22.852 -42.132 11.164  1.000 120.414 ? 81  LEU HHH N   1 
ATOM   9010  C CA  . LEU G 2 82  ? -21.511 -41.542 11.415  1.000 121.226 ? 81  LEU HHH CA  1 
ATOM   9011  C C   . LEU G 2 82  ? -20.499 -42.687 11.331  1.000 122.230 ? 81  LEU HHH C   1 
ATOM   9012  O O   . LEU G 2 82  ? -20.759 -43.738 11.963  1.000 122.180 ? 81  LEU HHH O   1 
ATOM   9013  C CB  . LEU G 2 82  ? -21.508 -40.895 12.806  1.000 119.670 ? 81  LEU HHH CB  1 
ATOM   9014  C CG  . LEU G 2 82  ? -20.143 -40.455 13.329  1.000 119.310 ? 81  LEU HHH CG  1 
ATOM   9015  C CD1 . LEU G 2 82  ? -19.663 -39.230 12.575  1.000 119.622 ? 81  LEU HHH CD1 1 
ATOM   9016  C CD2 . LEU G 2 82  ? -20.193 -40.176 14.820  1.000 118.376 ? 81  LEU HHH CD2 1 
ATOM   9017  N N   . GLN G 2 83  ? -19.408 -42.525 10.577  1.000 121.250 ? 82  GLN HHH N   1 
ATOM   9018  C CA  . GLN G 2 83  ? -18.424 -43.625 10.406  1.000 122.618 ? 82  GLN HHH CA  1 
ATOM   9019  C C   . GLN G 2 83  ? -16.990 -43.110 10.528  1.000 123.339 ? 82  GLN HHH C   1 
ATOM   9020  O O   . GLN G 2 83  ? -16.789 -41.879 10.447  1.000 124.899 ? 82  GLN HHH O   1 
ATOM   9021  C CB  . GLN G 2 83  ? -18.642 -44.347 9.080   1.000 125.988 ? 82  GLN HHH CB  1 
ATOM   9022  C CG  . GLN G 2 83  ? -19.049 -43.442 7.928   1.000 127.447 ? 82  GLN HHH CG  1 
ATOM   9023  C CD  . GLN G 2 83  ? -19.193 -44.265 6.675   1.000 132.128 ? 82  GLN HHH CD  1 
ATOM   9024  O OE1 . GLN G 2 83  ? -18.349 -45.114 6.377   1.000 133.978 ? 82  GLN HHH OE1 1 
ATOM   9025  N NE2 . GLN G 2 83  ? -20.272 -44.023 5.943   1.000 134.142 ? 82  GLN HHH NE2 1 
ATOM   9026  N N   . TRP G 2 84  ? -16.055 -44.045 10.734  1.000 123.476 ? 83  TRP HHH N   1 
ATOM   9027  C CA  . TRP G 2 84  ? -14.602 -43.804 10.933  1.000 124.330 ? 83  TRP HHH CA  1 
ATOM   9028  C C   . TRP G 2 84  ? -13.798 -44.631 9.930   1.000 128.173 ? 83  TRP HHH C   1 
ATOM   9029  O O   . TRP G 2 84  ? -13.931 -45.867 9.910   1.000 127.993 ? 83  TRP HHH O   1 
ATOM   9030  C CB  . TRP G 2 84  ? -14.180 -44.120 12.370  1.000 123.027 ? 83  TRP HHH CB  1 
ATOM   9031  C CG  . TRP G 2 84  ? -14.494 -43.018 13.327  1.000 120.385 ? 83  TRP HHH CG  1 
ATOM   9032  C CD1 . TRP G 2 84  ? -13.749 -41.900 13.568  1.000 122.554 ? 83  TRP HHH CD1 1 
ATOM   9033  C CD2 . TRP G 2 84  ? -15.655 -42.921 14.164  1.000 116.172 ? 83  TRP HHH CD2 1 
ATOM   9034  N NE1 . TRP G 2 84  ? -14.365 -41.120 14.508  1.000 120.650 ? 83  TRP HHH NE1 1 
ATOM   9035  C CE2 . TRP G 2 84  ? -15.536 -41.718 14.890  1.000 116.461 ? 83  TRP HHH CE2 1 
ATOM   9036  C CE3 . TRP G 2 84  ? -16.773 -43.732 14.378  1.000 114.672 ? 83  TRP HHH CE3 1 
ATOM   9037  C CZ2 . TRP G 2 84  ? -16.500 -41.306 15.805  1.000 114.977 ? 83  TRP HHH CZ2 1 
ATOM   9038  C CZ3 . TRP G 2 84  ? -17.729 -43.322 15.279  1.000 113.590 ? 83  TRP HHH CZ3 1 
ATOM   9039  C CH2 . TRP G 2 84  ? -17.594 -42.122 15.979  1.000 113.851 ? 83  TRP HHH CH2 1 
ATOM   9040  N N   . SER G 2 85  ? -12.988 -43.935 9.134   1.000 131.958 ? 84  SER HHH N   1 
ATOM   9041  C CA  . SER G 2 85  ? -12.007 -44.488 8.168   1.000 135.446 ? 84  SER HHH CA  1 
ATOM   9042  C C   . SER G 2 85  ? -11.070 -45.470 8.886   1.000 135.992 ? 84  SER HHH C   1 
ATOM   9043  O O   . SER G 2 85  ? -10.761 -46.520 8.309   1.000 139.600 ? 84  SER HHH O   1 
ATOM   9044  C CB  . SER G 2 85  ? -11.253 -43.348 7.512   1.000 137.774 ? 84  SER HHH CB  1 
ATOM   9045  O OG  . SER G 2 85  ? -12.010 -42.126 7.536   1.000 133.218 ? 84  SER HHH OG  1 
ATOM   9046  N N   . SER G 2 86  ? -10.664 -45.130 10.113  1.000 133.654 ? 85  SER HHH N   1 
ATOM   9047  C CA  . SER G 2 86  ? -9.733  -45.899 10.980  1.000 132.919 ? 85  SER HHH CA  1 
ATOM   9048  C C   . SER G 2 86  ? -9.692  -45.246 12.370  1.000 130.165 ? 85  SER HHH C   1 
ATOM   9049  O O   . SER G 2 86  ? -9.433  -44.030 12.450  1.000 127.139 ? 85  SER HHH O   1 
ATOM   9050  C CB  . SER G 2 86  ? -8.376  -45.955 10.349  1.000 136.953 ? 85  SER HHH CB  1 
ATOM   9051  O OG  . SER G 2 86  ? -7.458  -46.614 11.195  1.000 139.281 ? 85  SER HHH OG  1 
ATOM   9052  N N   . LEU G 2 87  ? -9.950  -46.024 13.423  1.000 130.856 ? 86  LEU HHH N   1 
ATOM   9053  C CA  . LEU G 2 87  ? -10.282 -45.504 14.779  1.000 129.543 ? 86  LEU HHH CA  1 
ATOM   9054  C C   . LEU G 2 87  ? -9.013  -45.236 15.590  1.000 133.679 ? 86  LEU HHH C   1 
ATOM   9055  O O   . LEU G 2 87  ? -8.209  -46.177 15.749  1.000 136.863 ? 86  LEU HHH O   1 
ATOM   9056  C CB  . LEU G 2 87  ? -11.143 -46.531 15.517  1.000 127.517 ? 86  LEU HHH CB  1 
ATOM   9057  C CG  . LEU G 2 87  ? -12.633 -46.514 15.186  1.000 125.260 ? 86  LEU HHH CG  1 
ATOM   9058  C CD1 . LEU G 2 87  ? -13.306 -47.756 15.745  1.000 123.680 ? 86  LEU HHH CD1 1 
ATOM   9059  C CD2 . LEU G 2 87  ? -13.304 -45.248 15.710  1.000 122.906 ? 86  LEU HHH CD2 1 
ATOM   9060  N N   . LYS G 2 88  ? -8.891  -44.023 16.139  1.000 134.801 ? 87  LYS HHH N   1 
ATOM   9061  C CA  . LYS G 2 88  ? -7.879  -43.665 17.168  1.000 137.063 ? 87  LYS HHH CA  1 
ATOM   9062  C C   . LYS G 2 88  ? -8.358  -44.154 18.541  1.000 133.128 ? 87  LYS HHH C   1 
ATOM   9063  O O   . LYS G 2 88  ? -9.581  -44.317 18.721  1.000 129.250 ? 87  LYS HHH O   1 
ATOM   9064  C CB  . LYS G 2 88  ? -7.684  -42.147 17.236  1.000 140.230 ? 87  LYS HHH CB  1 
ATOM   9065  C CG  . LYS G 2 88  ? -7.219  -41.458 15.957  1.000 144.880 ? 87  LYS HHH CG  1 
ATOM   9066  C CD  . LYS G 2 88  ? -7.764  -40.033 15.810  1.000 146.453 ? 87  LYS HHH CD  1 
ATOM   9067  C CE  . LYS G 2 88  ? -6.732  -38.997 15.398  1.000 151.896 ? 87  LYS HHH CE  1 
ATOM   9068  N NZ  . LYS G 2 88  ? -6.427  -39.045 13.948  1.000 155.260 ? 87  LYS HHH NZ  1 
ATOM   9069  N N   . ALA G 2 89  ? -7.435  -44.344 19.487  1.000 132.444 ? 88  ALA HHH N   1 
ATOM   9070  C CA  . ALA G 2 89  ? -7.749  -44.464 20.929  1.000 128.829 ? 88  ALA HHH CA  1 
ATOM   9071  C C   . ALA G 2 89  ? -8.564  -43.234 21.331  1.000 125.028 ? 88  ALA HHH C   1 
ATOM   9072  O O   . ALA G 2 89  ? -9.642  -43.424 21.881  1.000 123.220 ? 88  ALA HHH O   1 
ATOM   9073  C CB  . ALA G 2 89  ? -6.493  -44.597 21.754  1.000 131.457 ? 88  ALA HHH CB  1 
ATOM   9074  N N   . SER G 2 90  ? -8.087  -42.030 20.998  1.000 126.989 ? 89  SER HHH N   1 
ATOM   9075  C CA  . SER G 2 90  ? -8.750  -40.728 21.288  1.000 128.208 ? 89  SER HHH CA  1 
ATOM   9076  C C   . SER G 2 90  ? -10.255 -40.829 21.015  1.000 127.773 ? 89  SER HHH C   1 
ATOM   9077  O O   . SER G 2 90  ? -11.040 -40.369 21.870  1.000 130.474 ? 89  SER HHH O   1 
ATOM   9078  C CB  . SER G 2 90  ? -8.137  -39.586 20.497  1.000 130.883 ? 89  SER HHH CB  1 
ATOM   9079  O OG  . SER G 2 90  ? -8.881  -39.299 19.316  1.000 129.218 ? 89  SER HHH OG  1 
ATOM   9080  N N   . ASP G 2 91  ? -10.637 -41.424 19.879  1.000 128.971 ? 90  ASP HHH N   1 
ATOM   9081  C CA  . ASP G 2 91  ? -12.046 -41.515 19.406  1.000 128.214 ? 90  ASP HHH CA  1 
ATOM   9082  C C   . ASP G 2 91  ? -12.879 -42.355 20.392  1.000 126.422 ? 90  ASP HHH C   1 
ATOM   9083  O O   . ASP G 2 91  ? -14.094 -42.506 20.148  1.000 126.771 ? 90  ASP HHH O   1 
ATOM   9084  C CB  . ASP G 2 91  ? -12.114 -42.046 17.968  1.000 129.262 ? 90  ASP HHH CB  1 
ATOM   9085  C CG  . ASP G 2 91  ? -11.566 -41.091 16.918  1.000 130.648 ? 90  ASP HHH CG  1 
ATOM   9086  O OD1 . ASP G 2 91  ? -11.680 -39.858 17.109  1.000 129.609 ? 90  ASP HHH OD1 1 
ATOM   9087  O OD2 . ASP G 2 91  ? -11.028 -41.590 15.910  1.000 132.909 ? 90  ASP HHH OD2 1 
ATOM   9088  N N   . THR G 2 92  ? -12.267 -42.886 21.459  1.000 125.612 ? 91  THR HHH N   1 
ATOM   9089  C CA  . THR G 2 92  ? -12.985 -43.421 22.648  1.000 122.923 ? 91  THR HHH CA  1 
ATOM   9090  C C   . THR G 2 92  ? -13.772 -42.286 23.293  1.000 117.970 ? 91  THR HHH C   1 
ATOM   9091  O O   . THR G 2 92  ? -13.157 -41.281 23.703  1.000 114.930 ? 91  THR HHH O   1 
ATOM   9092  C CB  . THR G 2 92  ? -12.069 -44.012 23.725  1.000 127.059 ? 91  THR HHH CB  1 
ATOM   9093  O OG1 . THR G 2 92  ? -11.360 -45.133 23.196  1.000 133.078 ? 91  THR HHH OG1 1 
ATOM   9094  C CG2 . THR G 2 92  ? -12.843 -44.442 24.952  1.000 126.362 ? 91  THR HHH CG2 1 
ATOM   9095  N N   . ALA G 2 93  ? -15.081 -42.476 23.387  1.000 116.270 ? 92  ALA HHH N   1 
ATOM   9096  C CA  . ALA G 2 93  ? -16.062 -41.454 23.800  1.000 117.768 ? 92  ALA HHH CA  1 
ATOM   9097  C C   . ALA G 2 93  ? -17.465 -42.044 23.687  1.000 117.570 ? 92  ALA HHH C   1 
ATOM   9098  O O   . ALA G 2 93  ? -17.599 -43.189 23.206  1.000 117.422 ? 92  ALA HHH O   1 
ATOM   9099  C CB  . ALA G 2 93  ? -15.931 -40.222 22.937  1.000 118.938 ? 92  ALA HHH CB  1 
ATOM   9100  N N   . ILE G 2 94  ? -18.460 -41.280 24.132  1.000 117.729 ? 93  ILE HHH N   1 
ATOM   9101  C CA  . ILE G 2 94  ? -19.901 -41.558 23.877  1.000 115.439 ? 93  ILE HHH CA  1 
ATOM   9102  C C   . ILE G 2 94  ? -20.368 -40.537 22.838  1.000 110.334 ? 93  ILE HHH C   1 
ATOM   9103  O O   . ILE G 2 94  ? -19.970 -39.357 22.949  1.000 108.905 ? 93  ILE HHH O   1 
ATOM   9104  C CB  . ILE G 2 94  ? -20.741 -41.553 25.173  1.000 118.198 ? 93  ILE HHH CB  1 
ATOM   9105  C CG1 . ILE G 2 94  ? -22.232 -41.664 24.846  1.000 120.766 ? 93  ILE HHH CG1 1 
ATOM   9106  C CG2 . ILE G 2 94  ? -20.438 -40.351 26.058  1.000 117.832 ? 93  ILE HHH CG2 1 
ATOM   9107  C CD1 . ILE G 2 94  ? -23.058 -42.299 25.943  1.000 124.642 ? 93  ILE HHH CD1 1 
ATOM   9108  N N   . TYR G 2 95  ? -21.117 -41.008 21.838  1.000 105.458 ? 94  TYR HHH N   1 
ATOM   9109  C CA  . TYR G 2 95  ? -21.518 -40.240 20.631  1.000 101.800 ? 94  TYR HHH CA  1 
ATOM   9110  C C   . TYR G 2 95  ? -23.040 -40.157 20.600  1.000 100.574 ? 94  TYR HHH C   1 
ATOM   9111  O O   . TYR G 2 95  ? -23.701 -41.185 20.437  1.000 100.075 ? 94  TYR HHH O   1 
ATOM   9112  C CB  . TYR G 2 95  ? -20.927 -40.880 19.372  1.000 99.390  ? 94  TYR HHH CB  1 
ATOM   9113  C CG  . TYR G 2 95  ? -19.424 -40.803 19.312  1.000 98.694  ? 94  TYR HHH CG  1 
ATOM   9114  C CD1 . TYR G 2 95  ? -18.796 -39.670 18.834  1.000 98.057  ? 94  TYR HHH CD1 1 
ATOM   9115  C CD2 . TYR G 2 95  ? -18.626 -41.840 19.772  1.000 98.396  ? 94  TYR HHH CD2 1 
ATOM   9116  C CE1 . TYR G 2 95  ? -17.415 -39.579 18.789  1.000 99.400  ? 94  TYR HHH CE1 1 
ATOM   9117  C CE2 . TYR G 2 95  ? -17.243 -41.764 19.735  1.000 98.244  ? 94  TYR HHH CE2 1 
ATOM   9118  C CZ  . TYR G 2 95  ? -16.635 -40.628 19.239  1.000 99.264  ? 94  TYR HHH CZ  1 
ATOM   9119  O OH  . TYR G 2 95  ? -15.276 -40.529 19.190  1.000 101.590 ? 94  TYR HHH OH  1 
ATOM   9120  N N   . TYR G 2 96  ? -23.570 -38.961 20.824  1.000 101.762 ? 95  TYR HHH N   1 
ATOM   9121  C CA  . TYR G 2 96  ? -25.021 -38.673 20.806  1.000 104.360 ? 95  TYR HHH CA  1 
ATOM   9122  C C   . TYR G 2 96  ? -25.385 -38.190 19.405  1.000 104.213 ? 95  TYR HHH C   1 
ATOM   9123  O O   . TYR G 2 96  ? -24.711 -37.280 18.923  1.000 104.641 ? 95  TYR HHH O   1 
ATOM   9124  C CB  . TYR G 2 96  ? -25.366 -37.599 21.839  1.000 107.591 ? 95  TYR HHH CB  1 
ATOM   9125  C CG  . TYR G 2 96  ? -25.093 -37.948 23.283  1.000 111.159 ? 95  TYR HHH CG  1 
ATOM   9126  C CD1 . TYR G 2 96  ? -25.913 -38.827 23.978  1.000 113.972 ? 95  TYR HHH CD1 1 
ATOM   9127  C CD2 . TYR G 2 96  ? -24.040 -37.368 23.976  1.000 112.919 ? 95  TYR HHH CD2 1 
ATOM   9128  C CE1 . TYR G 2 96  ? -25.683 -39.136 25.311  1.000 116.157 ? 95  TYR HHH CE1 1 
ATOM   9129  C CE2 . TYR G 2 96  ? -23.794 -37.669 25.307  1.000 115.069 ? 95  TYR HHH CE2 1 
ATOM   9130  C CZ  . TYR G 2 96  ? -24.623 -38.550 25.979  1.000 117.225 ? 95  TYR HHH CZ  1 
ATOM   9131  O OH  . TYR G 2 96  ? -24.410 -38.848 27.294  1.000 123.768 ? 95  TYR HHH OH  1 
ATOM   9132  N N   . CYS G 2 97  ? -26.398 -38.781 18.772  1.000 105.850 ? 96  CYS HHH N   1 
ATOM   9133  C CA  . CYS G 2 97  ? -27.075 -38.187 17.590  1.000 108.583 ? 96  CYS HHH CA  1 
ATOM   9134  C C   . CYS G 2 97  ? -28.221 -37.319 18.123  1.000 109.347 ? 96  CYS HHH C   1 
ATOM   9135  O O   . CYS G 2 97  ? -28.869 -37.744 19.100  1.000 109.497 ? 96  CYS HHH O   1 
ATOM   9136  C CB  . CYS G 2 97  ? -27.533 -39.247 16.590  1.000 110.101 ? 96  CYS HHH CB  1 
ATOM   9137  S SG  . CYS G 2 97  ? -29.160 -39.981 16.911  1.000 113.697 ? 96  CYS HHH SG  1 
ATOM   9138  N N   . ALA G 2 98  ? -28.420 -36.129 17.549  1.000 110.517 ? 97  ALA HHH N   1 
ATOM   9139  C CA  . ALA G 2 98  ? -29.356 -35.103 18.064  1.000 112.977 ? 97  ALA HHH CA  1 
ATOM   9140  C C   . ALA G 2 98  ? -30.042 -34.361 16.911  1.000 114.834 ? 97  ALA HHH C   1 
ATOM   9141  O O   . ALA G 2 98  ? -29.356 -33.640 16.144  1.000 116.072 ? 97  ALA HHH O   1 
ATOM   9142  C CB  . ALA G 2 98  ? -28.612 -34.153 18.961  1.000 114.717 ? 97  ALA HHH CB  1 
ATOM   9143  N N   . GLY G 2 99  ? -31.365 -34.502 16.833  1.000 116.667 ? 98  GLY HHH N   1 
ATOM   9144  C CA  . GLY G 2 99  ? -32.204 -33.869 15.802  1.000 119.431 ? 98  GLY HHH CA  1 
ATOM   9145  C C   . GLY G 2 99  ? -32.712 -32.504 16.233  1.000 121.709 ? 98  GLY HHH C   1 
ATOM   9146  O O   . GLY G 2 99  ? -33.102 -32.336 17.407  1.000 124.700 ? 98  GLY HHH O   1 
ATOM   9147  N N   . GLY G 2 100 ? -32.672 -31.542 15.319  1.000 122.865 ? 99  GLY HHH N   1 
ATOM   9148  C CA  . GLY G 2 100 ? -33.602 -30.400 15.305  1.000 124.275 ? 99  GLY HHH CA  1 
ATOM   9149  C C   . GLY G 2 100 ? -34.501 -30.512 14.091  1.000 122.883 ? 99  GLY HHH C   1 
ATOM   9150  O O   . GLY G 2 100 ? -34.085 -31.199 13.135  1.000 123.668 ? 99  GLY HHH O   1 
ATOM   9151  N N   . SER G 2 101 ? -35.688 -29.902 14.115  1.000 121.833 ? 100 SER HHH N   1 
ATOM   9152  C CA  . SER G 2 101 ? -36.554 -29.755 12.914  1.000 122.433 ? 100 SER HHH CA  1 
ATOM   9153  C C   . SER G 2 101 ? -36.130 -28.484 12.185  1.000 120.817 ? 100 SER HHH C   1 
ATOM   9154  O O   . SER G 2 101 ? -36.661 -27.427 12.494  1.000 127.524 ? 100 SER HHH O   1 
ATOM   9155  C CB  . SER G 2 101 ? -38.016 -29.749 13.263  1.000 126.851 ? 100 SER HHH CB  1 
ATOM   9156  O OG  . SER G 2 101 ? -38.277 -28.891 14.364  1.000 133.159 ? 100 SER HHH OG  1 
ATOM   9157  N N   . GLY G 2 102 ? -35.143 -28.585 11.303  1.000 119.256 ? 101 GLY HHH N   1 
ATOM   9158  C CA  . GLY G 2 102 ? -34.529 -27.423 10.637  1.000 119.201 ? 101 GLY HHH CA  1 
ATOM   9159  C C   . GLY G 2 102 ? -33.131 -27.132 11.159  1.000 117.200 ? 101 GLY HHH C   1 
ATOM   9160  O O   . GLY G 2 102 ? -32.766 -27.621 12.238  1.000 114.003 ? 101 GLY HHH O   1 
ATOM   9161  N N   . ILE G 2 103 ? -32.369 -26.367 10.382  1.000 119.674 ? 102 ILE HHH N   1 
ATOM   9162  C CA  . ILE G 2 103 ? -30.983 -25.919 10.692  1.000 121.523 ? 102 ILE HHH CA  1 
ATOM   9163  C C   . ILE G 2 103 ? -31.084 -24.544 11.362  1.000 120.200 ? 102 ILE HHH C   1 
ATOM   9164  O O   . ILE G 2 103 ? -32.160 -23.919 11.256  1.000 121.227 ? 102 ILE HHH O   1 
ATOM   9165  C CB  . ILE G 2 103 ? -30.121 -25.910 9.407   1.000 125.466 ? 102 ILE HHH CB  1 
ATOM   9166  C CG1 . ILE G 2 103 ? -28.616 -25.821 9.689   1.000 129.433 ? 102 ILE HHH CG1 1 
ATOM   9167  C CG2 . ILE G 2 103 ? -30.561 -24.810 8.451   1.000 126.827 ? 102 ILE HHH CG2 1 
ATOM   9168  C CD1 . ILE G 2 103 ? -28.076 -26.876 10.641  1.000 130.617 ? 102 ILE HHH CD1 1 
ATOM   9169  N N   . SER G 2 104 ? -30.012 -24.099 12.027  1.000 117.849 ? 103 SER HHH N   1 
ATOM   9170  C CA  . SER G 2 104 ? -30.021 -22.946 12.962  1.000 118.299 ? 103 SER HHH CA  1 
ATOM   9171  C C   . SER G 2 104 ? -31.204 -23.129 13.914  1.000 117.429 ? 103 SER HHH C   1 
ATOM   9172  O O   . SER G 2 104 ? -31.989 -22.185 14.098  1.000 117.382 ? 103 SER HHH O   1 
ATOM   9173  C CB  . SER G 2 104 ? -30.056 -21.630 12.229  1.000 119.974 ? 103 SER HHH CB  1 
ATOM   9174  O OG  . SER G 2 104 ? -28.760 -21.058 12.188  1.000 122.006 ? 103 SER HHH OG  1 
ATOM   9175  N N   . THR G 2 105 ? -31.322 -24.339 14.461  1.000 116.886 ? 104 THR HHH N   1 
ATOM   9176  C CA  . THR G 2 105 ? -32.374 -24.752 15.413  1.000 119.310 ? 104 THR HHH CA  1 
ATOM   9177  C C   . THR G 2 105 ? -31.705 -25.457 16.587  1.000 120.090 ? 104 THR HHH C   1 
ATOM   9178  O O   . THR G 2 105 ? -30.760 -26.237 16.430  1.000 118.043 ? 104 THR HHH O   1 
ATOM   9179  C CB  . THR G 2 105 ? -33.442 -25.623 14.737  1.000 120.781 ? 104 THR HHH CB  1 
ATOM   9180  O OG1 . THR G 2 105 ? -34.730 -25.241 15.219  1.000 120.551 ? 104 THR HHH OG1 1 
ATOM   9181  C CG2 . THR G 2 105 ? -33.262 -27.105 14.989  1.000 121.818 ? 104 THR HHH CG2 1 
ATOM   9182  N N   . PRO G 2 106 ? -32.219 -25.222 17.808  1.000 123.329 ? 105 PRO HHH N   1 
ATOM   9183  C CA  . PRO G 2 106 ? -31.670 -25.859 18.991  1.000 122.814 ? 105 PRO HHH CA  1 
ATOM   9184  C C   . PRO G 2 106 ? -32.032 -27.333 18.848  1.000 120.777 ? 105 PRO HHH C   1 
ATOM   9185  O O   . PRO G 2 106 ? -33.119 -27.616 18.372  1.000 118.654 ? 105 PRO HHH O   1 
ATOM   9186  C CB  . PRO G 2 106 ? -32.406 -25.191 20.153  1.000 126.762 ? 105 PRO HHH CB  1 
ATOM   9187  C CG  . PRO G 2 106 ? -33.727 -24.748 19.551  1.000 128.311 ? 105 PRO HHH CG  1 
ATOM   9188  C CD  . PRO G 2 106 ? -33.428 -24.433 18.102  1.000 127.606 ? 105 PRO HHH CD  1 
ATOM   9189  N N   . MET G 2 107 ? -31.109 -28.207 19.225  1.000 122.277 ? 106 MET HHH N   1 
ATOM   9190  C CA  . MET G 2 107 ? -31.319 -29.673 19.202  1.000 125.462 ? 106 MET HHH CA  1 
ATOM   9191  C C   . MET G 2 107 ? -32.333 -30.034 20.289  1.000 123.628 ? 106 MET HHH C   1 
ATOM   9192  O O   . MET G 2 107 ? -31.941 -30.048 21.466  1.000 123.094 ? 106 MET HHH O   1 
ATOM   9193  C CB  . MET G 2 107 ? -29.987 -30.385 19.430  1.000 130.807 ? 106 MET HHH CB  1 
ATOM   9194  C CG  . MET G 2 107 ? -29.034 -30.173 18.273  1.000 136.883 ? 106 MET HHH CG  1 
ATOM   9195  S SD  . MET G 2 107 ? -27.280 -30.224 18.727  1.000 141.420 ? 106 MET HHH SD  1 
ATOM   9196  C CE  . MET G 2 107 ? -26.638 -30.677 17.117  1.000 141.664 ? 106 MET HHH CE  1 
ATOM   9197  N N   . ASP G 2 108 ? -33.591 -30.272 19.893  1.000 123.832 ? 107 ASP HHH N   1 
ATOM   9198  C CA  . ASP G 2 108 ? -34.760 -30.406 20.810  1.000 125.986 ? 107 ASP HHH CA  1 
ATOM   9199  C C   . ASP G 2 108 ? -35.063 -31.886 21.071  1.000 118.751 ? 107 ASP HHH C   1 
ATOM   9200  O O   . ASP G 2 108 ? -35.995 -32.141 21.860  1.000 119.786 ? 107 ASP HHH O   1 
ATOM   9201  C CB  . ASP G 2 108 ? -35.997 -29.616 20.332  1.000 134.104 ? 107 ASP HHH CB  1 
ATOM   9202  C CG  . ASP G 2 108 ? -36.505 -29.837 18.904  1.000 137.764 ? 107 ASP HHH CG  1 
ATOM   9203  O OD1 . ASP G 2 108 ? -35.952 -29.202 17.959  1.000 139.171 ? 107 ASP HHH OD1 1 
ATOM   9204  O OD2 . ASP G 2 108 ? -37.501 -30.588 18.746  1.000 140.750 ? 107 ASP HHH OD2 1 
ATOM   9205  N N   . VAL G 2 109 ? -34.290 -32.810 20.480  1.000 110.427 ? 108 VAL HHH N   1 
ATOM   9206  C CA  . VAL G 2 109 ? -34.472 -34.288 20.627  1.000 107.508 ? 108 VAL HHH CA  1 
ATOM   9207  C C   . VAL G 2 109 ? -33.106 -34.988 20.550  1.000 103.889 ? 108 VAL HHH C   1 
ATOM   9208  O O   . VAL G 2 109 ? -32.336 -34.682 19.622  1.000 104.118 ? 108 VAL HHH O   1 
ATOM   9209  C CB  . VAL G 2 109 ? -35.467 -34.834 19.581  1.000 108.080 ? 108 VAL HHH CB  1 
ATOM   9210  C CG1 . VAL G 2 109 ? -35.397 -34.093 18.256  1.000 109.174 ? 108 VAL HHH CG1 1 
ATOM   9211  C CG2 . VAL G 2 109 ? -35.302 -36.329 19.353  1.000 107.433 ? 108 VAL HHH CG2 1 
ATOM   9212  N N   . TRP G 2 110 ? -32.827 -35.903 21.488  1.000 102.764 ? 109 TRP HHH N   1 
ATOM   9213  C CA  . TRP G 2 110 ? -31.507 -36.568 21.672  1.000 100.463 ? 109 TRP HHH CA  1 
ATOM   9214  C C   . TRP G 2 110 ? -31.687 -38.079 21.759  1.000 99.924  ? 109 TRP HHH C   1 
ATOM   9215  O O   . TRP G 2 110 ? -32.591 -38.520 22.476  1.000 101.592 ? 109 TRP HHH O   1 
ATOM   9216  C CB  . TRP G 2 110 ? -30.806 -36.060 22.937  1.000 100.754 ? 109 TRP HHH CB  1 
ATOM   9217  C CG  . TRP G 2 110 ? -30.285 -34.662 22.826  1.000 100.119 ? 109 TRP HHH CG  1 
ATOM   9218  C CD1 . TRP G 2 110 ? -31.008 -33.506 22.890  1.000 102.572 ? 109 TRP HHH CD1 1 
ATOM   9219  C CD2 . TRP G 2 110 ? -28.920 -34.263 22.637  1.000 96.441  ? 109 TRP HHH CD2 1 
ATOM   9220  N NE1 . TRP G 2 110 ? -30.190 -32.420 22.733  1.000 101.239 ? 109 TRP HHH NE1 1 
ATOM   9221  C CE2 . TRP G 2 110 ? -28.903 -32.853 22.583  1.000 97.787  ? 109 TRP HHH CE2 1 
ATOM   9222  C CE3 . TRP G 2 110 ? -27.718 -34.959 22.509  1.000 94.848  ? 109 TRP HHH CE3 1 
ATOM   9223  C CZ2 . TRP G 2 110 ? -27.732 -32.123 22.409  1.000 97.448  ? 109 TRP HHH CZ2 1 
ATOM   9224  C CZ3 . TRP G 2 110 ? -26.558 -34.239 22.339  1.000 96.188  ? 109 TRP HHH CZ3 1 
ATOM   9225  C CH2 . TRP G 2 110 ? -26.567 -32.842 22.293  1.000 97.332  ? 109 TRP HHH CH2 1 
ATOM   9226  N N   . GLY G 2 111 ? -30.824 -38.833 21.081  1.000 100.992 ? 110 GLY HHH N   1 
ATOM   9227  C CA  . GLY G 2 111 ? -30.683 -40.286 21.293  1.000 104.126 ? 110 GLY HHH CA  1 
ATOM   9228  C C   . GLY G 2 111 ? -29.924 -40.538 22.578  1.000 105.266 ? 110 GLY HHH C   1 
ATOM   9229  O O   . GLY G 2 111 ? -29.174 -39.635 22.979  1.000 105.543 ? 110 GLY HHH O   1 
ATOM   9230  N N   . GLN G 2 112 ? -30.096 -41.701 23.212  1.000 107.603 ? 111 GLN HHH N   1 
ATOM   9231  C CA  . GLN G 2 112 ? -29.492 -41.962 24.549  1.000 110.007 ? 111 GLN HHH CA  1 
ATOM   9232  C C   . GLN G 2 112 ? -27.965 -42.015 24.415  1.000 110.483 ? 111 GLN HHH C   1 
ATOM   9233  O O   . GLN G 2 112 ? -27.272 -41.939 25.461  1.000 112.355 ? 111 GLN HHH O   1 
ATOM   9234  C CB  . GLN G 2 112 ? -30.082 -43.211 25.209  1.000 110.973 ? 111 GLN HHH CB  1 
ATOM   9235  C CG  . GLN G 2 112 ? -29.737 -44.538 24.549  1.000 109.715 ? 111 GLN HHH CG  1 
ATOM   9236  C CD  . GLN G 2 112 ? -30.408 -45.678 25.277  1.000 110.062 ? 111 GLN HHH CD  1 
ATOM   9237  O OE1 . GLN G 2 112 ? -31.631 -45.718 25.422  1.000 109.104 ? 111 GLN HHH OE1 1 
ATOM   9238  N NE2 . GLN G 2 112 ? -29.604 -46.618 25.747  1.000 109.595 ? 111 GLN HHH NE2 1 
ATOM   9239  N N   . GLY G 2 113 ? -27.468 -42.113 23.180  1.000 109.665 ? 112 GLY HHH N   1 
ATOM   9240  C CA  . GLY G 2 113 ? -26.030 -42.088 22.876  1.000 111.640 ? 112 GLY HHH CA  1 
ATOM   9241  C C   . GLY G 2 113 ? -25.500 -43.486 22.639  1.000 114.480 ? 112 GLY HHH C   1 
ATOM   9242  O O   . GLY G 2 113 ? -26.023 -44.441 23.253  1.000 117.217 ? 112 GLY HHH O   1 
ATOM   9243  N N   . THR G 2 114 ? -24.511 -43.587 21.750  1.000 116.896 ? 113 THR HHH N   1 
ATOM   9244  C CA  . THR G 2 114 ? -23.718 -44.804 21.448  1.000 119.392 ? 113 THR HHH CA  1 
ATOM   9245  C C   . THR G 2 114 ? -22.353 -44.652 22.132  1.000 120.438 ? 113 THR HHH C   1 
ATOM   9246  O O   . THR G 2 114 ? -21.672 -43.650 21.838  1.000 118.165 ? 113 THR HHH O   1 
ATOM   9247  C CB  . THR G 2 114 ? -23.572 -44.988 19.930  1.000 121.189 ? 113 THR HHH CB  1 
ATOM   9248  O OG1 . THR G 2 114 ? -24.857 -44.964 19.297  1.000 121.114 ? 113 THR HHH OG1 1 
ATOM   9249  C CG2 . THR G 2 114 ? -22.852 -46.270 19.577  1.000 122.804 ? 113 THR HHH CG2 1 
ATOM   9250  N N   . THR G 2 115 ? -21.983 -45.579 23.028  1.000 122.020 ? 114 THR HHH N   1 
ATOM   9251  C CA  . THR G 2 115 ? -20.639 -45.644 23.672  1.000 122.039 ? 114 THR HHH CA  1 
ATOM   9252  C C   . THR G 2 115 ? -19.686 -46.442 22.783  1.000 122.519 ? 114 THR HHH C   1 
ATOM   9253  O O   . THR G 2 115 ? -19.972 -47.619 22.529  1.000 124.057 ? 114 THR HHH O   1 
ATOM   9254  C CB  . THR G 2 115 ? -20.666 -46.271 25.071  1.000 122.842 ? 114 THR HHH CB  1 
ATOM   9255  O OG1 . THR G 2 115 ? -21.973 -46.799 25.286  1.000 124.309 ? 114 THR HHH OG1 1 
ATOM   9256  C CG2 . THR G 2 115 ? -20.302 -45.288 26.162  1.000 123.991 ? 114 THR HHH CG2 1 
ATOM   9257  N N   . VAL G 2 116 ? -18.601 -45.806 22.339  1.000 120.893 ? 115 VAL HHH N   1 
ATOM   9258  C CA  . VAL G 2 116 ? -17.521 -46.432 21.526  1.000 121.569 ? 115 VAL HHH CA  1 
ATOM   9259  C C   . VAL G 2 116 ? -16.254 -46.441 22.385  1.000 124.009 ? 115 VAL HHH C   1 
ATOM   9260  O O   . VAL G 2 116 ? -15.877 -45.363 22.881  1.000 126.550 ? 115 VAL HHH O   1 
ATOM   9261  C CB  . VAL G 2 116 ? -17.317 -45.677 20.198  1.000 120.450 ? 115 VAL HHH CB  1 
ATOM   9262  C CG1 . VAL G 2 116 ? -16.173 -46.248 19.380  1.000 122.404 ? 115 VAL HHH CG1 1 
ATOM   9263  C CG2 . VAL G 2 116 ? -18.591 -45.644 19.370  1.000 118.512 ? 115 VAL HHH CG2 1 
ATOM   9264  N N   . THR G 2 117 ? -15.651 -47.617 22.583  1.000 124.954 ? 116 THR HHH N   1 
ATOM   9265  C CA  . THR G 2 117 ? -14.348 -47.780 23.283  1.000 127.181 ? 116 THR HHH CA  1 
ATOM   9266  C C   . THR G 2 117 ? -13.354 -48.465 22.334  1.000 129.543 ? 116 THR HHH C   1 
ATOM   9267  O O   . THR G 2 117 ? -13.557 -49.647 21.985  1.000 132.212 ? 116 THR HHH O   1 
ATOM   9268  C CB  . THR G 2 117 ? -14.506 -48.465 24.648  1.000 126.997 ? 116 THR HHH CB  1 
ATOM   9269  O OG1 . THR G 2 117 ? -15.248 -49.667 24.450  1.000 127.439 ? 116 THR HHH OG1 1 
ATOM   9270  C CG2 . THR G 2 117 ? -15.177 -47.585 25.680  1.000 126.185 ? 116 THR HHH CG2 1 
ATOM   9271  N N   . VAL G 2 118 ? -12.330 -47.715 21.917  1.000 127.826 ? 117 VAL HHH N   1 
ATOM   9272  C CA  . VAL G 2 118 ? -11.237 -48.158 21.006  1.000 127.192 ? 117 VAL HHH CA  1 
ATOM   9273  C C   . VAL G 2 118 ? -10.041 -48.567 21.861  1.000 128.275 ? 117 VAL HHH C   1 
ATOM   9274  O O   . VAL G 2 118 ? -9.229  -47.680 22.194  1.000 130.922 ? 117 VAL HHH O   1 
ATOM   9275  C CB  . VAL G 2 118 ? -10.849 -47.036 20.031  1.000 128.526 ? 117 VAL HHH CB  1 
ATOM   9276  C CG1 . VAL G 2 118 ? -9.767  -47.481 19.056  1.000 132.000 ? 117 VAL HHH CG1 1 
ATOM   9277  C CG2 . VAL G 2 118 ? -12.067 -46.498 19.298  1.000 127.995 ? 117 VAL HHH CG2 1 
ATOM   9278  N N   . ALA G 2 119 ? -9.951  -49.851 22.211  1.000 127.971 ? 118 ALA HHH N   1 
ATOM   9279  C CA  . ALA G 2 119 ? -8.823  -50.432 22.972  1.000 130.574 ? 118 ALA HHH CA  1 
ATOM   9280  C C   . ALA G 2 119 ? -8.928  -51.956 22.965  1.000 131.676 ? 118 ALA HHH C   1 
ATOM   9281  O O   . ALA G 2 119 ? -10.057 -52.482 23.048  1.000 128.077 ? 118 ALA HHH O   1 
ATOM   9282  C CB  . ALA G 2 119 ? -8.808  -49.912 24.392  1.000 129.770 ? 118 ALA HHH CB  1 
ATOM   9283  N N   . SER G 2 120 ? -7.776  -52.623 22.874  1.000 136.702 ? 119 SER HHH N   1 
ATOM   9284  C CA  . SER G 2 120 ? -7.605  -54.053 23.235  1.000 139.949 ? 119 SER HHH CA  1 
ATOM   9285  C C   . SER G 2 120 ? -7.985  -54.216 24.708  1.000 137.983 ? 119 SER HHH C   1 
ATOM   9286  O O   . SER G 2 120 ? -7.785  -53.254 25.484  1.000 135.046 ? 119 SER HHH O   1 
ATOM   9287  C CB  . SER G 2 120 ? -6.202  -54.535 22.961  1.000 144.700 ? 119 SER HHH CB  1 
ATOM   9288  O OG  . SER G 2 120 ? -5.256  -53.497 23.179  1.000 146.960 ? 119 SER HHH OG  1 
ATOM   9289  N N   . THR G 2 121 ? -8.521  -55.384 25.063  1.000 139.150 ? 120 THR HHH N   1 
ATOM   9290  C CA  . THR G 2 121 ? -9.125  -55.663 26.393  1.000 138.990 ? 120 THR HHH CA  1 
ATOM   9291  C C   . THR G 2 121 ? -8.100  -56.346 27.306  1.000 142.000 ? 120 THR HHH C   1 
ATOM   9292  O O   . THR G 2 121 ? -7.076  -56.853 26.810  1.000 145.658 ? 120 THR HHH O   1 
ATOM   9293  C CB  . THR G 2 121 ? -10.401 -56.508 26.275  1.000 138.716 ? 120 THR HHH CB  1 
ATOM   9294  O OG1 . THR G 2 121 ? -10.054 -57.885 26.112  1.000 141.604 ? 120 THR HHH OG1 1 
ATOM   9295  C CG2 . THR G 2 121 ? -11.285 -56.059 25.133  1.000 138.221 ? 120 THR HHH CG2 1 
ATOM   9296  N N   . LYS G 2 122 ? -8.388  -56.326 28.604  1.000 140.747 ? 121 LYS HHH N   1 
ATOM   9297  C CA  . LYS G 2 122 ? -7.654  -57.050 29.670  1.000 142.510 ? 121 LYS HHH CA  1 
ATOM   9298  C C   . LYS G 2 122 ? -8.587  -57.083 30.884  1.000 139.889 ? 121 LYS HHH C   1 
ATOM   9299  O O   . LYS G 2 122 ? -9.065  -56.007 31.297  1.000 136.126 ? 121 LYS HHH O   1 
ATOM   9300  C CB  . LYS G 2 122 ? -6.303  -56.381 29.946  1.000 145.985 ? 121 LYS HHH CB  1 
ATOM   9301  C CG  . LYS G 2 122 ? -5.300  -57.210 30.746  1.000 150.464 ? 121 LYS HHH CG  1 
ATOM   9302  C CD  . LYS G 2 122 ? -5.364  -57.014 32.258  1.000 150.155 ? 121 LYS HHH CD  1 
ATOM   9303  C CE  . LYS G 2 122 ? -4.070  -57.370 32.967  1.000 153.503 ? 121 LYS HHH CE  1 
ATOM   9304  N NZ  . LYS G 2 122 ? -3.764  -58.819 32.902  1.000 156.806 ? 121 LYS HHH NZ  1 
ATOM   9305  N N   . GLY G 2 123 ? -8.883  -58.286 31.376  1.000 142.190 ? 122 GLY HHH N   1 
ATOM   9306  C CA  . GLY G 2 123 ? -9.892  -58.538 32.421  1.000 141.399 ? 122 GLY HHH CA  1 
ATOM   9307  C C   . GLY G 2 123 ? -9.394  -58.154 33.814  1.000 141.094 ? 122 GLY HHH C   1 
ATOM   9308  O O   . GLY G 2 123 ? -8.212  -58.305 34.137  1.000 141.542 ? 122 GLY HHH O   1 
ATOM   9309  N N   . PRO G 2 124 ? -10.306 -57.674 34.690  1.000 137.841 ? 123 PRO HHH N   1 
ATOM   9310  C CA  . PRO G 2 124 ? -9.925  -57.150 35.998  1.000 137.779 ? 123 PRO HHH CA  1 
ATOM   9311  C C   . PRO G 2 124 ? -9.630  -58.249 37.021  1.000 139.256 ? 123 PRO HHH C   1 
ATOM   9312  O O   . PRO G 2 124 ? -10.384 -59.196 37.068  1.000 137.575 ? 123 PRO HHH O   1 
ATOM   9313  C CB  . PRO G 2 124 ? -11.192 -56.398 36.431  1.000 135.881 ? 123 PRO HHH CB  1 
ATOM   9314  C CG  . PRO G 2 124 ? -12.319 -57.199 35.807  1.000 134.174 ? 123 PRO HHH CG  1 
ATOM   9315  C CD  . PRO G 2 124 ? -11.761 -57.633 34.470  1.000 135.123 ? 123 PRO HHH CD  1 
ATOM   9316  N N   . SER G 2 125 ? -8.560  -58.082 37.803  1.000 141.883 ? 124 SER HHH N   1 
ATOM   9317  C CA  . SER G 2 125 ? -8.334  -58.803 39.082  1.000 143.586 ? 124 SER HHH CA  1 
ATOM   9318  C C   . SER G 2 125 ? -9.255  -58.198 40.144  1.000 142.124 ? 124 SER HHH C   1 
ATOM   9319  O O   . SER G 2 125 ? -9.423  -56.958 40.160  1.000 138.868 ? 124 SER HHH O   1 
ATOM   9320  C CB  . SER G 2 125 ? -6.892  -58.757 39.522  1.000 146.697 ? 124 SER HHH CB  1 
ATOM   9321  O OG  . SER G 2 125 ? -6.164  -59.847 38.983  1.000 149.688 ? 124 SER HHH OG  1 
ATOM   9322  N N   . VAL G 2 126 ? -9.853  -59.047 40.977  1.000 144.722 ? 125 VAL HHH N   1 
ATOM   9323  C CA  . VAL G 2 126 ? -10.776 -58.611 42.060  1.000 146.421 ? 125 VAL HHH CA  1 
ATOM   9324  C C   . VAL G 2 126 ? -10.245 -59.141 43.390  1.000 149.322 ? 125 VAL HHH C   1 
ATOM   9325  O O   . VAL G 2 126 ? -10.249 -60.379 43.601  1.000 150.407 ? 125 VAL HHH O   1 
ATOM   9326  C CB  . VAL G 2 126 ? -12.223 -59.063 41.803  1.000 147.526 ? 125 VAL HHH CB  1 
ATOM   9327  C CG1 . VAL G 2 126 ? -13.157 -58.589 42.904  1.000 149.034 ? 125 VAL HHH CG1 1 
ATOM   9328  C CG2 . VAL G 2 126 ? -12.715 -58.585 40.448  1.000 145.504 ? 125 VAL HHH CG2 1 
ATOM   9329  N N   . PHE G 2 127 ? -9.812  -58.213 44.243  1.000 149.979 ? 126 PHE HHH N   1 
ATOM   9330  C CA  . PHE G 2 127 ? -9.331  -58.466 45.621  1.000 152.924 ? 126 PHE HHH CA  1 
ATOM   9331  C C   . PHE G 2 127 ? -10.355 -57.885 46.594  1.000 151.075 ? 126 PHE HHH C   1 
ATOM   9332  O O   . PHE G 2 127 ? -10.998 -56.880 46.297  1.000 149.438 ? 126 PHE HHH O   1 
ATOM   9333  C CB  . PHE G 2 127 ? -7.928  -57.877 45.786  1.000 156.689 ? 126 PHE HHH CB  1 
ATOM   9334  C CG  . PHE G 2 127 ? -6.951  -58.240 44.691  1.000 158.707 ? 126 PHE HHH CG  1 
ATOM   9335  C CD1 . PHE G 2 127 ? -6.637  -59.565 44.424  1.000 160.844 ? 126 PHE HHH CD1 1 
ATOM   9336  C CD2 . PHE G 2 127 ? -6.328  -57.257 43.931  1.000 159.832 ? 126 PHE HHH CD2 1 
ATOM   9337  C CE1 . PHE G 2 127 ? -5.739  -59.895 43.418  1.000 161.692 ? 126 PHE HHH CE1 1 
ATOM   9338  C CE2 . PHE G 2 127 ? -5.427  -57.590 42.928  1.000 160.396 ? 126 PHE HHH CE2 1 
ATOM   9339  C CZ  . PHE G 2 127 ? -5.133  -58.909 42.673  1.000 161.345 ? 126 PHE HHH CZ  1 
ATOM   9340  N N   . PRO G 2 128 ? -10.571 -58.520 47.766  1.000 150.906 ? 127 PRO HHH N   1 
ATOM   9341  C CA  . PRO G 2 128 ? -11.473 -57.978 48.782  1.000 150.889 ? 127 PRO HHH CA  1 
ATOM   9342  C C   . PRO G 2 128 ? -10.794 -56.976 49.730  1.000 151.506 ? 127 PRO HHH C   1 
ATOM   9343  O O   . PRO G 2 128 ? -9.577  -56.922 49.756  1.000 152.183 ? 127 PRO HHH O   1 
ATOM   9344  C CB  . PRO G 2 128 ? -11.889 -59.248 49.537  1.000 154.141 ? 127 PRO HHH CB  1 
ATOM   9345  C CG  . PRO G 2 128 ? -10.638 -60.117 49.491  1.000 155.749 ? 127 PRO HHH CG  1 
ATOM   9346  C CD  . PRO G 2 128 ? -9.984  -59.810 48.158  1.000 152.981 ? 127 PRO HHH CD  1 
ATOM   9347  N N   . LEU G 2 129 ? -11.602 -56.225 50.484  1.000 151.402 ? 128 LEU HHH N   1 
ATOM   9348  C CA  . LEU G 2 129 ? -11.160 -55.269 51.535  1.000 154.443 ? 128 LEU HHH CA  1 
ATOM   9349  C C   . LEU G 2 129 ? -11.915 -55.579 52.837  1.000 158.243 ? 128 LEU HHH C   1 
ATOM   9350  O O   . LEU G 2 129 ? -12.980 -54.983 53.064  1.000 159.536 ? 128 LEU HHH O   1 
ATOM   9351  C CB  . LEU G 2 129 ? -11.427 -53.839 51.046  1.000 152.082 ? 128 LEU HHH CB  1 
ATOM   9352  C CG  . LEU G 2 129 ? -10.725 -53.430 49.750  1.000 148.642 ? 128 LEU HHH CG  1 
ATOM   9353  C CD1 . LEU G 2 129 ? -11.270 -52.112 49.222  1.000 146.744 ? 128 LEU HHH CD1 1 
ATOM   9354  C CD2 . LEU G 2 129 ? -9.217  -53.344 49.951  1.000 149.874 ? 128 LEU HHH CD2 1 
ATOM   9355  N N   . ALA G 2 130 ? -11.383 -56.479 53.665  1.000 162.141 ? 129 ALA HHH N   1 
ATOM   9356  C CA  . ALA G 2 130 ? -12.028 -56.944 54.917  1.000 168.298 ? 129 ALA HHH CA  1 
ATOM   9357  C C   . ALA G 2 130 ? -12.002 -55.842 55.977  1.000 174.171 ? 129 ALA HHH C   1 
ATOM   9358  O O   . ALA G 2 130 ? -11.017 -55.118 56.114  1.000 175.326 ? 129 ALA HHH O   1 
ATOM   9359  C CB  . ALA G 2 130 ? -11.347 -58.191 55.415  1.000 171.395 ? 129 ALA HHH CB  1 
ATOM   9360  N N   . PRO G 2 131 ? -13.081 -55.708 56.783  1.000 175.133 ? 130 PRO HHH N   1 
ATOM   9361  C CA  . PRO G 2 131 ? -13.200 -54.621 57.761  1.000 176.507 ? 130 PRO HHH CA  1 
ATOM   9362  C C   . PRO G 2 131 ? -12.522 -54.846 59.123  1.000 179.406 ? 130 PRO HHH C   1 
ATOM   9363  O O   . PRO G 2 131 ? -11.973 -55.910 59.345  1.000 178.235 ? 130 PRO HHH O   1 
ATOM   9364  C CB  . PRO G 2 131 ? -14.724 -54.554 57.955  1.000 179.179 ? 130 PRO HHH CB  1 
ATOM   9365  C CG  . PRO G 2 131 ? -15.188 -55.988 57.792  1.000 180.990 ? 130 PRO HHH CG  1 
ATOM   9366  C CD  . PRO G 2 131 ? -14.262 -56.586 56.757  1.000 177.825 ? 130 PRO HHH CD  1 
ATOM   9367  N N   . SER G 2 132 ? -12.603 -53.839 60.006  1.000 182.180 ? 131 SER HHH N   1 
ATOM   9368  C CA  . SER G 2 132 ? -12.096 -53.863 61.407  1.000 186.449 ? 131 SER HHH CA  1 
ATOM   9369  C C   . SER G 2 132 ? -13.176 -53.382 62.388  1.000 189.016 ? 131 SER HHH C   1 
ATOM   9370  O O   . SER G 2 132 ? -14.114 -52.666 61.955  1.000 189.264 ? 131 SER HHH O   1 
ATOM   9371  C CB  A SER G 2 132 ? -10.838 -53.044 61.521  0.500 185.354 ? 131 SER HHH CB  1 
ATOM   9372  C CB  B SER G 2 132 ? -10.830 -53.058 61.547  0.500 185.598 ? 131 SER HHH CB  1 
ATOM   9373  O OG  A SER G 2 132 ? -11.069 -51.699 61.113  0.500 182.433 ? 131 SER HHH OG  1 
ATOM   9374  O OG  B SER G 2 132 ? -9.691  -53.905 61.542  0.500 185.809 ? 131 SER HHH OG  1 
ATOM   9375  N N   . SER G 2 133 ? -13.032 -53.763 63.665  1.000 189.489 ? 132 SER HHH N   1 
ATOM   9376  C CA  . SER G 2 133 ? -13.966 -53.442 64.777  1.000 191.668 ? 132 SER HHH CA  1 
ATOM   9377  C C   . SER G 2 133 ? -13.177 -53.220 66.072  1.000 195.215 ? 132 SER HHH C   1 
ATOM   9378  O O   . SER G 2 133 ? -12.082 -52.632 65.969  1.000 192.835 ? 132 SER HHH O   1 
ATOM   9379  C CB  . SER G 2 133 ? -14.996 -54.527 64.931  1.000 193.052 ? 132 SER HHH CB  1 
ATOM   9380  O OG  . SER G 2 133 ? -15.918 -54.214 65.963  1.000 196.790 ? 132 SER HHH OG  1 
ATOM   9381  N N   . GLY G 2 138 ? -17.844 -52.519 69.356  1.000 207.319 ? 137 GLY HHH N   1 
ATOM   9382  C CA  . GLY G 2 138 ? -17.863 -52.050 67.957  1.000 203.343 ? 137 GLY HHH CA  1 
ATOM   9383  C C   . GLY G 2 138 ? -19.133 -51.283 67.615  1.000 205.177 ? 137 GLY HHH C   1 
ATOM   9384  O O   . GLY G 2 138 ? -20.198 -51.633 68.171  1.000 207.948 ? 137 GLY HHH O   1 
ATOM   9385  N N   . GLY G 2 139 ? -19.023 -50.290 66.717  1.000 203.232 ? 138 GLY HHH N   1 
ATOM   9386  C CA  . GLY G 2 139 ? -20.119 -49.394 66.283  1.000 203.023 ? 138 GLY HHH CA  1 
ATOM   9387  C C   . GLY G 2 139 ? -20.495 -49.605 64.823  1.000 198.521 ? 138 GLY HHH C   1 
ATOM   9388  O O   . GLY G 2 139 ? -21.320 -50.498 64.545  1.000 198.897 ? 138 GLY HHH O   1 
ATOM   9389  N N   . THR G 2 140 ? -19.926 -48.810 63.915  1.000 195.113 ? 139 THR HHH N   1 
ATOM   9390  C CA  . THR G 2 140 ? -20.025 -49.022 62.444  1.000 192.606 ? 139 THR HHH CA  1 
ATOM   9391  C C   . THR G 2 140 ? -18.703 -49.621 61.947  1.000 191.582 ? 139 THR HHH C   1 
ATOM   9392  O O   . THR G 2 140 ? -17.640 -49.329 62.558  1.000 193.522 ? 139 THR HHH O   1 
ATOM   9393  C CB  . THR G 2 140 ? -20.391 -47.745 61.674  1.000 189.859 ? 139 THR HHH CB  1 
ATOM   9394  O OG1 . THR G 2 140 ? -20.372 -48.054 60.277  1.000 183.905 ? 139 THR HHH OG1 1 
ATOM   9395  C CG2 . THR G 2 140 ? -19.458 -46.584 61.945  1.000 188.899 ? 139 THR HHH CG2 1 
ATOM   9396  N N   . ALA G 2 141 ? -18.787 -50.449 60.903  1.000 188.076 ? 140 ALA HHH N   1 
ATOM   9397  C CA  . ALA G 2 141 ? -17.638 -51.073 60.208  1.000 182.860 ? 140 ALA HHH CA  1 
ATOM   9398  C C   . ALA G 2 141 ? -17.984 -51.198 58.723  1.000 176.689 ? 140 ALA HHH C   1 
ATOM   9399  O O   . ALA G 2 141 ? -19.133 -51.547 58.425  1.000 174.744 ? 140 ALA HHH O   1 
ATOM   9400  C CB  . ALA G 2 141 ? -17.316 -52.412 60.828  1.000 185.740 ? 140 ALA HHH CB  1 
ATOM   9401  N N   . ALA G 2 142 ? -17.017 -50.915 57.845  1.000 172.119 ? 141 ALA HHH N   1 
ATOM   9402  C CA  . ALA G 2 142 ? -17.179 -50.853 56.373  1.000 166.974 ? 141 ALA HHH CA  1 
ATOM   9403  C C   . ALA G 2 142 ? -16.230 -51.845 55.694  1.000 163.211 ? 141 ALA HHH C   1 
ATOM   9404  O O   . ALA G 2 142 ? -15.143 -52.096 56.237  1.000 163.391 ? 141 ALA HHH O   1 
ATOM   9405  C CB  . ALA G 2 142 ? -16.919 -49.449 55.891  1.000 165.342 ? 141 ALA HHH CB  1 
ATOM   9406  N N   . LEU G 2 143 ? -16.637 -52.356 54.531  1.000 160.759 ? 142 LEU HHH N   1 
ATOM   9407  C CA  . LEU G 2 143 ? -15.899 -53.372 53.732  1.000 161.457 ? 142 LEU HHH CA  1 
ATOM   9408  C C   . LEU G 2 143 ? -16.127 -53.090 52.240  1.000 158.743 ? 142 LEU HHH C   1 
ATOM   9409  O O   . LEU G 2 143 ? -17.023 -52.274 51.932  1.000 158.865 ? 142 LEU HHH O   1 
ATOM   9410  C CB  . LEU G 2 143 ? -16.384 -54.771 54.131  1.000 166.212 ? 142 LEU HHH CB  1 
ATOM   9411  C CG  . LEU G 2 143 ? -17.880 -55.043 53.925  1.000 169.465 ? 142 LEU HHH CG  1 
ATOM   9412  C CD1 . LEU G 2 143 ? -18.175 -55.561 52.520  1.000 167.363 ? 142 LEU HHH CD1 1 
ATOM   9413  C CD2 . LEU G 2 143 ? -18.406 -56.027 54.961  1.000 174.552 ? 142 LEU HHH CD2 1 
ATOM   9414  N N   . GLY G 2 144 ? -15.367 -53.745 51.351  1.000 156.300 ? 143 GLY HHH N   1 
ATOM   9415  C CA  . GLY G 2 144 ? -15.422 -53.472 49.901  1.000 151.898 ? 143 GLY HHH CA  1 
ATOM   9416  C C   . GLY G 2 144 ? -14.585 -54.409 49.045  1.000 150.770 ? 143 GLY HHH C   1 
ATOM   9417  O O   . GLY G 2 144 ? -13.952 -55.332 49.588  1.000 149.525 ? 143 GLY HHH O   1 
ATOM   9418  N N   . CYS G 2 145 ? -14.612 -54.160 47.731  1.000 150.419 ? 144 CYS HHH N   1 
ATOM   9419  C CA  . CYS G 2 145 ? -13.827 -54.840 46.665  1.000 149.706 ? 144 CYS HHH CA  1 
ATOM   9420  C C   . CYS G 2 145 ? -12.815 -53.859 46.055  1.000 146.865 ? 144 CYS HHH C   1 
ATOM   9421  O O   . CYS G 2 145 ? -13.124 -52.653 45.970  1.000 145.959 ? 144 CYS HHH O   1 
ATOM   9422  C CB  . CYS G 2 145 ? -14.752 -55.372 45.575  1.000 150.003 ? 144 CYS HHH CB  1 
ATOM   9423  S SG  . CYS G 2 145 ? -15.356 -57.043 45.924  1.000 156.846 ? 144 CYS HHH SG  1 
ATOM   9424  N N   . LEU G 2 146 ? -11.646 -54.356 45.649  1.000 145.511 ? 145 LEU HHH N   1 
ATOM   9425  C CA  . LEU G 2 146 ? -10.688 -53.608 44.796  1.000 142.332 ? 145 LEU HHH CA  1 
ATOM   9426  C C   . LEU G 2 146 ? -10.632 -54.275 43.417  1.000 144.683 ? 145 LEU HHH C   1 
ATOM   9427  O O   . LEU G 2 146 ? -10.283 -55.475 43.347  1.000 148.631 ? 145 LEU HHH O   1 
ATOM   9428  C CB  . LEU G 2 146 ? -9.306  -53.590 45.447  1.000 140.132 ? 145 LEU HHH CB  1 
ATOM   9429  C CG  . LEU G 2 146 ? -8.269  -52.772 44.684  1.000 138.206 ? 145 LEU HHH CG  1 
ATOM   9430  C CD1 . LEU G 2 146 ? -8.644  -51.302 44.703  1.000 137.231 ? 145 LEU HHH CD1 1 
ATOM   9431  C CD2 . LEU G 2 146 ? -6.875  -52.985 45.243  1.000 140.421 ? 145 LEU HHH CD2 1 
ATOM   9432  N N   . VAL G 2 147 ? -10.965 -53.514 42.372  1.000 144.003 ? 146 VAL HHH N   1 
ATOM   9433  C CA  . VAL G 2 147 ? -10.965 -53.956 40.948  1.000 143.744 ? 146 VAL HHH CA  1 
ATOM   9434  C C   . VAL G 2 147 ? -9.746  -53.336 40.261  1.000 144.784 ? 146 VAL HHH C   1 
ATOM   9435  O O   . VAL G 2 147 ? -9.804  -52.138 39.925  1.000 141.992 ? 146 VAL HHH O   1 
ATOM   9436  C CB  . VAL G 2 147 ? -12.274 -53.544 40.258  1.000 143.277 ? 146 VAL HHH CB  1 
ATOM   9437  C CG1 . VAL G 2 147 ? -12.313 -54.010 38.817  1.000 145.270 ? 146 VAL HHH CG1 1 
ATOM   9438  C CG2 . VAL G 2 147 ? -13.488 -54.053 41.013  1.000 144.496 ? 146 VAL HHH CG2 1 
ATOM   9439  N N   . LYS G 2 148 ? -8.693  -54.133 40.062  1.000 149.679 ? 147 LYS HHH N   1 
ATOM   9440  C CA  . LYS G 2 148 ? -7.330  -53.659 39.704  1.000 151.820 ? 147 LYS HHH CA  1 
ATOM   9441  C C   . LYS G 2 148 ? -6.929  -54.174 38.317  1.000 151.852 ? 147 LYS HHH C   1 
ATOM   9442  O O   . LYS G 2 148 ? -7.324  -55.298 37.956  1.000 153.423 ? 147 LYS HHH O   1 
ATOM   9443  C CB  . LYS G 2 148 ? -6.323  -54.131 40.757  1.000 155.048 ? 147 LYS HHH CB  1 
ATOM   9444  C CG  . LYS G 2 148 ? -4.987  -53.408 40.724  1.000 158.779 ? 147 LYS HHH CG  1 
ATOM   9445  C CD  . LYS G 2 148 ? -3.892  -54.083 41.520  1.000 165.221 ? 147 LYS HHH CD  1 
ATOM   9446  C CE  . LYS G 2 148 ? -2.527  -53.460 41.289  1.000 169.530 ? 147 LYS HHH CE  1 
ATOM   9447  N NZ  . LYS G 2 148 ? -2.399  -52.125 41.924  1.000 171.165 ? 147 LYS HHH NZ  1 
ATOM   9448  N N   . ASP G 2 149 ? -6.170  -53.362 37.577  1.000 151.778 ? 148 ASP HHH N   1 
ATOM   9449  C CA  . ASP G 2 149 ? -5.437  -53.745 36.341  1.000 153.810 ? 148 ASP HHH CA  1 
ATOM   9450  C C   . ASP G 2 149 ? -6.421  -54.328 35.312  1.000 152.565 ? 148 ASP HHH C   1 
ATOM   9451  O O   . ASP G 2 149 ? -6.328  -55.542 35.013  1.000 152.433 ? 148 ASP HHH O   1 
ATOM   9452  C CB  . ASP G 2 149 ? -4.270  -54.684 36.679  1.000 157.805 ? 148 ASP HHH CB  1 
ATOM   9453  C CG  . ASP G 2 149 ? -3.117  -54.030 37.436  1.000 160.810 ? 148 ASP HHH CG  1 
ATOM   9454  O OD1 . ASP G 2 149 ? -2.915  -52.800 37.276  1.000 161.959 ? 148 ASP HHH OD1 1 
ATOM   9455  O OD2 . ASP G 2 149 ? -2.411  -54.760 38.175  1.000 163.173 ? 148 ASP HHH OD2 1 
ATOM   9456  N N   . TYR G 2 150 ? -7.326  -53.483 34.798  1.000 150.676 ? 149 TYR HHH N   1 
ATOM   9457  C CA  . TYR G 2 150 ? -8.295  -53.786 33.707  1.000 148.768 ? 149 TYR HHH CA  1 
ATOM   9458  C C   . TYR G 2 150 ? -8.288  -52.647 32.680  1.000 146.861 ? 149 TYR HHH C   1 
ATOM   9459  O O   . TYR G 2 150 ? -7.898  -51.518 33.032  1.000 145.144 ? 149 TYR HHH O   1 
ATOM   9460  C CB  . TYR G 2 150 ? -9.703  -54.002 34.267  1.000 147.947 ? 149 TYR HHH CB  1 
ATOM   9461  C CG  . TYR G 2 150 ? -10.407 -52.758 34.753  1.000 146.960 ? 149 TYR HHH CG  1 
ATOM   9462  C CD1 . TYR G 2 150 ? -11.145 -51.969 33.885  1.000 146.843 ? 149 TYR HHH CD1 1 
ATOM   9463  C CD2 . TYR G 2 150 ? -10.363 -52.378 36.088  1.000 146.541 ? 149 TYR HHH CD2 1 
ATOM   9464  C CE1 . TYR G 2 150 ? -11.804 -50.830 34.326  1.000 146.222 ? 149 TYR HHH CE1 1 
ATOM   9465  C CE2 . TYR G 2 150 ? -11.020 -51.243 36.543  1.000 144.926 ? 149 TYR HHH CE2 1 
ATOM   9466  C CZ  . TYR G 2 150 ? -11.748 -50.467 35.659  1.000 144.462 ? 149 TYR HHH CZ  1 
ATOM   9467  O OH  . TYR G 2 150 ? -12.410 -49.351 36.078  1.000 142.469 ? 149 TYR HHH OH  1 
ATOM   9468  N N   . PHE G 2 151 ? -8.741  -52.936 31.456  1.000 147.649 ? 150 PHE HHH N   1 
ATOM   9469  C CA  . PHE G 2 151 ? -8.683  -52.030 30.275  1.000 147.941 ? 150 PHE HHH CA  1 
ATOM   9470  C C   . PHE G 2 151 ? -9.540  -52.628 29.160  1.000 148.524 ? 150 PHE HHH C   1 
ATOM   9471  O O   . PHE G 2 151 ? -9.567  -53.845 28.996  1.000 150.754 ? 150 PHE HHH O   1 
ATOM   9472  C CB  . PHE G 2 151 ? -7.226  -51.845 29.828  1.000 149.816 ? 150 PHE HHH CB  1 
ATOM   9473  C CG  . PHE G 2 151 ? -6.926  -50.664 28.935  1.000 149.537 ? 150 PHE HHH CG  1 
ATOM   9474  C CD1 . PHE G 2 151 ? -7.183  -49.369 29.356  1.000 148.125 ? 150 PHE HHH CD1 1 
ATOM   9475  C CD2 . PHE G 2 151 ? -6.322  -50.840 27.698  1.000 152.271 ? 150 PHE HHH CD2 1 
ATOM   9476  C CE1 . PHE G 2 151 ? -6.891  -48.283 28.545  1.000 149.031 ? 150 PHE HHH CE1 1 
ATOM   9477  C CE2 . PHE G 2 151 ? -6.032  -49.753 26.887  1.000 153.373 ? 150 PHE HHH CE2 1 
ATOM   9478  C CZ  . PHE G 2 151 ? -6.320  -48.477 27.310  1.000 151.453 ? 150 PHE HHH CZ  1 
ATOM   9479  N N   . PRO G 2 152 ? -10.312 -51.820 28.399  1.000 147.723 ? 151 PRO HHH N   1 
ATOM   9480  C CA  . PRO G 2 152 ? -10.565 -50.423 28.736  1.000 145.995 ? 151 PRO HHH CA  1 
ATOM   9481  C C   . PRO G 2 152 ? -11.693 -50.344 29.767  1.000 144.431 ? 151 PRO HHH C   1 
ATOM   9482  O O   . PRO G 2 152 ? -12.187 -51.379 30.170  1.000 144.462 ? 151 PRO HHH O   1 
ATOM   9483  C CB  . PRO G 2 152 ? -11.025 -49.823 27.407  1.000 148.240 ? 151 PRO HHH CB  1 
ATOM   9484  C CG  . PRO G 2 152 ? -11.757 -50.970 26.738  1.000 149.807 ? 151 PRO HHH CG  1 
ATOM   9485  C CD  . PRO G 2 152 ? -11.006 -52.222 27.164  1.000 150.515 ? 151 PRO HHH CD  1 
ATOM   9486  N N   . GLU G 2 153 ? -12.092 -49.137 30.155  1.000 144.113 ? 152 GLU HHH N   1 
ATOM   9487  C CA  . GLU G 2 153 ? -13.249 -48.977 31.074  1.000 144.848 ? 152 GLU HHH CA  1 
ATOM   9488  C C   . GLU G 2 153 ? -14.504 -49.008 30.200  1.000 146.502 ? 152 GLU HHH C   1 
ATOM   9489  O O   . GLU G 2 153 ? -14.413 -48.959 28.970  1.000 146.912 ? 152 GLU HHH O   1 
ATOM   9490  C CB  . GLU G 2 153 ? -13.029 -47.827 32.069  1.000 143.691 ? 152 GLU HHH CB  1 
ATOM   9491  C CG  . GLU G 2 153 ? -13.012 -46.418 31.513  1.000 144.500 ? 152 GLU HHH CG  1 
ATOM   9492  C CD  . GLU G 2 153 ? -13.258 -45.398 32.614  1.000 144.113 ? 152 GLU HHH CD  1 
ATOM   9493  O OE1 . GLU G 2 153 ? -13.863 -45.786 33.642  1.000 142.867 ? 152 GLU HHH OE1 1 
ATOM   9494  O OE2 . GLU G 2 153 ? -12.845 -44.227 32.455  1.000 144.055 ? 152 GLU HHH OE2 1 
ATOM   9495  N N   . PRO G 2 154 ? -15.711 -49.186 30.787  1.000 146.555 ? 153 PRO HHH N   1 
ATOM   9496  C CA  . PRO G 2 154 ? -15.908 -49.245 32.233  1.000 145.267 ? 153 PRO HHH CA  1 
ATOM   9497  C C   . PRO G 2 154 ? -16.184 -50.631 32.827  1.000 145.797 ? 153 PRO HHH C   1 
ATOM   9498  O O   . PRO G 2 154 ? -16.365 -51.581 32.076  1.000 146.503 ? 153 PRO HHH O   1 
ATOM   9499  C CB  . PRO G 2 154 ? -17.168 -48.385 32.345  1.000 146.727 ? 153 PRO HHH CB  1 
ATOM   9500  C CG  . PRO G 2 154 ? -17.983 -48.746 31.104  1.000 147.799 ? 153 PRO HHH CG  1 
ATOM   9501  C CD  . PRO G 2 154 ? -16.995 -49.278 30.083  1.000 147.721 ? 153 PRO HHH CD  1 
ATOM   9502  N N   . VAL G 2 155 ? -16.205 -50.683 34.165  1.000 144.477 ? 154 VAL HHH N   1 
ATOM   9503  C CA  . VAL G 2 155 ? -16.592 -51.868 34.985  1.000 144.659 ? 154 VAL HHH CA  1 
ATOM   9504  C C   . VAL G 2 155 ? -17.783 -51.473 35.857  1.000 143.781 ? 154 VAL HHH C   1 
ATOM   9505  O O   . VAL G 2 155 ? -17.862 -50.282 36.230  1.000 141.543 ? 154 VAL HHH O   1 
ATOM   9506  C CB  . VAL G 2 155 ? -15.422 -52.368 35.850  1.000 145.199 ? 154 VAL HHH CB  1 
ATOM   9507  C CG1 . VAL G 2 155 ? -15.837 -53.485 36.793  1.000 146.915 ? 154 VAL HHH CG1 1 
ATOM   9508  C CG2 . VAL G 2 155 ? -14.261 -52.829 34.992  1.000 146.991 ? 154 VAL HHH CG2 1 
ATOM   9509  N N   . THR G 2 156 ? -18.642 -52.453 36.170  1.000 145.647 ? 155 THR HHH N   1 
ATOM   9510  C CA  . THR G 2 156 ? -19.848 -52.335 37.039  1.000 145.614 ? 155 THR HHH CA  1 
ATOM   9511  C C   . THR G 2 156 ? -19.763 -53.352 38.185  1.000 145.060 ? 155 THR HHH C   1 
ATOM   9512  O O   . THR G 2 156 ? -19.327 -54.499 37.942  1.000 144.862 ? 155 THR HHH O   1 
ATOM   9513  C CB  . THR G 2 156 ? -21.150 -52.552 36.254  1.000 147.919 ? 155 THR HHH CB  1 
ATOM   9514  O OG1 . THR G 2 156 ? -21.169 -53.908 35.799  1.000 151.391 ? 155 THR HHH OG1 1 
ATOM   9515  C CG2 . THR G 2 156 ? -21.311 -51.597 35.090  1.000 147.029 ? 155 THR HHH CG2 1 
ATOM   9516  N N   . VAL G 2 157 ? -20.198 -52.945 39.378  1.000 144.092 ? 156 VAL HHH N   1 
ATOM   9517  C CA  . VAL G 2 157 ? -20.134 -53.767 40.621  1.000 145.603 ? 156 VAL HHH CA  1 
ATOM   9518  C C   . VAL G 2 157 ? -21.524 -53.820 41.255  1.000 149.354 ? 156 VAL HHH C   1 
ATOM   9519  O O   . VAL G 2 157 ? -22.230 -52.800 41.197  1.000 150.714 ? 156 VAL HHH O   1 
ATOM   9520  C CB  . VAL G 2 157 ? -19.115 -53.185 41.613  1.000 142.780 ? 156 VAL HHH CB  1 
ATOM   9521  C CG1 . VAL G 2 157 ? -18.804 -54.186 42.713  1.000 145.021 ? 156 VAL HHH CG1 1 
ATOM   9522  C CG2 . VAL G 2 157 ? -17.846 -52.716 40.919  1.000 139.251 ? 156 VAL HHH CG2 1 
ATOM   9523  N N   . SER G 2 158 ? -21.884 -54.954 41.858  1.000 153.097 ? 157 SER HHH N   1 
ATOM   9524  C CA  . SER G 2 158 ? -23.120 -55.118 42.669  1.000 157.433 ? 157 SER HHH CA  1 
ATOM   9525  C C   . SER G 2 158 ? -22.818 -56.017 43.876  1.000 158.137 ? 157 SER HHH C   1 
ATOM   9526  O O   . SER G 2 158 ? -21.774 -56.698 43.857  1.000 157.182 ? 157 SER HHH O   1 
ATOM   9527  C CB  . SER G 2 158 ? -24.270 -55.618 41.819  1.000 161.362 ? 157 SER HHH CB  1 
ATOM   9528  O OG  . SER G 2 158 ? -24.136 -56.997 41.507  1.000 165.515 ? 157 SER HHH OG  1 
ATOM   9529  N N   . TRP G 2 159 ? -23.675 -55.989 44.899  1.000 159.412 ? 158 TRP HHH N   1 
ATOM   9530  C CA  . TRP G 2 159 ? -23.412 -56.636 46.211  1.000 161.813 ? 158 TRP HHH CA  1 
ATOM   9531  C C   . TRP G 2 159 ? -24.527 -57.632 46.541  1.000 167.071 ? 158 TRP HHH C   1 
ATOM   9532  O O   . TRP G 2 159 ? -25.717 -57.253 46.448  1.000 167.497 ? 158 TRP HHH O   1 
ATOM   9533  C CB  . TRP G 2 159 ? -23.228 -55.576 47.300  1.000 160.959 ? 158 TRP HHH CB  1 
ATOM   9534  C CG  . TRP G 2 159 ? -21.906 -54.873 47.221  1.000 155.937 ? 158 TRP HHH CG  1 
ATOM   9535  C CD1 . TRP G 2 159 ? -21.642 -53.696 46.587  1.000 151.754 ? 158 TRP HHH CD1 1 
ATOM   9536  C CD2 . TRP G 2 159 ? -20.656 -55.302 47.788  1.000 155.159 ? 158 TRP HHH CD2 1 
ATOM   9537  N NE1 . TRP G 2 159 ? -20.324 -53.362 46.724  1.000 149.160 ? 158 TRP HHH NE1 1 
ATOM   9538  C CE2 . TRP G 2 159 ? -19.691 -54.325 47.459  1.000 151.163 ? 158 TRP HHH CE2 1 
ATOM   9539  C CE3 . TRP G 2 159 ? -20.257 -56.410 48.544  1.000 158.869 ? 158 TRP HHH CE3 1 
ATOM   9540  C CZ2 . TRP G 2 159 ? -18.355 -54.426 47.852  1.000 151.304 ? 158 TRP HHH CZ2 1 
ATOM   9541  C CZ3 . TRP G 2 159 ? -18.940 -56.508 48.941  1.000 158.460 ? 158 TRP HHH CZ3 1 
ATOM   9542  C CH2 . TRP G 2 159 ? -18.001 -55.529 48.596  1.000 154.669 ? 158 TRP HHH CH2 1 
ATOM   9543  N N   . ASN G 2 160 ? -24.123 -58.856 46.905  1.000 171.155 ? 159 ASN HHH N   1 
ATOM   9544  C CA  . ASN G 2 160 ? -24.999 -60.027 47.177  1.000 177.928 ? 159 ASN HHH CA  1 
ATOM   9545  C C   . ASN G 2 160 ? -25.885 -60.294 45.956  1.000 178.503 ? 159 ASN HHH C   1 
ATOM   9546  O O   . ASN G 2 160 ? -27.085 -60.589 46.146  1.000 183.709 ? 159 ASN HHH O   1 
ATOM   9547  C CB  . ASN G 2 160 ? -25.806 -59.838 48.465  1.000 182.921 ? 159 ASN HHH CB  1 
ATOM   9548  C CG  . ASN G 2 160 ? -24.997 -60.157 49.702  1.000 184.627 ? 159 ASN HHH CG  1 
ATOM   9549  O OD1 . ASN G 2 160 ? -23.847 -59.726 49.819  1.000 181.352 ? 159 ASN HHH OD1 1 
ATOM   9550  N ND2 . ASN G 2 160 ? -25.587 -60.921 50.612  1.000 189.986 ? 159 ASN HHH ND2 1 
ATOM   9551  N N   . SER G 2 161 ? -25.299 -60.201 44.758  1.000 173.624 ? 160 SER HHH N   1 
ATOM   9552  C CA  . SER G 2 161 ? -25.966 -60.404 43.444  1.000 174.126 ? 160 SER HHH CA  1 
ATOM   9553  C C   . SER G 2 161 ? -26.582 -59.085 42.951  1.000 170.824 ? 160 SER HHH C   1 
ATOM   9554  O O   . SER G 2 161 ? -26.850 -58.991 41.739  1.000 170.690 ? 160 SER HHH O   1 
ATOM   9555  C CB  . SER G 2 161 ? -27.013 -61.503 43.527  1.000 180.400 ? 160 SER HHH CB  1 
ATOM   9556  O OG  . SER G 2 161 ? -27.316 -62.042 42.251  1.000 181.072 ? 160 SER HHH OG  1 
ATOM   9557  N N   . GLY G 2 162 ? -26.786 -58.105 43.840  1.000 168.676 ? 161 GLY HHH N   1 
ATOM   9558  C CA  . GLY G 2 162 ? -27.428 -56.816 43.518  1.000 166.325 ? 161 GLY HHH CA  1 
ATOM   9559  C C   . GLY G 2 162 ? -28.568 -56.485 44.458  1.000 169.375 ? 161 GLY HHH C   1 
ATOM   9560  O O   . GLY G 2 162 ? -29.190 -55.426 44.259  1.000 167.316 ? 161 GLY HHH O   1 
ATOM   9561  N N   . ALA G 2 163 ? -28.839 -57.354 45.438  1.000 174.833 ? 162 ALA HHH N   1 
ATOM   9562  C CA  . ALA G 2 163 ? -29.851 -57.153 46.503  1.000 180.417 ? 162 ALA HHH CA  1 
ATOM   9563  C C   . ALA G 2 163 ? -29.173 -56.566 47.752  1.000 180.533 ? 162 ALA HHH C   1 
ATOM   9564  O O   . ALA G 2 163 ? -29.350 -57.133 48.851  1.000 186.853 ? 162 ALA HHH O   1 
ATOM   9565  C CB  . ALA G 2 163 ? -30.555 -58.461 46.788  1.000 185.405 ? 162 ALA HHH CB  1 
ATOM   9566  N N   . LEU G 2 164 ? -28.413 -55.477 47.578  1.000 175.800 ? 163 LEU HHH N   1 
ATOM   9567  C CA  . LEU G 2 164 ? -27.781 -54.688 48.674  1.000 173.933 ? 163 LEU HHH CA  1 
ATOM   9568  C C   . LEU G 2 164 ? -27.161 -53.412 48.086  1.000 168.764 ? 163 LEU HHH C   1 
ATOM   9569  O O   . LEU G 2 164 ? -25.950 -53.425 47.811  1.000 163.588 ? 163 LEU HHH O   1 
ATOM   9570  C CB  . LEU G 2 164 ? -26.724 -55.552 49.375  1.000 174.062 ? 163 LEU HHH CB  1 
ATOM   9571  C CG  . LEU G 2 164 ? -26.384 -55.142 50.807  1.000 175.073 ? 163 LEU HHH CG  1 
ATOM   9572  C CD1 . LEU G 2 164 ? -27.274 -55.878 51.808  1.000 180.704 ? 163 LEU HHH CD1 1 
ATOM   9573  C CD2 . LEU G 2 164 ? -24.914 -55.388 51.114  1.000 170.966 ? 163 LEU HHH CD2 1 
ATOM   9574  N N   . THR G 2 165 ? -27.980 -52.377 47.848  1.000 170.365 ? 164 THR HHH N   1 
ATOM   9575  C CA  . THR G 2 165 ? -27.559 -51.002 47.445  1.000 167.186 ? 164 THR HHH CA  1 
ATOM   9576  C C   . THR G 2 165 ? -27.697 -50.052 48.638  1.000 167.436 ? 164 THR HHH C   1 
ATOM   9577  O O   . THR G 2 165 ? -27.353 -48.861 48.490  1.000 164.164 ? 164 THR HHH O   1 
ATOM   9578  C CB  . THR G 2 165 ? -28.396 -50.453 46.281  1.000 168.891 ? 164 THR HHH CB  1 
ATOM   9579  O OG1 . THR G 2 165 ? -29.759 -50.350 46.702  1.000 173.397 ? 164 THR HHH OG1 1 
ATOM   9580  C CG2 . THR G 2 165 ? -28.299 -51.308 45.037  1.000 168.981 ? 164 THR HHH CG2 1 
ATOM   9581  N N   . SER G 2 166 ? -28.204 -50.568 49.762  1.000 171.096 ? 165 SER HHH N   1 
ATOM   9582  C CA  . SER G 2 166 ? -28.412 -49.815 51.025  1.000 172.893 ? 165 SER HHH CA  1 
ATOM   9583  C C   . SER G 2 166 ? -27.055 -49.276 51.520  1.000 171.021 ? 165 SER HHH C   1 
ATOM   9584  O O   . SER G 2 166 ? -26.368 -49.967 52.318  1.000 172.578 ? 165 SER HHH O   1 
ATOM   9585  C CB  . SER G 2 166 ? -29.133 -50.685 52.029  1.000 176.907 ? 165 SER HHH CB  1 
ATOM   9586  O OG  . SER G 2 166 ? -30.284 -51.277 51.432  1.000 176.619 ? 165 SER HHH OG  1 
ATOM   9587  N N   . GLY G 2 167 ? -26.659 -48.105 51.002  1.000 167.801 ? 166 GLY HHH N   1 
ATOM   9588  C CA  . GLY G 2 167 ? -25.512 -47.301 51.479  1.000 164.675 ? 166 GLY HHH CA  1 
ATOM   9589  C C   . GLY G 2 167 ? -24.175 -47.770 50.924  1.000 160.170 ? 166 GLY HHH C   1 
ATOM   9590  O O   . GLY G 2 167 ? -23.244 -47.984 51.725  1.000 157.364 ? 166 GLY HHH O   1 
ATOM   9591  N N   . VAL G 2 168 ? -24.067 -47.868 49.594  1.000 157.355 ? 167 VAL HHH N   1 
ATOM   9592  C CA  . VAL G 2 168 ? -22.896 -48.427 48.853  1.000 154.068 ? 167 VAL HHH CA  1 
ATOM   9593  C C   . VAL G 2 168 ? -22.335 -47.357 47.909  1.000 154.009 ? 167 VAL HHH C   1 
ATOM   9594  O O   . VAL G 2 168 ? -23.086 -46.921 47.010  1.000 158.155 ? 167 VAL HHH O   1 
ATOM   9595  C CB  . VAL G 2 168 ? -23.292 -49.675 48.044  1.000 151.970 ? 167 VAL HHH CB  1 
ATOM   9596  C CG1 . VAL G 2 168 ? -22.068 -50.390 47.509  1.000 147.948 ? 167 VAL HHH CG1 1 
ATOM   9597  C CG2 . VAL G 2 168 ? -24.176 -50.627 48.835  1.000 156.906 ? 167 VAL HHH CG2 1 
ATOM   9598  N N   . HIS G 2 169 ? -21.051 -47.005 48.056  1.000 153.637 ? 168 HIS HHH N   1 
ATOM   9599  C CA  . HIS G 2 169 ? -20.309 -46.044 47.191  1.000 152.662 ? 168 HIS HHH CA  1 
ATOM   9600  C C   . HIS G 2 169 ? -19.309 -46.800 46.308  1.000 152.347 ? 168 HIS HHH C   1 
ATOM   9601  O O   . HIS G 2 169 ? -18.461 -47.518 46.871  1.000 151.293 ? 168 HIS HHH O   1 
ATOM   9602  C CB  . HIS G 2 169 ? -19.571 -45.003 48.038  1.000 153.484 ? 168 HIS HHH CB  1 
ATOM   9603  C CG  . HIS G 2 169 ? -20.425 -44.319 49.051  1.000 158.519 ? 168 HIS HHH CG  1 
ATOM   9604  N ND1 . HIS G 2 169 ? -20.862 -43.020 48.879  1.000 160.381 ? 168 HIS HHH ND1 1 
ATOM   9605  C CD2 . HIS G 2 169 ? -20.904 -44.736 50.247  1.000 162.640 ? 168 HIS HHH CD2 1 
ATOM   9606  C CE1 . HIS G 2 169 ? -21.580 -42.663 49.927  1.000 165.417 ? 168 HIS HHH CE1 1 
ATOM   9607  N NE2 . HIS G 2 169 ? -21.623 -43.703 50.785  1.000 165.698 ? 168 HIS HHH NE2 1 
ATOM   9608  N N   . THR G 2 170 ? -19.398 -46.628 44.984  1.000 153.182 ? 169 THR HHH N   1 
ATOM   9609  C CA  . THR G 2 170 ? -18.472 -47.226 43.981  1.000 151.056 ? 169 THR HHH CA  1 
ATOM   9610  C C   . THR G 2 170 ? -17.811 -46.106 43.172  1.000 147.419 ? 169 THR HHH C   1 
ATOM   9611  O O   . THR G 2 170 ? -18.520 -45.441 42.386  1.000 148.923 ? 169 THR HHH O   1 
ATOM   9612  C CB  . THR G 2 170 ? -19.209 -48.244 43.104  1.000 153.396 ? 169 THR HHH CB  1 
ATOM   9613  O OG1 . THR G 2 170 ? -19.398 -49.389 43.934  1.000 155.742 ? 169 THR HHH OG1 1 
ATOM   9614  C CG2 . THR G 2 170 ? -18.455 -48.628 41.849  1.000 152.930 ? 169 THR HHH CG2 1 
ATOM   9615  N N   . PHE G 2 171 ? -16.497 -45.944 43.342  1.000 143.496 ? 170 PHE HHH N   1 
ATOM   9616  C CA  . PHE G 2 171 ? -15.733 -44.726 42.971  1.000 141.620 ? 170 PHE HHH CA  1 
ATOM   9617  C C   . PHE G 2 171 ? -15.444 -44.713 41.477  1.000 139.023 ? 170 PHE HHH C   1 
ATOM   9618  O O   . PHE G 2 171 ? -15.513 -45.744 40.819  1.000 137.921 ? 170 PHE HHH O   1 
ATOM   9619  C CB  . PHE G 2 171 ? -14.437 -44.647 43.776  1.000 142.109 ? 170 PHE HHH CB  1 
ATOM   9620  C CG  . PHE G 2 171 ? -14.670 -44.547 45.259  1.000 143.883 ? 170 PHE HHH CG  1 
ATOM   9621  C CD1 . PHE G 2 171 ? -14.973 -43.330 45.842  1.000 144.712 ? 170 PHE HHH CD1 1 
ATOM   9622  C CD2 . PHE G 2 171 ? -14.626 -45.673 46.064  1.000 144.822 ? 170 PHE HHH CD2 1 
ATOM   9623  C CE1 . PHE G 2 171 ? -15.203 -43.240 47.206  1.000 146.978 ? 170 PHE HHH CE1 1 
ATOM   9624  C CE2 . PHE G 2 171 ? -14.848 -45.580 47.428  1.000 146.825 ? 170 PHE HHH CE2 1 
ATOM   9625  C CZ  . PHE G 2 171 ? -15.144 -44.364 47.995  1.000 147.911 ? 170 PHE HHH CZ  1 
ATOM   9626  N N   . PRO G 2 172 ? -15.136 -43.527 40.906  1.000 138.931 ? 171 PRO HHH N   1 
ATOM   9627  C CA  . PRO G 2 172 ? -14.596 -43.431 39.553  1.000 138.522 ? 171 PRO HHH CA  1 
ATOM   9628  C C   . PRO G 2 172 ? -13.328 -44.280 39.398  1.000 137.623 ? 171 PRO HHH C   1 
ATOM   9629  O O   . PRO G 2 172 ? -12.599 -44.409 40.354  1.000 138.789 ? 171 PRO HHH O   1 
ATOM   9630  C CB  . PRO G 2 172 ? -14.240 -41.946 39.392  1.000 139.625 ? 171 PRO HHH CB  1 
ATOM   9631  C CG  . PRO G 2 172 ? -15.129 -41.230 40.385  1.000 140.544 ? 171 PRO HHH CG  1 
ATOM   9632  C CD  . PRO G 2 172 ? -15.324 -42.208 41.525  1.000 141.063 ? 171 PRO HHH CD  1 
ATOM   9633  N N   . ALA G 2 173 ? -13.107 -44.838 38.208  1.000 136.834 ? 172 ALA HHH N   1 
ATOM   9634  C CA  . ALA G 2 173 ? -11.862 -45.548 37.849  1.000 135.984 ? 172 ALA HHH CA  1 
ATOM   9635  C C   . ALA G 2 173 ? -10.738 -44.519 37.764  1.000 135.488 ? 172 ALA HHH C   1 
ATOM   9636  O O   . ALA G 2 173 ? -11.020 -43.358 37.414  1.000 134.781 ? 172 ALA HHH O   1 
ATOM   9637  C CB  . ALA G 2 173 ? -12.026 -46.291 36.548  1.000 136.420 ? 172 ALA HHH CB  1 
ATOM   9638  N N   . VAL G 2 174 ? -9.520  -44.935 38.094  1.000 136.457 ? 173 VAL HHH N   1 
ATOM   9639  C CA  . VAL G 2 174 ? -8.289  -44.112 37.928  1.000 139.370 ? 173 VAL HHH CA  1 
ATOM   9640  C C   . VAL G 2 174 ? -7.290  -44.952 37.136  1.000 138.064 ? 173 VAL HHH C   1 
ATOM   9641  O O   . VAL G 2 174 ? -7.154  -46.147 37.438  1.000 138.552 ? 173 VAL HHH O   1 
ATOM   9642  C CB  . VAL G 2 174 ? -7.726  -43.638 39.282  1.000 144.541 ? 173 VAL HHH CB  1 
ATOM   9643  C CG1 . VAL G 2 174 ? -8.597  -42.549 39.895  1.000 146.439 ? 173 VAL HHH CG1 1 
ATOM   9644  C CG2 . VAL G 2 174 ? -7.532  -44.783 40.271  1.000 146.208 ? 173 VAL HHH CG2 1 
ATOM   9645  N N   . LEU G 2 175 ? -6.668  -44.356 36.123  1.000 138.338 ? 174 LEU HHH N   1 
ATOM   9646  C CA  . LEU G 2 175 ? -5.707  -45.041 35.221  1.000 140.479 ? 174 LEU HHH CA  1 
ATOM   9647  C C   . LEU G 2 175 ? -4.331  -45.046 35.900  1.000 141.949 ? 174 LEU HHH C   1 
ATOM   9648  O O   . LEU G 2 175 ? -3.694  -43.978 35.955  1.000 143.197 ? 174 LEU HHH O   1 
ATOM   9649  C CB  . LEU G 2 175 ? -5.727  -44.308 33.875  1.000 141.894 ? 174 LEU HHH CB  1 
ATOM   9650  C CG  . LEU G 2 175 ? -4.543  -44.514 32.933  1.000 144.928 ? 174 LEU HHH CG  1 
ATOM   9651  C CD1 . LEU G 2 175 ? -4.475  -45.946 32.424  1.000 144.443 ? 174 LEU HHH CD1 1 
ATOM   9652  C CD2 . LEU G 2 175 ? -4.629  -43.527 31.776  1.000 147.513 ? 174 LEU HHH CD2 1 
ATOM   9653  N N   . GLN G 2 176 ? -3.906  -46.202 36.418  1.000 142.483 ? 175 GLN HHH N   1 
ATOM   9654  C CA  . GLN G 2 176 ? -2.572  -46.396 37.051  1.000 145.363 ? 175 GLN HHH CA  1 
ATOM   9655  C C   . GLN G 2 176 ? -1.474  -46.040 36.042  1.000 147.445 ? 175 GLN HHH C   1 
ATOM   9656  O O   . GLN G 2 176 ? -1.777  -46.004 34.834  1.000 147.193 ? 175 GLN HHH O   1 
ATOM   9657  C CB  . GLN G 2 176 ? -2.372  -47.846 37.494  1.000 145.935 ? 175 GLN HHH CB  1 
ATOM   9658  C CG  . GLN G 2 176 ? -3.025  -48.196 38.818  1.000 145.223 ? 175 GLN HHH CG  1 
ATOM   9659  C CD  . GLN G 2 176 ? -3.231  -49.684 38.924  1.000 145.285 ? 175 GLN HHH CD  1 
ATOM   9660  O OE1 . GLN G 2 176 ? -4.358  -50.157 38.988  1.000 144.312 ? 175 GLN HHH OE1 1 
ATOM   9661  N NE2 . GLN G 2 176 ? -2.141  -50.437 38.914  1.000 147.534 ? 175 GLN HHH NE2 1 
ATOM   9662  N N   . SER G 2 177 ? -0.247  -45.816 36.526  1.000 149.900 ? 176 SER HHH N   1 
ATOM   9663  C CA  . SER G 2 177 ? 0.994   -45.717 35.708  1.000 151.886 ? 176 SER HHH CA  1 
ATOM   9664  C C   . SER G 2 177 ? 1.061   -46.911 34.747  1.000 151.540 ? 176 SER HHH C   1 
ATOM   9665  O O   . SER G 2 177 ? 1.413   -46.720 33.568  1.000 153.830 ? 176 SER HHH O   1 
ATOM   9666  C CB  . SER G 2 177 ? 2.215   -45.643 36.592  1.000 154.009 ? 176 SER HHH CB  1 
ATOM   9667  O OG  . SER G 2 177 ? 2.133   -46.598 37.638  1.000 153.060 ? 176 SER HHH OG  1 
ATOM   9668  N N   . SER G 2 178 ? 0.690   -48.091 35.250  1.000 150.416 ? 177 SER HHH N   1 
ATOM   9669  C CA  . SER G 2 178 ? 0.597   -49.395 34.540  1.000 150.602 ? 177 SER HHH CA  1 
ATOM   9670  C C   . SER G 2 178 ? -0.080  -49.252 33.168  1.000 147.550 ? 177 SER HHH C   1 
ATOM   9671  O O   . SER G 2 178 ? 0.182   -50.106 32.310  1.000 149.167 ? 177 SER HHH O   1 
ATOM   9672  C CB  . SER G 2 178 ? -0.133  -50.400 35.411  1.000 150.871 ? 177 SER HHH CB  1 
ATOM   9673  O OG  . SER G 2 178 ? 0.105   -51.731 34.986  1.000 153.512 ? 177 SER HHH OG  1 
ATOM   9674  N N   . GLY G 2 179 ? -0.917  -48.229 32.965  1.000 143.330 ? 178 GLY HHH N   1 
ATOM   9675  C CA  . GLY G 2 179 ? -1.649  -48.003 31.704  1.000 142.039 ? 178 GLY HHH CA  1 
ATOM   9676  C C   . GLY G 2 179 ? -2.986  -48.720 31.703  1.000 139.125 ? 178 GLY HHH C   1 
ATOM   9677  O O   . GLY G 2 179 ? -3.652  -48.720 30.639  1.000 138.358 ? 178 GLY HHH O   1 
ATOM   9678  N N   . LEU G 2 180 ? -3.352  -49.314 32.850  1.000 138.614 ? 179 LEU HHH N   1 
ATOM   9679  C CA  . LEU G 2 180 ? -4.631  -50.036 33.104  1.000 137.714 ? 179 LEU HHH CA  1 
ATOM   9680  C C   . LEU G 2 180 ? -5.356  -49.393 34.292  1.000 136.470 ? 179 LEU HHH C   1 
ATOM   9681  O O   . LEU G 2 180 ? -4.668  -48.993 35.259  1.000 137.670 ? 179 LEU HHH O   1 
ATOM   9682  C CB  . LEU G 2 180 ? -4.343  -51.506 33.422  1.000 138.645 ? 179 LEU HHH CB  1 
ATOM   9683  C CG  . LEU G 2 180 ? -3.268  -52.192 32.585  1.000 141.625 ? 179 LEU HHH CG  1 
ATOM   9684  C CD1 . LEU G 2 180 ? -3.151  -53.651 32.997  1.000 142.886 ? 179 LEU HHH CD1 1 
ATOM   9685  C CD2 . LEU G 2 180 ? -3.552  -52.084 31.091  1.000 143.295 ? 179 LEU HHH CD2 1 
ATOM   9686  N N   . TYR G 2 181 ? -6.693  -49.355 34.244  1.000 133.930 ? 180 TYR HHH N   1 
ATOM   9687  C CA  . TYR G 2 181 ? -7.569  -48.707 35.255  1.000 132.558 ? 180 TYR HHH CA  1 
ATOM   9688  C C   . TYR G 2 181 ? -7.668  -49.558 36.530  1.000 134.042 ? 180 TYR HHH C   1 
ATOM   9689  O O   . TYR G 2 181 ? -7.486  -50.794 36.466  1.000 135.850 ? 180 TYR HHH O   1 
ATOM   9690  C CB  . TYR G 2 181 ? -8.964  -48.468 34.677  1.000 130.079 ? 180 TYR HHH CB  1 
ATOM   9691  C CG  . TYR G 2 181 ? -9.020  -47.489 33.534  1.000 128.835 ? 180 TYR HHH CG  1 
ATOM   9692  C CD1 . TYR G 2 181 ? -8.888  -46.131 33.752  1.000 128.765 ? 180 TYR HHH CD1 1 
ATOM   9693  C CD2 . TYR G 2 181 ? -9.231  -47.913 32.237  1.000 128.871 ? 180 TYR HHH CD2 1 
ATOM   9694  C CE1 . TYR G 2 181 ? -8.966  -45.218 32.713  1.000 129.041 ? 180 TYR HHH CE1 1 
ATOM   9695  C CE2 . TYR G 2 181 ? -9.301  -47.016 31.185  1.000 129.794 ? 180 TYR HHH CE2 1 
ATOM   9696  C CZ  . TYR G 2 181 ? -9.173  -45.662 31.422  1.000 129.764 ? 180 TYR HHH CZ  1 
ATOM   9697  O OH  . TYR G 2 181 ? -9.249  -44.782 30.380  1.000 132.371 ? 180 TYR HHH OH  1 
ATOM   9698  N N   . SER G 2 182 ? -7.946  -48.893 37.659  1.000 134.572 ? 181 SER HHH N   1 
ATOM   9699  C CA  . SER G 2 182 ? -8.307  -49.498 38.971  1.000 133.870 ? 181 SER HHH CA  1 
ATOM   9700  C C   . SER G 2 182 ? -9.427  -48.673 39.614  1.000 131.566 ? 181 SER HHH C   1 
ATOM   9701  O O   . SER G 2 182 ? -9.534  -47.464 39.322  1.000 130.528 ? 181 SER HHH O   1 
ATOM   9702  C CB  . SER G 2 182 ? -7.114  -49.626 39.891  1.000 135.233 ? 181 SER HHH CB  1 
ATOM   9703  O OG  . SER G 2 182 ? -7.521  -49.919 41.221  1.000 134.813 ? 181 SER HHH OG  1 
ATOM   9704  N N   . LEU G 2 183 ? -10.226 -49.310 40.466  1.000 130.252 ? 182 LEU HHH N   1 
ATOM   9705  C CA  . LEU G 2 183 ? -11.532 -48.772 40.915  1.000 130.114 ? 182 LEU HHH CA  1 
ATOM   9706  C C   . LEU G 2 183 ? -11.983 -49.551 42.147  1.000 132.283 ? 182 LEU HHH C   1 
ATOM   9707  O O   . LEU G 2 183 ? -12.046 -50.788 42.061  1.000 132.326 ? 182 LEU HHH O   1 
ATOM   9708  C CB  . LEU G 2 183 ? -12.510 -48.932 39.750  1.000 130.511 ? 182 LEU HHH CB  1 
ATOM   9709  C CG  . LEU G 2 183 ? -13.984 -48.677 40.053  1.000 132.064 ? 182 LEU HHH CG  1 
ATOM   9710  C CD1 . LEU G 2 183 ? -14.728 -48.241 38.798  1.000 132.771 ? 182 LEU HHH CD1 1 
ATOM   9711  C CD2 . LEU G 2 183 ? -14.649 -49.910 40.642  1.000 133.946 ? 182 LEU HHH CD2 1 
ATOM   9712  N N   . SER G 2 184 ? -12.271 -48.849 43.245  1.000 135.522 ? 183 SER HHH N   1 
ATOM   9713  C CA  . SER G 2 184 ? -12.685 -49.427 44.553  1.000 138.145 ? 183 SER HHH CA  1 
ATOM   9714  C C   . SER G 2 184 ? -14.206 -49.316 44.689  1.000 137.957 ? 183 SER HHH C   1 
ATOM   9715  O O   . SER G 2 184 ? -14.773 -48.356 44.124  1.000 136.968 ? 183 SER HHH O   1 
ATOM   9716  C CB  . SER G 2 184 ? -11.979 -48.744 45.701  1.000 140.450 ? 183 SER HHH CB  1 
ATOM   9717  O OG  . SER G 2 184 ? -10.602 -48.546 45.405  1.000 143.529 ? 183 SER HHH OG  1 
ATOM   9718  N N   . SER G 2 185 ? -14.830 -50.274 45.384  1.000 139.662 ? 184 SER HHH N   1 
ATOM   9719  C CA  . SER G 2 185 ? -16.275 -50.284 45.742  1.000 141.038 ? 184 SER HHH CA  1 
ATOM   9720  C C   . SER G 2 185 ? -16.443 -50.769 47.186  1.000 143.680 ? 184 SER HHH C   1 
ATOM   9721  O O   . SER G 2 185 ? -15.898 -51.835 47.507  1.000 147.083 ? 184 SER HHH O   1 
ATOM   9722  C CB  . SER G 2 185 ? -17.065 -51.146 44.809  1.000 140.435 ? 184 SER HHH CB  1 
ATOM   9723  O OG  . SER G 2 185 ? -18.364 -51.364 45.332  1.000 141.690 ? 184 SER HHH OG  1 
ATOM   9724  N N   . VAL G 2 186 ? -17.198 -50.033 48.006  1.000 143.123 ? 185 VAL HHH N   1 
ATOM   9725  C CA  . VAL G 2 186 ? -17.283 -50.241 49.483  1.000 144.690 ? 185 VAL HHH CA  1 
ATOM   9726  C C   . VAL G 2 186 ? -18.733 -50.043 49.952  1.000 148.353 ? 185 VAL HHH C   1 
ATOM   9727  O O   . VAL G 2 186 ? -19.480 -49.348 49.248  1.000 150.953 ? 185 VAL HHH O   1 
ATOM   9728  C CB  . VAL G 2 186 ? -16.307 -49.293 50.203  1.000 143.596 ? 185 VAL HHH CB  1 
ATOM   9729  C CG1 . VAL G 2 186 ? -14.857 -49.665 49.931  1.000 142.663 ? 185 VAL HHH CG1 1 
ATOM   9730  C CG2 . VAL G 2 186 ? -16.559 -47.837 49.837  1.000 141.954 ? 185 VAL HHH CG2 1 
ATOM   9731  N N   . VAL G 2 187 ? -19.112 -50.636 51.091  1.000 151.127 ? 186 VAL HHH N   1 
ATOM   9732  C CA  . VAL G 2 187 ? -20.468 -50.502 51.711  1.000 153.862 ? 186 VAL HHH CA  1 
ATOM   9733  C C   . VAL G 2 187 ? -20.315 -50.335 53.230  1.000 156.856 ? 186 VAL HHH C   1 
ATOM   9734  O O   . VAL G 2 187 ? -19.536 -51.104 53.830  1.000 157.530 ? 186 VAL HHH O   1 
ATOM   9735  C CB  . VAL G 2 187 ? -21.367 -51.705 51.364  1.000 156.207 ? 186 VAL HHH CB  1 
ATOM   9736  C CG1 . VAL G 2 187 ? -20.666 -53.037 51.616  1.000 157.192 ? 186 VAL HHH CG1 1 
ATOM   9737  C CG2 . VAL G 2 187 ? -22.708 -51.636 52.085  1.000 160.464 ? 186 VAL HHH CG2 1 
ATOM   9738  N N   . THR G 2 188 ? -21.029 -49.372 53.830  1.000 158.384 ? 187 THR HHH N   1 
ATOM   9739  C CA  . THR G 2 188 ? -21.067 -49.164 55.306  1.000 161.773 ? 187 THR HHH CA  1 
ATOM   9740  C C   . THR G 2 188 ? -22.117 -50.117 55.886  1.000 166.962 ? 187 THR HHH C   1 
ATOM   9741  O O   . THR G 2 188 ? -23.256 -50.112 55.391  1.000 166.048 ? 187 THR HHH O   1 
ATOM   9742  C CB  . THR G 2 188 ? -21.349 -47.708 55.702  1.000 161.455 ? 187 THR HHH CB  1 
ATOM   9743  O OG1 . THR G 2 188 ? -20.881 -46.870 54.649  1.000 158.781 ? 187 THR HHH OG1 1 
ATOM   9744  C CG2 . THR G 2 188 ? -20.690 -47.296 57.004  1.000 162.577 ? 187 THR HHH CG2 1 
ATOM   9745  N N   . VAL G 2 189 ? -21.723 -50.907 56.886  1.000 172.296 ? 188 VAL HHH N   1 
ATOM   9746  C CA  . VAL G 2 189 ? -22.539 -51.993 57.493  1.000 177.834 ? 188 VAL HHH CA  1 
ATOM   9747  C C   . VAL G 2 189 ? -22.407 -51.896 59.013  1.000 184.999 ? 188 VAL HHH C   1 
ATOM   9748  O O   . VAL G 2 189 ? -21.338 -51.557 59.532  1.000 184.378 ? 188 VAL HHH O   1 
ATOM   9749  C CB  . VAL G 2 189 ? -22.085 -53.361 56.948  1.000 175.696 ? 188 VAL HHH CB  1 
ATOM   9750  C CG1 . VAL G 2 189 ? -22.722 -54.517 57.680  1.000 180.279 ? 188 VAL HHH CG1 1 
ATOM   9751  C CG2 . VAL G 2 189 ? -22.321 -53.485 55.452  1.000 171.862 ? 188 VAL HHH CG2 1 
ATOM   9752  N N   . PRO G 2 190 ? -23.496 -52.164 59.774  1.000 192.650 ? 189 PRO HHH N   1 
ATOM   9753  C CA  . PRO G 2 190 ? -23.412 -52.263 61.235  1.000 199.670 ? 189 PRO HHH CA  1 
ATOM   9754  C C   . PRO G 2 190 ? -22.354 -53.282 61.695  1.000 202.652 ? 189 PRO HHH C   1 
ATOM   9755  O O   . PRO G 2 190 ? -22.283 -54.351 61.096  1.000 202.626 ? 189 PRO HHH O   1 
ATOM   9756  C CB  . PRO G 2 190 ? -24.824 -52.705 61.657  1.000 202.526 ? 189 PRO HHH CB  1 
ATOM   9757  C CG  . PRO G 2 190 ? -25.723 -52.243 60.524  1.000 198.635 ? 189 PRO HHH CG  1 
ATOM   9758  C CD  . PRO G 2 190 ? -24.871 -52.329 59.275  1.000 192.756 ? 189 PRO HHH CD  1 
ATOM   9759  N N   . SER G 2 191 ? -21.563 -52.939 62.723  1.000 205.598 ? 190 SER HHH N   1 
ATOM   9760  C CA  . SER G 2 191 ? -20.443 -53.773 63.240  1.000 207.794 ? 190 SER HHH CA  1 
ATOM   9761  C C   . SER G 2 191 ? -20.826 -55.257 63.174  1.000 209.613 ? 190 SER HHH C   1 
ATOM   9762  O O   . SER G 2 191 ? -20.189 -55.997 62.409  1.000 207.208 ? 190 SER HHH O   1 
ATOM   9763  C CB  . SER G 2 191 ? -20.044 -53.388 64.648  1.000 213.215 ? 190 SER HHH CB  1 
ATOM   9764  O OG  . SER G 2 191 ? -19.066 -52.356 64.648  1.000 211.152 ? 190 SER HHH OG  1 
ATOM   9765  N N   . SER G 2 192 ? -21.869 -55.653 63.908  1.000 212.521 ? 191 SER HHH N   1 
ATOM   9766  C CA  . SER G 2 192 ? -22.228 -57.064 64.205  1.000 214.767 ? 191 SER HHH CA  1 
ATOM   9767  C C   . SER G 2 192 ? -22.995 -57.716 63.044  1.000 210.699 ? 191 SER HHH C   1 
ATOM   9768  O O   . SER G 2 192 ? -23.573 -58.800 63.261  1.000 214.080 ? 191 SER HHH O   1 
ATOM   9769  C CB  . SER G 2 192 ? -23.014 -57.123 65.482  1.000 222.315 ? 191 SER HHH CB  1 
ATOM   9770  O OG  . SER G 2 192 ? -24.108 -56.222 65.425  1.000 224.343 ? 191 SER HHH OG  1 
ATOM   9771  N N   . SER G 2 193 ? -22.987 -57.113 61.852  1.000 203.102 ? 192 SER HHH N   1 
ATOM   9772  C CA  . SER G 2 193 ? -23.575 -57.687 60.611  1.000 200.978 ? 192 SER HHH CA  1 
ATOM   9773  C C   . SER G 2 193 ? -22.751 -58.893 60.131  1.000 198.667 ? 192 SER HHH C   1 
ATOM   9774  O O   . SER G 2 193 ? -23.347 -59.874 59.633  1.000 199.947 ? 192 SER HHH O   1 
ATOM   9775  C CB  . SER G 2 193 ? -23.657 -56.648 59.527  1.000 196.339 ? 192 SER HHH CB  1 
ATOM   9776  O OG  . SER G 2 193 ? -24.257 -55.452 60.004  1.000 196.924 ? 192 SER HHH OG  1 
ATOM   9777  N N   . LEU G 2 194 ? -21.428 -58.804 60.281  1.000 194.890 ? 193 LEU HHH N   1 
ATOM   9778  C CA  . LEU G 2 194 ? -20.420 -59.717 59.674  1.000 192.781 ? 193 LEU HHH CA  1 
ATOM   9779  C C   . LEU G 2 194 ? -20.601 -61.130 60.240  1.000 197.152 ? 193 LEU HHH C   1 
ATOM   9780  O O   . LEU G 2 194 ? -20.373 -62.095 59.493  1.000 193.800 ? 193 LEU HHH O   1 
ATOM   9781  C CB  . LEU G 2 194 ? -19.013 -59.178 59.965  1.000 190.827 ? 193 LEU HHH CB  1 
ATOM   9782  C CG  . LEU G 2 194 ? -18.791 -57.675 59.756  1.000 187.624 ? 193 LEU HHH CG  1 
ATOM   9783  C CD1 . LEU G 2 194 ? -17.374 -57.276 60.137  1.000 186.248 ? 193 LEU HHH CD1 1 
ATOM   9784  C CD2 . LEU G 2 194 ? -19.090 -57.238 58.329  1.000 184.084 ? 193 LEU HHH CD2 1 
ATOM   9785  N N   . GLY G 2 195 ? -20.994 -61.233 61.514  1.000 203.752 ? 194 GLY HHH N   1 
ATOM   9786  C CA  . GLY G 2 195 ? -21.131 -62.495 62.271  1.000 210.435 ? 194 GLY HHH CA  1 
ATOM   9787  C C   . GLY G 2 195 ? -21.968 -63.547 61.553  1.000 213.263 ? 194 GLY HHH C   1 
ATOM   9788  O O   . GLY G 2 195 ? -21.771 -64.741 61.853  1.000 218.298 ? 194 GLY HHH O   1 
ATOM   9789  N N   . THR G 2 196 ? -22.878 -63.135 60.662  1.000 210.652 ? 195 THR HHH N   1 
ATOM   9790  C CA  . THR G 2 196 ? -23.674 -64.038 59.784  1.000 212.046 ? 195 THR HHH CA  1 
ATOM   9791  C C   . THR G 2 196 ? -23.711 -63.486 58.357  1.000 208.052 ? 195 THR HHH C   1 
ATOM   9792  O O   . THR G 2 196 ? -23.040 -64.088 57.491  1.000 206.484 ? 195 THR HHH O   1 
ATOM   9793  C CB  . THR G 2 196 ? -25.103 -64.245 60.299  1.000 216.593 ? 195 THR HHH CB  1 
ATOM   9794  O OG1 . THR G 2 196 ? -25.679 -62.957 60.518  1.000 214.049 ? 195 THR HHH OG1 1 
ATOM   9795  C CG2 . THR G 2 196 ? -25.154 -65.095 61.549  1.000 222.981 ? 195 THR HHH CG2 1 
ATOM   9796  N N   . GLN G 2 197 ? -24.456 -62.393 58.138  1.000 207.509 ? 196 GLN HHH N   1 
ATOM   9797  C CA  . GLN G 2 197 ? -24.800 -61.851 56.792  1.000 203.704 ? 196 GLN HHH CA  1 
ATOM   9798  C C   . GLN G 2 197 ? -23.575 -61.931 55.878  1.000 197.679 ? 196 GLN HHH C   1 
ATOM   9799  O O   . GLN G 2 197 ? -22.554 -61.288 56.194  1.000 193.798 ? 196 GLN HHH O   1 
ATOM   9800  C CB  . GLN G 2 197 ? -25.312 -60.409 56.878  1.000 201.348 ? 196 GLN HHH CB  1 
ATOM   9801  C CG  . GLN G 2 197 ? -25.576 -59.753 55.524  1.000 196.292 ? 196 GLN HHH CG  1 
ATOM   9802  C CD  . GLN G 2 197 ? -26.616 -60.448 54.678  1.000 198.576 ? 196 GLN HHH CD  1 
ATOM   9803  O OE1 . GLN G 2 197 ? -27.482 -61.166 55.174  1.000 203.754 ? 196 GLN HHH OE1 1 
ATOM   9804  N NE2 . GLN G 2 197 ? -26.552 -60.214 53.378  1.000 193.547 ? 196 GLN HHH NE2 1 
ATOM   9805  N N   . THR G 2 198 ? -23.691 -62.699 54.789  1.000 196.942 ? 197 THR HHH N   1 
ATOM   9806  C CA  . THR G 2 198 ? -22.667 -62.825 53.721  1.000 192.696 ? 197 THR HHH CA  1 
ATOM   9807  C C   . THR G 2 198 ? -22.537 -61.473 53.029  1.000 188.076 ? 197 THR HHH C   1 
ATOM   9808  O O   . THR G 2 198 ? -23.558 -60.753 52.956  1.000 190.159 ? 197 THR HHH O   1 
ATOM   9809  C CB  . THR G 2 198 ? -23.052 -63.900 52.700  1.000 194.941 ? 197 THR HHH CB  1 
ATOM   9810  O OG1 . THR G 2 198 ? -23.282 -65.120 53.404  1.000 202.341 ? 197 THR HHH OG1 1 
ATOM   9811  C CG2 . THR G 2 198 ? -22.005 -64.106 51.630  1.000 190.884 ? 197 THR HHH CG2 1 
ATOM   9812  N N   . TYR G 2 199 ? -21.342 -61.152 52.530  1.000 183.559 ? 198 TYR HHH N   1 
ATOM   9813  C CA  . TYR G 2 199 ? -21.095 -59.990 51.638  1.000 178.107 ? 198 TYR HHH CA  1 
ATOM   9814  C C   . TYR G 2 199 ? -20.211 -60.442 50.473  1.000 175.631 ? 198 TYR HHH C   1 
ATOM   9815  O O   . TYR G 2 199 ? -18.970 -60.445 50.611  1.000 175.679 ? 198 TYR HHH O   1 
ATOM   9816  C CB  . TYR G 2 199 ? -20.508 -58.824 52.436  1.000 175.566 ? 198 TYR HHH CB  1 
ATOM   9817  C CG  . TYR G 2 199 ? -21.480 -58.208 53.410  1.000 178.084 ? 198 TYR HHH CG  1 
ATOM   9818  C CD1 . TYR G 2 199 ? -22.489 -57.365 52.973  1.000 177.243 ? 198 TYR HHH CD1 1 
ATOM   9819  C CD2 . TYR G 2 199 ? -21.406 -58.484 54.767  1.000 181.581 ? 198 TYR HHH CD2 1 
ATOM   9820  C CE1 . TYR G 2 199 ? -23.390 -56.796 53.858  1.000 180.390 ? 198 TYR HHH CE1 1 
ATOM   9821  C CE2 . TYR G 2 199 ? -22.304 -57.930 55.665  1.000 184.867 ? 198 TYR HHH CE2 1 
ATOM   9822  C CZ  . TYR G 2 199 ? -23.296 -57.078 55.210  1.000 184.421 ? 198 TYR HHH CZ  1 
ATOM   9823  O OH  . TYR G 2 199 ? -24.179 -56.529 56.095  1.000 187.895 ? 198 TYR HHH OH  1 
ATOM   9824  N N   . ILE G 2 200 ? -20.853 -60.862 49.379  1.000 174.970 ? 199 ILE HHH N   1 
ATOM   9825  C CA  . ILE G 2 200 ? -20.210 -61.138 48.062  1.000 171.737 ? 199 ILE HHH CA  1 
ATOM   9826  C C   . ILE G 2 200 ? -20.322 -59.856 47.239  1.000 166.274 ? 199 ILE HHH C   1 
ATOM   9827  O O   . ILE G 2 200 ? -21.323 -59.135 47.415  1.000 165.380 ? 199 ILE HHH O   1 
ATOM   9828  C CB  . ILE G 2 200 ? -20.871 -62.342 47.356  1.000 175.920 ? 199 ILE HHH CB  1 
ATOM   9829  C CG1 . ILE G 2 200 ? -20.512 -63.666 48.039  1.000 179.435 ? 199 ILE HHH CG1 1 
ATOM   9830  C CG2 . ILE G 2 200 ? -20.526 -62.357 45.871  1.000 174.363 ? 199 ILE HHH CG2 1 
ATOM   9831  C CD1 . ILE G 2 200 ? -21.294 -64.865 47.545  1.000 183.750 ? 199 ILE HHH CD1 1 
ATOM   9832  N N   . CYS G 2 201 ? -19.333 -59.582 46.388  1.000 163.721 ? 200 CYS HHH N   1 
ATOM   9833  C CA  . CYS G 2 201 ? -19.398 -58.487 45.387  1.000 163.369 ? 200 CYS HHH CA  1 
ATOM   9834  C C   . CYS G 2 201 ? -19.273 -59.098 43.989  1.000 164.316 ? 200 CYS HHH C   1 
ATOM   9835  O O   . CYS G 2 201 ? -18.378 -59.942 43.794  1.000 163.220 ? 200 CYS HHH O   1 
ATOM   9836  C CB  . CYS G 2 201 ? -18.362 -57.406 45.685  1.000 161.589 ? 200 CYS HHH CB  1 
ATOM   9837  S SG  . CYS G 2 201 ? -16.894 -57.391 44.621  1.000 159.456 ? 200 CYS HHH SG  1 
ATOM   9838  N N   . ASN G 2 202 ? -20.179 -58.709 43.082  1.000 166.738 ? 201 ASN HHH N   1 
ATOM   9839  C CA  . ASN G 2 202 ? -20.286 -59.216 41.685  1.000 167.306 ? 201 ASN HHH CA  1 
ATOM   9840  C C   . ASN G 2 202 ? -19.746 -58.131 40.739  1.000 161.495 ? 201 ASN HHH C   1 
ATOM   9841  O O   . ASN G 2 202 ? -20.300 -57.013 40.733  1.000 158.515 ? 201 ASN HHH O   1 
ATOM   9842  C CB  . ASN G 2 202 ? -21.722 -59.633 41.336  1.000 171.349 ? 201 ASN HHH CB  1 
ATOM   9843  C CG  . ASN G 2 202 ? -22.433 -60.395 42.441  1.000 174.822 ? 201 ASN HHH CG  1 
ATOM   9844  O OD1 . ASN G 2 202 ? -22.804 -59.820 43.463  1.000 173.385 ? 201 ASN HHH OD1 1 
ATOM   9845  N ND2 . ASN G 2 202 ? -22.648 -61.687 42.242  1.000 178.614 ? 201 ASN HHH ND2 1 
ATOM   9846  N N   . VAL G 2 203 ? -18.699 -58.446 39.973  1.000 158.526 ? 202 VAL HHH N   1 
ATOM   9847  C CA  . VAL G 2 203 ? -17.949 -57.466 39.131  1.000 154.687 ? 202 VAL HHH CA  1 
ATOM   9848  C C   . VAL G 2 203 ? -17.976 -57.930 37.677  1.000 155.905 ? 202 VAL HHH C   1 
ATOM   9849  O O   . VAL G 2 203 ? -17.482 -59.038 37.420  1.000 157.518 ? 202 VAL HHH O   1 
ATOM   9850  C CB  . VAL G 2 203 ? -16.498 -57.312 39.613  1.000 152.024 ? 202 VAL HHH CB  1 
ATOM   9851  C CG1 . VAL G 2 203 ? -15.750 -56.269 38.797  1.000 148.728 ? 202 VAL HHH CG1 1 
ATOM   9852  C CG2 . VAL G 2 203 ? -16.435 -56.998 41.097  1.000 151.899 ? 202 VAL HHH CG2 1 
ATOM   9853  N N   . ASN G 2 204 ? -18.496 -57.084 36.780  1.000 155.376 ? 203 ASN HHH N   1 
ATOM   9854  C CA  . ASN G 2 204 ? -18.669 -57.374 35.331  1.000 156.417 ? 203 ASN HHH CA  1 
ATOM   9855  C C   . ASN G 2 204 ? -17.844 -56.376 34.511  1.000 154.307 ? 203 ASN HHH C   1 
ATOM   9856  O O   . ASN G 2 204 ? -17.925 -55.153 34.779  1.000 153.318 ? 203 ASN HHH O   1 
ATOM   9857  C CB  . ASN G 2 204 ? -20.145 -57.336 34.924  1.000 157.057 ? 203 ASN HHH CB  1 
ATOM   9858  C CG  . ASN G 2 204 ? -21.026 -58.151 35.847  1.000 160.040 ? 203 ASN HHH CG  1 
ATOM   9859  O OD1 . ASN G 2 204 ? -20.578 -59.134 36.430  1.000 161.013 ? 203 ASN HHH OD1 1 
ATOM   9860  N ND2 . ASN G 2 204 ? -22.277 -57.746 35.995  1.000 162.437 ? 203 ASN HHH ND2 1 
ATOM   9861  N N   . HIS G 2 205 ? -17.063 -56.897 33.564  1.000 154.144 ? 204 HIS HHH N   1 
ATOM   9862  C CA  . HIS G 2 205 ? -16.297 -56.130 32.549  1.000 150.552 ? 204 HIS HHH CA  1 
ATOM   9863  C C   . HIS G 2 205 ? -16.784 -56.587 31.178  1.000 152.294 ? 204 HIS HHH C   1 
ATOM   9864  O O   . HIS G 2 205 ? -16.538 -57.750 30.831  1.000 154.661 ? 204 HIS HHH O   1 
ATOM   9865  C CB  . HIS G 2 205 ? -14.793 -56.353 32.737  1.000 149.480 ? 204 HIS HHH CB  1 
ATOM   9866  C CG  . HIS G 2 205 ? -13.931 -55.473 31.899  1.000 147.324 ? 204 HIS HHH CG  1 
ATOM   9867  N ND1 . HIS G 2 205 ? -12.830 -55.959 31.217  1.000 148.381 ? 204 HIS HHH ND1 1 
ATOM   9868  C CD2 . HIS G 2 205 ? -13.988 -54.146 31.651  1.000 145.140 ? 204 HIS HHH CD2 1 
ATOM   9869  C CE1 . HIS G 2 205 ? -12.245 -54.968 30.580  1.000 147.827 ? 204 HIS HHH CE1 1 
ATOM   9870  N NE2 . HIS G 2 205 ? -12.938 -53.843 30.828  1.000 145.690 ? 204 HIS HHH NE2 1 
ATOM   9871  N N   . LYS G 2 206 ? -17.480 -55.714 30.452  1.000 152.205 ? 205 LYS HHH N   1 
ATOM   9872  C CA  . LYS G 2 206 ? -18.164 -56.081 29.182  1.000 155.079 ? 205 LYS HHH CA  1 
ATOM   9873  C C   . LYS G 2 206 ? -17.105 -56.451 28.145  1.000 155.241 ? 205 LYS HHH C   1 
ATOM   9874  O O   . LYS G 2 206 ? -17.138 -57.559 27.619  1.000 158.097 ? 205 LYS HHH O   1 
ATOM   9875  C CB  . LYS G 2 206 ? -19.117 -54.972 28.716  1.000 155.577 ? 205 LYS HHH CB  1 
ATOM   9876  C CG  . LYS G 2 206 ? -19.932 -54.294 29.819  1.000 155.323 ? 205 LYS HHH CG  1 
ATOM   9877  C CD  . LYS G 2 206 ? -21.369 -53.955 29.442  1.000 156.625 ? 205 LYS HHH CD  1 
ATOM   9878  C CE  . LYS G 2 206 ? -22.284 -55.161 29.504  1.000 158.768 ? 205 LYS HHH CE  1 
ATOM   9879  N NZ  . LYS G 2 206 ? -23.701 -54.794 29.277  1.000 159.639 ? 205 LYS HHH NZ  1 
ATOM   9880  N N   . PRO G 2 207 ? -16.104 -55.584 27.861  1.000 153.039 ? 206 PRO HHH N   1 
ATOM   9881  C CA  . PRO G 2 207 ? -15.115 -55.864 26.816  1.000 153.643 ? 206 PRO HHH CA  1 
ATOM   9882  C C   . PRO G 2 207 ? -14.467 -57.260 26.874  1.000 155.008 ? 206 PRO HHH C   1 
ATOM   9883  O O   . PRO G 2 207 ? -14.242 -57.843 25.827  1.000 157.118 ? 206 PRO HHH O   1 
ATOM   9884  C CB  . PRO G 2 207 ? -14.046 -54.785 27.059  1.000 151.920 ? 206 PRO HHH CB  1 
ATOM   9885  C CG  . PRO G 2 207 ? -14.820 -53.632 27.660  1.000 150.133 ? 206 PRO HHH CG  1 
ATOM   9886  C CD  . PRO G 2 207 ? -15.849 -54.303 28.544  1.000 150.550 ? 206 PRO HHH CD  1 
ATOM   9887  N N   . SER G 2 208 ? -14.179 -57.761 28.080  1.000 154.218 ? 207 SER HHH N   1 
ATOM   9888  C CA  . SER G 2 208 ? -13.496 -59.063 28.318  1.000 155.410 ? 207 SER HHH CA  1 
ATOM   9889  C C   . SER G 2 208 ? -14.505 -60.146 28.735  1.000 156.213 ? 207 SER HHH C   1 
ATOM   9890  O O   . SER G 2 208 ? -14.053 -61.243 29.092  1.000 156.781 ? 207 SER HHH O   1 
ATOM   9891  C CB  . SER G 2 208 ? -12.371 -58.906 29.331  1.000 154.379 ? 207 SER HHH CB  1 
ATOM   9892  O OG  . SER G 2 208 ? -12.871 -58.661 30.640  1.000 152.667 ? 207 SER HHH OG  1 
ATOM   9893  N N   . ASN G 2 209 ? -15.813 -59.858 28.680  1.000 155.444 ? 208 ASN HHH N   1 
ATOM   9894  C CA  . ASN G 2 209 ? -16.920 -60.802 29.006  1.000 159.004 ? 208 ASN HHH CA  1 
ATOM   9895  C C   . ASN G 2 209 ? -16.496 -61.675 30.198  1.000 161.419 ? 208 ASN HHH C   1 
ATOM   9896  O O   . ASN G 2 209 ? -16.508 -62.919 30.050  1.000 166.176 ? 208 ASN HHH O   1 
ATOM   9897  C CB  . ASN G 2 209 ? -17.331 -61.623 27.773  1.000 162.104 ? 208 ASN HHH CB  1 
ATOM   9898  C CG  . ASN G 2 209 ? -18.816 -61.950 27.672  1.000 163.928 ? 208 ASN HHH CG  1 
ATOM   9899  O OD1 . ASN G 2 209 ? -19.200 -62.889 26.976  1.000 165.919 ? 208 ASN HHH OD1 1 
ATOM   9900  N ND2 . ASN G 2 209 ? -19.675 -61.178 28.323  1.000 161.318 ? 208 ASN HHH ND2 1 
ATOM   9901  N N   . THR G 2 210 ? -16.115 -61.045 31.323  1.000 159.724 ? 209 THR HHH N   1 
ATOM   9902  C CA  . THR G 2 210 ? -15.762 -61.712 32.613  1.000 160.845 ? 209 THR HHH CA  1 
ATOM   9903  C C   . THR G 2 210 ? -16.518 -61.079 33.785  1.000 159.908 ? 209 THR HHH C   1 
ATOM   9904  O O   . THR G 2 210 ? -16.308 -59.881 34.059  1.000 155.131 ? 209 THR HHH O   1 
ATOM   9905  C CB  . THR G 2 210 ? -14.262 -61.671 32.933  1.000 158.697 ? 209 THR HHH CB  1 
ATOM   9906  O OG1 . THR G 2 210 ? -13.766 -60.377 32.599  1.000 153.857 ? 209 THR HHH OG1 1 
ATOM   9907  C CG2 . THR G 2 210 ? -13.480 -62.745 32.210  1.000 161.589 ? 209 THR HHH CG2 1 
ATOM   9908  N N   . LYS G 2 211 ? -17.358 -61.887 34.438  1.000 164.760 ? 210 LYS HHH N   1 
ATOM   9909  C CA  . LYS G 2 211 ? -17.967 -61.613 35.765  1.000 165.991 ? 210 LYS HHH CA  1 
ATOM   9910  C C   . LYS G 2 211 ? -16.971 -62.102 36.818  1.000 165.766 ? 210 LYS HHH C   1 
ATOM   9911  O O   . LYS G 2 211 ? -16.053 -62.850 36.442  1.000 166.304 ? 210 LYS HHH O   1 
ATOM   9912  C CB  . LYS G 2 211 ? -19.337 -62.299 35.869  1.000 171.036 ? 210 LYS HHH CB  1 
ATOM   9913  C CG  . LYS G 2 211 ? -20.044 -62.227 37.220  1.000 172.081 ? 210 LYS HHH CG  1 
ATOM   9914  C CD  . LYS G 2 211 ? -21.575 -62.280 37.139  1.000 174.763 ? 210 LYS HHH CD  1 
ATOM   9915  C CE  . LYS G 2 211 ? -22.143 -63.536 36.505  1.000 179.935 ? 210 LYS HHH CE  1 
ATOM   9916  N NZ  . LYS G 2 211 ? -22.262 -64.649 37.478  1.000 184.735 ? 210 LYS HHH NZ  1 
ATOM   9917  N N   . VAL G 2 212 ? -17.113 -61.649 38.064  1.000 165.589 ? 211 VAL HHH N   1 
ATOM   9918  C CA  . VAL G 2 212 ? -16.383 -62.201 39.243  1.000 167.628 ? 211 VAL HHH CA  1 
ATOM   9919  C C   . VAL G 2 212 ? -17.289 -62.103 40.470  1.000 170.681 ? 211 VAL HHH C   1 
ATOM   9920  O O   . VAL G 2 212 ? -17.677 -60.976 40.816  1.000 168.422 ? 211 VAL HHH O   1 
ATOM   9921  C CB  . VAL G 2 212 ? -15.051 -61.476 39.501  1.000 164.062 ? 211 VAL HHH CB  1 
ATOM   9922  C CG1 . VAL G 2 212 ? -14.277 -62.162 40.619  1.000 165.717 ? 211 VAL HHH CG1 1 
ATOM   9923  C CG2 . VAL G 2 212 ? -14.200 -61.359 38.243  1.000 162.572 ? 211 VAL HHH CG2 1 
ATOM   9924  N N   . ASP G 2 213 ? -17.599 -63.248 41.085  1.000 177.011 ? 212 ASP HHH N   1 
ATOM   9925  C CA  . ASP G 2 213 ? -18.352 -63.358 42.361  1.000 180.605 ? 212 ASP HHH CA  1 
ATOM   9926  C C   . ASP G 2 213 ? -17.335 -63.536 43.492  1.000 180.905 ? 212 ASP HHH C   1 
ATOM   9927  O O   . ASP G 2 213 ? -17.032 -64.702 43.831  1.000 187.771 ? 212 ASP HHH O   1 
ATOM   9928  C CB  . ASP G 2 213 ? -19.360 -64.512 42.300  1.000 186.793 ? 212 ASP HHH CB  1 
ATOM   9929  C CG  . ASP G 2 213 ? -20.499 -64.305 41.312  1.000 188.099 ? 212 ASP HHH CG  1 
ATOM   9930  O OD1 . ASP G 2 213 ? -20.567 -63.212 40.706  1.000 184.369 ? 212 ASP HHH OD1 1 
ATOM   9931  O OD2 . ASP G 2 213 ? -21.311 -65.240 41.157  1.000 192.956 ? 212 ASP HHH OD2 1 
ATOM   9932  N N   . LYS G 2 214 ? -16.821 -62.426 44.038  1.000 176.161 ? 213 LYS HHH N   1 
ATOM   9933  C CA  . LYS G 2 214 ? -15.732 -62.422 45.053  1.000 174.726 ? 213 LYS HHH CA  1 
ATOM   9934  C C   . LYS G 2 214 ? -16.303 -62.222 46.463  1.000 173.194 ? 213 LYS HHH C   1 
ATOM   9935  O O   . LYS G 2 214 ? -16.740 -61.092 46.783  1.000 168.748 ? 213 LYS HHH O   1 
ATOM   9936  C CB  . LYS G 2 214 ? -14.695 -61.342 44.740  1.000 172.189 ? 213 LYS HHH CB  1 
ATOM   9937  C CG  . LYS G 2 214 ? -13.456 -61.383 45.621  1.000 174.142 ? 213 LYS HHH CG  1 
ATOM   9938  C CD  . LYS G 2 214 ? -12.843 -62.760 45.715  1.000 179.769 ? 213 LYS HHH CD  1 
ATOM   9939  C CE  . LYS G 2 214 ? -11.621 -62.796 46.601  1.000 183.273 ? 213 LYS HHH CE  1 
ATOM   9940  N NZ  . LYS G 2 214 ? -11.167 -64.189 46.832  1.000 188.892 ? 213 LYS HHH NZ  1 
ATOM   9941  N N   . LYS G 2 215 ? -16.276 -63.291 47.268  1.000 173.498 ? 214 LYS HHH N   1 
ATOM   9942  C CA  . LYS G 2 215 ? -16.711 -63.301 48.688  1.000 173.317 ? 214 LYS HHH CA  1 
ATOM   9943  C C   . LYS G 2 215 ? -15.729 -62.448 49.499  1.000 169.077 ? 214 LYS HHH C   1 
ATOM   9944  O O   . LYS G 2 215 ? -14.512 -62.585 49.281  1.000 166.239 ? 214 LYS HHH O   1 
ATOM   9945  C CB  . LYS G 2 215 ? -16.796 -64.746 49.196  1.000 177.819 ? 214 LYS HHH CB  1 
ATOM   9946  C CG  . LYS G 2 215 ? -16.930 -64.915 50.707  1.000 180.960 ? 214 LYS HHH CG  1 
ATOM   9947  C CD  . LYS G 2 215 ? -18.338 -65.200 51.201  1.000 184.263 ? 214 LYS HHH CD  1 
ATOM   9948  C CE  . LYS G 2 215 ? -18.351 -65.746 52.614  1.000 187.961 ? 214 LYS HHH CE  1 
ATOM   9949  N NZ  . LYS G 2 215 ? -19.702 -66.180 53.035  1.000 192.594 ? 214 LYS HHH NZ  1 
ATOM   9950  N N   . VAL G 2 216 ? -16.255 -61.583 50.370  1.000 168.118 ? 215 VAL HHH N   1 
ATOM   9951  C CA  . VAL G 2 216 ? -15.484 -60.764 51.348  1.000 166.570 ? 215 VAL HHH CA  1 
ATOM   9952  C C   . VAL G 2 216 ? -15.845 -61.263 52.748  1.000 171.007 ? 215 VAL HHH C   1 
ATOM   9953  O O   . VAL G 2 216 ? -17.008 -61.662 52.933  1.000 174.385 ? 215 VAL HHH O   1 
ATOM   9954  C CB  . VAL G 2 216 ? -15.803 -59.265 51.193  1.000 163.157 ? 215 VAL HHH CB  1 
ATOM   9955  C CG1 . VAL G 2 216 ? -14.896 -58.408 52.058  1.000 162.513 ? 215 VAL HHH CG1 1 
ATOM   9956  C CG2 . VAL G 2 216 ? -15.728 -58.816 49.742  1.000 160.243 ? 215 VAL HHH CG2 1 
ATOM   9957  N N   . GLU G 2 217 ? -14.896 -61.240 53.688  1.000 172.551 ? 216 GLU HHH N   1 
ATOM   9958  C CA  . GLU G 2 217 ? -15.139 -61.586 55.116  1.000 178.971 ? 216 GLU HHH CA  1 
ATOM   9959  C C   . GLU G 2 217 ? -13.969 -61.104 55.970  1.000 179.058 ? 216 GLU HHH C   1 
ATOM   9960  O O   . GLU G 2 217 ? -12.913 -60.801 55.428  1.000 178.430 ? 216 GLU HHH O   1 
ATOM   9961  C CB  . GLU G 2 217 ? -15.385 -63.091 55.246  1.000 185.649 ? 216 GLU HHH CB  1 
ATOM   9962  C CG  . GLU G 2 217 ? -14.349 -63.980 54.582  1.000 187.816 ? 216 GLU HHH CG  1 
ATOM   9963  C CD  . GLU G 2 217 ? -14.630 -65.460 54.820  1.000 196.028 ? 216 GLU HHH CD  1 
ATOM   9964  O OE1 . GLU G 2 217 ? -15.635 -65.958 54.263  1.000 198.879 ? 216 GLU HHH OE1 1 
ATOM   9965  O OE2 . GLU G 2 217 ? -13.872 -66.107 55.594  1.000 201.551 ? 216 GLU HHH OE2 1 
ATOM   9966  N N   . PRO G 2 218 ? -14.113 -60.998 57.315  1.000 181.932 ? 217 PRO HHH N   1 
ATOM   9967  C CA  . PRO G 2 218 ? -13.006 -60.580 58.178  1.000 182.930 ? 217 PRO HHH CA  1 
ATOM   9968  C C   . PRO G 2 218 ? -11.846 -61.593 58.216  1.000 185.278 ? 217 PRO HHH C   1 
ATOM   9969  O O   . PRO G 2 218 ? -12.071 -62.757 57.941  1.000 186.859 ? 217 PRO HHH O   1 
ATOM   9970  C CB  . PRO G 2 218 ? -13.668 -60.428 59.558  1.000 185.965 ? 217 PRO HHH CB  1 
ATOM   9971  C CG  . PRO G 2 218 ? -14.853 -61.363 59.506  1.000 188.338 ? 217 PRO HHH CG  1 
ATOM   9972  C CD  . PRO G 2 218 ? -15.341 -61.265 58.078  1.000 185.058 ? 217 PRO HHH CD  1 
ATOM   9973  N N   . LYS G 2 219 ? -10.648 -61.114 58.569  1.000 185.478 ? 218 LYS HHH N   1 
ATOM   9974  C CA  . LYS G 2 219 ? -9.336  -61.799 58.385  1.000 187.312 ? 218 LYS HHH CA  1 
ATOM   9975  C C   . LYS G 2 219 ? -8.947  -62.572 59.661  1.000 190.504 ? 218 LYS HHH C   1 
ATOM   9976  O O   . LYS G 2 219 ? -9.725  -62.547 60.631  1.000 193.605 ? 218 LYS HHH O   1 
ATOM   9977  C CB  . LYS G 2 219 ? -8.302  -60.722 58.028  1.000 186.691 ? 218 LYS HHH CB  1 
ATOM   9978  C CG  . LYS G 2 219 ? -7.055  -61.187 57.285  1.000 188.034 ? 218 LYS HHH CG  1 
ATOM   9979  C CD  . LYS G 2 219 ? -5.884  -60.211 57.376  1.000 187.185 ? 218 LYS HHH CD  1 
ATOM   9980  C CE  . LYS G 2 219 ? -6.178  -58.823 56.840  1.000 182.724 ? 218 LYS HHH CE  1 
ATOM   9981  N NZ  . LYS G 2 219 ? -6.505  -58.845 55.395  1.000 178.908 ? 218 LYS HHH NZ  1 
ATOM   9982  N N   . SER G 2 220 ? -7.796  -63.260 59.650  1.000 189.274 ? 219 SER HHH N   1 
ATOM   9983  C CA  . SER G 2 220 ? -7.049  -63.722 60.852  1.000 192.327 ? 219 SER HHH CA  1 
ATOM   9984  C C   . SER G 2 220 ? -5.553  -63.437 60.661  1.000 191.269 ? 219 SER HHH C   1 
ATOM   9985  O O   . SER G 2 220 ? -4.904  -62.721 61.431  1.000 191.726 ? 219 SER HHH O   1 
ATOM   9986  C CB  . SER G 2 220 ? -7.302  -65.183 61.128  1.000 195.792 ? 219 SER HHH CB  1 
ATOM   9987  O OG  . SER G 2 220 ? -6.846  -65.553 62.425  1.000 198.643 ? 219 SER HHH OG  1 
ATOM   9988  N N   . ASP H 3 1   ? -17.593 -17.988 12.947  1.000 154.968 ? 1   ASP LLL N   1 
ATOM   9989  C CA  . ASP H 3 1   ? -16.528 -18.717 13.704  1.000 154.038 ? 1   ASP LLL CA  1 
ATOM   9990  C C   . ASP H 3 1   ? -16.665 -18.420 15.208  1.000 151.403 ? 1   ASP LLL C   1 
ATOM   9991  O O   . ASP H 3 1   ? -15.637 -18.081 15.847  1.000 153.202 ? 1   ASP LLL O   1 
ATOM   9992  C CB  . ASP H 3 1   ? -15.151 -18.347 13.146  1.000 160.047 ? 1   ASP LLL CB  1 
ATOM   9993  C CG  . ASP H 3 1   ? -14.031 -19.272 13.592  1.000 160.647 ? 1   ASP LLL CG  1 
ATOM   9994  O OD1 . ASP H 3 1   ? -14.326 -20.230 14.346  1.000 154.215 ? 1   ASP LLL OD1 1 
ATOM   9995  O OD2 . ASP H 3 1   ? -12.870 -19.022 13.186  1.000 164.471 ? 1   ASP LLL OD2 1 
ATOM   9996  N N   . ILE H 3 2   ? -17.863 -18.639 15.770  1.000 147.627 ? 2   ILE LLL N   1 
ATOM   9997  C CA  . ILE H 3 2   ? -18.282 -18.217 17.152  1.000 144.782 ? 2   ILE LLL CA  1 
ATOM   9998  C C   . ILE H 3 2   ? -17.678 -19.147 18.215  1.000 144.130 ? 2   ILE LLL C   1 
ATOM   9999  O O   . ILE H 3 2   ? -17.364 -20.303 17.895  1.000 145.987 ? 2   ILE LLL O   1 
ATOM   10000 C CB  . ILE H 3 2   ? -19.817 -18.166 17.296  1.000 139.482 ? 2   ILE LLL CB  1 
ATOM   10001 C CG1 . ILE H 3 2   ? -20.452 -17.243 16.253  1.000 142.392 ? 2   ILE LLL CG1 1 
ATOM   10002 C CG2 . ILE H 3 2   ? -20.220 -17.772 18.712  1.000 136.600 ? 2   ILE LLL CG2 1 
ATOM   10003 C CD1 . ILE H 3 2   ? -21.964 -17.250 16.257  1.000 140.666 ? 2   ILE LLL CD1 1 
ATOM   10004 N N   . GLN H 3 3   ? -17.540 -18.650 19.443  1.000 144.442 ? 3   GLN LLL N   1 
ATOM   10005 C CA  . GLN H 3 3   ? -16.888 -19.381 20.555  1.000 144.536 ? 3   GLN LLL CA  1 
ATOM   10006 C C   . GLN H 3 3   ? -17.421 -18.878 21.896  1.000 142.038 ? 3   GLN LLL C   1 
ATOM   10007 O O   . GLN H 3 3   ? -17.589 -17.648 22.042  1.000 144.034 ? 3   GLN LLL O   1 
ATOM   10008 C CB  . GLN H 3 3   ? -15.380 -19.180 20.462  1.000 153.026 ? 3   GLN LLL CB  1 
ATOM   10009 C CG  . GLN H 3 3   ? -14.599 -20.127 21.351  1.000 157.068 ? 3   GLN LLL CG  1 
ATOM   10010 C CD  . GLN H 3 3   ? -13.188 -20.318 20.851  1.000 166.109 ? 3   GLN LLL CD  1 
ATOM   10011 O OE1 . GLN H 3 3   ? -12.778 -19.763 19.829  1.000 174.049 ? 3   GLN LLL OE1 1 
ATOM   10012 N NE2 . GLN H 3 3   ? -12.429 -21.121 21.576  1.000 169.077 ? 3   GLN LLL NE2 1 
ATOM   10013 N N   . LEU H 3 4   ? -17.654 -19.805 22.835  1.000 137.696 ? 4   LEU LLL N   1 
ATOM   10014 C CA  . LEU H 3 4   ? -18.366 -19.559 24.118  1.000 133.753 ? 4   LEU LLL CA  1 
ATOM   10015 C C   . LEU H 3 4   ? -17.459 -19.877 25.307  1.000 135.009 ? 4   LEU LLL C   1 
ATOM   10016 O O   . LEU H 3 4   ? -16.707 -20.881 25.235  1.000 133.201 ? 4   LEU LLL O   1 
ATOM   10017 C CB  . LEU H 3 4   ? -19.619 -20.433 24.176  1.000 127.936 ? 4   LEU LLL CB  1 
ATOM   10018 C CG  . LEU H 3 4   ? -20.722 -20.076 23.185  1.000 127.071 ? 4   LEU LLL CG  1 
ATOM   10019 C CD1 . LEU H 3 4   ? -21.921 -20.988 23.370  1.000 123.689 ? 4   LEU LLL CD1 1 
ATOM   10020 C CD2 . LEU H 3 4   ? -21.133 -18.620 23.324  1.000 129.181 ? 4   LEU LLL CD2 1 
ATOM   10021 N N   . THR H 3 5   ? -17.566 -19.054 26.357  1.000 137.452 ? 5   THR LLL N   1 
ATOM   10022 C CA  . THR H 3 5   ? -16.918 -19.246 27.683  1.000 139.164 ? 5   THR LLL CA  1 
ATOM   10023 C C   . THR H 3 5   ? -17.962 -19.003 28.781  1.000 135.829 ? 5   THR LLL C   1 
ATOM   10024 O O   . THR H 3 5   ? -18.457 -17.865 28.877  1.000 136.023 ? 5   THR LLL O   1 
ATOM   10025 C CB  . THR H 3 5   ? -15.656 -18.380 27.833  1.000 146.188 ? 5   THR LLL CB  1 
ATOM   10026 O OG1 . THR H 3 5   ? -15.646 -17.341 26.850  1.000 151.213 ? 5   THR LLL OG1 1 
ATOM   10027 C CG2 . THR H 3 5   ? -14.381 -19.184 27.682  1.000 147.346 ? 5   THR LLL CG2 1 
ATOM   10028 N N   . GLN H 3 6   ? -18.299 -20.056 29.535  1.000 133.104 ? 6   GLN LLL N   1 
ATOM   10029 C CA  . GLN H 3 6   ? -19.208 -20.019 30.712  1.000 134.093 ? 6   GLN LLL CA  1 
ATOM   10030 C C   . GLN H 3 6   ? -18.401 -19.607 31.947  1.000 139.549 ? 6   GLN LLL C   1 
ATOM   10031 O O   . GLN H 3 6   ? -17.160 -19.673 31.875  1.000 145.298 ? 6   GLN LLL O   1 
ATOM   10032 C CB  . GLN H 3 6   ? -19.856 -21.385 30.961  1.000 131.495 ? 6   GLN LLL CB  1 
ATOM   10033 C CG  . GLN H 3 6   ? -20.835 -21.825 29.879  1.000 130.112 ? 6   GLN LLL CG  1 
ATOM   10034 C CD  . GLN H 3 6   ? -21.379 -23.226 30.068  1.000 127.180 ? 6   GLN LLL CD  1 
ATOM   10035 O OE1 . GLN H 3 6   ? -21.068 -24.142 29.309  1.000 126.308 ? 6   GLN LLL OE1 1 
ATOM   10036 N NE2 . GLN H 3 6   ? -22.212 -23.408 31.081  1.000 124.320 ? 6   GLN LLL NE2 1 
ATOM   10037 N N   . SER H 3 7   ? -19.077 -19.211 33.033  1.000 141.199 ? 7   SER LLL N   1 
ATOM   10038 C CA  . SER H 3 7   ? -18.480 -18.956 34.375  1.000 143.744 ? 7   SER LLL CA  1 
ATOM   10039 C C   . SER H 3 7   ? -19.596 -18.838 35.415  1.000 143.577 ? 7   SER LLL C   1 
ATOM   10040 O O   . SER H 3 7   ? -20.646 -18.271 35.120  1.000 142.583 ? 7   SER LLL O   1 
ATOM   10041 C CB  . SER H 3 7   ? -17.589 -17.733 34.362  1.000 147.720 ? 7   SER LLL CB  1 
ATOM   10042 O OG  . SER H 3 7   ? -18.282 -16.604 33.853  1.000 148.810 ? 7   SER LLL OG  1 
ATOM   10043 N N   . PRO H 3 8   ? -19.429 -19.375 36.649  1.000 144.761 ? 8   PRO LLL N   1 
ATOM   10044 C CA  . PRO H 3 8   ? -18.200 -20.050 37.066  1.000 145.315 ? 8   PRO LLL CA  1 
ATOM   10045 C C   . PRO H 3 8   ? -18.217 -21.507 36.587  1.000 140.477 ? 8   PRO LLL C   1 
ATOM   10046 O O   . PRO H 3 8   ? -19.203 -21.899 35.991  1.000 135.974 ? 8   PRO LLL O   1 
ATOM   10047 C CB  . PRO H 3 8   ? -18.270 -19.944 38.595  1.000 149.625 ? 8   PRO LLL CB  1 
ATOM   10048 C CG  . PRO H 3 8   ? -19.756 -20.055 38.887  1.000 148.266 ? 8   PRO LLL CG  1 
ATOM   10049 C CD  . PRO H 3 8   ? -20.449 -19.391 37.711  1.000 146.233 ? 8   PRO LLL CD  1 
ATOM   10050 N N   . ASP H 3 9   ? -17.140 -22.254 36.856  1.000 142.471 ? 9   ASP LLL N   1 
ATOM   10051 C CA  . ASP H 3 9   ? -16.966 -23.679 36.455  1.000 140.854 ? 9   ASP LLL CA  1 
ATOM   10052 C C   . ASP H 3 9   ? -17.724 -24.577 37.448  1.000 139.219 ? 9   ASP LLL C   1 
ATOM   10053 O O   . ASP H 3 9   ? -18.344 -25.565 37.006  1.000 134.318 ? 9   ASP LLL O   1 
ATOM   10054 C CB  . ASP H 3 9   ? -15.479 -24.042 36.359  1.000 145.247 ? 9   ASP LLL CB  1 
ATOM   10055 C CG  . ASP H 3 9   ? -14.724 -23.355 35.224  1.000 149.084 ? 9   ASP LLL CG  1 
ATOM   10056 O OD1 . ASP H 3 9   ? -14.940 -23.740 34.050  1.000 148.040 ? 9   ASP LLL OD1 1 
ATOM   10057 O OD2 . ASP H 3 9   ? -13.914 -22.444 35.519  1.000 154.944 ? 9   ASP LLL OD2 1 
ATOM   10058 N N   . SER H 3 10  ? -17.678 -24.236 38.740  1.000 144.246 ? 10  SER LLL N   1 
ATOM   10059 C CA  . SER H 3 10  ? -18.429 -24.898 39.839  1.000 144.277 ? 10  SER LLL CA  1 
ATOM   10060 C C   . SER H 3 10  ? -19.367 -23.891 40.513  1.000 144.123 ? 10  SER LLL C   1 
ATOM   10061 O O   . SER H 3 10  ? -19.056 -22.685 40.516  1.000 148.037 ? 10  SER LLL O   1 
ATOM   10062 C CB  . SER H 3 10  ? -17.492 -25.505 40.846  1.000 149.626 ? 10  SER LLL CB  1 
ATOM   10063 O OG  . SER H 3 10  ? -18.202 -25.905 42.011  1.000 153.011 ? 10  SER LLL OG  1 
ATOM   10064 N N   . LEU H 3 11  ? -20.459 -24.377 41.102  1.000 140.443 ? 11  LEU LLL N   1 
ATOM   10065 C CA  . LEU H 3 11  ? -21.413 -23.531 41.857  1.000 141.327 ? 11  LEU LLL CA  1 
ATOM   10066 C C   . LEU H 3 11  ? -22.101 -24.376 42.931  1.000 138.679 ? 11  LEU LLL C   1 
ATOM   10067 O O   . LEU H 3 11  ? -22.869 -25.283 42.580  1.000 134.460 ? 11  LEU LLL O   1 
ATOM   10068 C CB  . LEU H 3 11  ? -22.415 -22.919 40.874  1.000 141.148 ? 11  LEU LLL CB  1 
ATOM   10069 C CG  . LEU H 3 11  ? -23.270 -21.777 41.431  1.000 145.914 ? 11  LEU LLL CG  1 
ATOM   10070 C CD1 . LEU H 3 11  ? -22.400 -20.634 41.950  1.000 151.048 ? 11  LEU LLL CD1 1 
ATOM   10071 C CD2 . LEU H 3 11  ? -24.257 -21.285 40.387  1.000 143.272 ? 11  LEU LLL CD2 1 
ATOM   10072 N N   . ALA H 3 12  ? -21.821 -24.070 44.195  1.000 142.014 ? 12  ALA LLL N   1 
ATOM   10073 C CA  . ALA H 3 12  ? -22.453 -24.688 45.380  1.000 144.190 ? 12  ALA LLL CA  1 
ATOM   10074 C C   . ALA H 3 12  ? -23.462 -23.703 45.983  1.000 145.902 ? 12  ALA LLL C   1 
ATOM   10075 O O   . ALA H 3 12  ? -23.059 -22.571 46.315  1.000 149.948 ? 12  ALA LLL O   1 
ATOM   10076 C CB  . ALA H 3 12  ? -21.382 -25.070 46.368  1.000 148.726 ? 12  ALA LLL CB  1 
ATOM   10077 N N   . VAL H 3 13  ? -24.719 -24.128 46.139  1.000 143.525 ? 13  VAL LLL N   1 
ATOM   10078 C CA  . VAL H 3 13  ? -25.852 -23.261 46.584  1.000 145.714 ? 13  VAL LLL CA  1 
ATOM   10079 C C   . VAL H 3 13  ? -26.725 -24.027 47.586  1.000 147.488 ? 13  VAL LLL C   1 
ATOM   10080 O O   . VAL H 3 13  ? -26.977 -25.226 47.346  1.000 146.133 ? 13  VAL LLL O   1 
ATOM   10081 C CB  . VAL H 3 13  ? -26.659 -22.793 45.360  1.000 142.806 ? 13  VAL LLL CB  1 
ATOM   10082 C CG1 . VAL H 3 13  ? -28.015 -22.210 45.738  1.000 145.351 ? 13  VAL LLL CG1 1 
ATOM   10083 C CG2 . VAL H 3 13  ? -25.849 -21.803 44.536  1.000 142.846 ? 13  VAL LLL CG2 1 
ATOM   10084 N N   . SER H 3 14  ? -27.172 -23.353 48.653  1.000 150.073 ? 14  SER LLL N   1 
ATOM   10085 C CA  . SER H 3 14  ? -28.146 -23.876 49.650  1.000 150.335 ? 14  SER LLL CA  1 
ATOM   10086 C C   . SER H 3 14  ? -29.509 -24.094 48.976  1.000 146.157 ? 14  SER LLL C   1 
ATOM   10087 O O   . SER H 3 14  ? -29.976 -23.174 48.280  1.000 144.713 ? 14  SER LLL O   1 
ATOM   10088 C CB  . SER H 3 14  ? -28.257 -22.961 50.849  1.000 156.656 ? 14  SER LLL CB  1 
ATOM   10089 O OG  . SER H 3 14  ? -27.171 -23.144 51.747  1.000 159.796 ? 14  SER LLL OG  1 
ATOM   10090 N N   . LEU H 3 15  ? -30.108 -25.276 49.161  1.000 144.087 ? 15  LEU LLL N   1 
ATOM   10091 C CA  . LEU H 3 15  ? -31.451 -25.649 48.634  1.000 143.228 ? 15  LEU LLL CA  1 
ATOM   10092 C C   . LEU H 3 15  ? -32.415 -24.470 48.776  1.000 145.224 ? 15  LEU LLL C   1 
ATOM   10093 O O   . LEU H 3 15  ? -32.726 -24.105 49.916  1.000 150.296 ? 15  LEU LLL O   1 
ATOM   10094 C CB  . LEU H 3 15  ? -31.989 -26.846 49.423  1.000 147.082 ? 15  LEU LLL CB  1 
ATOM   10095 C CG  . LEU H 3 15  ? -31.564 -28.223 48.919  1.000 146.232 ? 15  LEU LLL CG  1 
ATOM   10096 C CD1 . LEU H 3 15  ? -31.311 -29.184 50.077  1.000 150.260 ? 15  LEU LLL CD1 1 
ATOM   10097 C CD2 . LEU H 3 15  ? -32.596 -28.796 47.955  1.000 143.952 ? 15  LEU LLL CD2 1 
ATOM   10098 N N   . GLY H 3 16  ? -32.880 -23.911 47.662  1.000 143.040 ? 16  GLY LLL N   1 
ATOM   10099 C CA  . GLY H 3 16  ? -33.968 -22.917 47.650  1.000 147.270 ? 16  GLY LLL CA  1 
ATOM   10100 C C   . GLY H 3 16  ? -33.463 -21.486 47.566  1.000 150.345 ? 16  GLY LLL C   1 
ATOM   10101 O O   . GLY H 3 16  ? -34.302 -20.562 47.662  1.000 152.573 ? 16  GLY LLL O   1 
ATOM   10102 N N   . GLU H 3 17  ? -32.147 -21.296 47.420  1.000 151.315 ? 17  GLU LLL N   1 
ATOM   10103 C CA  . GLU H 3 17  ? -31.529 -19.991 47.061  1.000 154.513 ? 17  GLU LLL CA  1 
ATOM   10104 C C   . GLU H 3 17  ? -31.392 -19.954 45.539  1.000 149.627 ? 17  GLU LLL C   1 
ATOM   10105 O O   . GLU H 3 17  ? -31.487 -21.031 44.918  1.000 143.896 ? 17  GLU LLL O   1 
ATOM   10106 C CB  . GLU H 3 17  ? -30.161 -19.789 47.723  1.000 158.114 ? 17  GLU LLL CB  1 
ATOM   10107 C CG  . GLU H 3 17  ? -30.134 -20.045 49.224  1.000 166.286 ? 17  GLU LLL CG  1 
ATOM   10108 C CD  . GLU H 3 17  ? -30.782 -18.993 50.123  1.000 175.971 ? 17  GLU LLL CD  1 
ATOM   10109 O OE1 . GLU H 3 17  ? -31.823 -18.419 49.724  1.000 178.705 ? 17  GLU LLL OE1 1 
ATOM   10110 O OE2 . GLU H 3 17  ? -30.255 -18.760 51.244  1.000 182.311 ? 17  GLU LLL OE2 1 
ATOM   10111 N N   . ARG H 3 18  ? -31.193 -18.758 44.978  1.000 150.356 ? 18  ARG LLL N   1 
ATOM   10112 C CA  . ARG H 3 18  ? -30.945 -18.516 43.532  1.000 145.831 ? 18  ARG LLL CA  1 
ATOM   10113 C C   . ARG H 3 18  ? -29.594 -19.133 43.159  1.000 142.892 ? 18  ARG LLL C   1 
ATOM   10114 O O   . ARG H 3 18  ? -28.805 -19.410 44.066  1.000 144.370 ? 18  ARG LLL O   1 
ATOM   10115 C CB  . ARG H 3 18  ? -30.964 -17.007 43.254  1.000 149.545 ? 18  ARG LLL CB  1 
ATOM   10116 C CG  . ARG H 3 18  ? -30.928 -16.603 41.784  1.000 146.833 ? 18  ARG LLL CG  1 
ATOM   10117 C CD  . ARG H 3 18  ? -31.082 -15.105 41.563  1.000 150.714 ? 18  ARG LLL CD  1 
ATOM   10118 N NE  . ARG H 3 18  ? -32.216 -14.565 42.309  1.000 156.388 ? 18  ARG LLL NE  1 
ATOM   10119 C CZ  . ARG H 3 18  ? -33.481 -14.508 41.884  1.000 156.964 ? 18  ARG LLL CZ  1 
ATOM   10120 N NH1 . ARG H 3 18  ? -33.819 -14.936 40.678  1.000 152.029 ? 18  ARG LLL NH1 1 
ATOM   10121 N NH2 . ARG H 3 18  ? -34.412 -14.016 42.683  1.000 162.634 ? 18  ARG LLL NH2 1 
ATOM   10122 N N   . ALA H 3 19  ? -29.358 -19.349 41.867  1.000 140.420 ? 19  ALA LLL N   1 
ATOM   10123 C CA  . ALA H 3 19  ? -28.076 -19.823 41.299  1.000 139.206 ? 19  ALA LLL CA  1 
ATOM   10124 C C   . ALA H 3 19  ? -27.977 -19.310 39.866  1.000 139.852 ? 19  ALA LLL C   1 
ATOM   10125 O O   . ALA H 3 19  ? -28.821 -19.707 39.040  1.000 138.262 ? 19  ALA LLL O   1 
ATOM   10126 C CB  . ALA H 3 19  ? -28.001 -21.325 41.342  1.000 135.914 ? 19  ALA LLL CB  1 
ATOM   10127 N N   . THR H 3 20  ? -27.004 -18.438 39.601  1.000 144.784 ? 20  THR LLL N   1 
ATOM   10128 C CA  . THR H 3 20  ? -26.777 -17.786 38.283  1.000 143.596 ? 20  THR LLL CA  1 
ATOM   10129 C C   . THR H 3 20  ? -25.560 -18.438 37.609  1.000 139.690 ? 20  THR LLL C   1 
ATOM   10130 O O   . THR H 3 20  ? -24.618 -18.849 38.319  1.000 142.395 ? 20  THR LLL O   1 
ATOM   10131 C CB  . THR H 3 20  ? -26.669 -16.262 38.451  1.000 149.198 ? 20  THR LLL CB  1 
ATOM   10132 O OG1 . THR H 3 20  ? -25.982 -15.959 39.668  1.000 155.261 ? 20  THR LLL OG1 1 
ATOM   10133 C CG2 . THR H 3 20  ? -28.015 -15.573 38.497  1.000 150.936 ? 20  THR LLL CG2 1 
ATOM   10134 N N   . ILE H 3 21  ? -25.608 -18.580 36.286  1.000 135.403 ? 21  ILE LLL N   1 
ATOM   10135 C CA  . ILE H 3 21  ? -24.469 -19.063 35.452  1.000 134.538 ? 21  ILE LLL CA  1 
ATOM   10136 C C   . ILE H 3 21  ? -24.328 -18.139 34.237  1.000 137.071 ? 21  ILE LLL C   1 
ATOM   10137 O O   . ILE H 3 21  ? -25.312 -18.018 33.464  1.000 137.188 ? 21  ILE LLL O   1 
ATOM   10138 C CB  . ILE H 3 21  ? -24.666 -20.523 35.016  1.000 129.705 ? 21  ILE LLL CB  1 
ATOM   10139 C CG1 . ILE H 3 21  ? -25.052 -21.426 36.186  1.000 129.801 ? 21  ILE LLL CG1 1 
ATOM   10140 C CG2 . ILE H 3 21  ? -23.424 -21.034 34.301  1.000 128.734 ? 21  ILE LLL CG2 1 
ATOM   10141 C CD1 . ILE H 3 21  ? -25.449 -22.821 35.748  1.000 127.796 ? 21  ILE LLL CD1 1 
ATOM   10142 N N   . ASN H 3 22  ? -23.141 -17.539 34.081  1.000 137.844 ? 22  ASN LLL N   1 
ATOM   10143 C CA  . ASN H 3 22  ? -22.781 -16.624 32.966  1.000 136.291 ? 22  ASN LLL CA  1 
ATOM   10144 C C   . ASN H 3 22  ? -22.204 -17.437 31.806  1.000 133.383 ? 22  ASN LLL C   1 
ATOM   10145 O O   . ASN H 3 22  ? -21.473 -18.412 32.069  1.000 133.465 ? 22  ASN LLL O   1 
ATOM   10146 C CB  . ASN H 3 22  ? -21.795 -15.546 33.418  1.000 139.806 ? 22  ASN LLL CB  1 
ATOM   10147 C CG  . ASN H 3 22  ? -22.459 -14.475 34.253  1.000 143.643 ? 22  ASN LLL CG  1 
ATOM   10148 O OD1 . ASN H 3 22  ? -23.684 -14.377 34.275  1.000 142.417 ? 22  ASN LLL OD1 1 
ATOM   10149 N ND2 . ASN H 3 22  ? -21.664 -13.669 34.939  1.000 149.570 ? 22  ASN LLL ND2 1 
ATOM   10150 N N   . CYS H 3 23  ? -22.533 -17.024 30.579  1.000 131.664 ? 23  CYS LLL N   1 
ATOM   10151 C CA  . CYS H 3 23  ? -22.064 -17.608 29.295  1.000 129.335 ? 23  CYS LLL CA  1 
ATOM   10152 C C   . CYS H 3 23  ? -21.840 -16.458 28.312  1.000 131.317 ? 23  CYS LLL C   1 
ATOM   10153 O O   . CYS H 3 23  ? -22.842 -15.838 27.925  1.000 130.987 ? 23  CYS LLL O   1 
ATOM   10154 C CB  . CYS H 3 23  ? -23.093 -18.602 28.768  1.000 126.175 ? 23  CYS LLL CB  1 
ATOM   10155 S SG  . CYS H 3 23  ? -22.833 -19.127 27.054  1.000 126.110 ? 23  CYS LLL SG  1 
ATOM   10156 N N   . LYS H 3 24  ? -20.582 -16.155 27.973  1.000 133.650 ? 24  LYS LLL N   1 
ATOM   10157 C CA  . LYS H 3 24  ? -20.223 -15.026 27.074  1.000 137.108 ? 24  LYS LLL CA  1 
ATOM   10158 C C   . LYS H 3 24  ? -19.811 -15.584 25.708  1.000 136.926 ? 24  LYS LLL C   1 
ATOM   10159 O O   . LYS H 3 24  ? -19.124 -16.627 25.676  1.000 135.489 ? 24  LYS LLL O   1 
ATOM   10160 C CB  . LYS H 3 24  ? -19.119 -14.163 27.689  1.000 141.810 ? 24  LYS LLL CB  1 
ATOM   10161 C CG  . LYS H 3 24  ? -18.816 -12.893 26.905  1.000 146.943 ? 24  LYS LLL CG  1 
ATOM   10162 C CD  . LYS H 3 24  ? -17.658 -12.083 27.443  1.000 153.583 ? 24  LYS LLL CD  1 
ATOM   10163 C CE  . LYS H 3 24  ? -18.072 -10.750 28.036  1.000 159.323 ? 24  LYS LLL CE  1 
ATOM   10164 N NZ  . LYS H 3 24  ? -18.753 -9.878  27.046  1.000 160.547 ? 24  LYS LLL NZ  1 
ATOM   10165 N N   . SER H 3 25  ? -20.232 -14.904 24.634  1.000 139.230 ? 25  SER LLL N   1 
ATOM   10166 C CA  . SER H 3 25  ? -19.960 -15.264 23.216  1.000 140.284 ? 25  SER LLL CA  1 
ATOM   10167 C C   . SER H 3 25  ? -19.098 -14.185 22.560  1.000 145.791 ? 25  SER LLL C   1 
ATOM   10168 O O   . SER H 3 25  ? -19.419 -12.990 22.727  1.000 150.239 ? 25  SER LLL O   1 
ATOM   10169 C CB  . SER H 3 25  ? -21.239 -15.431 22.454  1.000 138.632 ? 25  SER LLL CB  1 
ATOM   10170 O OG  . SER H 3 25  ? -21.753 -14.163 22.070  1.000 143.146 ? 25  SER LLL OG  1 
ATOM   10171 N N   . SER H 3 26  ? -18.081 -14.599 21.801  1.000 147.292 ? 26  SER LLL N   1 
ATOM   10172 C CA  . SER H 3 26  ? -17.090 -13.705 21.146  1.000 152.620 ? 26  SER LLL CA  1 
ATOM   10173 C C   . SER H 3 26  ? -17.745 -12.925 19.998  1.000 151.696 ? 26  SER LLL C   1 
ATOM   10174 O O   . SER H 3 26  ? -17.202 -11.863 19.639  1.000 157.521 ? 26  SER LLL O   1 
ATOM   10175 C CB  . SER H 3 26  ? -15.881 -14.485 20.683  1.000 155.845 ? 26  SER LLL CB  1 
ATOM   10176 O OG  . SER H 3 26  ? -16.228 -15.827 20.360  1.000 154.056 ? 26  SER LLL OG  1 
ATOM   10177 N N   . GLN H 3 27  ? -18.863 -13.426 19.458  1.000 145.697 ? 27  GLN LLL N   1 
ATOM   10178 C CA  . GLN H 3 27  ? -19.633 -12.800 18.346  1.000 147.220 ? 27  GLN LLL CA  1 
ATOM   10179 C C   . GLN H 3 27  ? -21.092 -12.665 18.798  1.000 142.754 ? 27  GLN LLL C   1 
ATOM   10180 O O   . GLN H 3 27  ? -21.534 -13.530 19.570  1.000 137.161 ? 27  GLN LLL O   1 
ATOM   10181 C CB  . GLN H 3 27  ? -19.493 -13.649 17.074  1.000 147.780 ? 27  GLN LLL CB  1 
ATOM   10182 C CG  . GLN H 3 27  ? -19.690 -12.884 15.766  1.000 151.695 ? 27  GLN LLL CG  1 
ATOM   10183 C CD  . GLN H 3 27  ? -19.125 -13.585 14.550  1.000 152.379 ? 27  GLN LLL CD  1 
ATOM   10184 O OE1 . GLN H 3 27  ? -18.933 -14.798 14.525  1.000 148.260 ? 27  GLN LLL OE1 1 
ATOM   10185 N NE2 . GLN H 3 27  ? -18.856 -12.813 13.508  1.000 157.485 ? 27  GLN LLL NE2 1 
ATOM   10186 N N   . SER H 3 28  ? -21.797 -11.617 18.353  1.000 145.308 ? 28  SER LLL N   1 
ATOM   10187 C CA  . SER H 3 28  ? -23.252 -11.411 18.598  1.000 144.112 ? 28  SER LLL CA  1 
ATOM   10188 C C   . SER H 3 28  ? -24.028 -12.529 17.903  1.000 140.939 ? 28  SER LLL C   1 
ATOM   10189 O O   . SER H 3 28  ? -23.587 -12.948 16.810  1.000 145.366 ? 28  SER LLL O   1 
ATOM   10190 C CB  . SER H 3 28  ? -23.736 -10.062 18.127  1.000 148.294 ? 28  SER LLL CB  1 
ATOM   10191 O OG  . SER H 3 28  ? -25.147 -9.954  18.282  1.000 146.263 ? 28  SER LLL OG  1 
ATOM   10192 N N   . VAL H 3 29  ? -25.135 -12.972 18.504  1.000 136.282 ? 29  VAL LLL N   1 
ATOM   10193 C CA  . VAL H 3 29  ? -25.951 -14.123 18.015  1.000 132.274 ? 29  VAL LLL CA  1 
ATOM   10194 C C   . VAL H 3 29  ? -27.382 -13.656 17.735  1.000 133.378 ? 29  VAL LLL C   1 
ATOM   10195 O O   . VAL H 3 29  ? -28.269 -14.516 17.576  1.000 129.153 ? 29  VAL LLL O   1 
ATOM   10196 C CB  . VAL H 3 29  ? -25.926 -15.280 19.026  1.000 127.777 ? 29  VAL LLL CB  1 
ATOM   10197 C CG1 . VAL H 3 29  ? -24.499 -15.656 19.397  1.000 127.367 ? 29  VAL LLL CG1 1 
ATOM   10198 C CG2 . VAL H 3 29  ? -26.745 -14.960 20.265  1.000 127.328 ? 29  VAL LLL CG2 1 
ATOM   10199 N N   . LEU H 3 30  ? -27.586 -12.342 17.658  1.000 139.725 ? 30  LEU LLL N   1 
ATOM   10200 C CA  . LEU H 3 30  ? -28.914 -11.720 17.438  1.000 143.907 ? 30  LEU LLL CA  1 
ATOM   10201 C C   . LEU H 3 30  ? -29.344 -11.934 15.978  1.000 142.896 ? 30  LEU LLL C   1 
ATOM   10202 O O   . LEU H 3 30  ? -28.548 -11.627 15.069  1.000 145.702 ? 30  LEU LLL O   1 
ATOM   10203 C CB  . LEU H 3 30  ? -28.802 -10.234 17.803  1.000 152.154 ? 30  LEU LLL CB  1 
ATOM   10204 C CG  . LEU H 3 30  ? -30.109 -9.438  17.869  1.000 158.127 ? 30  LEU LLL CG  1 
ATOM   10205 C CD1 . LEU H 3 30  ? -30.471 -8.841  16.515  1.000 163.054 ? 30  LEU LLL CD1 1 
ATOM   10206 C CD2 . LEU H 3 30  ? -31.257 -10.282 18.399  1.000 156.018 ? 30  LEU LLL CD2 1 
ATOM   10207 N N   . TYR H 3 31  ? -30.555 -12.458 15.772  1.000 140.146 ? 31  TYR LLL N   1 
ATOM   10208 C CA  . TYR H 3 31  ? -31.246 -12.536 14.456  1.000 141.406 ? 31  TYR LLL CA  1 
ATOM   10209 C C   . TYR H 3 31  ? -31.984 -11.213 14.219  1.000 143.899 ? 31  TYR LLL C   1 
ATOM   10210 O O   . TYR H 3 31  ? -33.143 -11.073 14.668  1.000 144.408 ? 31  TYR LLL O   1 
ATOM   10211 C CB  . TYR H 3 31  ? -32.193 -13.743 14.399  1.000 139.128 ? 31  TYR LLL CB  1 
ATOM   10212 C CG  . TYR H 3 31  ? -31.730 -14.886 13.524  1.000 137.090 ? 31  TYR LLL CG  1 
ATOM   10213 C CD1 . TYR H 3 31  ? -30.667 -15.699 13.885  1.000 133.028 ? 31  TYR LLL CD1 1 
ATOM   10214 C CD2 . TYR H 3 31  ? -32.370 -15.163 12.326  1.000 138.997 ? 31  TYR LLL CD2 1 
ATOM   10215 C CE1 . TYR H 3 31  ? -30.250 -16.746 13.079  1.000 131.354 ? 31  TYR LLL CE1 1 
ATOM   10216 C CE2 . TYR H 3 31  ? -31.968 -16.209 11.513  1.000 137.548 ? 31  TYR LLL CE2 1 
ATOM   10217 C CZ  . TYR H 3 31  ? -30.902 -17.001 11.888  1.000 133.858 ? 31  TYR LLL CZ  1 
ATOM   10218 O OH  . TYR H 3 31  ? -30.522 -18.020 11.066  1.000 134.954 ? 31  TYR LLL OH  1 
ATOM   10219 N N   . SER H 3 32  ? -31.318 -10.260 13.559  1.000 145.747 ? 32  SER LLL N   1 
ATOM   10220 C CA  . SER H 3 32  ? -31.858 -8.903  13.286  1.000 150.861 ? 32  SER LLL CA  1 
ATOM   10221 C C   . SER H 3 32  ? -33.334 -9.022  12.899  1.000 150.983 ? 32  SER LLL C   1 
ATOM   10222 O O   . SER H 3 32  ? -34.145 -8.278  13.472  1.000 153.007 ? 32  SER LLL O   1 
ATOM   10223 C CB  . SER H 3 32  ? -31.059 -8.192  12.230  1.000 156.374 ? 32  SER LLL CB  1 
ATOM   10224 O OG  . SER H 3 32  ? -31.522 -6.856  12.064  1.000 163.113 ? 32  SER LLL OG  1 
ATOM   10225 N N   . SER H 3 33  ? -33.655 -9.956  11.994  1.000 150.333 ? 33  SER LLL N   1 
ATOM   10226 C CA  . SER H 3 33  ? -35.020 -10.266 11.484  1.000 152.579 ? 33  SER LLL CA  1 
ATOM   10227 C C   . SER H 3 33  ? -36.046 -10.201 12.614  1.000 150.790 ? 33  SER LLL C   1 
ATOM   10228 O O   . SER H 3 33  ? -36.861 -9.272  12.626  1.000 153.657 ? 33  SER LLL O   1 
ATOM   10229 C CB  . SER H 3 33  ? -35.056 -11.620 10.827  1.000 152.259 ? 33  SER LLL CB  1 
ATOM   10230 O OG  . SER H 3 33  ? -34.379 -11.586 9.583   1.000 159.357 ? 33  SER LLL OG  1 
ATOM   10231 N N   . ILE H 3 34  ? -35.993 -11.168 13.528  1.000 147.306 ? 34  ILE LLL N   1 
ATOM   10232 C CA  . ILE H 3 34  ? -36.901 -11.263 14.709  1.000 147.179 ? 34  ILE LLL CA  1 
ATOM   10233 C C   . ILE H 3 34  ? -36.035 -11.109 15.961  1.000 145.410 ? 34  ILE LLL C   1 
ATOM   10234 O O   . ILE H 3 34  ? -35.435 -12.109 16.377  1.000 141.712 ? 34  ILE LLL O   1 
ATOM   10235 C CB  . ILE H 3 34  ? -37.719 -12.576 14.687  1.000 145.487 ? 34  ILE LLL CB  1 
ATOM   10236 C CG1 . ILE H 3 34  ? -36.908 -13.790 14.214  1.000 142.237 ? 34  ILE LLL CG1 1 
ATOM   10237 C CG2 . ILE H 3 34  ? -38.970 -12.393 13.844  1.000 149.637 ? 34  ILE LLL CG2 1 
ATOM   10238 C CD1 . ILE H 3 34  ? -37.617 -15.120 14.385  1.000 139.828 ? 34  ILE LLL CD1 1 
ATOM   10239 N N   . ASN H 3 35  ? -35.937 -9.889  16.498  1.000 149.469 ? 35  ASN LLL N   1 
ATOM   10240 C CA  . ASN H 3 35  ? -35.027 -9.537  17.623  1.000 150.363 ? 35  ASN LLL CA  1 
ATOM   10241 C C   . ASN H 3 35  ? -35.082 -10.655 18.674  1.000 146.015 ? 35  ASN LLL C   1 
ATOM   10242 O O   . ASN H 3 35  ? -35.672 -10.455 19.757  1.000 145.823 ? 35  ASN LLL O   1 
ATOM   10243 C CB  . ASN H 3 35  ? -35.313 -8.149  18.198  1.000 157.466 ? 35  ASN LLL CB  1 
ATOM   10244 C CG  . ASN H 3 35  ? -36.788 -7.874  18.395  1.000 163.774 ? 35  ASN LLL CG  1 
ATOM   10245 O OD1 . ASN H 3 35  ? -37.561 -8.779  18.707  1.000 164.809 ? 35  ASN LLL OD1 1 
ATOM   10246 N ND2 . ASN H 3 35  ? -37.195 -6.627  18.207  1.000 171.595 ? 35  ASN LLL ND2 1 
ATOM   10247 N N   . LYS H 3 36  ? -34.438 -11.786 18.348  1.000 142.636 ? 36  LYS LLL N   1 
ATOM   10248 C CA  . LYS H 3 36  ? -34.209 -12.962 19.230  1.000 139.433 ? 36  LYS LLL CA  1 
ATOM   10249 C C   . LYS H 3 36  ? -32.752 -13.398 19.098  1.000 134.185 ? 36  LYS LLL C   1 
ATOM   10250 O O   . LYS H 3 36  ? -32.263 -13.466 17.963  1.000 133.432 ? 36  LYS LLL O   1 
ATOM   10251 C CB  . LYS H 3 36  ? -35.112 -14.140 18.856  1.000 140.540 ? 36  LYS LLL CB  1 
ATOM   10252 C CG  . LYS H 3 36  ? -36.602 -13.826 18.892  1.000 147.787 ? 36  LYS LLL CG  1 
ATOM   10253 C CD  . LYS H 3 36  ? -37.146 -13.507 20.278  1.000 152.553 ? 36  LYS LLL CD  1 
ATOM   10254 C CE  . LYS H 3 36  ? -37.543 -14.752 21.050  1.000 153.202 ? 36  LYS LLL CE  1 
ATOM   10255 N NZ  . LYS H 3 36  ? -37.645 -14.520 22.512  1.000 155.035 ? 36  LYS LLL NZ  1 
ATOM   10256 N N   . ASN H 3 37  ? -32.095 -13.671 20.223  1.000 131.649 ? 37  ASN LLL N   1 
ATOM   10257 C CA  . ASN H 3 37  ? -30.711 -14.206 20.257  1.000 130.791 ? 37  ASN LLL CA  1 
ATOM   10258 C C   . ASN H 3 37  ? -30.808 -15.729 20.140  1.000 126.233 ? 37  ASN LLL C   1 
ATOM   10259 O O   . ASN H 3 37  ? -31.641 -16.327 20.857  1.000 122.455 ? 37  ASN LLL O   1 
ATOM   10260 C CB  . ASN H 3 37  ? -29.960 -13.738 21.504  1.000 133.001 ? 37  ASN LLL CB  1 
ATOM   10261 C CG  . ASN H 3 37  ? -29.420 -12.325 21.384  1.000 138.850 ? 37  ASN LLL CG  1 
ATOM   10262 O OD1 . ASN H 3 37  ? -29.798 -11.446 22.157  1.000 145.371 ? 37  ASN LLL OD1 1 
ATOM   10263 N ND2 . ASN H 3 37  ? -28.528 -12.091 20.432  1.000 139.151 ? 37  ASN LLL ND2 1 
ATOM   10264 N N   . TYR H 3 38  ? -30.022 -16.321 19.236  1.000 125.577 ? 38  TYR LLL N   1 
ATOM   10265 C CA  . TYR H 3 38  ? -30.079 -17.763 18.876  1.000 123.580 ? 38  TYR LLL CA  1 
ATOM   10266 C C   . TYR H 3 38  ? -29.077 -18.506 19.768  1.000 123.239 ? 38  TYR LLL C   1 
ATOM   10267 O O   . TYR H 3 38  ? -28.048 -19.021 19.287  1.000 125.192 ? 38  TYR LLL O   1 
ATOM   10268 C CB  . TYR H 3 38  ? -29.926 -17.933 17.358  1.000 123.681 ? 38  TYR LLL CB  1 
ATOM   10269 C CG  . TYR H 3 38  ? -31.240 -17.864 16.618  1.000 123.748 ? 38  TYR LLL CG  1 
ATOM   10270 C CD1 . TYR H 3 38  ? -32.149 -16.855 16.890  1.000 126.495 ? 38  TYR LLL CD1 1 
ATOM   10271 C CD2 . TYR H 3 38  ? -31.605 -18.816 15.681  1.000 123.201 ? 38  TYR LLL CD2 1 
ATOM   10272 C CE1 . TYR H 3 38  ? -33.376 -16.781 16.256  1.000 127.391 ? 38  TYR LLL CE1 1 
ATOM   10273 C CE2 . TYR H 3 38  ? -32.825 -18.750 15.022  1.000 125.396 ? 38  TYR LLL CE2 1 
ATOM   10274 C CZ  . TYR H 3 38  ? -33.716 -17.731 15.316  1.000 127.328 ? 38  TYR LLL CZ  1 
ATOM   10275 O OH  . TYR H 3 38  ? -34.931 -17.622 14.705  1.000 131.223 ? 38  TYR LLL OH  1 
ATOM   10276 N N   . LEU H 3 39  ? -29.409 -18.547 21.061  1.000 123.145 ? 39  LEU LLL N   1 
ATOM   10277 C CA  . LEU H 3 39  ? -28.588 -19.107 22.168  1.000 122.603 ? 39  LEU LLL CA  1 
ATOM   10278 C C   . LEU H 3 39  ? -29.500 -20.010 23.008  1.000 118.038 ? 39  LEU LLL C   1 
ATOM   10279 O O   . LEU H 3 39  ? -30.683 -19.641 23.214  1.000 116.302 ? 39  LEU LLL O   1 
ATOM   10280 C CB  . LEU H 3 39  ? -28.010 -17.928 22.968  1.000 127.873 ? 39  LEU LLL CB  1 
ATOM   10281 C CG  . LEU H 3 39  ? -27.102 -18.216 24.173  1.000 128.969 ? 39  LEU LLL CG  1 
ATOM   10282 C CD1 . LEU H 3 39  ? -27.912 -18.530 25.422  1.000 129.692 ? 39  LEU LLL CD1 1 
ATOM   10283 C CD2 . LEU H 3 39  ? -26.087 -19.316 23.898  1.000 127.765 ? 39  LEU LLL CD2 1 
ATOM   10284 N N   . ALA H 3 40  ? -28.981 -21.166 23.429  1.000 115.080 ? 40  ALA LLL N   1 
ATOM   10285 C CA  . ALA H 3 40  ? -29.728 -22.205 24.174  1.000 115.586 ? 40  ALA LLL CA  1 
ATOM   10286 C C   . ALA H 3 40  ? -28.940 -22.671 25.407  1.000 116.865 ? 40  ALA LLL C   1 
ATOM   10287 O O   . ALA H 3 40  ? -27.741 -22.326 25.538  1.000 117.681 ? 40  ALA LLL O   1 
ATOM   10288 C CB  . ALA H 3 40  ? -30.044 -23.367 23.267  1.000 114.436 ? 40  ALA LLL CB  1 
ATOM   10289 N N   . TRP H 3 41  ? -29.618 -23.436 26.271  1.000 116.743 ? 41  TRP LLL N   1 
ATOM   10290 C CA  . TRP H 3 41  ? -29.140 -23.941 27.585  1.000 115.271 ? 41  TRP LLL CA  1 
ATOM   10291 C C   . TRP H 3 41  ? -29.520 -25.426 27.712  1.000 113.807 ? 41  TRP LLL C   1 
ATOM   10292 O O   . TRP H 3 41  ? -30.717 -25.766 27.527  1.000 112.442 ? 41  TRP LLL O   1 
ATOM   10293 C CB  . TRP H 3 41  ? -29.738 -23.101 28.725  1.000 115.670 ? 41  TRP LLL CB  1 
ATOM   10294 C CG  . TRP H 3 41  ? -29.143 -21.735 28.902  1.000 115.435 ? 41  TRP LLL CG  1 
ATOM   10295 C CD1 . TRP H 3 41  ? -29.686 -20.526 28.559  1.000 117.266 ? 41  TRP LLL CD1 1 
ATOM   10296 C CD2 . TRP H 3 41  ? -27.878 -21.437 29.509  1.000 114.610 ? 41  TRP LLL CD2 1 
ATOM   10297 N NE1 . TRP H 3 41  ? -28.846 -19.499 28.901  1.000 117.969 ? 41  TRP LLL NE1 1 
ATOM   10298 C CE2 . TRP H 3 41  ? -27.728 -20.033 29.488  1.000 117.844 ? 41  TRP LLL CE2 1 
ATOM   10299 C CE3 . TRP H 3 41  ? -26.866 -22.223 30.067  1.000 113.939 ? 41  TRP LLL CE3 1 
ATOM   10300 C CZ2 . TRP H 3 41  ? -26.604 -19.406 30.019  1.000 121.459 ? 41  TRP LLL CZ2 1 
ATOM   10301 C CZ3 . TRP H 3 41  ? -25.755 -21.601 30.588  1.000 116.685 ? 41  TRP LLL CZ3 1 
ATOM   10302 C CH2 . TRP H 3 41  ? -25.629 -20.212 30.565  1.000 120.552 ? 41  TRP LLL CH2 1 
ATOM   10303 N N   . TYR H 3 42  ? -28.539 -26.279 28.019  1.000 112.493 ? 42  TYR LLL N   1 
ATOM   10304 C CA  . TYR H 3 42  ? -28.708 -27.744 28.179  1.000 111.748 ? 42  TYR LLL CA  1 
ATOM   10305 C C   . TYR H 3 42  ? -28.277 -28.161 29.598  1.000 111.860 ? 42  TYR LLL C   1 
ATOM   10306 O O   . TYR H 3 42  ? -27.252 -27.665 30.110  1.000 110.204 ? 42  TYR LLL O   1 
ATOM   10307 C CB  . TYR H 3 42  ? -27.916 -28.478 27.093  1.000 112.935 ? 42  TYR LLL CB  1 
ATOM   10308 C CG  . TYR H 3 42  ? -28.347 -28.239 25.661  1.000 113.515 ? 42  TYR LLL CG  1 
ATOM   10309 C CD1 . TYR H 3 42  ? -27.805 -27.212 24.899  1.000 112.833 ? 42  TYR LLL CD1 1 
ATOM   10310 C CD2 . TYR H 3 42  ? -29.262 -29.078 25.041  1.000 114.879 ? 42  TYR LLL CD2 1 
ATOM   10311 C CE1 . TYR H 3 42  ? -28.174 -27.012 23.577  1.000 111.695 ? 42  TYR LLL CE1 1 
ATOM   10312 C CE2 . TYR H 3 42  ? -29.639 -28.894 23.718  1.000 114.322 ? 42  TYR LLL CE2 1 
ATOM   10313 C CZ  . TYR H 3 42  ? -29.095 -27.856 22.983  1.000 113.364 ? 42  TYR LLL CZ  1 
ATOM   10314 O OH  . TYR H 3 42  ? -29.461 -27.668 21.680  1.000 116.143 ? 42  TYR LLL OH  1 
ATOM   10315 N N   . GLN H 3 43  ? -29.075 -29.025 30.232  1.000 113.297 ? 43  GLN LLL N   1 
ATOM   10316 C CA  . GLN H 3 43  ? -28.731 -29.766 31.478  1.000 114.193 ? 43  GLN LLL CA  1 
ATOM   10317 C C   . GLN H 3 43  ? -28.327 -31.185 31.071  1.000 112.798 ? 43  GLN LLL C   1 
ATOM   10318 O O   . GLN H 3 43  ? -28.969 -31.753 30.171  1.000 114.073 ? 43  GLN LLL O   1 
ATOM   10319 C CB  . GLN H 3 43  ? -29.906 -29.794 32.469  1.000 115.796 ? 43  GLN LLL CB  1 
ATOM   10320 C CG  . GLN H 3 43  ? -30.147 -31.158 33.118  1.000 116.411 ? 43  GLN LLL CG  1 
ATOM   10321 C CD  . GLN H 3 43  ? -31.336 -31.191 34.041  1.000 117.537 ? 43  GLN LLL CD  1 
ATOM   10322 O OE1 . GLN H 3 43  ? -32.197 -32.074 33.952  1.000 116.399 ? 43  GLN LLL OE1 1 
ATOM   10323 N NE2 . GLN H 3 43  ? -31.364 -30.234 34.956  1.000 118.035 ? 43  GLN LLL NE2 1 
ATOM   10324 N N   . GLN H 3 44  ? -27.308 -31.740 31.716  1.000 111.425 ? 44  GLN LLL N   1 
ATOM   10325 C CA  . GLN H 3 44  ? -26.963 -33.171 31.570  1.000 112.640 ? 44  GLN LLL CA  1 
ATOM   10326 C C   . GLN H 3 44  ? -26.732 -33.748 32.964  1.000 115.823 ? 44  GLN LLL C   1 
ATOM   10327 O O   . GLN H 3 44  ? -25.672 -33.478 33.546  1.000 116.184 ? 44  GLN LLL O   1 
ATOM   10328 C CB  . GLN H 3 44  ? -25.747 -33.314 30.664  1.000 111.872 ? 44  GLN LLL CB  1 
ATOM   10329 C CG  . GLN H 3 44  ? -25.144 -34.703 30.687  1.000 113.367 ? 44  GLN LLL CG  1 
ATOM   10330 C CD  . GLN H 3 44  ? -24.164 -34.893 29.557  1.000 111.954 ? 44  GLN LLL CD  1 
ATOM   10331 O OE1 . GLN H 3 44  ? -23.272 -34.073 29.338  1.000 109.236 ? 44  GLN LLL OE1 1 
ATOM   10332 N NE2 . GLN H 3 44  ? -24.312 -35.999 28.848  1.000 111.080 ? 44  GLN LLL NE2 1 
ATOM   10333 N N   . LYS H 3 45  ? -27.712 -34.480 33.491  1.000 119.900 ? 45  LYS LLL N   1 
ATOM   10334 C CA  . LYS H 3 45  ? -27.509 -35.359 34.671  1.000 123.910 ? 45  LYS LLL CA  1 
ATOM   10335 C C   . LYS H 3 45  ? -26.697 -36.550 34.166  1.000 125.414 ? 45  LYS LLL C   1 
ATOM   10336 O O   . LYS H 3 45  ? -27.025 -37.104 33.120  1.000 126.611 ? 45  LYS LLL O   1 
ATOM   10337 C CB  . LYS H 3 45  ? -28.847 -35.738 35.324  1.000 127.268 ? 45  LYS LLL CB  1 
ATOM   10338 C CG  . LYS H 3 45  ? -29.394 -34.756 36.361  1.000 128.979 ? 45  LYS LLL CG  1 
ATOM   10339 C CD  . LYS H 3 45  ? -30.808 -35.063 36.870  1.000 131.899 ? 45  LYS LLL CD  1 
ATOM   10340 C CE  . LYS H 3 45  ? -31.905 -34.431 36.031  1.000 132.256 ? 45  LYS LLL CE  1 
ATOM   10341 N NZ  . LYS H 3 45  ? -33.264 -34.818 36.482  1.000 134.732 ? 45  LYS LLL NZ  1 
ATOM   10342 N N   . PRO H 3 46  ? -25.566 -36.904 34.825  1.000 128.154 ? 46  PRO LLL N   1 
ATOM   10343 C CA  . PRO H 3 46  ? -24.744 -38.052 34.427  1.000 128.118 ? 46  PRO LLL CA  1 
ATOM   10344 C C   . PRO H 3 46  ? -25.507 -39.351 34.126  1.000 128.373 ? 46  PRO LLL C   1 
ATOM   10345 O O   . PRO H 3 46  ? -26.402 -39.681 34.868  1.000 129.349 ? 46  PRO LLL O   1 
ATOM   10346 C CB  . PRO H 3 46  ? -23.868 -38.277 35.668  1.000 131.317 ? 46  PRO LLL CB  1 
ATOM   10347 C CG  . PRO H 3 46  ? -23.686 -36.885 36.249  1.000 132.785 ? 46  PRO LLL CG  1 
ATOM   10348 C CD  . PRO H 3 46  ? -24.987 -36.165 35.961  1.000 130.998 ? 46  PRO LLL CD  1 
ATOM   10349 N N   . GLY H 3 47  ? -25.125 -40.057 33.055  1.000 128.792 ? 47  GLY LLL N   1 
ATOM   10350 C CA  . GLY H 3 47  ? -25.744 -41.332 32.633  1.000 129.562 ? 47  GLY LLL CA  1 
ATOM   10351 C C   . GLY H 3 47  ? -26.811 -41.108 31.581  1.000 127.053 ? 47  GLY LLL C   1 
ATOM   10352 O O   . GLY H 3 47  ? -27.104 -42.051 30.835  1.000 127.756 ? 47  GLY LLL O   1 
ATOM   10353 N N   . GLN H 3 48  ? -27.336 -39.885 31.518  1.000 125.967 ? 48  GLN LLL N   1 
ATOM   10354 C CA  . GLN H 3 48  ? -28.396 -39.437 30.582  1.000 125.442 ? 48  GLN LLL CA  1 
ATOM   10355 C C   . GLN H 3 48  ? -27.758 -38.680 29.423  1.000 121.178 ? 48  GLN LLL C   1 
ATOM   10356 O O   . GLN H 3 48  ? -26.600 -38.285 29.498  1.000 121.087 ? 48  GLN LLL O   1 
ATOM   10357 C CB  . GLN H 3 48  ? -29.387 -38.534 31.321  1.000 126.448 ? 48  GLN LLL CB  1 
ATOM   10358 C CG  . GLN H 3 48  ? -29.967 -39.156 32.590  1.000 130.321 ? 48  GLN LLL CG  1 
ATOM   10359 C CD  . GLN H 3 48  ? -30.852 -38.193 33.348  1.000 132.331 ? 48  GLN LLL CD  1 
ATOM   10360 O OE1 . GLN H 3 48  ? -31.037 -37.043 32.949  1.000 133.441 ? 48  GLN LLL OE1 1 
ATOM   10361 N NE2 . GLN H 3 48  ? -31.415 -38.658 34.454  1.000 135.352 ? 48  GLN LLL NE2 1 
ATOM   10362 N N   . PRO H 3 49  ? -28.491 -38.458 28.312  1.000 118.461 ? 49  PRO LLL N   1 
ATOM   10363 C CA  . PRO H 3 49  ? -28.087 -37.486 27.306  1.000 115.222 ? 49  PRO LLL CA  1 
ATOM   10364 C C   . PRO H 3 49  ? -28.403 -36.091 27.824  1.000 111.962 ? 49  PRO LLL C   1 
ATOM   10365 O O   . PRO H 3 49  ? -29.010 -35.962 28.889  1.000 113.871 ? 49  PRO LLL O   1 
ATOM   10366 C CB  . PRO H 3 49  ? -28.965 -37.848 26.105  1.000 117.046 ? 49  PRO LLL CB  1 
ATOM   10367 C CG  . PRO H 3 49  ? -30.232 -38.361 26.736  1.000 118.827 ? 49  PRO LLL CG  1 
ATOM   10368 C CD  . PRO H 3 49  ? -29.758 -39.113 27.962  1.000 120.510 ? 49  PRO LLL CD  1 
ATOM   10369 N N   . PRO H 3 50  ? -27.953 -35.029 27.114  1.000 106.634 ? 50  PRO LLL N   1 
ATOM   10370 C CA  . PRO H 3 50  ? -28.371 -33.655 27.386  1.000 103.952 ? 50  PRO LLL CA  1 
ATOM   10371 C C   . PRO H 3 50  ? -29.852 -33.365 27.131  1.000 103.396 ? 50  PRO LLL C   1 
ATOM   10372 O O   . PRO H 3 50  ? -30.427 -33.862 26.182  1.000 100.429 ? 50  PRO LLL O   1 
ATOM   10373 C CB  . PRO H 3 50  ? -27.539 -32.798 26.430  1.000 101.543 ? 50  PRO LLL CB  1 
ATOM   10374 C CG  . PRO H 3 50  ? -26.340 -33.658 26.148  1.000 103.501 ? 50  PRO LLL CG  1 
ATOM   10375 C CD  . PRO H 3 50  ? -26.895 -35.068 26.100  1.000 105.898 ? 50  PRO LLL CD  1 
ATOM   10376 N N   . LYS H 3 51  ? -30.409 -32.565 28.035  1.000 107.422 ? 51  LYS LLL N   1 
ATOM   10377 C CA  . LYS H 3 51  ? -31.810 -32.093 28.042  1.000 112.093 ? 51  LYS LLL CA  1 
ATOM   10378 C C   . LYS H 3 51  ? -31.769 -30.618 27.653  1.000 110.020 ? 51  LYS LLL C   1 
ATOM   10379 O O   . LYS H 3 51  ? -30.915 -29.898 28.185  1.000 106.026 ? 51  LYS LLL O   1 
ATOM   10380 C CB  . LYS H 3 51  ? -32.446 -32.322 29.423  1.000 116.671 ? 51  LYS LLL CB  1 
ATOM   10381 C CG  . LYS H 3 51  ? -33.940 -32.033 29.517  1.000 120.406 ? 51  LYS LLL CG  1 
ATOM   10382 C CD  . LYS H 3 51  ? -34.602 -32.604 30.752  1.000 125.829 ? 51  LYS LLL CD  1 
ATOM   10383 C CE  . LYS H 3 51  ? -35.993 -32.049 30.997  1.000 131.006 ? 51  LYS LLL CE  1 
ATOM   10384 N NZ  . LYS H 3 51  ? -37.052 -32.784 30.260  1.000 134.724 ? 51  LYS LLL NZ  1 
ATOM   10385 N N   . LEU H 3 52  ? -32.629 -30.214 26.722  1.000 112.444 ? 52  LEU LLL N   1 
ATOM   10386 C CA  . LEU H 3 52  ? -32.861 -28.791 26.381  1.000 113.408 ? 52  LEU LLL CA  1 
ATOM   10387 C C   . LEU H 3 52  ? -33.719 -28.160 27.485  1.000 111.428 ? 52  LEU LLL C   1 
ATOM   10388 O O   . LEU H 3 52  ? -34.819 -28.693 27.769  1.000 110.045 ? 52  LEU LLL O   1 
ATOM   10389 C CB  . LEU H 3 52  ? -33.540 -28.711 25.008  1.000 116.508 ? 52  LEU LLL CB  1 
ATOM   10390 C CG  . LEU H 3 52  ? -33.711 -27.300 24.440  1.000 118.310 ? 52  LEU LLL CG  1 
ATOM   10391 C CD1 . LEU H 3 52  ? -32.371 -26.689 24.054  1.000 117.391 ? 52  LEU LLL CD1 1 
ATOM   10392 C CD2 . LEU H 3 52  ? -34.650 -27.302 23.248  1.000 120.198 ? 52  LEU LLL CD2 1 
ATOM   10393 N N   . LEU H 3 53  ? -33.220 -27.081 28.092  1.000 109.492 ? 53  LEU LLL N   1 
ATOM   10394 C CA  . LEU H 3 53  ? -33.950 -26.289 29.115  1.000 113.517 ? 53  LEU LLL CA  1 
ATOM   10395 C C   . LEU H 3 53  ? -34.524 -25.018 28.477  1.000 114.804 ? 53  LEU LLL C   1 
ATOM   10396 O O   . LEU H 3 53  ? -35.730 -24.741 28.678  1.000 116.336 ? 53  LEU LLL O   1 
ATOM   10397 C CB  . LEU H 3 53  ? -32.995 -25.934 30.261  1.000 115.043 ? 53  LEU LLL CB  1 
ATOM   10398 C CG  . LEU H 3 53  ? -32.435 -27.105 31.068  1.000 114.160 ? 53  LEU LLL CG  1 
ATOM   10399 C CD1 . LEU H 3 53  ? -31.395 -26.607 32.055  1.000 114.004 ? 53  LEU LLL CD1 1 
ATOM   10400 C CD2 . LEU H 3 53  ? -33.536 -27.863 31.795  1.000 115.327 ? 53  LEU LLL CD2 1 
ATOM   10401 N N   . ILE H 3 54  ? -33.692 -24.258 27.756  1.000 114.298 ? 54  ILE LLL N   1 
ATOM   10402 C CA  . ILE H 3 54  ? -34.071 -22.915 27.225  1.000 116.950 ? 54  ILE LLL CA  1 
ATOM   10403 C C   . ILE H 3 54  ? -33.524 -22.693 25.804  1.000 116.656 ? 54  ILE LLL C   1 
ATOM   10404 O O   . ILE H 3 54  ? -32.375 -23.073 25.537  1.000 114.550 ? 54  ILE LLL O   1 
ATOM   10405 C CB  . ILE H 3 54  ? -33.615 -21.835 28.220  1.000 118.264 ? 54  ILE LLL CB  1 
ATOM   10406 C CG1 . ILE H 3 54  ? -34.517 -21.852 29.456  1.000 120.987 ? 54  ILE LLL CG1 1 
ATOM   10407 C CG2 . ILE H 3 54  ? -33.566 -20.466 27.552  1.000 121.691 ? 54  ILE LLL CG2 1 
ATOM   10408 C CD1 . ILE H 3 54  ? -34.217 -20.771 30.466  1.000 125.475 ? 54  ILE LLL CD1 1 
ATOM   10409 N N   . TYR H 3 55  ? -34.343 -22.093 24.933  1.000 117.548 ? 55  TYR LLL N   1 
ATOM   10410 C CA  . TYR H 3 55  ? -33.995 -21.677 23.551  1.000 117.604 ? 55  TYR LLL CA  1 
ATOM   10411 C C   . TYR H 3 55  ? -34.370 -20.201 23.379  1.000 120.566 ? 55  TYR LLL C   1 
ATOM   10412 O O   . TYR H 3 55  ? -34.985 -19.645 24.297  1.000 122.858 ? 55  TYR LLL O   1 
ATOM   10413 C CB  . TYR H 3 55  ? -34.666 -22.599 22.528  1.000 118.835 ? 55  TYR LLL CB  1 
ATOM   10414 C CG  . TYR H 3 55  ? -36.172 -22.560 22.493  1.000 120.713 ? 55  TYR LLL CG  1 
ATOM   10415 C CD1 . TYR H 3 55  ? -36.918 -23.417 23.284  1.000 121.462 ? 55  TYR LLL CD1 1 
ATOM   10416 C CD2 . TYR H 3 55  ? -36.851 -21.702 21.642  1.000 124.344 ? 55  TYR LLL CD2 1 
ATOM   10417 C CE1 . TYR H 3 55  ? -38.302 -23.413 23.252  1.000 124.878 ? 55  TYR LLL CE1 1 
ATOM   10418 C CE2 . TYR H 3 55  ? -38.238 -21.687 21.600  1.000 127.541 ? 55  TYR LLL CE2 1 
ATOM   10419 C CZ  . TYR H 3 55  ? -38.969 -22.536 22.417  1.000 127.432 ? 55  TYR LLL CZ  1 
ATOM   10420 O OH  . TYR H 3 55  ? -40.338 -22.543 22.408  1.000 130.128 ? 55  TYR LLL OH  1 
ATOM   10421 N N   . TRP H 3 56  ? -34.009 -19.597 22.237  1.000 123.682 ? 56  TRP LLL N   1 
ATOM   10422 C CA  . TRP H 3 56  ? -33.973 -18.122 21.992  1.000 124.759 ? 56  TRP LLL CA  1 
ATOM   10423 C C   . TRP H 3 56  ? -33.750 -17.404 23.334  1.000 120.531 ? 56  TRP LLL C   1 
ATOM   10424 O O   . TRP H 3 56  ? -34.569 -16.523 23.683  1.000 120.089 ? 56  TRP LLL O   1 
ATOM   10425 C CB  . TRP H 3 56  ? -35.216 -17.587 21.234  1.000 129.181 ? 56  TRP LLL CB  1 
ATOM   10426 C CG  . TRP H 3 56  ? -35.562 -18.278 19.943  1.000 130.043 ? 56  TRP LLL CG  1 
ATOM   10427 C CD1 . TRP H 3 56  ? -34.749 -19.068 19.182  1.000 129.956 ? 56  TRP LLL CD1 1 
ATOM   10428 C CD2 . TRP H 3 56  ? -36.821 -18.237 19.247  1.000 131.331 ? 56  TRP LLL CD2 1 
ATOM   10429 N NE1 . TRP H 3 56  ? -35.415 -19.545 18.087  1.000 130.684 ? 56  TRP LLL NE1 1 
ATOM   10430 C CE2 . TRP H 3 56  ? -36.688 -19.044 18.094  1.000 133.148 ? 56  TRP LLL CE2 1 
ATOM   10431 C CE3 . TRP H 3 56  ? -38.054 -17.628 19.495  1.000 132.404 ? 56  TRP LLL CE3 1 
ATOM   10432 C CZ2 . TRP H 3 56  ? -37.734 -19.240 17.190  1.000 135.321 ? 56  TRP LLL CZ2 1 
ATOM   10433 C CZ3 . TRP H 3 56  ? -39.086 -17.822 18.602  1.000 135.516 ? 56  TRP LLL CZ3 1 
ATOM   10434 C CH2 . TRP H 3 56  ? -38.928 -18.616 17.464  1.000 135.808 ? 56  TRP LLL CH2 1 
ATOM   10435 N N   . ALA H 3 57  ? -32.722 -17.840 24.080  1.000 113.785 ? 57  ALA LLL N   1 
ATOM   10436 C CA  . ALA H 3 57  ? -32.072 -17.124 25.207  1.000 112.638 ? 57  ALA LLL CA  1 
ATOM   10437 C C   . ALA H 3 57  ? -32.889 -17.172 26.506  1.000 111.094 ? 57  ALA LLL C   1 
ATOM   10438 O O   . ALA H 3 57  ? -32.247 -17.087 27.583  1.000 107.006 ? 57  ALA LLL O   1 
ATOM   10439 C CB  . ALA H 3 57  ? -31.803 -15.696 24.803  1.000 116.484 ? 57  ALA LLL CB  1 
ATOM   10440 N N   . SER H 3 58  ? -34.223 -17.305 26.409  1.000 111.881 ? 58  SER LLL N   1 
ATOM   10441 C CA  . SER H 3 58  ? -35.203 -16.982 27.483  1.000 115.658 ? 58  SER LLL CA  1 
ATOM   10442 C C   . SER H 3 58  ? -36.465 -17.868 27.481  1.000 116.629 ? 58  SER LLL C   1 
ATOM   10443 O O   . SER H 3 58  ? -37.126 -17.925 28.537  1.000 117.781 ? 58  SER LLL O   1 
ATOM   10444 C CB  . SER H 3 58  ? -35.592 -15.542 27.369  1.000 120.036 ? 58  SER LLL CB  1 
ATOM   10445 O OG  . SER H 3 58  ? -36.187 -15.295 26.102  1.000 121.862 ? 58  SER LLL OG  1 
ATOM   10446 N N   . THR H 3 59  ? -36.846 -18.484 26.356  1.000 118.391 ? 59  THR LLL N   1 
ATOM   10447 C CA  . THR H 3 59  ? -38.067 -19.332 26.240  1.000 121.575 ? 59  THR LLL CA  1 
ATOM   10448 C C   . THR H 3 59  ? -37.773 -20.719 26.819  1.000 119.135 ? 59  THR LLL C   1 
ATOM   10449 O O   . THR H 3 59  ? -36.751 -21.300 26.443  1.000 116.387 ? 59  THR LLL O   1 
ATOM   10450 C CB  . THR H 3 59  ? -38.546 -19.462 24.785  1.000 124.902 ? 59  THR LLL CB  1 
ATOM   10451 O OG1 . THR H 3 59  ? -38.215 -18.283 24.044  1.000 128.672 ? 59  THR LLL OG1 1 
ATOM   10452 C CG2 . THR H 3 59  ? -40.036 -19.725 24.689  1.000 128.367 ? 59  THR LLL CG2 1 
ATOM   10453 N N   . ARG H 3 60  ? -38.652 -21.243 27.673  1.000 123.417 ? 60  ARG LLL N   1 
ATOM   10454 C CA  . ARG H 3 60  ? -38.474 -22.572 28.316  1.000 124.618 ? 60  ARG LLL CA  1 
ATOM   10455 C C   . ARG H 3 60  ? -39.040 -23.657 27.396  1.000 124.853 ? 60  ARG LLL C   1 
ATOM   10456 O O   . ARG H 3 60  ? -40.080 -23.406 26.750  1.000 127.392 ? 60  ARG LLL O   1 
ATOM   10457 C CB  . ARG H 3 60  ? -39.169 -22.615 29.681  1.000 129.391 ? 60  ARG LLL CB  1 
ATOM   10458 C CG  . ARG H 3 60  ? -38.872 -21.411 30.560  1.000 132.951 ? 60  ARG LLL CG  1 
ATOM   10459 C CD  . ARG H 3 60  ? -38.918 -21.757 32.030  1.000 134.812 ? 60  ARG LLL CD  1 
ATOM   10460 N NE  . ARG H 3 60  ? -40.204 -22.291 32.445  1.000 138.968 ? 60  ARG LLL NE  1 
ATOM   10461 C CZ  . ARG H 3 60  ? -41.309 -21.569 32.599  1.000 143.684 ? 60  ARG LLL CZ  1 
ATOM   10462 N NH1 . ARG H 3 60  ? -41.295 -20.268 32.349  1.000 145.577 ? 60  ARG LLL NH1 1 
ATOM   10463 N NH2 . ARG H 3 60  ? -42.429 -22.154 32.998  1.000 145.663 ? 60  ARG LLL NH2 1 
ATOM   10464 N N   . GLU H 3 61  ? -38.379 -24.815 27.352  1.000 124.212 ? 61  GLU LLL N   1 
ATOM   10465 C CA  . GLU H 3 61  ? -38.857 -26.028 26.637  1.000 126.439 ? 61  GLU LLL CA  1 
ATOM   10466 C C   . GLU H 3 61  ? -39.919 -26.718 27.507  1.000 126.246 ? 61  GLU LLL C   1 
ATOM   10467 O O   . GLU H 3 61  ? -39.909 -26.527 28.732  1.000 123.649 ? 61  GLU LLL O   1 
ATOM   10468 C CB  . GLU H 3 61  ? -37.665 -26.936 26.308  1.000 127.623 ? 61  GLU LLL CB  1 
ATOM   10469 C CG  . GLU H 3 61  ? -38.016 -28.227 25.579  1.000 131.569 ? 61  GLU LLL CG  1 
ATOM   10470 C CD  . GLU H 3 61  ? -38.557 -28.083 24.163  1.000 135.294 ? 61  GLU LLL CD  1 
ATOM   10471 O OE1 . GLU H 3 61  ? -39.730 -27.660 24.003  1.000 140.131 ? 61  GLU LLL OE1 1 
ATOM   10472 O OE2 . GLU H 3 61  ? -37.812 -28.420 23.217  1.000 136.108 ? 61  GLU LLL OE2 1 
ATOM   10473 N N   . SER H 3 62  ? -40.826 -27.468 26.882  1.000 127.965 ? 62  SER LLL N   1 
ATOM   10474 C CA  . SER H 3 62  ? -41.809 -28.347 27.560  1.000 131.151 ? 62  SER LLL CA  1 
ATOM   10475 C C   . SER H 3 62  ? -41.052 -29.274 28.514  1.000 129.515 ? 62  SER LLL C   1 
ATOM   10476 O O   . SER H 3 62  ? -39.992 -29.805 28.105  1.000 124.587 ? 62  SER LLL O   1 
ATOM   10477 C CB  . SER H 3 62  ? -42.627 -29.124 26.557  1.000 135.731 ? 62  SER LLL CB  1 
ATOM   10478 O OG  . SER H 3 62  ? -41.800 -29.689 25.541  1.000 135.123 ? 62  SER LLL OG  1 
ATOM   10479 N N   . GLY H 3 63  ? -41.569 -29.430 29.738  1.000 133.031 ? 63  GLY LLL N   1 
ATOM   10480 C CA  . GLY H 3 63  ? -41.057 -30.368 30.761  1.000 133.437 ? 63  GLY LLL CA  1 
ATOM   10481 C C   . GLY H 3 63  ? -40.008 -29.738 31.661  1.000 130.151 ? 63  GLY LLL C   1 
ATOM   10482 O O   . GLY H 3 63  ? -39.222 -30.508 32.285  1.000 127.769 ? 63  GLY LLL O   1 
ATOM   10483 N N   . VAL H 3 64  ? -40.012 -28.401 31.732  1.000 128.695 ? 64  VAL LLL N   1 
ATOM   10484 C CA  . VAL H 3 64  ? -38.989 -27.571 32.431  1.000 126.955 ? 64  VAL LLL CA  1 
ATOM   10485 C C   . VAL H 3 64  ? -39.689 -26.679 33.446  1.000 126.835 ? 64  VAL LLL C   1 
ATOM   10486 O O   . VAL H 3 64  ? -40.543 -25.873 33.086  1.000 127.077 ? 64  VAL LLL O   1 
ATOM   10487 C CB  . VAL H 3 64  ? -38.174 -26.719 31.444  1.000 126.884 ? 64  VAL LLL CB  1 
ATOM   10488 C CG1 . VAL H 3 64  ? -37.117 -25.899 32.168  1.000 127.034 ? 64  VAL LLL CG1 1 
ATOM   10489 C CG2 . VAL H 3 64  ? -37.544 -27.576 30.357  1.000 125.829 ? 64  VAL LLL CG2 1 
ATOM   10490 N N   . PRO H 3 65  ? -39.321 -26.782 34.738  1.000 126.160 ? 65  PRO LLL N   1 
ATOM   10491 C CA  . PRO H 3 65  ? -39.955 -25.983 35.786  1.000 130.720 ? 65  PRO LLL CA  1 
ATOM   10492 C C   . PRO H 3 65  ? -39.831 -24.459 35.604  1.000 132.165 ? 65  PRO LLL C   1 
ATOM   10493 O O   . PRO H 3 65  ? -38.972 -24.027 34.841  1.000 126.684 ? 65  PRO LLL O   1 
ATOM   10494 C CB  . PRO H 3 65  ? -39.209 -26.431 37.053  1.000 131.864 ? 65  PRO LLL CB  1 
ATOM   10495 C CG  . PRO H 3 65  ? -38.696 -27.815 36.723  1.000 128.927 ? 65  PRO LLL CG  1 
ATOM   10496 C CD  . PRO H 3 65  ? -38.316 -27.719 35.264  1.000 125.010 ? 65  PRO LLL CD  1 
ATOM   10497 N N   . ASP H 3 66  ? -40.687 -23.714 36.326  1.000 137.902 ? 66  ASP LLL N   1 
ATOM   10498 C CA  . ASP H 3 66  ? -40.800 -22.224 36.351  1.000 139.080 ? 66  ASP LLL CA  1 
ATOM   10499 C C   . ASP H 3 66  ? -39.474 -21.597 36.803  1.000 134.910 ? 66  ASP LLL C   1 
ATOM   10500 O O   . ASP H 3 66  ? -39.101 -20.528 36.290  1.000 132.826 ? 66  ASP LLL O   1 
ATOM   10501 C CB  . ASP H 3 66  ? -41.884 -21.714 37.316  1.000 146.320 ? 66  ASP LLL CB  1 
ATOM   10502 C CG  . ASP H 3 66  ? -42.847 -22.748 37.876  1.000 150.330 ? 66  ASP LLL CG  1 
ATOM   10503 O OD1 . ASP H 3 66  ? -42.433 -23.518 38.772  1.000 150.748 ? 66  ASP LLL OD1 1 
ATOM   10504 O OD2 . ASP H 3 66  ? -44.009 -22.755 37.431  1.000 155.327 ? 66  ASP LLL OD2 1 
ATOM   10505 N N   . ARG H 3 67  ? -38.819 -22.235 37.769  1.000 133.294 ? 67  ARG LLL N   1 
ATOM   10506 C CA  . ARG H 3 67  ? -37.650 -21.690 38.499  1.000 134.471 ? 67  ARG LLL CA  1 
ATOM   10507 C C   . ARG H 3 67  ? -36.479 -21.462 37.542  1.000 129.812 ? 67  ARG LLL C   1 
ATOM   10508 O O   . ARG H 3 67  ? -35.613 -20.637 37.876  1.000 128.543 ? 67  ARG LLL O   1 
ATOM   10509 C CB  . ARG H 3 67  ? -37.274 -22.619 39.655  1.000 136.795 ? 67  ARG LLL CB  1 
ATOM   10510 C CG  . ARG H 3 67  ? -36.970 -24.061 39.273  1.000 134.261 ? 67  ARG LLL CG  1 
ATOM   10511 C CD  . ARG H 3 67  ? -36.377 -24.787 40.461  1.000 136.740 ? 67  ARG LLL CD  1 
ATOM   10512 N NE  . ARG H 3 67  ? -36.108 -26.195 40.196  1.000 134.514 ? 67  ARG LLL NE  1 
ATOM   10513 C CZ  . ARG H 3 67  ? -36.991 -27.186 40.312  1.000 136.338 ? 67  ARG LLL CZ  1 
ATOM   10514 N NH1 . ARG H 3 67  ? -38.239 -26.942 40.687  1.000 140.118 ? 67  ARG LLL NH1 1 
ATOM   10515 N NH2 . ARG H 3 67  ? -36.616 -28.428 40.049  1.000 133.800 ? 67  ARG LLL NH2 1 
ATOM   10516 N N   . PHE H 3 68  ? -36.459 -22.157 36.403  1.000 129.719 ? 68  PHE LLL N   1 
ATOM   10517 C CA  . PHE H 3 68  ? -35.487 -21.936 35.298  1.000 129.641 ? 68  PHE LLL CA  1 
ATOM   10518 C C   . PHE H 3 68  ? -35.937 -20.747 34.445  1.000 133.511 ? 68  PHE LLL C   1 
ATOM   10519 O O   . PHE H 3 68  ? -37.109 -20.710 34.030  1.000 137.495 ? 68  PHE LLL O   1 
ATOM   10520 C CB  . PHE H 3 68  ? -35.341 -23.179 34.418  1.000 125.104 ? 68  PHE LLL CB  1 
ATOM   10521 C CG  . PHE H 3 68  ? -34.534 -24.283 35.046  1.000 123.579 ? 68  PHE LLL CG  1 
ATOM   10522 C CD1 . PHE H 3 68  ? -33.157 -24.324 34.907  1.000 120.543 ? 68  PHE LLL CD1 1 
ATOM   10523 C CD2 . PHE H 3 68  ? -35.151 -25.276 35.792  1.000 127.360 ? 68  PHE LLL CD2 1 
ATOM   10524 C CE1 . PHE H 3 68  ? -32.415 -25.338 35.495  1.000 120.703 ? 68  PHE LLL CE1 1 
ATOM   10525 C CE2 . PHE H 3 68  ? -34.406 -26.287 36.383  1.000 126.698 ? 68  PHE LLL CE2 1 
ATOM   10526 C CZ  . PHE H 3 68  ? -33.039 -26.316 36.234  1.000 123.106 ? 68  PHE LLL CZ  1 
ATOM   10527 N N   . SER H 3 69  ? -35.024 -19.809 34.192  1.000 133.965 ? 69  SER LLL N   1 
ATOM   10528 C CA  . SER H 3 69  ? -35.268 -18.587 33.384  1.000 135.137 ? 69  SER LLL CA  1 
ATOM   10529 C C   . SER H 3 69  ? -33.932 -18.039 32.892  1.000 132.424 ? 69  SER LLL C   1 
ATOM   10530 O O   . SER H 3 69  ? -32.989 -17.931 33.702  1.000 132.925 ? 69  SER LLL O   1 
ATOM   10531 C CB  . SER H 3 69  ? -36.020 -17.555 34.171  1.000 141.628 ? 69  SER LLL CB  1 
ATOM   10532 O OG  . SER H 3 69  ? -35.348 -17.278 35.392  1.000 145.838 ? 69  SER LLL OG  1 
ATOM   10533 N N   . GLY H 3 70  ? -33.869 -17.723 31.605  1.000 130.932 ? 70  GLY LLL N   1 
ATOM   10534 C CA  . GLY H 3 70  ? -32.670 -17.180 30.955  1.000 133.048 ? 70  GLY LLL CA  1 
ATOM   10535 C C   . GLY H 3 70  ? -32.902 -15.738 30.568  1.000 138.746 ? 70  GLY LLL C   1 
ATOM   10536 O O   . GLY H 3 70  ? -34.061 -15.380 30.287  1.000 140.845 ? 70  GLY LLL O   1 
ATOM   10537 N N   . SER H 3 71  ? -31.844 -14.934 30.596  1.000 143.225 ? 71  SER LLL N   1 
ATOM   10538 C CA  . SER H 3 71  ? -31.805 -13.565 30.024  1.000 146.864 ? 71  SER LLL CA  1 
ATOM   10539 C C   . SER H 3 71  ? -30.542 -13.451 29.170  1.000 145.406 ? 71  SER LLL C   1 
ATOM   10540 O O   . SER H 3 71  ? -29.742 -14.427 29.156  1.000 141.684 ? 71  SER LLL O   1 
ATOM   10541 C CB  . SER H 3 71  ? -31.843 -12.519 31.105  1.000 152.856 ? 71  SER LLL CB  1 
ATOM   10542 O OG  . SER H 3 71  ? -30.759 -12.696 32.005  1.000 155.027 ? 71  SER LLL OG  1 
ATOM   10543 N N   . GLY H 3 72  ? -30.379 -12.319 28.480  1.000 146.648 ? 72  GLY LLL N   1 
ATOM   10544 C CA  . GLY H 3 72  ? -29.160 -12.037 27.702  1.000 145.125 ? 72  GLY LLL CA  1 
ATOM   10545 C C   . GLY H 3 72  ? -29.327 -10.909 26.702  1.000 144.965 ? 72  GLY LLL C   1 
ATOM   10546 O O   . GLY H 3 72  ? -30.409 -10.785 26.096  1.000 141.689 ? 72  GLY LLL O   1 
ATOM   10547 N N   . SER H 3 73  ? -28.250 -10.143 26.534  1.000 146.609 ? 73  SER LLL N   1 
ATOM   10548 C CA  . SER H 3 73  ? -28.159 -8.896  25.741  1.000 151.339 ? 73  SER LLL CA  1 
ATOM   10549 C C   . SER H 3 73  ? -26.932 -8.986  24.824  1.000 151.823 ? 73  SER LLL C   1 
ATOM   10550 O O   . SER H 3 73  ? -25.864 -8.494  25.223  1.000 155.463 ? 73  SER LLL O   1 
ATOM   10551 C CB  . SER H 3 73  ? -28.109 -7.710  26.681  1.000 156.957 ? 73  SER LLL CB  1 
ATOM   10552 O OG  . SER H 3 73  ? -27.937 -6.491  25.978  1.000 163.292 ? 73  SER LLL OG  1 
ATOM   10553 N N   . GLY H 3 74  ? -27.074 -9.654  23.672  1.000 150.638 ? 74  GLY LLL N   1 
ATOM   10554 C CA  . GLY H 3 74  ? -26.118 -9.624  22.545  1.000 152.012 ? 74  GLY LLL CA  1 
ATOM   10555 C C   . GLY H 3 74  ? -24.969 -10.614 22.694  1.000 149.800 ? 74  GLY LLL C   1 
ATOM   10556 O O   . GLY H 3 74  ? -24.958 -11.616 21.951  1.000 147.738 ? 74  GLY LLL O   1 
ATOM   10557 N N   . THR H 3 75  ? -24.004 -10.310 23.572  1.000 151.800 ? 75  THR LLL N   1 
ATOM   10558 C CA  . THR H 3 75  ? -22.730 -11.062 23.763  1.000 151.058 ? 75  THR LLL CA  1 
ATOM   10559 C C   . THR H 3 75  ? -22.683 -11.711 25.154  1.000 147.927 ? 75  THR LLL C   1 
ATOM   10560 O O   . THR H 3 75  ? -21.754 -12.512 25.383  1.000 144.195 ? 75  THR LLL O   1 
ATOM   10561 C CB  . THR H 3 75  ? -21.515 -10.142 23.559  1.000 158.262 ? 75  THR LLL CB  1 
ATOM   10562 O OG1 . THR H 3 75  ? -21.463 -9.178  24.610  1.000 163.892 ? 75  THR LLL OG1 1 
ATOM   10563 C CG2 . THR H 3 75  ? -21.536 -9.394  22.243  1.000 161.521 ? 75  THR LLL CG2 1 
ATOM   10564 N N   . ASP H 3 76  ? -23.644 -11.386 26.034  1.000 148.706 ? 76  ASP LLL N   1 
ATOM   10565 C CA  . ASP H 3 76  ? -23.691 -11.786 27.471  1.000 149.008 ? 76  ASP LLL CA  1 
ATOM   10566 C C   . ASP H 3 76  ? -25.049 -12.424 27.792  1.000 147.672 ? 76  ASP LLL C   1 
ATOM   10567 O O   . ASP H 3 76  ? -26.062 -11.729 27.595  1.000 151.373 ? 76  ASP LLL O   1 
ATOM   10568 C CB  . ASP H 3 76  ? -23.488 -10.573 28.381  1.000 152.709 ? 76  ASP LLL CB  1 
ATOM   10569 C CG  . ASP H 3 76  ? -22.085 -9.998  28.318  1.000 156.451 ? 76  ASP LLL CG  1 
ATOM   10570 O OD1 . ASP H 3 76  ? -21.126 -10.775 28.507  1.000 156.416 ? 76  ASP LLL OD1 1 
ATOM   10571 O OD2 . ASP H 3 76  ? -21.961 -8.786  28.063  1.000 160.566 ? 76  ASP LLL OD2 1 
ATOM   10572 N N   . PHE H 3 77  ? -25.061 -13.672 28.288  1.000 145.632 ? 77  PHE LLL N   1 
ATOM   10573 C CA  . PHE H 3 77  ? -26.282 -14.471 28.604  1.000 144.540 ? 77  PHE LLL CA  1 
ATOM   10574 C C   . PHE H 3 77  ? -26.145 -15.151 29.966  1.000 142.450 ? 77  PHE LLL C   1 
ATOM   10575 O O   . PHE H 3 77  ? -25.020 -15.561 30.331  1.000 141.783 ? 77  PHE LLL O   1 
ATOM   10576 C CB  . PHE H 3 77  ? -26.541 -15.529 27.529  1.000 144.254 ? 77  PHE LLL CB  1 
ATOM   10577 C CG  . PHE H 3 77  ? -26.570 -14.940 26.147  1.000 148.782 ? 77  PHE LLL CG  1 
ATOM   10578 C CD1 . PHE H 3 77  ? -27.727 -14.357 25.662  1.000 151.876 ? 77  PHE LLL CD1 1 
ATOM   10579 C CD2 . PHE H 3 77  ? -25.425 -14.891 25.369  1.000 151.922 ? 77  PHE LLL CD2 1 
ATOM   10580 C CE1 . PHE H 3 77  ? -27.749 -13.766 24.411  1.000 154.722 ? 77  PHE LLL CE1 1 
ATOM   10581 C CE2 . PHE H 3 77  ? -25.448 -14.296 24.117  1.000 155.098 ? 77  PHE LLL CE2 1 
ATOM   10582 C CZ  . PHE H 3 77  ? -26.609 -13.732 23.644  1.000 156.524 ? 77  PHE LLL CZ  1 
ATOM   10583 N N   . THR H 3 78  ? -27.268 -15.280 30.680  1.000 140.284 ? 78  THR LLL N   1 
ATOM   10584 C CA  . THR H 3 78  ? -27.322 -15.848 32.050  1.000 138.232 ? 78  THR LLL CA  1 
ATOM   10585 C C   . THR H 3 78  ? -28.483 -16.827 32.177  1.000 135.733 ? 78  THR LLL C   1 
ATOM   10586 O O   . THR H 3 78  ? -29.571 -16.539 31.633  1.000 137.579 ? 78  THR LLL O   1 
ATOM   10587 C CB  . THR H 3 78  ? -27.488 -14.768 33.119  1.000 141.441 ? 78  THR LLL CB  1 
ATOM   10588 O OG1 . THR H 3 78  ? -26.656 -13.672 32.748  1.000 145.286 ? 78  THR LLL OG1 1 
ATOM   10589 C CG2 . THR H 3 78  ? -27.123 -15.269 34.500  1.000 142.572 ? 78  THR LLL CG2 1 
ATOM   10590 N N   . LEU H 3 79  ? -28.227 -17.924 32.890  1.000 133.726 ? 79  LEU LLL N   1 
ATOM   10591 C CA  . LEU H 3 79  ? -29.240 -18.908 33.339  1.000 132.110 ? 79  LEU LLL CA  1 
ATOM   10592 C C   . LEU H 3 79  ? -29.406 -18.775 34.854  1.000 135.370 ? 79  LEU LLL C   1 
ATOM   10593 O O   . LEU H 3 79  ? -28.400 -18.937 35.574  1.000 137.584 ? 79  LEU LLL O   1 
ATOM   10594 C CB  . LEU H 3 79  ? -28.773 -20.318 32.973  1.000 128.398 ? 79  LEU LLL CB  1 
ATOM   10595 C CG  . LEU H 3 79  ? -29.676 -21.447 33.468  1.000 127.760 ? 79  LEU LLL CG  1 
ATOM   10596 C CD1 . LEU H 3 79  ? -31.141 -21.135 33.181  1.000 128.829 ? 79  LEU LLL CD1 1 
ATOM   10597 C CD2 . LEU H 3 79  ? -29.274 -22.782 32.852  1.000 124.763 ? 79  LEU LLL CD2 1 
ATOM   10598 N N   . THR H 3 80  ? -30.628 -18.510 35.311  1.000 134.956 ? 80  THR LLL N   1 
ATOM   10599 C CA  . THR H 3 80  ? -30.950 -18.324 36.743  1.000 135.711 ? 80  THR LLL CA  1 
ATOM   10600 C C   . THR H 3 80  ? -31.916 -19.416 37.188  1.000 133.938 ? 80  THR LLL C   1 
ATOM   10601 O O   . THR H 3 80  ? -32.980 -19.555 36.557  1.000 130.522 ? 80  THR LLL O   1 
ATOM   10602 C CB  . THR H 3 80  ? -31.516 -16.927 36.987  1.000 140.412 ? 80  THR LLL CB  1 
ATOM   10603 O OG1 . THR H 3 80  ? -30.790 -16.061 36.117  1.000 142.557 ? 80  THR LLL OG1 1 
ATOM   10604 C CG2 . THR H 3 80  ? -31.391 -16.490 38.429  1.000 144.805 ? 80  THR LLL CG2 1 
ATOM   10605 N N   . ILE H 3 81  ? -31.530 -20.144 38.237  1.000 136.233 ? 81  ILE LLL N   1 
ATOM   10606 C CA  . ILE H 3 81  ? -32.328 -21.217 38.898  1.000 137.103 ? 81  ILE LLL CA  1 
ATOM   10607 C C   . ILE H 3 81  ? -32.778 -20.709 40.271  1.000 141.031 ? 81  ILE LLL C   1 
ATOM   10608 O O   . ILE H 3 81  ? -32.180 -21.137 41.265  1.000 142.578 ? 81  ILE LLL O   1 
ATOM   10609 C CB  . ILE H 3 81  ? -31.501 -22.515 39.037  1.000 134.977 ? 81  ILE LLL CB  1 
ATOM   10610 C CG1 . ILE H 3 81  ? -30.689 -22.831 37.776  1.000 132.084 ? 81  ILE LLL CG1 1 
ATOM   10611 C CG2 . ILE H 3 81  ? -32.400 -23.675 39.436  1.000 134.745 ? 81  ILE LLL CG2 1 
ATOM   10612 C CD1 . ILE H 3 81  ? -29.823 -24.078 37.884  1.000 130.512 ? 81  ILE LLL CD1 1 
ATOM   10613 N N   . SER H 3 82  ? -33.779 -19.828 40.342  1.000 144.549 ? 82  SER LLL N   1 
ATOM   10614 C CA  . SER H 3 82  ? -34.382 -19.422 41.640  1.000 150.637 ? 82  SER LLL CA  1 
ATOM   10615 C C   . SER H 3 82  ? -34.865 -20.702 42.332  1.000 150.316 ? 82  SER LLL C   1 
ATOM   10616 O O   . SER H 3 82  ? -35.249 -21.639 41.612  1.000 151.009 ? 82  SER LLL O   1 
ATOM   10617 C CB  . SER H 3 82  ? -35.483 -18.385 41.478  1.000 155.151 ? 82  SER LLL CB  1 
ATOM   10618 O OG  . SER H 3 82  ? -36.714 -18.972 41.073  1.000 156.203 ? 82  SER LLL OG  1 
ATOM   10619 N N   . SER H 3 83  ? -34.774 -20.778 43.661  1.000 151.087 ? 83  SER LLL N   1 
ATOM   10620 C CA  . SER H 3 83  ? -35.274 -21.909 44.489  1.000 149.837 ? 83  SER LLL CA  1 
ATOM   10621 C C   . SER H 3 83  ? -34.662 -23.236 44.023  1.000 142.643 ? 83  SER LLL C   1 
ATOM   10622 O O   . SER H 3 83  ? -35.435 -24.118 43.590  1.000 139.233 ? 83  SER LLL O   1 
ATOM   10623 C CB  . SER H 3 83  ? -36.785 -21.978 44.455  1.000 153.373 ? 83  SER LLL CB  1 
ATOM   10624 O OG  . SER H 3 83  ? -37.370 -20.764 44.906  1.000 159.861 ? 83  SER LLL OG  1 
ATOM   10625 N N   . LEU H 3 84  ? -33.337 -23.390 44.113  1.000 141.071 ? 84  LEU LLL N   1 
ATOM   10626 C CA  . LEU H 3 84  ? -32.633 -24.625 43.662  1.000 139.394 ? 84  LEU LLL CA  1 
ATOM   10627 C C   . LEU H 3 84  ? -33.250 -25.825 44.379  1.000 141.512 ? 84  LEU LLL C   1 
ATOM   10628 O O   . LEU H 3 84  ? -33.675 -25.654 45.535  1.000 149.052 ? 84  LEU LLL O   1 
ATOM   10629 C CB  . LEU H 3 84  ? -31.132 -24.532 43.960  1.000 139.032 ? 84  LEU LLL CB  1 
ATOM   10630 C CG  . LEU H 3 84  ? -30.278 -25.688 43.431  1.000 134.967 ? 84  LEU LLL CG  1 
ATOM   10631 C CD1 . LEU H 3 84  ? -30.303 -25.756 41.908  1.000 131.293 ? 84  LEU LLL CD1 1 
ATOM   10632 C CD2 . LEU H 3 84  ? -28.844 -25.566 43.917  1.000 135.216 ? 84  LEU LLL CD2 1 
ATOM   10633 N N   . GLN H 3 85  ? -33.296 -26.981 43.717  1.000 138.911 ? 85  GLN LLL N   1 
ATOM   10634 C CA  . GLN H 3 85  ? -33.920 -28.210 44.265  1.000 142.140 ? 85  GLN LLL CA  1 
ATOM   10635 C C   . GLN H 3 85  ? -32.943 -29.384 44.159  1.000 141.891 ? 85  GLN LLL C   1 
ATOM   10636 O O   . GLN H 3 85  ? -31.912 -29.256 43.463  1.000 136.250 ? 85  GLN LLL O   1 
ATOM   10637 C CB  . GLN H 3 85  ? -35.221 -28.516 43.523  1.000 141.888 ? 85  GLN LLL CB  1 
ATOM   10638 C CG  . GLN H 3 85  ? -36.344 -27.547 43.846  1.000 144.888 ? 85  GLN LLL CG  1 
ATOM   10639 C CD  . GLN H 3 85  ? -37.103 -28.043 45.052  1.000 149.926 ? 85  GLN LLL CD  1 
ATOM   10640 O OE1 . GLN H 3 85  ? -36.550 -28.182 46.145  1.000 151.373 ? 85  GLN LLL OE1 1 
ATOM   10641 N NE2 . GLN H 3 85  ? -38.380 -28.341 44.851  1.000 151.602 ? 85  GLN LLL NE2 1 
ATOM   10642 N N   . ALA H 3 86  ? -33.280 -30.474 44.853  1.000 146.570 ? 86  ALA LLL N   1 
ATOM   10643 C CA  . ALA H 3 86  ? -32.612 -31.795 44.794  1.000 145.573 ? 86  ALA LLL CA  1 
ATOM   10644 C C   . ALA H 3 86  ? -32.158 -32.095 43.359  1.000 140.541 ? 86  ALA LLL C   1 
ATOM   10645 O O   . ALA H 3 86  ? -30.948 -32.011 43.094  1.000 133.880 ? 86  ALA LLL O   1 
ATOM   10646 C CB  . ALA H 3 86  ? -33.559 -32.856 45.309  1.000 148.110 ? 86  ALA LLL CB  1 
ATOM   10647 N N   . GLU H 3 87  ? -33.111 -32.377 42.465  1.000 141.435 ? 87  GLU LLL N   1 
ATOM   10648 C CA  . GLU H 3 87  ? -32.867 -33.034 41.152  1.000 140.636 ? 87  GLU LLL CA  1 
ATOM   10649 C C   . GLU H 3 87  ? -32.262 -32.049 40.139  1.000 135.973 ? 87  GLU LLL C   1 
ATOM   10650 O O   . GLU H 3 87  ? -32.104 -32.459 38.971  1.000 132.147 ? 87  GLU LLL O   1 
ATOM   10651 C CB  . GLU H 3 87  ? -34.160 -33.674 40.629  1.000 144.285 ? 87  GLU LLL CB  1 
ATOM   10652 C CG  . GLU H 3 87  ? -35.360 -32.736 40.561  1.000 146.505 ? 87  GLU LLL CG  1 
ATOM   10653 C CD  . GLU H 3 87  ? -36.509 -33.206 39.679  1.000 148.531 ? 87  GLU LLL CD  1 
ATOM   10654 O OE1 . GLU H 3 87  ? -36.311 -34.148 38.878  1.000 150.072 ? 87  GLU LLL OE1 1 
ATOM   10655 O OE2 . GLU H 3 87  ? -37.603 -32.619 39.782  1.000 148.956 ? 87  GLU LLL OE2 1 
ATOM   10656 N N   . ASP H 3 88  ? -31.911 -30.825 40.564  1.000 134.940 ? 88  ASP LLL N   1 
ATOM   10657 C CA  . ASP H 3 88  ? -31.295 -29.774 39.705  1.000 132.614 ? 88  ASP LLL CA  1 
ATOM   10658 C C   . ASP H 3 88  ? -29.772 -29.936 39.653  1.000 129.633 ? 88  ASP LLL C   1 
ATOM   10659 O O   . ASP H 3 88  ? -29.151 -29.282 38.803  1.000 124.819 ? 88  ASP LLL O   1 
ATOM   10660 C CB  . ASP H 3 88  ? -31.620 -28.362 40.197  1.000 136.027 ? 88  ASP LLL CB  1 
ATOM   10661 C CG  . ASP H 3 88  ? -33.070 -27.956 40.003  1.000 139.174 ? 88  ASP LLL CG  1 
ATOM   10662 O OD1 . ASP H 3 88  ? -33.644 -28.301 38.951  1.000 137.655 ? 88  ASP LLL OD1 1 
ATOM   10663 O OD2 . ASP H 3 88  ? -33.619 -27.302 40.911  1.000 146.576 ? 88  ASP LLL OD2 1 
ATOM   10664 N N   . VAL H 3 89  ? -29.193 -30.747 40.541  1.000 130.685 ? 89  VAL LLL N   1 
ATOM   10665 C CA  . VAL H 3 89  ? -27.735 -31.072 40.531  1.000 129.408 ? 89  VAL LLL CA  1 
ATOM   10666 C C   . VAL H 3 89  ? -27.412 -31.731 39.187  1.000 128.565 ? 89  VAL LLL C   1 
ATOM   10667 O O   . VAL H 3 89  ? -28.047 -32.767 38.869  1.000 131.780 ? 89  VAL LLL O   1 
ATOM   10668 C CB  . VAL H 3 89  ? -27.333 -31.991 41.701  1.000 131.736 ? 89  VAL LLL CB  1 
ATOM   10669 C CG1 . VAL H 3 89  ? -25.883 -32.445 41.603  1.000 131.002 ? 89  VAL LLL CG1 1 
ATOM   10670 C CG2 . VAL H 3 89  ? -27.587 -31.337 43.048  1.000 136.037 ? 89  VAL LLL CG2 1 
ATOM   10671 N N   . ALA H 3 90  ? -26.462 -31.157 38.441  1.000 125.996 ? 90  ALA LLL N   1 
ATOM   10672 C CA  . ALA H 3 90  ? -25.981 -31.661 37.133  1.000 122.101 ? 90  ALA LLL CA  1 
ATOM   10673 C C   . ALA H 3 90  ? -24.939 -30.703 36.548  1.000 119.478 ? 90  ALA LLL C   1 
ATOM   10674 O O   . ALA H 3 90  ? -24.655 -29.670 37.183  1.000 118.789 ? 90  ALA LLL O   1 
ATOM   10675 C CB  . ALA H 3 90  ? -27.152 -31.812 36.193  1.000 121.906 ? 90  ALA LLL CB  1 
ATOM   10676 N N   . VAL H 3 91  ? -24.428 -31.041 35.361  1.000 118.472 ? 91  VAL LLL N   1 
ATOM   10677 C CA  . VAL H 3 91  ? -23.592 -30.167 34.482  1.000 116.139 ? 91  VAL LLL CA  1 
ATOM   10678 C C   . VAL H 3 91  ? -24.528 -29.352 33.580  1.000 113.022 ? 91  VAL LLL C   1 
ATOM   10679 O O   . VAL H 3 91  ? -25.516 -29.919 33.061  1.000 112.073 ? 91  VAL LLL O   1 
ATOM   10680 C CB  . VAL H 3 91  ? -22.616 -30.988 33.616  1.000 116.998 ? 91  VAL LLL CB  1 
ATOM   10681 C CG1 . VAL H 3 91  ? -21.473 -30.118 33.117  1.000 118.075 ? 91  VAL LLL CG1 1 
ATOM   10682 C CG2 . VAL H 3 91  ? -22.097 -32.239 34.322  1.000 117.988 ? 91  VAL LLL CG2 1 
ATOM   10683 N N   . TYR H 3 92  ? -24.217 -28.076 33.374  1.000 110.887 ? 92  TYR LLL N   1 
ATOM   10684 C CA  . TYR H 3 92  ? -25.024 -27.138 32.558  1.000 110.457 ? 92  TYR LLL CA  1 
ATOM   10685 C C   . TYR H 3 92  ? -24.126 -26.562 31.462  1.000 110.937 ? 92  TYR LLL C   1 
ATOM   10686 O O   . TYR H 3 92  ? -23.073 -25.991 31.796  1.000 112.624 ? 92  TYR LLL O   1 
ATOM   10687 C CB  . TYR H 3 92  ? -25.637 -26.050 33.448  1.000 112.557 ? 92  TYR LLL CB  1 
ATOM   10688 C CG  . TYR H 3 92  ? -26.749 -26.544 34.332  1.000 112.016 ? 92  TYR LLL CG  1 
ATOM   10689 C CD1 . TYR H 3 92  ? -26.480 -27.142 35.548  1.000 113.896 ? 92  TYR LLL CD1 1 
ATOM   10690 C CD2 . TYR H 3 92  ? -28.068 -26.468 33.928  1.000 112.712 ? 92  TYR LLL CD2 1 
ATOM   10691 C CE1 . TYR H 3 92  ? -27.495 -27.633 36.353  1.000 116.371 ? 92  TYR LLL CE1 1 
ATOM   10692 C CE2 . TYR H 3 92  ? -29.096 -26.954 34.721  1.000 114.704 ? 92  TYR LLL CE2 1 
ATOM   10693 C CZ  . TYR H 3 92  ? -28.813 -27.534 35.942  1.000 115.939 ? 92  TYR LLL CZ  1 
ATOM   10694 O OH  . TYR H 3 92  ? -29.835 -28.015 36.710  1.000 116.075 ? 92  TYR LLL OH  1 
ATOM   10695 N N   . TYR H 3 93  ? -24.533 -26.726 30.200  1.000 109.566 ? 93  TYR LLL N   1 
ATOM   10696 C CA  . TYR H 3 93  ? -23.850 -26.180 28.997  1.000 108.144 ? 93  TYR LLL CA  1 
ATOM   10697 C C   . TYR H 3 93  ? -24.771 -25.151 28.329  1.000 106.906 ? 93  TYR LLL C   1 
ATOM   10698 O O   . TYR H 3 93  ? -25.986 -25.382 28.255  1.000 103.215 ? 93  TYR LLL O   1 
ATOM   10699 C CB  . TYR H 3 93  ? -23.475 -27.299 28.012  1.000 106.669 ? 93  TYR LLL CB  1 
ATOM   10700 C CG  . TYR H 3 93  ? -22.740 -28.484 28.592  1.000 106.434 ? 93  TYR LLL CG  1 
ATOM   10701 C CD1 . TYR H 3 93  ? -23.439 -29.554 29.123  1.000 106.819 ? 93  TYR LLL CD1 1 
ATOM   10702 C CD2 . TYR H 3 93  ? -21.354 -28.556 28.600  1.000 108.596 ? 93  TYR LLL CD2 1 
ATOM   10703 C CE1 . TYR H 3 93  ? -22.790 -30.647 29.676  1.000 108.912 ? 93  TYR LLL CE1 1 
ATOM   10704 C CE2 . TYR H 3 93  ? -20.687 -29.645 29.143  1.000 111.011 ? 93  TYR LLL CE2 1 
ATOM   10705 C CZ  . TYR H 3 93  ? -21.408 -30.704 29.680  1.000 111.297 ? 93  TYR LLL CZ  1 
ATOM   10706 O OH  . TYR H 3 93  ? -20.808 -31.811 30.223  1.000 112.711 ? 93  TYR LLL OH  1 
ATOM   10707 N N   . CYS H 3 94  ? -24.207 -24.038 27.865  1.000 110.557 ? 94  CYS LLL N   1 
ATOM   10708 C CA  . CYS H 3 94  ? -24.840 -23.137 26.867  1.000 113.989 ? 94  CYS LLL CA  1 
ATOM   10709 C C   . CYS H 3 94  ? -24.274 -23.469 25.479  1.000 114.891 ? 94  CYS LLL C   1 
ATOM   10710 O O   . CYS H 3 94  ? -23.076 -23.816 25.394  1.000 116.060 ? 94  CYS LLL O   1 
ATOM   10711 C CB  . CYS H 3 94  ? -24.608 -21.669 27.202  1.000 118.466 ? 94  CYS LLL CB  1 
ATOM   10712 S SG  . CYS H 3 94  ? -22.865 -21.179 27.115  1.000 123.744 ? 94  CYS LLL SG  1 
ATOM   10713 N N   . GLN H 3 95  ? -25.118 -23.377 24.447  1.000 114.980 ? 95  GLN LLL N   1 
ATOM   10714 C CA  . GLN H 3 95  ? -24.797 -23.659 23.021  1.000 114.750 ? 95  GLN LLL CA  1 
ATOM   10715 C C   . GLN H 3 95  ? -25.322 -22.507 22.163  1.000 116.181 ? 95  GLN LLL C   1 
ATOM   10716 O O   . GLN H 3 95  ? -26.488 -22.130 22.353  1.000 118.085 ? 95  GLN LLL O   1 
ATOM   10717 C CB  . GLN H 3 95  ? -25.484 -24.946 22.564  1.000 113.233 ? 95  GLN LLL CB  1 
ATOM   10718 C CG  . GLN H 3 95  ? -25.176 -25.338 21.125  1.000 115.687 ? 95  GLN LLL CG  1 
ATOM   10719 C CD  . GLN H 3 95  ? -26.390 -25.825 20.368  1.000 117.960 ? 95  GLN LLL CD  1 
ATOM   10720 O OE1 . GLN H 3 95  ? -26.508 -27.006 20.037  1.000 120.098 ? 95  GLN LLL OE1 1 
ATOM   10721 N NE2 . GLN H 3 95  ? -27.299 -24.911 20.066  1.000 119.528 ? 95  GLN LLL NE2 1 
ATOM   10722 N N   . GLN H 3 96  ? -24.509 -21.979 21.246  1.000 116.576 ? 96  GLN LLL N   1 
ATOM   10723 C CA  . GLN H 3 96  ? -24.981 -21.011 20.223  1.000 117.014 ? 96  GLN LLL CA  1 
ATOM   10724 C C   . GLN H 3 96  ? -25.443 -21.807 19.004  1.000 115.231 ? 96  GLN LLL C   1 
ATOM   10725 O O   . GLN H 3 96  ? -24.827 -22.841 18.699  1.000 114.905 ? 96  GLN LLL O   1 
ATOM   10726 C CB  . GLN H 3 96  ? -23.891 -20.005 19.858  1.000 120.448 ? 96  GLN LLL CB  1 
ATOM   10727 C CG  . GLN H 3 96  ? -22.780 -20.584 18.995  1.000 123.021 ? 96  GLN LLL CG  1 
ATOM   10728 C CD  . GLN H 3 96  ? -23.152 -20.709 17.539  1.000 124.344 ? 96  GLN LLL CD  1 
ATOM   10729 O OE1 . GLN H 3 96  ? -24.052 -20.033 17.037  1.000 125.497 ? 96  GLN LLL OE1 1 
ATOM   10730 N NE2 . GLN H 3 96  ? -22.455 -21.596 16.849  1.000 125.011 ? 96  GLN LLL NE2 1 
ATOM   10731 N N   . TYR H 3 97  ? -26.499 -21.345 18.344  1.000 115.232 ? 97  TYR LLL N   1 
ATOM   10732 C CA  . TYR H 3 97  ? -26.974 -21.903 17.056  1.000 117.831 ? 97  TYR LLL CA  1 
ATOM   10733 C C   . TYR H 3 97  ? -27.387 -20.745 16.135  1.000 122.499 ? 97  TYR LLL C   1 
ATOM   10734 O O   . TYR H 3 97  ? -28.386 -20.889 15.409  1.000 125.541 ? 97  TYR LLL O   1 
ATOM   10735 C CB  . TYR H 3 97  ? -28.064 -22.947 17.314  1.000 115.628 ? 97  TYR LLL CB  1 
ATOM   10736 C CG  . TYR H 3 97  ? -29.304 -22.435 18.000  1.000 115.055 ? 97  TYR LLL CG  1 
ATOM   10737 C CD1 . TYR H 3 97  ? -29.369 -22.293 19.375  1.000 112.890 ? 97  TYR LLL CD1 1 
ATOM   10738 C CD2 . TYR H 3 97  ? -30.429 -22.102 17.268  1.000 117.774 ? 97  TYR LLL CD2 1 
ATOM   10739 C CE1 . TYR H 3 97  ? -30.512 -21.821 20.004  1.000 112.154 ? 97  TYR LLL CE1 1 
ATOM   10740 C CE2 . TYR H 3 97  ? -31.579 -21.631 17.881  1.000 118.552 ? 97  TYR LLL CE2 1 
ATOM   10741 C CZ  . TYR H 3 97  ? -31.626 -21.495 19.255  1.000 114.177 ? 97  TYR LLL CZ  1 
ATOM   10742 O OH  . TYR H 3 97  ? -32.775 -21.040 19.828  1.000 112.780 ? 97  TYR LLL OH  1 
ATOM   10743 N N   . TYR H 3 98  ? -26.632 -19.636 16.149  1.000 124.962 ? 98  TYR LLL N   1 
ATOM   10744 C CA  . TYR H 3 98  ? -26.759 -18.533 15.155  1.000 127.291 ? 98  TYR LLL CA  1 
ATOM   10745 C C   . TYR H 3 98  ? -26.316 -19.068 13.791  1.000 129.348 ? 98  TYR LLL C   1 
ATOM   10746 O O   . TYR H 3 98  ? -26.931 -18.720 12.766  1.000 134.213 ? 98  TYR LLL O   1 
ATOM   10747 C CB  . TYR H 3 98  ? -25.936 -17.292 15.524  1.000 128.407 ? 98  TYR LLL CB  1 
ATOM   10748 C CG  . TYR H 3 98  ? -26.051 -16.155 14.535  1.000 131.688 ? 98  TYR LLL CG  1 
ATOM   10749 C CD1 . TYR H 3 98  ? -27.130 -15.287 14.561  1.000 133.116 ? 98  TYR LLL CD1 1 
ATOM   10750 C CD2 . TYR H 3 98  ? -25.097 -15.959 13.548  1.000 135.037 ? 98  TYR LLL CD2 1 
ATOM   10751 C CE1 . TYR H 3 98  ? -27.256 -14.255 13.643  1.000 137.722 ? 98  TYR LLL CE1 1 
ATOM   10752 C CE2 . TYR H 3 98  ? -25.203 -14.930 12.624  1.000 139.116 ? 98  TYR LLL CE2 1 
ATOM   10753 C CZ  . TYR H 3 98  ? -26.283 -14.067 12.674  1.000 140.438 ? 98  TYR LLL CZ  1 
ATOM   10754 O OH  . TYR H 3 98  ? -26.393 -13.044 11.776  1.000 143.740 ? 98  TYR LLL OH  1 
ATOM   10755 N N   . SER H 3 99  ? -25.266 -19.890 13.783  1.000 128.341 ? 99  SER LLL N   1 
ATOM   10756 C CA  . SER H 3 99  ? -24.671 -20.468 12.553  1.000 132.043 ? 99  SER LLL CA  1 
ATOM   10757 C C   . SER H 3 99  ? -23.782 -21.656 12.909  1.000 129.966 ? 99  SER LLL C   1 
ATOM   10758 O O   . SER H 3 99  ? -23.293 -21.715 14.044  1.000 128.478 ? 99  SER LLL O   1 
ATOM   10759 C CB  . SER H 3 99  ? -23.887 -19.426 11.793  1.000 139.048 ? 99  SER LLL CB  1 
ATOM   10760 O OG  . SER H 3 99  ? -22.630 -19.177 12.416  1.000 140.992 ? 99  SER LLL OG  1 
ATOM   10761 N N   . THR H 3 100 ? -23.570 -22.549 11.944  1.000 132.145 ? 100 THR LLL N   1 
ATOM   10762 C CA  . THR H 3 100 ? -22.576 -23.646 12.021  1.000 133.691 ? 100 THR LLL CA  1 
ATOM   10763 C C   . THR H 3 100 ? -21.183 -23.022 11.977  1.000 137.322 ? 100 THR LLL C   1 
ATOM   10764 O O   . THR H 3 100 ? -20.977 -22.020 11.296  1.000 144.792 ? 100 THR LLL O   1 
ATOM   10765 C CB  . THR H 3 100 ? -22.801 -24.686 10.917  1.000 135.706 ? 100 THR LLL CB  1 
ATOM   10766 O OG1 . THR H 3 100 ? -22.560 -24.072 9.649   1.000 141.647 ? 100 THR LLL OG1 1 
ATOM   10767 C CG2 . THR H 3 100 ? -24.196 -25.273 10.955  1.000 133.141 ? 100 THR LLL CG2 1 
ATOM   10768 N N   . PRO H 3 101 ? -20.192 -23.568 12.716  1.000 136.103 ? 101 PRO LLL N   1 
ATOM   10769 C CA  . PRO H 3 101 ? -20.404 -24.755 13.535  1.000 133.000 ? 101 PRO LLL CA  1 
ATOM   10770 C C   . PRO H 3 101 ? -21.074 -24.354 14.854  1.000 131.591 ? 101 PRO LLL C   1 
ATOM   10771 O O   . PRO H 3 101 ? -20.565 -23.457 15.496  1.000 132.135 ? 101 PRO LLL O   1 
ATOM   10772 C CB  . PRO H 3 101 ? -18.978 -25.273 13.762  1.000 134.793 ? 101 PRO LLL CB  1 
ATOM   10773 C CG  . PRO H 3 101 ? -18.119 -24.019 13.759  1.000 138.155 ? 101 PRO LLL CG  1 
ATOM   10774 C CD  . PRO H 3 101 ? -18.824 -23.037 12.841  1.000 139.330 ? 101 PRO LLL CD  1 
ATOM   10775 N N   . TYR H 3 102 ? -22.196 -24.988 15.212  1.000 131.161 ? 102 TYR LLL N   1 
ATOM   10776 C CA  . TYR H 3 102 ? -22.775 -24.907 16.577  1.000 128.906 ? 102 TYR LLL CA  1 
ATOM   10777 C C   . TYR H 3 102 ? -21.602 -25.111 17.549  1.000 127.686 ? 102 TYR LLL C   1 
ATOM   10778 O O   . TYR H 3 102 ? -20.722 -25.942 17.237  1.000 130.050 ? 102 TYR LLL O   1 
ATOM   10779 C CB  . TYR H 3 102 ? -23.846 -25.981 16.802  1.000 129.422 ? 102 TYR LLL CB  1 
ATOM   10780 C CG  . TYR H 3 102 ? -25.141 -25.902 16.023  1.000 132.409 ? 102 TYR LLL CG  1 
ATOM   10781 C CD1 . TYR H 3 102 ? -25.345 -25.047 14.947  1.000 134.577 ? 102 TYR LLL CD1 1 
ATOM   10782 C CD2 . TYR H 3 102 ? -26.174 -26.766 16.353  1.000 135.785 ? 102 TYR LLL CD2 1 
ATOM   10783 C CE1 . TYR H 3 102 ? -26.548 -25.038 14.250  1.000 136.257 ? 102 TYR LLL CE1 1 
ATOM   10784 C CE2 . TYR H 3 102 ? -27.381 -26.770 15.672  1.000 137.908 ? 102 TYR LLL CE2 1 
ATOM   10785 C CZ  . TYR H 3 102 ? -27.571 -25.905 14.613  1.000 137.546 ? 102 TYR LLL CZ  1 
ATOM   10786 O OH  . TYR H 3 102 ? -28.780 -25.951 13.978  1.000 137.684 ? 102 TYR LLL OH  1 
ATOM   10787 N N   . THR H 3 103 ? -21.541 -24.370 18.659  1.000 125.159 ? 103 THR LLL N   1 
ATOM   10788 C CA  . THR H 3 103 ? -20.455 -24.503 19.670  1.000 125.141 ? 103 THR LLL CA  1 
ATOM   10789 C C   . THR H 3 103 ? -21.044 -24.438 21.077  1.000 121.622 ? 103 THR LLL C   1 
ATOM   10790 O O   . THR H 3 103 ? -21.972 -23.633 21.284  1.000 121.108 ? 103 THR LLL O   1 
ATOM   10791 C CB  . THR H 3 103 ? -19.368 -23.438 19.483  1.000 129.887 ? 103 THR LLL CB  1 
ATOM   10792 O OG1 . THR H 3 103 ? -19.978 -22.148 19.440  1.000 129.256 ? 103 THR LLL OG1 1 
ATOM   10793 C CG2 . THR H 3 103 ? -18.554 -23.668 18.229  1.000 134.643 ? 103 THR LLL CG2 1 
ATOM   10794 N N   . PHE H 3 104 ? -20.517 -25.262 21.987  1.000 118.966 ? 104 PHE LLL N   1 
ATOM   10795 C CA  . PHE H 3 104 ? -20.929 -25.314 23.412  1.000 115.976 ? 104 PHE LLL CA  1 
ATOM   10796 C C   . PHE H 3 104 ? -19.887 -24.587 24.261  1.000 117.375 ? 104 PHE LLL C   1 
ATOM   10797 O O   . PHE H 3 104 ? -18.742 -24.412 23.772  1.000 122.600 ? 104 PHE LLL O   1 
ATOM   10798 C CB  . PHE H 3 104 ? -21.042 -26.755 23.910  1.000 114.629 ? 104 PHE LLL CB  1 
ATOM   10799 C CG  . PHE H 3 104 ? -22.131 -27.592 23.288  1.000 112.985 ? 104 PHE LLL CG  1 
ATOM   10800 C CD1 . PHE H 3 104 ? -23.410 -27.603 23.815  1.000 112.233 ? 104 PHE LLL CD1 1 
ATOM   10801 C CD2 . PHE H 3 104 ? -21.866 -28.413 22.204  1.000 115.266 ? 104 PHE LLL CD2 1 
ATOM   10802 C CE1 . PHE H 3 104 ? -24.404 -28.391 23.254  1.000 112.368 ? 104 PHE LLL CE1 1 
ATOM   10803 C CE2 . PHE H 3 104 ? -22.862 -29.200 21.642  1.000 114.531 ? 104 PHE LLL CE2 1 
ATOM   10804 C CZ  . PHE H 3 104 ? -24.132 -29.184 22.165  1.000 112.620 ? 104 PHE LLL CZ  1 
ATOM   10805 N N   . GLY H 3 105 ? -20.281 -24.194 25.479  1.000 113.123 ? 105 GLY LLL N   1 
ATOM   10806 C CA  . GLY H 3 105 ? -19.372 -23.766 26.560  1.000 114.034 ? 105 GLY LLL CA  1 
ATOM   10807 C C   . GLY H 3 105 ? -18.781 -24.973 27.264  1.000 113.069 ? 105 GLY LLL C   1 
ATOM   10808 O O   . GLY H 3 105 ? -19.229 -26.094 26.975  1.000 110.406 ? 105 GLY LLL O   1 
ATOM   10809 N N   . GLN H 3 106 ? -17.828 -24.758 28.173  1.000 115.592 ? 106 GLN LLL N   1 
ATOM   10810 C CA  . GLN H 3 106 ? -17.016 -25.834 28.809  1.000 117.853 ? 106 GLN LLL CA  1 
ATOM   10811 C C   . GLN H 3 106 ? -17.819 -26.557 29.902  1.000 113.545 ? 106 GLN LLL C   1 
ATOM   10812 O O   . GLN H 3 106 ? -17.329 -27.576 30.428  1.000 112.378 ? 106 GLN LLL O   1 
ATOM   10813 C CB  . GLN H 3 106 ? -15.705 -25.256 29.352  1.000 126.174 ? 106 GLN LLL CB  1 
ATOM   10814 C CG  . GLN H 3 106 ? -15.844 -24.381 30.598  1.000 130.956 ? 106 GLN LLL CG  1 
ATOM   10815 C CD  . GLN H 3 106 ? -16.298 -22.965 30.325  1.000 133.602 ? 106 GLN LLL CD  1 
ATOM   10816 O OE1 . GLN H 3 106 ? -16.215 -22.452 29.207  1.000 136.601 ? 106 GLN LLL OE1 1 
ATOM   10817 N NE2 . GLN H 3 106 ? -16.778 -22.309 31.370  1.000 133.954 ? 106 GLN LLL NE2 1 
ATOM   10818 N N   . GLY H 3 107 ? -19.012 -26.062 30.227  1.000 110.998 ? 107 GLY LLL N   1 
ATOM   10819 C CA  . GLY H 3 107 ? -19.913 -26.679 31.212  1.000 111.497 ? 107 GLY LLL CA  1 
ATOM   10820 C C   . GLY H 3 107 ? -19.766 -26.019 32.571  1.000 116.218 ? 107 GLY LLL C   1 
ATOM   10821 O O   . GLY H 3 107 ? -18.717 -25.394 32.816  1.000 118.836 ? 107 GLY LLL O   1 
ATOM   10822 N N   . THR H 3 108 ? -20.792 -26.152 33.417  1.000 118.458 ? 108 THR LLL N   1 
ATOM   10823 C CA  . THR H 3 108 ? -20.839 -25.667 34.824  1.000 120.196 ? 108 THR LLL CA  1 
ATOM   10824 C C   . THR H 3 108 ? -21.403 -26.778 35.721  1.000 121.756 ? 108 THR LLL C   1 
ATOM   10825 O O   . THR H 3 108 ? -22.579 -27.155 35.515  1.000 121.865 ? 108 THR LLL O   1 
ATOM   10826 C CB  . THR H 3 108 ? -21.687 -24.396 34.934  1.000 119.305 ? 108 THR LLL CB  1 
ATOM   10827 O OG1 . THR H 3 108 ? -21.163 -23.435 34.021  1.000 118.223 ? 108 THR LLL OG1 1 
ATOM   10828 C CG2 . THR H 3 108 ? -21.708 -23.826 36.334  1.000 122.891 ? 108 THR LLL CG2 1 
ATOM   10829 N N   . LYS H 3 109 ? -20.609 -27.303 36.665  1.000 123.367 ? 109 LYS LLL N   1 
ATOM   10830 C CA  . LYS H 3 109 ? -21.110 -28.267 37.683  1.000 122.510 ? 109 LYS LLL CA  1 
ATOM   10831 C C   . LYS H 3 109 ? -21.893 -27.437 38.706  1.000 123.634 ? 109 LYS LLL C   1 
ATOM   10832 O O   . LYS H 3 109 ? -21.386 -26.366 39.106  1.000 123.763 ? 109 LYS LLL O   1 
ATOM   10833 C CB  . LYS H 3 109 ? -19.981 -29.116 38.288  1.000 123.295 ? 109 LYS LLL CB  1 
ATOM   10834 C CG  . LYS H 3 109 ? -20.425 -30.299 39.152  1.000 123.184 ? 109 LYS LLL CG  1 
ATOM   10835 C CD  . LYS H 3 109 ? -21.048 -31.479 38.398  1.000 121.345 ? 109 LYS LLL CD  1 
ATOM   10836 C CE  . LYS H 3 109 ? -21.973 -32.359 39.232  1.000 121.083 ? 109 LYS LLL CE  1 
ATOM   10837 N NZ  . LYS H 3 109 ? -22.802 -33.279 38.401  1.000 117.080 ? 109 LYS LLL NZ  1 
ATOM   10838 N N   . VAL H 3 110 ? -23.119 -27.869 39.021  1.000 123.170 ? 110 VAL LLL N   1 
ATOM   10839 C CA  . VAL H 3 110 ? -23.992 -27.264 40.068  1.000 127.002 ? 110 VAL LLL CA  1 
ATOM   10840 C C   . VAL H 3 110 ? -24.303 -28.347 41.099  1.000 130.003 ? 110 VAL LLL C   1 
ATOM   10841 O O   . VAL H 3 110 ? -24.925 -29.355 40.725  1.000 126.878 ? 110 VAL LLL O   1 
ATOM   10842 C CB  . VAL H 3 110 ? -25.276 -26.651 39.482  1.000 125.537 ? 110 VAL LLL CB  1 
ATOM   10843 C CG1 . VAL H 3 110 ? -26.283 -26.271 40.562  1.000 128.334 ? 110 VAL LLL CG1 1 
ATOM   10844 C CG2 . VAL H 3 110 ? -24.948 -25.448 38.623  1.000 125.291 ? 110 VAL LLL CG2 1 
ATOM   10845 N N   . GLU H 3 111 ? -23.873 -28.117 42.343  1.000 134.767 ? 111 GLU LLL N   1 
ATOM   10846 C CA  . GLU H 3 111 ? -24.008 -29.059 43.479  1.000 137.103 ? 111 GLU LLL CA  1 
ATOM   10847 C C   . GLU H 3 111 ? -24.694 -28.331 44.644  1.000 138.239 ? 111 GLU LLL C   1 
ATOM   10848 O O   . GLU H 3 111 ? -24.678 -27.082 44.668  1.000 138.015 ? 111 GLU LLL O   1 
ATOM   10849 C CB  . GLU H 3 111 ? -22.628 -29.642 43.803  1.000 141.230 ? 111 GLU LLL CB  1 
ATOM   10850 C CG  . GLU H 3 111 ? -22.064 -30.500 42.673  1.000 141.102 ? 111 GLU LLL CG  1 
ATOM   10851 C CD  . GLU H 3 111 ? -21.027 -31.551 43.052  1.000 145.415 ? 111 GLU LLL CD  1 
ATOM   10852 O OE1 . GLU H 3 111 ? -19.909 -31.167 43.498  1.000 145.919 ? 111 GLU LLL OE1 1 
ATOM   10853 O OE2 . GLU H 3 111 ? -21.327 -32.762 42.877  1.000 147.234 ? 111 GLU LLL OE2 1 
ATOM   10854 N N   . ILE H 3 112 ? -25.312 -29.102 45.543  1.000 138.983 ? 112 ILE LLL N   1 
ATOM   10855 C CA  . ILE H 3 112 ? -26.126 -28.625 46.702  1.000 142.781 ? 112 ILE LLL CA  1 
ATOM   10856 C C   . ILE H 3 112 ? -25.202 -28.337 47.882  1.000 146.102 ? 112 ILE LLL C   1 
ATOM   10857 O O   . ILE H 3 112 ? -24.679 -29.306 48.465  1.000 146.675 ? 112 ILE LLL O   1 
ATOM   10858 C CB  . ILE H 3 112 ? -27.172 -29.681 47.106  1.000 145.462 ? 112 ILE LLL CB  1 
ATOM   10859 C CG1 . ILE H 3 112 ? -28.217 -29.908 46.010  1.000 143.596 ? 112 ILE LLL CG1 1 
ATOM   10860 C CG2 . ILE H 3 112 ? -27.799 -29.331 48.452  1.000 150.710 ? 112 ILE LLL CG2 1 
ATOM   10861 C CD1 . ILE H 3 112 ? -29.221 -28.786 45.856  1.000 144.971 ? 112 ILE LLL CD1 1 
ATOM   10862 N N   . LYS H 3 113 ? -25.055 -27.065 48.252  1.000 149.439 ? 113 LYS LLL N   1 
ATOM   10863 C CA  . LYS H 3 113 ? -24.322 -26.661 49.479  1.000 155.854 ? 113 LYS LLL CA  1 
ATOM   10864 C C   . LYS H 3 113 ? -25.163 -27.079 50.683  1.000 159.411 ? 113 LYS LLL C   1 
ATOM   10865 O O   . LYS H 3 113 ? -26.353 -26.710 50.741  1.000 160.055 ? 113 LYS LLL O   1 
ATOM   10866 C CB  . LYS H 3 113 ? -24.048 -25.159 49.507  1.000 159.434 ? 113 LYS LLL CB  1 
ATOM   10867 C CG  . LYS H 3 113 ? -23.030 -24.708 50.539  1.000 165.753 ? 113 LYS LLL CG  1 
ATOM   10868 C CD  . LYS H 3 113 ? -22.618 -23.265 50.335  1.000 169.162 ? 113 LYS LLL CD  1 
ATOM   10869 C CE  . LYS H 3 113 ? -23.731 -22.273 50.610  1.000 172.662 ? 113 LYS LLL CE  1 
ATOM   10870 N NZ  . LYS H 3 113 ? -23.669 -21.103 49.700  1.000 172.420 ? 113 LYS LLL NZ  1 
ATOM   10871 N N   . ARG H 3 114 ? -24.561 -27.845 51.591  1.000 161.990 ? 114 ARG LLL N   1 
ATOM   10872 C CA  . ARG H 3 114 ? -25.253 -28.449 52.755  1.000 164.803 ? 114 ARG LLL CA  1 
ATOM   10873 C C   . ARG H 3 114 ? -24.432 -28.203 54.016  1.000 166.249 ? 114 ARG LLL C   1 
ATOM   10874 O O   . ARG H 3 114 ? -23.290 -27.721 53.913  1.000 164.426 ? 114 ARG LLL O   1 
ATOM   10875 C CB  . ARG H 3 114 ? -25.455 -29.950 52.534  1.000 165.007 ? 114 ARG LLL CB  1 
ATOM   10876 C CG  . ARG H 3 114 ? -24.166 -30.727 52.314  1.000 164.746 ? 114 ARG LLL CG  1 
ATOM   10877 C CD  . ARG H 3 114 ? -24.288 -32.133 52.857  1.000 166.268 ? 114 ARG LLL CD  1 
ATOM   10878 N NE  . ARG H 3 114 ? -24.296 -32.135 54.314  1.000 171.868 ? 114 ARG LLL NE  1 
ATOM   10879 C CZ  . ARG H 3 114 ? -24.631 -33.179 55.063  1.000 175.424 ? 114 ARG LLL CZ  1 
ATOM   10880 N NH1 . ARG H 3 114 ? -24.998 -34.316 54.492  1.000 173.208 ? 114 ARG LLL NH1 1 
ATOM   10881 N NH2 . ARG H 3 114 ? -24.602 -33.076 56.382  1.000 181.871 ? 114 ARG LLL NH2 1 
ATOM   10882 N N   . THR H 3 115 ? -25.010 -28.563 55.155  1.000 161.910 ? 115 THR LLL N   1 
ATOM   10883 C CA  . THR H 3 115 ? -24.363 -28.509 56.487  1.000 164.315 ? 115 THR LLL CA  1 
ATOM   10884 C C   . THR H 3 115 ? -22.999 -29.205 56.387  1.000 157.896 ? 115 THR LLL C   1 
ATOM   10885 O O   . THR H 3 115 ? -22.919 -30.248 55.710  1.000 151.089 ? 115 THR LLL O   1 
ATOM   10886 C CB  . THR H 3 115 ? -25.282 -29.141 57.538  1.000 170.400 ? 115 THR LLL CB  1 
ATOM   10887 O OG1 . THR H 3 115 ? -25.188 -30.558 57.387  1.000 168.717 ? 115 THR LLL OG1 1 
ATOM   10888 C CG2 . THR H 3 115 ? -26.722 -28.687 57.409  1.000 174.829 ? 115 THR LLL CG2 1 
ATOM   10889 N N   . VAL H 3 116 ? -21.967 -28.635 57.019  1.000 158.441 ? 116 VAL LLL N   1 
ATOM   10890 C CA  . VAL H 3 116 ? -20.601 -29.237 57.119  1.000 155.043 ? 116 VAL LLL CA  1 
ATOM   10891 C C   . VAL H 3 116 ? -20.770 -30.660 57.659  1.000 154.844 ? 116 VAL LLL C   1 
ATOM   10892 O O   . VAL H 3 116 ? -21.756 -30.896 58.378  1.000 162.607 ? 116 VAL LLL O   1 
ATOM   10893 C CB  . VAL H 3 116 ? -19.660 -28.415 58.023  1.000 157.673 ? 116 VAL LLL CB  1 
ATOM   10894 C CG1 . VAL H 3 116 ? -18.215 -28.886 57.903  1.000 153.986 ? 116 VAL LLL CG1 1 
ATOM   10895 C CG2 . VAL H 3 116 ? -19.761 -26.916 57.758  1.000 159.773 ? 116 VAL LLL CG2 1 
ATOM   10896 N N   . ALA H 3 117 ? -19.859 -31.576 57.331  1.000 150.145 ? 117 ALA LLL N   1 
ATOM   10897 C CA  . ALA H 3 117 ? -19.938 -32.992 57.760  1.000 151.559 ? 117 ALA LLL CA  1 
ATOM   10898 C C   . ALA H 3 117 ? -18.568 -33.668 57.647  1.000 150.425 ? 117 ALA LLL C   1 
ATOM   10899 O O   . ALA H 3 117 ? -18.005 -33.686 56.538  1.000 148.820 ? 117 ALA LLL O   1 
ATOM   10900 C CB  . ALA H 3 117 ? -20.974 -33.711 56.939  1.000 149.845 ? 117 ALA LLL CB  1 
ATOM   10901 N N   . ALA H 3 118 ? -18.074 -34.222 58.759  1.000 154.350 ? 118 ALA LLL N   1 
ATOM   10902 C CA  . ALA H 3 118 ? -16.740 -34.857 58.872  1.000 151.425 ? 118 ALA LLL CA  1 
ATOM   10903 C C   . ALA H 3 118 ? -16.795 -36.266 58.290  1.000 147.668 ? 118 ALA LLL C   1 
ATOM   10904 O O   . ALA H 3 118 ? -17.852 -36.896 58.261  1.000 147.603 ? 118 ALA LLL O   1 
ATOM   10905 C CB  . ALA H 3 118 ? -16.281 -34.869 60.310  1.000 156.802 ? 118 ALA LLL CB  1 
ATOM   10906 N N   . PRO H 3 119 ? -15.649 -36.796 57.811  1.000 144.829 ? 119 PRO LLL N   1 
ATOM   10907 C CA  . PRO H 3 119 ? -15.610 -38.083 57.120  1.000 143.327 ? 119 PRO LLL CA  1 
ATOM   10908 C C   . PRO H 3 119 ? -15.279 -39.275 58.026  1.000 145.088 ? 119 PRO LLL C   1 
ATOM   10909 O O   . PRO H 3 119 ? -14.392 -39.151 58.848  1.000 144.594 ? 119 PRO LLL O   1 
ATOM   10910 C CB  . PRO H 3 119 ? -14.470 -37.862 56.118  1.000 140.061 ? 119 PRO LLL CB  1 
ATOM   10911 C CG  . PRO H 3 119 ? -13.511 -36.921 56.836  1.000 141.873 ? 119 PRO LLL CG  1 
ATOM   10912 C CD  . PRO H 3 119 ? -14.321 -36.170 57.876  1.000 144.931 ? 119 PRO LLL CD  1 
ATOM   10913 N N   . SER H 3 120 ? -15.986 -40.392 57.825  1.000 148.015 ? 120 SER LLL N   1 
ATOM   10914 C CA  . SER H 3 120 ? -15.763 -41.694 58.510  1.000 151.876 ? 120 SER LLL CA  1 
ATOM   10915 C C   . SER H 3 120 ? -14.591 -42.425 57.840  1.000 147.696 ? 120 SER LLL C   1 
ATOM   10916 O O   . SER H 3 120 ? -14.821 -43.104 56.818  1.000 147.520 ? 120 SER LLL O   1 
ATOM   10917 C CB  . SER H 3 120 ? -17.021 -42.544 58.498  1.000 156.035 ? 120 SER LLL CB  1 
ATOM   10918 O OG  . SER H 3 120 ? -18.117 -41.877 59.118  1.000 160.585 ? 120 SER LLL OG  1 
ATOM   10919 N N   . VAL H 3 121 ? -13.383 -42.305 58.397  1.000 145.333 ? 121 VAL LLL N   1 
ATOM   10920 C CA  . VAL H 3 121 ? -12.147 -42.895 57.809  1.000 140.641 ? 121 VAL LLL CA  1 
ATOM   10921 C C   . VAL H 3 121 ? -12.056 -44.375 58.177  1.000 143.122 ? 121 VAL LLL C   1 
ATOM   10922 O O   . VAL H 3 121 ? -12.388 -44.748 59.314  1.000 147.473 ? 121 VAL LLL O   1 
ATOM   10923 C CB  . VAL H 3 121 ? -10.871 -42.159 58.243  1.000 139.258 ? 121 VAL LLL CB  1 
ATOM   10924 C CG1 . VAL H 3 121 ? -9.634  -42.834 57.672  1.000 136.653 ? 121 VAL LLL CG1 1 
ATOM   10925 C CG2 . VAL H 3 121 ? -10.912 -40.688 57.861  1.000 138.518 ? 121 VAL LLL CG2 1 
ATOM   10926 N N   . PHE H 3 122 ? -11.593 -45.160 57.214  1.000 142.858 ? 122 PHE LLL N   1 
ATOM   10927 C CA  . PHE H 3 122 ? -11.304 -46.607 57.309  1.000 147.249 ? 122 PHE LLL CA  1 
ATOM   10928 C C   . PHE H 3 122 ? -10.045 -46.860 56.487  1.000 144.591 ? 122 PHE LLL C   1 
ATOM   10929 O O   . PHE H 3 122 ? -9.915  -46.251 55.409  1.000 142.900 ? 122 PHE LLL O   1 
ATOM   10930 C CB  . PHE H 3 122 ? -12.488 -47.416 56.778  1.000 150.841 ? 122 PHE LLL CB  1 
ATOM   10931 C CG  . PHE H 3 122 ? -13.565 -47.663 57.797  1.000 157.850 ? 122 PHE LLL CG  1 
ATOM   10932 C CD1 . PHE H 3 122 ? -13.358 -48.576 58.823  1.000 165.366 ? 122 PHE LLL CD1 1 
ATOM   10933 C CD2 . PHE H 3 122 ? -14.769 -46.981 57.737  1.000 158.568 ? 122 PHE LLL CD2 1 
ATOM   10934 C CE1 . PHE H 3 122 ? -14.344 -48.818 59.769  1.000 172.374 ? 122 PHE LLL CE1 1 
ATOM   10935 C CE2 . PHE H 3 122 ? -15.754 -47.220 58.684  1.000 167.355 ? 122 PHE LLL CE2 1 
ATOM   10936 C CZ  . PHE H 3 122 ? -15.540 -48.136 59.698  1.000 173.804 ? 122 PHE LLL CZ  1 
ATOM   10937 N N   . ILE H 3 123 ? -9.146  -47.711 56.973  1.000 146.619 ? 123 ILE LLL N   1 
ATOM   10938 C CA  . ILE H 3 123 ? -7.949  -48.145 56.195  1.000 146.245 ? 123 ILE LLL CA  1 
ATOM   10939 C C   . ILE H 3 123 ? -8.047  -49.652 55.941  1.000 147.742 ? 123 ILE LLL C   1 
ATOM   10940 O O   . ILE H 3 123 ? -8.642  -50.370 56.772  1.000 150.051 ? 123 ILE LLL O   1 
ATOM   10941 C CB  . ILE H 3 123 ? -6.644  -47.732 56.901  1.000 147.475 ? 123 ILE LLL CB  1 
ATOM   10942 C CG1 . ILE H 3 123 ? -5.466  -47.702 55.925  1.000 146.658 ? 123 ILE LLL CG1 1 
ATOM   10943 C CG2 . ILE H 3 123 ? -6.370  -48.618 58.103  1.000 151.555 ? 123 ILE LLL CG2 1 
ATOM   10944 C CD1 . ILE H 3 123 ? -4.229  -47.023 56.481  1.000 146.820 ? 123 ILE LLL CD1 1 
ATOM   10945 N N   . PHE H 3 124 ? -7.507  -50.093 54.805  1.000 147.191 ? 124 PHE LLL N   1 
ATOM   10946 C CA  . PHE H 3 124 ? -7.570  -51.495 54.324  1.000 149.807 ? 124 PHE LLL CA  1 
ATOM   10947 C C   . PHE H 3 124 ? -6.183  -51.953 53.902  1.000 149.398 ? 124 PHE LLL C   1 
ATOM   10948 O O   . PHE H 3 124 ? -5.575  -51.357 53.011  1.000 147.715 ? 124 PHE LLL O   1 
ATOM   10949 C CB  . PHE H 3 124 ? -8.537  -51.622 53.150  1.000 150.629 ? 124 PHE LLL CB  1 
ATOM   10950 C CG  . PHE H 3 124 ? -9.969  -51.365 53.529  1.000 153.933 ? 124 PHE LLL CG  1 
ATOM   10951 C CD1 . PHE H 3 124 ? -10.625 -52.217 54.402  1.000 159.428 ? 124 PHE LLL CD1 1 
ATOM   10952 C CD2 . PHE H 3 124 ? -10.655 -50.269 53.030  1.000 153.615 ? 124 PHE LLL CD2 1 
ATOM   10953 C CE1 . PHE H 3 124 ? -11.942 -51.981 54.765  1.000 163.520 ? 124 PHE LLL CE1 1 
ATOM   10954 C CE2 . PHE H 3 124 ? -11.972 -50.033 53.395  1.000 156.257 ? 124 PHE LLL CE2 1 
ATOM   10955 C CZ  . PHE H 3 124 ? -12.614 -50.889 54.260  1.000 161.073 ? 124 PHE LLL CZ  1 
ATOM   10956 N N   . PRO H 3 125 ? -5.653  -53.039 54.506  1.000 151.384 ? 125 PRO LLL N   1 
ATOM   10957 C CA  . PRO H 3 125 ? -4.379  -53.592 54.069  1.000 150.553 ? 125 PRO LLL CA  1 
ATOM   10958 C C   . PRO H 3 125 ? -4.582  -54.214 52.692  1.000 149.929 ? 125 PRO LLL C   1 
ATOM   10959 O O   . PRO H 3 125 ? -5.687  -54.213 52.151  1.000 149.785 ? 125 PRO LLL O   1 
ATOM   10960 C CB  . PRO H 3 125 ? -4.043  -54.627 55.152  1.000 153.835 ? 125 PRO LLL CB  1 
ATOM   10961 C CG  . PRO H 3 125 ? -5.394  -55.062 55.677  1.000 156.888 ? 125 PRO LLL CG  1 
ATOM   10962 C CD  . PRO H 3 125 ? -6.270  -53.829 55.585  1.000 154.596 ? 125 PRO LLL CD  1 
ATOM   10963 N N   . PRO H 3 126 ? -3.514  -54.731 52.059  1.000 149.984 ? 126 PRO LLL N   1 
ATOM   10964 C CA  . PRO H 3 126 ? -3.680  -55.586 50.891  1.000 151.165 ? 126 PRO LLL CA  1 
ATOM   10965 C C   . PRO H 3 126 ? -4.220  -56.964 51.311  1.000 151.663 ? 126 PRO LLL C   1 
ATOM   10966 O O   . PRO H 3 126 ? -4.087  -57.333 52.461  1.000 148.870 ? 126 PRO LLL O   1 
ATOM   10967 C CB  . PRO H 3 126 ? -2.271  -55.649 50.281  1.000 153.445 ? 126 PRO LLL CB  1 
ATOM   10968 C CG  . PRO H 3 126 ? -1.326  -55.346 51.437  1.000 152.978 ? 126 PRO LLL CG  1 
ATOM   10969 C CD  . PRO H 3 126 ? -2.110  -54.495 52.414  1.000 150.578 ? 126 PRO LLL CD  1 
ATOM   10970 N N   . SER H 3 127 ? -4.859  -57.659 50.368  1.000 152.963 ? 127 SER LLL N   1 
ATOM   10971 C CA  . SER H 3 127 ? -5.318  -59.064 50.492  1.000 156.715 ? 127 SER LLL CA  1 
ATOM   10972 C C   . SER H 3 127 ? -4.104  -59.985 50.387  1.000 158.135 ? 127 SER LLL C   1 
ATOM   10973 O O   . SER H 3 127 ? -3.105  -59.565 49.784  1.000 154.914 ? 127 SER LLL O   1 
ATOM   10974 C CB  . SER H 3 127 ? -6.328  -59.384 49.425  1.000 158.492 ? 127 SER LLL CB  1 
ATOM   10975 O OG  . SER H 3 127 ? -5.815  -59.051 48.143  1.000 156.558 ? 127 SER LLL OG  1 
ATOM   10976 N N   . ASP H 3 128 ? -4.190  -61.190 50.950  1.000 163.788 ? 128 ASP LLL N   1 
ATOM   10977 C CA  . ASP H 3 128 ? -3.176  -62.257 50.738  1.000 169.837 ? 128 ASP LLL CA  1 
ATOM   10978 C C   . ASP H 3 128 ? -3.173  -62.598 49.243  1.000 172.304 ? 128 ASP LLL C   1 
ATOM   10979 O O   . ASP H 3 128 ? -2.074  -62.658 48.646  1.000 172.786 ? 128 ASP LLL O   1 
ATOM   10980 C CB  . ASP H 3 128 ? -3.431  -63.483 51.628  1.000 176.011 ? 128 ASP LLL CB  1 
ATOM   10981 C CG  . ASP H 3 128 ? -2.477  -63.652 52.807  1.000 176.418 ? 128 ASP LLL CG  1 
ATOM   10982 O OD1 . ASP H 3 128 ? -1.686  -62.720 53.086  1.000 172.903 ? 128 ASP LLL OD1 1 
ATOM   10983 O OD2 . ASP H 3 128 ? -2.526  -64.726 53.440  1.000 180.528 ? 128 ASP LLL OD2 1 
ATOM   10984 N N   . GLU H 3 129 ? -4.364  -62.779 48.665  1.000 174.796 ? 129 GLU LLL N   1 
ATOM   10985 C CA  . GLU H 3 129 ? -4.564  -63.042 47.218  1.000 178.342 ? 129 GLU LLL CA  1 
ATOM   10986 C C   . GLU H 3 129 ? -3.664  -62.097 46.412  1.000 174.636 ? 129 GLU LLL C   1 
ATOM   10987 O O   . GLU H 3 129 ? -2.806  -62.606 45.665  1.000 178.185 ? 129 GLU LLL O   1 
ATOM   10988 C CB  . GLU H 3 129 ? -6.041  -62.876 46.867  1.000 180.858 ? 129 GLU LLL CB  1 
ATOM   10989 C CG  . GLU H 3 129 ? -6.417  -63.398 45.490  1.000 187.800 ? 129 GLU LLL CG  1 
ATOM   10990 C CD  . GLU H 3 129 ? -7.906  -63.316 45.181  1.000 191.953 ? 129 GLU LLL CD  1 
ATOM   10991 O OE1 . GLU H 3 129 ? -8.695  -63.352 46.145  1.000 193.959 ? 129 GLU LLL OE1 1 
ATOM   10992 O OE2 . GLU H 3 129 ? -8.282  -63.211 43.981  1.000 195.049 ? 129 GLU LLL OE2 1 
ATOM   10993 N N   . GLN H 3 130 ? -3.821  -60.779 46.599  1.000 168.436 ? 130 GLN LLL N   1 
ATOM   10994 C CA  . GLN H 3 130 ? -3.117  -59.726 45.814  1.000 164.942 ? 130 GLN LLL CA  1 
ATOM   10995 C C   . GLN H 3 130 ? -1.596  -59.845 45.971  1.000 167.482 ? 130 GLN LLL C   1 
ATOM   10996 O O   . GLN H 3 130 ? -0.889  -59.663 44.962  1.000 171.032 ? 130 GLN LLL O   1 
ATOM   10997 C CB  . GLN H 3 130 ? -3.540  -58.317 46.236  1.000 156.708 ? 130 GLN LLL CB  1 
ATOM   10998 C CG  . GLN H 3 130 ? -2.755  -57.231 45.511  1.000 151.880 ? 130 GLN LLL CG  1 
ATOM   10999 C CD  . GLN H 3 130 ? -3.277  -55.843 45.774  1.000 144.929 ? 130 GLN LLL CD  1 
ATOM   11000 O OE1 . GLN H 3 130 ? -4.100  -55.620 46.661  1.000 140.851 ? 130 GLN LLL OE1 1 
ATOM   11001 N NE2 . GLN H 3 130 ? -2.778  -54.895 44.999  1.000 140.806 ? 130 GLN LLL NE2 1 
ATOM   11002 N N   . LEU H 3 131 ? -1.109  -60.085 47.190  1.000 168.545 ? 131 LEU LLL N   1 
ATOM   11003 C CA  . LEU H 3 131 ? 0.346   -60.072 47.502  1.000 169.983 ? 131 LEU LLL CA  1 
ATOM   11004 C C   . LEU H 3 131 ? 1.067   -61.084 46.611  1.000 174.773 ? 131 LEU LLL C   1 
ATOM   11005 O O   . LEU H 3 131 ? 2.125   -60.724 46.054  1.000 175.344 ? 131 LEU LLL O   1 
ATOM   11006 C CB  . LEU H 3 131 ? 0.563   -60.390 48.982  1.000 171.043 ? 131 LEU LLL CB  1 
ATOM   11007 C CG  . LEU H 3 131 ? 0.300   -59.232 49.942  1.000 167.588 ? 131 LEU LLL CG  1 
ATOM   11008 C CD1 . LEU H 3 131 ? 0.217   -59.734 51.376  1.000 169.649 ? 131 LEU LLL CD1 1 
ATOM   11009 C CD2 . LEU H 3 131 ? 1.365   -58.148 49.810  1.000 165.282 ? 131 LEU LLL CD2 1 
ATOM   11010 N N   . LYS H 3 132 ? 0.499   -62.286 46.472  1.000 178.841 ? 132 LYS LLL N   1 
ATOM   11011 C CA  . LYS H 3 132 ? 1.072   -63.388 45.659  1.000 185.968 ? 132 LYS LLL CA  1 
ATOM   11012 C C   . LYS H 3 132 ? 1.195   -62.954 44.192  1.000 188.203 ? 132 LYS LLL C   1 
ATOM   11013 O O   . LYS H 3 132 ? 2.120   -63.455 43.519  1.000 192.391 ? 132 LYS LLL O   1 
ATOM   11014 C CB  . LYS H 3 132 ? 0.203   -64.642 45.770  1.000 191.290 ? 132 LYS LLL CB  1 
ATOM   11015 C CG  . LYS H 3 132 ? 0.216   -65.323 47.130  1.000 193.090 ? 132 LYS LLL CG  1 
ATOM   11016 C CD  . LYS H 3 132 ? -0.688  -66.540 47.191  1.000 199.284 ? 132 LYS LLL CD  1 
ATOM   11017 C CE  . LYS H 3 132 ? -2.162  -66.191 47.121  1.000 198.444 ? 132 LYS LLL CE  1 
ATOM   11018 N NZ  . LYS H 3 132 ? -3.004  -67.382 46.854  1.000 205.166 ? 132 LYS LLL NZ  1 
ATOM   11019 N N   . SER H 3 133 ? 0.300   -62.074 43.719  1.000 186.983 ? 133 SER LLL N   1 
ATOM   11020 C CA  . SER H 3 133 ? 0.247   -61.586 42.311  1.000 189.353 ? 133 SER LLL CA  1 
ATOM   11021 C C   . SER H 3 133 ? 1.545   -60.845 41.957  1.000 186.899 ? 133 SER LLL C   1 
ATOM   11022 O O   . SER H 3 133 ? 2.042   -61.041 40.825  1.000 192.306 ? 133 SER LLL O   1 
ATOM   11023 C CB  . SER H 3 133 ? -0.981  -60.726 42.045  1.000 188.119 ? 133 SER LLL CB  1 
ATOM   11024 O OG  . SER H 3 133 ? -0.757  -59.356 42.362  1.000 184.331 ? 133 SER LLL OG  1 
ATOM   11025 N N   . GLY H 3 134 ? 2.067   -60.028 42.882  1.000 178.440 ? 134 GLY LLL N   1 
ATOM   11026 C CA  . GLY H 3 134 ? 3.301   -59.242 42.690  1.000 174.706 ? 134 GLY LLL CA  1 
ATOM   11027 C C   . GLY H 3 134 ? 3.193   -57.859 43.302  1.000 167.486 ? 134 GLY LLL C   1 
ATOM   11028 O O   . GLY H 3 134 ? 4.148   -57.445 43.962  1.000 166.558 ? 134 GLY LLL O   1 
ATOM   11029 N N   . THR H 3 135 ? 2.078   -57.161 43.079  1.000 164.509 ? 135 THR LLL N   1 
ATOM   11030 C CA  . THR H 3 135 ? 1.790   -55.824 43.665  1.000 158.983 ? 135 THR LLL CA  1 
ATOM   11031 C C   . THR H 3 135 ? 1.130   -56.008 45.035  1.000 153.310 ? 135 THR LLL C   1 
ATOM   11032 O O   . THR H 3 135 ? 0.769   -57.147 45.387  1.000 152.911 ? 135 THR LLL O   1 
ATOM   11033 C CB  . THR H 3 135 ? 0.927   -54.950 42.740  1.000 159.889 ? 135 THR LLL CB  1 
ATOM   11034 O OG1 . THR H 3 135 ? -0.190  -55.715 42.275  1.000 163.167 ? 135 THR LLL OG1 1 
ATOM   11035 C CG2 . THR H 3 135 ? 1.707   -54.390 41.570  1.000 162.315 ? 135 THR LLL CG2 1 
ATOM   11036 N N   . ALA H 3 136 ? 1.016   -54.907 45.776  1.000 147.381 ? 136 ALA LLL N   1 
ATOM   11037 C CA  . ALA H 3 136 ? 0.317   -54.798 47.072  1.000 142.925 ? 136 ALA LLL CA  1 
ATOM   11038 C C   . ALA H 3 136 ? -0.340  -53.418 47.146  1.000 138.885 ? 136 ALA LLL C   1 
ATOM   11039 O O   . ALA H 3 136 ? 0.388   -52.410 47.076  1.000 138.756 ? 136 ALA LLL O   1 
ATOM   11040 C CB  . ALA H 3 136 ? 1.302   -55.000 48.188  1.000 142.383 ? 136 ALA LLL CB  1 
ATOM   11041 N N   . SER H 3 137 ? -1.666  -53.370 47.247  1.000 137.741 ? 137 SER LLL N   1 
ATOM   11042 C CA  . SER H 3 137 ? -2.452  -52.112 47.246  1.000 135.704 ? 137 SER LLL CA  1 
ATOM   11043 C C   . SER H 3 137 ? -3.015  -51.876 48.649  1.000 133.996 ? 137 SER LLL C   1 
ATOM   11044 O O   . SER H 3 137 ? -3.692  -52.776 49.197  1.000 134.949 ? 137 SER LLL O   1 
ATOM   11045 C CB  . SER H 3 137 ? -3.539  -52.130 46.201  1.000 136.632 ? 137 SER LLL CB  1 
ATOM   11046 O OG  . SER H 3 137 ? -2.991  -51.997 44.899  1.000 136.821 ? 137 SER LLL OG  1 
ATOM   11047 N N   . VAL H 3 138 ? -2.733  -50.697 49.198  1.000 131.697 ? 138 VAL LLL N   1 
ATOM   11048 C CA  . VAL H 3 138 ? -3.286  -50.228 50.496  1.000 131.597 ? 138 VAL LLL CA  1 
ATOM   11049 C C   . VAL H 3 138 ? -4.337  -49.161 50.202  1.000 130.250 ? 138 VAL LLL C   1 
ATOM   11050 O O   . VAL H 3 138 ? -3.967  -48.110 49.653  1.000 127.314 ? 138 VAL LLL O   1 
ATOM   11051 C CB  . VAL H 3 138 ? -2.175  -49.673 51.395  1.000 132.651 ? 138 VAL LLL CB  1 
ATOM   11052 C CG1 . VAL H 3 138 ? -2.703  -49.338 52.778  1.000 133.697 ? 138 VAL LLL CG1 1 
ATOM   11053 C CG2 . VAL H 3 138 ? -1.009  -50.638 51.478  1.000 135.804 ? 138 VAL LLL CG2 1 
ATOM   11054 N N   . VAL H 3 139 ? -5.592  -49.434 50.559  1.000 133.228 ? 139 VAL LLL N   1 
ATOM   11055 C CA  . VAL H 3 139 ? -6.738  -48.521 50.293  1.000 133.085 ? 139 VAL LLL CA  1 
ATOM   11056 C C   . VAL H 3 139 ? -7.104  -47.808 51.594  1.000 132.605 ? 139 VAL LLL C   1 
ATOM   11057 O O   . VAL H 3 139 ? -7.145  -48.449 52.659  1.000 130.824 ? 139 VAL LLL O   1 
ATOM   11058 C CB  . VAL H 3 139 ? -7.955  -49.259 49.709  1.000 135.554 ? 139 VAL LLL CB  1 
ATOM   11059 C CG1 . VAL H 3 139 ? -8.949  -48.273 49.107  1.000 134.247 ? 139 VAL LLL CG1 1 
ATOM   11060 C CG2 . VAL H 3 139 ? -7.546  -50.318 48.694  1.000 137.397 ? 139 VAL LLL CG2 1 
ATOM   11061 N N   . CYS H 3 140 ? -7.369  -46.513 51.477  1.000 133.343 ? 140 CYS LLL N   1 
ATOM   11062 C CA  . CYS H 3 140 ? -7.899  -45.646 52.549  1.000 135.047 ? 140 CYS LLL CA  1 
ATOM   11063 C C   . CYS H 3 140 ? -9.210  -45.033 52.058  1.000 135.309 ? 140 CYS LLL C   1 
ATOM   11064 O O   . CYS H 3 140 ? -9.257  -44.630 50.875  1.000 138.521 ? 140 CYS LLL O   1 
ATOM   11065 C CB  . CYS H 3 140 ? -6.897  -44.560 52.897  1.000 136.650 ? 140 CYS LLL CB  1 
ATOM   11066 S SG  . CYS H 3 140 ? -7.360  -43.660 54.395  1.000 142.778 ? 140 CYS LLL SG  1 
ATOM   11067 N N   . LEU H 3 141 ? -10.217 -44.977 52.932  1.000 134.521 ? 141 LEU LLL N   1 
ATOM   11068 C CA  . LEU H 3 141 ? -11.622 -44.647 52.580  1.000 133.579 ? 141 LEU LLL CA  1 
ATOM   11069 C C   . LEU H 3 141 ? -12.141 -43.543 53.507  1.000 133.865 ? 141 LEU LLL C   1 
ATOM   11070 O O   . LEU H 3 141 ? -12.192 -43.774 54.725  1.000 138.278 ? 141 LEU LLL O   1 
ATOM   11071 C CB  . LEU H 3 141 ? -12.446 -45.932 52.698  1.000 135.951 ? 141 LEU LLL CB  1 
ATOM   11072 C CG  . LEU H 3 141 ? -13.963 -45.764 52.765  1.000 138.606 ? 141 LEU LLL CG  1 
ATOM   11073 C CD1 . LEU H 3 141 ? -14.492 -45.060 51.530  1.000 137.392 ? 141 LEU LLL CD1 1 
ATOM   11074 C CD2 . LEU H 3 141 ? -14.646 -47.110 52.943  1.000 141.925 ? 141 LEU LLL CD2 1 
ATOM   11075 N N   . LEU H 3 142 ? -12.505 -42.390 52.939  1.000 133.348 ? 142 LEU LLL N   1 
ATOM   11076 C CA  . LEU H 3 142 ? -13.198 -41.271 53.636  1.000 136.551 ? 142 LEU LLL CA  1 
ATOM   11077 C C   . LEU H 3 142 ? -14.675 -41.303 53.241  1.000 139.829 ? 142 LEU LLL C   1 
ATOM   11078 O O   . LEU H 3 142 ? -14.984 -40.868 52.111  1.000 142.408 ? 142 LEU LLL O   1 
ATOM   11079 C CB  . LEU H 3 142 ? -12.579 -39.935 53.212  1.000 134.683 ? 142 LEU LLL CB  1 
ATOM   11080 C CG  . LEU H 3 142 ? -11.194 -39.629 53.770  1.000 134.629 ? 142 LEU LLL CG  1 
ATOM   11081 C CD1 . LEU H 3 142 ? -10.157 -40.627 53.270  1.000 133.747 ? 142 LEU LLL CD1 1 
ATOM   11082 C CD2 . LEU H 3 142 ? -10.793 -38.209 53.407  1.000 134.089 ? 142 LEU LLL CD2 1 
ATOM   11083 N N   . ASN H 3 143 ? -15.553 -41.792 54.119  1.000 141.734 ? 143 ASN LLL N   1 
ATOM   11084 C CA  . ASN H 3 143 ? -16.974 -42.038 53.765  1.000 142.357 ? 143 ASN LLL CA  1 
ATOM   11085 C C   . ASN H 3 143 ? -17.835 -40.860 54.224  1.000 142.493 ? 143 ASN LLL C   1 
ATOM   11086 O O   . ASN H 3 143 ? -17.626 -40.380 55.348  1.000 142.896 ? 143 ASN LLL O   1 
ATOM   11087 C CB  . ASN H 3 143 ? -17.489 -43.353 54.346  1.000 146.089 ? 143 ASN LLL CB  1 
ATOM   11088 C CG  . ASN H 3 143 ? -18.645 -43.906 53.544  1.000 148.708 ? 143 ASN LLL CG  1 
ATOM   11089 O OD1 . ASN H 3 143 ? -18.578 -43.964 52.319  1.000 145.186 ? 143 ASN LLL OD1 1 
ATOM   11090 N ND2 . ASN H 3 143 ? -19.707 -44.307 54.224  1.000 155.827 ? 143 ASN LLL ND2 1 
ATOM   11091 N N   . ASN H 3 144 ? -18.752 -40.419 53.356  1.000 142.210 ? 144 ASN LLL N   1 
ATOM   11092 C CA  . ASN H 3 144 ? -19.872 -39.488 53.661  1.000 144.512 ? 144 ASN LLL CA  1 
ATOM   11093 C C   . ASN H 3 144 ? -19.342 -38.234 54.359  1.000 142.791 ? 144 ASN LLL C   1 
ATOM   11094 O O   . ASN H 3 144 ? -19.264 -38.238 55.603  1.000 146.326 ? 144 ASN LLL O   1 
ATOM   11095 C CB  . ASN H 3 144 ? -20.951 -40.156 54.519  1.000 150.698 ? 144 ASN LLL CB  1 
ATOM   11096 C CG  . ASN H 3 144 ? -21.550 -41.386 53.871  1.000 152.708 ? 144 ASN LLL CG  1 
ATOM   11097 O OD1 . ASN H 3 144 ? -21.712 -42.412 54.524  1.000 158.629 ? 144 ASN LLL OD1 1 
ATOM   11098 N ND2 . ASN H 3 144 ? -21.871 -41.299 52.590  1.000 150.506 ? 144 ASN LLL ND2 1 
ATOM   11099 N N   . PHE H 3 145 ? -19.019 -37.195 53.589  1.000 139.062 ? 145 PHE LLL N   1 
ATOM   11100 C CA  . PHE H 3 145 ? -18.557 -35.892 54.130  1.000 140.163 ? 145 PHE LLL CA  1 
ATOM   11101 C C   . PHE H 3 145 ? -18.878 -34.751 53.163  1.000 138.613 ? 145 PHE LLL C   1 
ATOM   11102 O O   . PHE H 3 145 ? -19.095 -34.998 51.964  1.000 138.764 ? 145 PHE LLL O   1 
ATOM   11103 C CB  . PHE H 3 145 ? -17.059 -35.952 54.424  1.000 139.665 ? 145 PHE LLL CB  1 
ATOM   11104 C CG  . PHE H 3 145 ? -16.190 -36.146 53.209  1.000 137.326 ? 145 PHE LLL CG  1 
ATOM   11105 C CD1 . PHE H 3 145 ? -15.908 -37.414 52.729  1.000 135.341 ? 145 PHE LLL CD1 1 
ATOM   11106 C CD2 . PHE H 3 145 ? -15.654 -35.056 52.543  1.000 137.131 ? 145 PHE LLL CD2 1 
ATOM   11107 C CE1 . PHE H 3 145 ? -15.100 -37.586 51.616  1.000 131.899 ? 145 PHE LLL CE1 1 
ATOM   11108 C CE2 . PHE H 3 145 ? -14.860 -35.232 51.422  1.000 133.914 ? 145 PHE LLL CE2 1 
ATOM   11109 C CZ  . PHE H 3 145 ? -14.583 -36.497 50.962  1.000 131.515 ? 145 PHE LLL CZ  1 
ATOM   11110 N N   . TYR H 3 146 ? -18.897 -33.533 53.707  1.000 140.008 ? 146 TYR LLL N   1 
ATOM   11111 C CA  . TYR H 3 146 ? -19.015 -32.244 52.983  1.000 140.845 ? 146 TYR LLL CA  1 
ATOM   11112 C C   . TYR H 3 146 ? -18.246 -31.190 53.769  1.000 144.353 ? 146 TYR LLL C   1 
ATOM   11113 O O   . TYR H 3 146 ? -18.379 -31.132 54.986  1.000 151.319 ? 146 TYR LLL O   1 
ATOM   11114 C CB  . TYR H 3 146 ? -20.480 -31.828 52.827  1.000 143.621 ? 146 TYR LLL CB  1 
ATOM   11115 C CG  . TYR H 3 146 ? -20.649 -30.644 51.914  1.000 144.959 ? 146 TYR LLL CG  1 
ATOM   11116 C CD1 . TYR H 3 146 ? -20.682 -30.817 50.539  1.000 143.224 ? 146 TYR LLL CD1 1 
ATOM   11117 C CD2 . TYR H 3 146 ? -20.698 -29.351 52.413  1.000 147.886 ? 146 TYR LLL CD2 1 
ATOM   11118 C CE1 . TYR H 3 146 ? -20.784 -29.738 49.677  1.000 143.851 ? 146 TYR LLL CE1 1 
ATOM   11119 C CE2 . TYR H 3 146 ? -20.812 -28.261 51.565  1.000 149.198 ? 146 TYR LLL CE2 1 
ATOM   11120 C CZ  . TYR H 3 146 ? -20.854 -28.456 50.193  1.000 147.272 ? 146 TYR LLL CZ  1 
ATOM   11121 O OH  . TYR H 3 146 ? -20.963 -27.400 49.338  1.000 148.471 ? 146 TYR LLL OH  1 
ATOM   11122 N N   . PRO H 3 147 ? -17.452 -30.300 53.135  1.000 145.342 ? 147 PRO LLL N   1 
ATOM   11123 C CA  . PRO H 3 147 ? -17.375 -30.180 51.679  1.000 144.976 ? 147 PRO LLL CA  1 
ATOM   11124 C C   . PRO H 3 147 ? -16.392 -31.156 51.011  1.000 144.265 ? 147 PRO LLL C   1 
ATOM   11125 O O   . PRO H 3 147 ? -15.927 -32.067 51.672  1.000 143.946 ? 147 PRO LLL O   1 
ATOM   11126 C CB  . PRO H 3 147 ? -16.910 -28.726 51.521  1.000 147.159 ? 147 PRO LLL CB  1 
ATOM   11127 C CG  . PRO H 3 147 ? -15.985 -28.509 52.703  1.000 148.820 ? 147 PRO LLL CG  1 
ATOM   11128 C CD  . PRO H 3 147 ? -16.588 -29.328 53.824  1.000 148.852 ? 147 PRO LLL CD  1 
ATOM   11129 N N   . ARG H 3 148 ? -16.130 -30.943 49.717  1.000 144.935 ? 148 ARG LLL N   1 
ATOM   11130 C CA  . ARG H 3 148 ? -15.273 -31.799 48.852  1.000 144.631 ? 148 ARG LLL CA  1 
ATOM   11131 C C   . ARG H 3 148 ? -13.823 -31.776 49.346  1.000 145.817 ? 148 ARG LLL C   1 
ATOM   11132 O O   . ARG H 3 148 ? -13.228 -32.853 49.485  1.000 142.101 ? 148 ARG LLL O   1 
ATOM   11133 C CB  . ARG H 3 148 ? -15.338 -31.279 47.415  1.000 146.874 ? 148 ARG LLL CB  1 
ATOM   11134 C CG  . ARG H 3 148 ? -15.052 -32.321 46.343  1.000 147.154 ? 148 ARG LLL CG  1 
ATOM   11135 C CD  . ARG H 3 148 ? -15.683 -31.912 45.020  1.000 150.859 ? 148 ARG LLL CD  1 
ATOM   11136 N NE  . ARG H 3 148 ? -16.108 -33.041 44.202  1.000 151.637 ? 148 ARG LLL NE  1 
ATOM   11137 C CZ  . ARG H 3 148 ? -15.299 -33.810 43.483  1.000 153.931 ? 148 ARG LLL CZ  1 
ATOM   11138 N NH1 . ARG H 3 148 ? -13.994 -33.582 43.473  1.000 155.478 ? 148 ARG LLL NH1 1 
ATOM   11139 N NH2 . ARG H 3 148 ? -15.801 -34.810 42.779  1.000 154.329 ? 148 ARG LLL NH2 1 
ATOM   11140 N N   . GLU H 3 149 ? -13.291 -30.577 49.596  1.000 151.849 ? 149 GLU LLL N   1 
ATOM   11141 C CA  . GLU H 3 149 ? -11.847 -30.321 49.853  1.000 154.766 ? 149 GLU LLL CA  1 
ATOM   11142 C C   . GLU H 3 149 ? -11.448 -31.046 51.139  1.000 151.488 ? 149 GLU LLL C   1 
ATOM   11143 O O   . GLU H 3 149 ? -11.609 -30.463 52.234  1.000 153.469 ? 149 GLU LLL O   1 
ATOM   11144 C CB  . GLU H 3 149 ? -11.538 -28.823 49.938  1.000 163.378 ? 149 GLU LLL CB  1 
ATOM   11145 C CG  . GLU H 3 149 ? -12.170 -27.997 48.827  1.000 169.459 ? 149 GLU LLL CG  1 
ATOM   11146 C CD  . GLU H 3 149 ? -13.564 -27.466 49.138  1.000 175.160 ? 149 GLU LLL CD  1 
ATOM   11147 O OE1 . GLU H 3 149 ? -13.663 -26.540 49.976  1.000 182.883 ? 149 GLU LLL OE1 1 
ATOM   11148 O OE2 . GLU H 3 149 ? -14.555 -27.989 48.561  1.000 175.165 ? 149 GLU LLL OE2 1 
ATOM   11149 N N   . ALA H 3 150 ? -10.982 -32.285 50.989  1.000 146.172 ? 150 ALA LLL N   1 
ATOM   11150 C CA  . ALA H 3 150 ? -10.409 -33.124 52.062  1.000 144.432 ? 150 ALA LLL CA  1 
ATOM   11151 C C   . ALA H 3 150 ? -8.978  -33.509 51.677  1.000 141.528 ? 150 ALA LLL C   1 
ATOM   11152 O O   . ALA H 3 150 ? -8.803  -34.066 50.583  1.000 139.535 ? 150 ALA LLL O   1 
ATOM   11153 C CB  . ALA H 3 150 ? -11.275 -34.339 52.271  1.000 143.260 ? 150 ALA LLL CB  1 
ATOM   11154 N N   . LYS H 3 151 ? -8.003  -33.194 52.532  1.000 142.784 ? 151 LYS LLL N   1 
ATOM   11155 C CA  . LYS H 3 151 ? -6.578  -33.576 52.354  1.000 142.733 ? 151 LYS LLL CA  1 
ATOM   11156 C C   . LYS H 3 151 ? -6.371  -34.974 52.946  1.000 138.010 ? 151 LYS LLL C   1 
ATOM   11157 O O   . LYS H 3 151 ? -6.671  -35.165 54.137  1.000 138.737 ? 151 LYS LLL O   1 
ATOM   11158 C CB  . LYS H 3 151 ? -5.648  -32.547 53.009  1.000 149.140 ? 151 LYS LLL CB  1 
ATOM   11159 C CG  . LYS H 3 151 ? -4.168  -32.908 52.983  1.000 151.948 ? 151 LYS LLL CG  1 
ATOM   11160 C CD  . LYS H 3 151 ? -3.247  -31.756 53.338  1.000 157.905 ? 151 LYS LLL CD  1 
ATOM   11161 C CE  . LYS H 3 151 ? -1.781  -32.112 53.192  1.000 160.355 ? 151 LYS LLL CE  1 
ATOM   11162 N NZ  . LYS H 3 151 ? -0.898  -30.934 53.388  1.000 165.830 ? 151 LYS LLL NZ  1 
ATOM   11163 N N   . VAL H 3 152 ? -5.911  -35.914 52.121  1.000 133.153 ? 152 VAL LLL N   1 
ATOM   11164 C CA  . VAL H 3 152 ? -5.441  -37.266 52.535  1.000 130.396 ? 152 VAL LLL CA  1 
ATOM   11165 C C   . VAL H 3 152 ? -3.938  -37.311 52.279  1.000 133.487 ? 152 VAL LLL C   1 
ATOM   11166 O O   . VAL H 3 152 ? -3.529  -36.917 51.163  1.000 134.837 ? 152 VAL LLL O   1 
ATOM   11167 C CB  . VAL H 3 152 ? -6.161  -38.377 51.752  1.000 126.278 ? 152 VAL LLL CB  1 
ATOM   11168 C CG1 . VAL H 3 152 ? -5.604  -39.756 52.068  1.000 124.303 ? 152 VAL LLL CG1 1 
ATOM   11169 C CG2 . VAL H 3 152 ? -7.657  -38.338 51.992  1.000 126.588 ? 152 VAL LLL CG2 1 
ATOM   11170 N N   . GLN H 3 153 ? -3.152  -37.754 53.266  1.000 136.077 ? 153 GLN LLL N   1 
ATOM   11171 C CA  . GLN H 3 153 ? -1.702  -38.031 53.087  1.000 138.012 ? 153 GLN LLL CA  1 
ATOM   11172 C C   . GLN H 3 153 ? -1.334  -39.378 53.715  1.000 135.099 ? 153 GLN LLL C   1 
ATOM   11173 O O   . GLN H 3 153 ? -1.845  -39.692 54.804  1.000 135.890 ? 153 GLN LLL O   1 
ATOM   11174 C CB  . GLN H 3 153 ? -0.821  -36.924 53.665  1.000 143.455 ? 153 GLN LLL CB  1 
ATOM   11175 C CG  . GLN H 3 153 ? 0.651   -37.159 53.347  1.000 147.323 ? 153 GLN LLL CG  1 
ATOM   11176 C CD  . GLN H 3 153 ? 1.406   -35.920 52.944  1.000 152.264 ? 153 GLN LLL CD  1 
ATOM   11177 O OE1 . GLN H 3 153 ? 1.068   -34.804 53.335  1.000 157.256 ? 153 GLN LLL OE1 1 
ATOM   11178 N NE2 . GLN H 3 153 ? 2.444   -36.118 52.145  1.000 152.694 ? 153 GLN LLL NE2 1 
ATOM   11179 N N   . TRP H 3 154 ? -0.460  -40.122 53.032  1.000 132.586 ? 154 TRP LLL N   1 
ATOM   11180 C CA  . TRP H 3 154 ? 0.099   -41.420 53.478  1.000 131.990 ? 154 TRP LLL CA  1 
ATOM   11181 C C   . TRP H 3 154 ? 1.385   -41.190 54.273  1.000 135.403 ? 154 TRP LLL C   1 
ATOM   11182 O O   . TRP H 3 154 ? 2.207   -40.347 53.866  1.000 137.219 ? 154 TRP LLL O   1 
ATOM   11183 C CB  . TRP H 3 154 ? 0.355   -42.331 52.279  1.000 130.230 ? 154 TRP LLL CB  1 
ATOM   11184 C CG  . TRP H 3 154 ? -0.907  -42.753 51.602  1.000 127.818 ? 154 TRP LLL CG  1 
ATOM   11185 C CD1 . TRP H 3 154 ? -1.546  -42.107 50.588  1.000 128.939 ? 154 TRP LLL CD1 1 
ATOM   11186 C CD2 . TRP H 3 154 ? -1.702  -43.906 51.906  1.000 125.603 ? 154 TRP LLL CD2 1 
ATOM   11187 N NE1 . TRP H 3 154 ? -2.676  -42.789 50.232  1.000 127.563 ? 154 TRP LLL NE1 1 
ATOM   11188 C CE2 . TRP H 3 154 ? -2.801  -43.893 51.026  1.000 125.455 ? 154 TRP LLL CE2 1 
ATOM   11189 C CE3 . TRP H 3 154 ? -1.593  -44.947 52.828  1.000 127.541 ? 154 TRP LLL CE3 1 
ATOM   11190 C CZ2 . TRP H 3 154 ? -3.779  -44.883 51.037  1.000 126.085 ? 154 TRP LLL CZ2 1 
ATOM   11191 C CZ3 . TRP H 3 154 ? -2.561  -45.927 52.841  1.000 128.291 ? 154 TRP LLL CZ3 1 
ATOM   11192 C CH2 . TRP H 3 154 ? -3.640  -45.893 51.958  1.000 127.390 ? 154 TRP LLL CH2 1 
ATOM   11193 N N   . LYS H 3 155 ? 1.522   -41.915 55.382  1.000 136.568 ? 155 LYS LLL N   1 
ATOM   11194 C CA  . LYS H 3 155 ? 2.807   -42.146 56.086  1.000 139.706 ? 155 LYS LLL CA  1 
ATOM   11195 C C   . LYS H 3 155 ? 3.128   -43.632 55.954  1.000 138.043 ? 155 LYS LLL C   1 
ATOM   11196 O O   . LYS H 3 155 ? 2.202   -44.449 56.091  1.000 136.482 ? 155 LYS LLL O   1 
ATOM   11197 C CB  . LYS H 3 155 ? 2.741   -41.734 57.561  1.000 144.319 ? 155 LYS LLL CB  1 
ATOM   11198 C CG  . LYS H 3 155 ? 2.089   -40.382 57.814  1.000 147.235 ? 155 LYS LLL CG  1 
ATOM   11199 C CD  . LYS H 3 155 ? 2.248   -39.840 59.216  1.000 152.991 ? 155 LYS LLL CD  1 
ATOM   11200 C CE  . LYS H 3 155 ? 1.551   -38.502 59.378  1.000 155.458 ? 155 LYS LLL CE  1 
ATOM   11201 N NZ  . LYS H 3 155 ? 1.959   -37.792 60.615  1.000 161.724 ? 155 LYS LLL NZ  1 
ATOM   11202 N N   . VAL H 3 156 ? 4.385   -43.945 55.663  1.000 139.878 ? 156 VAL LLL N   1 
ATOM   11203 C CA  . VAL H 3 156 ? 4.935   -45.326 55.738  1.000 140.641 ? 156 VAL LLL CA  1 
ATOM   11204 C C   . VAL H 3 156 ? 6.150   -45.260 56.663  1.000 145.414 ? 156 VAL LLL C   1 
ATOM   11205 O O   . VAL H 3 156 ? 7.170   -44.669 56.261  1.000 147.000 ? 156 VAL LLL O   1 
ATOM   11206 C CB  . VAL H 3 156 ? 5.264   -45.872 54.337  1.000 138.591 ? 156 VAL LLL CB  1 
ATOM   11207 C CG1 . VAL H 3 156 ? 6.046   -47.178 54.386  1.000 139.806 ? 156 VAL LLL CG1 1 
ATOM   11208 C CG2 . VAL H 3 156 ? 3.996   -46.034 53.518  1.000 134.921 ? 156 VAL LLL CG2 1 
ATOM   11209 N N   . ASP H 3 157 ? 6.017   -45.799 57.875  1.000 148.161 ? 157 ASP LLL N   1 
ATOM   11210 C CA  . ASP H 3 157 ? 7.035   -45.672 58.950  1.000 153.606 ? 157 ASP LLL CA  1 
ATOM   11211 C C   . ASP H 3 157 ? 7.148   -44.182 59.309  1.000 155.458 ? 157 ASP LLL C   1 
ATOM   11212 O O   . ASP H 3 157 ? 8.273   -43.644 59.269  1.000 156.518 ? 157 ASP LLL O   1 
ATOM   11213 C CB  . ASP H 3 157 ? 8.364   -46.318 58.529  1.000 156.131 ? 157 ASP LLL CB  1 
ATOM   11214 C CG  . ASP H 3 157 ? 8.246   -47.763 58.056  1.000 155.123 ? 157 ASP LLL CG  1 
ATOM   11215 O OD1 . ASP H 3 157 ? 7.242   -48.419 58.419  1.000 153.916 ? 157 ASP LLL OD1 1 
ATOM   11216 O OD2 . ASP H 3 157 ? 9.162   -48.227 57.333  1.000 154.829 ? 157 ASP LLL OD2 1 
ATOM   11217 N N   . ASN H 3 158 ? 6.009   -43.552 59.634  1.000 155.778 ? 158 ASN LLL N   1 
ATOM   11218 C CA  . ASN H 3 158 ? 5.882   -42.115 60.010  1.000 158.055 ? 158 ASN LLL CA  1 
ATOM   11219 C C   . ASN H 3 158 ? 6.850   -41.299 59.149  1.000 157.710 ? 158 ASN LLL C   1 
ATOM   11220 O O   . ASN H 3 158 ? 7.705   -40.563 59.706  1.000 161.389 ? 158 ASN LLL O   1 
ATOM   11221 C CB  . ASN H 3 158 ? 6.088   -41.891 61.513  1.000 163.597 ? 158 ASN LLL CB  1 
ATOM   11222 C CG  . ASN H 3 158 ? 4.859   -42.214 62.343  1.000 163.936 ? 158 ASN LLL CG  1 
ATOM   11223 O OD1 . ASN H 3 158 ? 3.721   -42.117 61.872  1.000 159.979 ? 158 ASN LLL OD1 1 
ATOM   11224 N ND2 . ASN H 3 158 ? 5.077   -42.588 63.594  1.000 167.105 ? 158 ASN LLL ND2 1 
ATOM   11225 N N   . ALA H 3 159 ? 6.717   -41.480 57.833  1.000 152.889 ? 159 ALA LLL N   1 
ATOM   11226 C CA  . ALA H 3 159 ? 7.427   -40.741 56.766  1.000 152.395 ? 159 ALA LLL CA  1 
ATOM   11227 C C   . ALA H 3 159 ? 6.462   -40.567 55.595  1.000 147.885 ? 159 ALA LLL C   1 
ATOM   11228 O O   . ALA H 3 159 ? 6.023   -41.587 55.035  1.000 145.259 ? 159 ALA LLL O   1 
ATOM   11229 C CB  . ALA H 3 159 ? 8.665   -41.490 56.357  1.000 153.700 ? 159 ALA LLL CB  1 
ATOM   11230 N N   . LEU H 3 160 ? 6.120   -39.323 55.256  1.000 147.872 ? 160 LEU LLL N   1 
ATOM   11231 C CA  . LEU H 3 160 ? 5.084   -39.021 54.238  1.000 145.009 ? 160 LEU LLL CA  1 
ATOM   11232 C C   . LEU H 3 160 ? 5.511   -39.622 52.903  1.000 143.699 ? 160 LEU LLL C   1 
ATOM   11233 O O   . LEU H 3 160 ? 6.626   -39.323 52.443  1.000 148.414 ? 160 LEU LLL O   1 
ATOM   11234 C CB  . LEU H 3 160 ? 4.912   -37.510 54.091  1.000 147.710 ? 160 LEU LLL CB  1 
ATOM   11235 C CG  . LEU H 3 160 ? 4.494   -36.751 55.345  1.000 149.656 ? 160 LEU LLL CG  1 
ATOM   11236 C CD1 . LEU H 3 160 ? 4.449   -35.258 55.066  1.000 152.889 ? 160 LEU LLL CD1 1 
ATOM   11237 C CD2 . LEU H 3 160 ? 3.151   -37.236 55.854  1.000 146.527 ? 160 LEU LLL CD2 1 
ATOM   11238 N N   . GLN H 3 161 ? 4.650   -40.448 52.319  1.000 139.666 ? 161 GLN LLL N   1 
ATOM   11239 C CA  . GLN H 3 161 ? 4.742   -40.860 50.899  1.000 140.405 ? 161 GLN LLL CA  1 
ATOM   11240 C C   . GLN H 3 161 ? 3.914   -39.850 50.089  1.000 140.761 ? 161 GLN LLL C   1 
ATOM   11241 O O   . GLN H 3 161 ? 2.947   -39.268 50.648  1.000 137.217 ? 161 GLN LLL O   1 
ATOM   11242 C CB  . GLN H 3 161 ? 4.289   -42.317 50.760  1.000 138.457 ? 161 GLN LLL CB  1 
ATOM   11243 C CG  . GLN H 3 161 ? 5.173   -43.327 51.496  1.000 139.436 ? 161 GLN LLL CG  1 
ATOM   11244 C CD  . GLN H 3 161 ? 6.442   -43.674 50.751  1.000 141.929 ? 161 GLN LLL CD  1 
ATOM   11245 O OE1 . GLN H 3 161 ? 6.802   -43.018 49.776  1.000 146.327 ? 161 GLN LLL OE1 1 
ATOM   11246 N NE2 . GLN H 3 161 ? 7.116   -44.734 51.183  1.000 140.347 ? 161 GLN LLL NE2 1 
ATOM   11247 N N   . SER H 3 162 ? 4.292   -39.633 48.825  1.000 143.883 ? 162 SER LLL N   1 
ATOM   11248 C CA  . SER H 3 162 ? 3.769   -38.550 47.951  1.000 144.259 ? 162 SER LLL CA  1 
ATOM   11249 C C   . SER H 3 162 ? 4.091   -38.850 46.479  1.000 146.098 ? 162 SER LLL C   1 
ATOM   11250 O O   . SER H 3 162 ? 5.273   -38.704 46.102  1.000 149.938 ? 162 SER LLL O   1 
ATOM   11251 C CB  . SER H 3 162 ? 4.339   -37.224 48.391  1.000 146.743 ? 162 SER LLL CB  1 
ATOM   11252 O OG  . SER H 3 162 ? 3.928   -36.180 47.527  1.000 147.615 ? 162 SER LLL OG  1 
ATOM   11253 N N   . GLY H 3 163 ? 3.084   -39.255 45.691  1.000 143.804 ? 163 GLY LLL N   1 
ATOM   11254 C CA  . GLY H 3 163 ? 3.204   -39.516 44.241  1.000 145.328 ? 163 GLY LLL CA  1 
ATOM   11255 C C   . GLY H 3 163 ? 2.880   -40.952 43.852  1.000 143.954 ? 163 GLY LLL C   1 
ATOM   11256 O O   . GLY H 3 163 ? 2.753   -41.198 42.642  1.000 146.659 ? 163 GLY LLL O   1 
ATOM   11257 N N   . ASN H 3 164 ? 2.750   -41.864 44.825  1.000 141.709 ? 164 ASN LLL N   1 
ATOM   11258 C CA  . ASN H 3 164 ? 2.478   -43.321 44.619  1.000 140.279 ? 164 ASN LLL CA  1 
ATOM   11259 C C   . ASN H 3 164 ? 1.072   -43.669 45.131  1.000 135.344 ? 164 ASN LLL C   1 
ATOM   11260 O O   . ASN H 3 164 ? 0.728   -44.882 45.230  1.000 133.927 ? 164 ASN LLL O   1 
ATOM   11261 C CB  . ASN H 3 164 ? 3.543   -44.193 45.294  1.000 142.195 ? 164 ASN LLL CB  1 
ATOM   11262 C CG  . ASN H 3 164 ? 3.953   -43.673 46.658  1.000 142.615 ? 164 ASN LLL CG  1 
ATOM   11263 O OD1 . ASN H 3 164 ? 3.133   -43.105 47.384  1.000 141.490 ? 164 ASN LLL OD1 1 
ATOM   11264 N ND2 . ASN H 3 164 ? 5.225   -43.831 47.002  1.000 145.049 ? 164 ASN LLL ND2 1 
ATOM   11265 N N   . SER H 3 165 ? 0.295   -42.635 45.464  1.000 132.658 ? 165 SER LLL N   1 
ATOM   11266 C CA  . SER H 3 165 ? -1.137  -42.706 45.835  1.000 129.935 ? 165 SER LLL CA  1 
ATOM   11267 C C   . SER H 3 165 ? -1.960  -42.185 44.658  1.000 128.846 ? 165 SER LLL C   1 
ATOM   11268 O O   . SER H 3 165 ? -1.375  -41.549 43.762  1.000 129.618 ? 165 SER LLL O   1 
ATOM   11269 C CB  . SER H 3 165 ? -1.406  -41.921 47.088  1.000 128.283 ? 165 SER LLL CB  1 
ATOM   11270 O OG  . SER H 3 165 ? -1.540  -40.537 46.807  1.000 129.493 ? 165 SER LLL OG  1 
ATOM   11271 N N   . GLN H 3 166 ? -3.266  -42.450 44.678  1.000 126.917 ? 166 GLN LLL N   1 
ATOM   11272 C CA  . GLN H 3 166 ? -4.235  -42.004 43.646  1.000 127.585 ? 166 GLN LLL CA  1 
ATOM   11273 C C   . GLN H 3 166 ? -5.617  -41.898 44.286  1.000 129.287 ? 166 GLN LLL C   1 
ATOM   11274 O O   . GLN H 3 166 ? -6.116  -42.929 44.768  1.000 128.813 ? 166 GLN LLL O   1 
ATOM   11275 C CB  . GLN H 3 166 ? -4.259  -42.985 42.477  1.000 126.787 ? 166 GLN LLL CB  1 
ATOM   11276 C CG  . GLN H 3 166 ? -3.486  -42.499 41.264  1.000 127.892 ? 166 GLN LLL CG  1 
ATOM   11277 C CD  . GLN H 3 166 ? -3.448  -43.564 40.202  1.000 128.565 ? 166 GLN LLL CD  1 
ATOM   11278 O OE1 . GLN H 3 166 ? -3.252  -44.742 40.482  1.000 128.020 ? 166 GLN LLL OE1 1 
ATOM   11279 N NE2 . GLN H 3 166 ? -3.647  -43.151 38.967  1.000 131.281 ? 166 GLN LLL NE2 1 
ATOM   11280 N N   . GLU H 3 167 ? -6.199  -40.698 44.282  1.000 133.387 ? 167 GLU LLL N   1 
ATOM   11281 C CA  . GLU H 3 167 ? -7.525  -40.421 44.892  1.000 133.913 ? 167 GLU LLL CA  1 
ATOM   11282 C C   . GLU H 3 167 ? -8.617  -40.616 43.838  1.000 132.939 ? 167 GLU LLL C   1 
ATOM   11283 O O   . GLU H 3 167 ? -8.377  -40.330 42.642  1.000 133.388 ? 167 GLU LLL O   1 
ATOM   11284 C CB  . GLU H 3 167 ? -7.579  -39.007 45.472  1.000 138.199 ? 167 GLU LLL CB  1 
ATOM   11285 C CG  . GLU H 3 167 ? -6.656  -38.798 46.663  1.000 142.916 ? 167 GLU LLL CG  1 
ATOM   11286 C CD  . GLU H 3 167 ? -6.772  -37.446 47.359  1.000 147.672 ? 167 GLU LLL CD  1 
ATOM   11287 O OE1 . GLU H 3 167 ? -7.753  -36.715 47.077  1.000 150.744 ? 167 GLU LLL OE1 1 
ATOM   11288 O OE2 . GLU H 3 167 ? -5.884  -37.125 48.194  1.000 150.949 ? 167 GLU LLL OE2 1 
ATOM   11289 N N   . SER H 3 168 ? -9.773  -41.097 44.286  1.000 131.024 ? 168 SER LLL N   1 
ATOM   11290 C CA  . SER H 3 168 ? -11.013 -41.200 43.484  1.000 131.343 ? 168 SER LLL CA  1 
ATOM   11291 C C   . SER H 3 168 ? -12.199 -40.784 44.360  1.000 130.505 ? 168 SER LLL C   1 
ATOM   11292 O O   . SER H 3 168 ? -12.398 -41.402 45.423  1.000 130.690 ? 168 SER LLL O   1 
ATOM   11293 C CB  . SER H 3 168 ? -11.176 -42.575 42.929  1.000 131.987 ? 168 SER LLL CB  1 
ATOM   11294 O OG  . SER H 3 168 ? -12.200 -42.580 41.954  1.000 133.514 ? 168 SER LLL OG  1 
ATOM   11295 N N   . VAL H 3 169 ? -12.941 -39.767 43.916  1.000 129.504 ? 169 VAL LLL N   1 
ATOM   11296 C CA  . VAL H 3 169 ? -13.994 -39.049 44.694  1.000 126.720 ? 169 VAL LLL CA  1 
ATOM   11297 C C   . VAL H 3 169 ? -15.349 -39.263 44.015  1.000 128.854 ? 169 VAL LLL C   1 
ATOM   11298 O O   . VAL H 3 169 ? -15.472 -38.918 42.818  1.000 131.922 ? 169 VAL LLL O   1 
ATOM   11299 C CB  . VAL H 3 169 ? -13.671 -37.547 44.776  1.000 124.784 ? 169 VAL LLL CB  1 
ATOM   11300 C CG1 . VAL H 3 169 ? -14.727 -36.780 45.551  1.000 124.701 ? 169 VAL LLL CG1 1 
ATOM   11301 C CG2 . VAL H 3 169 ? -12.291 -37.300 45.355  1.000 124.251 ? 169 VAL LLL CG2 1 
ATOM   11302 N N   . THR H 3 170 ? -16.334 -39.764 44.761  1.000 129.353 ? 170 THR LLL N   1 
ATOM   11303 C CA  . THR H 3 170 ? -17.732 -39.923 44.282  1.000 133.528 ? 170 THR LLL CA  1 
ATOM   11304 C C   . THR H 3 170 ? -18.371 -38.537 44.167  1.000 135.613 ? 170 THR LLL C   1 
ATOM   11305 O O   . THR H 3 170 ? -18.064 -37.682 45.019  1.000 135.305 ? 170 THR LLL O   1 
ATOM   11306 C CB  . THR H 3 170 ? -18.566 -40.817 45.207  1.000 136.572 ? 170 THR LLL CB  1 
ATOM   11307 O OG1 . THR H 3 170 ? -18.974 -40.051 46.344  1.000 138.413 ? 170 THR LLL OG1 1 
ATOM   11308 C CG2 . THR H 3 170 ? -17.823 -42.057 45.649  1.000 137.672 ? 170 THR LLL CG2 1 
ATOM   11309 N N   . GLU H 3 171 ? -19.229 -38.332 43.161  1.000 139.579 ? 171 GLU LLL N   1 
ATOM   11310 C CA  . GLU H 3 171 ? -20.046 -37.097 43.003  1.000 141.318 ? 171 GLU LLL CA  1 
ATOM   11311 C C   . GLU H 3 171 ? -21.028 -37.025 44.171  1.000 140.412 ? 171 GLU LLL C   1 
ATOM   11312 O O   . GLU H 3 171 ? -21.160 -38.035 44.884  1.000 142.057 ? 171 GLU LLL O   1 
ATOM   11313 C CB  . GLU H 3 171 ? -20.773 -37.092 41.657  1.000 146.202 ? 171 GLU LLL CB  1 
ATOM   11314 C CG  . GLU H 3 171 ? -19.835 -36.927 40.477  1.000 148.723 ? 171 GLU LLL CG  1 
ATOM   11315 C CD  . GLU H 3 171 ? -18.932 -35.715 40.612  1.000 151.098 ? 171 GLU LLL CD  1 
ATOM   11316 O OE1 . GLU H 3 171 ? -19.449 -34.584 40.484  1.000 156.013 ? 171 GLU LLL OE1 1 
ATOM   11317 O OE2 . GLU H 3 171 ? -17.729 -35.903 40.912  1.000 150.864 ? 171 GLU LLL OE2 1 
ATOM   11318 N N   . GLN H 3 172 ? -21.681 -35.881 44.373  1.000 139.636 ? 172 GLN LLL N   1 
ATOM   11319 C CA  . GLN H 3 172 ? -22.608 -35.687 45.520  1.000 140.439 ? 172 GLN LLL CA  1 
ATOM   11320 C C   . GLN H 3 172 ? -23.610 -36.846 45.544  1.000 140.779 ? 172 GLN LLL C   1 
ATOM   11321 O O   . GLN H 3 172 ? -23.953 -37.354 44.457  1.000 140.935 ? 172 GLN LLL O   1 
ATOM   11322 C CB  . GLN H 3 172 ? -23.307 -34.331 45.449  1.000 142.359 ? 172 GLN LLL CB  1 
ATOM   11323 C CG  . GLN H 3 172 ? -22.684 -33.301 46.375  1.000 142.357 ? 172 GLN LLL CG  1 
ATOM   11324 C CD  . GLN H 3 172 ? -23.463 -32.013 46.423  1.000 145.297 ? 172 GLN LLL CD  1 
ATOM   11325 O OE1 . GLN H 3 172 ? -24.569 -31.913 45.897  1.000 146.815 ? 172 GLN LLL OE1 1 
ATOM   11326 N NE2 . GLN H 3 172 ? -22.889 -31.015 47.074  1.000 148.322 ? 172 GLN LLL NE2 1 
ATOM   11327 N N   . ASP H 3 173 ? -24.036 -37.257 46.740  1.000 141.352 ? 173 ASP LLL N   1 
ATOM   11328 C CA  . ASP H 3 173 ? -24.831 -38.496 46.945  1.000 145.231 ? 173 ASP LLL CA  1 
ATOM   11329 C C   . ASP H 3 173 ? -26.288 -38.271 46.522  1.000 147.496 ? 173 ASP LLL C   1 
ATOM   11330 O O   . ASP H 3 173 ? -26.821 -37.163 46.754  1.000 146.956 ? 173 ASP LLL O   1 
ATOM   11331 C CB  . ASP H 3 173 ? -24.779 -38.983 48.394  1.000 149.785 ? 173 ASP LLL CB  1 
ATOM   11332 C CG  . ASP H 3 173 ? -25.689 -40.173 48.667  1.000 155.417 ? 173 ASP LLL CG  1 
ATOM   11333 O OD1 . ASP H 3 173 ? -25.763 -41.071 47.794  1.000 156.538 ? 173 ASP LLL OD1 1 
ATOM   11334 O OD2 . ASP H 3 173 ? -26.346 -40.179 49.734  1.000 160.023 ? 173 ASP LLL OD2 1 
ATOM   11335 N N   . SER H 3 174 ? -26.889 -39.330 45.965  1.000 149.163 ? 174 SER LLL N   1 
ATOM   11336 C CA  . SER H 3 174 ? -28.309 -39.458 45.535  1.000 152.226 ? 174 SER LLL CA  1 
ATOM   11337 C C   . SER H 3 174 ? -29.275 -39.066 46.668  1.000 155.693 ? 174 SER LLL C   1 
ATOM   11338 O O   . SER H 3 174 ? -30.393 -38.606 46.352  1.000 155.316 ? 174 SER LLL O   1 
ATOM   11339 C CB  . SER H 3 174 ? -28.578 -40.875 45.057  1.000 153.658 ? 174 SER LLL CB  1 
ATOM   11340 O OG  . SER H 3 174 ? -27.373 -41.536 44.676  1.000 149.515 ? 174 SER LLL OG  1 
ATOM   11341 N N   . LYS H 3 175 ? -28.855 -39.246 47.929  1.000 157.924 ? 175 LYS LLL N   1 
ATOM   11342 C CA  . LYS H 3 175 ? -29.703 -39.137 49.149  1.000 162.835 ? 175 LYS LLL CA  1 
ATOM   11343 C C   . LYS H 3 175 ? -29.262 -37.930 49.997  1.000 163.349 ? 175 LYS LLL C   1 
ATOM   11344 O O   . LYS H 3 175 ? -30.081 -37.003 50.152  1.000 164.341 ? 175 LYS LLL O   1 
ATOM   11345 C CB  . LYS H 3 175 ? -29.638 -40.446 49.947  1.000 164.388 ? 175 LYS LLL CB  1 
ATOM   11346 C CG  . LYS H 3 175 ? -29.925 -41.728 49.166  1.000 165.305 ? 175 LYS LLL CG  1 
ATOM   11347 C CD  . LYS H 3 175 ? -31.338 -42.250 49.304  1.000 172.010 ? 175 LYS LLL CD  1 
ATOM   11348 C CE  . LYS H 3 175 ? -31.518 -43.646 48.743  1.000 174.746 ? 175 LYS LLL CE  1 
ATOM   11349 N NZ  . LYS H 3 175 ? -32.939 -44.071 48.796  1.000 182.332 ? 175 LYS LLL NZ  1 
ATOM   11350 N N   . ASP H 3 176 ? -28.023 -37.921 50.507  1.000 163.656 ? 176 ASP LLL N   1 
ATOM   11351 C CA  . ASP H 3 176 ? -27.588 -37.032 51.624  1.000 168.240 ? 176 ASP LLL CA  1 
ATOM   11352 C C   . ASP H 3 176 ? -26.636 -35.907 51.166  1.000 166.014 ? 176 ASP LLL C   1 
ATOM   11353 O O   . ASP H 3 176 ? -26.133 -35.170 52.052  1.000 164.009 ? 176 ASP LLL O   1 
ATOM   11354 C CB  . ASP H 3 176 ? -26.949 -37.861 52.744  1.000 171.632 ? 176 ASP LLL CB  1 
ATOM   11355 C CG  . ASP H 3 176 ? -25.548 -38.376 52.444  1.000 168.999 ? 176 ASP LLL CG  1 
ATOM   11356 O OD1 . ASP H 3 176 ? -24.985 -37.995 51.401  1.000 166.956 ? 176 ASP LLL OD1 1 
ATOM   11357 O OD2 . ASP H 3 176 ? -25.019 -39.144 53.271  1.000 172.443 ? 176 ASP LLL OD2 1 
ATOM   11358 N N   . SER H 3 177 ? -26.367 -35.776 49.859  1.000 166.137 ? 177 SER LLL N   1 
ATOM   11359 C CA  . SER H 3 177 ? -25.581 -34.665 49.246  1.000 164.446 ? 177 SER LLL CA  1 
ATOM   11360 C C   . SER H 3 177 ? -24.148 -34.606 49.806  1.000 160.439 ? 177 SER LLL C   1 
ATOM   11361 O O   . SER H 3 177 ? -23.591 -33.483 49.901  1.000 159.533 ? 177 SER LLL O   1 
ATOM   11362 C CB  . SER H 3 177 ? -26.281 -33.339 49.439  1.000 169.357 ? 177 SER LLL CB  1 
ATOM   11363 O OG  . SER H 3 177 ? -27.652 -33.426 49.080  1.000 175.180 ? 177 SER LLL OG  1 
ATOM   11364 N N   . THR H 3 178 ? -23.568 -35.762 50.151  1.000 156.573 ? 178 THR LLL N   1 
ATOM   11365 C CA  . THR H 3 178 ? -22.159 -35.899 50.607  1.000 150.288 ? 178 THR LLL CA  1 
ATOM   11366 C C   . THR H 3 178 ? -21.310 -36.539 49.506  1.000 144.820 ? 178 THR LLL C   1 
ATOM   11367 O O   . THR H 3 178 ? -21.865 -37.238 48.626  1.000 143.248 ? 178 THR LLL O   1 
ATOM   11368 C CB  . THR H 3 178 ? -22.019 -36.749 51.877  1.000 150.245 ? 178 THR LLL CB  1 
ATOM   11369 O OG1 . THR H 3 178 ? -22.317 -38.109 51.553  1.000 149.054 ? 178 THR LLL OG1 1 
ATOM   11370 C CG2 . THR H 3 178 ? -22.894 -36.266 53.012  1.000 153.953 ? 178 THR LLL CG2 1 
ATOM   11371 N N   . TYR H 3 179 ? -20.002 -36.316 49.592  1.000 140.661 ? 179 TYR LLL N   1 
ATOM   11372 C CA  . TYR H 3 179 ? -18.963 -37.020 48.810  1.000 136.135 ? 179 TYR LLL CA  1 
ATOM   11373 C C   . TYR H 3 179 ? -18.400 -38.156 49.669  1.000 134.935 ? 179 TYR LLL C   1 
ATOM   11374 O O   . TYR H 3 179 ? -18.664 -38.192 50.885  1.000 138.277 ? 179 TYR LLL O   1 
ATOM   11375 C CB  . TYR H 3 179 ? -17.875 -36.032 48.394  1.000 134.395 ? 179 TYR LLL CB  1 
ATOM   11376 C CG  . TYR H 3 179 ? -18.370 -34.748 47.772  1.000 136.623 ? 179 TYR LLL CG  1 
ATOM   11377 C CD1 . TYR H 3 179 ? -18.831 -34.707 46.461  1.000 138.317 ? 179 TYR LLL CD1 1 
ATOM   11378 C CD2 . TYR H 3 179 ? -18.344 -33.557 48.480  1.000 138.387 ? 179 TYR LLL CD2 1 
ATOM   11379 C CE1 . TYR H 3 179 ? -19.257 -33.523 45.877  1.000 139.193 ? 179 TYR LLL CE1 1 
ATOM   11380 C CE2 . TYR H 3 179 ? -18.769 -32.363 47.912  1.000 140.647 ? 179 TYR LLL CE2 1 
ATOM   11381 C CZ  . TYR H 3 179 ? -19.231 -32.343 46.605  1.000 140.275 ? 179 TYR LLL CZ  1 
ATOM   11382 O OH  . TYR H 3 179 ? -19.652 -31.168 46.045  1.000 138.129 ? 179 TYR LLL OH  1 
ATOM   11383 N N   . SER H 3 180 ? -17.672 -39.073 49.034  1.000 131.236 ? 180 SER LLL N   1 
ATOM   11384 C CA  . SER H 3 180 ? -16.800 -40.092 49.673  1.000 129.300 ? 180 SER LLL CA  1 
ATOM   11385 C C   . SER H 3 180 ? -15.518 -40.190 48.840  1.000 128.098 ? 180 SER LLL C   1 
ATOM   11386 O O   . SER H 3 180 ? -15.534 -39.683 47.700  1.000 131.262 ? 180 SER LLL O   1 
ATOM   11387 C CB  . SER H 3 180 ? -17.504 -41.411 49.797  1.000 129.594 ? 180 SER LLL CB  1 
ATOM   11388 O OG  . SER H 3 180 ? -18.775 -41.241 50.406  1.000 131.402 ? 180 SER LLL OG  1 
ATOM   11389 N N   . LEU H 3 181 ? -14.456 -40.809 49.364  1.000 126.443 ? 181 LEU LLL N   1 
ATOM   11390 C CA  . LEU H 3 181 ? -13.112 -40.789 48.722  1.000 124.812 ? 181 LEU LLL CA  1 
ATOM   11391 C C   . LEU H 3 181 ? -12.387 -42.123 48.941  1.000 124.982 ? 181 LEU LLL C   1 
ATOM   11392 O O   . LEU H 3 181 ? -12.437 -42.638 50.064  1.000 127.088 ? 181 LEU LLL O   1 
ATOM   11393 C CB  . LEU H 3 181 ? -12.329 -39.617 49.319  1.000 124.831 ? 181 LEU LLL CB  1 
ATOM   11394 C CG  . LEU H 3 181 ? -11.102 -39.163 48.529  1.000 125.575 ? 181 LEU LLL CG  1 
ATOM   11395 C CD1 . LEU H 3 181 ? -10.725 -37.732 48.888  1.000 126.070 ? 181 LEU LLL CD1 1 
ATOM   11396 C CD2 . LEU H 3 181 ? -9.919  -40.094 48.757  1.000 126.302 ? 181 LEU LLL CD2 1 
ATOM   11397 N N   . SER H 3 182 ? -11.738 -42.651 47.898  1.000 125.056 ? 182 SER LLL N   1 
ATOM   11398 C CA  . SER H 3 182 ? -10.816 -43.815 47.967  1.000 126.636 ? 182 SER LLL CA  1 
ATOM   11399 C C   . SER H 3 182 ? -9.434  -43.381 47.480  1.000 126.074 ? 182 SER LLL C   1 
ATOM   11400 O O   . SER H 3 182 ? -9.253  -43.236 46.250  1.000 126.249 ? 182 SER LLL O   1 
ATOM   11401 C CB  . SER H 3 182 ? -11.313 -44.996 47.170  1.000 129.671 ? 182 SER LLL CB  1 
ATOM   11402 O OG  . SER H 3 182 ? -10.482 -45.244 46.034  1.000 131.792 ? 182 SER LLL OG  1 
ATOM   11403 N N   . SER H 3 183 ? -8.504  -43.166 48.411  1.000 126.498 ? 183 SER LLL N   1 
ATOM   11404 C CA  . SER H 3 183 ? -7.059  -43.032 48.104  1.000 128.436 ? 183 SER LLL CA  1 
ATOM   11405 C C   . SER H 3 183 ? -6.424  -44.418 48.153  1.000 129.320 ? 183 SER LLL C   1 
ATOM   11406 O O   . SER H 3 183 ? -6.467  -45.063 49.212  1.000 129.774 ? 183 SER LLL O   1 
ATOM   11407 C CB  . SER H 3 183 ? -6.349  -42.084 49.016  1.000 129.944 ? 183 SER LLL CB  1 
ATOM   11408 O OG  . SER H 3 183 ? -5.057  -41.808 48.497  1.000 130.467 ? 183 SER LLL OG  1 
ATOM   11409 N N   . THR H 3 184 ? -5.891  -44.858 47.022  1.000 132.158 ? 184 THR LLL N   1 
ATOM   11410 C CA  . THR H 3 184 ? -5.221  -46.166 46.870  1.000 135.447 ? 184 THR LLL CA  1 
ATOM   11411 C C   . THR H 3 184 ? -3.721  -45.884 46.791  1.000 135.197 ? 184 THR LLL C   1 
ATOM   11412 O O   . THR H 3 184 ? -3.332  -44.985 46.024  1.000 136.172 ? 184 THR LLL O   1 
ATOM   11413 C CB  . THR H 3 184 ? -5.772  -46.936 45.660  1.000 140.011 ? 184 THR LLL CB  1 
ATOM   11414 O OG1 . THR H 3 184 ? -7.189  -46.752 45.535  1.000 140.925 ? 184 THR LLL OG1 1 
ATOM   11415 C CG2 . THR H 3 184 ? -5.428  -48.407 45.739  1.000 141.735 ? 184 THR LLL CG2 1 
ATOM   11416 N N   . LEU H 3 185 ? -2.938  -46.587 47.610  1.000 135.922 ? 185 LEU LLL N   1 
ATOM   11417 C CA  . LEU H 3 185 ? -1.451  -46.578 47.612  1.000 136.885 ? 185 LEU LLL CA  1 
ATOM   11418 C C   . LEU H 3 185 ? -0.971  -47.903 47.015  1.000 137.756 ? 185 LEU LLL C   1 
ATOM   11419 O O   . LEU H 3 185 ? -1.247  -48.959 47.629  1.000 138.039 ? 185 LEU LLL O   1 
ATOM   11420 C CB  . LEU H 3 185 ? -0.970  -46.420 49.058  1.000 137.004 ? 185 LEU LLL CB  1 
ATOM   11421 C CG  . LEU H 3 185 ? 0.545   -46.368 49.250  1.000 137.377 ? 185 LEU LLL CG  1 
ATOM   11422 C CD1 . LEU H 3 185 ? 1.091   -44.993 48.890  1.000 137.650 ? 185 LEU LLL CD1 1 
ATOM   11423 C CD2 . LEU H 3 185 ? 0.913   -46.723 50.681  1.000 137.338 ? 185 LEU LLL CD2 1 
ATOM   11424 N N   . THR H 3 186 ? -0.325  -47.860 45.851  1.000 139.664 ? 186 THR LLL N   1 
ATOM   11425 C CA  . THR H 3 186 ? 0.147   -49.068 45.124  1.000 145.214 ? 186 THR LLL CA  1 
ATOM   11426 C C   . THR H 3 186 ? 1.672   -49.131 45.234  1.000 146.609 ? 186 THR LLL C   1 
ATOM   11427 O O   . THR H 3 186 ? 2.311   -48.052 45.189  1.000 147.482 ? 186 THR LLL O   1 
ATOM   11428 C CB  . THR H 3 186 ? -0.325  -49.063 43.662  1.000 150.581 ? 186 THR LLL CB  1 
ATOM   11429 O OG1 . THR H 3 186 ? -1.754  -49.021 43.637  1.000 150.504 ? 186 THR LLL OG1 1 
ATOM   11430 C CG2 . THR H 3 186 ? 0.161   -50.265 42.877  1.000 155.318 ? 186 THR LLL CG2 1 
ATOM   11431 N N   . LEU H 3 187 ? 2.215   -50.345 45.387  1.000 147.636 ? 187 LEU LLL N   1 
ATOM   11432 C CA  . LEU H 3 187 ? 3.676   -50.641 45.379  1.000 149.086 ? 187 LEU LLL CA  1 
ATOM   11433 C C   . LEU H 3 187 ? 3.899   -52.151 45.222  1.000 153.127 ? 187 LEU LLL C   1 
ATOM   11434 O O   . LEU H 3 187 ? 2.943   -52.931 45.428  1.000 153.429 ? 187 LEU LLL O   1 
ATOM   11435 C CB  . LEU H 3 187 ? 4.327   -50.132 46.669  1.000 144.973 ? 187 LEU LLL CB  1 
ATOM   11436 C CG  . LEU H 3 187 ? 3.899   -50.838 47.955  1.000 142.468 ? 187 LEU LLL CG  1 
ATOM   11437 C CD1 . LEU H 3 187 ? 4.999   -50.791 48.990  1.000 142.434 ? 187 LEU LLL CD1 1 
ATOM   11438 C CD2 . LEU H 3 187 ? 2.634   -50.225 48.528  1.000 140.058 ? 187 LEU LLL CD2 1 
ATOM   11439 N N   . SER H 3 188 ? 5.128   -52.541 44.880  1.000 157.282 ? 188 SER LLL N   1 
ATOM   11440 C CA  . SER H 3 188 ? 5.546   -53.953 44.700  1.000 161.403 ? 188 SER LLL CA  1 
ATOM   11441 C C   . SER H 3 188 ? 5.440   -54.674 46.045  1.000 161.690 ? 188 SER LLL C   1 
ATOM   11442 O O   . SER H 3 188 ? 5.717   -54.033 47.072  1.000 159.318 ? 188 SER LLL O   1 
ATOM   11443 C CB  . SER H 3 188 ? 6.941   -54.039 44.148  1.000 165.277 ? 188 SER LLL CB  1 
ATOM   11444 O OG  . SER H 3 188 ? 7.867   -53.451 45.047  1.000 165.413 ? 188 SER LLL OG  1 
ATOM   11445 N N   . LYS H 3 189 ? 5.044   -55.949 46.024  1.000 167.132 ? 189 LYS LLL N   1 
ATOM   11446 C CA  . LYS H 3 189 ? 5.064   -56.862 47.199  1.000 169.187 ? 189 LYS LLL CA  1 
ATOM   11447 C C   . LYS H 3 189 ? 6.435   -56.740 47.870  1.000 170.608 ? 189 LYS LLL C   1 
ATOM   11448 O O   . LYS H 3 189 ? 6.480   -56.598 49.103  1.000 169.714 ? 189 LYS LLL O   1 
ATOM   11449 C CB  . LYS H 3 189 ? 4.772   -58.304 46.763  1.000 173.107 ? 189 LYS LLL CB  1 
ATOM   11450 C CG  . LYS H 3 189 ? 4.863   -59.362 47.854  1.000 174.318 ? 189 LYS LLL CG  1 
ATOM   11451 C CD  . LYS H 3 189 ? 6.221   -60.031 47.945  1.000 177.594 ? 189 LYS LLL CD  1 
ATOM   11452 C CE  . LYS H 3 189 ? 6.242   -61.192 48.914  1.000 180.256 ? 189 LYS LLL CE  1 
ATOM   11453 N NZ  . LYS H 3 189 ? 5.706   -62.437 48.314  1.000 184.575 ? 189 LYS LLL NZ  1 
ATOM   11454 N N   . ALA H 3 190 ? 7.500   -56.775 47.065  1.000 174.091 ? 190 ALA LLL N   1 
ATOM   11455 C CA  . ALA H 3 190 ? 8.901   -56.550 47.484  1.000 177.162 ? 190 ALA LLL CA  1 
ATOM   11456 C C   . ALA H 3 190 ? 8.976   -55.358 48.447  1.000 173.480 ? 190 ALA LLL C   1 
ATOM   11457 O O   . ALA H 3 190 ? 9.337   -55.557 49.625  1.000 171.481 ? 190 ALA LLL O   1 
ATOM   11458 C CB  . ALA H 3 190 ? 9.760   -56.321 46.262  1.000 181.243 ? 190 ALA LLL CB  1 
ATOM   11459 N N   . ASP H 3 191 ? 8.632   -54.165 47.956  1.000 172.355 ? 191 ASP LLL N   1 
ATOM   11460 C CA  . ASP H 3 191 ? 8.791   -52.877 48.682  1.000 169.945 ? 191 ASP LLL CA  1 
ATOM   11461 C C   . ASP H 3 191 ? 7.793   -52.820 49.851  1.000 163.106 ? 191 ASP LLL C   1 
ATOM   11462 O O   . ASP H 3 191 ? 8.083   -52.111 50.833  1.000 162.255 ? 191 ASP LLL O   1 
ATOM   11463 C CB  . ASP H 3 191 ? 8.676   -51.689 47.717  1.000 172.538 ? 191 ASP LLL CB  1 
ATOM   11464 C CG  . ASP H 3 191 ? 9.800   -51.585 46.688  1.000 178.001 ? 191 ASP LLL CG  1 
ATOM   11465 O OD1 . ASP H 3 191 ? 10.965  -51.866 47.045  1.000 181.132 ? 191 ASP LLL OD1 1 
ATOM   11466 O OD2 . ASP H 3 191 ? 9.511   -51.204 45.534  1.000 179.704 ? 191 ASP LLL OD2 1 
ATOM   11467 N N   . TYR H 3 192 ? 6.666   -53.537 49.764  1.000 158.029 ? 192 TYR LLL N   1 
ATOM   11468 C CA  . TYR H 3 192 ? 5.626   -53.569 50.827  1.000 153.768 ? 192 TYR LLL CA  1 
ATOM   11469 C C   . TYR H 3 192 ? 6.153   -54.329 52.044  1.000 156.898 ? 192 TYR LLL C   1 
ATOM   11470 O O   . TYR H 3 192 ? 5.839   -53.934 53.182  1.000 156.797 ? 192 TYR LLL O   1 
ATOM   11471 C CB  . TYR H 3 192 ? 4.324   -54.206 50.344  1.000 150.417 ? 192 TYR LLL CB  1 
ATOM   11472 C CG  . TYR H 3 192 ? 3.297   -54.385 51.436  1.000 147.601 ? 192 TYR LLL CG  1 
ATOM   11473 C CD1 . TYR H 3 192 ? 2.558   -53.312 51.907  1.000 143.749 ? 192 TYR LLL CD1 1 
ATOM   11474 C CD2 . TYR H 3 192 ? 3.075   -55.625 52.015  1.000 149.393 ? 192 TYR LLL CD2 1 
ATOM   11475 C CE1 . TYR H 3 192 ? 1.621   -53.468 52.916  1.000 142.721 ? 192 TYR LLL CE1 1 
ATOM   11476 C CE2 . TYR H 3 192 ? 2.135   -55.799 53.019  1.000 148.579 ? 192 TYR LLL CE2 1 
ATOM   11477 C CZ  . TYR H 3 192 ? 1.404   -54.715 53.473  1.000 145.293 ? 192 TYR LLL CZ  1 
ATOM   11478 O OH  . TYR H 3 192 ? 0.474   -54.876 54.462  1.000 144.909 ? 192 TYR LLL OH  1 
ATOM   11479 N N   . GLU H 3 193 ? 6.922   -55.393 51.808  1.000 161.736 ? 193 GLU LLL N   1 
ATOM   11480 C CA  . GLU H 3 193 ? 7.492   -56.249 52.879  1.000 165.579 ? 193 GLU LLL CA  1 
ATOM   11481 C C   . GLU H 3 193 ? 8.677   -55.532 53.544  1.000 165.324 ? 193 GLU LLL C   1 
ATOM   11482 O O   . GLU H 3 193 ? 9.096   -55.997 54.616  1.000 166.550 ? 193 GLU LLL O   1 
ATOM   11483 C CB  . GLU H 3 193 ? 7.878   -57.622 52.319  1.000 171.835 ? 193 GLU LLL CB  1 
ATOM   11484 C CG  . GLU H 3 193 ? 6.680   -58.516 52.018  1.000 174.005 ? 193 GLU LLL CG  1 
ATOM   11485 C CD  . GLU H 3 193 ? 6.963   -60.012 51.976  1.000 179.728 ? 193 GLU LLL CD  1 
ATOM   11486 O OE1 . GLU H 3 193 ? 8.104   -60.397 51.648  1.000 184.933 ? 193 GLU LLL OE1 1 
ATOM   11487 O OE2 . GLU H 3 193 ? 6.041   -60.798 52.278  1.000 180.606 ? 193 GLU LLL OE2 1 
ATOM   11488 N N   . LYS H 3 194 ? 9.182   -54.440 52.957  1.000 165.182 ? 194 LYS LLL N   1 
ATOM   11489 C CA  . LYS H 3 194 ? 10.337  -53.663 53.490  1.000 168.083 ? 194 LYS LLL CA  1 
ATOM   11490 C C   . LYS H 3 194 ? 9.888   -52.805 54.683  1.000 166.227 ? 194 LYS LLL C   1 
ATOM   11491 O O   . LYS H 3 194 ? 10.564  -52.862 55.731  1.000 171.481 ? 194 LYS LLL O   1 
ATOM   11492 C CB  . LYS H 3 194 ? 10.979  -52.802 52.396  1.000 170.219 ? 194 LYS LLL CB  1 
ATOM   11493 C CG  . LYS H 3 194 ? 12.072  -53.485 51.581  1.000 174.696 ? 194 LYS LLL CG  1 
ATOM   11494 C CD  . LYS H 3 194 ? 12.379  -52.824 50.240  1.000 176.474 ? 194 LYS LLL CD  1 
ATOM   11495 C CE  . LYS H 3 194 ? 12.631  -51.325 50.301  1.000 175.373 ? 194 LYS LLL CE  1 
ATOM   11496 N NZ  . LYS H 3 194 ? 12.957  -50.749 48.973  1.000 176.065 ? 194 LYS LLL NZ  1 
ATOM   11497 N N   . HIS H 3 195 ? 8.796   -52.049 54.540  1.000 160.788 ? 195 HIS LLL N   1 
ATOM   11498 C CA  . HIS H 3 195 ? 8.259   -51.132 55.582  1.000 158.411 ? 195 HIS LLL CA  1 
ATOM   11499 C C   . HIS H 3 195 ? 7.230   -51.894 56.433  1.000 157.434 ? 195 HIS LLL C   1 
ATOM   11500 O O   . HIS H 3 195 ? 6.725   -52.916 55.931  1.000 158.534 ? 195 HIS LLL O   1 
ATOM   11501 C CB  . HIS H 3 195 ? 7.701   -49.869 54.912  1.000 155.677 ? 195 HIS LLL CB  1 
ATOM   11502 C CG  . HIS H 3 195 ? 8.584   -49.298 53.849  1.000 156.832 ? 195 HIS LLL CG  1 
ATOM   11503 N ND1 . HIS H 3 195 ? 9.921   -49.011 54.062  1.000 159.612 ? 195 HIS LLL ND1 1 
ATOM   11504 C CD2 . HIS H 3 195 ? 8.323   -48.943 52.571  1.000 156.534 ? 195 HIS LLL CD2 1 
ATOM   11505 C CE1 . HIS H 3 195 ? 10.443  -48.520 52.954  1.000 161.617 ? 195 HIS LLL CE1 1 
ATOM   11506 N NE2 . HIS H 3 195 ? 9.482   -48.459 52.025  1.000 159.203 ? 195 HIS LLL NE2 1 
ATOM   11507 N N   . LYS H 3 196 ? 6.938   -51.445 57.664  1.000 156.397 ? 196 LYS LLL N   1 
ATOM   11508 C CA  . LYS H 3 196 ? 6.017   -52.161 58.594  1.000 156.995 ? 196 LYS LLL CA  1 
ATOM   11509 C C   . LYS H 3 196 ? 4.764   -51.337 58.934  1.000 154.831 ? 196 LYS LLL C   1 
ATOM   11510 O O   . LYS H 3 196 ? 3.682   -51.957 59.035  1.000 157.620 ? 196 LYS LLL O   1 
ATOM   11511 C CB  . LYS H 3 196 ? 6.722   -52.576 59.886  1.000 161.241 ? 196 LYS LLL CB  1 
ATOM   11512 C CG  . LYS H 3 196 ? 5.917   -53.587 60.690  1.000 165.751 ? 196 LYS LLL CG  1 
ATOM   11513 C CD  . LYS H 3 196 ? 6.282   -53.705 62.148  1.000 172.835 ? 196 LYS LLL CD  1 
ATOM   11514 C CE  . LYS H 3 196 ? 5.403   -54.702 62.884  1.000 176.753 ? 196 LYS LLL CE  1 
ATOM   11515 N NZ  . LYS H 3 196 ? 5.776   -54.838 64.315  1.000 182.411 ? 196 LYS LLL NZ  1 
ATOM   11516 N N   . VAL H 3 197 ? 4.875   -50.018 59.122  1.000 152.230 ? 197 VAL LLL N   1 
ATOM   11517 C CA  . VAL H 3 197 ? 3.746   -49.164 59.605  1.000 150.533 ? 197 VAL LLL CA  1 
ATOM   11518 C C   . VAL H 3 197 ? 3.151   -48.352 58.452  1.000 146.348 ? 197 VAL LLL C   1 
ATOM   11519 O O   . VAL H 3 197 ? 3.790   -47.369 58.043  1.000 145.864 ? 197 VAL LLL O   1 
ATOM   11520 C CB  . VAL H 3 197 ? 4.201   -48.227 60.733  1.000 153.359 ? 197 VAL LLL CB  1 
ATOM   11521 C CG1 . VAL H 3 197 ? 3.067   -47.306 61.166  1.000 152.991 ? 197 VAL LLL CG1 1 
ATOM   11522 C CG2 . VAL H 3 197 ? 4.766   -49.010 61.909  1.000 157.395 ? 197 VAL LLL CG2 1 
ATOM   11523 N N   . TYR H 3 198 ? 1.941   -48.710 58.010  1.000 144.401 ? 198 TYR LLL N   1 
ATOM   11524 C CA  . TYR H 3 198 ? 1.178   -48.033 56.927  1.000 142.910 ? 198 TYR LLL CA  1 
ATOM   11525 C C   . TYR H 3 198 ? 0.035   -47.223 57.543  1.000 144.013 ? 198 TYR LLL C   1 
ATOM   11526 O O   . TYR H 3 198 ? -0.774  -47.811 58.274  1.000 150.771 ? 198 TYR LLL O   1 
ATOM   11527 C CB  . TYR H 3 198 ? 0.657   -49.063 55.923  1.000 141.501 ? 198 TYR LLL CB  1 
ATOM   11528 C CG  . TYR H 3 198 ? 1.758   -49.709 55.120  1.000 141.543 ? 198 TYR LLL CG  1 
ATOM   11529 C CD1 . TYR H 3 198 ? 2.383   -50.856 55.576  1.000 143.885 ? 198 TYR LLL CD1 1 
ATOM   11530 C CD2 . TYR H 3 198 ? 2.217   -49.147 53.939  1.000 138.537 ? 198 TYR LLL CD2 1 
ATOM   11531 C CE1 . TYR H 3 198 ? 3.415   -51.447 54.866  1.000 143.696 ? 198 TYR LLL CE1 1 
ATOM   11532 C CE2 . TYR H 3 198 ? 3.243   -49.730 53.214  1.000 138.424 ? 198 TYR LLL CE2 1 
ATOM   11533 C CZ  . TYR H 3 198 ? 3.845   -50.884 53.679  1.000 140.828 ? 198 TYR LLL CZ  1 
ATOM   11534 O OH  . TYR H 3 198 ? 4.854   -51.468 52.974  1.000 142.183 ? 198 TYR LLL OH  1 
ATOM   11535 N N   . ALA H 3 199 ? -0.045  -45.925 57.239  1.000 142.784 ? 199 ALA LLL N   1 
ATOM   11536 C CA  . ALA H 3 199 ? -0.960  -44.971 57.910  1.000 143.464 ? 199 ALA LLL CA  1 
ATOM   11537 C C   . ALA H 3 199 ? -1.591  -44.000 56.906  1.000 140.895 ? 199 ALA LLL C   1 
ATOM   11538 O O   . ALA H 3 199 ? -1.053  -43.845 55.801  1.000 140.822 ? 199 ALA LLL O   1 
ATOM   11539 C CB  . ALA H 3 199 ? -0.209  -44.234 58.991  1.000 147.341 ? 199 ALA LLL CB  1 
ATOM   11540 N N   . CYS H 3 200 ? -2.686  -43.357 57.320  1.000 141.296 ? 200 CYS LLL N   1 
ATOM   11541 C CA  . CYS H 3 200 ? -3.565  -42.500 56.485  1.000 140.630 ? 200 CYS LLL CA  1 
ATOM   11542 C C   . CYS H 3 200 ? -3.987  -41.259 57.288  1.000 140.622 ? 200 CYS LLL C   1 
ATOM   11543 O O   . CYS H 3 200 ? -4.962  -41.351 58.049  1.000 141.661 ? 200 CYS LLL O   1 
ATOM   11544 C CB  . CYS H 3 200 ? -4.771  -43.307 56.012  1.000 142.227 ? 200 CYS LLL CB  1 
ATOM   11545 S SG  . CYS H 3 200 ? -5.768  -42.459 54.758  1.000 147.730 ? 200 CYS LLL SG  1 
ATOM   11546 N N   . GLU H 3 201 ? -3.265  -40.145 57.121  1.000 141.866 ? 201 GLU LLL N   1 
ATOM   11547 C CA  . GLU H 3 201 ? -3.492  -38.846 57.819  1.000 146.636 ? 201 GLU LLL CA  1 
ATOM   11548 C C   . GLU H 3 201 ? -4.506  -38.019 57.014  1.000 145.503 ? 201 GLU LLL C   1 
ATOM   11549 O O   . GLU H 3 201 ? -4.250  -37.803 55.814  1.000 146.061 ? 201 GLU LLL O   1 
ATOM   11550 C CB  . GLU H 3 201 ? -2.156  -38.108 57.980  1.000 150.943 ? 201 GLU LLL CB  1 
ATOM   11551 C CG  . GLU H 3 201 ? -2.154  -37.007 59.036  1.000 156.060 ? 201 GLU LLL CG  1 
ATOM   11552 C CD  . GLU H 3 201 ? -0.885  -36.163 59.100  1.000 159.334 ? 201 GLU LLL CD  1 
ATOM   11553 O OE1 . GLU H 3 201 ? -0.431  -35.695 58.032  1.000 159.602 ? 201 GLU LLL OE1 1 
ATOM   11554 O OE2 . GLU H 3 201 ? -0.358  -35.962 60.216  1.000 161.618 ? 201 GLU LLL OE2 1 
ATOM   11555 N N   . VAL H 3 202 ? -5.593  -37.561 57.653  1.000 146.378 ? 202 VAL LLL N   1 
ATOM   11556 C CA  . VAL H 3 202 ? -6.764  -36.894 56.999  1.000 144.945 ? 202 VAL LLL CA  1 
ATOM   11557 C C   . VAL H 3 202 ? -7.042  -35.535 57.660  1.000 149.115 ? 202 VAL LLL C   1 
ATOM   11558 O O   . VAL H 3 202 ? -7.523  -35.530 58.811  1.000 152.012 ? 202 VAL LLL O   1 
ATOM   11559 C CB  . VAL H 3 202 ? -8.020  -37.784 57.065  1.000 142.464 ? 202 VAL LLL CB  1 
ATOM   11560 C CG1 . VAL H 3 202 ? -9.222  -37.096 56.438  1.000 141.287 ? 202 VAL LLL CG1 1 
ATOM   11561 C CG2 . VAL H 3 202 ? -7.787  -39.147 56.432  1.000 139.180 ? 202 VAL LLL CG2 1 
ATOM   11562 N N   . THR H 3 203 ? -6.809  -34.432 56.935  1.000 150.804 ? 203 THR LLL N   1 
ATOM   11563 C CA  . THR H 3 203 ? -7.172  -33.043 57.340  1.000 155.118 ? 203 THR LLL CA  1 
ATOM   11564 C C   . THR H 3 203 ? -8.419  -32.597 56.567  1.000 154.880 ? 203 THR LLL C   1 
ATOM   11565 O O   . THR H 3 203 ? -8.261  -32.113 55.426  1.000 156.603 ? 203 THR LLL O   1 
ATOM   11566 C CB  . THR H 3 203 ? -6.008  -32.062 57.123  1.000 156.650 ? 203 THR LLL CB  1 
ATOM   11567 O OG1 . THR H 3 203 ? -5.038  -32.327 58.138  1.000 160.253 ? 203 THR LLL OG1 1 
ATOM   11568 C CG2 . THR H 3 203 ? -6.414  -30.604 57.194  1.000 159.353 ? 203 THR LLL CG2 1 
ATOM   11569 N N   . HIS H 3 204 ? -9.606  -32.741 57.167  1.000 155.538 ? 204 HIS LLL N   1 
ATOM   11570 C CA  . HIS H 3 204 ? -10.885 -32.229 56.606  1.000 154.452 ? 204 HIS LLL CA  1 
ATOM   11571 C C   . HIS H 3 204 ? -11.423 -31.074 57.453  1.000 158.580 ? 204 HIS LLL C   1 
ATOM   11572 O O   . HIS H 3 204 ? -11.259 -31.111 58.692  1.000 163.333 ? 204 HIS LLL O   1 
ATOM   11573 C CB  . HIS H 3 204 ? -11.940 -33.331 56.480  1.000 152.632 ? 204 HIS LLL CB  1 
ATOM   11574 C CG  . HIS H 3 204 ? -13.159 -32.855 55.767  1.000 151.984 ? 204 HIS LLL CG  1 
ATOM   11575 N ND1 . HIS H 3 204 ? -14.426 -32.971 56.300  1.000 154.211 ? 204 HIS LLL ND1 1 
ATOM   11576 C CD2 . HIS H 3 204 ? -13.300 -32.216 54.585  1.000 150.269 ? 204 HIS LLL CD2 1 
ATOM   11577 C CE1 . HIS H 3 204 ? -15.297 -32.446 55.463  1.000 153.536 ? 204 HIS LLL CE1 1 
ATOM   11578 N NE2 . HIS H 3 204 ? -14.632 -31.976 54.404  1.000 151.383 ? 204 HIS LLL NE2 1 
ATOM   11579 N N   . GLN H 3 205 ? -12.071 -30.111 56.791  1.000 157.436 ? 205 GLN LLL N   1 
ATOM   11580 C CA  . GLN H 3 205 ? -12.687 -28.902 57.401  1.000 160.030 ? 205 GLN LLL CA  1 
ATOM   11581 C C   . GLN H 3 205 ? -13.581 -29.296 58.578  1.000 161.608 ? 205 GLN LLL C   1 
ATOM   11582 O O   . GLN H 3 205 ? -13.640 -28.518 59.538  1.000 165.776 ? 205 GLN LLL O   1 
ATOM   11583 C CB  . GLN H 3 205 ? -13.509 -28.154 56.359  1.000 158.811 ? 205 GLN LLL CB  1 
ATOM   11584 C CG  . GLN H 3 205 ? -14.021 -26.814 56.849  1.000 162.669 ? 205 GLN LLL CG  1 
ATOM   11585 C CD  . GLN H 3 205 ? -14.262 -25.890 55.684  1.000 161.588 ? 205 GLN LLL CD  1 
ATOM   11586 O OE1 . GLN H 3 205 ? -14.200 -26.286 54.519  1.000 155.825 ? 205 GLN LLL OE1 1 
ATOM   11587 N NE2 . GLN H 3 205 ? -14.530 -24.636 55.998  1.000 165.639 ? 205 GLN LLL NE2 1 
ATOM   11588 N N   . GLY H 3 206 ? -14.265 -30.439 58.480  1.000 159.493 ? 206 GLY LLL N   1 
ATOM   11589 C CA  . GLY H 3 206 ? -15.121 -30.998 59.543  1.000 164.031 ? 206 GLY LLL CA  1 
ATOM   11590 C C   . GLY H 3 206 ? -14.343 -31.278 60.821  1.000 169.321 ? 206 GLY LLL C   1 
ATOM   11591 O O   . GLY H 3 206 ? -14.862 -30.952 61.916  1.000 175.649 ? 206 GLY LLL O   1 
ATOM   11592 N N   . LEU H 3 207 ? -13.138 -31.842 60.700  1.000 168.449 ? 207 LEU LLL N   1 
ATOM   11593 C CA  . LEU H 3 207 ? -12.338 -32.343 61.848  1.000 172.294 ? 207 LEU LLL CA  1 
ATOM   11594 C C   . LEU H 3 207 ? -11.419 -31.247 62.389  1.000 175.357 ? 207 LEU LLL C   1 
ATOM   11595 O O   . LEU H 3 207 ? -10.489 -30.832 61.664  1.000 172.135 ? 207 LEU LLL O   1 
ATOM   11596 C CB  . LEU H 3 207 ? -11.540 -33.566 61.396  1.000 169.237 ? 207 LEU LLL CB  1 
ATOM   11597 C CG  . LEU H 3 207 ? -12.382 -34.828 61.240  1.000 169.348 ? 207 LEU LLL CG  1 
ATOM   11598 C CD1 . LEU H 3 207 ? -11.681 -35.840 60.344  1.000 164.341 ? 207 LEU LLL CD1 1 
ATOM   11599 C CD2 . LEU H 3 207 ? -12.708 -35.422 62.609  1.000 175.563 ? 207 LEU LLL CD2 1 
ATOM   11600 N N   . SER H 3 208 ? -11.682 -30.825 63.631  1.000 181.064 ? 208 SER LLL N   1 
ATOM   11601 C CA  . SER H 3 208 ? -10.851 -29.892 64.433  1.000 185.675 ? 208 SER LLL CA  1 
ATOM   11602 C C   . SER H 3 208 ? -9.375  -30.280 64.294  1.000 183.073 ? 208 SER LLL C   1 
ATOM   11603 O O   . SER H 3 208 ? -8.655  -29.595 63.538  1.000 181.894 ? 208 SER LLL O   1 
ATOM   11604 C CB  . SER H 3 208 ? -11.300 -29.893 65.874  1.000 192.096 ? 208 SER LLL CB  1 
ATOM   11605 O OG  . SER H 3 208 ? -11.545 -31.220 66.320  1.000 190.508 ? 208 SER LLL OG  1 
ATOM   11606 N N   . SER H 3 209 ? -8.960  -31.356 64.972  1.000 181.996 ? 209 SER LLL N   1 
ATOM   11607 C CA  . SER H 3 209 ? -7.587  -31.923 64.908  1.000 179.605 ? 209 SER LLL CA  1 
ATOM   11608 C C   . SER H 3 209 ? -7.543  -33.014 63.840  1.000 173.235 ? 209 SER LLL C   1 
ATOM   11609 O O   . SER H 3 209 ? -8.428  -33.867 63.799  1.000 173.054 ? 209 SER LLL O   1 
ATOM   11610 C CB  . SER H 3 209 ? -7.150  -32.443 66.248  1.000 183.003 ? 209 SER LLL CB  1 
ATOM   11611 O OG  . SER H 3 209 ? -5.737  -32.554 66.303  1.000 181.839 ? 209 SER LLL OG  1 
ATOM   11612 N N   . PRO H 3 210 ? -6.528  -33.013 62.940  1.000 168.195 ? 210 PRO LLL N   1 
ATOM   11613 C CA  . PRO H 3 210 ? -6.403  -34.041 61.903  1.000 161.200 ? 210 PRO LLL CA  1 
ATOM   11614 C C   . PRO H 3 210 ? -6.522  -35.474 62.442  1.000 159.884 ? 210 PRO LLL C   1 
ATOM   11615 O O   . PRO H 3 210 ? -6.149  -35.706 63.574  1.000 163.460 ? 210 PRO LLL O   1 
ATOM   11616 C CB  . PRO H 3 210 ? -4.994  -33.807 61.344  1.000 160.181 ? 210 PRO LLL CB  1 
ATOM   11617 C CG  . PRO H 3 210 ? -4.776  -32.326 61.540  1.000 164.613 ? 210 PRO LLL CG  1 
ATOM   11618 C CD  . PRO H 3 210 ? -5.458  -32.005 62.855  1.000 169.819 ? 210 PRO LLL CD  1 
ATOM   11619 N N   . VAL H 3 211 ? -7.036  -36.386 61.613  1.000 156.010 ? 211 VAL LLL N   1 
ATOM   11620 C CA  . VAL H 3 211 ? -7.334  -37.805 61.977  1.000 156.865 ? 211 VAL LLL CA  1 
ATOM   11621 C C   . VAL H 3 211 ? -6.362  -38.734 61.246  1.000 154.887 ? 211 VAL LLL C   1 
ATOM   11622 O O   . VAL H 3 211 ? -6.383  -38.725 60.004  1.000 154.916 ? 211 VAL LLL O   1 
ATOM   11623 C CB  . VAL H 3 211 ? -8.788  -38.172 61.623  1.000 155.465 ? 211 VAL LLL CB  1 
ATOM   11624 C CG1 . VAL H 3 211 ? -8.993  -39.681 61.562  1.000 153.278 ? 211 VAL LLL CG1 1 
ATOM   11625 C CG2 . VAL H 3 211 ? -9.775  -37.529 62.587  1.000 161.440 ? 211 VAL LLL CG2 1 
ATOM   11626 N N   . THR H 3 212 ? -5.587  -39.539 61.982  1.000 156.377 ? 212 THR LLL N   1 
ATOM   11627 C CA  . THR H 3 212 ? -4.729  -40.622 61.423  1.000 152.743 ? 212 THR LLL CA  1 
ATOM   11628 C C   . THR H 3 212 ? -5.318  -41.983 61.806  1.000 154.470 ? 212 THR LLL C   1 
ATOM   11629 O O   . THR H 3 212 ? -5.586  -42.196 63.006  1.000 163.292 ? 212 THR LLL O   1 
ATOM   11630 C CB  . THR H 3 212 ? -3.271  -40.516 61.890  1.000 152.911 ? 212 THR LLL CB  1 
ATOM   11631 O OG1 . THR H 3 212 ? -2.818  -39.170 61.737  1.000 152.379 ? 212 THR LLL OG1 1 
ATOM   11632 C CG2 . THR H 3 212 ? -2.356  -41.442 61.118  1.000 150.165 ? 212 THR LLL CG2 1 
ATOM   11633 N N   . LYS H 3 213 ? -5.530  -42.847 60.814  1.000 151.193 ? 213 LYS LLL N   1 
ATOM   11634 C CA  . LYS H 3 213 ? -5.911  -44.270 60.992  1.000 154.128 ? 213 LYS LLL CA  1 
ATOM   11635 C C   . LYS H 3 213 ? -4.837  -45.114 60.308  1.000 152.077 ? 213 LYS LLL C   1 
ATOM   11636 O O   . LYS H 3 213 ? -4.473  -44.763 59.181  1.000 150.370 ? 213 LYS LLL O   1 
ATOM   11637 C CB  . LYS H 3 213 ? -7.307  -44.523 60.416  1.000 155.408 ? 213 LYS LLL CB  1 
ATOM   11638 C CG  . LYS H 3 213 ? -8.450  -43.891 61.206  1.000 161.651 ? 213 LYS LLL CG  1 
ATOM   11639 C CD  . LYS H 3 213 ? -9.172  -44.830 62.167  1.000 167.653 ? 213 LYS LLL CD  1 
ATOM   11640 C CE  . LYS H 3 213 ? -10.148 -45.753 61.461  1.000 167.927 ? 213 LYS LLL CE  1 
ATOM   11641 N NZ  . LYS H 3 213 ? -11.300 -46.125 62.319  1.000 172.924 ? 213 LYS LLL NZ  1 
ATOM   11642 N N   . SER H 3 214 ? -4.338  -46.161 60.972  1.000 156.428 ? 214 SER LLL N   1 
ATOM   11643 C CA  . SER H 3 214 ? -3.133  -46.929 60.555  1.000 156.942 ? 214 SER LLL CA  1 
ATOM   11644 C C   . SER H 3 214 ? -3.204  -48.390 61.019  1.000 158.730 ? 214 SER LLL C   1 
ATOM   11645 O O   . SER H 3 214 ? -4.029  -48.700 61.907  1.000 163.270 ? 214 SER LLL O   1 
ATOM   11646 C CB  . SER H 3 214 ? -1.876  -46.273 61.078  1.000 159.205 ? 214 SER LLL CB  1 
ATOM   11647 O OG  . SER H 3 214 ? -1.653  -46.598 62.445  1.000 164.590 ? 214 SER LLL OG  1 
ATOM   11648 N N   . PHE H 3 215 ? -2.341  -49.235 60.445  1.000 156.237 ? 215 PHE LLL N   1 
ATOM   11649 C CA  . PHE H 3 215 ? -2.057  -50.621 60.897  1.000 157.876 ? 215 PHE LLL CA  1 
ATOM   11650 C C   . PHE H 3 215 ? -0.556  -50.898 60.770  1.000 158.368 ? 215 PHE LLL C   1 
ATOM   11651 O O   . PHE H 3 215 ? 0.073   -50.487 59.775  1.000 155.962 ? 215 PHE LLL O   1 
ATOM   11652 C CB  . PHE H 3 215 ? -2.863  -51.642 60.089  1.000 156.620 ? 215 PHE LLL CB  1 
ATOM   11653 C CG  . PHE H 3 215 ? -2.486  -51.739 58.632  1.000 152.793 ? 215 PHE LLL CG  1 
ATOM   11654 C CD1 . PHE H 3 215 ? -3.006  -50.855 57.700  1.000 147.727 ? 215 PHE LLL CD1 1 
ATOM   11655 C CD2 . PHE H 3 215 ? -1.608  -52.717 58.190  1.000 154.104 ? 215 PHE LLL CD2 1 
ATOM   11656 C CE1 . PHE H 3 215 ? -2.658  -50.951 56.362  1.000 144.982 ? 215 PHE LLL CE1 1 
ATOM   11657 C CE2 . PHE H 3 215 ? -1.258  -52.808 56.851  1.000 150.586 ? 215 PHE LLL CE2 1 
ATOM   11658 C CZ  . PHE H 3 215 ? -1.781  -51.922 55.942  1.000 146.212 ? 215 PHE LLL CZ  1 
ATOM   11659 N N   . ASN H 3 216 ? 0.006   -51.572 61.770  1.000 163.662 ? 216 ASN LLL N   1 
ATOM   11660 C CA  . ASN H 3 216 ? 1.304   -52.279 61.640  1.000 164.899 ? 216 ASN LLL CA  1 
ATOM   11661 C C   . ASN H 3 216 ? 1.011   -53.538 60.823  1.000 162.237 ? 216 ASN LLL C   1 
ATOM   11662 O O   . ASN H 3 216 ? -0.129  -54.032 60.892  1.000 159.386 ? 216 ASN LLL O   1 
ATOM   11663 C CB  . ASN H 3 216 ? 1.943   -52.555 63.006  1.000 171.649 ? 216 ASN LLL CB  1 
ATOM   11664 C CG  . ASN H 3 216 ? 2.085   -51.308 63.857  1.000 174.638 ? 216 ASN LLL CG  1 
ATOM   11665 O OD1 . ASN H 3 216 ? 1.178   -50.478 63.910  1.000 175.311 ? 216 ASN LLL OD1 1 
ATOM   11666 N ND2 . ASN H 3 216 ? 3.214   -51.164 64.534  1.000 178.375 ? 216 ASN LLL ND2 1 
ATOM   11667 N N   . ARG H 3 217 ? 1.985   -54.007 60.044  1.000 161.766 ? 217 ARG LLL N   1 
ATOM   11668 C CA  . ARG H 3 217 ? 1.858   -55.220 59.196  1.000 163.033 ? 217 ARG LLL CA  1 
ATOM   11669 C C   . ARG H 3 217 ? 1.789   -56.455 60.104  1.000 169.586 ? 217 ARG LLL C   1 
ATOM   11670 O O   . ARG H 3 217 ? 2.486   -56.458 61.145  1.000 171.681 ? 217 ARG LLL O   1 
ATOM   11671 C CB  . ARG H 3 217 ? 3.037   -55.281 58.225  1.000 160.910 ? 217 ARG LLL CB  1 
ATOM   11672 C CG  . ARG H 3 217 ? 2.824   -56.194 57.031  1.000 161.422 ? 217 ARG LLL CG  1 
ATOM   11673 C CD  . ARG H 3 217 ? 3.653   -55.696 55.859  1.000 161.631 ? 217 ARG LLL CD  1 
ATOM   11674 N NE  . ARG H 3 217 ? 5.043   -55.501 56.234  1.000 164.995 ? 217 ARG LLL NE  1 
ATOM   11675 C CZ  . ARG H 3 217 ? 5.974   -56.450 56.221  1.000 170.052 ? 217 ARG LLL CZ  1 
ATOM   11676 N NH1 . ARG H 3 217 ? 5.675   -57.680 55.833  1.000 171.737 ? 217 ARG LLL NH1 1 
ATOM   11677 N NH2 . ARG H 3 217 ? 7.210   -56.163 56.597  1.000 173.785 ? 217 ARG LLL NH2 1 
ATOM   11678 N N   . GLY H 3 218 ? 0.960   -57.442 59.741  1.000 174.387 ? 218 GLY LLL N   1 
ATOM   11679 C CA  . GLY H 3 218 ? 0.736   -58.683 60.514  1.000 183.077 ? 218 GLY LLL CA  1 
ATOM   11680 C C   . GLY H 3 218 ? -0.343  -58.550 61.587  1.000 190.406 ? 218 GLY LLL C   1 
ATOM   11681 O O   . GLY H 3 218 ? -0.394  -59.426 62.479  1.000 196.423 ? 218 GLY LLL O   1 
ATOM   11682 N N   . GLU H 3 219 ? -1.191  -57.518 61.495  1.000 192.264 ? 219 GLU LLL N   1 
ATOM   11683 C CA  . GLU H 3 219 ? -2.274  -57.208 62.470  1.000 196.210 ? 219 GLU LLL CA  1 
ATOM   11684 C C   . GLU H 3 219 ? -3.455  -56.590 61.706  1.000 194.016 ? 219 GLU LLL C   1 
ATOM   11685 O O   . GLU H 3 219 ? -4.588  -56.519 62.179  1.000 197.224 ? 219 GLU LLL O   1 
ATOM   11686 C CB  . GLU H 3 219 ? -1.758  -56.251 63.550  1.000 197.040 ? 219 GLU LLL CB  1 
ATOM   11687 C CG  . GLU H 3 219 ? -0.716  -56.852 64.486  1.000 200.887 ? 219 GLU LLL CG  1 
ATOM   11688 C CD  . GLU H 3 219 ? 0.325   -55.873 65.014  1.000 200.296 ? 219 GLU LLL CD  1 
ATOM   11689 O OE1 . GLU H 3 219 ? -0.049  -54.735 65.368  1.000 198.426 ? 219 GLU LLL OE1 1 
ATOM   11690 O OE2 . GLU H 3 219 ? 1.516   -56.248 65.071  1.000 200.850 ? 219 GLU LLL OE2 1 
HETATM 11691 C C1  . NAG I 5 .   ? -46.604 -23.702 46.517  1.000 162.826 ? 601 NAG AAA C1  1 
HETATM 11692 C C2  . NAG I 5 .   ? -46.738 -23.771 45.003  1.000 169.758 ? 601 NAG AAA C2  1 
HETATM 11693 C C3  . NAG I 5 .   ? -45.398 -24.212 44.414  1.000 174.188 ? 601 NAG AAA C3  1 
HETATM 11694 C C4  . NAG I 5 .   ? -44.274 -23.260 44.855  1.000 176.299 ? 601 NAG AAA C4  1 
HETATM 11695 C C5  . NAG I 5 .   ? -44.298 -22.996 46.363  1.000 176.468 ? 601 NAG AAA C5  1 
HETATM 11696 C C6  . NAG I 5 .   ? -43.338 -21.857 46.723  1.000 176.748 ? 601 NAG AAA C6  1 
HETATM 11697 C C7  . NAG I 5 .   ? -48.931 -24.204 44.000  1.000 169.592 ? 601 NAG AAA C7  1 
HETATM 11698 C C8  . NAG I 5 .   ? -49.904 -25.260 43.572  1.000 170.443 ? 601 NAG AAA C8  1 
HETATM 11699 N N2  . NAG I 5 .   ? -47.818 -24.655 44.591  1.000 168.759 ? 601 NAG AAA N2  1 
HETATM 11700 O O3  . NAG I 5 .   ? -45.500 -24.248 42.983  1.000 172.489 ? 601 NAG AAA O3  1 
HETATM 11701 O O4  . NAG I 5 .   ? -42.980 -23.788 44.522  1.000 176.231 ? 601 NAG AAA O4  1 
HETATM 11702 O O5  . NAG I 5 .   ? -45.628 -22.693 46.811  1.000 172.556 ? 601 NAG AAA O5  1 
HETATM 11703 O O6  . NAG I 5 .   ? -44.040 -20.776 47.350  1.000 179.786 ? 601 NAG AAA O6  1 
HETATM 11704 O O7  . NAG I 5 .   ? -49.160 -23.019 43.796  1.000 167.648 ? 601 NAG AAA O7  1 
HETATM 11705 C C1  . NAG J 5 .   ? -53.147 -30.231 -1.459  1.000 140.670 ? 601 NAG EEE C1  1 
HETATM 11706 C C2  . NAG J 5 .   ? -53.180 -30.147 0.059   1.000 148.025 ? 601 NAG EEE C2  1 
HETATM 11707 C C3  . NAG J 5 .   ? -52.705 -31.489 0.604   1.000 152.248 ? 601 NAG EEE C3  1 
HETATM 11708 C C4  . NAG J 5 .   ? -53.722 -32.537 0.138   1.000 153.692 ? 601 NAG EEE C4  1 
HETATM 11709 C C5  . NAG J 5 .   ? -53.798 -32.524 -1.393  1.000 150.751 ? 601 NAG EEE C5  1 
HETATM 11710 C C6  . NAG J 5 .   ? -54.870 -33.461 -1.925  1.000 149.956 ? 601 NAG EEE C6  1 
HETATM 11711 C C7  . NAG J 5 .   ? -52.859 -28.141 1.403   1.000 154.050 ? 601 NAG EEE C7  1 
HETATM 11712 C C8  . NAG J 5 .   ? -51.914 -27.036 1.768   1.000 156.024 ? 601 NAG EEE C8  1 
HETATM 11713 N N2  . NAG J 5 .   ? -52.380 -29.038 0.540   1.000 150.531 ? 601 NAG EEE N2  1 
HETATM 11714 O O3  . NAG J 5 .   ? -52.560 -31.444 2.031   1.000 150.463 ? 601 NAG EEE O3  1 
HETATM 11715 O O4  . NAG J 5 .   ? -53.375 -33.849 0.602   1.000 157.509 ? 601 NAG EEE O4  1 
HETATM 11716 O O5  . NAG J 5 .   ? -54.096 -31.211 -1.873  1.000 144.668 ? 601 NAG EEE O5  1 
HETATM 11717 O O6  . NAG J 5 .   ? -55.238 -33.024 -3.237  1.000 150.409 ? 601 NAG EEE O6  1 
HETATM 11718 O O7  . NAG J 5 .   ? -53.987 -28.195 1.871   1.000 156.008 ? 601 NAG EEE O7  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   . ASN A 5   ? 2.784 2.286 3.264 0.569  0.643  0.449  334 ASN AAA N   
2     C CA  . ASN A 5   ? 2.657 2.300 3.086 0.559  0.541  0.430  334 ASN AAA CA  
3     C C   . ASN A 5   ? 2.590 2.264 2.980 0.507  0.526  0.406  334 ASN AAA C   
4     O O   . ASN A 5   ? 2.612 2.293 2.889 0.523  0.495  0.452  334 ASN AAA O   
5     C CB  . ASN A 5   ? 2.703 2.373 3.032 0.626  0.489  0.498  334 ASN AAA CB  
6     C CG  . ASN A 5   ? 2.868 2.416 3.114 0.689  0.540  0.587  334 ASN AAA CG  
7     O OD1 . ASN A 5   ? 2.933 2.392 3.131 0.678  0.592  0.613  334 ASN AAA OD1 
8     N ND2 . ASN A 5   ? 2.934 2.473 3.161 0.760  0.528  0.635  334 ASN AAA ND2 
9     N N   . LEU A 6   ? 2.517 2.213 3.000 0.448  0.546  0.332  335 LEU AAA N   
10    C CA  . LEU A 6   ? 2.458 2.195 2.929 0.397  0.531  0.295  335 LEU AAA CA  
11    C C   . LEU A 6   ? 2.343 2.214 2.849 0.367  0.462  0.232  335 LEU AAA C   
12    O O   . LEU A 6   ? 2.321 2.225 2.923 0.355  0.467  0.175  335 LEU AAA O   
13    C CB  . LEU A 6   ? 2.494 2.156 3.053 0.359  0.612  0.257  335 LEU AAA CB  
14    C CG  . LEU A 6   ? 2.405 2.130 3.009 0.302  0.599  0.190  335 LEU AAA CG  
15    C CD1 . LEU A 6   ? 2.388 2.132 2.880 0.297  0.564  0.226  335 LEU AAA CD1 
16    C CD2 . LEU A 6   ? 2.446 2.101 3.156 0.268  0.683  0.147  335 LEU AAA CD2 
17    N N   . CYS A 7   ? 2.304 2.242 2.733 0.357  0.406  0.239  336 CYS AAA N   
18    C CA  . CYS A 7   ? 2.194 2.252 2.632 0.339  0.342  0.196  336 CYS AAA CA  
19    C C   . CYS A 7   ? 2.107 2.204 2.643 0.302  0.353  0.118  336 CYS AAA C   
20    O O   . CYS A 7   ? 2.091 2.178 2.649 0.271  0.375  0.091  336 CYS AAA O   
21    C CB  . CYS A 7   ? 2.176 2.278 2.527 0.325  0.300  0.211  336 CYS AAA CB  
22    S SG  . CYS A 7   ? 2.266 2.364 2.499 0.367  0.265  0.284  336 CYS AAA SG  
23    N N   . PRO A 8   ? 2.049 2.199 2.648 0.307  0.338  0.076  337 PRO AAA N   
24    C CA  . PRO A 8   ? 2.000 2.196 2.690 0.278  0.346  -0.003 337 PRO AAA CA  
25    C C   . PRO A 8   ? 1.904 2.198 2.564 0.260  0.294  -0.035 337 PRO AAA C   
26    O O   . PRO A 8   ? 1.860 2.223 2.522 0.268  0.261  -0.058 337 PRO AAA O   
27    C CB  . PRO A 8   ? 2.014 2.221 2.766 0.299  0.351  -0.025 337 PRO AAA CB  
28    C CG  . PRO A 8   ? 2.009 2.238 2.687 0.333  0.311  0.032  337 PRO AAA CG  
29    C CD  . PRO A 8   ? 2.051 2.226 2.640 0.342  0.311  0.100  337 PRO AAA CD  
30    N N   . PHE A 9   ? 1.900 2.191 2.529 0.239  0.295  -0.033 338 PHE AAA N   
31    C CA  . PHE A 9   ? 1.854 2.227 2.472 0.221  0.260  -0.072 338 PHE AAA CA  
32    C C   . PHE A 9   ? 1.846 2.259 2.564 0.206  0.273  -0.153 338 PHE AAA C   
33    O O   . PHE A 9   ? 1.787 2.283 2.504 0.204  0.239  -0.195 338 PHE AAA O   
34    C CB  . PHE A 9   ? 1.876 2.226 2.436 0.207  0.262  -0.041 338 PHE AAA CB  
35    C CG  . PHE A 9   ? 1.901 2.227 2.363 0.220  0.243  0.026  338 PHE AAA CG  
36    C CD1 . PHE A 9   ? 1.853 2.236 2.270 0.233  0.201  0.039  338 PHE AAA CD1 
37    C CD2 . PHE A 9   ? 1.974 2.224 2.388 0.219  0.270  0.073  338 PHE AAA CD2 
38    C CE1 . PHE A 9   ? 1.869 2.242 2.208 0.243  0.182  0.089  338 PHE AAA CE1 
39    C CE2 . PHE A 9   ? 1.996 2.236 2.319 0.233  0.248  0.127  338 PHE AAA CE2 
40    C CZ  . PHE A 9   ? 1.942 2.248 2.233 0.244  0.203  0.131  338 PHE AAA CZ  
41    N N   . GLY A 10  ? 1.919 2.272 2.718 0.198  0.324  -0.175 339 GLY AAA N   
42    C CA  . GLY A 10  ? 1.930 2.317 2.844 0.181  0.344  -0.262 339 GLY AAA CA  
43    C C   . GLY A 10  ? 1.888 2.368 2.816 0.193  0.304  -0.313 339 GLY AAA C   
44    O O   . GLY A 10  ? 1.871 2.429 2.843 0.183  0.286  -0.384 339 GLY AAA O   
45    N N   . GLU A 11  ? 1.879 2.356 2.769 0.217  0.289  -0.278 340 GLU AAA N   
46    C CA  . GLU A 11  ? 1.842 2.397 2.742 0.230  0.259  -0.322 340 GLU AAA CA  
47    C C   . GLU A 11  ? 1.767 2.387 2.568 0.243  0.208  -0.294 340 GLU AAA C   
48    O O   . GLU A 11  ? 1.751 2.413 2.532 0.261  0.188  -0.299 340 GLU AAA O   
49    C CB  . GLU A 11  ? 1.895 2.405 2.828 0.248  0.283  -0.307 340 GLU AAA CB  
50    C CG  . GLU A 11  ? 1.913 2.380 2.770 0.271  0.273  -0.220 340 GLU AAA CG  
51    C CD  . GLU A 11  ? 1.964 2.391 2.860 0.295  0.295  -0.203 340 GLU AAA CD  
52    O OE1 . GLU A 11  ? 1.945 2.417 2.814 0.315  0.266  -0.193 340 GLU AAA OE1 
53    O OE2 . GLU A 11  ? 2.029 2.375 2.981 0.296  0.345  -0.199 340 GLU AAA OE2 
54    N N   . VAL A 12  ? 1.719 2.343 2.464 0.235  0.193  -0.267 341 VAL AAA N   
55    C CA  . VAL A 12  ? 1.664 2.342 2.321 0.245  0.154  -0.244 341 VAL AAA CA  
56    C C   . VAL A 12  ? 1.649 2.379 2.310 0.238  0.140  -0.286 341 VAL AAA C   
57    O O   . VAL A 12  ? 1.631 2.436 2.275 0.254  0.115  -0.321 341 VAL AAA O   
58    C CB  . VAL A 12  ? 1.638 2.270 2.219 0.245  0.150  -0.167 341 VAL AAA CB  
59    C CG1 . VAL A 12  ? 1.584 2.262 2.087 0.250  0.120  -0.147 341 VAL AAA CG1 
60    C CG2 . VAL A 12  ? 1.663 2.258 2.241 0.259  0.156  -0.129 341 VAL AAA CG2 
61    N N   . PHE A 13  ? 1.679 2.371 2.362 0.220  0.159  -0.281 342 PHE AAA N   
62    C CA  . PHE A 13  ? 1.697 2.436 2.393 0.214  0.148  -0.317 342 PHE AAA CA  
63    C C   . PHE A 13  ? 1.751 2.555 2.543 0.213  0.147  -0.409 342 PHE AAA C   
64    O O   . PHE A 13  ? 1.737 2.629 2.514 0.232  0.113  -0.451 342 PHE AAA O   
65    C CB  . PHE A 13  ? 1.702 2.375 2.406 0.192  0.177  -0.287 342 PHE AAA CB  
66    C CG  . PHE A 13  ? 1.678 2.306 2.284 0.193  0.172  -0.209 342 PHE AAA CG  
67    C CD1 . PHE A 13  ? 1.695 2.260 2.263 0.195  0.183  -0.154 342 PHE AAA CD1 
68    C CD2 . PHE A 13  ? 1.650 2.303 2.204 0.195  0.155  -0.195 342 PHE AAA CD2 
69    C CE1 . PHE A 13  ? 1.691 2.227 2.174 0.196  0.175  -0.093 342 PHE AAA CE1 
70    C CE2 . PHE A 13  ? 1.649 2.261 2.120 0.192  0.153  -0.131 342 PHE AAA CE2 
71    C CZ  . PHE A 13  ? 1.669 2.227 2.105 0.191  0.162  -0.084 342 PHE AAA CZ  
72    N N   . ASN A 14  ? 1.840 2.599 2.725 0.193  0.186  -0.440 343 ASN AAA N   
73    C CA  . ASN A 14  ? 1.884 2.696 2.883 0.184  0.196  -0.539 343 ASN AAA CA  
74    C C   . ASN A 14  ? 1.838 2.700 2.839 0.202  0.178  -0.575 343 ASN AAA C   
75    O O   . ASN A 14  ? 1.849 2.766 2.940 0.196  0.181  -0.665 343 ASN AAA O   
76    C CB  . ASN A 14  ? 1.993 2.723 3.096 0.153  0.258  -0.555 343 ASN AAA CB  
77    C CG  . ASN A 14  ? 2.067 2.782 3.206 0.131  0.278  -0.562 343 ASN AAA CG  
78    O OD1 . ASN A 14  ? 2.018 2.819 3.215 0.126  0.259  -0.634 343 ASN AAA OD1 
79    N ND2 . ASN A 14  ? 2.283 2.895 3.390 0.120  0.316  -0.490 343 ASN AAA ND2 
80    N N   . ALA A 15  ? 1.769 2.615 2.681 0.223  0.161  -0.514 344 ALA AAA N   
81    C CA  . ALA A 15  ? 1.742 2.630 2.645 0.243  0.147  -0.541 344 ALA AAA CA  
82    C C   . ALA A 15  ? 1.715 2.716 2.630 0.257  0.114  -0.625 344 ALA AAA C   
83    O O   . ALA A 15  ? 1.679 2.730 2.535 0.272  0.083  -0.618 344 ALA AAA O   
84    C CB  . ALA A 15  ? 1.727 2.599 2.525 0.262  0.130  -0.464 344 ALA AAA CB  
85    N N   . THR A 16  ? 1.729 2.769 2.715 0.257  0.121  -0.702 345 THR AAA N   
86    C CA  . THR A 16  ? 1.730 2.886 2.745 0.271  0.091  -0.802 345 THR AAA CA  
87    C C   . THR A 16  ? 1.717 2.943 2.604 0.313  0.044  -0.778 345 THR AAA C   
88    O O   . THR A 16  ? 1.672 2.969 2.536 0.329  0.012  -0.805 345 THR AAA O   
89    C CB  . THR A 16  ? 1.765 2.937 2.870 0.263  0.112  -0.881 345 THR AAA CB  
90    O OG1 . THR A 16  ? 1.766 2.867 2.840 0.268  0.135  -0.823 345 THR AAA OG1 
91    C CG2 . THR A 16  ? 1.785 2.926 3.037 0.224  0.155  -0.946 345 THR AAA CG2 
92    N N   . ARG A 17  ? 1.758 2.963 2.570 0.331  0.045  -0.730 346 ARG AAA N   
93    C CA  . ARG A 17  ? 1.800 3.052 2.485 0.370  0.015  -0.697 346 ARG AAA CA  
94    C C   . ARG A 17  ? 1.798 2.976 2.405 0.367  0.024  -0.590 346 ARG AAA C   
95    O O   . ARG A 17  ? 1.811 2.910 2.453 0.343  0.051  -0.547 346 ARG AAA O   
96    C CB  . ARG A 17  ? 1.844 3.134 2.508 0.391  0.015  -0.733 346 ARG AAA CB  
97    C CG  . ARG A 17  ? 1.886 3.243 2.429 0.437  -0.013 -0.727 346 ARG AAA CG  
98    C CD  . ARG A 17  ? 1.937 3.317 2.447 0.458  -0.004 -0.751 346 ARG AAA CD  
99    N NE  . ARG A 17  ? 1.977 3.417 2.569 0.454  -0.007 -0.856 346 ARG AAA NE  
100   C CZ  . ARG A 17  ? 1.985 3.392 2.665 0.430  0.023  -0.889 346 ARG AAA CZ  
101   N NH1 . ARG A 17  ? 1.963 3.282 2.660 0.412  0.055  -0.822 346 ARG AAA NH1 
102   N NH2 . ARG A 17  ? 2.017 3.484 2.772 0.426  0.021  -0.994 346 ARG AAA NH2 
103   N N   . PHE A 18  ? 1.801 3.003 2.305 0.395  0.005  -0.550 347 PHE AAA N   
104   C CA  . PHE A 18  ? 1.777 2.920 2.204 0.393  0.015  -0.457 347 PHE AAA CA  
105   C C   . PHE A 18  ? 1.784 2.943 2.125 0.422  0.018  -0.433 347 PHE AAA C   
106   O O   . PHE A 18  ? 1.846 3.066 2.172 0.448  0.009  -0.486 347 PHE AAA O   
107   C CB  . PHE A 18  ? 1.802 2.947 2.185 0.399  0.002  -0.429 347 PHE AAA CB  
108   C CG  . PHE A 18  ? 1.804 2.884 2.235 0.363  0.016  -0.397 347 PHE AAA CG  
109   C CD1 . PHE A 18  ? 1.825 2.897 2.358 0.338  0.025  -0.444 347 PHE AAA CD1 
110   C CD2 . PHE A 18  ? 1.799 2.824 2.173 0.355  0.025  -0.324 347 PHE AAA CD2 
111   C CE1 . PHE A 18  ? 1.820 2.826 2.387 0.308  0.044  -0.412 347 PHE AAA CE1 
112   C CE2 . PHE A 18  ? 1.786 2.752 2.193 0.324  0.039  -0.296 347 PHE AAA CE2 
113   C CZ  . PHE A 18  ? 1.801 2.755 2.300 0.303  0.049  -0.337 347 PHE AAA CZ  
114   N N   . ALA A 19  ? 1.744 2.852 2.031 0.416  0.034  -0.360 348 ALA AAA N   
115   C CA  . ALA A 19  ? 1.751 2.861 1.966 0.437  0.050  -0.330 348 ALA AAA CA  
116   C C   . ALA A 19  ? 1.760 2.888 1.872 0.470  0.047  -0.303 348 ALA AAA C   
117   O O   . ALA A 19  ? 1.729 2.859 1.832 0.472  0.033  -0.295 348 ALA AAA O   
118   C CB  . ALA A 19  ? 1.728 2.777 1.958 0.410  0.071  -0.274 348 ALA AAA CB  
119   N N   . SER A 20  ? 1.779 2.920 1.818 0.499  0.064  -0.290 349 SER AAA N   
120   C CA  . SER A 20  ? 1.808 2.948 1.737 0.536  0.077  -0.249 349 SER AAA CA  
121   C C   . SER A 20  ? 1.732 2.802 1.649 0.509  0.106  -0.179 349 SER AAA C   
122   O O   . SER A 20  ? 1.675 2.714 1.644 0.475  0.122  -0.166 349 SER AAA O   
123   C CB  . SER A 20  ? 1.903 3.072 1.757 0.577  0.095  -0.258 349 SER AAA CB  
124   O OG  . SER A 20  ? 1.957 3.200 1.812 0.606  0.065  -0.329 349 SER AAA OG  
125   N N   . VAL A 21  ? 1.706 2.756 1.561 0.525  0.113  -0.140 350 VAL AAA N   
126   C CA  . VAL A 21  ? 1.651 2.637 1.506 0.494  0.137  -0.084 350 VAL AAA CA  
127   C C   . VAL A 21  ? 1.616 2.568 1.479 0.471  0.175  -0.058 350 VAL AAA C   
128   O O   . VAL A 21  ? 1.568 2.493 1.492 0.429  0.175  -0.048 350 VAL AAA O   
129   C CB  . VAL A 21  ? 1.701 2.670 1.477 0.524  0.150  -0.046 350 VAL AAA CB  
130   C CG1 . VAL A 21  ? 1.794 2.766 1.469 0.575  0.181  -0.026 350 VAL AAA CG1 
131   C CG2 . VAL A 21  ? 1.682 2.587 1.469 0.487  0.175  0.000  350 VAL AAA CG2 
132   N N   . TYR A 22  ? 1.651 2.607 1.454 0.500  0.208  -0.050 351 TYR AAA N   
133   C CA  . TYR A 22  ? 1.649 2.575 1.462 0.480  0.254  -0.027 351 TYR AAA CA  
134   C C   . TYR A 22  ? 1.585 2.530 1.493 0.449  0.239  -0.058 351 TYR AAA C   
135   O O   . TYR A 22  ? 1.547 2.474 1.494 0.422  0.266  -0.042 351 TYR AAA O   
136   C CB  . TYR A 22  ? 1.728 2.657 1.459 0.523  0.295  -0.019 351 TYR AAA CB  
137   C CG  . TYR A 22  ? 1.729 2.711 1.461 0.547  0.278  -0.067 351 TYR AAA CG  
138   C CD1 . TYR A 22  ? 1.739 2.771 1.446 0.580  0.234  -0.106 351 TYR AAA CD1 
139   C CD2 . TYR A 22  ? 1.715 2.701 1.481 0.535  0.305  -0.081 351 TYR AAA CD2 
140   C CE1 . TYR A 22  ? 1.743 2.828 1.457 0.599  0.218  -0.160 351 TYR AAA CE1 
141   C CE2 . TYR A 22  ? 1.725 2.758 1.496 0.556  0.291  -0.129 351 TYR AAA CE2 
142   C CZ  . TYR A 22  ? 1.737 2.818 1.480 0.587  0.248  -0.170 351 TYR AAA CZ  
143   O OH  . TYR A 22  ? 1.753 2.884 1.503 0.606  0.235  -0.226 351 TYR AAA OH  
144   N N   . ALA A 23  ? 1.567 2.551 1.513 0.456  0.201  -0.103 352 ALA AAA N   
145   C CA  . ALA A 23  ? 1.542 2.542 1.576 0.435  0.187  -0.135 352 ALA AAA CA  
146   C C   . ALA A 23  ? 1.500 2.490 1.602 0.408  0.152  -0.142 352 ALA AAA C   
147   O O   . ALA A 23  ? 1.480 2.487 1.643 0.406  0.134  -0.180 352 ALA AAA O   
148   C CB  . ALA A 23  ? 1.572 2.617 1.599 0.465  0.180  -0.185 352 ALA AAA CB  
149   N N   . TRP A 24  ? 1.494 2.450 1.586 0.389  0.150  -0.107 353 TRP AAA N   
150   C CA  . TRP A 24  ? 1.460 2.396 1.595 0.367  0.124  -0.105 353 TRP AAA CA  
151   C C   . TRP A 24  ? 1.431 2.359 1.645 0.348  0.115  -0.114 353 TRP AAA C   
152   O O   . TRP A 24  ? 1.421 2.353 1.656 0.343  0.128  -0.105 353 TRP AAA O   
153   C CB  . TRP A 24  ? 1.465 2.363 1.568 0.349  0.132  -0.063 353 TRP AAA CB  
154   C CG  . TRP A 24  ? 1.461 2.342 1.559 0.332  0.158  -0.033 353 TRP AAA CG  
155   C CD1 . TRP A 24  ? 1.502 2.378 1.552 0.342  0.194  -0.015 353 TRP AAA CD1 
156   C CD2 . TRP A 24  ? 1.428 2.296 1.575 0.302  0.153  -0.019 353 TRP AAA CD2 
157   N NE1 . TRP A 24  ? 1.496 2.358 1.574 0.314  0.213  0.001  353 TRP AAA NE1 
158   C CE2 . TRP A 24  ? 1.450 2.314 1.586 0.291  0.184  -0.002 353 TRP AAA CE2 
159   C CE3 . TRP A 24  ? 1.411 2.268 1.605 0.287  0.127  -0.020 353 TRP AAA CE3 
160   C CZ2 . TRP A 24  ? 1.448 2.313 1.628 0.264  0.182  0.005  353 TRP AAA CZ2 
161   C CZ3 . TRP A 24  ? 1.426 2.281 1.648 0.267  0.124  -0.005 353 TRP AAA CZ3 
162   C CH2 . TRP A 24  ? 1.432 2.298 1.652 0.255  0.148  0.003  353 TRP AAA CH2 
163   N N   . ASN A 25  ? 1.428 2.345 1.686 0.340  0.097  -0.131 354 ASN AAA N   
164   C CA  . ASN A 25  ? 1.431 2.335 1.762 0.332  0.092  -0.143 354 ASN AAA CA  
165   C C   . ASN A 25  ? 1.424 2.284 1.767 0.312  0.086  -0.104 354 ASN AAA C   
166   O O   . ASN A 25  ? 1.414 2.250 1.744 0.302  0.081  -0.097 354 ASN AAA O   
167   C CB  . ASN A 25  ? 1.444 2.362 1.820 0.340  0.087  -0.193 354 ASN AAA CB  
168   C CG  . ASN A 25  ? 1.466 2.399 1.897 0.349  0.095  -0.225 354 ASN AAA CG  
169   O OD1 . ASN A 25  ? 1.464 2.383 1.921 0.348  0.101  -0.203 354 ASN AAA OD1 
170   N ND2 . ASN A 25  ? 1.493 2.458 1.944 0.360  0.094  -0.282 354 ASN AAA ND2 
171   N N   . ARG A 26  ? 1.432 2.287 1.798 0.309  0.087  -0.081 355 ARG AAA N   
172   C CA  . ARG A 26  ? 1.435 2.256 1.804 0.297  0.077  -0.046 355 ARG AAA CA  
173   C C   . ARG A 26  ? 1.454 2.249 1.879 0.307  0.076  -0.049 355 ARG AAA C   
174   O O   . ARG A 26  ? 1.456 2.268 1.926 0.321  0.081  -0.068 355 ARG AAA O   
175   C CB  . ARG A 26  ? 1.434 2.277 1.799 0.292  0.074  -0.024 355 ARG AAA CB  
176   C CG  . ARG A 26  ? 1.436 2.258 1.804 0.287  0.058  0.006  355 ARG AAA CG  
177   C CD  . ARG A 26  ? 1.427 2.275 1.777 0.273  0.054  0.019  355 ARG AAA CD  
178   N NE  . ARG A 26  ? 1.417 2.251 1.715 0.252  0.065  0.026  355 ARG AAA NE  
179   C CZ  . ARG A 26  ? 1.422 2.263 1.700 0.232  0.066  0.036  355 ARG AAA CZ  
180   N NH1 . ARG A 26  ? 1.432 2.305 1.739 0.230  0.050  0.036  355 ARG AAA NH1 
181   N NH2 . ARG A 26  ? 1.422 2.240 1.654 0.216  0.082  0.042  355 ARG AAA NH2 
182   N N   . LYS A 27  ? 1.473 2.220 1.892 0.300  0.075  -0.028 356 LYS AAA N   
183   C CA  . LYS A 27  ? 1.517 2.219 1.977 0.312  0.082  -0.017 356 LYS AAA CA  
184   C C   . LYS A 27  ? 1.543 2.220 1.968 0.315  0.070  0.031  356 LYS AAA C   
185   O O   . LYS A 27  ? 1.512 2.171 1.888 0.299  0.068  0.048  356 LYS AAA O   
186   C CB  . LYS A 27  ? 1.543 2.204 2.027 0.303  0.101  -0.038 356 LYS AAA CB  
187   C CG  . LYS A 27  ? 1.594 2.207 2.137 0.317  0.124  -0.039 356 LYS AAA CG  
188   C CD  . LYS A 27  ? 1.604 2.244 2.211 0.324  0.135  -0.090 356 LYS AAA CD  
189   C CE  . LYS A 27  ? 1.655 2.241 2.329 0.339  0.164  -0.091 356 LYS AAA CE  
190   N NZ  . LYS A 27  ? 1.676 2.255 2.350 0.367  0.157  -0.050 356 LYS AAA NZ  
191   N N   . ARG A 28  ? 1.598 2.280 2.047 0.338  0.062  0.049  357 ARG AAA N   
192   C CA  . ARG A 28  ? 1.664 2.335 2.079 0.352  0.044  0.091  357 ARG AAA CA  
193   C C   . ARG A 28  ? 1.738 2.331 2.145 0.368  0.063  0.120  357 ARG AAA C   
194   O O   . ARG A 28  ? 1.783 2.350 2.233 0.396  0.075  0.128  357 ARG AAA O   
195   C CB  . ARG A 28  ? 1.686 2.408 2.136 0.377  0.025  0.095  357 ARG AAA CB  
196   C CG  . ARG A 28  ? 1.736 2.473 2.151 0.395  -0.004 0.129  357 ARG AAA CG  
197   C CD  . ARG A 28  ? 1.741 2.562 2.193 0.403  -0.028 0.113  357 ARG AAA CD  
198   N NE  . ARG A 28  ? 1.777 2.638 2.196 0.407  -0.061 0.127  357 ARG AAA NE  
199   C CZ  . ARG A 28  ? 1.869 2.729 2.272 0.447  -0.085 0.158  357 ARG AAA CZ  
200   N NH1 . ARG A 28  ? 1.934 2.742 2.348 0.486  -0.073 0.185  357 ARG AAA NH1 
201   N NH2 . ARG A 28  ? 1.896 2.809 2.270 0.449  -0.119 0.160  357 ARG AAA NH2 
202   N N   . ILE A 29  ? 1.762 2.314 2.119 0.351  0.070  0.137  358 ILE AAA N   
203   C CA  . ILE A 29  ? 1.828 2.296 2.165 0.364  0.096  0.170  358 ILE AAA CA  
204   C C   . ILE A 29  ? 1.880 2.344 2.164 0.396  0.074  0.218  358 ILE AAA C   
205   O O   . ILE A 29  ? 1.850 2.357 2.084 0.386  0.044  0.224  358 ILE AAA O   
206   C CB  . ILE A 29  ? 1.835 2.265 2.142 0.332  0.116  0.166  358 ILE AAA CB  
207   C CG1 . ILE A 29  ? 1.792 2.249 2.146 0.305  0.126  0.114  358 ILE AAA CG1 
208   C CG2 . ILE A 29  ? 1.920 2.257 2.215 0.344  0.154  0.197  358 ILE AAA CG2 
209   C CD1 . ILE A 29  ? 1.821 2.250 2.253 0.309  0.157  0.083  358 ILE AAA CD1 
210   N N   . SER A 30  ? 1.956 2.372 2.252 0.437  0.089  0.249  359 SER AAA N   
211   C CA  . SER A 30  ? 2.045 2.457 2.289 0.484  0.067  0.298  359 SER AAA CA  
212   C C   . SER A 30  ? 2.140 2.453 2.382 0.523  0.110  0.340  359 SER AAA C   
213   O O   . SER A 30  ? 2.136 2.401 2.446 0.514  0.152  0.320  359 SER AAA O   
214   C CB  . SER A 30  ? 2.033 2.535 2.311 0.507  0.025  0.286  359 SER AAA CB  
215   O OG  . SER A 30  ? 1.961 2.546 2.246 0.468  -0.003 0.247  359 SER AAA OG  
216   N N   . ASN A 31  ? 2.227 2.509 2.392 0.568  0.101  0.395  360 ASN AAA N   
217   C CA  . ASN A 31  ? 2.352 2.530 2.491 0.619  0.144  0.451  360 ASN AAA CA  
218   C C   . ASN A 31  ? 2.379 2.456 2.558 0.587  0.216  0.441  360 ASN AAA C   
219   O O   . ASN A 31  ? 2.385 2.411 2.638 0.599  0.259  0.435  360 ASN AAA O   
220   C CB  . ASN A 31  ? 2.379 2.574 2.565 0.675  0.134  0.469  360 ASN AAA CB  
221   C CG  . ASN A 31  ? 2.374 2.673 2.522 0.711  0.063  0.478  360 ASN AAA CG  
222   O OD1 . ASN A 31  ? 2.282 2.676 2.439 0.673  0.020  0.435  360 ASN AAA OD1 
223   N ND2 . ASN A 31  ? 2.472 2.752 2.579 0.785  0.054  0.532  360 ASN AAA ND2 
224   N N   . CYS A 32  ? 2.394 2.447 2.531 0.546  0.230  0.434  361 CYS AAA N   
225   C CA  . CYS A 32  ? 2.435 2.397 2.605 0.513  0.298  0.421  361 CYS AAA CA  
226   C C   . CYS A 32  ? 2.442 2.382 2.531 0.488  0.302  0.435  361 CYS AAA C   
227   O O   . CYS A 32  ? 2.399 2.414 2.430 0.478  0.248  0.431  361 CYS AAA O   
228   C CB  . CYS A 32  ? 2.359 2.367 2.638 0.464  0.303  0.348  361 CYS AAA CB  
229   S SG  . CYS A 32  ? 2.260 2.395 2.528 0.420  0.237  0.299  361 CYS AAA SG  
230   N N   . VAL A 33  ? 2.491 2.329 2.581 0.475  0.370  0.448  362 VAL AAA N   
231   C CA  . VAL A 33  ? 2.481 2.291 2.515 0.443  0.388  0.451  362 VAL AAA CA  
232   C C   . VAL A 33  ? 2.366 2.202 2.494 0.382  0.404  0.382  362 VAL AAA C   
233   O O   . VAL A 33  ? 2.348 2.158 2.577 0.371  0.443  0.349  362 VAL AAA O   
234   C CB  . VAL A 33  ? 2.640 2.318 2.610 0.471  0.457  0.511  362 VAL AAA CB  
235   C CG1 . VAL A 33  ? 2.657 2.300 2.587 0.432  0.487  0.506  362 VAL AAA CG1 
236   C CG2 . VAL A 33  ? 2.755 2.414 2.612 0.540  0.435  0.582  362 VAL AAA CG2 
237   N N   . ALA A 34  ? 2.290 2.178 2.389 0.347  0.375  0.359  363 ALA AAA N   
238   C CA  . ALA A 34  ? 2.209 2.132 2.383 0.296  0.384  0.297  363 ALA AAA CA  
239   C C   . ALA A 34  ? 2.237 2.107 2.367 0.274  0.419  0.309  363 ALA AAA C   
240   O O   . ALA A 34  ? 2.253 2.138 2.288 0.278  0.391  0.337  363 ALA AAA O   
241   C CB  . ALA A 34  ? 2.107 2.143 2.287 0.280  0.319  0.261  363 ALA AAA CB  
242   N N   . ASP A 35  ? 2.255 2.069 2.459 0.249  0.480  0.284  364 ASP AAA N   
243   C CA  . ASP A 35  ? 2.260 2.055 2.457 0.216  0.508  0.271  364 ASP AAA CA  
244   C C   . ASP A 35  ? 2.114 2.016 2.361 0.185  0.459  0.211  364 ASP AAA C   
245   O O   . ASP A 35  ? 2.069 2.009 2.424 0.168  0.465  0.154  364 ASP AAA O   
246   C CB  . ASP A 35  ? 2.356 2.058 2.624 0.199  0.594  0.260  364 ASP AAA CB  
247   C CG  . ASP A 35  ? 2.413 2.068 2.640 0.177  0.633  0.272  364 ASP AAA CG  
248   O OD1 . ASP A 35  ? 2.363 2.078 2.540 0.164  0.588  0.266  364 ASP AAA OD1 
249   O OD2 . ASP A 35  ? 2.515 2.068 2.761 0.174  0.713  0.289  364 ASP AAA OD2 
250   N N   . TYR A 36  ? 2.048 2.002 2.218 0.183  0.411  0.224  365 TYR AAA N   
251   C CA  . TYR A 36  ? 1.930 1.977 2.128 0.162  0.368  0.179  365 TYR AAA CA  
252   C C   . TYR A 36  ? 1.904 1.943 2.158 0.132  0.403  0.144  365 TYR AAA C   
253   O O   . TYR A 36  ? 1.817 1.929 2.131 0.119  0.379  0.095  365 TYR AAA O   
254   C CB  . TYR A 36  ? 1.905 1.994 2.009 0.167  0.320  0.204  365 TYR AAA CB  
255   C CG  . TYR A 36  ? 1.924 2.038 1.986 0.196  0.282  0.230  365 TYR AAA CG  
256   C CD1 . TYR A 36  ? 2.035 2.098 2.020 0.222  0.288  0.281  365 TYR AAA CD1 
257   C CD2 . TYR A 36  ? 1.843 2.036 1.937 0.200  0.240  0.205  365 TYR AAA CD2 
258   C CE1 . TYR A 36  ? 2.047 2.145 1.998 0.252  0.248  0.301  365 TYR AAA CE1 
259   C CE2 . TYR A 36  ? 1.863 2.085 1.929 0.225  0.207  0.225  365 TYR AAA CE2 
260   C CZ  . TYR A 36  ? 1.959 2.138 1.958 0.251  0.209  0.272  365 TYR AAA CZ  
261   O OH  . TYR A 36  ? 1.956 2.173 1.933 0.280  0.172  0.288  365 TYR AAA OH  
262   N N   . SER A 37  ? 1.982 1.935 2.221 0.124  0.459  0.166  366 SER AAA N   
263   C CA  . SER A 37  ? 1.992 1.928 2.303 0.095  0.505  0.130  366 SER AAA CA  
264   C C   . SER A 37  ? 1.949 1.942 2.397 0.083  0.505  0.059  366 SER AAA C   
265   O O   . SER A 37  ? 1.920 1.969 2.431 0.063  0.499  0.010  366 SER AAA O   
266   C CB  . SER A 37  ? 2.096 1.918 2.382 0.092  0.579  0.165  366 SER AAA CB  
267   O OG  . SER A 37  ? 2.141 1.908 2.510 0.092  0.632  0.153  366 SER AAA OG  
268   N N   . VAL A 38  ? 1.958 1.943 2.448 0.096  0.508  0.052  367 VAL AAA N   
269   C CA  . VAL A 38  ? 1.898 1.945 2.513 0.087  0.503  -0.021 367 VAL AAA CA  
270   C C   . VAL A 38  ? 1.777 1.940 2.409 0.084  0.443  -0.067 367 VAL AAA C   
271   O O   . VAL A 38  ? 1.739 1.956 2.475 0.068  0.448  -0.136 367 VAL AAA O   
272   C CB  . VAL A 38  ? 1.928 1.968 2.552 0.110  0.494  -0.012 367 VAL AAA CB  
273   C CG1 . VAL A 38  ? 1.874 1.997 2.607 0.104  0.473  -0.091 367 VAL AAA CG1 
274   C CG2 . VAL A 38  ? 2.048 1.968 2.674 0.119  0.562  0.028  367 VAL AAA CG2 
275   N N   . LEU A 39  ? 1.717 1.919 2.254 0.099  0.391  -0.033 368 LEU AAA N   
276   C CA  . LEU A 39  ? 1.635 1.939 2.170 0.105  0.336  -0.065 368 LEU AAA CA  
277   C C   . LEU A 39  ? 1.631 1.952 2.160 0.093  0.339  -0.072 368 LEU AAA C   
278   O O   . LEU A 39  ? 1.610 2.000 2.211 0.091  0.326  -0.129 368 LEU AAA O   
279   C CB  . LEU A 39  ? 1.604 1.929 2.047 0.125  0.292  -0.023 368 LEU AAA CB  
280   C CG  . LEU A 39  ? 1.608 1.955 2.071 0.142  0.275  -0.031 368 LEU AAA CG  
281   C CD1 . LEU A 39  ? 1.679 1.947 2.173 0.144  0.317  -0.016 368 LEU AAA CD1 
282   C CD2 . LEU A 39  ? 1.593 1.964 1.972 0.158  0.235  0.007  368 LEU AAA CD2 
283   N N   . TYR A 40  ? 1.655 1.920 2.101 0.087  0.353  -0.021 369 TYR AAA N   
284   C CA  . TYR A 40  ? 1.625 1.904 2.050 0.077  0.353  -0.021 369 TYR AAA CA  
285   C C   . TYR A 40  ? 1.635 1.898 2.151 0.057  0.398  -0.060 369 TYR AAA C   
286   O O   . TYR A 40  ? 1.579 1.898 2.132 0.056  0.387  -0.092 369 TYR AAA O   
287   C CB  . TYR A 40  ? 1.652 1.882 1.961 0.076  0.353  0.037  369 TYR AAA CB  
288   C CG  . TYR A 40  ? 1.734 1.871 1.987 0.072  0.390  0.083  369 TYR AAA CG  
289   C CD1 . TYR A 40  ? 1.794 1.865 2.047 0.055  0.442  0.091  369 TYR AAA CD1 
290   C CD2 . TYR A 40  ? 1.764 1.879 1.952 0.089  0.373  0.121  369 TYR AAA CD2 
291   C CE1 . TYR A 40  ? 1.878 1.859 2.061 0.058  0.479  0.139  369 TYR AAA CE1 
292   C CE2 . TYR A 40  ? 1.840 1.874 1.961 0.095  0.403  0.167  369 TYR AAA CE2 
293   C CZ  . TYR A 40  ? 1.901 1.864 2.013 0.081  0.457  0.178  369 TYR AAA CZ  
294   O OH  . TYR A 40  ? 1.998 1.878 2.031 0.094  0.489  0.228  369 TYR AAA OH  
295   N N   . ASN A 41  ? 1.708 1.902 2.268 0.045  0.450  -0.061 370 ASN AAA N   
296   C CA  . ASN A 41  ? 1.758 1.931 2.419 0.020  0.505  -0.101 370 ASN AAA CA  
297   C C   . ASN A 41  ? 1.737 2.004 2.532 0.018  0.488  -0.186 370 ASN AAA C   
298   O O   . ASN A 41  ? 1.743 2.021 2.643 -0.002 0.524  -0.236 370 ASN AAA O   
299   C CB  . ASN A 41  ? 1.848 1.901 2.503 0.009  0.577  -0.068 370 ASN AAA CB  
300   C CG  . ASN A 41  ? 1.897 1.867 2.435 0.008  0.605  -0.001 370 ASN AAA CG  
301   O OD1 . ASN A 41  ? 1.857 1.846 2.368 0.000  0.598  0.000  370 ASN AAA OD1 
302   N ND2 . ASN A 41  ? 1.979 1.855 2.445 0.019  0.638  0.054  370 ASN AAA ND2 
303   N N   . SER A 42  ? 1.727 2.067 2.523 0.038  0.434  -0.207 371 SER AAA N   
304   C CA  . SER A 42  ? 1.706 2.155 2.610 0.044  0.403  -0.291 371 SER AAA CA  
305   C C   . SER A 42  ? 1.688 2.231 2.569 0.064  0.351  -0.306 371 SER AAA C   
306   O O   . SER A 42  ? 1.657 2.211 2.432 0.086  0.312  -0.259 371 SER AAA O   
307   C CB  . SER A 42  ? 1.682 2.160 2.591 0.059  0.376  -0.306 371 SER AAA CB  
308   O OG  . SER A 42  ? 1.623 2.221 2.595 0.074  0.330  -0.378 371 SER AAA OG  
309   N N   . ALA A 43  ? 1.703 2.317 2.688 0.060  0.351  -0.374 372 ALA AAA N   
310   C CA  . ALA A 43  ? 1.682 2.378 2.657 0.084  0.313  -0.387 372 ALA AAA CA  
311   C C   . ALA A 43  ? 1.635 2.431 2.574 0.124  0.245  -0.405 372 ALA AAA C   
312   O O   . ALA A 43  ? 1.627 2.468 2.508 0.154  0.212  -0.387 372 ALA AAA O   
313   C CB  . ALA A 43  ? 1.695 2.443 2.807 0.069  0.334  -0.460 372 ALA AAA CB  
314   N N   . SER A 44  ? 1.607 2.428 2.573 0.128  0.231  -0.437 373 SER AAA N   
315   C CA  . SER A 44  ? 1.569 2.497 2.526 0.165  0.173  -0.477 373 SER AAA CA  
316   C C   . SER A 44  ? 1.547 2.446 2.369 0.187  0.149  -0.408 373 SER AAA C   
317   O O   . SER A 44  ? 1.540 2.448 2.358 0.192  0.137  -0.420 373 SER AAA O   
318   C CB  . SER A 44  ? 1.575 2.548 2.647 0.152  0.178  -0.559 373 SER AAA CB  
319   O OG  . SER A 44  ? 1.598 2.467 2.715 0.112  0.239  -0.546 373 SER AAA OG  
320   N N   . PHE A 45  ? 1.540 2.406 2.264 0.199  0.144  -0.343 374 PHE AAA N   
321   C CA  . PHE A 45  ? 1.534 2.391 2.139 0.224  0.120  -0.285 374 PHE AAA CA  
322   C C   . PHE A 45  ? 1.515 2.395 2.063 0.251  0.107  -0.258 374 PHE AAA C   
323   O O   . PHE A 45  ? 1.529 2.366 2.084 0.234  0.133  -0.239 374 PHE AAA O   
324   C CB  . PHE A 45  ? 1.563 2.320 2.101 0.199  0.146  -0.219 374 PHE AAA CB  
325   C CG  . PHE A 45  ? 1.595 2.318 2.165 0.182  0.159  -0.227 374 PHE AAA CG  
326   C CD1 . PHE A 45  ? 1.610 2.385 2.197 0.199  0.135  -0.260 374 PHE AAA CD1 
327   C CD2 . PHE A 45  ? 1.630 2.264 2.207 0.153  0.199  -0.198 374 PHE AAA CD2 
328   C CE1 . PHE A 45  ? 1.627 2.366 2.248 0.186  0.151  -0.266 374 PHE AAA CE1 
329   C CE2 . PHE A 45  ? 1.664 2.261 2.268 0.144  0.215  -0.199 374 PHE AAA CE2 
330   C CZ  . PHE A 45  ? 1.657 2.306 2.287 0.160  0.191  -0.234 374 PHE AAA CZ  
331   N N   . SER A 46  ? 1.499 2.437 1.989 0.295  0.074  -0.255 375 SER AAA N   
332   C CA  . SER A 46  ? 1.511 2.469 1.941 0.331  0.064  -0.225 375 SER AAA CA  
333   C C   . SER A 46  ? 1.515 2.377 1.865 0.311  0.096  -0.151 375 SER AAA C   
334   O O   . SER A 46  ? 1.519 2.358 1.863 0.310  0.113  -0.132 375 SER AAA O   
335   C CB  . SER A 46  ? 1.528 2.557 1.902 0.387  0.029  -0.231 375 SER AAA CB  
336   O OG  . SER A 46  ? 1.540 2.676 1.981 0.419  -0.005 -0.301 375 SER AAA OG  
337   N N   . THR A 47  ? 1.522 2.337 1.819 0.295  0.102  -0.117 376 THR AAA N   
338   C CA  . THR A 47  ? 1.547 2.291 1.762 0.281  0.124  -0.055 376 THR AAA CA  
339   C C   . THR A 47  ? 1.542 2.226 1.759 0.240  0.139  -0.040 376 THR AAA C   
340   O O   . THR A 47  ? 1.546 2.245 1.768 0.241  0.126  -0.049 376 THR AAA O   
341   C CB  . THR A 47  ? 1.578 2.344 1.720 0.317  0.114  -0.032 376 THR AAA CB  
342   O OG1 . THR A 47  ? 1.589 2.415 1.726 0.366  0.097  -0.047 376 THR AAA OG1 
343   C CG2 . THR A 47  ? 1.595 2.295 1.667 0.303  0.141  0.022  376 THR AAA CG2 
344   N N   . PHE A 48  ? 1.542 2.164 1.756 0.208  0.165  -0.019 377 PHE AAA N   
345   C CA  . PHE A 48  ? 1.532 2.093 1.726 0.176  0.179  0.006  377 PHE AAA CA  
346   C C   . PHE A 48  ? 1.582 2.095 1.704 0.162  0.195  0.048  377 PHE AAA C   
347   O O   . PHE A 48  ? 1.601 2.063 1.712 0.139  0.218  0.062  377 PHE AAA O   
348   C CB  . PHE A 48  ? 1.503 2.031 1.755 0.154  0.200  -0.011 377 PHE AAA CB  
349   C CG  . PHE A 48  ? 1.480 1.966 1.730 0.140  0.207  0.001  377 PHE AAA CG  
350   C CD1 . PHE A 48  ? 1.472 1.911 1.653 0.129  0.211  0.044  377 PHE AAA CD1 
351   C CD2 . PHE A 48  ? 1.474 1.968 1.797 0.139  0.211  -0.032 377 PHE AAA CD2 
352   C CE1 . PHE A 48  ? 1.474 1.878 1.651 0.124  0.215  0.059  377 PHE AAA CE1 
353   C CE2 . PHE A 48  ? 1.482 1.930 1.802 0.131  0.223  -0.014 377 PHE AAA CE2 
354   C CZ  . PHE A 48  ? 1.481 1.884 1.724 0.128  0.223  0.034  377 PHE AAA CZ  
355   N N   . LYS A 49  ? 1.618 2.148 1.695 0.177  0.188  0.065  378 LYS AAA N   
356   C CA  . LYS A 49  ? 1.665 2.156 1.684 0.161  0.205  0.097  378 LYS AAA CA  
357   C C   . LYS A 49  ? 1.658 2.128 1.657 0.139  0.199  0.108  378 LYS AAA C   
358   O O   . LYS A 49  ? 1.625 2.126 1.633 0.150  0.181  0.103  378 LYS AAA O   
359   C CB  . LYS A 49  ? 1.711 2.221 1.697 0.185  0.210  0.108  378 LYS AAA CB  
360   C CG  . LYS A 49  ? 1.755 2.272 1.738 0.210  0.222  0.110  378 LYS AAA CG  
361   C CD  . LYS A 49  ? 1.809 2.337 1.751 0.243  0.232  0.129  378 LYS AAA CD  
362   C CE  . LYS A 49  ? 1.841 2.413 1.779 0.265  0.211  0.120  378 LYS AAA CE  
363   N NZ  . LYS A 49  ? 1.903 2.505 1.809 0.317  0.212  0.127  378 LYS AAA NZ  
364   N N   . CYS A 50  ? 1.675 2.101 1.649 0.114  0.213  0.122  379 CYS AAA N   
365   C CA  . CYS A 50  ? 1.683 2.095 1.628 0.098  0.204  0.133  379 CYS AAA CA  
366   C C   . CYS A 50  ? 1.658 2.063 1.563 0.081  0.215  0.142  379 CYS AAA C   
367   O O   . CYS A 50  ? 1.718 2.095 1.605 0.070  0.239  0.145  379 CYS AAA O   
368   C CB  . CYS A 50  ? 1.744 2.113 1.682 0.087  0.213  0.141  379 CYS AAA CB  
369   S SG  . CYS A 50  ? 1.764 2.137 1.759 0.103  0.205  0.130  379 CYS AAA SG  
370   N N   . TYR A 51  ? 1.584 2.014 1.483 0.078  0.201  0.141  380 TYR AAA N   
371   C CA  . TYR A 51  ? 1.569 2.002 1.446 0.058  0.213  0.138  380 TYR AAA CA  
372   C C   . TYR A 51  ? 1.578 2.020 1.436 0.044  0.192  0.134  380 TYR AAA C   
373   O O   . TYR A 51  ? 1.579 2.054 1.456 0.057  0.166  0.133  380 TYR AAA O   
374   C CB  . TYR A 51  ? 1.559 2.023 1.455 0.069  0.219  0.134  380 TYR AAA CB  
375   C CG  . TYR A 51  ? 1.547 2.005 1.446 0.092  0.238  0.141  380 TYR AAA CG  
376   C CD1 . TYR A 51  ? 1.536 2.019 1.456 0.121  0.220  0.138  380 TYR AAA CD1 
377   C CD2 . TYR A 51  ? 1.576 2.005 1.457 0.087  0.274  0.149  380 TYR AAA CD2 
378   C CE1 . TYR A 51  ? 1.565 2.053 1.481 0.149  0.231  0.141  380 TYR AAA CE1 
379   C CE2 . TYR A 51  ? 1.603 2.029 1.479 0.118  0.290  0.160  380 TYR AAA CE2 
380   C CZ  . TYR A 51  ? 1.599 2.059 1.490 0.151  0.265  0.155  380 TYR AAA CZ  
381   O OH  . TYR A 51  ? 1.623 2.090 1.503 0.188  0.275  0.164  380 TYR AAA OH  
382   N N   . GLY A 52  ? 1.596 2.012 1.416 0.023  0.203  0.132  381 GLY AAA N   
383   C CA  . GLY A 52  ? 1.613 2.047 1.404 0.012  0.182  0.123  381 GLY AAA CA  
384   C C   . GLY A 52  ? 1.611 2.039 1.381 0.033  0.157  0.140  381 GLY AAA C   
385   O O   . GLY A 52  ? 1.615 2.078 1.371 0.040  0.127  0.135  381 GLY AAA O   
386   N N   . VAL A 53  ? 1.592 1.977 1.362 0.045  0.169  0.158  382 VAL AAA N   
387   C CA  . VAL A 53  ? 1.627 1.983 1.369 0.064  0.161  0.179  382 VAL AAA CA  
388   C C   . VAL A 53  ? 1.613 1.913 1.366 0.065  0.193  0.190  382 VAL AAA C   
389   O O   . VAL A 53  ? 1.523 1.832 1.331 0.068  0.201  0.181  382 VAL AAA O   
390   C CB  . VAL A 53  ? 1.616 2.006 1.389 0.091  0.132  0.186  382 VAL AAA CB  
391   C CG1 . VAL A 53  ? 1.564 1.965 1.402 0.100  0.137  0.178  382 VAL AAA CG1 
392   C CG2 . VAL A 53  ? 1.695 2.049 1.428 0.115  0.128  0.213  382 VAL AAA CG2 
393   N N   . SER A 54  ? 1.697 1.947 1.398 0.064  0.211  0.206  383 SER AAA N   
394   C CA  . SER A 54  ? 1.734 1.924 1.448 0.063  0.248  0.216  383 SER AAA CA  
395   C C   . SER A 54  ? 1.737 1.917 1.489 0.087  0.246  0.227  383 SER AAA C   
396   O O   . SER A 54  ? 1.824 1.987 1.535 0.107  0.237  0.250  383 SER AAA O   
397   C CB  . SER A 54  ? 1.827 1.961 1.466 0.056  0.274  0.232  383 SER AAA CB  
398   O OG  . SER A 54  ? 1.827 1.946 1.462 0.031  0.301  0.218  383 SER AAA OG  
399   N N   . PRO A 55  ? 1.681 1.873 1.514 0.087  0.254  0.209  384 PRO AAA N   
400   C CA  . PRO A 55  ? 1.697 1.874 1.577 0.105  0.261  0.212  384 PRO AAA CA  
401   C C   . PRO A 55  ? 1.793 1.890 1.664 0.105  0.307  0.230  384 PRO AAA C   
402   O O   . PRO A 55  ? 1.832 1.896 1.714 0.123  0.319  0.246  384 PRO AAA O   
403   C CB  . PRO A 55  ? 1.605 1.826 1.571 0.101  0.257  0.176  384 PRO AAA CB  
404   C CG  . PRO A 55  ? 1.590 1.813 1.550 0.083  0.271  0.164  384 PRO AAA CG  
405   C CD  . PRO A 55  ? 1.615 1.837 1.496 0.075  0.259  0.183  384 PRO AAA CD  
406   N N   . THR A 56  ? 1.836 1.900 1.689 0.086  0.338  0.228  385 THR AAA N   
407   C CA  . THR A 56  ? 1.941 1.922 1.776 0.082  0.392  0.247  385 THR AAA CA  
408   C C   . THR A 56  ? 2.044 1.977 1.777 0.106  0.393  0.292  385 THR AAA C   
409   O O   . THR A 56  ? 2.154 2.009 1.868 0.116  0.440  0.318  385 THR AAA O   
410   C CB  . THR A 56  ? 1.962 1.925 1.790 0.057  0.421  0.235  385 THR AAA CB  
411   O OG1 . THR A 56  ? 1.976 1.958 1.722 0.052  0.397  0.244  385 THR AAA OG1 
412   C CG2 . THR A 56  ? 1.893 1.904 1.821 0.044  0.421  0.192  385 THR AAA CG2 
413   N N   . LYS A 57  ? 2.041 2.020 1.711 0.115  0.346  0.300  386 LYS AAA N   
414   C CA  . LYS A 57  ? 2.147 2.100 1.705 0.140  0.336  0.336  386 LYS AAA CA  
415   C C   . LYS A 57  ? 2.177 2.160 1.732 0.176  0.299  0.353  386 LYS AAA C   
416   O O   . LYS A 57  ? 2.269 2.216 1.742 0.210  0.300  0.391  386 LYS AAA O   
417   C CB  . LYS A 57  ? 2.132 2.120 1.626 0.121  0.315  0.322  386 LYS AAA CB  
418   C CG  . LYS A 57  ? 2.137 2.075 1.612 0.094  0.362  0.315  386 LYS AAA CG  
419   C CD  . LYS A 57  ? 2.100 2.073 1.537 0.069  0.347  0.291  386 LYS AAA CD  
420   C CE  . LYS A 57  ? 2.172 2.156 1.499 0.083  0.322  0.302  386 LYS AAA CE  
421   N NZ  . LYS A 57  ? 2.298 2.202 1.535 0.101  0.362  0.336  386 LYS AAA NZ  
422   N N   . LEU A 58  ? 2.136 2.180 1.773 0.174  0.269  0.329  387 LEU AAA N   
423   C CA  . LEU A 58  ? 2.198 2.277 1.840 0.208  0.232  0.341  387 LEU AAA CA  
424   C C   . LEU A 58  ? 2.292 2.306 1.965 0.235  0.268  0.367  387 LEU AAA C   
425   O O   . LEU A 58  ? 2.294 2.331 1.987 0.265  0.244  0.377  387 LEU AAA O   
426   C CB  . LEU A 58  ? 2.105 2.272 1.818 0.196  0.192  0.305  387 LEU AAA CB  
427   C CG  . LEU A 58  ? 2.010 2.192 1.817 0.173  0.207  0.271  387 LEU AAA CG  
428   C CD1 . LEU A 58  ? 2.028 2.153 1.889 0.181  0.247  0.275  387 LEU AAA CD1 
429   C CD2 . LEU A 58  ? 1.926 2.186 1.784 0.175  0.169  0.246  387 LEU AAA CD2 
430   N N   . ASN A 59  ? 2.398 2.332 2.082 0.224  0.327  0.376  388 ASN AAA N   
431   C CA  . ASN A 59  ? 2.545 2.392 2.239 0.250  0.377  0.408  388 ASN AAA CA  
432   C C   . ASN A 59  ? 2.704 2.487 2.270 0.288  0.392  0.465  388 ASN AAA C   
433   O O   . ASN A 59  ? 2.828 2.513 2.380 0.308  0.452  0.501  388 ASN AAA O   
434   C CB  . ASN A 59  ? 2.561 2.357 2.347 0.220  0.438  0.382  388 ASN AAA CB  
435   C CG  . ASN A 59  ? 2.619 2.375 2.379 0.191  0.478  0.378  388 ASN AAA CG  
436   O OD1 . ASN A 59  ? 2.726 2.401 2.401 0.205  0.518  0.419  388 ASN AAA OD1 
437   N ND2 . ASN A 59  ? 2.562 2.368 2.393 0.154  0.470  0.330  388 ASN AAA ND2 
438   N N   . ASP A 60  ? 2.724 2.557 2.198 0.299  0.343  0.473  389 ASP AAA N   
439   C CA  . ASP A 60  ? 2.852 2.650 2.193 0.348  0.338  0.524  389 ASP AAA CA  
440   C C   . ASP A 60  ? 2.816 2.722 2.113 0.362  0.258  0.509  389 ASP AAA C   
441   O O   . ASP A 60  ? 2.913 2.824 2.097 0.380  0.241  0.524  389 ASP AAA O   
442   C CB  . ASP A 60  ? 2.961 2.673 2.214 0.342  0.393  0.548  389 ASP AAA CB  
443   C CG  . ASP A 60  ? 2.895 2.635 2.157 0.288  0.395  0.507  389 ASP AAA CG  
444   O OD1 . ASP A 60  ? 2.850 2.675 2.089 0.275  0.339  0.479  389 ASP AAA OD1 
445   O OD2 . ASP A 60  ? 2.897 2.572 2.194 0.259  0.456  0.501  389 ASP AAA OD2 
446   N N   . LEU A 61  ? 2.699 2.690 2.082 0.355  0.212  0.477  390 LEU AAA N   
447   C CA  . LEU A 61  ? 2.659 2.759 2.028 0.366  0.140  0.455  390 LEU AAA CA  
448   C C   . LEU A 61  ? 2.598 2.751 2.061 0.379  0.113  0.442  390 LEU AAA C   
449   O O   . LEU A 61  ? 2.514 2.658 2.072 0.351  0.135  0.420  390 LEU AAA O   
450   C CB  . LEU A 61  ? 2.569 2.728 1.951 0.312  0.123  0.406  390 LEU AAA CB  
451   C CG  . LEU A 61  ? 2.552 2.814 1.908 0.315  0.060  0.377  390 LEU AAA CG  
452   C CD1 . LEU A 61  ? 2.572 2.840 1.858 0.287  0.062  0.356  390 LEU AAA CD1 
453   C CD2 . LEU A 61  ? 2.425 2.770 1.888 0.290  0.032  0.334  390 LEU AAA CD2 
454   N N   . CYS A 62  ? 2.660 2.874 2.100 0.423  0.063  0.452  391 CYS AAA N   
455   C CA  . CYS A 62  ? 2.648 2.902 2.164 0.451  0.041  0.452  391 CYS AAA CA  
456   C C   . CYS A 62  ? 2.549 2.922 2.133 0.426  -0.010 0.399  391 CYS AAA C   
457   O O   . CYS A 62  ? 2.608 3.056 2.151 0.435  -0.057 0.384  391 CYS AAA O   
458   C CB  . CYS A 62  ? 2.780 3.022 2.229 0.525  0.024  0.502  391 CYS AAA CB  
459   S SG  . CYS A 62  ? 2.937 3.020 2.327 0.563  0.102  0.572  391 CYS AAA SG  
460   N N   . PHE A 63  ? 2.427 2.816 2.112 0.397  0.000  0.370  392 PHE AAA N   
461   C CA  . PHE A 63  ? 2.308 2.797 2.067 0.373  -0.035 0.323  392 PHE AAA CA  
462   C C   . PHE A 63  ? 2.274 2.799 2.094 0.412  -0.054 0.328  392 PHE AAA C   
463   O O   . PHE A 63  ? 2.329 2.788 2.167 0.437  -0.025 0.356  392 PHE AAA O   
464   C CB  . PHE A 63  ? 2.229 2.710 2.048 0.322  -0.007 0.290  392 PHE AAA CB  
465   C CG  . PHE A 63  ? 2.240 2.708 2.018 0.282  0.006  0.276  392 PHE AAA CG  
466   C CD1 . PHE A 63  ? 2.220 2.754 1.991 0.257  -0.018 0.245  392 PHE AAA CD1 
467   C CD2 . PHE A 63  ? 2.271 2.658 2.024 0.267  0.049  0.291  392 PHE AAA CD2 
468   C CE1 . PHE A 63  ? 2.216 2.731 1.953 0.220  0.000  0.232  392 PHE AAA CE1 
469   C CE2 . PHE A 63  ? 2.269 2.643 1.989 0.232  0.063  0.278  392 PHE AAA CE2 
470   C CZ  . PHE A 63  ? 2.246 2.682 1.955 0.209  0.039  0.250  392 PHE AAA CZ  
471   N N   . THR A 64  ? 2.181 2.805 2.038 0.414  -0.097 0.298  393 THR AAA N   
472   C CA  . THR A 64  ? 2.123 2.799 2.047 0.450  -0.121 0.295  393 THR AAA CA  
473   C C   . THR A 64  ? 2.014 2.663 2.020 0.432  -0.088 0.281  393 THR AAA C   
474   O O   . THR A 64  ? 2.012 2.635 2.052 0.469  -0.078 0.301  393 THR AAA O   
475   C CB  . THR A 64  ? 2.090 2.886 2.048 0.445  -0.169 0.255  393 THR AAA CB  
476   O OG1 . THR A 64  ? 2.033 2.853 1.995 0.387  -0.161 0.216  393 THR AAA OG1 
477   C CG2 . THR A 64  ? 2.180 3.024 2.076 0.492  -0.215 0.269  393 THR AAA CG2 
478   N N   . ASN A 65  ? 1.910 2.568 1.945 0.381  -0.070 0.247  394 ASN AAA N   
479   C CA  . ASN A 65  ? 1.823 2.470 1.928 0.363  -0.044 0.225  394 ASN AAA CA  
480   C C   . ASN A 65  ? 1.755 2.368 1.848 0.319  -0.016 0.209  394 ASN AAA C   
481   O O   . ASN A 65  ? 1.723 2.359 1.785 0.291  -0.022 0.197  394 ASN AAA O   
482   C CB  . ASN A 65  ? 1.774 2.505 1.947 0.359  -0.063 0.191  394 ASN AAA CB  
483   C CG  . ASN A 65  ? 1.829 2.594 2.038 0.406  -0.085 0.203  394 ASN AAA CG  
484   O OD1 . ASN A 65  ? 1.867 2.588 2.104 0.432  -0.067 0.218  394 ASN AAA OD1 
485   N ND2 . ASN A 65  ? 1.858 2.701 2.070 0.418  -0.124 0.193  394 ASN AAA ND2 
486   N N   . VAL A 66  ? 1.722 2.287 1.848 0.316  0.015  0.206  395 VAL AAA N   
487   C CA  . VAL A 66  ? 1.661 2.211 1.797 0.282  0.038  0.182  395 VAL AAA CA  
488   C C   . VAL A 66  ? 1.587 2.179 1.787 0.281  0.040  0.149  395 VAL AAA C   
489   O O   . VAL A 66  ? 1.589 2.169 1.835 0.301  0.048  0.145  395 VAL AAA O   
490   C CB  . VAL A 66  ? 1.707 2.179 1.836 0.279  0.072  0.194  395 VAL AAA CB  
491   C CG1 . VAL A 66  ? 1.659 2.132 1.808 0.249  0.090  0.164  395 VAL AAA CG1 
492   C CG2 . VAL A 66  ? 1.787 2.211 1.844 0.286  0.076  0.231  395 VAL AAA CG2 
493   N N   . TYR A 67  ? 1.526 2.163 1.725 0.259  0.035  0.127  396 TYR AAA N   
494   C CA  . TYR A 67  ? 1.478 2.152 1.719 0.258  0.042  0.096  396 TYR AAA CA  
495   C C   . TYR A 67  ? 1.471 2.123 1.707 0.245  0.060  0.079  396 TYR AAA C   
496   O O   . TYR A 67  ? 1.441 2.075 1.637 0.227  0.066  0.088  396 TYR AAA O   
497   C CB  . TYR A 67  ? 1.447 2.176 1.685 0.248  0.033  0.086  396 TYR AAA CB  
498   C CG  . TYR A 67  ? 1.456 2.225 1.717 0.262  0.011  0.092  396 TYR AAA CG  
499   C CD1 . TYR A 67  ? 1.479 2.249 1.780 0.292  0.003  0.097  396 TYR AAA CD1 
500   C CD2 . TYR A 67  ? 1.458 2.266 1.708 0.247  0.000  0.088  396 TYR AAA CD2 
501   C CE1 . TYR A 67  ? 1.500 2.315 1.826 0.312  -0.021 0.101  396 TYR AAA CE1 
502   C CE2 . TYR A 67  ? 1.484 2.344 1.765 0.262  -0.025 0.085  396 TYR AAA CE2 
503   C CZ  . TYR A 67  ? 1.497 2.362 1.814 0.297  -0.038 0.093  396 TYR AAA CZ  
504   O OH  . TYR A 67  ? 1.490 2.413 1.841 0.319  -0.066 0.091  396 TYR AAA OH  
505   N N   . ALA A 68  ? 1.500 2.158 1.780 0.254  0.069  0.052  397 ALA AAA N   
506   C CA  . ALA A 68  ? 1.525 2.181 1.814 0.248  0.080  0.024  397 ALA AAA CA  
507   C C   . ALA A 68  ? 1.536 2.245 1.834 0.257  0.078  -0.007 397 ALA AAA C   
508   O O   . ALA A 68  ? 1.570 2.297 1.913 0.271  0.079  -0.032 397 ALA AAA O   
509   C CB  . ALA A 68  ? 1.557 2.175 1.893 0.251  0.095  0.012  397 ALA AAA CB  
510   N N   . ASP A 69  ? 1.522 2.253 1.777 0.253  0.078  -0.004 398 ASP AAA N   
511   C CA  . ASP A 69  ? 1.496 2.270 1.737 0.267  0.081  -0.025 398 ASP AAA CA  
512   C C   . ASP A 69  ? 1.493 2.281 1.734 0.277  0.080  -0.054 398 ASP AAA C   
513   O O   . ASP A 69  ? 1.467 2.237 1.685 0.268  0.081  -0.043 398 ASP AAA O   
514   C CB  . ASP A 69  ? 1.496 2.277 1.690 0.261  0.091  -0.001 398 ASP AAA CB  
515   C CG  . ASP A 69  ? 1.493 2.269 1.697 0.246  0.088  0.020  398 ASP AAA CG  
516   O OD1 . ASP A 69  ? 1.495 2.280 1.741 0.254  0.079  0.015  398 ASP AAA OD1 
517   O OD2 . ASP A 69  ? 1.461 2.227 1.635 0.230  0.096  0.038  398 ASP AAA OD2 
518   N N   . SER A 70  ? 1.438 2.082 1.653 0.117  0.171  -0.071 399 SER AAA N   
519   C CA  . SER A 70  ? 1.500 2.137 1.713 0.117  0.162  -0.101 399 SER AAA CA  
520   C C   . SER A 70  ? 1.527 2.176 1.707 0.121  0.152  -0.104 399 SER AAA C   
521   O O   . SER A 70  ? 1.565 2.223 1.731 0.124  0.165  -0.094 399 SER AAA O   
522   C CB  . SER A 70  ? 1.534 2.158 1.768 0.120  0.181  -0.126 399 SER AAA CB  
523   O OG  . SER A 70  ? 1.570 2.195 1.803 0.128  0.205  -0.119 399 SER AAA OG  
524   N N   . PHE A 71  ? 1.507 2.159 1.676 0.120  0.130  -0.115 400 PHE AAA N   
525   C CA  . PHE A 71  ? 1.519 2.182 1.649 0.124  0.117  -0.118 400 PHE AAA CA  
526   C C   . PHE A 71  ? 1.548 2.218 1.678 0.127  0.090  -0.132 400 PHE AAA C   
527   O O   . PHE A 71  ? 1.583 2.249 1.746 0.125  0.084  -0.139 400 PHE AAA O   
528   C CB  . PHE A 71  ? 1.498 2.160 1.599 0.123  0.116  -0.086 400 PHE AAA CB  
529   C CG  . PHE A 71  ? 1.454 2.105 1.561 0.119  0.105  -0.066 400 PHE AAA CG  
530   C CD1 . PHE A 71  ? 1.468 2.112 1.563 0.124  0.084  -0.065 400 PHE AAA CD1 
531   C CD2 . PHE A 71  ? 1.414 2.060 1.538 0.111  0.117  -0.050 400 PHE AAA CD2 
532   C CE1 . PHE A 71  ? 1.457 2.084 1.557 0.120  0.080  -0.048 400 PHE AAA CE1 
533   C CE2 . PHE A 71  ? 1.409 2.042 1.535 0.103  0.110  -0.035 400 PHE AAA CE2 
534   C CZ  . PHE A 71  ? 1.430 2.048 1.542 0.108  0.094  -0.035 400 PHE AAA CZ  
535   N N   . VAL A 72  ? 1.573 2.256 1.666 0.131  0.075  -0.135 401 VAL AAA N   
536   C CA  . VAL A 72  ? 1.582 2.282 1.671 0.138  0.045  -0.146 401 VAL AAA CA  
537   C C   . VAL A 72  ? 1.589 2.284 1.638 0.148  0.029  -0.116 401 VAL AAA C   
538   O O   . VAL A 72  ? 1.598 2.287 1.605 0.147  0.037  -0.100 401 VAL AAA O   
539   C CB  . VAL A 72  ? 1.635 2.359 1.711 0.134  0.040  -0.179 401 VAL AAA CB  
540   C CG1 . VAL A 72  ? 1.672 2.424 1.730 0.143  0.005  -0.182 401 VAL AAA CG1 
541   C CG2 . VAL A 72  ? 1.626 2.353 1.746 0.124  0.055  -0.213 401 VAL AAA CG2 
542   N N   . ILE A 73  ? 1.586 2.281 1.649 0.158  0.008  -0.108 402 ILE AAA N   
543   C CA  . ILE A 73  ? 1.636 2.323 1.663 0.172  -0.010 -0.079 402 ILE AAA CA  
544   C C   . ILE A 73  ? 1.640 2.353 1.689 0.187  -0.039 -0.090 402 ILE AAA C   
545   O O   . ILE A 73  ? 1.593 2.327 1.690 0.182  -0.041 -0.118 402 ILE AAA O   
546   C CB  . ILE A 73  ? 1.637 2.287 1.664 0.169  0.004  -0.050 402 ILE AAA CB  
547   C CG1 . ILE A 73  ? 1.607 2.249 1.688 0.162  0.013  -0.060 402 ILE AAA CG1 
548   C CG2 . ILE A 73  ? 1.637 2.272 1.632 0.156  0.027  -0.034 402 ILE AAA CG2 
549   C CD1 . ILE A 73  ? 1.606 2.213 1.687 0.161  0.021  -0.035 402 ILE AAA CD1 
550   N N   . ARG A 74  ? 1.712 2.425 1.728 0.205  -0.060 -0.067 403 ARG AAA N   
551   C CA  . ARG A 74  ? 1.790 2.534 1.832 0.225  -0.090 -0.070 403 ARG AAA CA  
552   C C   . ARG A 74  ? 1.762 2.482 1.852 0.231  -0.082 -0.060 403 ARG AAA C   
553   O O   . ARG A 74  ? 1.759 2.432 1.832 0.227  -0.062 -0.037 403 ARG AAA O   
554   C CB  . ARG A 74  ? 1.904 2.658 1.890 0.246  -0.116 -0.046 403 ARG AAA CB  
555   C CG  . ARG A 74  ? 1.971 2.675 1.918 0.259  -0.109 -0.002 403 ARG AAA CG  
556   C CD  . ARG A 74  ? 2.071 2.782 1.950 0.276  -0.130 0.021  403 ARG AAA CD  
557   N NE  . ARG A 74  ? 2.141 2.799 1.979 0.291  -0.122 0.065  403 ARG AAA NE  
558   C CZ  . ARG A 74  ? 2.185 2.826 2.038 0.317  -0.132 0.090  403 ARG AAA CZ  
559   N NH1 . ARG A 74  ? 2.173 2.853 2.087 0.333  -0.152 0.075  403 ARG AAA NH1 
560   N NH2 . ARG A 74  ? 2.236 2.820 2.046 0.327  -0.117 0.129  403 ARG AAA NH2 
561   N N   . GLY A 75  ? 1.763 2.513 1.909 0.238  -0.095 -0.081 404 GLY AAA N   
562   C CA  . GLY A 75  ? 1.751 2.483 1.951 0.242  -0.084 -0.080 404 GLY AAA CA  
563   C C   . GLY A 75  ? 1.797 2.480 1.976 0.255  -0.076 -0.043 404 GLY AAA C   
564   O O   . GLY A 75  ? 1.794 2.441 1.997 0.245  -0.052 -0.041 404 GLY AAA O   
565   N N   . ASP A 76  ? 1.850 2.528 1.984 0.277  -0.092 -0.014 405 ASP AAA N   
566   C CA  . ASP A 76  ? 1.877 2.500 1.985 0.292  -0.082 0.024  405 ASP AAA CA  
567   C C   . ASP A 76  ? 1.855 2.424 1.940 0.265  -0.047 0.033  405 ASP AAA C   
568   O O   . ASP A 76  ? 1.846 2.369 1.938 0.265  -0.028 0.048  405 ASP AAA O   
569   C CB  . ASP A 76  ? 1.937 2.559 1.984 0.314  -0.101 0.055  405 ASP AAA CB  
570   C CG  . ASP A 76  ? 1.979 2.640 2.048 0.350  -0.135 0.064  405 ASP AAA CG  
571   O OD1 . ASP A 76  ? 1.955 2.644 2.093 0.358  -0.140 0.045  405 ASP AAA OD1 
572   O OD2 . ASP A 76  ? 2.056 2.722 2.074 0.371  -0.155 0.090  405 ASP AAA OD2 
573   N N   . GLU A 77  ? 1.857 2.434 1.917 0.242  -0.038 0.022  406 GLU AAA N   
574   C CA  . GLU A 77  ? 1.886 2.425 1.918 0.217  -0.010 0.034  406 GLU AAA CA  
575   C C   . GLU A 77  ? 1.829 2.365 1.905 0.194  0.009  0.013  406 GLU AAA C   
576   O O   . GLU A 77  ? 1.870 2.380 1.930 0.173  0.031  0.022  406 GLU AAA O   
577   C CB  . GLU A 77  ? 1.941 2.495 1.927 0.208  -0.010 0.035  406 GLU AAA CB  
578   C CG  . GLU A 77  ? 2.029 2.582 1.960 0.228  -0.027 0.057  406 GLU AAA CG  
579   C CD  . GLU A 77  ? 2.063 2.643 1.953 0.222  -0.033 0.049  406 GLU AAA CD  
580   O OE1 . GLU A 77  ? 2.039 2.651 1.955 0.209  -0.030 0.019  406 GLU AAA OE1 
581   O OE2 . GLU A 77  ? 2.126 2.692 1.957 0.231  -0.037 0.072  406 GLU AAA OE2 
582   N N   . VAL A 78  ? 1.754 2.318 1.881 0.197  0.002  -0.013 407 VAL AAA N   
583   C CA  . VAL A 78  ? 1.683 2.242 1.850 0.177  0.021  -0.032 407 VAL AAA CA  
584   C C   . VAL A 78  ? 1.653 2.164 1.812 0.165  0.042  -0.015 407 VAL AAA C   
585   O O   . VAL A 78  ? 1.569 2.069 1.722 0.141  0.060  -0.016 407 VAL AAA O   
586   C CB  . VAL A 78  ? 1.692 2.278 1.916 0.184  0.012  -0.060 407 VAL AAA CB  
587   C CG1 . VAL A 78  ? 1.686 2.248 1.945 0.171  0.032  -0.068 407 VAL AAA CG1 
588   C CG2 . VAL A 78  ? 1.683 2.309 1.919 0.178  0.005  -0.086 407 VAL AAA CG2 
589   N N   . ARG A 79  ? 1.703 2.187 1.863 0.181  0.041  -0.001 408 ARG AAA N   
590   C CA  . ARG A 79  ? 1.762 2.193 1.913 0.168  0.065  0.012  408 ARG AAA CA  
591   C C   . ARG A 79  ? 1.768 2.178 1.873 0.143  0.081  0.027  408 ARG AAA C   
592   O O   . ARG A 79  ? 1.795 2.178 1.899 0.118  0.102  0.025  408 ARG AAA O   
593   C CB  . ARG A 79  ? 1.855 2.256 2.002 0.195  0.062  0.031  408 ARG AAA CB  
594   C CG  . ARG A 79  ? 1.953 2.331 2.043 0.204  0.059  0.062  408 ARG AAA CG  
595   C CD  . ARG A 79  ? 2.052 2.391 2.138 0.233  0.061  0.084  408 ARG AAA CD  
596   N NE  . ARG A 79  ? 2.096 2.477 2.222 0.269  0.033  0.080  408 ARG AAA NE  
597   C CZ  . ARG A 79  ? 2.107 2.504 2.294 0.280  0.032  0.062  408 ARG AAA CZ  
598   N NH1 . ARG A 79  ? 2.082 2.452 2.295 0.257  0.059  0.045  408 ARG AAA NH1 
599   N NH2 . ARG A 79  ? 2.128 2.573 2.349 0.312  0.004  0.059  408 ARG AAA NH2 
600   N N   . GLN A 80  ? 1.775 2.199 1.843 0.147  0.072  0.040  409 GLN AAA N   
601   C CA  . GLN A 80  ? 1.798 2.206 1.823 0.125  0.087  0.056  409 GLN AAA CA  
602   C C   . GLN A 80  ? 1.724 2.159 1.763 0.099  0.096  0.043  409 GLN AAA C   
603   O O   . GLN A 80  ? 1.700 2.128 1.716 0.076  0.111  0.054  409 GLN AAA O   
604   C CB  . GLN A 80  ? 1.873 2.291 1.855 0.138  0.077  0.072  409 GLN AAA CB  
605   C CG  . GLN A 80  ? 1.964 2.345 1.914 0.161  0.073  0.096  409 GLN AAA CG  
606   C CD  . GLN A 80  ? 2.025 2.392 1.917 0.158  0.079  0.118  409 GLN AAA CD  
607   O OE1 . GLN A 80  ? 1.987 2.384 1.863 0.149  0.077  0.113  409 GLN AAA OE1 
608   N NE2 . GLN A 80  ? 2.110 2.424 1.966 0.165  0.090  0.144  409 GLN AAA NE2 
609   N N   . ILE A 81  ? 1.675 2.141 1.752 0.102  0.089  0.021  410 ILE AAA N   
610   C CA  . ILE A 81  ? 1.614 2.102 1.708 0.081  0.098  0.011  410 ILE AAA CA  
611   C C   . ILE A 81  ? 1.565 2.030 1.675 0.062  0.112  0.006  410 ILE AAA C   
612   O O   . ILE A 81  ? 1.530 1.997 1.673 0.065  0.112  -0.011 410 ILE AAA O   
613   C CB  . ILE A 81  ? 1.588 2.113 1.710 0.093  0.088  -0.009 410 ILE AAA CB  
614   C CG1 . ILE A 81  ? 1.605 2.149 1.709 0.112  0.073  -0.010 410 ILE AAA CG1 
615   C CG2 . ILE A 81  ? 1.552 2.096 1.684 0.077  0.100  -0.012 410 ILE AAA CG2 
616   C CD1 . ILE A 81  ? 1.618 2.162 1.680 0.107  0.079  0.009  410 ILE AAA CD1 
617   N N   . ALA A 82  ? 1.534 1.975 1.617 0.040  0.126  0.020  411 ALA AAA N   
618   C CA  . ALA A 82  ? 1.520 1.932 1.604 0.016  0.142  0.016  411 ALA AAA CA  
619   C C   . ALA A 82  ? 1.537 1.935 1.586 -0.011 0.156  0.031  411 ALA AAA C   
620   O O   . ALA A 82  ? 1.591 1.980 1.615 -0.004 0.156  0.046  411 ALA AAA O   
621   C CB  . ALA A 82  ? 1.536 1.909 1.633 0.030  0.146  0.010  411 ALA AAA CB  
622   N N   . PRO A 83  ? 1.523 1.921 1.568 -0.043 0.169  0.028  412 PRO AAA N   
623   C CA  . PRO A 83  ? 1.575 1.966 1.590 -0.075 0.182  0.038  412 PRO AAA CA  
624   C C   . PRO A 83  ? 1.649 1.979 1.636 -0.076 0.198  0.045  412 PRO AAA C   
625   O O   . PRO A 83  ? 1.655 1.945 1.650 -0.063 0.203  0.039  412 PRO AAA O   
626   C CB  . PRO A 83  ? 1.572 1.971 1.590 -0.108 0.190  0.028  412 PRO AAA CB  
627   C CG  . PRO A 83  ? 1.546 1.927 1.589 -0.092 0.189  0.012  412 PRO AAA CG  
628   C CD  . PRO A 83  ? 1.496 1.902 1.563 -0.054 0.170  0.013  412 PRO AAA CD  
629   N N   . GLY A 84  ? 1.704 2.027 1.660 -0.091 0.208  0.059  413 GLY AAA N   
630   C CA  . GLY A 84  ? 1.793 2.052 1.716 -0.098 0.229  0.069  413 GLY AAA CA  
631   C C   . GLY A 84  ? 1.830 2.062 1.742 -0.057 0.222  0.084  413 GLY AAA C   
632   O O   . GLY A 84  ? 1.900 2.078 1.779 -0.059 0.240  0.098  413 GLY AAA O   
633   N N   . GLN A 85  ? 1.803 2.069 1.740 -0.022 0.197  0.082  414 GLN AAA N   
634   C CA  . GLN A 85  ? 1.836 2.092 1.762 0.018  0.183  0.096  414 GLN AAA CA  
635   C C   . GLN A 85  ? 1.859 2.127 1.749 0.013  0.184  0.112  414 GLN AAA C   
636   O O   . GLN A 85  ? 1.826 2.133 1.718 -0.011 0.188  0.108  414 GLN AAA O   
637   C CB  . GLN A 85  ? 1.810 2.111 1.772 0.047  0.156  0.083  414 GLN AAA CB  
638   C CG  . GLN A 85  ? 1.824 2.115 1.825 0.056  0.154  0.067  414 GLN AAA CG  
639   C CD  . GLN A 85  ? 1.889 2.141 1.891 0.087  0.153  0.078  414 GLN AAA CD  
640   O OE1 . GLN A 85  ? 1.930 2.177 1.909 0.112  0.142  0.096  414 GLN AAA OE1 
641   N NE2 . GLN A 85  ? 1.899 2.122 1.927 0.087  0.165  0.067  414 GLN AAA NE2 
642   N N   . THR A 86  ? 1.918 2.154 1.775 0.038  0.183  0.132  415 THR AAA N   
643   C CA  . THR A 86  ? 1.951 2.187 1.763 0.037  0.187  0.150  415 THR AAA CA  
644   C C   . THR A 86  ? 1.945 2.179 1.738 0.079  0.166  0.164  415 THR AAA C   
645   O O   . THR A 86  ? 1.933 2.148 1.741 0.107  0.155  0.166  415 THR AAA O   
646   C CB  . THR A 86  ? 2.036 2.214 1.808 0.010  0.220  0.165  415 THR AAA CB  
647   O OG1 . THR A 86  ? 2.105 2.219 1.872 0.025  0.230  0.173  415 THR AAA OG1 
648   C CG2 . THR A 86  ? 2.013 2.209 1.797 -0.038 0.239  0.151  415 THR AAA CG2 
649   N N   . GLY A 87  ? 1.951 2.206 1.712 0.082  0.161  0.173  416 GLY AAA N   
650   C CA  . GLY A 87  ? 1.991 2.253 1.724 0.117  0.139  0.185  416 GLY AAA CA  
651   C C   . GLY A 87  ? 1.973 2.288 1.698 0.113  0.132  0.175  416 GLY AAA C   
652   O O   . GLY A 87  ? 1.925 2.253 1.650 0.083  0.151  0.171  416 GLY AAA O   
653   N N   . LYS A 88  ? 2.015 2.360 1.734 0.139  0.105  0.170  417 LYS AAA N   
654   C CA  . LYS A 88  ? 2.034 2.423 1.739 0.137  0.100  0.160  417 LYS AAA CA  
655   C C   . LYS A 88  ? 1.949 2.383 1.709 0.121  0.102  0.132  417 LYS AAA C   
656   O O   . LYS A 88  ? 1.926 2.378 1.686 0.100  0.120  0.129  417 LYS AAA O   
657   C CB  . LYS A 88  ? 2.084 2.491 1.764 0.167  0.071  0.159  417 LYS AAA CB  
658   C CG  . LYS A 88  ? 2.196 2.561 1.821 0.190  0.064  0.191  417 LYS AAA CG  
659   C CD  . LYS A 88  ? 2.285 2.603 1.850 0.174  0.094  0.217  417 LYS AAA CD  
660   C CE  . LYS A 88  ? 2.351 2.601 1.900 0.177  0.111  0.245  417 LYS AAA CE  
661   N NZ  . LYS A 88  ? 2.360 2.576 1.893 0.141  0.150  0.251  417 LYS AAA NZ  
662   N N   . ILE A 89  ? 1.914 2.367 1.721 0.132  0.085  0.114  418 ILE AAA N   
663   C CA  . ILE A 89  ? 1.873 2.366 1.731 0.122  0.085  0.088  418 ILE AAA CA  
664   C C   . ILE A 89  ? 1.876 2.361 1.754 0.095  0.106  0.091  418 ILE AAA C   
665   O O   . ILE A 89  ? 1.857 2.373 1.751 0.080  0.117  0.084  418 ILE AAA O   
666   C CB  . ILE A 89  ? 1.848 2.356 1.748 0.138  0.064  0.068  418 ILE AAA CB  
667   C CG1 . ILE A 89  ? 1.896 2.419 1.776 0.164  0.039  0.066  418 ILE AAA CG1 
668   C CG2 . ILE A 89  ? 1.790 2.331 1.736 0.128  0.068  0.044  418 ILE AAA CG2 
669   C CD1 . ILE A 89  ? 1.917 2.464 1.762 0.163  0.038  0.059  418 ILE AAA CD1 
670   N N   . ALA A 90  ? 1.924 2.371 1.803 0.089  0.112  0.100  419 ALA AAA N   
671   C CA  . ALA A 90  ? 1.926 2.364 1.822 0.059  0.132  0.101  419 ALA AAA CA  
672   C C   . ALA A 90  ? 1.918 2.372 1.794 0.036  0.150  0.110  419 ALA AAA C   
673   O O   . ALA A 90  ? 1.880 2.371 1.786 0.020  0.155  0.101  419 ALA AAA O   
674   C CB  . ALA A 90  ? 1.990 2.373 1.873 0.056  0.141  0.112  419 ALA AAA CB  
675   N N   . ASP A 91  ? 1.958 2.387 1.788 0.036  0.159  0.127  420 ASP AAA N   
676   C CA  . ASP A 91  ? 1.973 2.405 1.782 0.008  0.183  0.138  420 ASP AAA CA  
677   C C   . ASP A 91  ? 1.957 2.428 1.757 0.013  0.185  0.136  420 ASP AAA C   
678   O O   . ASP A 91  ? 1.975 2.468 1.778 -0.011 0.204  0.139  420 ASP AAA O   
679   C CB  . ASP A 91  ? 2.056 2.426 1.817 0.000  0.200  0.158  420 ASP AAA CB  
680   C CG  . ASP A 91  ? 2.071 2.401 1.842 -0.018 0.211  0.157  420 ASP AAA CG  
681   O OD1 . ASP A 91  ? 2.017 2.376 1.823 -0.042 0.215  0.143  420 ASP AAA OD1 
682   O OD2 . ASP A 91  ? 2.131 2.401 1.872 -0.008 0.218  0.171  420 ASP AAA OD2 
683   N N   . TYR A 92  ? 1.930 2.412 1.721 0.040  0.169  0.130  421 TYR AAA N   
684   C CA  . TYR A 92  ? 1.910 2.421 1.683 0.044  0.175  0.127  421 TYR AAA CA  
685   C C   . TYR A 92  ? 1.837 2.393 1.650 0.056  0.165  0.105  421 TYR AAA C   
686   O O   . TYR A 92  ? 1.823 2.403 1.627 0.058  0.175  0.100  421 TYR AAA O   
687   C CB  . TYR A 92  ? 1.976 2.455 1.686 0.060  0.171  0.140  421 TYR AAA CB  
688   C CG  . TYR A 92  ? 2.052 2.481 1.715 0.049  0.188  0.165  421 TYR AAA CG  
689   C CD1 . TYR A 92  ? 2.069 2.496 1.729 0.018  0.217  0.172  421 TYR AAA CD1 
690   C CD2 . TYR A 92  ? 2.123 2.504 1.741 0.069  0.176  0.182  421 TYR AAA CD2 
691   C CE1 . TYR A 92  ? 2.142 2.516 1.756 0.005  0.237  0.193  421 TYR AAA CE1 
692   C CE2 . TYR A 92  ? 2.194 2.520 1.764 0.061  0.196  0.207  421 TYR AAA CE2 
693   C CZ  . TYR A 92  ? 2.205 2.523 1.770 0.027  0.228  0.212  421 TYR AAA CZ  
694   O OH  . TYR A 92  ? 2.272 2.530 1.789 0.015  0.252  0.235  421 TYR AAA OH  
695   N N   . ASN A 93  ? 1.776 2.340 1.630 0.064  0.149  0.091  422 ASN AAA N   
696   C CA  . ASN A 93  ? 1.721 2.316 1.607 0.078  0.140  0.069  422 ASN AAA CA  
697   C C   . ASN A 93  ? 1.659 2.277 1.600 0.070  0.143  0.061  422 ASN AAA C   
698   O O   . ASN A 93  ? 1.657 2.307 1.621 0.068  0.156  0.056  422 ASN AAA O   
699   C CB  . ASN A 93  ? 1.714 2.299 1.591 0.099  0.117  0.057  422 ASN AAA CB  
700   C CG  . ASN A 93  ? 1.774 2.347 1.594 0.108  0.112  0.066  422 ASN AAA CG  
701   O OD1 . ASN A 93  ? 1.783 2.374 1.587 0.115  0.111  0.052  422 ASN AAA OD1 
702   N ND2 . ASN A 93  ? 1.829 2.366 1.612 0.109  0.111  0.089  422 ASN AAA ND2 
703   N N   . TYR A 94  ? 1.613 2.214 1.573 0.067  0.134  0.060  423 TYR AAA N   
704   C CA  . TYR A 94  ? 1.544 2.159 1.548 0.058  0.135  0.054  423 TYR AAA CA  
705   C C   . TYR A 94  ? 1.539 2.128 1.541 0.040  0.137  0.063  423 TYR AAA C   
706   O O   . TYR A 94  ? 1.500 2.060 1.502 0.047  0.127  0.058  423 TYR AAA O   
707   C CB  . TYR A 94  ? 1.502 2.120 1.533 0.075  0.123  0.033  423 TYR AAA CB  
708   C CG  . TYR A 94  ? 1.453 2.084 1.524 0.069  0.127  0.026  423 TYR AAA CG  
709   C CD1 . TYR A 94  ? 1.438 2.099 1.529 0.067  0.139  0.029  423 TYR AAA CD1 
710   C CD2 . TYR A 94  ? 1.442 2.054 1.530 0.066  0.120  0.019  423 TYR AAA CD2 
711   C CE1 . TYR A 94  ? 1.417 2.089 1.541 0.063  0.142  0.028  423 TYR AAA CE1 
712   C CE2 . TYR A 94  ? 1.419 2.039 1.536 0.060  0.125  0.014  423 TYR AAA CE2 
713   C CZ  . TYR A 94  ? 1.404 2.053 1.536 0.058  0.134  0.020  423 TYR AAA CZ  
714   O OH  . TYR A 94  ? 1.375 2.030 1.532 0.054  0.138  0.019  423 TYR AAA OH  
715   N N   . LYS A 95  ? 1.558 2.161 1.562 0.016  0.150  0.074  424 LYS AAA N   
716   C CA  . LYS A 95  ? 1.592 2.171 1.590 -0.008 0.155  0.080  424 LYS AAA CA  
717   C C   . LYS A 95  ? 1.566 2.164 1.599 -0.016 0.152  0.071  424 LYS AAA C   
718   O O   . LYS A 95  ? 1.540 2.179 1.598 -0.010 0.151  0.069  424 LYS AAA O   
719   C CB  . LYS A 95  ? 1.626 2.214 1.606 -0.036 0.172  0.093  424 LYS AAA CB  
720   C CG  . LYS A 95  ? 1.657 2.209 1.619 -0.064 0.182  0.097  424 LYS AAA CG  
721   C CD  . LYS A 95  ? 1.720 2.219 1.638 -0.064 0.193  0.108  424 LYS AAA CD  
722   C CE  . LYS A 95  ? 1.753 2.203 1.652 -0.091 0.208  0.109  424 LYS AAA CE  
723   N NZ  . LYS A 95  ? 1.757 2.163 1.659 -0.073 0.201  0.103  424 LYS AAA NZ  
724   N N   . LEU A 96  ? 1.579 2.145 1.611 -0.028 0.152  0.066  425 LEU AAA N   
725   C CA  . LEU A 96  ? 1.565 2.143 1.618 -0.044 0.152  0.060  425 LEU AAA CA  
726   C C   . LEU A 96  ? 1.578 2.147 1.614 -0.081 0.163  0.065  425 LEU AAA C   
727   O O   . LEU A 96  ? 1.606 2.133 1.615 -0.090 0.173  0.068  425 LEU AAA O   
728   C CB  . LEU A 96  ? 1.568 2.114 1.634 -0.030 0.146  0.045  425 LEU AAA CB  
729   C CG  . LEU A 96  ? 1.545 2.109 1.638 -0.003 0.136  0.034  425 LEU AAA CG  
730   C CD1 . LEU A 96  ? 1.544 2.079 1.653 0.005  0.133  0.018  425 LEU AAA CD1 
731   C CD2 . LEU A 96  ? 1.526 2.133 1.640 -0.005 0.137  0.037  425 LEU AAA CD2 
732   N N   . PRO A 97  ? 1.555 2.162 1.604 -0.103 0.163  0.066  426 PRO AAA N   
733   C CA  . PRO A 97  ? 1.592 2.199 1.623 -0.144 0.173  0.067  426 PRO AAA CA  
734   C C   . PRO A 97  ? 1.638 2.193 1.656 -0.158 0.179  0.054  426 PRO AAA C   
735   O O   . PRO A 97  ? 1.625 2.164 1.658 -0.139 0.173  0.045  426 PRO AAA O   
736   C CB  . PRO A 97  ? 1.561 2.236 1.614 -0.155 0.165  0.073  426 PRO AAA CB  
737   C CG  . PRO A 97  ? 1.524 2.207 1.602 -0.122 0.154  0.071  426 PRO AAA CG  
738   C CD  . PRO A 97  ? 1.514 2.168 1.593 -0.090 0.154  0.067  426 PRO AAA CD  
739   N N   . ASP A 98  ? 1.728 2.260 1.721 -0.195 0.194  0.051  427 ASP AAA N   
740   C CA  . ASP A 98  ? 1.800 2.276 1.775 -0.216 0.208  0.037  427 ASP AAA CA  
741   C C   . ASP A 98  ? 1.789 2.287 1.775 -0.226 0.200  0.028  427 ASP AAA C   
742   O O   . ASP A 98  ? 1.787 2.241 1.773 -0.220 0.207  0.015  427 ASP AAA O   
743   C CB  . ASP A 98  ? 1.881 2.332 1.824 -0.259 0.229  0.035  427 ASP AAA CB  
744   C CG  . ASP A 98  ? 1.923 2.365 1.853 -0.253 0.237  0.048  427 ASP AAA CG  
745   O OD1 . ASP A 98  ? 1.944 2.354 1.873 -0.215 0.234  0.055  427 ASP AAA OD1 
746   O OD2 . ASP A 98  ? 1.941 2.411 1.860 -0.287 0.245  0.051  427 ASP AAA OD2 
747   N N   . ASP A 99  ? 1.764 2.331 1.761 -0.238 0.188  0.035  428 ASP AAA N   
748   C CA  . ASP A 99  ? 1.727 2.321 1.730 -0.247 0.179  0.032  428 ASP AAA CA  
749   C C   . ASP A 99  ? 1.645 2.257 1.678 -0.203 0.166  0.038  428 ASP AAA C   
750   O O   . ASP A 99  ? 1.604 2.268 1.650 -0.201 0.154  0.049  428 ASP AAA O   
751   C CB  . ASP A 99  ? 1.754 2.413 1.750 -0.283 0.172  0.039  428 ASP AAA CB  
752   C CG  . ASP A 99  ? 1.747 2.476 1.769 -0.270 0.160  0.058  428 ASP AAA CG  
753   O OD1 . ASP A 99  ? 1.709 2.441 1.754 -0.229 0.155  0.066  428 ASP AAA OD1 
754   O OD2 . ASP A 99  ? 1.784 2.567 1.803 -0.303 0.157  0.063  428 ASP AAA OD2 
755   N N   . PHE A 100 ? 1.597 2.170 1.642 -0.171 0.168  0.033  429 PHE AAA N   
756   C CA  . PHE A 100 ? 1.540 2.122 1.612 -0.133 0.159  0.033  429 PHE AAA CA  
757   C C   . PHE A 100 ? 1.546 2.111 1.622 -0.137 0.161  0.023  429 PHE AAA C   
758   O O   . PHE A 100 ? 1.577 2.097 1.638 -0.152 0.173  0.009  429 PHE AAA O   
759   C CB  . PHE A 100 ? 1.513 2.064 1.594 -0.103 0.159  0.028  429 PHE AAA CB  
760   C CG  . PHE A 100 ? 1.475 2.034 1.583 -0.070 0.152  0.022  429 PHE AAA CG  
761   C CD1 . PHE A 100 ? 1.458 2.061 1.582 -0.058 0.146  0.032  429 PHE AAA CD1 
762   C CD2 . PHE A 100 ? 1.483 2.007 1.604 -0.052 0.152  0.007  429 PHE AAA CD2 
763   C CE1 . PHE A 100 ? 1.462 2.066 1.609 -0.030 0.144  0.024  429 PHE AAA CE1 
764   C CE2 . PHE A 100 ? 1.478 2.011 1.624 -0.027 0.147  -0.002 429 PHE AAA CE2 
765   C CZ  . PHE A 100 ? 1.469 2.038 1.626 -0.017 0.145  0.006  429 PHE AAA CZ  
766   N N   . THR A 101 ? 1.535 2.132 1.626 -0.122 0.154  0.030  430 THR AAA N   
767   C CA  . THR A 101 ? 1.545 2.126 1.637 -0.124 0.159  0.023  430 THR AAA CA  
768   C C   . THR A 101 ? 1.484 2.066 1.606 -0.088 0.158  0.021  430 THR AAA C   
769   O O   . THR A 101 ? 1.487 2.098 1.617 -0.077 0.154  0.035  430 THR AAA O   
770   C CB  . THR A 101 ? 1.604 2.221 1.677 -0.148 0.154  0.036  430 THR AAA CB  
771   O OG1 . THR A 101 ? 1.649 2.323 1.740 -0.131 0.143  0.058  430 THR AAA OG1 
772   C CG2 . THR A 101 ? 1.652 2.269 1.694 -0.190 0.157  0.033  430 THR AAA CG2 
773   N N   . GLY A 102 ? 1.444 1.994 1.581 -0.070 0.161  0.005  431 GLY AAA N   
774   C CA  . GLY A 102 ? 1.428 1.976 1.593 -0.040 0.161  -0.004 431 GLY AAA CA  
775   C C   . GLY A 102 ? 1.437 1.950 1.616 -0.030 0.164  -0.026 431 GLY AAA C   
776   O O   . GLY A 102 ? 1.434 1.918 1.603 -0.045 0.170  -0.033 431 GLY AAA O   
777   N N   . CYS A 103 ? 1.449 1.966 1.653 -0.006 0.162  -0.036 432 CYS AAA N   
778   C CA  . CYS A 103 ? 1.471 1.969 1.697 0.006  0.161  -0.058 432 CYS AAA CA  
779   C C   . CYS A 103 ? 1.455 1.972 1.688 0.028  0.148  -0.060 432 CYS AAA C   
780   O O   . CYS A 103 ? 1.482 2.022 1.714 0.036  0.147  -0.053 432 CYS AAA O   
781   C CB  . CYS A 103 ? 1.497 1.979 1.747 0.008  0.172  -0.077 432 CYS AAA CB  
782   S SG  . CYS A 103 ? 1.558 2.016 1.790 -0.020 0.189  -0.074 432 CYS AAA SG  
783   N N   . VAL A 104 ? 1.414 1.923 1.655 0.038  0.140  -0.069 433 VAL AAA N   
784   C CA  . VAL A 104 ? 1.383 1.909 1.628 0.059  0.126  -0.074 433 VAL AAA CA  
785   C C   . VAL A 104 ? 1.382 1.912 1.664 0.069  0.125  -0.100 433 VAL AAA C   
786   O O   . VAL A 104 ? 1.354 1.868 1.654 0.067  0.128  -0.110 433 VAL AAA O   
787   C CB  . VAL A 104 ? 1.388 1.902 1.612 0.063  0.118  -0.061 433 VAL AAA CB  
788   C CG1 . VAL A 104 ? 1.413 1.943 1.640 0.085  0.101  -0.066 433 VAL AAA CG1 
789   C CG2 . VAL A 104 ? 1.380 1.895 1.570 0.049  0.121  -0.038 433 VAL AAA CG2 
790   N N   . ILE A 105 ? 1.422 1.972 1.715 0.077  0.124  -0.113 434 ILE AAA N   
791   C CA  . ILE A 105 ? 1.474 2.032 1.803 0.082  0.124  -0.143 434 ILE AAA CA  
792   C C   . ILE A 105 ? 1.489 2.076 1.817 0.096  0.106  -0.153 434 ILE AAA C   
793   O O   . ILE A 105 ? 1.484 2.081 1.792 0.098  0.107  -0.148 434 ILE AAA O   
794   C CB  . ILE A 105 ? 1.488 2.037 1.830 0.073  0.145  -0.154 434 ILE AAA CB  
795   C CG1 . ILE A 105 ? 1.494 2.018 1.823 0.059  0.160  -0.137 434 ILE AAA CG1 
796   C CG2 . ILE A 105 ? 1.478 2.032 1.860 0.072  0.151  -0.187 434 ILE AAA CG2 
797   C CD1 . ILE A 105 ? 1.506 2.024 1.830 0.055  0.177  -0.131 434 ILE AAA CD1 
798   N N   . ALA A 106 ? 1.499 2.101 1.849 0.106  0.091  -0.166 435 ALA AAA N   
799   C CA  . ALA A 106 ? 1.527 2.160 1.871 0.120  0.068  -0.173 435 ALA AAA CA  
800   C C   . ALA A 106 ? 1.524 2.186 1.914 0.123  0.060  -0.205 435 ALA AAA C   
801   O O   . ALA A 106 ? 1.507 2.165 1.930 0.125  0.061  -0.210 435 ALA AAA O   
802   C CB  . ALA A 106 ? 1.560 2.188 1.877 0.133  0.052  -0.147 435 ALA AAA CB  
803   N N   . TRP A 107 ? 1.543 2.235 1.935 0.122  0.052  -0.228 436 TRP AAA N   
804   C CA  . TRP A 107 ? 1.563 2.296 1.997 0.123  0.038  -0.261 436 TRP AAA CA  
805   C C   . TRP A 107 ? 1.588 2.362 2.000 0.134  0.009  -0.264 436 TRP AAA C   
806   O O   . TRP A 107 ? 1.587 2.352 1.951 0.133  0.010  -0.253 436 TRP AAA O   
807   C CB  . TRP A 107 ? 1.558 2.288 2.021 0.103  0.062  -0.294 436 TRP AAA CB  
808   C CG  . TRP A 107 ? 1.562 2.283 1.995 0.094  0.076  -0.302 436 TRP AAA CG  
809   C CD1 . TRP A 107 ? 1.593 2.343 2.020 0.089  0.068  -0.329 436 TRP AAA CD1 
810   C CD2 . TRP A 107 ? 1.534 2.214 1.939 0.090  0.101  -0.283 436 TRP AAA CD2 
811   N NE1 . TRP A 107 ? 1.599 2.323 1.998 0.082  0.091  -0.329 436 TRP AAA NE1 
812   C CE2 . TRP A 107 ? 1.558 2.242 1.946 0.085  0.110  -0.300 436 TRP AAA CE2 
813   C CE3 . TRP A 107 ? 1.518 2.162 1.912 0.090  0.116  -0.254 436 TRP AAA CE3 
814   C CZ2 . TRP A 107 ? 1.560 2.213 1.925 0.084  0.135  -0.286 436 TRP AAA CZ2 
815   C CZ3 . TRP A 107 ? 1.536 2.158 1.907 0.088  0.136  -0.240 436 TRP AAA CZ3 
816   C CH2 . TRP A 107 ? 1.557 2.182 1.915 0.087  0.146  -0.255 436 TRP AAA CH2 
817   N N   . ASN A 108 ? 1.595 2.413 2.039 0.144  -0.016 -0.278 437 ASN AAA N   
818   C CA  . ASN A 108 ? 1.628 2.496 2.052 0.153  -0.048 -0.284 437 ASN AAA CA  
819   C C   . ASN A 108 ? 1.631 2.515 2.049 0.131  -0.038 -0.320 437 ASN AAA C   
820   O O   . ASN A 108 ? 1.601 2.482 2.059 0.113  -0.017 -0.351 437 ASN AAA O   
821   C CB  . ASN A 108 ? 1.645 2.566 2.116 0.170  -0.077 -0.292 437 ASN AAA CB  
822   C CG  . ASN A 108 ? 1.696 2.670 2.139 0.183  -0.115 -0.290 437 ASN AAA CG  
823   O OD1 . ASN A 108 ? 1.709 2.712 2.136 0.167  -0.121 -0.317 437 ASN AAA OD1 
824   N ND2 . ASN A 108 ? 1.735 2.718 2.169 0.212  -0.139 -0.257 437 ASN AAA ND2 
825   N N   . SER A 109 ? 1.672 2.565 2.036 0.132  -0.050 -0.317 438 SER AAA N   
826   C CA  . SER A 109 ? 1.690 2.588 2.034 0.111  -0.036 -0.349 438 SER AAA CA  
827   C C   . SER A 109 ? 1.735 2.682 2.042 0.114  -0.068 -0.358 438 SER AAA C   
828   O O   . SER A 109 ? 1.797 2.733 2.056 0.104  -0.058 -0.365 438 SER AAA O   
829   C CB  . SER A 109 ? 1.678 2.522 1.988 0.105  -0.003 -0.333 438 SER AAA CB  
830   O OG  . SER A 109 ? 1.681 2.508 1.943 0.122  -0.012 -0.293 438 SER AAA OG  
831   N N   . ASN A 110 ? 1.707 2.708 2.034 0.128  -0.106 -0.357 439 ASN AAA N   
832   C CA  . ASN A 110 ? 1.716 2.779 2.016 0.128  -0.142 -0.372 439 ASN AAA CA  
833   C C   . ASN A 110 ? 1.723 2.804 2.030 0.094  -0.126 -0.426 439 ASN AAA C   
834   O O   . ASN A 110 ? 1.736 2.820 1.988 0.083  -0.126 -0.438 439 ASN AAA O   
835   C CB  . ASN A 110 ? 1.701 2.825 2.042 0.150  -0.183 -0.365 439 ASN AAA CB  
836   C CG  . ASN A 110 ? 1.743 2.916 2.034 0.167  -0.226 -0.349 439 ASN AAA CG  
837   O OD1 . ASN A 110 ? 1.777 2.922 1.994 0.170  -0.225 -0.328 439 ASN AAA OD1 
838   N ND2 . ASN A 110 ? 1.736 2.984 2.067 0.179  -0.264 -0.358 439 ASN AAA ND2 
839   N N   . ASN A 111 ? 1.706 2.791 2.079 0.078  -0.107 -0.458 440 ASN AAA N   
840   C CA  . ASN A 111 ? 1.730 2.829 2.124 0.042  -0.086 -0.514 440 ASN AAA CA  
841   C C   . ASN A 111 ? 1.747 2.793 2.086 0.025  -0.051 -0.524 440 ASN AAA C   
842   O O   . ASN A 111 ? 1.776 2.837 2.112 -0.004 -0.039 -0.571 440 ASN AAA O   
843   C CB  . ASN A 111 ? 1.704 2.792 2.172 0.030  -0.061 -0.536 440 ASN AAA CB  
844   C CG  . ASN A 111 ? 1.670 2.680 2.143 0.038  -0.024 -0.506 440 ASN AAA CG  
845   O OD1 . ASN A 111 ? 1.637 2.627 2.103 0.063  -0.033 -0.463 440 ASN AAA OD1 
846   N ND2 . ASN A 111 ? 1.665 2.631 2.151 0.016  0.019  -0.530 440 ASN AAA ND2 
847   N N   . LEU A 112 ? 1.737 2.726 2.036 0.041  -0.034 -0.483 441 LEU AAA N   
848   C CA  . LEU A 112 ? 1.760 2.694 2.019 0.029  0.006  -0.488 441 LEU AAA CA  
849   C C   . LEU A 112 ? 1.794 2.722 1.982 0.041  -0.004 -0.462 441 LEU AAA C   
850   O O   . LEU A 112 ? 1.830 2.738 1.981 0.026  0.020  -0.482 441 LEU AAA O   
851   C CB  . LEU A 112 ? 1.723 2.595 2.007 0.037  0.042  -0.464 441 LEU AAA CB  
852   C CG  . LEU A 112 ? 1.694 2.558 2.042 0.023  0.062  -0.490 441 LEU AAA CG  
853   C CD1 . LEU A 112 ? 1.653 2.466 2.019 0.035  0.085  -0.455 441 LEU AAA CD1 
854   C CD2 . LEU A 112 ? 1.710 2.562 2.064 -0.007 0.095  -0.538 441 LEU AAA CD2 
855   N N   . ASP A 113 ? 1.798 2.736 1.964 0.066  -0.034 -0.420 442 ASP AAA N   
856   C CA  . ASP A 113 ? 1.843 2.759 1.943 0.079  -0.034 -0.385 442 ASP AAA CA  
857   C C   . ASP A 113 ? 1.901 2.864 1.956 0.089  -0.078 -0.376 442 ASP AAA C   
858   O O   . ASP A 113 ? 1.911 2.854 1.914 0.104  -0.083 -0.338 442 ASP AAA O   
859   C CB  . ASP A 113 ? 1.815 2.688 1.922 0.098  -0.023 -0.338 442 ASP AAA CB  
860   C CG  . ASP A 113 ? 1.775 2.603 1.918 0.091  0.018  -0.341 442 ASP AAA CG  
861   O OD1 . ASP A 113 ? 1.800 2.606 1.928 0.079  0.049  -0.357 442 ASP AAA OD1 
862   O OD2 . ASP A 113 ? 1.720 2.534 1.903 0.098  0.020  -0.324 442 ASP AAA OD2 
863   N N   . SER A 114 ? 1.954 2.977 2.024 0.080  -0.108 -0.408 443 SER AAA N   
864   C CA  . SER A 114 ? 2.025 3.105 2.057 0.091  -0.156 -0.399 443 SER AAA CA  
865   C C   . SER A 114 ? 2.068 3.198 2.076 0.063  -0.167 -0.449 443 SER AAA C   
866   O O   . SER A 114 ? 2.062 3.227 2.124 0.043  -0.167 -0.492 443 SER AAA O   
867   C CB  . SER A 114 ? 2.027 3.147 2.112 0.115  -0.191 -0.381 443 SER AAA CB  
868   O OG  . SER A 114 ? 2.014 3.085 2.116 0.138  -0.178 -0.337 443 SER AAA OG  
869   N N   . LYS A 115 ? 2.113 3.248 2.040 0.060  -0.177 -0.444 444 LYS AAA N   
870   C CA  . LYS A 115 ? 2.178 3.363 2.066 0.032  -0.192 -0.491 444 LYS AAA CA  
871   C C   . LYS A 115 ? 2.195 3.454 2.056 0.048  -0.252 -0.475 444 LYS AAA C   
872   O O   . LYS A 115 ? 2.183 3.432 2.027 0.083  -0.274 -0.420 444 LYS AAA O   
873   C CB  . LYS A 115 ? 2.255 3.392 2.064 0.015  -0.158 -0.498 444 LYS AAA CB  
874   C CG  . LYS A 115 ? 2.239 3.303 2.071 0.005  -0.098 -0.506 444 LYS AAA CG  
875   C CD  . LYS A 115 ? 2.305 3.322 2.062 -0.002 -0.065 -0.503 444 LYS AAA CD  
876   C CE  . LYS A 115 ? 2.278 3.226 2.062 -0.002 -0.008 -0.497 444 LYS AAA CE  
877   N NZ  . LYS A 115 ? 2.313 3.220 2.035 0.006  0.015  -0.470 444 LYS AAA NZ  
878   N N   . VAL A 116 ? 2.213 3.543 2.068 0.023  -0.278 -0.520 445 VAL AAA N   
879   C CA  . VAL A 116 ? 2.257 3.670 2.076 0.035  -0.339 -0.510 445 VAL AAA CA  
880   C C   . VAL A 116 ? 2.318 3.698 2.033 0.051  -0.345 -0.467 445 VAL AAA C   
881   O O   . VAL A 116 ? 2.333 3.733 2.028 0.088  -0.384 -0.418 445 VAL AAA O   
882   C CB  . VAL A 116 ? 2.287 3.781 2.108 -0.006 -0.360 -0.575 445 VAL AAA CB  
883   C CG1 . VAL A 116 ? 2.219 3.752 2.148 -0.020 -0.357 -0.613 445 VAL AAA CG1 
884   C CG2 . VAL A 116 ? 2.341 3.798 2.095 -0.048 -0.321 -0.620 445 VAL AAA CG2 
885   N N   . GLY A 117 ? 2.357 3.679 2.009 0.028  -0.304 -0.483 446 GLY AAA N   
886   C CA  . GLY A 117 ? 2.419 3.703 1.971 0.038  -0.299 -0.448 446 GLY AAA CA  
887   C C   . GLY A 117 ? 2.385 3.601 1.941 0.074  -0.281 -0.386 446 GLY AAA C   
888   O O   . GLY A 117 ? 2.404 3.592 1.880 0.087  -0.284 -0.349 446 GLY AAA O   
889   N N   . GLY A 118 ? 2.332 3.521 1.974 0.085  -0.263 -0.378 447 GLY AAA N   
890   C CA  . GLY A 118 ? 2.306 3.432 1.966 0.113  -0.242 -0.327 447 GLY AAA CA  
891   C C   . GLY A 118 ? 2.289 3.346 1.951 0.097  -0.184 -0.334 447 GLY AAA C   
892   O O   . GLY A 118 ? 2.354 3.387 1.946 0.083  -0.163 -0.340 447 GLY AAA O   
893   N N   . ASN A 119 ? 2.216 3.242 1.952 0.100  -0.158 -0.333 448 ASN AAA N   
894   C CA  . ASN A 119 ? 2.184 3.149 1.932 0.089  -0.105 -0.337 448 ASN AAA CA  
895   C C   . ASN A 119 ? 2.190 3.109 1.902 0.108  -0.092 -0.285 448 ASN AAA C   
896   O O   . ASN A 119 ? 2.134 3.031 1.885 0.126  -0.091 -0.253 448 ASN AAA O   
897   C CB  . ASN A 119 ? 2.114 3.066 1.949 0.085  -0.084 -0.353 448 ASN AAA CB  
898   C CG  . ASN A 119 ? 2.084 2.984 1.930 0.072  -0.031 -0.363 448 ASN AAA CG  
899   O OD1 . ASN A 119 ? 2.090 2.959 1.889 0.073  -0.008 -0.348 448 ASN AAA OD1 
900   N ND2 . ASN A 119 ? 2.027 2.917 1.937 0.063  -0.010 -0.388 448 ASN AAA ND2 
901   N N   . TYR A 120 ? 2.276 3.178 1.913 0.101  -0.078 -0.280 449 TYR AAA N   
902   C CA  . TYR A 120 ? 2.327 3.187 1.918 0.115  -0.064 -0.234 449 TYR AAA CA  
903   C C   . TYR A 120 ? 2.285 3.101 1.906 0.107  -0.013 -0.233 449 TYR AAA C   
904   O O   . TYR A 120 ? 2.299 3.083 1.894 0.115  0.004  -0.199 449 TYR AAA O   
905   C CB  . TYR A 120 ? 2.435 3.302 1.930 0.110  -0.074 -0.230 449 TYR AAA CB  
906   C CG  . TYR A 120 ? 2.487 3.401 1.944 0.121  -0.126 -0.223 449 TYR AAA CG  
907   C CD1 . TYR A 120 ? 2.473 3.387 1.930 0.150  -0.157 -0.177 449 TYR AAA CD1 
908   C CD2 . TYR A 120 ? 2.550 3.509 1.966 0.102  -0.145 -0.261 449 TYR AAA CD2 
909   C CE1 . TYR A 120 ? 2.515 3.475 1.939 0.165  -0.206 -0.166 449 TYR AAA CE1 
910   C CE2 . TYR A 120 ? 2.593 3.604 1.974 0.114  -0.198 -0.253 449 TYR AAA CE2 
911   C CZ  . TYR A 120 ? 2.580 3.593 1.967 0.148  -0.229 -0.203 449 TYR AAA CZ  
912   O OH  . TYR A 120 ? 2.635 3.702 1.990 0.164  -0.281 -0.190 449 TYR AAA OH  
913   N N   . ASN A 121 ? 2.227 3.041 1.902 0.094  0.010  -0.268 450 ASN AAA N   
914   C CA  . ASN A 121 ? 2.167 2.945 1.869 0.089  0.059  -0.271 450 ASN AAA CA  
915   C C   . ASN A 121 ? 2.048 2.805 1.806 0.103  0.066  -0.237 450 ASN AAA C   
916   O O   . ASN A 121 ? 1.951 2.684 1.731 0.102  0.103  -0.231 450 ASN AAA O   
917   C CB  . ASN A 121 ? 2.185 2.963 1.920 0.071  0.084  -0.319 450 ASN AAA CB  
918   C CG  . ASN A 121 ? 2.273 3.063 1.951 0.050  0.088  -0.358 450 ASN AAA CG  
919   O OD1 . ASN A 121 ? 2.313 3.139 1.985 0.039  0.060  -0.388 450 ASN AAA OD1 
920   N ND2 . ASN A 121 ? 2.299 3.063 1.934 0.044  0.124  -0.361 450 ASN AAA ND2 
921   N N   . TYR A 122 ? 2.016 2.785 1.797 0.115  0.034  -0.217 451 TYR AAA N   
922   C CA  . TYR A 122 ? 1.961 2.711 1.782 0.127  0.038  -0.183 451 TYR AAA CA  
923   C C   . TYR A 122 ? 1.970 2.706 1.742 0.137  0.028  -0.142 451 TYR AAA C   
924   O O   . TYR A 122 ? 2.011 2.761 1.742 0.145  -0.002 -0.135 451 TYR AAA O   
925   C CB  . TYR A 122 ? 1.936 2.700 1.814 0.133  0.015  -0.189 451 TYR AAA CB  
926   C CG  . TYR A 122 ? 1.918 2.681 1.851 0.122  0.035  -0.221 451 TYR AAA CG  
927   C CD1 . TYR A 122 ? 1.872 2.609 1.843 0.121  0.063  -0.210 451 TYR AAA CD1 
928   C CD2 . TYR A 122 ? 1.949 2.738 1.894 0.111  0.026  -0.262 451 TYR AAA CD2 
929   C CE1 . TYR A 122 ? 1.848 2.579 1.865 0.113  0.084  -0.236 451 TYR AAA CE1 
930   C CE2 . TYR A 122 ? 1.919 2.700 1.912 0.099  0.049  -0.292 451 TYR AAA CE2 
931   C CZ  . TYR A 122 ? 1.869 2.618 1.897 0.102  0.079  -0.277 451 TYR AAA CZ  
932   O OH  . TYR A 122 ? 1.845 2.581 1.916 0.092  0.103  -0.303 451 TYR AAA OH  
933   N N   . LEU A 123 ? 1.915 2.624 1.692 0.137  0.053  -0.116 452 LEU AAA N   
934   C CA  . LEU A 123 ? 1.921 2.611 1.647 0.140  0.057  -0.081 452 LEU AAA CA  
935   C C   . LEU A 123 ? 1.850 2.520 1.607 0.144  0.059  -0.050 452 LEU AAA C   
936   O O   . LEU A 123 ? 1.811 2.485 1.627 0.143  0.060  -0.058 452 LEU AAA O   
937   C CB  . LEU A 123 ? 1.942 2.624 1.644 0.129  0.093  -0.084 452 LEU AAA CB  
938   C CG  . LEU A 123 ? 1.973 2.668 1.653 0.120  0.103  -0.121 452 LEU AAA CG  
939   C CD1 . LEU A 123 ? 1.978 2.663 1.650 0.112  0.145  -0.124 452 LEU AAA CD1 
940   C CD2 . LEU A 123 ? 2.033 2.740 1.646 0.122  0.075  -0.126 452 LEU AAA CD2 
941   N N   . TYR A 124 ? 1.845 2.493 1.559 0.145  0.063  -0.018 453 TYR AAA N   
942   C CA  . TYR A 124 ? 1.831 2.454 1.561 0.144  0.069  0.011  453 TYR AAA CA  
943   C C   . TYR A 124 ? 1.871 2.470 1.545 0.138  0.086  0.039  453 TYR AAA C   
944   O O   . TYR A 124 ? 1.914 2.507 1.527 0.143  0.079  0.044  453 TYR AAA O   
945   C CB  . TYR A 124 ? 1.843 2.459 1.586 0.159  0.040  0.020  453 TYR AAA CB  
946   C CG  . TYR A 124 ? 1.915 2.519 1.601 0.174  0.019  0.041  453 TYR AAA CG  
947   C CD1 . TYR A 124 ? 1.964 2.594 1.618 0.184  -0.005 0.027  453 TYR AAA CD1 
948   C CD2 . TYR A 124 ? 1.949 2.514 1.611 0.180  0.022  0.076  453 TYR AAA CD2 
949   C CE1 . TYR A 124 ? 2.036 2.658 1.635 0.201  -0.028 0.050  453 TYR AAA CE1 
950   C CE2 . TYR A 124 ? 2.029 2.577 1.636 0.198  0.004  0.100  453 TYR AAA CE2 
951   C CZ  . TYR A 124 ? 2.071 2.650 1.647 0.211  -0.023 0.089  453 TYR AAA CZ  
952   O OH  . TYR A 124 ? 2.130 2.698 1.648 0.232  -0.044 0.115  453 TYR AAA OH  
953   N N   . ARG A 125 ? 1.890 2.476 1.583 0.125  0.109  0.054  454 ARG AAA N   
954   C CA  . ARG A 125 ? 1.981 2.544 1.631 0.114  0.131  0.080  454 ARG AAA CA  
955   C C   . ARG A 125 ? 2.047 2.570 1.661 0.122  0.118  0.107  454 ARG AAA C   
956   O O   . ARG A 125 ? 2.020 2.538 1.665 0.132  0.098  0.107  454 ARG AAA O   
957   C CB  . ARG A 125 ? 1.972 2.544 1.664 0.094  0.158  0.084  454 ARG AAA CB  
958   C CG  . ARG A 125 ? 2.027 2.584 1.681 0.078  0.186  0.104  454 ARG AAA CG  
959   C CD  . ARG A 125 ? 1.995 2.577 1.699 0.058  0.210  0.105  454 ARG AAA CD  
960   N NE  . ARG A 125 ? 1.952 2.575 1.694 0.062  0.220  0.085  454 ARG AAA NE  
961   C CZ  . ARG A 125 ? 1.958 2.595 1.682 0.059  0.243  0.080  454 ARG AAA CZ  
962   N NH1 . ARG A 125 ? 2.000 2.615 1.665 0.051  0.258  0.093  454 ARG AAA NH1 
963   N NH2 . ARG A 125 ? 1.931 2.601 1.695 0.065  0.255  0.062  454 ARG AAA NH2 
964   N N   . LEU A 126 ? 2.144 2.638 1.696 0.117  0.132  0.130  455 LEU AAA N   
965   C CA  . LEU A 126 ? 2.226 2.674 1.727 0.130  0.122  0.159  455 LEU AAA CA  
966   C C   . LEU A 126 ? 2.265 2.671 1.742 0.110  0.154  0.184  455 LEU AAA C   
967   O O   . LEU A 126 ? 2.297 2.660 1.763 0.116  0.152  0.206  455 LEU AAA O   
968   C CB  . LEU A 126 ? 2.295 2.744 1.727 0.146  0.106  0.164  455 LEU AAA CB  
969   C CG  . LEU A 126 ? 2.345 2.765 1.737 0.172  0.080  0.189  455 LEU AAA CG  
970   C CD1 . LEU A 126 ? 2.289 2.724 1.743 0.189  0.053  0.180  455 LEU AAA CD1 
971   C CD2 . LEU A 126 ? 2.404 2.837 1.727 0.186  0.060  0.191  455 LEU AAA CD2 
972   N N   . PHE A 127 ? 2.259 2.678 1.730 0.088  0.184  0.180  456 PHE AAA N   
973   C CA  . PHE A 127 ? 2.282 2.671 1.735 0.062  0.218  0.199  456 PHE AAA CA  
974   C C   . PHE A 127 ? 2.203 2.636 1.719 0.037  0.240  0.182  456 PHE AAA C   
975   O O   . PHE A 127 ? 2.133 2.614 1.692 0.042  0.233  0.159  456 PHE AAA O   
976   C CB  . PHE A 127 ? 2.368 2.730 1.743 0.058  0.238  0.215  456 PHE AAA CB  
977   C CG  . PHE A 127 ? 2.436 2.772 1.744 0.087  0.213  0.229  456 PHE AAA CG  
978   C CD1 . PHE A 127 ? 2.466 2.756 1.751 0.105  0.198  0.254  456 PHE AAA CD1 
979   C CD2 . PHE A 127 ? 2.469 2.829 1.738 0.095  0.204  0.217  456 PHE AAA CD2 
980   C CE1 . PHE A 127 ? 2.525 2.800 1.752 0.134  0.171  0.270  456 PHE AAA CE1 
981   C CE2 . PHE A 127 ? 2.533 2.877 1.739 0.120  0.177  0.230  456 PHE AAA CE2 
982   C CZ  . PHE A 127 ? 2.563 2.867 1.749 0.141  0.159  0.258  456 PHE AAA CZ  
983   N N   . ARG A 128 ? 2.204 2.619 1.721 0.011  0.266  0.195  457 ARG AAA N   
984   C CA  . ARG A 128 ? 2.149 2.610 1.723 -0.016 0.288  0.184  457 ARG AAA CA  
985   C C   . ARG A 128 ? 2.194 2.624 1.751 -0.047 0.316  0.200  457 ARG AAA C   
986   O O   . ARG A 128 ? 2.224 2.599 1.756 -0.047 0.313  0.214  457 ARG AAA O   
987   C CB  . ARG A 128 ? 2.081 2.579 1.727 -0.012 0.267  0.168  457 ARG AAA CB  
988   C CG  . ARG A 128 ? 2.040 2.604 1.745 -0.020 0.276  0.152  457 ARG AAA CG  
989   C CD  . ARG A 128 ? 1.977 2.569 1.740 -0.008 0.253  0.137  457 ARG AAA CD  
990   N NE  . ARG A 128 ? 1.930 2.582 1.752 -0.018 0.264  0.130  457 ARG AAA NE  
991   C CZ  . ARG A 128 ? 1.925 2.602 1.779 -0.044 0.274  0.136  457 ARG AAA CZ  
992   N NH1 . ARG A 128 ? 1.958 2.599 1.790 -0.067 0.278  0.145  457 ARG AAA NH1 
993   N NH2 . ARG A 128 ? 1.891 2.629 1.800 -0.048 0.280  0.131  457 ARG AAA NH2 
994   N N   . LYS A 129 ? 2.204 2.667 1.777 -0.073 0.345  0.197  458 LYS AAA N   
995   C CA  . LYS A 129 ? 2.257 2.698 1.816 -0.110 0.378  0.208  458 LYS AAA CA  
996   C C   . LYS A 129 ? 2.237 2.667 1.830 -0.127 0.370  0.206  458 LYS AAA C   
997   O O   . LYS A 129 ? 2.314 2.686 1.870 -0.145 0.388  0.219  458 LYS AAA O   
998   C CB  . LYS A 129 ? 2.245 2.742 1.832 -0.135 0.408  0.201  458 LYS AAA CB  
999   C CG  . LYS A 129 ? 2.289 2.784 1.831 -0.122 0.423  0.202  458 LYS AAA CG  
1000  C CD  . LYS A 129 ? 2.331 2.829 1.855 -0.153 0.467  0.208  458 LYS AAA CD  
1001  C CE  . LYS A 129 ? 2.375 2.858 1.841 -0.140 0.483  0.210  458 LYS AAA CE  
1002  N NZ  . LYS A 129 ? 2.436 2.897 1.862 -0.170 0.528  0.219  458 LYS AAA NZ  
1003  N N   . SER A 130 ? 2.156 2.634 1.811 -0.119 0.346  0.191  459 SER AAA N   
1004  C CA  . SER A 130 ? 2.114 2.587 1.802 -0.135 0.337  0.186  459 SER AAA CA  
1005  C C   . SER A 130 ? 2.028 2.512 1.746 -0.104 0.302  0.176  459 SER AAA C   
1006  O O   . SER A 130 ? 2.005 2.505 1.722 -0.074 0.287  0.171  459 SER AAA O   
1007  C CB  . SER A 130 ? 2.098 2.632 1.837 -0.172 0.351  0.177  459 SER AAA CB  
1008  O OG  . SER A 130 ? 2.038 2.645 1.838 -0.158 0.331  0.164  459 SER AAA OG  
1009  N N   . ASN A 131 ? 1.976 2.450 1.719 -0.115 0.294  0.170  460 ASN AAA N   
1010  C CA  . ASN A 131 ? 1.890 2.374 1.666 -0.092 0.265  0.159  460 ASN AAA CA  
1011  C C   . ASN A 131 ? 1.799 2.361 1.635 -0.094 0.256  0.146  460 ASN AAA C   
1012  O O   . ASN A 131 ? 1.783 2.388 1.640 -0.121 0.272  0.146  460 ASN AAA O   
1013  C CB  . ASN A 131 ? 1.889 2.328 1.664 -0.104 0.265  0.159  460 ASN AAA CB  
1014  C CG  . ASN A 131 ? 1.948 2.306 1.667 -0.098 0.277  0.175  460 ASN AAA CG  
1015  O OD1 . ASN A 131 ? 1.949 2.281 1.640 -0.064 0.264  0.184  460 ASN AAA OD1 
1016  N ND2 . ASN A 131 ? 1.974 2.292 1.676 -0.132 0.302  0.179  460 ASN AAA ND2 
1017  N N   . LEU A 132 ? 1.745 2.324 1.607 -0.066 0.234  0.136  461 LEU AAA N   
1018  C CA  . LEU A 132 ? 1.693 2.335 1.609 -0.062 0.226  0.126  461 LEU AAA CA  
1019  C C   . LEU A 132 ? 1.690 2.350 1.635 -0.090 0.225  0.124  461 LEU AAA C   
1020  O O   . LEU A 132 ? 1.705 2.320 1.634 -0.099 0.222  0.123  461 LEU AAA O   
1021  C CB  . LEU A 132 ? 1.671 2.310 1.601 -0.029 0.205  0.115  461 LEU AAA CB  
1022  C CG  . LEU A 132 ? 1.694 2.335 1.606 -0.004 0.204  0.110  461 LEU AAA CG  
1023  C CD1 . LEU A 132 ? 1.665 2.303 1.593 0.022  0.183  0.095  461 LEU AAA CD1 
1024  C CD2 . LEU A 132 ? 1.696 2.386 1.629 -0.006 0.220  0.110  461 LEU AAA CD2 
1025  N N   . LYS A 133 ? 1.686 2.412 1.673 -0.101 0.227  0.124  462 LYS AAA N   
1026  C CA  . LYS A 133 ? 1.690 2.448 1.709 -0.121 0.219  0.121  462 LYS AAA CA  
1027  C C   . LYS A 133 ? 1.655 2.401 1.690 -0.095 0.200  0.113  462 LYS AAA C   
1028  O O   . LYS A 133 ? 1.652 2.391 1.689 -0.064 0.194  0.109  462 LYS AAA O   
1029  C CB  . LYS A 133 ? 1.699 2.539 1.760 -0.133 0.224  0.126  462 LYS AAA CB  
1030  C CG  . LYS A 133 ? 1.739 2.606 1.799 -0.177 0.237  0.130  462 LYS AAA CG  
1031  C CD  . LYS A 133 ? 1.719 2.669 1.827 -0.194 0.228  0.133  462 LYS AAA CD  
1032  C CE  . LYS A 133 ? 1.760 2.736 1.866 -0.245 0.237  0.130  462 LYS AAA CE  
1033  N NZ  . LYS A 133 ? 1.801 2.817 1.917 -0.261 0.258  0.135  462 LYS AAA NZ  
1034  N N   . PRO A 134 ? 1.633 2.376 1.678 -0.110 0.191  0.108  463 PRO AAA N   
1035  C CA  . PRO A 134 ? 1.588 2.321 1.650 -0.089 0.177  0.100  463 PRO AAA CA  
1036  C C   . PRO A 134 ? 1.534 2.312 1.630 -0.061 0.172  0.101  463 PRO AAA C   
1037  O O   . PRO A 134 ? 1.471 2.304 1.591 -0.067 0.176  0.111  463 PRO AAA O   
1038  C CB  . PRO A 134 ? 1.589 2.330 1.656 -0.118 0.173  0.097  463 PRO AAA CB  
1039  C CG  . PRO A 134 ? 1.631 2.356 1.671 -0.154 0.187  0.099  463 PRO AAA CG  
1040  C CD  . PRO A 134 ? 1.650 2.398 1.688 -0.152 0.198  0.108  463 PRO AAA CD  
1041  N N   . PHE A 135 ? 1.540 2.292 1.639 -0.032 0.165  0.092  464 PHE AAA N   
1042  C CA  . PHE A 135 ? 1.539 2.318 1.667 -0.005 0.165  0.090  464 PHE AAA CA  
1043  C C   . PHE A 135 ? 1.541 2.353 1.673 0.002  0.178  0.097  464 PHE AAA C   
1044  O O   . PHE A 135 ? 1.506 2.358 1.671 0.016  0.184  0.102  464 PHE AAA O   
1045  C CB  . PHE A 135 ? 1.546 2.361 1.706 -0.008 0.161  0.096  464 PHE AAA CB  
1046  C CG  . PHE A 135 ? 1.565 2.349 1.721 -0.014 0.152  0.088  464 PHE AAA CG  
1047  C CD1 . PHE A 135 ? 1.571 2.311 1.723 0.003  0.149  0.072  464 PHE AAA CD1 
1048  C CD2 . PHE A 135 ? 1.577 2.380 1.736 -0.038 0.148  0.095  464 PHE AAA CD2 
1049  C CE1 . PHE A 135 ? 1.565 2.279 1.718 -0.003 0.144  0.063  464 PHE AAA CE1 
1050  C CE2 . PHE A 135 ? 1.593 2.366 1.746 -0.045 0.143  0.086  464 PHE AAA CE2 
1051  C CZ  . PHE A 135 ? 1.582 2.309 1.734 -0.027 0.142  0.071  464 PHE AAA CZ  
1052  N N   . GLU A 136 ? 1.584 2.377 1.684 -0.005 0.185  0.098  465 GLU AAA N   
1053  C CA  . GLU A 136 ? 1.616 2.433 1.714 0.003  0.201  0.102  465 GLU AAA CA  
1054  C C   . GLU A 136 ? 1.632 2.421 1.714 0.029  0.200  0.088  465 GLU AAA C   
1055  O O   . GLU A 136 ? 1.634 2.382 1.695 0.035  0.187  0.078  465 GLU AAA O   
1056  C CB  . GLU A 136 ? 1.664 2.475 1.733 -0.021 0.212  0.110  465 GLU AAA CB  
1057  C CG  . GLU A 136 ? 1.689 2.529 1.759 -0.017 0.232  0.114  465 GLU AAA CG  
1058  C CD  . GLU A 136 ? 1.724 2.571 1.774 -0.045 0.249  0.124  465 GLU AAA CD  
1059  O OE1 . GLU A 136 ? 1.745 2.568 1.776 -0.070 0.246  0.128  465 GLU AAA OE1 
1060  O OE2 . GLU A 136 ? 1.711 2.587 1.767 -0.043 0.269  0.127  465 GLU AAA OE2 
1061  N N   . ARG A 137 ? 1.657 2.470 1.751 0.044  0.215  0.086  466 ARG AAA N   
1062  C CA  . ARG A 137 ? 1.707 2.500 1.789 0.066  0.219  0.069  466 ARG AAA CA  
1063  C C   . ARG A 137 ? 1.757 2.557 1.813 0.066  0.239  0.070  466 ARG AAA C   
1064  O O   . ARG A 137 ? 1.739 2.571 1.823 0.075  0.259  0.071  466 ARG AAA O   
1065  C CB  . ARG A 137 ? 1.715 2.525 1.839 0.085  0.224  0.062  466 ARG AAA CB  
1066  C CG  . ARG A 137 ? 1.771 2.557 1.885 0.103  0.229  0.040  466 ARG AAA CG  
1067  C CD  . ARG A 137 ? 1.792 2.586 1.948 0.120  0.239  0.034  466 ARG AAA CD  
1068  N NE  . ARG A 137 ? 1.856 2.626 2.001 0.133  0.249  0.009  466 ARG AAA NE  
1069  C CZ  . ARG A 137 ? 1.911 2.684 2.045 0.140  0.272  0.000  466 ARG AAA CZ  
1070  N NH1 . ARG A 137 ? 1.938 2.738 2.073 0.137  0.287  0.016  466 ARG AAA NH1 
1071  N NH2 . ARG A 137 ? 1.930 2.679 2.051 0.148  0.281  -0.027 466 ARG AAA NH2 
1072  N N   . ASP A 138 ? 1.810 2.578 1.814 0.057  0.235  0.072  467 ASP AAA N   
1073  C CA  . ASP A 138 ? 1.830 2.597 1.798 0.053  0.255  0.075  467 ASP AAA CA  
1074  C C   . ASP A 138 ? 1.822 2.567 1.758 0.070  0.255  0.056  467 ASP AAA C   
1075  O O   . ASP A 138 ? 1.826 2.541 1.735 0.076  0.232  0.048  467 ASP AAA O   
1076  C CB  . ASP A 138 ? 1.871 2.611 1.794 0.034  0.254  0.089  467 ASP AAA CB  
1077  C CG  . ASP A 138 ? 1.921 2.665 1.812 0.025  0.280  0.095  467 ASP AAA CG  
1078  O OD1 . ASP A 138 ? 1.946 2.710 1.846 0.036  0.298  0.085  467 ASP AAA OD1 
1079  O OD2 . ASP A 138 ? 1.961 2.684 1.819 0.006  0.287  0.109  467 ASP AAA OD2 
1080  N N   . ILE A 139 ? 1.794 2.557 1.733 0.076  0.280  0.048  468 ILE AAA N   
1081  C CA  . ILE A 139 ? 1.808 2.554 1.715 0.089  0.286  0.026  468 ILE AAA CA  
1082  C C   . ILE A 139 ? 1.861 2.606 1.726 0.082  0.313  0.027  468 ILE AAA C   
1083  O O   . ILE A 139 ? 1.896 2.630 1.733 0.088  0.324  0.007  468 ILE AAA O   
1084  C CB  . ILE A 139 ? 1.763 2.525 1.720 0.104  0.297  0.009  468 ILE AAA CB  
1085  C CG1 . ILE A 139 ? 1.761 2.558 1.761 0.109  0.331  0.016  468 ILE AAA CG1 
1086  C CG2 . ILE A 139 ? 1.715 2.476 1.711 0.109  0.275  0.009  468 ILE AAA CG2 
1087  C CD1 . ILE A 139 ? 1.747 2.548 1.787 0.128  0.348  0.000  468 ILE AAA CD1 
1088  N N   . SER A 140 ? 1.879 2.633 1.736 0.066  0.325  0.048  469 SER AAA N   
1089  C CA  . SER A 140 ? 1.943 2.693 1.758 0.056  0.354  0.050  469 SER AAA CA  
1090  C C   . SER A 140 ? 2.008 2.712 1.737 0.055  0.340  0.047  469 SER AAA C   
1091  O O   . SER A 140 ? 2.017 2.697 1.728 0.057  0.309  0.055  469 SER AAA O   
1092  C CB  . SER A 140 ? 1.946 2.716 1.776 0.036  0.370  0.072  469 SER AAA CB  
1093  O OG  . SER A 140 ? 1.962 2.699 1.752 0.022  0.352  0.088  469 SER AAA OG  
1094  N N   . THR A 141 ? 2.055 2.748 1.735 0.054  0.362  0.036  470 THR AAA N   
1095  C CA  . THR A 141 ? 2.117 2.771 1.707 0.053  0.350  0.035  470 THR AAA CA  
1096  C C   . THR A 141 ? 2.205 2.843 1.743 0.037  0.377  0.053  470 THR AAA C   
1097  O O   . THR A 141 ? 2.293 2.913 1.766 0.034  0.392  0.045  470 THR AAA O   
1098  C CB  . THR A 141 ? 2.118 2.769 1.681 0.063  0.351  0.005  470 THR AAA CB  
1099  O OG1 . THR A 141 ? 2.132 2.792 1.688 0.057  0.394  -0.007 470 THR AAA OG1 
1100  C CG2 . THR A 141 ? 2.050 2.718 1.674 0.075  0.335  -0.016 470 THR AAA CG2 
1101  N N   . GLU A 142 ? 2.202 2.846 1.767 0.023  0.385  0.076  471 GLU AAA N   
1102  C CA  . GLU A 142 ? 2.269 2.895 1.791 0.003  0.413  0.095  471 GLU AAA CA  
1103  C C   . GLU A 142 ? 2.328 2.899 1.756 0.005  0.396  0.109  471 GLU AAA C   
1104  O O   . GLU A 142 ? 2.291 2.841 1.716 0.014  0.362  0.119  471 GLU AAA O   
1105  C CB  . GLU A 142 ? 2.254 2.900 1.831 -0.015 0.420  0.112  471 GLU AAA CB  
1106  C CG  . GLU A 142 ? 2.238 2.946 1.895 -0.021 0.448  0.104  471 GLU AAA CG  
1107  C CD  . GLU A 142 ? 2.317 3.034 1.956 -0.038 0.494  0.106  471 GLU AAA CD  
1108  O OE1 . GLU A 142 ? 2.407 3.090 1.974 -0.036 0.507  0.101  471 GLU AAA OE1 
1109  O OE2 . GLU A 142 ? 2.318 3.079 2.013 -0.055 0.515  0.112  471 GLU AAA OE2 
1110  N N   . ILE A 143 ? 2.412 2.958 1.766 -0.002 0.419  0.112  472 ILE AAA N   
1111  C CA  . ILE A 143 ? 2.505 2.996 1.758 0.001  0.405  0.131  472 ILE AAA CA  
1112  C C   . ILE A 143 ? 2.523 2.982 1.771 -0.011 0.407  0.161  472 ILE AAA C   
1113  O O   . ILE A 143 ? 2.554 3.011 1.804 -0.035 0.445  0.170  472 ILE AAA O   
1114  C CB  . ILE A 143 ? 2.595 3.068 1.767 -0.008 0.436  0.127  472 ILE AAA CB  
1115  C CG1 . ILE A 143 ? 2.571 3.078 1.762 -0.002 0.446  0.091  472 ILE AAA CG1 
1116  C CG2 . ILE A 143 ? 2.693 3.113 1.758 -0.001 0.416  0.148  472 ILE AAA CG2 
1117  C CD1 . ILE A 143 ? 2.520 3.043 1.735 0.018  0.404  0.071  472 ILE AAA CD1 
1118  N N   . TYR A 144 ? 2.507 2.942 1.752 0.003  0.371  0.175  473 TYR AAA N   
1119  C CA  . TYR A 144 ? 2.490 2.897 1.752 -0.007 0.371  0.198  473 TYR AAA CA  
1120  C C   . TYR A 144 ? 2.583 2.927 1.759 -0.018 0.392  0.228  473 TYR AAA C   
1121  O O   . TYR A 144 ? 2.626 2.928 1.726 0.001  0.373  0.244  473 TYR AAA O   
1122  C CB  . TYR A 144 ? 2.444 2.843 1.731 0.014  0.328  0.201  473 TYR AAA CB  
1123  C CG  . TYR A 144 ? 2.450 2.808 1.740 0.004  0.331  0.224  473 TYR AAA CG  
1124  C CD1 . TYR A 144 ? 2.395 2.771 1.743 -0.023 0.354  0.221  473 TYR AAA CD1 
1125  C CD2 . TYR A 144 ? 2.516 2.816 1.748 0.021  0.315  0.249  473 TYR AAA CD2 
1126  C CE1 . TYR A 144 ? 2.407 2.741 1.753 -0.037 0.362  0.239  473 TYR AAA CE1 
1127  C CE2 . TYR A 144 ? 2.521 2.775 1.754 0.011  0.324  0.270  473 TYR AAA CE2 
1128  C CZ  . TYR A 144 ? 2.462 2.731 1.751 -0.020 0.349  0.262  473 TYR AAA CZ  
1129  O OH  . TYR A 144 ? 2.466 2.686 1.752 -0.034 0.362  0.278  473 TYR AAA OH  
1130  N N   . GLN A 145 ? 2.589 2.927 1.778 -0.048 0.431  0.235  474 GLN AAA N   
1131  C CA  . GLN A 145 ? 2.676 2.950 1.792 -0.065 0.462  0.263  474 GLN AAA CA  
1132  C C   . GLN A 145 ? 2.683 2.904 1.792 -0.061 0.447  0.286  474 GLN AAA C   
1133  O O   . GLN A 145 ? 2.639 2.872 1.811 -0.081 0.455  0.281  474 GLN AAA O   
1134  C CB  . GLN A 145 ? 2.675 2.972 1.823 -0.103 0.511  0.257  474 GLN AAA CB  
1135  C CG  . GLN A 145 ? 2.773 3.003 1.849 -0.127 0.549  0.282  474 GLN AAA CG  
1136  C CD  . GLN A 145 ? 2.764 3.027 1.879 -0.167 0.598  0.272  474 GLN AAA CD  
1137  O OE1 . GLN A 145 ? 2.659 2.999 1.864 -0.176 0.600  0.249  474 GLN AAA OE1 
1138  N NE2 . GLN A 145 ? 2.859 3.066 1.910 -0.191 0.639  0.291  474 GLN AAA NE2 
1139  N N   . ALA A 146 ? 2.738 2.903 1.773 -0.034 0.425  0.310  475 ALA AAA N   
1140  C CA  . ALA A 146 ? 2.765 2.867 1.779 -0.023 0.415  0.336  475 ALA AAA CA  
1141  C C   . ALA A 146 ? 2.859 2.890 1.814 -0.049 0.462  0.363  475 ALA AAA C   
1142  O O   . ALA A 146 ? 2.855 2.873 1.851 -0.077 0.485  0.361  475 ALA AAA O   
1143  C CB  . ALA A 146 ? 2.796 2.877 1.761 0.019  0.373  0.352  475 ALA AAA CB  
1144  N N   . GLY A 147 ? 2.942 2.929 1.801 -0.043 0.477  0.384  476 GLY AAA N   
1145  C CA  . GLY A 147 ? 3.032 2.938 1.818 -0.064 0.523  0.414  476 GLY AAA CA  
1146  C C   . GLY A 147 ? 3.019 2.950 1.830 -0.112 0.573  0.396  476 GLY AAA C   
1147  O O   . GLY A 147 ? 2.900 2.907 1.805 -0.129 0.571  0.365  476 GLY AAA O   
1148  N N   . SER A 148 ? 3.139 3.009 1.871 -0.131 0.618  0.418  477 SER AAA N   
1149  C CA  . SER A 148 ? 3.162 3.044 1.909 -0.180 0.675  0.405  477 SER AAA CA  
1150  C C   . SER A 148 ? 3.121 3.083 1.897 -0.186 0.679  0.376  477 SER AAA C   
1151  O O   . SER A 148 ? 3.018 3.058 1.892 -0.207 0.686  0.346  477 SER AAA O   
1152  C CB  . SER A 148 ? 3.305 3.090 1.948 -0.197 0.722  0.438  477 SER AAA CB  
1153  O OG  . SER A 148 ? 3.374 3.072 1.970 -0.176 0.712  0.471  477 SER AAA OG  
1154  N N   . THR A 149 ? 3.203 3.147 1.896 -0.166 0.676  0.385  478 THR AAA N   
1155  C CA  . THR A 149 ? 3.196 3.194 1.889 -0.174 0.695  0.360  478 THR AAA CA  
1156  C C   . THR A 149 ? 3.062 3.159 1.869 -0.168 0.670  0.323  478 THR AAA C   
1157  O O   . THR A 149 ? 2.983 3.102 1.826 -0.139 0.621  0.317  478 THR AAA O   
1158  C CB  . THR A 149 ? 3.282 3.242 1.861 -0.147 0.681  0.375  478 THR AAA CB  
1159  O OG1 . THR A 149 ? 3.287 3.223 1.839 -0.108 0.626  0.394  478 THR AAA OG1 
1160  C CG2 . THR A 149 ? 3.411 3.290 1.878 -0.166 0.728  0.405  478 THR AAA CG2 
1161  N N   . PRO A 150 ? 3.023 3.184 1.895 -0.194 0.704  0.297  479 PRO AAA N   
1162  C CA  . PRO A 150 ? 2.904 3.156 1.881 -0.185 0.685  0.265  479 PRO AAA CA  
1163  C C   . PRO A 150 ? 2.917 3.188 1.862 -0.159 0.670  0.249  479 PRO AAA C   
1164  O O   . PRO A 150 ? 2.985 3.234 1.861 -0.167 0.701  0.249  479 PRO AAA O   
1165  C CB  . PRO A 150 ? 2.875 3.181 1.926 -0.222 0.732  0.250  479 PRO AAA CB  
1166  C CG  . PRO A 150 ? 2.997 3.241 1.966 -0.252 0.784  0.268  479 PRO AAA CG  
1167  C CD  . PRO A 150 ? 3.096 3.244 1.944 -0.232 0.766  0.299  479 PRO AAA CD  
1168  N N   . CYS A 151 ? 2.868 3.177 1.862 -0.132 0.624  0.233  480 CYS AAA N   
1169  C CA  . CYS A 151 ? 2.884 3.216 1.859 -0.109 0.607  0.211  480 CYS AAA CA  
1170  C C   . CYS A 151 ? 2.782 3.188 1.848 -0.115 0.631  0.180  480 CYS AAA C   
1171  O O   . CYS A 151 ? 2.694 3.150 1.862 -0.118 0.625  0.173  480 CYS AAA O   
1172  C CB  . CYS A 151 ? 2.892 3.227 1.876 -0.077 0.548  0.209  480 CYS AAA CB  
1173  S SG  . CYS A 151 ? 2.959 3.245 1.936 -0.068 0.514  0.242  480 CYS AAA SG  
1174  N N   . ASN A 152 ? 2.796 3.209 1.825 -0.115 0.657  0.163  481 ASN AAA N   
1175  C CA  . ASN A 152 ? 2.742 3.217 1.848 -0.118 0.688  0.133  481 ASN AAA CA  
1176  C C   . ASN A 152 ? 2.694 3.187 1.808 -0.092 0.659  0.108  481 ASN AAA C   
1177  O O   . ASN A 152 ? 2.735 3.235 1.827 -0.091 0.687  0.085  481 ASN AAA O   
1178  C CB  . ASN A 152 ? 2.835 3.300 1.898 -0.142 0.748  0.130  481 ASN AAA CB  
1179  C CG  . ASN A 152 ? 2.974 3.363 1.897 -0.148 0.754  0.148  481 ASN AAA CG  
1180  O OD1 . ASN A 152 ? 3.010 3.352 1.876 -0.139 0.719  0.172  481 ASN AAA OD1 
1181  N ND2 . ASN A 152 ? 3.049 3.425 1.915 -0.161 0.800  0.137  481 ASN AAA ND2 
1182  N N   . GLY A 153 ? 2.614 3.111 1.755 -0.072 0.608  0.110  482 GLY AAA N   
1183  C CA  . GLY A 153 ? 2.573 3.081 1.716 -0.049 0.575  0.086  482 GLY AAA CA  
1184  C C   . GLY A 153 ? 2.663 3.124 1.687 -0.044 0.558  0.087  482 GLY AAA C   
1185  O O   . GLY A 153 ? 2.644 3.114 1.658 -0.030 0.534  0.063  482 GLY AAA O   
1186  N N   . VAL A 154 ? 2.754 3.167 1.691 -0.056 0.569  0.113  483 VAL AAA N   
1187  C CA  . VAL A 154 ? 2.862 3.229 1.674 -0.050 0.550  0.123  483 VAL AAA CA  
1188  C C   . VAL A 154 ? 2.842 3.187 1.641 -0.031 0.497  0.150  483 VAL AAA C   
1189  O O   . VAL A 154 ? 2.798 3.129 1.633 -0.035 0.498  0.174  483 VAL AAA O   
1190  C CB  . VAL A 154 ? 2.983 3.305 1.705 -0.071 0.595  0.142  483 VAL AAA CB  
1191  C CG1 . VAL A 154 ? 3.097 3.371 1.684 -0.065 0.574  0.158  483 VAL AAA CG1 
1192  C CG2 . VAL A 154 ? 2.992 3.338 1.738 -0.091 0.653  0.116  483 VAL AAA CG2 
1193  N N   . GLU A 155 ? 2.870 3.214 1.623 -0.012 0.453  0.143  484 GLU AAA N   
1194  C CA  . GLU A 155 ? 2.883 3.212 1.627 0.010  0.400  0.168  484 GLU AAA CA  
1195  C C   . GLU A 155 ? 3.000 3.271 1.625 0.014  0.395  0.206  484 GLU AAA C   
1196  O O   . GLU A 155 ? 3.073 3.321 1.615 -0.001 0.427  0.206  484 GLU AAA O   
1197  C CB  . GLU A 155 ? 2.866 3.232 1.632 0.028  0.354  0.141  484 GLU AAA CB  
1198  C CG  . GLU A 155 ? 2.787 3.179 1.651 0.043  0.322  0.139  484 GLU AAA CG  
1199  C CD  . GLU A 155 ? 2.747 3.186 1.660 0.052  0.295  0.100  484 GLU AAA CD  
1200  O OE1 . GLU A 155 ? 2.743 3.204 1.674 0.040  0.323  0.067  484 GLU AAA OE1 
1201  O OE2 . GLU A 155 ? 2.731 3.182 1.667 0.070  0.250  0.102  484 GLU AAA OE2 
1202  N N   . GLY A 156 ? 3.012 3.257 1.628 0.034  0.360  0.239  485 GLY AAA N   
1203  C CA  . GLY A 156 ? 3.139 3.330 1.643 0.048  0.344  0.279  485 GLY AAA CA  
1204  C C   . GLY A 156 ? 3.163 3.301 1.671 0.056  0.346  0.322  485 GLY AAA C   
1205  O O   . GLY A 156 ? 3.061 3.214 1.648 0.070  0.320  0.322  485 GLY AAA O   
1206  N N   . PHE A 157 ? 3.302 3.376 1.723 0.047  0.379  0.356  486 PHE AAA N   
1207  C CA  . PHE A 157 ? 3.367 3.372 1.765 0.052  0.390  0.401  486 PHE AAA CA  
1208  C C   . PHE A 157 ? 3.283 3.298 1.791 0.032  0.414  0.389  486 PHE AAA C   
1209  O O   . PHE A 157 ? 3.271 3.298 1.809 -0.001 0.460  0.371  486 PHE AAA O   
1210  C CB  . PHE A 157 ? 3.503 3.440 1.787 0.036  0.434  0.430  486 PHE AAA CB  
1211  C CG  . PHE A 157 ? 3.581 3.432 1.814 0.044  0.449  0.480  486 PHE AAA CG  
1212  C CD1 . PHE A 157 ? 3.551 3.370 1.834 0.017  0.493  0.485  486 PHE AAA CD1 
1213  C CD2 . PHE A 157 ? 3.689 3.491 1.821 0.077  0.422  0.524  486 PHE AAA CD2 
1214  C CE1 . PHE A 157 ? 3.630 3.362 1.864 0.022  0.512  0.530  486 PHE AAA CE1 
1215  C CE2 . PHE A 157 ? 3.765 3.480 1.848 0.086  0.440  0.572  486 PHE AAA CE2 
1216  C CZ  . PHE A 157 ? 3.738 3.414 1.872 0.058  0.487  0.574  486 PHE AAA CZ  
1217  N N   . ASN A 158 ? 3.237 3.253 1.806 0.052  0.383  0.397  487 ASN AAA N   
1218  C CA  . ASN A 158 ? 3.153 3.178 1.823 0.034  0.398  0.387  487 ASN AAA CA  
1219  C C   . ASN A 158 ? 3.053 3.159 1.821 0.018  0.400  0.341  487 ASN AAA C   
1220  O O   . ASN A 158 ? 2.985 3.105 1.827 -0.005 0.423  0.331  487 ASN AAA O   
1221  C CB  . ASN A 158 ? 3.206 3.173 1.854 0.002  0.453  0.406  487 ASN AAA CB  
1222  C CG  . ASN A 158 ? 3.347 3.224 1.885 0.013  0.466  0.453  487 ASN AAA CG  
1223  O OD1 . ASN A 158 ? 3.414 3.269 1.900 0.051  0.428  0.477  487 ASN AAA OD1 
1224  N ND2 . ASN A 158 ? 3.408 3.233 1.911 -0.019 0.520  0.467  487 ASN AAA ND2 
1225  N N   . CYS A 159 ? 3.055 3.211 1.821 0.028  0.379  0.314  488 CYS AAA N   
1226  C CA  . CYS A 159 ? 2.965 3.192 1.819 0.018  0.382  0.272  488 CYS AAA CA  
1227  C C   . CYS A 159 ? 2.914 3.185 1.784 0.043  0.335  0.249  488 CYS AAA C   
1228  O O   . CYS A 159 ? 2.959 3.227 1.754 0.052  0.322  0.246  488 CYS AAA O   
1229  C CB  . CYS A 159 ? 3.016 3.258 1.850 -0.007 0.427  0.255  488 CYS AAA CB  
1230  S SG  . CYS A 159 ? 3.106 3.310 1.930 -0.043 0.489  0.275  488 CYS AAA SG  
1231  N N   . TYR A 160 ? 2.814 3.124 1.779 0.049  0.314  0.230  489 TYR AAA N   
1232  C CA  . TYR A 160 ? 2.774 3.120 1.770 0.073  0.267  0.210  489 TYR AAA CA  
1233  C C   . TYR A 160 ? 2.660 3.062 1.752 0.065  0.273  0.173  489 TYR AAA C   
1234  O O   . TYR A 160 ? 2.599 3.010 1.749 0.047  0.301  0.172  489 TYR AAA O   
1235  C CB  . TYR A 160 ? 2.776 3.099 1.788 0.094  0.233  0.234  489 TYR AAA CB  
1236  C CG  . TYR A 160 ? 2.896 3.154 1.827 0.101  0.239  0.277  489 TYR AAA CG  
1237  C CD1 . TYR A 160 ? 3.003 3.241 1.836 0.115  0.226  0.294  489 TYR AAA CD1 
1238  C CD2 . TYR A 160 ? 2.897 3.111 1.844 0.091  0.261  0.301  489 TYR AAA CD2 
1239  C CE1 . TYR A 160 ? 3.098 3.270 1.851 0.124  0.233  0.338  489 TYR AAA CE1 
1240  C CE2 . TYR A 160 ? 2.999 3.144 1.869 0.097  0.273  0.342  489 TYR AAA CE2 
1241  C CZ  . TYR A 160 ? 3.098 3.220 1.870 0.115  0.259  0.362  489 TYR AAA CZ  
1242  O OH  . TYR A 160 ? 3.193 3.242 1.885 0.124  0.272  0.406  489 TYR AAA OH  
1243  N N   . PHE A 161 ? 2.638 3.075 1.743 0.076  0.248  0.144  490 PHE AAA N   
1244  C CA  . PHE A 161 ? 2.564 3.048 1.758 0.074  0.248  0.110  490 PHE AAA CA  
1245  C C   . PHE A 161 ? 2.519 3.009 1.782 0.085  0.220  0.116  490 PHE AAA C   
1246  O O   . PHE A 161 ? 2.553 3.031 1.795 0.103  0.186  0.129  490 PHE AAA O   
1247  C CB  . PHE A 161 ? 2.581 3.091 1.754 0.080  0.233  0.077  490 PHE AAA CB  
1248  C CG  . PHE A 161 ? 2.520 3.068 1.772 0.077  0.242  0.041  490 PHE AAA CG  
1249  C CD1 . PHE A 161 ? 2.527 3.086 1.804 0.064  0.286  0.027  490 PHE AAA CD1 
1250  C CD2 . PHE A 161 ? 2.466 3.037 1.765 0.089  0.210  0.022  490 PHE AAA CD2 
1251  C CE1 . PHE A 161 ? 2.465 3.054 1.813 0.065  0.297  -0.003 490 PHE AAA CE1 
1252  C CE2 . PHE A 161 ? 2.401 2.998 1.767 0.087  0.223  -0.010 490 PHE AAA CE2 
1253  C CZ  . PHE A 161 ? 2.401 3.006 1.790 0.076  0.266  -0.020 490 PHE AAA CZ  
1254  N N   . PRO A 162 ? 2.456 2.967 1.802 0.077  0.235  0.109  491 PRO AAA N   
1255  C CA  . PRO A 162 ? 2.395 2.902 1.795 0.082  0.216  0.120  491 PRO AAA CA  
1256  C C   . PRO A 162 ? 2.337 2.867 1.783 0.099  0.181  0.101  491 PRO AAA C   
1257  O O   . PRO A 162 ? 2.315 2.835 1.795 0.104  0.165  0.111  491 PRO AAA O   
1258  C CB  . PRO A 162 ? 2.344 2.872 1.810 0.063  0.246  0.118  491 PRO AAA CB  
1259  C CG  . PRO A 162 ? 2.337 2.898 1.814 0.059  0.269  0.093  491 PRO AAA CG  
1260  C CD  . PRO A 162 ? 2.421 2.962 1.812 0.063  0.270  0.091  491 PRO AAA CD  
1261  N N   . LEU A 163 ? 2.316 2.872 1.762 0.104  0.172  0.072  492 LEU AAA N   
1262  C CA  . LEU A 163 ? 2.253 2.833 1.743 0.117  0.142  0.049  492 LEU AAA CA  
1263  C C   . LEU A 163 ? 2.311 2.892 1.745 0.131  0.108  0.047  492 LEU AAA C   
1264  O O   . LEU A 163 ? 2.405 2.972 1.764 0.130  0.112  0.057  492 LEU AAA O   
1265  C CB  . LEU A 163 ? 2.194 2.805 1.727 0.110  0.159  0.015  492 LEU AAA CB  
1266  C CG  . LEU A 163 ? 2.135 2.756 1.729 0.101  0.191  0.016  492 LEU AAA CG  
1267  C CD1 . LEU A 163 ? 2.093 2.739 1.737 0.102  0.201  -0.015 492 LEU AAA CD1 
1268  C CD2 . LEU A 163 ? 2.087 2.701 1.724 0.100  0.182  0.037  492 LEU AAA CD2 
1269  N N   . GLN A 164 ? 2.277 2.878 1.749 0.143  0.076  0.034  493 GLN AAA N   
1270  C CA  . GLN A 164 ? 2.314 2.932 1.751 0.158  0.038  0.027  493 GLN AAA CA  
1271  C C   . GLN A 164 ? 2.271 2.926 1.771 0.158  0.021  -0.010 493 GLN AAA C   
1272  O O   . GLN A 164 ? 2.248 2.905 1.816 0.152  0.038  -0.021 493 GLN AAA O   
1273  C CB  . GLN A 164 ? 2.335 2.930 1.748 0.177  0.013  0.064  493 GLN AAA CB  
1274  C CG  . GLN A 164 ? 2.404 3.015 1.755 0.193  -0.022 0.070  493 GLN AAA CG  
1275  C CD  . GLN A 164 ? 2.461 3.041 1.774 0.217  -0.040 0.115  493 GLN AAA CD  
1276  O OE1 . GLN A 164 ? 2.556 3.120 1.780 0.223  -0.045 0.137  493 GLN AAA OE1 
1277  N NE2 . GLN A 164 ? 2.402 2.959 1.771 0.224  -0.036 0.131  493 GLN AAA NE2 
1278  N N   . SER A 165 ? 2.100 3.189 1.669 -0.188 0.228  -0.148 494 SER AAA N   
1279  C CA  . SER A 165 ? 2.040 3.052 1.656 -0.143 0.209  -0.191 494 SER AAA CA  
1280  C C   . SER A 165 ? 1.982 2.895 1.617 -0.153 0.166  -0.160 494 SER AAA C   
1281  O O   . SER A 165 ? 1.990 2.879 1.585 -0.191 0.145  -0.111 494 SER AAA O   
1282  C CB  . SER A 165 ? 2.104 3.119 1.671 -0.120 0.203  -0.238 494 SER AAA CB  
1283  O OG  . SER A 165 ? 2.096 3.033 1.711 -0.090 0.176  -0.267 494 SER AAA OG  
1284  N N   . TYR A 166 ? 1.913 2.773 1.605 -0.120 0.151  -0.186 495 TYR AAA N   
1285  C CA  . TYR A 166 ? 1.895 2.681 1.622 -0.118 0.117  -0.164 495 TYR AAA CA  
1286  C C   . TYR A 166 ? 1.925 2.674 1.626 -0.115 0.079  -0.173 495 TYR AAA C   
1287  O O   . TYR A 166 ? 1.920 2.625 1.607 -0.124 0.045  -0.142 495 TYR AAA O   
1288  C CB  . TYR A 166 ? 1.846 2.615 1.659 -0.088 0.129  -0.177 495 TYR AAA CB  
1289  C CG  . TYR A 166 ? 1.829 2.593 1.666 -0.094 0.140  -0.147 495 TYR AAA CG  
1290  C CD1 . TYR A 166 ? 1.849 2.569 1.658 -0.112 0.114  -0.109 495 TYR AAA CD1 
1291  C CD2 . TYR A 166 ? 1.792 2.587 1.674 -0.080 0.170  -0.159 495 TYR AAA CD2 
1292  C CE1 . TYR A 166 ? 1.826 2.528 1.646 -0.118 0.116  -0.085 495 TYR AAA CE1 
1293  C CE2 . TYR A 166 ? 1.760 2.548 1.659 -0.088 0.174  -0.133 495 TYR AAA CE2 
1294  C CZ  . TYR A 166 ? 1.791 2.530 1.656 -0.108 0.147  -0.096 495 TYR AAA CZ  
1295  O OH  . TYR A 166 ? 1.818 2.536 1.690 -0.116 0.143  -0.073 495 TYR AAA OH  
1296  N N   . GLY A 167 ? 1.949 2.710 1.645 -0.100 0.080  -0.216 496 GLY AAA N   
1297  C CA  . GLY A 167 ? 1.991 2.721 1.665 -0.100 0.039  -0.230 496 GLY AAA CA  
1298  C C   . GLY A 167 ? 1.933 2.624 1.684 -0.089 0.010  -0.218 496 GLY AAA C   
1299  O O   . GLY A 167 ? 1.921 2.590 1.661 -0.096 -0.022 -0.189 496 GLY AAA O   
1300  N N   . PHE A 168 ? 1.905 2.594 1.732 -0.071 0.023  -0.238 497 PHE AAA N   
1301  C CA  . PHE A 168 ? 1.898 2.571 1.808 -0.062 0.004  -0.227 497 PHE AAA CA  
1302  C C   . PHE A 168 ? 1.958 2.620 1.874 -0.069 -0.037 -0.248 497 PHE AAA C   
1303  O O   . PHE A 168 ? 1.979 2.629 1.883 -0.068 -0.038 -0.286 497 PHE AAA O   
1304  C CB  . PHE A 168 ? 1.868 2.545 1.848 -0.048 0.033  -0.233 497 PHE AAA CB  
1305  C CG  . PHE A 168 ? 1.844 2.531 1.822 -0.042 0.067  -0.212 497 PHE AAA CG  
1306  C CD1 . PHE A 168 ? 1.814 2.493 1.797 -0.040 0.062  -0.178 497 PHE AAA CD1 
1307  C CD2 . PHE A 168 ? 1.844 2.546 1.815 -0.036 0.099  -0.230 497 PHE AAA CD2 
1308  C CE1 . PHE A 168 ? 1.782 2.460 1.758 -0.038 0.085  -0.161 497 PHE AAA CE1 
1309  C CE2 . PHE A 168 ? 1.806 2.522 1.780 -0.035 0.125  -0.209 497 PHE AAA CE2 
1310  C CZ  . PHE A 168 ? 1.777 2.476 1.751 -0.039 0.116  -0.175 497 PHE AAA CZ  
1311  N N   . GLN A 169 ? 2.004 2.667 1.935 -0.073 -0.073 -0.225 498 GLN AAA N   
1312  C CA  . GLN A 169 ? 2.053 2.714 2.006 -0.082 -0.120 -0.237 498 GLN AAA CA  
1313  C C   . GLN A 169 ? 1.979 2.670 2.043 -0.076 -0.128 -0.215 498 GLN AAA C   
1314  O O   . GLN A 169 ? 1.922 2.630 2.018 -0.059 -0.110 -0.187 498 GLN AAA O   
1315  C CB  . GLN A 169 ? 2.130 2.784 2.009 -0.091 -0.158 -0.228 498 GLN AAA CB  
1316  C CG  . GLN A 169 ? 2.201 2.844 1.966 -0.099 -0.140 -0.237 498 GLN AAA CG  
1317  C CD  . GLN A 169 ? 2.327 2.957 2.008 -0.113 -0.178 -0.258 498 GLN AAA CD  
1318  O OE1 . GLN A 169 ? 2.404 3.026 2.085 -0.118 -0.227 -0.244 498 GLN AAA OE1 
1319  N NE2 . GLN A 169 ? 2.387 3.019 1.992 -0.114 -0.157 -0.292 498 GLN AAA NE2 
1320  N N   . PRO A 170 ? 1.969 2.667 2.093 -0.092 -0.153 -0.226 499 PRO AAA N   
1321  C CA  . PRO A 170 ? 1.904 2.652 2.139 -0.093 -0.161 -0.199 499 PRO AAA CA  
1322  C C   . PRO A 170 ? 1.882 2.674 2.141 -0.075 -0.184 -0.171 499 PRO AAA C   
1323  O O   . PRO A 170 ? 1.823 2.670 2.163 -0.060 -0.172 -0.146 499 PRO AAA O   
1324  C CB  . PRO A 170 ? 1.948 2.691 2.221 -0.124 -0.202 -0.216 499 PRO AAA CB  
1325  C CG  . PRO A 170 ? 2.012 2.684 2.201 -0.130 -0.200 -0.259 499 PRO AAA CG  
1326  C CD  . PRO A 170 ? 2.032 2.692 2.121 -0.110 -0.178 -0.266 499 PRO AAA CD  
1327  N N   . THR A 171 ? 1.922 2.691 2.106 -0.075 -0.217 -0.175 500 THR AAA N   
1328  C CA  . THR A 171 ? 1.923 2.717 2.114 -0.055 -0.253 -0.151 500 THR AAA CA  
1329  C C   . THR A 171 ? 1.897 2.661 2.035 -0.026 -0.230 -0.133 500 THR AAA C   
1330  O O   . THR A 171 ? 1.897 2.672 2.045 0.001  -0.258 -0.113 500 THR AAA O   
1331  C CB  . THR A 171 ? 2.012 2.783 2.138 -0.072 -0.308 -0.162 500 THR AAA CB  
1332  O OG1 . THR A 171 ? 2.065 2.776 2.076 -0.086 -0.292 -0.183 500 THR AAA OG1 
1333  C CG2 . THR A 171 ? 2.033 2.834 2.221 -0.100 -0.349 -0.176 500 THR AAA CG2 
1334  N N   . ASN A 172 ? 1.886 2.611 1.971 -0.031 -0.187 -0.140 501 ASN AAA N   
1335  C CA  . ASN A 172 ? 1.903 2.596 1.943 -0.012 -0.168 -0.121 501 ASN AAA CA  
1336  C C   . ASN A 172 ? 1.884 2.608 2.000 0.027  -0.161 -0.104 501 ASN AAA C   
1337  O O   . ASN A 172 ? 1.836 2.619 2.044 0.032  -0.145 -0.107 501 ASN AAA O   
1338  C CB  . ASN A 172 ? 1.873 2.543 1.876 -0.024 -0.119 -0.130 501 ASN AAA CB  
1339  C CG  . ASN A 172 ? 1.921 2.554 1.815 -0.048 -0.121 -0.129 501 ASN AAA CG  
1340  O OD1 . ASN A 172 ? 1.909 2.548 1.771 -0.066 -0.099 -0.151 501 ASN AAA OD1 
1341  N ND2 . ASN A 172 ? 1.962 2.558 1.798 -0.046 -0.147 -0.102 501 ASN AAA ND2 
1342  N N   . GLY A 173 ? 1.937 2.622 2.012 0.054  -0.175 -0.087 502 GLY AAA N   
1343  C CA  . GLY A 173 ? 1.919 2.621 2.043 0.103  -0.167 -0.078 502 GLY AAA CA  
1344  C C   . GLY A 173 ? 1.870 2.584 2.023 0.105  -0.113 -0.083 502 GLY AAA C   
1345  O O   . GLY A 173 ? 1.877 2.558 1.984 0.073  -0.088 -0.089 502 GLY AAA O   
1346  N N   . VAL A 174 ? 1.842 2.609 2.065 0.143  -0.095 -0.080 503 VAL AAA N   
1347  C CA  . VAL A 174 ? 1.766 2.562 2.029 0.144  -0.044 -0.082 503 VAL AAA CA  
1348  C C   . VAL A 174 ? 1.767 2.485 1.952 0.134  -0.026 -0.084 503 VAL AAA C   
1349  O O   . VAL A 174 ? 1.714 2.440 1.913 0.115  0.011  -0.088 503 VAL AAA O   
1350  C CB  . VAL A 174 ? 1.740 2.607 2.072 0.193  -0.029 -0.076 503 VAL AAA CB  
1351  C CG1 . VAL A 174 ? 1.678 2.575 2.043 0.188  0.022  -0.074 503 VAL AAA CG1 
1352  C CG2 . VAL A 174 ? 1.737 2.701 2.156 0.203  -0.049 -0.070 503 VAL AAA CG2 
1353  N N   . GLY A 175 ? 1.828 2.474 1.937 0.145  -0.055 -0.078 504 GLY AAA N   
1354  C CA  . GLY A 175 ? 1.870 2.442 1.903 0.128  -0.047 -0.073 504 GLY AAA CA  
1355  C C   . GLY A 175 ? 1.879 2.447 1.879 0.074  -0.033 -0.076 504 GLY AAA C   
1356  O O   . GLY A 175 ? 1.859 2.416 1.843 0.058  -0.004 -0.076 504 GLY AAA O   
1357  N N   . TYR A 176 ? 1.919 2.498 1.905 0.051  -0.053 -0.078 505 TYR AAA N   
1358  C CA  . TYR A 176 ? 1.928 2.511 1.872 0.008  -0.041 -0.085 505 TYR AAA CA  
1359  C C   . TYR A 176 ? 1.866 2.501 1.872 0.002  -0.018 -0.109 505 TYR AAA C   
1360  O O   . TYR A 176 ? 1.915 2.557 1.890 -0.023 -0.017 -0.125 505 TYR AAA O   
1361  C CB  . TYR A 176 ? 2.030 2.584 1.903 -0.012 -0.082 -0.074 505 TYR AAA CB  
1362  C CG  . TYR A 176 ? 2.130 2.615 1.934 -0.012 -0.113 -0.046 505 TYR AAA CG  
1363  C CD1 . TYR A 176 ? 2.185 2.636 1.997 0.027  -0.153 -0.036 505 TYR AAA CD1 
1364  C CD2 . TYR A 176 ? 2.196 2.650 1.926 -0.050 -0.107 -0.027 505 TYR AAA CD2 
1365  C CE1 . TYR A 176 ? 2.289 2.654 2.030 0.030  -0.191 -0.012 505 TYR AAA CE1 
1366  C CE2 . TYR A 176 ? 2.298 2.674 1.960 -0.059 -0.145 0.004  505 TYR AAA CE2 
1367  C CZ  . TYR A 176 ? 2.346 2.667 2.010 -0.017 -0.190 0.011  505 TYR AAA CZ  
1368  O OH  . TYR A 176 ? 2.435 2.658 2.025 -0.023 -0.236 0.040  505 TYR AAA OH  
1369  N N   . GLN A 177 ? 1.795 2.463 1.880 0.024  -0.003 -0.111 506 GLN AAA N   
1370  C CA  . GLN A 177 ? 1.758 2.461 1.903 0.014  0.020  -0.127 506 GLN AAA CA  
1371  C C   . GLN A 177 ? 1.721 2.412 1.859 0.013  0.058  -0.130 506 GLN AAA C   
1372  O O   . GLN A 177 ? 1.723 2.395 1.839 0.026  0.067  -0.117 506 GLN AAA O   
1373  C CB  . GLN A 177 ? 1.719 2.472 1.951 0.030  0.017  -0.117 506 GLN AAA CB  
1374  C CG  . GLN A 177 ? 1.737 2.520 1.997 0.025  -0.023 -0.116 506 GLN AAA CG  
1375  C CD  . GLN A 177 ? 1.698 2.554 2.057 0.034  -0.023 -0.103 506 GLN AAA CD  
1376  O OE1 . GLN A 177 ? 1.643 2.526 2.050 0.033  0.008  -0.095 506 GLN AAA OE1 
1377  N NE2 . GLN A 177 ? 1.735 2.632 2.127 0.041  -0.059 -0.096 506 GLN AAA NE2 
1378  N N   . PRO A 178 ? 1.702 2.399 1.858 0.000  0.074  -0.149 507 PRO AAA N   
1379  C CA  . PRO A 178 ? 1.673 2.363 1.825 0.003  0.106  -0.153 507 PRO AAA CA  
1380  C C   . PRO A 178 ? 1.622 2.322 1.830 0.018  0.125  -0.140 507 PRO AAA C   
1381  O O   . PRO A 178 ? 1.634 2.350 1.896 0.013  0.121  -0.138 507 PRO AAA O   
1382  C CB  . PRO A 178 ? 1.688 2.374 1.832 -0.009 0.107  -0.184 507 PRO AAA CB  
1383  C CG  . PRO A 178 ? 1.707 2.394 1.884 -0.019 0.078  -0.190 507 PRO AAA CG  
1384  C CD  . PRO A 178 ? 1.718 2.421 1.895 -0.016 0.057  -0.169 507 PRO AAA CD  
1385  N N   . TYR A 179 ? 1.571 2.262 1.764 0.031  0.143  -0.128 508 TYR AAA N   
1386  C CA  . TYR A 179 ? 1.518 2.217 1.749 0.045  0.164  -0.116 508 TYR AAA CA  
1387  C C   . TYR A 179 ? 1.523 2.209 1.748 0.041  0.181  -0.126 508 TYR AAA C   
1388  O O   . TYR A 179 ? 1.523 2.202 1.708 0.035  0.184  -0.134 508 TYR AAA O   
1389  C CB  . TYR A 179 ? 1.493 2.186 1.704 0.070  0.165  -0.100 508 TYR AAA CB  
1390  C CG  . TYR A 179 ? 1.501 2.221 1.736 0.089  0.153  -0.091 508 TYR AAA CG  
1391  C CD1 . TYR A 179 ? 1.529 2.248 1.754 0.085  0.125  -0.095 508 TYR AAA CD1 
1392  C CD2 . TYR A 179 ? 1.492 2.245 1.759 0.116  0.168  -0.078 508 TYR AAA CD2 
1393  C CE1 . TYR A 179 ? 1.536 2.289 1.790 0.109  0.110  -0.087 508 TYR AAA CE1 
1394  C CE2 . TYR A 179 ? 1.498 2.295 1.794 0.142  0.159  -0.072 508 TYR AAA CE2 
1395  C CZ  . TYR A 179 ? 1.509 2.306 1.803 0.140  0.128  -0.077 508 TYR AAA CZ  
1396  O OH  . TYR A 179 ? 1.492 2.340 1.821 0.170  0.115  -0.072 508 TYR AAA OH  
1397  N N   . ARG A 180 ? 1.542 2.230 1.809 0.042  0.191  -0.122 509 ARG AAA N   
1398  C CA  . ARG A 180 ? 1.559 2.232 1.829 0.046  0.203  -0.129 509 ARG AAA CA  
1399  C C   . ARG A 180 ? 1.530 2.202 1.793 0.061  0.218  -0.108 509 ARG AAA C   
1400  O O   . ARG A 180 ? 1.546 2.231 1.828 0.068  0.224  -0.087 509 ARG AAA O   
1401  C CB  . ARG A 180 ? 1.609 2.265 1.918 0.038  0.196  -0.133 509 ARG AAA CB  
1402  C CG  . ARG A 180 ? 1.668 2.310 1.971 0.027  0.176  -0.162 509 ARG AAA CG  
1403  C CD  . ARG A 180 ? 1.721 2.326 2.056 0.017  0.159  -0.168 509 ARG AAA CD  
1404  N NE  . ARG A 180 ? 1.762 2.340 2.073 0.018  0.138  -0.208 509 ARG AAA NE  
1405  C CZ  . ARG A 180 ? 1.822 2.345 2.139 0.019  0.116  -0.229 509 ARG AAA CZ  
1406  N NH1 . ARG A 180 ? 1.853 2.341 2.203 0.014  0.110  -0.207 509 ARG AAA NH1 
1407  N NH2 . ARG A 180 ? 1.873 2.372 2.156 0.027  0.097  -0.272 509 ARG AAA NH2 
1408  N N   . VAL A 181 ? 1.506 2.171 1.742 0.065  0.224  -0.114 510 VAL AAA N   
1409  C CA  . VAL A 181 ? 1.481 2.138 1.696 0.077  0.230  -0.098 510 VAL AAA CA  
1410  C C   . VAL A 181 ? 1.474 2.127 1.704 0.084  0.236  -0.099 510 VAL AAA C   
1411  O O   . VAL A 181 ? 1.481 2.145 1.713 0.081  0.235  -0.118 510 VAL AAA O   
1412  C CB  . VAL A 181 ? 1.488 2.137 1.655 0.070  0.219  -0.099 510 VAL AAA CB  
1413  C CG1 . VAL A 181 ? 1.505 2.133 1.643 0.080  0.216  -0.087 510 VAL AAA CG1 
1414  C CG2 . VAL A 181 ? 1.487 2.131 1.637 0.067  0.206  -0.098 510 VAL AAA CG2 
1415  N N   . VAL A 182 ? 1.452 2.093 1.688 0.094  0.242  -0.080 511 VAL AAA N   
1416  C CA  . VAL A 182 ? 1.425 2.056 1.663 0.104  0.242  -0.075 511 VAL AAA CA  
1417  C C   . VAL A 182 ? 1.402 2.026 1.599 0.113  0.240  -0.064 511 VAL AAA C   
1418  O O   . VAL A 182 ? 1.404 2.022 1.577 0.121  0.244  -0.054 511 VAL AAA O   
1419  C CB  . VAL A 182 ? 1.455 2.069 1.719 0.106  0.245  -0.056 511 VAL AAA CB  
1420  C CG1 . VAL A 182 ? 1.486 2.082 1.746 0.118  0.240  -0.048 511 VAL AAA CG1 
1421  C CG2 . VAL A 182 ? 1.474 2.078 1.774 0.094  0.237  -0.068 511 VAL AAA CG2 
1422  N N   . VAL A 183 ? 1.386 2.011 1.575 0.114  0.232  -0.067 512 VAL AAA N   
1423  C CA  . VAL A 183 ? 1.415 2.023 1.561 0.118  0.221  -0.058 512 VAL AAA CA  
1424  C C   . VAL A 183 ? 1.441 2.044 1.594 0.130  0.216  -0.048 512 VAL AAA C   
1425  O O   . VAL A 183 ? 1.448 2.074 1.630 0.128  0.209  -0.056 512 VAL AAA O   
1426  C CB  . VAL A 183 ? 1.416 2.034 1.544 0.098  0.206  -0.065 512 VAL AAA CB  
1427  C CG1 . VAL A 183 ? 1.436 2.031 1.525 0.097  0.185  -0.056 512 VAL AAA CG1 
1428  C CG2 . VAL A 183 ? 1.435 2.041 1.541 0.089  0.204  -0.069 512 VAL AAA CG2 
1429  N N   . LEU A 184 ? 1.463 2.042 1.590 0.144  0.221  -0.030 513 LEU AAA N   
1430  C CA  . LEU A 184 ? 1.481 2.047 1.601 0.156  0.213  -0.014 513 LEU AAA CA  
1431  C C   . LEU A 184 ? 1.512 2.062 1.583 0.158  0.192  -0.015 513 LEU AAA C   
1432  O O   . LEU A 184 ? 1.558 2.084 1.574 0.170  0.192  -0.011 513 LEU AAA O   
1433  C CB  . LEU A 184 ? 1.505 2.061 1.611 0.164  0.229  0.010  513 LEU AAA CB  
1434  C CG  . LEU A 184 ? 1.489 2.054 1.644 0.152  0.242  0.016  513 LEU AAA CG  
1435  C CD1 . LEU A 184 ? 1.515 2.084 1.659 0.151  0.258  0.051  513 LEU AAA CD1 
1436  C CD2 . LEU A 184 ? 1.485 2.037 1.683 0.149  0.228  0.007  513 LEU AAA CD2 
1437  N N   . SER A 185 ? 1.506 2.077 1.600 0.149  0.173  -0.023 514 SER AAA N   
1438  C CA  . SER A 185 ? 1.550 2.109 1.609 0.146  0.144  -0.019 514 SER AAA CA  
1439  C C   . SER A 185 ? 1.600 2.148 1.655 0.164  0.134  -0.003 514 SER AAA C   
1440  O O   . SER A 185 ? 1.616 2.178 1.718 0.174  0.140  0.000  514 SER AAA O   
1441  C CB  . SER A 185 ? 1.519 2.124 1.614 0.121  0.128  -0.028 514 SER AAA CB  
1442  O OG  . SER A 185 ? 1.463 2.117 1.617 0.119  0.148  -0.040 514 SER AAA OG  
1443  N N   . PHE A 186 ? 1.667 2.178 1.657 0.172  0.114  0.005  515 PHE AAA N   
1444  C CA  . PHE A 186 ? 1.728 2.222 1.697 0.188  0.097  0.023  515 PHE AAA CA  
1445  C C   . PHE A 186 ? 1.813 2.310 1.769 0.178  0.055  0.020  515 PHE AAA C   
1446  O O   . PHE A 186 ? 1.879 2.349 1.785 0.165  0.037  0.011  515 PHE AAA O   
1447  C CB  . PHE A 186 ? 1.763 2.216 1.652 0.206  0.109  0.037  515 PHE AAA CB  
1448  C CG  . PHE A 186 ? 1.717 2.180 1.621 0.210  0.148  0.047  515 PHE AAA CG  
1449  C CD1 . PHE A 186 ? 1.707 2.173 1.644 0.210  0.158  0.071  515 PHE AAA CD1 
1450  C CD2 . PHE A 186 ? 1.687 2.154 1.573 0.213  0.170  0.035  515 PHE AAA CD2 
1451  C CE1 . PHE A 186 ? 1.680 2.159 1.635 0.205  0.190  0.086  515 PHE AAA CE1 
1452  C CE2 . PHE A 186 ? 1.649 2.140 1.559 0.213  0.204  0.047  515 PHE AAA CE2 
1453  C CZ  . PHE A 186 ? 1.646 2.145 1.592 0.205  0.214  0.074  515 PHE AAA CZ  
1454  N N   . GLU A 187 ? 1.863 2.389 1.864 0.184  0.035  0.028  516 GLU AAA N   
1455  C CA  . GLU A 187 ? 1.931 2.468 1.924 0.174  -0.011 0.030  516 GLU AAA CA  
1456  C C   . GLU A 187 ? 2.017 2.518 1.968 0.198  -0.032 0.050  516 GLU AAA C   
1457  O O   . GLU A 187 ? 2.021 2.510 1.984 0.218  -0.014 0.064  516 GLU AAA O   
1458  C CB  . GLU A 187 ? 1.889 2.512 1.977 0.161  -0.021 0.022  516 GLU AAA CB  
1459  C CG  . GLU A 187 ? 1.865 2.528 2.027 0.189  -0.005 0.020  516 GLU AAA CG  
1460  C CD  . GLU A 187 ? 1.856 2.620 2.108 0.188  -0.018 0.010  516 GLU AAA CD  
1461  O OE1 . GLU A 187 ? 1.843 2.664 2.119 0.155  -0.016 0.003  516 GLU AAA OE1 
1462  O OE2 . GLU A 187 ? 1.890 2.679 2.189 0.221  -0.032 0.011  516 GLU AAA OE2 
1463  N N   . LEU A 188 ? 2.101 2.577 1.997 0.192  -0.074 0.053  517 LEU AAA N   
1464  C CA  . LEU A 188 ? 2.198 2.639 2.040 0.212  -0.105 0.072  517 LEU AAA CA  
1465  C C   . LEU A 188 ? 2.250 2.728 2.124 0.197  -0.160 0.072  517 LEU AAA C   
1466  O O   . LEU A 188 ? 2.306 2.757 2.128 0.174  -0.193 0.063  517 LEU AAA O   
1467  C CB  . LEU A 188 ? 2.270 2.638 1.988 0.222  -0.101 0.072  517 LEU AAA CB  
1468  C CG  . LEU A 188 ? 2.343 2.672 1.986 0.246  -0.109 0.098  517 LEU AAA CG  
1469  C CD1 . LEU A 188 ? 2.388 2.672 1.923 0.263  -0.079 0.096  517 LEU AAA CD1 
1470  C CD2 . LEU A 188 ? 2.406 2.721 2.017 0.246  -0.171 0.103  517 LEU AAA CD2 
1471  N N   . LEU A 189 ? 2.262 2.799 2.222 0.209  -0.174 0.080  518 LEU AAA N   
1472  C CA  . LEU A 189 ? 2.286 2.888 2.303 0.198  -0.225 0.082  518 LEU AAA CA  
1473  C C   . LEU A 189 ? 2.384 2.931 2.325 0.212  -0.275 0.100  518 LEU AAA C   
1474  O O   . LEU A 189 ? 2.436 2.897 2.262 0.217  -0.271 0.104  518 LEU AAA O   
1475  C CB  . LEU A 189 ? 2.224 2.919 2.365 0.219  -0.216 0.078  518 LEU AAA CB  
1476  C CG  . LEU A 189 ? 2.124 2.867 2.329 0.214  -0.164 0.059  518 LEU AAA CG  
1477  C CD1 . LEU A 189 ? 2.076 2.918 2.395 0.243  -0.162 0.048  518 LEU AAA CD1 
1478  C CD2 . LEU A 189 ? 2.082 2.853 2.284 0.166  -0.157 0.049  518 LEU AAA CD2 
1479  N N   . HIS A 190 ? 2.390 2.993 2.390 0.221  -0.322 0.109  519 HIS AAA N   
1480  C CA  . HIS A 190 ? 2.478 3.037 2.420 0.242  -0.372 0.130  519 HIS AAA CA  
1481  C C   . HIS A 190 ? 2.444 3.032 2.458 0.285  -0.374 0.144  519 HIS AAA C   
1482  O O   . HIS A 190 ? 2.511 3.095 2.517 0.304  -0.427 0.162  519 HIS AAA O   
1483  C CB  . HIS A 190 ? 2.552 3.137 2.487 0.214  -0.440 0.130  519 HIS AAA CB  
1484  C CG  . HIS A 190 ? 2.667 3.149 2.458 0.199  -0.467 0.128  519 HIS AAA CG  
1485  N ND1 . HIS A 190 ? 2.773 3.192 2.468 0.217  -0.512 0.144  519 HIS AAA ND1 
1486  C CD2 . HIS A 190 ? 2.687 3.114 2.405 0.172  -0.457 0.109  519 HIS AAA CD2 
1487  C CE1 . HIS A 190 ? 2.850 3.184 2.418 0.204  -0.527 0.130  519 HIS AAA CE1 
1488  N NE2 . HIS A 190 ? 2.805 3.139 2.386 0.178  -0.496 0.108  519 HIS AAA NE2 
1489  N N   . ALA A 191 ? 2.344 2.948 2.417 0.301  -0.324 0.135  520 ALA AAA N   
1490  C CA  . ALA A 191 ? 2.334 2.933 2.459 0.346  -0.324 0.144  520 ALA AAA CA  
1491  C C   . ALA A 191 ? 2.369 2.859 2.404 0.353  -0.296 0.167  520 ALA AAA C   
1492  O O   . ALA A 191 ? 2.342 2.799 2.318 0.328  -0.255 0.164  520 ALA AAA O   
1493  C CB  . ALA A 191 ? 2.238 2.924 2.481 0.359  -0.294 0.116  520 ALA AAA CB  
1494  N N   . PRO A 192 ? 2.438 2.873 2.460 0.384  -0.320 0.195  521 PRO AAA N   
1495  C CA  . PRO A 192 ? 2.501 2.839 2.437 0.379  -0.296 0.227  521 PRO AAA CA  
1496  C C   . PRO A 192 ? 2.450 2.783 2.409 0.364  -0.235 0.214  521 PRO AAA C   
1497  O O   . PRO A 192 ? 2.392 2.749 2.438 0.382  -0.228 0.194  521 PRO AAA O   
1498  C CB  . PRO A 192 ? 2.569 2.858 2.520 0.415  -0.342 0.255  521 PRO AAA CB  
1499  C CG  . PRO A 192 ? 2.582 2.932 2.583 0.439  -0.400 0.244  521 PRO AAA CG  
1500  C CD  . PRO A 192 ? 2.478 2.938 2.561 0.423  -0.377 0.200  521 PRO AAA CD  
1501  N N   . ALA A 193 ? 2.482 2.786 2.360 0.336  -0.195 0.224  522 ALA AAA N   
1502  C CA  . ALA A 193 ? 2.428 2.736 2.318 0.317  -0.137 0.212  522 ALA AAA CA  
1503  C C   . ALA A 193 ? 2.471 2.732 2.392 0.323  -0.129 0.233  522 ALA AAA C   
1504  O O   . ALA A 193 ? 2.573 2.779 2.471 0.337  -0.165 0.267  522 ALA AAA O   
1505  C CB  . ALA A 193 ? 2.444 2.733 2.234 0.297  -0.105 0.224  522 ALA AAA CB  
1506  N N   . THR A 194 ? 2.430 2.705 2.397 0.310  -0.089 0.215  523 THR AAA N   
1507  C CA  . THR A 194 ? 2.469 2.693 2.473 0.313  -0.089 0.226  523 THR AAA CA  
1508  C C   . THR A 194 ? 2.433 2.665 2.448 0.283  -0.039 0.220  523 THR AAA C   
1509  O O   . THR A 194 ? 2.440 2.643 2.505 0.286  -0.042 0.212  523 THR AAA O   
1510  C CB  . THR A 194 ? 2.449 2.689 2.543 0.350  -0.119 0.191  523 THR AAA CB  
1511  O OG1 . THR A 194 ? 2.347 2.665 2.498 0.347  -0.088 0.144  523 THR AAA OG1 
1512  C CG2 . THR A 194 ? 2.488 2.739 2.592 0.384  -0.170 0.193  523 THR AAA CG2 
1513  N N   . VAL A 195 ? 2.401 2.666 2.370 0.261  0.000  0.222  524 VAL AAA N   
1514  C CA  . VAL A 195 ? 2.342 2.622 2.323 0.234  0.044  0.222  524 VAL AAA CA  
1515  C C   . VAL A 195 ? 2.393 2.688 2.295 0.217  0.076  0.251  524 VAL AAA C   
1516  O O   . VAL A 195 ? 2.359 2.697 2.241 0.219  0.100  0.224  524 VAL AAA O   
1517  C CB  . VAL A 195 ? 2.213 2.546 2.252 0.235  0.064  0.171  524 VAL AAA CB  
1518  C CG1 . VAL A 195 ? 2.168 2.505 2.231 0.212  0.097  0.172  524 VAL AAA CG1 
1519  C CG2 . VAL A 195 ? 2.186 2.531 2.293 0.261  0.037  0.136  524 VAL AAA CG2 
1520  N N   . CYS A 196 ? 2.462 2.724 2.321 0.201  0.076  0.304  525 CYS AAA N   
1521  C CA  . CYS A 196 ? 2.489 2.776 2.267 0.188  0.109  0.340  525 CYS AAA CA  
1522  C C   . CYS A 196 ? 2.486 2.797 2.294 0.153  0.145  0.368  525 CYS AAA C   
1523  O O   . CYS A 196 ? 2.411 2.697 2.292 0.139  0.134  0.360  525 CYS AAA O   
1524  C CB  . CYS A 196 ? 2.580 2.826 2.280 0.190  0.083  0.388  525 CYS AAA CB  
1525  S SG  . CYS A 196 ? 2.558 2.761 2.258 0.225  0.019  0.365  525 CYS AAA SG  
1526  N N   . GLY A 197 ? 2.558 2.921 2.310 0.142  0.185  0.398  526 GLY AAA N   
1527  C CA  . GLY A 197 ? 2.595 3.001 2.372 0.104  0.220  0.438  526 GLY AAA CA  
1528  C C   . GLY A 197 ? 2.737 3.141 2.450 0.076  0.224  0.513  526 GLY AAA C   
1529  O O   . GLY A 197 ? 2.795 3.146 2.448 0.087  0.193  0.534  526 GLY AAA O   
1530  N N   . PRO A 198 ? 2.790 3.258 2.516 0.036  0.262  0.561  527 PRO AAA N   
1531  C CA  . PRO A 198 ? 2.911 3.392 2.577 -0.001 0.270  0.643  527 PRO AAA CA  
1532  C C   . PRO A 198 ? 2.993 3.523 2.543 0.029  0.296  0.655  527 PRO AAA C   
1533  O O   . PRO A 198 ? 3.071 3.528 2.556 0.041  0.258  0.668  527 PRO AAA O   
1534  C CB  . PRO A 198 ? 2.889 3.457 2.617 -0.051 0.309  0.681  527 PRO AAA CB  
1535  C CG  . PRO A 198 ? 2.763 3.392 2.553 -0.021 0.336  0.611  527 PRO AAA CG  
1536  C CD  . PRO A 198 ? 2.711 3.248 2.517 0.019  0.294  0.543  527 PRO AAA CD  
1537  N N   . LYS A 199 ? 2.983 3.631 2.506 0.044  0.355  0.649  528 LYS AAA N   
1538  C CA  . LYS A 199 ? 3.037 3.751 2.441 0.073  0.390  0.664  528 LYS AAA CA  
1539  C C   . LYS A 199 ? 3.096 3.714 2.409 0.106  0.343  0.647  528 LYS AAA C   
1540  O O   . LYS A 199 ? 3.139 3.783 2.340 0.141  0.357  0.642  528 LYS AAA O   
1541  C CB  . LYS A 199 ? 2.953 3.766 2.348 0.123  0.439  0.606  528 LYS AAA CB  
1542  C CG  . LYS A 199 ? 2.902 3.859 2.345 0.101  0.501  0.637  528 LYS AAA CG  
1543  C CD  . LYS A 199 ? 2.989 4.048 2.341 0.095  0.548  0.698  528 LYS AAA CD  
1544  C CE  . LYS A 199 ? 2.950 4.184 2.340 0.102  0.617  0.705  528 LYS AAA CE  
1545  N NZ  . LYS A 199 ? 3.060 4.411 2.352 0.105  0.668  0.760  528 LYS AAA NZ  
1546  N N   . THR B 1   ? 2.084 1.801 1.841 -0.019 0.267  0.042  0   THR BBB N   
1547  C CA  . THR B 1   ? 2.025 1.805 1.822 0.005  0.227  0.065  0   THR BBB CA  
1548  C C   . THR B 1   ? 1.917 1.750 1.757 -0.006 0.228  0.049  0   THR BBB C   
1549  O O   . THR B 1   ? 1.867 1.695 1.706 -0.032 0.254  0.018  0   THR BBB O   
1550  C CB  . THR B 1   ? 2.015 1.844 1.831 0.003  0.184  0.074  0   THR BBB CB  
1551  O OG1 . THR B 1   ? 2.000 1.888 1.857 0.020  0.152  0.092  0   THR BBB OG1 
1552  C CG2 . THR B 1   ? 1.967 1.830 1.801 -0.030 0.180  0.045  0   THR BBB CG2 
1553  N N   . GLN B 2   ? 1.862 1.746 1.737 0.013  0.200  0.068  1   GLN BBB N   
1554  C CA  . GLN B 2   ? 1.837 1.772 1.749 0.008  0.200  0.058  1   GLN BBB CA  
1555  C C   . GLN B 2   ? 1.762 1.749 1.697 -0.019 0.183  0.037  1   GLN BBB C   
1556  O O   . GLN B 2   ? 1.758 1.757 1.698 -0.037 0.202  0.009  1   GLN BBB O   
1557  C CB  . GLN B 2   ? 1.830 1.804 1.772 0.034  0.175  0.085  1   GLN BBB CB  
1558  C CG  . GLN B 2   ? 1.807 1.829 1.783 0.030  0.177  0.078  1   GLN BBB CG  
1559  C CD  . GLN B 2   ? 1.857 1.847 1.822 0.039  0.214  0.070  1   GLN BBB CD  
1560  O OE1 . GLN B 2   ? 1.896 1.845 1.844 0.064  0.227  0.085  1   GLN BBB OE1 
1561  N NE2 . GLN B 2   ? 1.817 1.826 1.791 0.019  0.229  0.045  1   GLN BBB NE2 
1562  N N   . MET B 3   ? 1.692 1.708 1.639 -0.018 0.150  0.049  2   MET BBB N   
1563  C CA  . MET B 3   ? 1.632 1.701 1.603 -0.034 0.127  0.038  2   MET BBB CA  
1564  C C   . MET B 3   ? 1.582 1.646 1.543 -0.040 0.107  0.039  2   MET BBB C   
1565  O O   . MET B 3   ? 1.613 1.660 1.565 -0.026 0.093  0.061  2   MET BBB O   
1566  C CB  . MET B 3   ? 1.621 1.737 1.624 -0.023 0.104  0.056  2   MET BBB CB  
1567  C CG  . MET B 3   ? 1.595 1.757 1.615 -0.035 0.087  0.047  2   MET BBB CG  
1568  S SD  . MET B 3   ? 1.608 1.786 1.622 -0.052 0.108  0.010  2   MET BBB SD  
1569  C CE  . MET B 3   ? 1.635 1.793 1.646 -0.047 0.142  0.005  2   MET BBB CE  
1570  N N   . GLN B 4   ? 1.512 1.593 1.474 -0.058 0.106  0.015  3   GLN BBB N   
1571  C CA  . GLN B 4   ? 1.460 1.543 1.416 -0.065 0.088  0.012  3   GLN BBB CA  
1572  C C   . GLN B 4   ? 1.407 1.542 1.386 -0.071 0.068  0.002  3   GLN BBB C   
1573  O O   . GLN B 4   ? 1.408 1.570 1.397 -0.076 0.079  -0.016 3   GLN BBB O   
1574  C CB  . GLN B 4   ? 1.472 1.519 1.402 -0.081 0.114  -0.011 3   GLN BBB CB  
1575  C CG  . GLN B 4   ? 1.444 1.486 1.363 -0.088 0.100  -0.015 3   GLN BBB CG  
1576  C CD  . GLN B 4   ? 1.472 1.484 1.369 -0.108 0.131  -0.044 3   GLN BBB CD  
1577  O OE1 . GLN B 4   ? 1.500 1.481 1.383 -0.116 0.164  -0.055 3   GLN BBB OE1 
1578  N NE2 . GLN B 4   ? 1.464 1.483 1.358 -0.118 0.124  -0.057 3   GLN BBB NE2 
1579  N N   . LEU B 5   ? 1.375 1.522 1.360 -0.067 0.041  0.014  4   LEU BBB N   
1580  C CA  . LEU B 5   ? 1.342 1.529 1.343 -0.067 0.023  0.009  4   LEU BBB CA  
1581  C C   . LEU B 5   ? 1.363 1.552 1.356 -0.075 0.017  -0.010 4   LEU BBB C   
1582  O O   . LEU B 5   ? 1.418 1.582 1.400 -0.076 0.009  -0.003 4   LEU BBB O   
1583  C CB  . LEU B 5   ? 1.324 1.519 1.338 -0.058 0.000  0.037  4   LEU BBB CB  
1584  C CG  . LEU B 5   ? 1.347 1.549 1.375 -0.050 0.006  0.055  4   LEU BBB CG  
1585  C CD1 . LEU B 5   ? 1.350 1.566 1.394 -0.046 -0.015 0.077  4   LEU BBB CD1 
1586  C CD2 . LEU B 5   ? 1.360 1.582 1.391 -0.051 0.022  0.041  4   LEU BBB CD2 
1587  N N   . VAL B 6   ? 1.342 1.563 1.341 -0.079 0.022  -0.036 5   VAL BBB N   
1588  C CA  . VAL B 6   ? 1.343 1.579 1.340 -0.083 0.016  -0.059 5   VAL BBB CA  
1589  C C   . VAL B 6   ? 1.342 1.605 1.347 -0.068 -0.009 -0.049 5   VAL BBB C   
1590  O O   . VAL B 6   ? 1.335 1.618 1.346 -0.059 -0.014 -0.038 5   VAL BBB O   
1591  C CB  . VAL B 6   ? 1.349 1.610 1.350 -0.097 0.038  -0.098 5   VAL BBB CB  
1592  C CG1 . VAL B 6   ? 1.361 1.593 1.354 -0.109 0.068  -0.103 5   VAL BBB CG1 
1593  C CG2 . VAL B 6   ? 1.355 1.673 1.370 -0.088 0.029  -0.113 5   VAL BBB CG2 
1594  N N   . GLN B 7   ? 1.368 1.629 1.371 -0.065 -0.023 -0.052 6   GLN BBB N   
1595  C CA  . GLN B 7   ? 1.389 1.662 1.392 -0.049 -0.045 -0.040 6   GLN BBB CA  
1596  C C   . GLN B 7   ? 1.419 1.723 1.424 -0.042 -0.049 -0.068 6   GLN BBB C   
1597  O O   . GLN B 7   ? 1.413 1.716 1.419 -0.055 -0.038 -0.092 6   GLN BBB O   
1598  C CB  . GLN B 7   ? 1.371 1.607 1.369 -0.049 -0.059 -0.015 6   GLN BBB CB  
1599  C CG  . GLN B 7   ? 1.348 1.566 1.349 -0.053 -0.058 0.011  6   GLN BBB CG  
1600  C CD  . GLN B 7   ? 1.345 1.545 1.347 -0.050 -0.074 0.035  6   GLN BBB CD  
1601  O OE1 . GLN B 7   ? 1.328 1.510 1.332 -0.057 -0.078 0.049  6   GLN BBB OE1 
1602  N NE2 . GLN B 7   ? 1.351 1.557 1.351 -0.040 -0.084 0.038  6   GLN BBB NE2 
1603  N N   . SER B 8   ? 1.465 1.793 1.469 -0.022 -0.064 -0.065 7   SER BBB N   
1604  C CA  . SER B 8   ? 1.486 1.846 1.491 -0.006 -0.073 -0.088 7   SER BBB CA  
1605  C C   . SER B 8   ? 1.530 1.862 1.531 -0.012 -0.076 -0.092 7   SER BBB C   
1606  O O   . SER B 8   ? 1.519 1.804 1.513 -0.022 -0.078 -0.069 7   SER BBB O   
1607  C CB  . SER B 8   ? 1.488 1.859 1.481 0.022  -0.090 -0.073 7   SER BBB CB  
1608  O OG  . SER B 8   ? 1.507 1.828 1.488 0.026  -0.099 -0.040 7   SER BBB OG  
1609  N N   . GLY B 9   ? 1.568 1.932 1.577 -0.007 -0.076 -0.122 8   GLY BBB N   
1610  C CA  . GLY B 9   ? 1.578 1.922 1.584 -0.011 -0.077 -0.131 8   GLY BBB CA  
1611  C C   . GLY B 9   ? 1.587 1.895 1.579 0.007  -0.094 -0.106 8   GLY BBB C   
1612  O O   . GLY B 9   ? 1.578 1.869 1.561 0.018  -0.104 -0.079 8   GLY BBB O   
1613  N N   . THR B 10  ? 1.590 1.882 1.577 0.007  -0.096 -0.117 9   THR BBB N   
1614  C CA  . THR B 10  ? 1.603 1.854 1.575 0.020  -0.110 -0.099 9   THR BBB CA  
1615  C C   . THR B 10  ? 1.632 1.906 1.601 0.055  -0.122 -0.101 9   THR BBB C   
1616  O O   . THR B 10  ? 1.615 1.943 1.598 0.068  -0.121 -0.130 9   THR BBB O   
1617  C CB  . THR B 10  ? 1.584 1.812 1.551 0.007  -0.105 -0.113 9   THR BBB CB  
1618  O OG1 . THR B 10  ? 1.534 1.749 1.500 -0.021 -0.092 -0.113 9   THR BBB OG1 
1619  C CG2 . THR B 10  ? 1.629 1.807 1.579 0.013  -0.116 -0.094 9   THR BBB CG2 
1620  N N   . GLU B 11  ? 1.667 1.900 1.617 0.070  -0.132 -0.072 10  GLU BBB N   
1621  C CA  . GLU B 11  ? 1.692 1.930 1.627 0.108  -0.142 -0.065 10  GLU BBB CA  
1622  C C   . GLU B 11  ? 1.722 1.907 1.638 0.121  -0.147 -0.057 10  GLU BBB C   
1623  O O   . GLU B 11  ? 1.740 1.867 1.643 0.105  -0.145 -0.034 10  GLU BBB O   
1624  C CB  . GLU B 11  ? 1.708 1.933 1.629 0.114  -0.144 -0.036 10  GLU BBB CB  
1625  C CG  . GLU B 11  ? 1.682 1.955 1.621 0.102  -0.138 -0.044 10  GLU BBB CG  
1626  C CD  . GLU B 11  ? 1.682 2.024 1.627 0.126  -0.142 -0.067 10  GLU BBB CD  
1627  O OE1 . GLU B 11  ? 1.688 2.054 1.631 0.154  -0.151 -0.084 10  GLU BBB OE1 
1628  O OE2 . GLU B 11  ? 1.671 2.046 1.623 0.119  -0.137 -0.071 10  GLU BBB OE2 
1629  N N   . VAL B 12  ? 1.738 1.947 1.655 0.148  -0.151 -0.079 11  VAL BBB N   
1630  C CA  . VAL B 12  ? 1.799 1.961 1.694 0.171  -0.155 -0.074 11  VAL BBB CA  
1631  C C   . VAL B 12  ? 1.832 1.991 1.703 0.217  -0.163 -0.058 11  VAL BBB C   
1632  O O   . VAL B 12  ? 1.835 2.059 1.715 0.248  -0.171 -0.078 11  VAL BBB O   
1633  C CB  . VAL B 12  ? 1.817 2.006 1.727 0.177  -0.153 -0.108 11  VAL BBB CB  
1634  C CG1 . VAL B 12  ? 1.873 2.002 1.761 0.193  -0.154 -0.102 11  VAL BBB CG1 
1635  C CG2 . VAL B 12  ? 1.777 1.983 1.709 0.135  -0.143 -0.128 11  VAL BBB CG2 
1636  N N   . LYS B 13  ? 1.862 1.952 1.703 0.222  -0.161 -0.025 12  LYS BBB N   
1637  C CA  . LYS B 13  ? 1.921 1.994 1.727 0.265  -0.165 -0.002 12  LYS BBB CA  
1638  C C   . LYS B 13  ? 2.002 1.991 1.771 0.286  -0.161 0.016  12  LYS BBB C   
1639  O O   . LYS B 13  ? 2.010 1.948 1.781 0.256  -0.153 0.015  12  LYS BBB O   
1640  C CB  . LYS B 13  ? 1.909 1.974 1.707 0.249  -0.161 0.024  12  LYS BBB CB  
1641  C CG  . LYS B 13  ? 1.850 1.992 1.680 0.232  -0.163 0.007  12  LYS BBB CG  
1642  C CD  . LYS B 13  ? 1.857 2.074 1.688 0.270  -0.174 -0.012 12  LYS BBB CD  
1643  C CE  . LYS B 13  ? 1.914 2.125 1.711 0.300  -0.177 0.014  12  LYS BBB CE  
1644  N NZ  . LYS B 13  ? 1.939 2.211 1.725 0.351  -0.192 -0.002 12  LYS BBB NZ  
1645  N N   . LYS B 14  ? 2.076 2.050 1.809 0.337  -0.165 0.029  13  LYS BBB N   
1646  C CA  . LYS B 14  ? 2.169 2.053 1.856 0.365  -0.157 0.051  13  LYS BBB CA  
1647  C C   . LYS B 14  ? 2.184 1.996 1.837 0.352  -0.143 0.090  13  LYS BBB C   
1648  O O   . LYS B 14  ? 2.159 2.001 1.808 0.353  -0.145 0.103  13  LYS BBB O   
1649  C CB  . LYS B 14  ? 2.258 2.166 1.921 0.433  -0.168 0.046  13  LYS BBB CB  
1650  C CG  . LYS B 14  ? 2.268 2.237 1.964 0.448  -0.178 0.006  13  LYS BBB CG  
1651  C CD  . LYS B 14  ? 2.343 2.240 2.028 0.445  -0.168 0.002  13  LYS BBB CD  
1652  C CE  . LYS B 14  ? 2.344 2.300 2.058 0.468  -0.175 -0.037 13  LYS BBB CE  
1653  N NZ  . LYS B 14  ? 2.267 2.293 2.035 0.420  -0.176 -0.069 13  LYS BBB NZ  
1654  N N   . PRO B 15  ? 2.214 1.928 1.839 0.339  -0.127 0.107  14  PRO BBB N   
1655  C CA  . PRO B 15  ? 2.252 1.890 1.840 0.327  -0.109 0.142  14  PRO BBB CA  
1656  C C   . PRO B 15  ? 2.273 1.906 1.814 0.380  -0.110 0.167  14  PRO BBB C   
1657  O O   . PRO B 15  ? 2.301 1.921 1.809 0.435  -0.116 0.168  14  PRO BBB O   
1658  C CB  . PRO B 15  ? 2.343 1.879 1.904 0.319  -0.092 0.149  14  PRO BBB CB  
1659  C CG  . PRO B 15  ? 2.298 1.866 1.897 0.301  -0.101 0.114  14  PRO BBB CG  
1660  C CD  . PRO B 15  ? 2.237 1.908 1.864 0.330  -0.123 0.091  14  PRO BBB CD  
1661  N N   . GLY B 16  ? 2.247 1.890 1.783 0.365  -0.105 0.186  15  GLY BBB N   
1662  C CA  . GLY B 16  ? 2.323 1.958 1.809 0.410  -0.103 0.213  15  GLY BBB CA  
1663  C C   . GLY B 16  ? 2.269 2.013 1.781 0.420  -0.123 0.198  15  GLY BBB C   
1664  O O   . GLY B 16  ? 2.321 2.066 1.807 0.427  -0.117 0.220  15  GLY BBB O   
1665  N N   . GLU B 17  ? 2.189 2.021 1.751 0.418  -0.142 0.161  16  GLU BBB N   
1666  C CA  . GLU B 17  ? 2.119 2.060 1.713 0.422  -0.158 0.139  16  GLU BBB CA  
1667  C C   . GLU B 17  ? 2.044 1.993 1.658 0.374  -0.148 0.149  16  GLU BBB C   
1668  O O   . GLU B 17  ? 2.046 1.935 1.665 0.332  -0.132 0.163  16  GLU BBB O   
1669  C CB  . GLU B 17  ? 2.072 2.092 1.720 0.414  -0.173 0.096  16  GLU BBB CB  
1670  C CG  . GLU B 17  ? 2.133 2.184 1.769 0.472  -0.188 0.079  16  GLU BBB CG  
1671  C CD  . GLU B 17  ? 2.087 2.207 1.775 0.463  -0.197 0.035  16  GLU BBB CD  
1672  O OE1 . GLU B 17  ? 2.029 2.154 1.756 0.410  -0.190 0.021  16  GLU BBB OE1 
1673  O OE2 . GLU B 17  ? 2.130 2.297 1.817 0.510  -0.211 0.015  16  GLU BBB OE2 
1674  N N   . SER B 18  ? 1.979 2.002 1.601 0.381  -0.157 0.141  17  SER BBB N   
1675  C CA  . SER B 18  ? 1.915 1.960 1.558 0.341  -0.148 0.146  17  SER BBB CA  
1676  C C   . SER B 18  ? 1.793 1.920 1.497 0.309  -0.156 0.109  17  SER BBB C   
1677  O O   . SER B 18  ? 1.749 1.931 1.471 0.329  -0.170 0.079  17  SER BBB O   
1678  C CB  . SER B 18  ? 1.968 2.031 1.572 0.372  -0.149 0.162  17  SER BBB CB  
1679  O OG  . SER B 18  ? 2.021 2.136 1.607 0.426  -0.168 0.147  17  SER BBB OG  
1680  N N   . LEU B 19  ? 1.743 1.875 1.476 0.264  -0.146 0.110  18  LEU BBB N   
1681  C CA  . LEU B 19  ? 1.689 1.874 1.474 0.229  -0.148 0.080  18  LEU BBB CA  
1682  C C   . LEU B 19  ? 1.662 1.864 1.464 0.197  -0.137 0.085  18  LEU BBB C   
1683  O O   . LEU B 19  ? 1.689 1.840 1.482 0.179  -0.126 0.113  18  LEU BBB O   
1684  C CB  . LEU B 19  ? 1.697 1.839 1.500 0.202  -0.144 0.077  18  LEU BBB CB  
1685  C CG  . LEU B 19  ? 1.646 1.822 1.494 0.163  -0.142 0.053  18  LEU BBB CG  
1686  C CD1 . LEU B 19  ? 1.629 1.871 1.498 0.175  -0.150 0.016  18  LEU BBB CD1 
1687  C CD2 . LEU B 19  ? 1.648 1.770 1.504 0.135  -0.138 0.060  18  LEU BBB CD2 
1688  N N   . LYS B 20  ? 1.637 1.908 1.467 0.189  -0.140 0.058  19  LYS BBB N   
1689  C CA  . LYS B 20  ? 1.627 1.918 1.477 0.160  -0.129 0.059  19  LYS BBB CA  
1690  C C   . LYS B 20  ? 1.576 1.894 1.466 0.129  -0.125 0.031  19  LYS BBB C   
1691  O O   . LYS B 20  ? 1.573 1.949 1.478 0.133  -0.128 -0.002 19  LYS BBB O   
1692  C CB  . LYS B 20  ? 1.670 2.012 1.505 0.181  -0.131 0.052  19  LYS BBB CB  
1693  C CG  . LYS B 20  ? 1.658 2.022 1.511 0.154  -0.117 0.049  19  LYS BBB CG  
1694  C CD  . LYS B 20  ? 1.704 2.096 1.529 0.174  -0.116 0.054  19  LYS BBB CD  
1695  C CE  . LYS B 20  ? 1.708 2.178 1.537 0.192  -0.127 0.017  19  LYS BBB CE  
1696  N NZ  . LYS B 20  ? 1.751 2.248 1.549 0.213  -0.127 0.023  19  LYS BBB NZ  
1697  N N   . ILE B 21  ? 1.548 1.828 1.454 0.098  -0.117 0.043  20  ILE BBB N   
1698  C CA  . ILE B 21  ? 1.490 1.785 1.427 0.069  -0.111 0.022  20  ILE BBB CA  
1699  C C   . ILE B 21  ? 1.452 1.767 1.402 0.053  -0.099 0.021  20  ILE BBB C   
1700  O O   . ILE B 21  ? 1.450 1.750 1.391 0.053  -0.094 0.045  20  ILE BBB O   
1701  C CB  . ILE B 21  ? 1.488 1.735 1.432 0.050  -0.112 0.033  20  ILE BBB CB  
1702  C CG1 . ILE B 21  ? 1.505 1.713 1.447 0.036  -0.107 0.063  20  ILE BBB CG1 
1703  C CG2 . ILE B 21  ? 1.516 1.743 1.446 0.066  -0.122 0.028  20  ILE BBB CG2 
1704  C CD1 . ILE B 21  ? 1.500 1.678 1.455 0.012  -0.108 0.067  20  ILE BBB CD1 
1705  N N   . SER B 22  ? 1.420 1.767 1.388 0.039  -0.091 -0.007 21  SER BBB N   
1706  C CA  . SER B 22  ? 1.392 1.761 1.372 0.025  -0.077 -0.015 21  SER BBB CA  
1707  C C   . SER B 22  ? 1.355 1.690 1.348 0.000  -0.066 -0.005 21  SER BBB C   
1708  O O   . SER B 22  ? 1.338 1.642 1.332 -0.006 -0.072 0.002  21  SER BBB O   
1709  C CB  . SER B 22  ? 1.398 1.819 1.387 0.023  -0.071 -0.054 21  SER BBB CB  
1710  O OG  . SER B 22  ? 1.405 1.818 1.410 -0.001 -0.057 -0.073 21  SER BBB OG  
1711  N N   . CYS B 23  ? 1.317 1.658 1.317 -0.010 -0.052 -0.004 22  CYS BBB N   
1712  C CA  . CYS B 23  ? 1.288 1.603 1.299 -0.027 -0.040 0.002  22  CYS BBB CA  
1713  C C   . CYS B 23  ? 1.259 1.593 1.274 -0.033 -0.021 -0.011 22  CYS BBB C   
1714  O O   . CYS B 23  ? 1.242 1.586 1.256 -0.026 -0.019 0.002  22  CYS BBB O   
1715  C CB  . CYS B 23  ? 1.310 1.596 1.324 -0.029 -0.046 0.035  22  CYS BBB CB  
1716  S SG  . CYS B 23  ? 1.353 1.622 1.380 -0.041 -0.033 0.045  22  CYS BBB SG  
1717  N N   . LYS B 24  ? 1.256 1.593 1.274 -0.046 -0.006 -0.038 23  LYS BBB N   
1718  C CA  . LYS B 24  ? 1.273 1.625 1.294 -0.055 0.016  -0.058 23  LYS BBB CA  
1719  C C   . LYS B 24  ? 1.257 1.569 1.279 -0.065 0.034  -0.047 23  LYS BBB C   
1720  O O   . LYS B 24  ? 1.288 1.567 1.305 -0.069 0.033  -0.039 23  LYS BBB O   
1721  C CB  . LYS B 24  ? 1.320 1.704 1.343 -0.064 0.025  -0.100 23  LYS BBB CB  
1722  C CG  . LYS B 24  ? 1.373 1.783 1.399 -0.074 0.046  -0.127 23  LYS BBB CG  
1723  C CD  . LYS B 24  ? 1.414 1.870 1.447 -0.085 0.053  -0.173 23  LYS BBB CD  
1724  C CE  . LYS B 24  ? 1.442 1.934 1.478 -0.092 0.068  -0.200 23  LYS BBB CE  
1725  N NZ  . LYS B 24  ? 1.465 1.994 1.512 -0.113 0.085  -0.252 23  LYS BBB NZ  
1726  N N   . GLY B 25  ? 1.266 1.580 1.289 -0.066 0.051  -0.047 24  GLY BBB N   
1727  C CA  . GLY B 25  ? 1.320 1.595 1.342 -0.069 0.070  -0.036 24  GLY BBB CA  
1728  C C   . GLY B 25  ? 1.384 1.644 1.398 -0.085 0.100  -0.067 24  GLY BBB C   
1729  O O   . GLY B 25  ? 1.421 1.699 1.436 -0.090 0.116  -0.085 24  GLY BBB O   
1730  N N   . SER B 26  ? 1.423 1.647 1.425 -0.094 0.109  -0.072 25  SER BBB N   
1731  C CA  . SER B 26  ? 1.468 1.658 1.456 -0.112 0.144  -0.098 25  SER BBB CA  
1732  C C   . SER B 26  ? 1.502 1.648 1.480 -0.104 0.165  -0.080 25  SER BBB C   
1733  O O   . SER B 26  ? 1.491 1.602 1.460 -0.090 0.158  -0.050 25  SER BBB O   
1734  C CB  . SER B 26  ? 1.511 1.668 1.484 -0.122 0.149  -0.104 25  SER BBB CB  
1735  O OG  . SER B 26  ? 1.587 1.683 1.536 -0.129 0.183  -0.106 25  SER BBB OG  
1736  N N   . GLY B 27  ? 1.548 1.699 1.527 -0.111 0.190  -0.101 26  GLY BBB N   
1737  C CA  . GLY B 27  ? 1.618 1.719 1.583 -0.106 0.218  -0.092 26  GLY BBB CA  
1738  C C   . GLY B 27  ? 1.605 1.733 1.584 -0.096 0.219  -0.087 26  GLY BBB C   
1739  O O   . GLY B 27  ? 1.556 1.741 1.550 -0.098 0.203  -0.097 26  GLY BBB O   
1740  N N   . TYR B 28  ? 1.652 1.738 1.622 -0.082 0.239  -0.071 27  TYR BBB N   
1741  C CA  . TYR B 28  ? 1.693 1.794 1.672 -0.075 0.252  -0.072 27  TYR BBB CA  
1742  C C   . TYR B 28  ? 1.672 1.789 1.669 -0.049 0.229  -0.033 27  TYR BBB C   
1743  O O   . TYR B 28  ? 1.707 1.805 1.702 -0.035 0.213  -0.007 27  TYR BBB O   
1744  C CB  . TYR B 28  ? 1.781 1.822 1.738 -0.078 0.295  -0.086 27  TYR BBB CB  
1745  C CG  . TYR B 28  ? 1.816 1.850 1.762 -0.110 0.323  -0.132 27  TYR BBB CG  
1746  C CD1 . TYR B 28  ? 1.832 1.834 1.761 -0.128 0.333  -0.146 27  TYR BBB CD1 
1747  C CD2 . TYR B 28  ? 1.821 1.883 1.772 -0.125 0.340  -0.164 27  TYR BBB CD2 
1748  C CE1 . TYR B 28  ? 1.849 1.851 1.772 -0.161 0.361  -0.192 27  TYR BBB CE1 
1749  C CE2 . TYR B 28  ? 1.839 1.905 1.784 -0.157 0.366  -0.212 27  TYR BBB CE2 
1750  C CZ  . TYR B 28  ? 1.856 1.893 1.790 -0.176 0.377  -0.226 27  TYR BBB CZ  
1751  O OH  . TYR B 28  ? 1.919 1.963 1.851 -0.211 0.404  -0.277 27  TYR BBB OH  
1752  N N   . GLY B 29  ? 1.631 1.783 1.642 -0.043 0.229  -0.033 28  GLY BBB N   
1753  C CA  . GLY B 29  ? 1.603 1.778 1.635 -0.022 0.213  -0.001 28  GLY BBB CA  
1754  C C   . GLY B 29  ? 1.534 1.749 1.582 -0.022 0.177  0.016  28  GLY BBB C   
1755  O O   . GLY B 29  ? 1.528 1.757 1.595 -0.008 0.162  0.043  28  GLY BBB O   
1756  N N   . PHE B 30  ? 1.488 1.722 1.529 -0.037 0.165  -0.001 29  PHE BBB N   
1757  C CA  . PHE B 30  ? 1.450 1.717 1.500 -0.036 0.134  0.013  29  PHE BBB CA  
1758  C C   . PHE B 30  ? 1.428 1.727 1.492 -0.028 0.128  0.030  29  PHE BBB C   
1759  O O   . PHE B 30  ? 1.410 1.724 1.484 -0.025 0.107  0.050  29  PHE BBB O   
1760  C CB  . PHE B 30  ? 1.442 1.730 1.481 -0.049 0.127  -0.014 29  PHE BBB CB  
1761  C CG  . PHE B 30  ? 1.425 1.738 1.468 -0.045 0.097  0.000  29  PHE BBB CG  
1762  C CD1 . PHE B 30  ? 1.413 1.710 1.456 -0.046 0.080  0.010  29  PHE BBB CD1 
1763  C CD2 . PHE B 30  ? 1.416 1.763 1.457 -0.040 0.089  0.004  29  PHE BBB CD2 
1764  C CE1 . PHE B 30  ? 1.381 1.694 1.425 -0.042 0.055  0.022  29  PHE BBB CE1 
1765  C CE2 . PHE B 30  ? 1.398 1.757 1.436 -0.034 0.065  0.018  29  PHE BBB CE2 
1766  C CZ  . PHE B 30  ? 1.384 1.725 1.425 -0.035 0.049  0.026  29  PHE BBB CZ  
1767  N N   . ILE B 31  ? 1.426 1.732 1.489 -0.026 0.150  0.019  30  ILE BBB N   
1768  C CA  . ILE B 31  ? 1.428 1.766 1.499 -0.021 0.151  0.030  30  ILE BBB CA  
1769  C C   . ILE B 31  ? 1.407 1.749 1.502 -0.011 0.141  0.062  30  ILE BBB C   
1770  O O   . ILE B 31  ? 1.416 1.783 1.516 -0.011 0.133  0.075  30  ILE BBB O   
1771  C CB  . ILE B 31  ? 1.477 1.816 1.541 -0.021 0.181  0.011  30  ILE BBB CB  
1772  C CG1 . ILE B 31  ? 1.497 1.871 1.561 -0.017 0.182  0.018  30  ILE BBB CG1 
1773  C CG2 . ILE B 31  ? 1.491 1.796 1.564 -0.012 0.201  0.016  30  ILE BBB CG2 
1774  C CD1 . ILE B 31  ? 1.497 1.899 1.542 -0.021 0.164  0.013  30  ILE BBB CD1 
1775  N N   . THR B 32  ? 1.408 1.727 1.516 -0.003 0.142  0.072  31  THR BBB N   
1776  C CA  . THR B 32  ? 1.408 1.741 1.545 0.008  0.133  0.098  31  THR BBB CA  
1777  C C   . THR B 32  ? 1.382 1.721 1.526 0.001  0.105  0.112  31  THR BBB C   
1778  O O   . THR B 32  ? 1.386 1.746 1.556 0.004  0.096  0.129  31  THR BBB O   
1779  C CB  . THR B 32  ? 1.437 1.746 1.581 0.024  0.141  0.104  31  THR BBB CB  
1780  O OG1 . THR B 32  ? 1.436 1.718 1.567 0.024  0.127  0.105  31  THR BBB OG1 
1781  C CG2 . THR B 32  ? 1.491 1.776 1.621 0.031  0.173  0.088  31  THR BBB CG2 
1782  N N   . TYR B 33  ? 1.361 1.683 1.483 -0.007 0.093  0.102  32  TYR BBB N   
1783  C CA  . TYR B 33  ? 1.340 1.657 1.464 -0.012 0.068  0.111  32  TYR BBB CA  
1784  C C   . TYR B 33  ? 1.293 1.629 1.418 -0.020 0.056  0.119  32  TYR BBB C   
1785  O O   . TYR B 33  ? 1.281 1.626 1.389 -0.022 0.062  0.110  32  TYR BBB O   
1786  C CB  . TYR B 33  ? 1.367 1.657 1.467 -0.018 0.065  0.095  32  TYR BBB CB  
1787  C CG  . TYR B 33  ? 1.391 1.649 1.485 -0.010 0.071  0.096  32  TYR BBB CG  
1788  C CD1 . TYR B 33  ? 1.401 1.653 1.501 -0.005 0.052  0.111  32  TYR BBB CD1 
1789  C CD2 . TYR B 33  ? 1.411 1.644 1.490 -0.007 0.096  0.082  32  TYR BBB CD2 
1790  C CE1 . TYR B 33  ? 1.431 1.652 1.519 0.006  0.057  0.114  32  TYR BBB CE1 
1791  C CE2 . TYR B 33  ? 1.456 1.651 1.522 0.004  0.105  0.086  32  TYR BBB CE2 
1792  C CZ  . TYR B 33  ? 1.469 1.658 1.537 0.012  0.084  0.104  32  TYR BBB CZ  
1793  O OH  . TYR B 33  ? 1.517 1.667 1.565 0.026  0.091  0.110  32  TYR BBB OH  
1794  N N   . TRP B 34  ? 1.278 1.618 1.419 -0.024 0.039  0.135  33  TRP BBB N   
1795  C CA  . TRP B 34  ? 1.306 1.651 1.445 -0.033 0.028  0.145  33  TRP BBB CA  
1796  C C   . TRP B 34  ? 1.299 1.623 1.428 -0.038 0.008  0.142  33  TRP BBB C   
1797  O O   . TRP B 34  ? 1.303 1.625 1.447 -0.039 -0.003 0.147  33  TRP BBB O   
1798  C CB  . TRP B 34  ? 1.334 1.699 1.504 -0.038 0.029  0.161  33  TRP BBB CB  
1799  C CG  . TRP B 34  ? 1.354 1.743 1.538 -0.035 0.050  0.164  33  TRP BBB CG  
1800  C CD1 . TRP B 34  ? 1.361 1.758 1.552 -0.023 0.066  0.158  33  TRP BBB CD1 
1801  C CD2 . TRP B 34  ? 1.345 1.748 1.537 -0.043 0.061  0.175  33  TRP BBB CD2 
1802  N NE1 . TRP B 34  ? 1.336 1.756 1.541 -0.023 0.084  0.163  33  TRP BBB NE1 
1803  C CE2 . TRP B 34  ? 1.338 1.762 1.543 -0.036 0.081  0.174  33  TRP BBB CE2 
1804  C CE3 . TRP B 34  ? 1.358 1.753 1.544 -0.057 0.058  0.186  33  TRP BBB CE3 
1805  C CZ2 . TRP B 34  ? 1.366 1.808 1.580 -0.043 0.099  0.183  33  TRP BBB CZ2 
1806  C CZ3 . TRP B 34  ? 1.382 1.788 1.574 -0.064 0.077  0.196  33  TRP BBB CZ3 
1807  C CH2 . TRP B 34  ? 1.385 1.817 1.591 -0.058 0.097  0.194  33  TRP BBB CH2 
1808  N N   . ILE B 35  ? 1.312 1.627 1.416 -0.038 0.003  0.135  34  ILE BBB N   
1809  C CA  . ILE B 35  ? 1.338 1.633 1.430 -0.041 -0.014 0.130  34  ILE BBB CA  
1810  C C   . ILE B 35  ? 1.350 1.636 1.444 -0.048 -0.025 0.144  34  ILE BBB C   
1811  O O   . ILE B 35  ? 1.346 1.631 1.425 -0.046 -0.020 0.150  34  ILE BBB O   
1812  C CB  . ILE B 35  ? 1.376 1.669 1.444 -0.036 -0.014 0.111  34  ILE BBB CB  
1813  C CG1 . ILE B 35  ? 1.404 1.697 1.469 -0.036 -0.002 0.092  34  ILE BBB CG1 
1814  C CG2 . ILE B 35  ? 1.403 1.679 1.459 -0.038 -0.031 0.108  34  ILE BBB CG2 
1815  C CD1 . ILE B 35  ? 1.442 1.751 1.509 -0.033 0.017  0.086  34  ILE BBB CD1 
1816  N N   . GLY B 36  ? 1.356 1.635 1.464 -0.056 -0.037 0.149  35  GLY BBB N   
1817  C CA  . GLY B 36  ? 1.375 1.639 1.484 -0.067 -0.047 0.157  35  GLY BBB CA  
1818  C C   . GLY B 36  ? 1.377 1.616 1.464 -0.066 -0.060 0.148  35  GLY BBB C   
1819  O O   . GLY B 36  ? 1.365 1.603 1.441 -0.058 -0.062 0.134  35  GLY BBB O   
1820  N N   . TRP B 37  ? 1.399 1.616 1.477 -0.072 -0.065 0.154  36  TRP BBB N   
1821  C CA  . TRP B 37  ? 1.407 1.597 1.466 -0.071 -0.077 0.146  36  TRP BBB CA  
1822  C C   . TRP B 37  ? 1.423 1.598 1.494 -0.089 -0.086 0.149  36  TRP BBB C   
1823  O O   . TRP B 37  ? 1.435 1.610 1.521 -0.102 -0.080 0.159  36  TRP BBB O   
1824  C CB  . TRP B 37  ? 1.428 1.598 1.457 -0.058 -0.074 0.149  36  TRP BBB CB  
1825  C CG  . TRP B 37  ? 1.406 1.596 1.421 -0.040 -0.070 0.140  36  TRP BBB CG  
1826  C CD1 . TRP B 37  ? 1.414 1.622 1.424 -0.033 -0.058 0.145  36  TRP BBB CD1 
1827  C CD2 . TRP B 37  ? 1.407 1.607 1.413 -0.030 -0.076 0.120  36  TRP BBB CD2 
1828  N NE1 . TRP B 37  ? 1.421 1.651 1.420 -0.018 -0.058 0.128  36  TRP BBB NE1 
1829  C CE2 . TRP B 37  ? 1.411 1.638 1.409 -0.018 -0.069 0.112  36  TRP BBB CE2 
1830  C CE3 . TRP B 37  ? 1.431 1.620 1.433 -0.032 -0.086 0.105  36  TRP BBB CE3 
1831  C CZ2 . TRP B 37  ? 1.430 1.677 1.421 -0.009 -0.071 0.088  36  TRP BBB CZ2 
1832  C CZ3 . TRP B 37  ? 1.439 1.646 1.435 -0.022 -0.086 0.084  36  TRP BBB CZ3 
1833  C CH2 . TRP B 37  ? 1.445 1.683 1.437 -0.012 -0.079 0.074  36  TRP BBB CH2 
1834  N N   . VAL B 38  ? 1.447 1.613 1.514 -0.091 -0.099 0.137  37  VAL BBB N   
1835  C CA  . VAL B 38  ? 1.481 1.636 1.557 -0.108 -0.110 0.135  37  VAL BBB CA  
1836  C C   . VAL B 38  ? 1.513 1.632 1.562 -0.105 -0.117 0.126  37  VAL BBB C   
1837  O O   . VAL B 38  ? 1.520 1.638 1.554 -0.092 -0.119 0.116  37  VAL BBB O   
1838  C CB  . VAL B 38  ? 1.471 1.652 1.564 -0.110 -0.120 0.130  37  VAL BBB CB  
1839  C CG1 . VAL B 38  ? 1.496 1.675 1.598 -0.127 -0.134 0.124  37  VAL BBB CG1 
1840  C CG2 . VAL B 38  ? 1.455 1.672 1.574 -0.108 -0.112 0.139  37  VAL BBB CG2 
1841  N N   . ARG B 39  ? 1.544 1.636 1.590 -0.119 -0.117 0.127  38  ARG BBB N   
1842  C CA  . ARG B 39  ? 1.570 1.624 1.594 -0.118 -0.123 0.118  38  ARG BBB CA  
1843  C C   . ARG B 39  ? 1.552 1.609 1.585 -0.136 -0.136 0.106  38  ARG BBB C   
1844  O O   . ARG B 39  ? 1.549 1.617 1.605 -0.157 -0.137 0.107  38  ARG BBB O   
1845  C CB  . ARG B 39  ? 1.650 1.661 1.655 -0.120 -0.112 0.127  38  ARG BBB CB  
1846  C CG  . ARG B 39  ? 1.713 1.680 1.693 -0.115 -0.115 0.118  38  ARG BBB CG  
1847  C CD  . ARG B 39  ? 1.791 1.705 1.745 -0.111 -0.101 0.131  38  ARG BBB CD  
1848  N NE  . ARG B 39  ? 1.837 1.727 1.802 -0.141 -0.090 0.135  38  ARG BBB NE  
1849  C CZ  . ARG B 39  ? 1.944 1.777 1.885 -0.145 -0.073 0.144  38  ARG BBB CZ  
1850  N NH1 . ARG B 39  ? 1.995 1.787 1.896 -0.114 -0.067 0.154  38  ARG BBB NH1 
1851  N NH2 . ARG B 39  ? 1.996 1.810 1.950 -0.178 -0.061 0.144  38  ARG BBB NH2 
1852  N N   . GLN B 40  ? 1.526 1.577 1.543 -0.129 -0.146 0.093  39  GLN BBB N   
1853  C CA  . GLN B 40  ? 1.545 1.588 1.559 -0.144 -0.158 0.079  39  GLN BBB CA  
1854  C C   . GLN B 40  ? 1.568 1.567 1.557 -0.140 -0.156 0.070  39  GLN BBB C   
1855  O O   . GLN B 40  ? 1.539 1.532 1.511 -0.121 -0.155 0.064  39  GLN BBB O   
1856  C CB  . GLN B 40  ? 1.536 1.603 1.547 -0.137 -0.167 0.073  39  GLN BBB CB  
1857  C CG  . GLN B 40  ? 1.564 1.625 1.565 -0.148 -0.181 0.059  39  GLN BBB CG  
1858  C CD  . GLN B 40  ? 1.553 1.642 1.554 -0.143 -0.191 0.059  39  GLN BBB CD  
1859  O OE1 . GLN B 40  ? 1.546 1.631 1.527 -0.129 -0.186 0.058  39  GLN BBB OE1 
1860  N NE2 . GLN B 40  ? 1.565 1.683 1.585 -0.153 -0.203 0.060  39  GLN BBB NE2 
1861  N N   . MET B 41  ? 1.604 1.572 1.591 -0.157 -0.154 0.068  40  MET BBB N   
1862  C CA  . MET B 41  ? 1.677 1.595 1.637 -0.153 -0.150 0.059  40  MET BBB CA  
1863  C C   . MET B 41  ? 1.731 1.648 1.681 -0.158 -0.163 0.039  40  MET BBB C   
1864  O O   . MET B 41  ? 1.799 1.748 1.761 -0.169 -0.174 0.034  40  MET BBB O   
1865  C CB  . MET B 41  ? 1.711 1.587 1.670 -0.172 -0.139 0.063  40  MET BBB CB  
1866  C CG  . MET B 41  ? 1.732 1.577 1.674 -0.155 -0.122 0.081  40  MET BBB CG  
1867  S SD  . MET B 41  ? 1.826 1.624 1.769 -0.184 -0.102 0.089  40  MET BBB SD  
1868  C CE  . MET B 41  ? 1.902 1.625 1.797 -0.153 -0.086 0.101  40  MET BBB CE  
1869  N N   . PRO B 42  ? 1.761 1.642 1.685 -0.147 -0.160 0.028  41  PRO BBB N   
1870  C CA  . PRO B 42  ? 1.741 1.619 1.652 -0.152 -0.170 0.008  41  PRO BBB CA  
1871  C C   . PRO B 42  ? 1.750 1.638 1.670 -0.180 -0.181 -0.001 41  PRO BBB C   
1872  O O   . PRO B 42  ? 1.781 1.639 1.700 -0.199 -0.177 -0.007 41  PRO BBB O   
1873  C CB  . PRO B 42  ? 1.797 1.624 1.684 -0.142 -0.161 -0.001 41  PRO BBB CB  
1874  C CG  . PRO B 42  ? 1.814 1.633 1.698 -0.117 -0.151 0.015  41  PRO BBB CG  
1875  C CD  . PRO B 42  ? 1.806 1.648 1.712 -0.127 -0.148 0.034  41  PRO BBB CD  
1876  N N   . GLY B 43  ? 1.726 1.654 1.651 -0.182 -0.193 -0.003 42  GLY BBB N   
1877  C CA  . GLY B 43  ? 1.735 1.685 1.665 -0.202 -0.208 -0.014 42  GLY BBB CA  
1878  C C   . GLY B 43  ? 1.733 1.705 1.695 -0.223 -0.210 -0.009 42  GLY BBB C   
1879  O O   . GLY B 43  ? 1.749 1.722 1.716 -0.248 -0.218 -0.025 42  GLY BBB O   
1880  N N   . LYS B 44  ? 1.727 1.717 1.711 -0.216 -0.202 0.010  43  LYS BBB N   
1881  C CA  . LYS B 44  ? 1.762 1.775 1.780 -0.236 -0.198 0.015  43  LYS BBB CA  
1882  C C   . LYS B 44  ? 1.738 1.805 1.779 -0.224 -0.204 0.029  43  LYS BBB C   
1883  O O   . LYS B 44  ? 1.727 1.804 1.754 -0.201 -0.208 0.035  43  LYS BBB O   
1884  C CB  . LYS B 44  ? 1.804 1.775 1.820 -0.236 -0.177 0.027  43  LYS BBB CB  
1885  C CG  . LYS B 44  ? 1.851 1.757 1.837 -0.236 -0.167 0.019  43  LYS BBB CG  
1886  C CD  . LYS B 44  ? 1.899 1.782 1.888 -0.269 -0.165 0.001  43  LYS BBB CD  
1887  C CE  . LYS B 44  ? 1.965 1.772 1.926 -0.269 -0.146 0.000  43  LYS BBB CE  
1888  N NZ  . LYS B 44  ? 2.042 1.823 2.007 -0.307 -0.140 -0.021 43  LYS BBB NZ  
1889  N N   . GLY B 45  ? 1.735 1.834 1.813 -0.240 -0.201 0.033  44  GLY BBB N   
1890  C CA  . GLY B 45  ? 1.688 1.840 1.793 -0.230 -0.204 0.045  44  GLY BBB CA  
1891  C C   . GLY B 45  ? 1.648 1.788 1.750 -0.211 -0.187 0.065  44  GLY BBB C   
1892  O O   . GLY B 45  ? 1.678 1.771 1.756 -0.204 -0.174 0.069  44  GLY BBB O   
1893  N N   . LEU B 46  ? 1.594 1.778 1.720 -0.201 -0.187 0.076  45  LEU BBB N   
1894  C CA  . LEU B 46  ? 1.567 1.749 1.692 -0.183 -0.171 0.093  45  LEU BBB CA  
1895  C C   . LEU B 46  ? 1.587 1.770 1.734 -0.198 -0.154 0.101  45  LEU BBB C   
1896  O O   . LEU B 46  ? 1.595 1.818 1.778 -0.214 -0.156 0.098  45  LEU BBB O   
1897  C CB  . LEU B 46  ? 1.524 1.746 1.659 -0.164 -0.178 0.099  45  LEU BBB CB  
1898  C CG  . LEU B 46  ? 1.514 1.731 1.623 -0.149 -0.191 0.093  45  LEU BBB CG  
1899  C CD1 . LEU B 46  ? 1.492 1.744 1.610 -0.130 -0.194 0.101  45  LEU BBB CD1 
1900  C CD2 . LEU B 46  ? 1.512 1.687 1.586 -0.138 -0.182 0.091  45  LEU BBB CD2 
1901  N N   . GLU B 47  ? 1.636 1.779 1.763 -0.192 -0.138 0.111  46  GLU BBB N   
1902  C CA  . GLU B 47  ? 1.698 1.833 1.835 -0.203 -0.117 0.123  46  GLU BBB CA  
1903  C C   . GLU B 47  ? 1.649 1.799 1.783 -0.180 -0.108 0.137  46  GLU BBB C   
1904  O O   . GLU B 47  ? 1.642 1.774 1.748 -0.158 -0.108 0.139  46  GLU BBB O   
1905  C CB  . GLU B 47  ? 1.813 1.884 1.919 -0.209 -0.104 0.125  46  GLU BBB CB  
1906  C CG  . GLU B 47  ? 1.880 1.923 1.977 -0.226 -0.114 0.108  46  GLU BBB CG  
1907  C CD  . GLU B 47  ? 1.956 1.928 2.013 -0.221 -0.102 0.111  46  GLU BBB CD  
1908  O OE1 . GLU B 47  ? 2.005 1.940 2.054 -0.232 -0.081 0.120  46  GLU BBB OE1 
1909  O OE2 . GLU B 47  ? 1.989 1.941 2.021 -0.205 -0.113 0.103  46  GLU BBB OE2 
1910  N N   . TRP B 48  ? 1.618 1.806 1.783 -0.186 -0.099 0.144  47  TRP BBB N   
1911  C CA  . TRP B 48  ? 1.603 1.803 1.765 -0.168 -0.086 0.156  47  TRP BBB CA  
1912  C C   . TRP B 48  ? 1.593 1.751 1.727 -0.168 -0.066 0.169  47  TRP BBB C   
1913  O O   . TRP B 48  ? 1.610 1.754 1.753 -0.190 -0.052 0.172  47  TRP BBB O   
1914  C CB  . TRP B 48  ? 1.648 1.903 1.852 -0.173 -0.082 0.158  47  TRP BBB CB  
1915  C CG  . TRP B 48  ? 1.698 1.967 1.899 -0.155 -0.068 0.168  47  TRP BBB CG  
1916  C CD1 . TRP B 48  ? 1.711 1.994 1.905 -0.132 -0.073 0.167  47  TRP BBB CD1 
1917  C CD2 . TRP B 48  ? 1.737 2.005 1.939 -0.159 -0.046 0.180  47  TRP BBB CD2 
1918  N NE1 . TRP B 48  ? 1.703 1.996 1.897 -0.123 -0.056 0.175  47  TRP BBB NE1 
1919  C CE2 . TRP B 48  ? 1.712 1.998 1.910 -0.138 -0.040 0.184  47  TRP BBB CE2 
1920  C CE3 . TRP B 48  ? 1.798 2.048 2.002 -0.180 -0.027 0.187  47  TRP BBB CE3 
1921  C CZ2 . TRP B 48  ? 1.728 2.018 1.923 -0.136 -0.018 0.194  47  TRP BBB CZ2 
1922  C CZ3 . TRP B 48  ? 1.833 2.085 2.032 -0.178 -0.005 0.199  47  TRP BBB CZ3 
1923  C CH2 . TRP B 48  ? 1.796 2.069 1.990 -0.155 -0.002 0.202  47  TRP BBB CH2 
1924  N N   . MET B 49  ? 1.576 1.717 1.678 -0.144 -0.064 0.174  48  MET BBB N   
1925  C CA  . MET B 49  ? 1.618 1.717 1.684 -0.134 -0.049 0.187  48  MET BBB CA  
1926  C C   . MET B 49  ? 1.603 1.720 1.671 -0.131 -0.030 0.200  48  MET BBB C   
1927  O O   . MET B 49  ? 1.643 1.733 1.702 -0.142 -0.011 0.212  48  MET BBB O   
1928  C CB  . MET B 49  ? 1.620 1.702 1.650 -0.107 -0.058 0.182  48  MET BBB CB  
1929  C CG  . MET B 49  ? 1.627 1.690 1.651 -0.108 -0.074 0.169  48  MET BBB CG  
1930  S SD  . MET B 49  ? 1.625 1.676 1.613 -0.075 -0.082 0.161  48  MET BBB SD  
1931  C CE  . MET B 49  ? 1.680 1.674 1.626 -0.063 -0.069 0.178  48  MET BBB CE  
1932  N N   . GLY B 50  ? 1.565 1.722 1.644 -0.116 -0.033 0.196  49  GLY BBB N   
1933  C CA  . GLY B 50  ? 1.582 1.759 1.660 -0.108 -0.017 0.205  49  GLY BBB CA  
1934  C C   . GLY B 50  ? 1.549 1.765 1.639 -0.094 -0.022 0.196  49  GLY BBB C   
1935  O O   . GLY B 50  ? 1.566 1.784 1.654 -0.086 -0.037 0.183  49  GLY BBB O   
1936  N N   . ILE B 51  ? 1.541 1.783 1.643 -0.091 -0.007 0.200  50  ILE BBB N   
1937  C CA  . ILE B 51  ? 1.501 1.774 1.610 -0.078 -0.006 0.191  50  ILE BBB CA  
1938  C C   . ILE B 51  ? 1.499 1.774 1.582 -0.065 0.009  0.196  50  ILE BBB C   
1939  O O   . ILE B 51  ? 1.519 1.781 1.590 -0.070 0.023  0.210  50  ILE BBB O   
1940  C CB  . ILE B 51  ? 1.501 1.809 1.654 -0.085 -0.003 0.190  50  ILE BBB CB  
1941  C CG1 . ILE B 51  ? 1.513 1.841 1.670 -0.070 -0.002 0.180  50  ILE BBB CG1 
1942  C CG2 . ILE B 51  ? 1.506 1.831 1.677 -0.096 0.017  0.201  50  ILE BBB CG2 
1943  C CD1 . ILE B 51  ? 1.530 1.876 1.717 -0.069 -0.012 0.176  50  ILE BBB CD1 
1944  N N   . ILE B 52  ? 1.479 1.768 1.551 -0.051 0.008  0.182  51  ILE BBB N   
1945  C CA  . ILE B 52  ? 1.478 1.780 1.527 -0.038 0.022  0.181  51  ILE BBB CA  
1946  C C   . ILE B 52  ? 1.439 1.769 1.508 -0.036 0.030  0.167  51  ILE BBB C   
1947  O O   . ILE B 52  ? 1.407 1.738 1.489 -0.036 0.021  0.155  51  ILE BBB O   
1948  C CB  . ILE B 52  ? 1.493 1.785 1.502 -0.022 0.013  0.173  51  ILE BBB CB  
1949  C CG1 . ILE B 52  ? 1.522 1.829 1.503 -0.009 0.025  0.174  51  ILE BBB CG1 
1950  C CG2 . ILE B 52  ? 1.481 1.783 1.495 -0.018 0.000  0.151  51  ILE BBB CG2 
1951  C CD1 . ILE B 52  ? 1.568 1.868 1.506 0.012  0.014  0.171  51  ILE BBB CD1 
1952  N N   . TYR B 53  ? 1.439 1.785 1.505 -0.033 0.048  0.169  52  TYR BBB N   
1953  C CA  . TYR B 53  ? 1.430 1.797 1.504 -0.027 0.060  0.154  52  TYR BBB CA  
1954  C C   . TYR B 53  ? 1.433 1.808 1.472 -0.017 0.062  0.138  52  TYR BBB C   
1955  O O   . TYR B 53  ? 1.453 1.835 1.469 -0.011 0.071  0.144  52  TYR BBB O   
1956  C CB  . TYR B 53  ? 1.437 1.822 1.535 -0.031 0.080  0.163  52  TYR BBB CB  
1957  C CG  . TYR B 53  ? 1.452 1.852 1.554 -0.024 0.095  0.147  52  TYR BBB CG  
1958  C CD1 . TYR B 53  ? 1.439 1.833 1.551 -0.021 0.092  0.133  52  TYR BBB CD1 
1959  C CD2 . TYR B 53  ? 1.499 1.914 1.590 -0.021 0.115  0.145  52  TYR BBB CD2 
1960  C CE1 . TYR B 53  ? 1.450 1.848 1.561 -0.016 0.110  0.117  52  TYR BBB CE1 
1961  C CE2 . TYR B 53  ? 1.496 1.921 1.589 -0.015 0.131  0.128  52  TYR BBB CE2 
1962  C CZ  . TYR B 53  ? 1.464 1.878 1.567 -0.013 0.129  0.113  52  TYR BBB CZ  
1963  O OH  . TYR B 53  ? 1.451 1.866 1.553 -0.009 0.149  0.095  52  TYR BBB OH  
1964  N N   . PRO B 54  ? 1.422 1.798 1.455 -0.014 0.053  0.116  53  PRO BBB N   
1965  C CA  . PRO B 54  ? 1.438 1.832 1.442 -0.005 0.052  0.096  53  PRO BBB CA  
1966  C C   . PRO B 54  ? 1.464 1.880 1.456 -0.001 0.071  0.089  53  PRO BBB C   
1967  O O   . PRO B 54  ? 1.470 1.903 1.431 0.010  0.068  0.082  53  PRO BBB O   
1968  C CB  . PRO B 54  ? 1.420 1.816 1.435 -0.011 0.051  0.069  53  PRO BBB CB  
1969  C CG  . PRO B 54  ? 1.391 1.761 1.426 -0.018 0.042  0.082  53  PRO BBB CG  
1970  C CD  . PRO B 54  ? 1.398 1.762 1.451 -0.020 0.046  0.109  53  PRO BBB CD  
1971  N N   . GLY B 55  ? 1.471 1.887 1.486 -0.007 0.089  0.091  54  GLY BBB N   
1972  C CA  . GLY B 55  ? 1.518 1.952 1.526 -0.005 0.110  0.084  54  GLY BBB CA  
1973  C C   . GLY B 55  ? 1.557 2.000 1.533 0.003  0.112  0.097  54  GLY BBB C   
1974  O O   . GLY B 55  ? 1.600 2.063 1.544 0.012  0.110  0.080  54  GLY BBB O   
1975  N N   . ASP B 56  ? 1.578 2.008 1.560 0.000  0.116  0.125  55  ASP BBB N   
1976  C CA  . ASP B 56  ? 1.667 2.093 1.612 0.007  0.122  0.143  55  ASP BBB CA  
1977  C C   . ASP B 56  ? 1.638 2.036 1.567 0.010  0.105  0.163  55  ASP BBB C   
1978  O O   . ASP B 56  ? 1.720 2.099 1.624 0.012  0.113  0.185  55  ASP BBB O   
1979  C CB  . ASP B 56  ? 1.761 2.190 1.721 -0.001 0.147  0.159  55  ASP BBB CB  
1980  C CG  . ASP B 56  ? 1.765 2.187 1.774 -0.015 0.150  0.173  55  ASP BBB CG  
1981  O OD1 . ASP B 56  ? 1.745 2.153 1.770 -0.019 0.131  0.177  55  ASP BBB OD1 
1982  O OD2 . ASP B 56  ? 1.806 2.240 1.838 -0.021 0.170  0.179  55  ASP BBB OD2 
1983  N N   . SER B 57  ? 1.546 1.937 1.487 0.010  0.084  0.154  56  SER BBB N   
1984  C CA  . SER B 57  ? 1.551 1.913 1.477 0.014  0.068  0.169  56  SER BBB CA  
1985  C C   . SER B 57  ? 1.603 1.936 1.535 0.002  0.079  0.197  56  SER BBB C   
1986  O O   . SER B 57  ? 1.672 1.975 1.570 0.009  0.077  0.215  56  SER BBB O   
1987  C CB  . SER B 57  ? 1.559 1.924 1.435 0.037  0.057  0.165  56  SER BBB CB  
1988  O OG  . SER B 57  ? 1.520 1.921 1.398 0.043  0.047  0.133  56  SER BBB OG  
1989  N N   . GLU B 58  ? 1.617 1.960 1.592 -0.016 0.091  0.200  57  GLU BBB N   
1990  C CA  . GLU B 58  ? 1.640 1.968 1.637 -0.034 0.103  0.220  57  GLU BBB CA  
1991  C C   . GLU B 58  ? 1.625 1.931 1.638 -0.043 0.085  0.222  57  GLU BBB C   
1992  O O   . GLU B 58  ? 1.592 1.914 1.641 -0.047 0.072  0.210  57  GLU BBB O   
1993  C CB  . GLU B 58  ? 1.623 1.982 1.668 -0.045 0.119  0.216  57  GLU BBB CB  
1994  C CG  . GLU B 58  ? 1.635 1.993 1.716 -0.067 0.128  0.229  57  GLU BBB CG  
1995  C CD  . GLU B 58  ? 1.631 2.029 1.760 -0.074 0.144  0.225  57  GLU BBB CD  
1996  O OE1 . GLU B 58  ? 1.593 2.013 1.733 -0.061 0.144  0.211  57  GLU BBB OE1 
1997  O OE2 . GLU B 58  ? 1.646 2.052 1.802 -0.092 0.158  0.234  57  GLU BBB OE2 
1998  N N   . THR B 59  ? 1.680 1.948 1.665 -0.044 0.084  0.238  58  THR BBB N   
1999  C CA  . THR B 59  ? 1.696 1.935 1.682 -0.049 0.066  0.238  58  THR BBB CA  
2000  C C   . THR B 59  ? 1.715 1.934 1.723 -0.075 0.079  0.251  58  THR BBB C   
2001  O O   . THR B 59  ? 1.832 2.033 1.821 -0.081 0.102  0.267  58  THR BBB O   
2002  C CB  . THR B 59  ? 1.756 1.964 1.688 -0.027 0.057  0.243  58  THR BBB CB  
2003  O OG1 . THR B 59  ? 1.784 2.021 1.695 -0.005 0.053  0.230  58  THR BBB OG1 
2004  C CG2 . THR B 59  ? 1.755 1.942 1.689 -0.025 0.036  0.236  58  THR BBB CG2 
2005  N N   . ARG B 60  ? 1.633 1.856 1.678 -0.090 0.065  0.244  59  ARG BBB N   
2006  C CA  . ARG B 60  ? 1.617 1.823 1.684 -0.118 0.073  0.250  59  ARG BBB CA  
2007  C C   . ARG B 60  ? 1.613 1.786 1.671 -0.120 0.054  0.246  59  ARG BBB C   
2008  O O   . ARG B 60  ? 1.615 1.801 1.676 -0.107 0.032  0.233  59  ARG BBB O   
2009  C CB  . ARG B 60  ? 1.563 1.821 1.692 -0.136 0.074  0.241  59  ARG BBB CB  
2010  C CG  . ARG B 60  ? 1.541 1.838 1.685 -0.128 0.090  0.241  59  ARG BBB CG  
2011  C CD  . ARG B 60  ? 1.504 1.853 1.709 -0.143 0.095  0.233  59  ARG BBB CD  
2012  N NE  . ARG B 60  ? 1.478 1.861 1.693 -0.130 0.108  0.231  59  ARG BBB NE  
2013  C CZ  . ARG B 60  ? 1.475 1.906 1.739 -0.135 0.117  0.226  59  ARG BBB CZ  
2014  N NH1 . ARG B 60  ? 1.470 1.929 1.782 -0.154 0.112  0.220  59  ARG BBB NH1 
2015  N NH2 . ARG B 60  ? 1.489 1.943 1.756 -0.120 0.130  0.224  59  ARG BBB NH2 
2016  N N   . TYR B 61  ? 1.649 1.778 1.693 -0.138 0.065  0.255  60  TYR BBB N   
2017  C CA  . TYR B 61  ? 1.668 1.756 1.698 -0.141 0.051  0.251  60  TYR BBB CA  
2018  C C   . TYR B 61  ? 1.674 1.767 1.747 -0.177 0.055  0.243  60  TYR BBB C   
2019  O O   . TYR B 61  ? 1.700 1.811 1.800 -0.200 0.075  0.245  60  TYR BBB O   
2020  C CB  . TYR B 61  ? 1.749 1.769 1.716 -0.126 0.063  0.267  60  TYR BBB CB  
2021  C CG  . TYR B 61  ? 1.743 1.764 1.667 -0.087 0.054  0.271  60  TYR BBB CG  
2022  C CD1 . TYR B 61  ? 1.699 1.737 1.622 -0.067 0.028  0.257  60  TYR BBB CD1 
2023  C CD2 . TYR B 61  ? 1.779 1.790 1.664 -0.072 0.072  0.287  60  TYR BBB CD2 
2024  C CE1 . TYR B 61  ? 1.690 1.738 1.579 -0.034 0.019  0.255  60  TYR BBB CE1 
2025  C CE2 . TYR B 61  ? 1.771 1.792 1.618 -0.036 0.061  0.287  60  TYR BBB CE2 
2026  C CZ  . TYR B 61  ? 1.725 1.768 1.577 -0.018 0.035  0.269  60  TYR BBB CZ  
2027  O OH  . TYR B 61  ? 1.730 1.792 1.550 0.015  0.024  0.264  60  TYR BBB OH  
2028  N N   . SER B 62  ? 1.673 1.756 1.753 -0.183 0.035  0.230  61  SER BBB N   
2029  C CA  . SER B 62  ? 1.723 1.795 1.829 -0.217 0.039  0.221  61  SER BBB CA  
2030  C C   . SER B 62  ? 1.834 1.832 1.898 -0.228 0.066  0.235  61  SER BBB C   
2031  O O   . SER B 62  ? 1.898 1.846 1.907 -0.202 0.068  0.249  61  SER BBB O   
2032  C CB  . SER B 62  ? 1.702 1.775 1.815 -0.217 0.012  0.205  61  SER BBB CB  
2033  O OG  . SER B 62  ? 1.735 1.784 1.860 -0.249 0.017  0.195  61  SER BBB OG  
2034  N N   . PRO B 63  ? 1.892 1.880 1.978 -0.266 0.089  0.233  62  PRO BBB N   
2035  C CA  . PRO B 63  ? 1.996 1.900 2.037 -0.281 0.119  0.245  62  PRO BBB CA  
2036  C C   . PRO B 63  ? 2.050 1.888 2.048 -0.266 0.107  0.245  62  PRO BBB C   
2037  O O   . PRO B 63  ? 2.124 1.885 2.064 -0.254 0.126  0.262  62  PRO BBB O   
2038  C CB  . PRO B 63  ? 2.014 1.933 2.103 -0.332 0.138  0.230  62  PRO BBB CB  
2039  C CG  . PRO B 63  ? 1.941 1.961 2.096 -0.337 0.125  0.217  62  PRO BBB CG  
2040  C CD  . PRO B 63  ? 1.860 1.916 2.013 -0.298 0.089  0.215  62  PRO BBB CD  
2041  N N   . SER B 64  ? 2.025 1.896 2.049 -0.264 0.075  0.225  63  SER BBB N   
2042  C CA  . SER B 64  ? 2.065 1.888 2.058 -0.251 0.061  0.219  63  SER BBB CA  
2043  C C   . SER B 64  ? 2.052 1.860 1.999 -0.202 0.046  0.231  63  SER BBB C   
2044  O O   . SER B 64  ? 2.082 1.865 2.010 -0.186 0.031  0.223  63  SER BBB O   
2045  C CB  . SER B 64  ? 2.040 1.909 2.076 -0.267 0.034  0.193  63  SER BBB CB  
2046  O OG  . SER B 64  ? 2.056 1.965 2.143 -0.308 0.042  0.179  63  SER BBB OG  
2047  N N   . PHE B 65  ? 2.013 1.844 1.948 -0.179 0.051  0.246  64  PHE BBB N   
2048  C CA  . PHE B 65  ? 1.980 1.810 1.876 -0.133 0.038  0.254  64  PHE BBB CA  
2049  C C   . PHE B 65  ? 2.017 1.827 1.871 -0.113 0.058  0.277  64  PHE BBB C   
2050  O O   . PHE B 65  ? 2.068 1.852 1.873 -0.074 0.053  0.287  64  PHE BBB O   
2051  C CB  . PHE B 65  ? 1.869 1.772 1.801 -0.123 0.010  0.236  64  PHE BBB CB  
2052  C CG  . PHE B 65  ? 1.843 1.754 1.798 -0.133 -0.011 0.216  64  PHE BBB CG  
2053  C CD1 . PHE B 65  ? 1.869 1.745 1.793 -0.114 -0.022 0.211  64  PHE BBB CD1 
2054  C CD2 . PHE B 65  ? 1.811 1.766 1.816 -0.161 -0.019 0.202  64  PHE BBB CD2 
2055  C CE1 . PHE B 65  ? 1.849 1.730 1.791 -0.124 -0.039 0.192  64  PHE BBB CE1 
2056  C CE2 . PHE B 65  ? 1.797 1.758 1.816 -0.170 -0.038 0.184  64  PHE BBB CE2 
2057  C CZ  . PHE B 65  ? 1.804 1.726 1.791 -0.153 -0.047 0.179  64  PHE BBB CZ  
2058  N N   . GLN B 66  ? 2.000 1.823 1.871 -0.135 0.081  0.286  65  GLN BBB N   
2059  C CA  . GLN B 66  ? 2.038 1.848 1.870 -0.118 0.103  0.307  65  GLN BBB CA  
2060  C C   . GLN B 66  ? 2.082 1.845 1.843 -0.073 0.098  0.322  65  GLN BBB C   
2061  O O   . GLN B 66  ? 2.055 1.862 1.808 -0.041 0.080  0.319  65  GLN BBB O   
2062  C CB  . GLN B 66  ? 2.117 1.886 1.945 -0.153 0.141  0.320  65  GLN BBB CB  
2063  C CG  . GLN B 66  ? 2.166 1.919 1.952 -0.139 0.167  0.343  65  GLN BBB CG  
2064  C CD  . GLN B 66  ? 2.103 1.938 1.923 -0.133 0.158  0.336  65  GLN BBB CD  
2065  O OE1 . GLN B 66  ? 2.127 1.971 1.910 -0.099 0.155  0.345  65  GLN BBB OE1 
2066  N NE2 . GLN B 66  ? 2.026 1.923 1.917 -0.163 0.154  0.318  65  GLN BBB NE2 
2067  N N   . GLY B 67  ? 2.152 1.832 1.867 -0.069 0.112  0.335  66  GLY BBB N   
2068  C CA  . GLY B 67  ? 2.222 1.845 1.860 -0.022 0.115  0.355  66  GLY BBB CA  
2069  C C   . GLY B 67  ? 2.215 1.827 1.840 0.007  0.088  0.344  66  GLY BBB C   
2070  O O   . GLY B 67  ? 2.287 1.833 1.849 0.041  0.094  0.360  66  GLY BBB O   
2071  N N   . GLN B 68  ? 2.145 1.817 1.826 -0.005 0.062  0.317  67  GLN BBB N   
2072  C CA  . GLN B 68  ? 2.164 1.839 1.841 0.021  0.036  0.302  67  GLN BBB CA  
2073  C C   . GLN B 68  ? 2.113 1.863 1.798 0.053  0.011  0.290  67  GLN BBB C   
2074  O O   . GLN B 68  ? 2.160 1.901 1.801 0.098  0.002  0.295  67  GLN BBB O   
2075  C CB  . GLN B 68  ? 2.131 1.818 1.859 -0.016 0.026  0.280  67  GLN BBB CB  
2076  C CG  . GLN B 68  ? 2.207 1.828 1.934 -0.054 0.051  0.285  67  GLN BBB CG  
2077  C CD  . GLN B 68  ? 2.314 1.845 1.987 -0.035 0.062  0.294  67  GLN BBB CD  
2078  O OE1 . GLN B 68  ? 2.332 1.858 2.007 -0.024 0.044  0.279  67  GLN BBB OE1 
2079  N NE2 . GLN B 68  ? 2.388 1.844 2.010 -0.031 0.092  0.320  67  GLN BBB NE2 
2080  N N   . VAL B 69  ? 2.020 1.840 1.756 0.032  0.003  0.275  68  VAL BBB N   
2081  C CA  . VAL B 69  ? 1.936 1.830 1.694 0.049  -0.020 0.255  68  VAL BBB CA  
2082  C C   . VAL B 69  ? 1.906 1.847 1.671 0.049  -0.013 0.259  68  VAL BBB C   
2083  O O   . VAL B 69  ? 1.886 1.818 1.663 0.023  0.006  0.271  68  VAL BBB O   
2084  C CB  . VAL B 69  ? 1.864 1.791 1.675 0.024  -0.035 0.231  68  VAL BBB CB  
2085  C CG1 . VAL B 69  ? 1.894 1.772 1.696 0.021  -0.040 0.227  68  VAL BBB CG1 
2086  C CG2 . VAL B 69  ? 1.824 1.775 1.680 -0.014 -0.027 0.230  68  VAL BBB CG2 
2087  N N   . THR B 70  ? 1.898 1.888 1.656 0.077  -0.027 0.246  69  THR BBB N   
2088  C CA  . THR B 70  ? 1.883 1.924 1.647 0.080  -0.023 0.242  69  THR BBB CA  
2089  C C   . THR B 70  ? 1.779 1.881 1.594 0.065  -0.036 0.215  69  THR BBB C   
2090  O O   . THR B 70  ? 1.737 1.860 1.559 0.076  -0.053 0.194  69  THR BBB O   
2091  C CB  . THR B 70  ? 1.941 1.992 1.653 0.123  -0.028 0.247  69  THR BBB CB  
2092  O OG1 . THR B 70  ? 2.038 2.024 1.697 0.135  -0.011 0.277  69  THR BBB OG1 
2093  C CG2 . THR B 70  ? 1.915 2.026 1.633 0.127  -0.027 0.236  69  THR BBB CG2 
2094  N N   . ILE B 71  ? 1.728 1.853 1.576 0.041  -0.025 0.215  70  ILE BBB N   
2095  C CA  . ILE B 71  ? 1.674 1.850 1.561 0.030  -0.030 0.192  70  ILE BBB CA  
2096  C C   . ILE B 71  ? 1.685 1.899 1.557 0.044  -0.024 0.186  70  ILE BBB C   
2097  O O   . ILE B 71  ? 1.712 1.920 1.576 0.039  -0.007 0.202  70  ILE BBB O   
2098  C CB  . ILE B 71  ? 1.655 1.833 1.585 -0.001 -0.023 0.195  70  ILE BBB CB  
2099  C CG1 . ILE B 71  ? 1.677 1.825 1.621 -0.016 -0.031 0.196  70  ILE BBB CG1 
2100  C CG2 . ILE B 71  ? 1.613 1.835 1.574 -0.007 -0.024 0.177  70  ILE BBB CG2 
2101  C CD1 . ILE B 71  ? 1.671 1.822 1.653 -0.045 -0.025 0.201  70  ILE BBB CD1 
2102  N N   . SER B 72  ? 1.683 1.935 1.552 0.060  -0.036 0.162  71  SER BBB N   
2103  C CA  . SER B 72  ? 1.675 1.972 1.533 0.072  -0.032 0.149  71  SER BBB CA  
2104  C C   . SER B 72  ? 1.616 1.948 1.513 0.054  -0.029 0.123  71  SER BBB C   
2105  O O   . SER B 72  ? 1.566 1.887 1.491 0.038  -0.032 0.117  71  SER BBB O   
2106  C CB  . SER B 72  ? 1.702 2.018 1.522 0.105  -0.046 0.138  71  SER BBB CB  
2107  O OG  . SER B 72  ? 1.711 2.016 1.532 0.114  -0.061 0.131  71  SER BBB OG  
2108  N N   . ALA B 73  ? 1.618 1.987 1.511 0.057  -0.020 0.108  72  ALA BBB N   
2109  C CA  . ALA B 73  ? 1.583 1.979 1.506 0.041  -0.012 0.082  72  ALA BBB CA  
2110  C C   . ALA B 73  ? 1.603 2.046 1.510 0.052  -0.010 0.056  72  ALA BBB C   
2111  O O   . ALA B 73  ? 1.644 2.095 1.529 0.060  -0.001 0.066  72  ALA BBB O   
2112  C CB  . ALA B 73  ? 1.569 1.950 1.516 0.023  0.004  0.096  72  ALA BBB CB  
2113  N N   . ASP B 74  ? 1.588 2.061 1.504 0.051  -0.017 0.023  73  ASP BBB N   
2114  C CA  . ASP B 74  ? 1.632 2.157 1.543 0.053  -0.012 -0.013 73  ASP BBB CA  
2115  C C   . ASP B 74  ? 1.603 2.124 1.542 0.026  0.009  -0.029 73  ASP BBB C   
2116  O O   . ASP B 74  ? 1.591 2.115 1.549 0.012  0.012  -0.054 73  ASP BBB O   
2117  C CB  . ASP B 74  ? 1.688 2.252 1.597 0.064  -0.030 -0.042 73  ASP BBB CB  
2118  C CG  . ASP B 74  ? 1.763 2.392 1.660 0.073  -0.032 -0.078 73  ASP BBB CG  
2119  O OD1 . ASP B 74  ? 1.836 2.477 1.725 0.069  -0.018 -0.081 73  ASP BBB OD1 
2120  O OD2 . ASP B 74  ? 1.796 2.468 1.694 0.086  -0.048 -0.104 73  ASP BBB OD2 
2121  N N   . LYS B 75  ? 1.616 2.126 1.554 0.021  0.026  -0.015 74  LYS BBB N   
2122  C CA  . LYS B 75  ? 1.600 2.095 1.562 0.002  0.049  -0.024 74  LYS BBB CA  
2123  C C   . LYS B 75  ? 1.573 2.097 1.539 -0.011 0.060  -0.068 74  LYS BBB C   
2124  O O   . LYS B 75  ? 1.574 2.075 1.558 -0.028 0.079  -0.079 74  LYS BBB O   
2125  C CB  . LYS B 75  ? 1.636 2.125 1.593 0.003  0.064  -0.004 74  LYS BBB CB  
2126  C CG  . LYS B 75  ? 1.693 2.219 1.622 0.014  0.069  -0.018 74  LYS BBB CG  
2127  C CD  . LYS B 75  ? 1.744 2.262 1.670 0.013  0.088  -0.001 74  LYS BBB CD  
2128  C CE  . LYS B 75  ? 1.805 2.361 1.702 0.021  0.095  -0.022 74  LYS BBB CE  
2129  N NZ  . LYS B 75  ? 1.842 2.390 1.737 0.018  0.119  -0.010 74  LYS BBB NZ  
2130  N N   . SER B 76  ? 1.547 2.121 1.498 -0.001 0.050  -0.095 75  SER BBB N   
2131  C CA  . SER B 76  ? 1.532 2.146 1.487 -0.015 0.061  -0.144 75  SER BBB CA  
2132  C C   . SER B 76  ? 1.490 2.101 1.467 -0.032 0.062  -0.169 75  SER BBB C   
2133  O O   . SER B 76  ? 1.490 2.129 1.475 -0.049 0.076  -0.212 75  SER BBB O   
2134  C CB  . SER B 76  ? 1.569 2.246 1.501 0.003  0.045  -0.165 75  SER BBB CB  
2135  O OG  . SER B 76  ? 1.563 2.271 1.498 0.014  0.023  -0.179 75  SER BBB OG  
2136  N N   . ILE B 77  ? 1.457 2.035 1.441 -0.027 0.049  -0.144 76  ILE BBB N   
2137  C CA  . ILE B 77  ? 1.442 2.006 1.444 -0.044 0.053  -0.162 76  ILE BBB CA  
2138  C C   . ILE B 77  ? 1.392 1.892 1.400 -0.047 0.054  -0.125 76  ILE BBB C   
2139  O O   . ILE B 77  ? 1.345 1.828 1.360 -0.053 0.050  -0.128 76  ILE BBB O   
2140  C CB  . ILE B 77  ? 1.468 2.074 1.470 -0.033 0.030  -0.181 76  ILE BBB CB  
2141  C CG1 . ILE B 77  ? 1.473 2.079 1.458 -0.003 0.003  -0.147 76  ILE BBB CG1 
2142  C CG2 . ILE B 77  ? 1.495 2.171 1.500 -0.038 0.034  -0.231 76  ILE BBB CG2 
2143  C CD1 . ILE B 77  ? 1.475 2.103 1.462 0.010  -0.018 -0.157 76  ILE BBB CD1 
2144  N N   . ASN B 78  ? 1.385 1.856 1.391 -0.043 0.061  -0.095 77  ASN BBB N   
2145  C CA  . ASN B 78  ? 1.387 1.808 1.402 -0.045 0.062  -0.062 77  ASN BBB CA  
2146  C C   . ASN B 78  ? 1.399 1.812 1.414 -0.038 0.038  -0.047 77  ASN BBB C   
2147  O O   . ASN B 78  ? 1.509 1.888 1.530 -0.045 0.038  -0.040 77  ASN BBB O   
2148  C CB  . ASN B 78  ? 1.391 1.778 1.413 -0.061 0.085  -0.075 77  ASN BBB CB  
2149  C CG  . ASN B 78  ? 1.408 1.787 1.430 -0.066 0.111  -0.081 77  ASN BBB CG  
2150  O OD1 . ASN B 78  ? 1.439 1.785 1.460 -0.077 0.134  -0.093 77  ASN BBB OD1 
2151  N ND2 . ASN B 78  ? 1.396 1.800 1.415 -0.056 0.109  -0.073 77  ASN BBB ND2 
2152  N N   . THR B 79  ? 1.352 1.790 1.355 -0.022 0.019  -0.043 78  THR BBB N   
2153  C CA  . THR B 79  ? 1.324 1.753 1.323 -0.013 -0.002 -0.032 78  THR BBB CA  
2154  C C   . THR B 79  ? 1.333 1.744 1.321 0.001  -0.013 0.005  78  THR BBB C   
2155  O O   . THR B 79  ? 1.361 1.793 1.330 0.016  -0.016 0.009  78  THR BBB O   
2156  C CB  . THR B 79  ? 1.328 1.798 1.321 -0.004 -0.013 -0.061 78  THR BBB CB  
2157  O OG1 . THR B 79  ? 1.305 1.792 1.311 -0.023 0.002  -0.098 78  THR BBB OG1 
2158  C CG2 . THR B 79  ? 1.337 1.794 1.326 0.007  -0.033 -0.051 78  THR BBB CG2 
2159  N N   . ALA B 80  ? 1.338 1.712 1.335 -0.005 -0.018 0.029  79  ALA BBB N   
2160  C CA  . ALA B 80  ? 1.377 1.728 1.365 0.003  -0.028 0.060  79  ALA BBB CA  
2161  C C   . ALA B 80  ? 1.409 1.751 1.386 0.013  -0.045 0.057  79  ALA BBB C   
2162  O O   . ALA B 80  ? 1.390 1.734 1.376 0.007  -0.049 0.038  79  ALA BBB O   
2163  C CB  . ALA B 80  ? 1.363 1.688 1.371 -0.011 -0.023 0.081  79  ALA BBB CB  
2164  N N   . TYR B 81  ? 1.465 1.796 1.419 0.029  -0.052 0.076  80  TYR BBB N   
2165  C CA  . TYR B 81  ? 1.509 1.826 1.446 0.045  -0.067 0.077  80  TYR BBB CA  
2166  C C   . TYR B 81  ? 1.543 1.811 1.472 0.041  -0.068 0.107  80  TYR BBB C   
2167  O O   . TYR B 81  ? 1.538 1.792 1.469 0.031  -0.057 0.127  80  TYR BBB O   
2168  C CB  . TYR B 81  ? 1.545 1.888 1.451 0.074  -0.074 0.071  80  TYR BBB CB  
2169  C CG  . TYR B 81  ? 1.533 1.934 1.446 0.078  -0.074 0.036  80  TYR BBB CG  
2170  C CD1 . TYR B 81  ? 1.516 1.940 1.449 0.071  -0.079 0.006  80  TYR BBB CD1 
2171  C CD2 . TYR B 81  ? 1.561 1.995 1.462 0.086  -0.069 0.031  80  TYR BBB CD2 
2172  C CE1 . TYR B 81  ? 1.525 2.005 1.467 0.070  -0.076 -0.031 80  TYR BBB CE1 
2173  C CE2 . TYR B 81  ? 1.562 2.053 1.470 0.087  -0.068 -0.006 80  TYR BBB CE2 
2174  C CZ  . TYR B 81  ? 1.540 2.055 1.471 0.077  -0.071 -0.038 80  TYR BBB CZ  
2175  O OH  . TYR B 81  ? 1.533 2.106 1.475 0.073  -0.068 -0.078 80  TYR BBB OH  
2176  N N   . LEU B 82  ? 1.578 1.820 1.497 0.048  -0.079 0.108  81  LEU BBB N   
2177  C CA  . LEU B 82  ? 1.604 1.795 1.508 0.048  -0.079 0.132  81  LEU BBB CA  
2178  C C   . LEU B 82  ? 1.627 1.805 1.499 0.078  -0.090 0.130  81  LEU BBB C   
2179  O O   . LEU B 82  ? 1.609 1.811 1.490 0.085  -0.100 0.106  81  LEU BBB O   
2180  C CB  . LEU B 82  ? 1.579 1.749 1.509 0.022  -0.082 0.131  81  LEU BBB CB  
2181  C CG  . LEU B 82  ? 1.618 1.736 1.536 0.017  -0.082 0.147  81  LEU BBB CG  
2182  C CD1 . LEU B 82  ? 1.663 1.757 1.577 0.006  -0.068 0.172  81  LEU BBB CD1 
2183  C CD2 . LEU B 82  ? 1.585 1.692 1.526 -0.004 -0.090 0.138  81  LEU BBB CD2 
2184  N N   . GLN B 83  ? 1.675 1.817 1.511 0.096  -0.086 0.153  82  GLN BBB N   
2185  C CA  . GLN B 83  ? 1.732 1.860 1.532 0.132  -0.096 0.153  82  GLN BBB CA  
2186  C C   . GLN B 83  ? 1.769 1.820 1.537 0.135  -0.087 0.180  82  GLN BBB C   
2187  O O   . GLN B 83  ? 1.790 1.808 1.563 0.109  -0.072 0.199  82  GLN BBB O   
2188  C CB  . GLN B 83  ? 1.788 1.955 1.559 0.165  -0.100 0.150  82  GLN BBB CB  
2189  C CG  . GLN B 83  ? 1.818 1.989 1.579 0.158  -0.085 0.167  82  GLN BBB CG  
2190  C CD  . GLN B 83  ? 1.870 2.074 1.592 0.196  -0.091 0.165  82  GLN BBB CD  
2191  O OE1 . GLN B 83  ? 1.900 2.090 1.584 0.233  -0.100 0.172  82  GLN BBB OE1 
2192  N NE2 . GLN B 83  ? 1.877 2.127 1.608 0.188  -0.086 0.156  82  GLN BBB NE2 
2193  N N   . TRP B 84  ? 1.779 1.806 1.518 0.166  -0.096 0.180  83  TRP BBB N   
2194  C CA  . TRP B 84  ? 1.831 1.776 1.534 0.175  -0.086 0.202  83  TRP BBB CA  
2195  C C   . TRP B 84  ? 1.901 1.827 1.546 0.226  -0.089 0.217  83  TRP BBB C   
2196  O O   . TRP B 84  ? 1.888 1.860 1.530 0.260  -0.107 0.198  83  TRP BBB O   
2197  C CB  . TRP B 84  ? 1.804 1.728 1.526 0.164  -0.094 0.187  83  TRP BBB CB  
2198  C CG  . TRP B 84  ? 1.751 1.665 1.512 0.115  -0.088 0.184  83  TRP BBB CG  
2199  C CD1 . TRP B 84  ? 1.788 1.644 1.545 0.088  -0.072 0.200  83  TRP BBB CD1 
2200  C CD2 . TRP B 84  ? 1.665 1.631 1.473 0.089  -0.096 0.161  83  TRP BBB CD2 
2201  N NE1 . TRP B 84  ? 1.737 1.614 1.538 0.049  -0.074 0.188  83  TRP BBB NE1 
2202  C CE2 . TRP B 84  ? 1.665 1.605 1.495 0.051  -0.089 0.167  83  TRP BBB CE2 
2203  C CE3 . TRP B 84  ? 1.615 1.645 1.447 0.094  -0.108 0.136  83  TRP BBB CE3 
2204  C CZ2 . TRP B 84  ? 1.617 1.592 1.487 0.024  -0.095 0.151  83  TRP BBB CZ2 
2205  C CZ3 . TRP B 84  ? 1.568 1.624 1.438 0.064  -0.110 0.121  83  TRP BBB CZ3 
2206  C CH2 . TRP B 84  ? 1.573 1.601 1.459 0.032  -0.105 0.130  83  TRP BBB CH2 
2207  N N   . SER B 85  ? 1.982 1.842 1.582 0.232  -0.069 0.249  84  SER BBB N   
2208  C CA  . SER B 85  ? 2.087 1.904 1.617 0.283  -0.066 0.272  84  SER BBB CA  
2209  C C   . SER B 85  ? 2.116 1.903 1.628 0.315  -0.077 0.265  84  SER BBB C   
2210  O O   . SER B 85  ? 2.143 1.948 1.618 0.369  -0.091 0.266  84  SER BBB O   
2211  C CB  . SER B 85  ? 2.182 1.915 1.670 0.270  -0.036 0.308  84  SER BBB CB  
2212  O OG  . SER B 85  ? 2.139 1.887 1.669 0.218  -0.022 0.307  84  SER BBB OG  
2213  N N   . SER B 86  ? 2.128 1.875 1.665 0.285  -0.072 0.258  85  SER BBB N   
2214  C CA  . SER B 86  ? 2.189 1.894 1.711 0.308  -0.077 0.252  85  SER BBB CA  
2215  C C   . SER B 86  ? 2.169 1.851 1.734 0.257  -0.072 0.238  85  SER BBB C   
2216  O O   . SER B 86  ? 2.211 1.844 1.779 0.218  -0.052 0.252  85  SER BBB O   
2217  C CB  . SER B 86  ? 2.324 1.935 1.772 0.346  -0.061 0.284  85  SER BBB CB  
2218  O OG  . SER B 86  ? 2.385 1.949 1.818 0.367  -0.063 0.277  85  SER BBB OG  
2219  N N   . LEU B 87  ? 2.157 1.877 1.755 0.258  -0.089 0.209  86  LEU BBB N   
2220  C CA  . LEU B 87  ? 2.157 1.882 1.802 0.210  -0.090 0.189  86  LEU BBB CA  
2221  C C   . LEU B 87  ? 2.235 1.872 1.859 0.200  -0.076 0.194  86  LEU BBB C   
2222  O O   . LEU B 87  ? 2.307 1.912 1.901 0.239  -0.079 0.193  86  LEU BBB O   
2223  C CB  . LEU B 87  ? 2.120 1.923 1.804 0.216  -0.110 0.155  86  LEU BBB CB  
2224  C CG  . LEU B 87  ? 2.066 1.955 1.788 0.201  -0.119 0.141  86  LEU BBB CG  
2225  C CD1 . LEU B 87  ? 2.029 1.987 1.778 0.214  -0.135 0.107  86  LEU BBB CD1 
2226  C CD2 . LEU B 87  ? 2.030 1.920 1.787 0.148  -0.112 0.142  86  LEU BBB CD2 
2227  N N   . LYS B 88  ? 2.235 1.839 1.878 0.151  -0.063 0.197  87  LYS BBB N   
2228  C CA  . LYS B 88  ? 2.278 1.812 1.915 0.128  -0.052 0.192  87  LYS BBB CA  
2229  C C   . LYS B 88  ? 2.205 1.783 1.880 0.115  -0.070 0.160  87  LYS BBB C   
2230  O O   . LYS B 88  ? 2.093 1.751 1.807 0.106  -0.086 0.145  87  LYS BBB O   
2231  C CB  . LYS B 88  ? 2.309 1.808 1.959 0.077  -0.033 0.201  87  LYS BBB CB  
2232  C CG  . LYS B 88  ? 2.384 1.831 1.996 0.080  -0.009 0.232  87  LYS BBB CG  
2233  C CD  . LYS B 88  ? 2.438 1.833 2.059 0.028  0.015  0.236  87  LYS BBB CD  
2234  C CE  . LYS B 88  ? 2.551 1.863 2.120 0.033  0.048  0.266  87  LYS BBB CE  
2235  N NZ  . LYS B 88  ? 2.542 1.895 2.121 0.024  0.054  0.282  87  LYS BBB NZ  
2236  N N   . ALA B 89  ? 2.255 1.778 1.918 0.111  -0.066 0.150  88  ALA BBB N   
2237  C CA  . ALA B 89  ? 2.205 1.753 1.900 0.086  -0.077 0.121  88  ALA BBB CA  
2238  C C   . ALA B 89  ? 2.147 1.732 1.883 0.035  -0.079 0.116  88  ALA BBB C   
2239  O O   . ALA B 89  ? 2.081 1.732 1.849 0.025  -0.095 0.100  88  ALA BBB O   
2240  C CB  . ALA B 89  ? 2.277 1.746 1.947 0.084  -0.065 0.114  88  ALA BBB CB  
2241  N N   . SER B 90  ? 2.201 1.744 1.933 0.005  -0.062 0.131  89  SER BBB N   
2242  C CA  . SER B 90  ? 2.169 1.748 1.941 -0.042 -0.063 0.128  89  SER BBB CA  
2243  C C   . SER B 90  ? 2.092 1.757 1.896 -0.038 -0.080 0.125  89  SER BBB C   
2244  O O   . SER B 90  ? 2.069 1.779 1.907 -0.064 -0.091 0.110  89  SER BBB O   
2245  C CB  . SER B 90  ? 2.225 1.759 1.987 -0.065 -0.040 0.147  89  SER BBB CB  
2246  O OG  . SER B 90  ? 2.197 1.768 1.965 -0.056 -0.038 0.166  89  SER BBB OG  
2247  N N   . ASP B 91  ? 2.073 1.759 1.864 -0.005 -0.080 0.139  90  ASP BBB N   
2248  C CA  . ASP B 91  ? 2.003 1.766 1.820 -0.001 -0.091 0.137  90  ASP BBB CA  
2249  C C   . ASP B 91  ? 1.946 1.756 1.783 0.003  -0.108 0.112  90  ASP BBB C   
2250  O O   . ASP B 91  ? 1.873 1.743 1.732 0.004  -0.114 0.107  90  ASP BBB O   
2251  C CB  . ASP B 91  ? 2.018 1.788 1.810 0.035  -0.086 0.154  90  ASP BBB CB  
2252  C CG  . ASP B 91  ? 2.077 1.806 1.850 0.027  -0.067 0.180  90  ASP BBB CG  
2253  O OD1 . ASP B 91  ? 2.083 1.811 1.880 -0.011 -0.058 0.183  90  ASP BBB OD1 
2254  O OD2 . ASP B 91  ? 2.114 1.814 1.846 0.061  -0.059 0.197  90  ASP BBB OD2 
2255  N N   . THR B 92  ? 1.968 1.752 1.798 0.004  -0.112 0.096  91  THR BBB N   
2256  C CA  . THR B 92  ? 1.906 1.726 1.754 -0.004 -0.124 0.072  91  THR BBB CA  
2257  C C   . THR B 92  ? 1.807 1.654 1.684 -0.040 -0.128 0.069  91  THR BBB C   
2258  O O   . THR B 92  ? 1.779 1.595 1.658 -0.067 -0.124 0.073  91  THR BBB O   
2259  C CB  . THR B 92  ? 1.976 1.757 1.808 -0.001 -0.125 0.056  91  THR BBB CB  
2260  O OG1 . THR B 92  ? 2.062 1.824 1.869 0.039  -0.122 0.056  91  THR BBB OG1 
2261  C CG2 . THR B 92  ? 1.936 1.752 1.784 -0.012 -0.134 0.032  91  THR BBB CG2 
2262  N N   . ALA B 93  ? 1.747 1.646 1.642 -0.041 -0.134 0.062  92  ALA BBB N   
2263  C CA  . ALA B 93  ? 1.729 1.659 1.648 -0.066 -0.139 0.062  92  ALA BBB CA  
2264  C C   . ALA B 93  ? 1.678 1.656 1.608 -0.057 -0.140 0.054  92  ALA BBB C   
2265  O O   . ALA B 93  ? 1.656 1.648 1.579 -0.034 -0.138 0.047  92  ALA BBB O   
2266  C CB  . ALA B 93  ? 1.728 1.657 1.659 -0.080 -0.132 0.082  92  ALA BBB CB  
2267  N N   . ILE B 94  ? 1.642 1.644 1.588 -0.073 -0.144 0.055  93  ILE BBB N   
2268  C CA  . ILE B 94  ? 1.587 1.627 1.542 -0.068 -0.140 0.051  93  ILE BBB CA  
2269  C C   . ILE B 94  ? 1.542 1.600 1.514 -0.072 -0.136 0.069  93  ILE BBB C   
2270  O O   . ILE B 94  ? 1.565 1.616 1.548 -0.087 -0.139 0.079  93  ILE BBB O   
2271  C CB  . ILE B 94  ? 1.606 1.651 1.559 -0.079 -0.143 0.039  93  ILE BBB CB  
2272  C CG1 . ILE B 94  ? 1.611 1.684 1.570 -0.076 -0.135 0.038  93  ILE BBB CG1 
2273  C CG2 . ILE B 94  ? 1.621 1.656 1.577 -0.097 -0.153 0.045  93  ILE BBB CG2 
2274  C CD1 . ILE B 94  ? 1.642 1.713 1.588 -0.080 -0.131 0.023  93  ILE BBB CD1 
2275  N N   . TYR B 95  ? 1.475 1.558 1.450 -0.059 -0.128 0.069  94  TYR BBB N   
2276  C CA  . TYR B 95  ? 1.430 1.531 1.417 -0.059 -0.121 0.084  94  TYR BBB CA  
2277  C C   . TYR B 95  ? 1.364 1.493 1.362 -0.060 -0.116 0.079  94  TYR BBB C   
2278  O O   . TYR B 95  ? 1.356 1.500 1.349 -0.052 -0.110 0.064  94  TYR BBB O   
2279  C CB  . TYR B 95  ? 1.441 1.541 1.415 -0.040 -0.116 0.089  94  TYR BBB CB  
2280  C CG  . TYR B 95  ? 1.474 1.534 1.432 -0.037 -0.118 0.099  94  TYR BBB CG  
2281  C CD1 . TYR B 95  ? 1.491 1.531 1.451 -0.048 -0.111 0.118  94  TYR BBB CD1 
2282  C CD2 . TYR B 95  ? 1.495 1.534 1.434 -0.023 -0.123 0.089  94  TYR BBB CD2 
2283  C CE1 . TYR B 95  ? 1.540 1.534 1.481 -0.048 -0.108 0.127  94  TYR BBB CE1 
2284  C CE2 . TYR B 95  ? 1.539 1.532 1.459 -0.019 -0.121 0.098  94  TYR BBB CE2 
2285  C CZ  . TYR B 95  ? 1.566 1.532 1.484 -0.032 -0.112 0.118  94  TYR BBB CZ  
2286  O OH  . TYR B 95  ? 1.632 1.543 1.527 -0.031 -0.106 0.127  94  TYR BBB OH  
2287  N N   . TYR B 96  ? 1.343 1.480 1.357 -0.071 -0.116 0.089  95  TYR BBB N   
2288  C CA  . TYR B 96  ? 1.353 1.509 1.375 -0.070 -0.108 0.088  95  TYR BBB CA  
2289  C C   . TYR B 96  ? 1.348 1.525 1.382 -0.065 -0.098 0.099  95  TYR BBB C   
2290  O O   . TYR B 96  ? 1.381 1.558 1.426 -0.070 -0.099 0.113  95  TYR BBB O   
2291  C CB  . TYR B 96  ? 1.378 1.534 1.408 -0.078 -0.116 0.095  95  TYR BBB CB  
2292  C CG  . TYR B 96  ? 1.432 1.569 1.446 -0.083 -0.126 0.085  95  TYR BBB CG  
2293  C CD1 . TYR B 96  ? 1.464 1.591 1.458 -0.079 -0.120 0.073  95  TYR BBB CD1 
2294  C CD2 . TYR B 96  ? 1.454 1.582 1.471 -0.093 -0.140 0.087  95  TYR BBB CD2 
2295  C CE1 . TYR B 96  ? 1.478 1.585 1.453 -0.083 -0.127 0.064  95  TYR BBB CE1 
2296  C CE2 . TYR B 96  ? 1.471 1.583 1.470 -0.098 -0.149 0.077  95  TYR BBB CE2 
2297  C CZ  . TYR B 96  ? 1.488 1.589 1.465 -0.091 -0.143 0.067  95  TYR BBB CZ  
2298  O OH  . TYR B 96  ? 1.542 1.625 1.497 -0.095 -0.150 0.057  95  TYR BBB OH  
2299  N N   . CYS B 97  ? 1.350 1.541 1.381 -0.058 -0.086 0.090  96  CYS BBB N   
2300  C CA  . CYS B 97  ? 1.365 1.576 1.408 -0.054 -0.074 0.098  96  CYS BBB CA  
2301  C C   . CYS B 97  ? 1.393 1.608 1.447 -0.056 -0.069 0.102  96  CYS BBB C   
2302  O O   . CYS B 97  ? 1.443 1.644 1.486 -0.057 -0.068 0.092  96  CYS BBB O   
2303  C CB  . CYS B 97  ? 1.353 1.581 1.386 -0.045 -0.064 0.083  96  CYS BBB CB  
2304  S SG  . CYS B 97  ? 1.335 1.567 1.364 -0.048 -0.048 0.061  96  CYS BBB SG  
2305  N N   . ALA B 98  ? 1.405 1.635 1.478 -0.056 -0.066 0.116  97  ALA BBB N   
2306  C CA  . ALA B 98  ? 1.424 1.660 1.510 -0.053 -0.064 0.123  97  ALA BBB CA  
2307  C C   . ALA B 98  ? 1.439 1.696 1.542 -0.047 -0.049 0.130  97  ALA BBB C   
2308  O O   . ALA B 98  ? 1.480 1.755 1.601 -0.052 -0.049 0.140  97  ALA BBB O   
2309  C CB  . ALA B 98  ? 1.438 1.679 1.539 -0.059 -0.081 0.132  97  ALA BBB CB  
2310  N N   . GLY B 99  ? 1.442 1.695 1.539 -0.039 -0.035 0.124  98  GLY BBB N   
2311  C CA  . GLY B 99  ? 1.451 1.720 1.561 -0.031 -0.018 0.128  98  GLY BBB CA  
2312  C C   . GLY B 99  ? 1.449 1.732 1.581 -0.022 -0.021 0.141  98  GLY BBB C   
2313  O O   . GLY B 99  ? 1.428 1.696 1.551 -0.015 -0.028 0.143  98  GLY BBB O   
2314  N N   . GLY B 100 ? 1.452 1.764 1.610 -0.020 -0.014 0.149  99  GLY BBB N   
2315  C CA  . GLY B 100 ? 1.468 1.797 1.646 -0.005 -0.007 0.156  99  GLY BBB CA  
2316  C C   . GLY B 100 ? 1.469 1.797 1.644 0.001  0.019  0.151  99  GLY BBB C   
2317  O O   . GLY B 100 ? 1.458 1.786 1.622 -0.009 0.026  0.145  99  GLY BBB O   
2318  N N   . SER B 101 ? 1.486 1.812 1.665 0.019  0.031  0.153  100 SER BBB N   
2319  C CA  . SER B 101 ? 1.506 1.834 1.687 0.026  0.057  0.148  100 SER BBB CA  
2320  C C   . SER B 101 ? 1.472 1.847 1.692 0.027  0.059  0.158  100 SER BBB C   
2321  O O   . SER B 101 ? 1.494 1.888 1.737 0.045  0.059  0.165  100 SER BBB O   
2322  C CB  . SER B 101 ? 1.574 1.870 1.738 0.046  0.074  0.146  100 SER BBB CB  
2323  O OG  . SER B 101 ? 1.642 1.942 1.816 0.065  0.060  0.159  100 SER BBB OG  
2324  N N   . GLY B 102 ? 1.460 1.852 1.685 0.010  0.059  0.158  101 GLY BBB N   
2325  C CA  . GLY B 102 ? 1.464 1.897 1.723 0.005  0.063  0.167  101 GLY BBB CA  
2326  C C   . GLY B 102 ? 1.459 1.906 1.734 -0.012 0.043  0.174  101 GLY BBB C   
2327  O O   . GLY B 102 ? 1.459 1.889 1.722 -0.015 0.024  0.173  101 GLY BBB O   
2328  N N   . ILE B 103 ? 1.483 1.958 1.781 -0.025 0.051  0.180  102 ILE BBB N   
2329  C CA  . ILE B 103 ? 1.512 2.000 1.827 -0.046 0.039  0.185  102 ILE BBB CA  
2330  C C   . ILE B 103 ? 1.499 2.035 1.864 -0.045 0.031  0.186  102 ILE BBB C   
2331  O O   . ILE B 103 ? 1.534 2.095 1.919 -0.025 0.039  0.184  102 ILE BBB O   
2332  C CB  . ILE B 103 ? 1.572 2.055 1.877 -0.062 0.058  0.191  102 ILE BBB CB  
2333  C CG1 . ILE B 103 ? 1.628 2.099 1.933 -0.086 0.050  0.196  102 ILE BBB CG1 
2334  C CG2 . ILE B 103 ? 1.585 2.105 1.920 -0.061 0.080  0.193  102 ILE BBB CG2 
2335  C CD1 . ILE B 103 ? 1.650 2.085 1.926 -0.087 0.028  0.194  102 ILE BBB CD1 
2336  N N   . SER B 104 ? 1.470 2.020 1.855 -0.064 0.017  0.185  103 SER BBB N   
2337  C CA  . SER B 104 ? 1.447 2.047 1.877 -0.062 0.001  0.180  103 SER BBB CA  
2338  C C   . SER B 104 ? 1.461 2.058 1.881 -0.031 -0.014 0.179  103 SER BBB C   
2339  O O   . SER B 104 ? 1.422 2.062 1.874 -0.010 -0.015 0.179  103 SER BBB O   
2340  C CB  . SER B 104 ? 1.424 2.082 1.905 -0.069 0.016  0.178  103 SER BBB CB  
2341  O OG  . SER B 104 ? 1.414 2.093 1.922 -0.102 0.015  0.173  103 SER BBB OG  
2342  N N   . THR B 105 ? 1.501 2.047 1.876 -0.027 -0.023 0.180  104 THR BBB N   
2343  C CA  . THR B 105 ? 1.525 2.049 1.875 -0.001 -0.033 0.180  104 THR BBB CA  
2344  C C   . THR B 105 ? 1.518 2.015 1.844 -0.010 -0.055 0.177  104 THR BBB C   
2345  O O   . THR B 105 ? 1.486 1.956 1.794 -0.031 -0.057 0.175  104 THR BBB O   
2346  C CB  . THR B 105 ? 1.567 2.048 1.882 0.013  -0.012 0.180  104 THR BBB CB  
2347  O OG1 . THR B 105 ? 1.628 2.107 1.940 0.043  -0.009 0.183  104 THR BBB OG1 
2348  C CG2 . THR B 105 ? 1.595 2.024 1.865 0.004  -0.014 0.176  104 THR BBB CG2 
2349  N N   . PRO B 106 ? 1.549 2.050 1.868 0.010  -0.073 0.178  105 PRO BBB N   
2350  C CA  . PRO B 106 ? 1.554 2.029 1.846 0.003  -0.093 0.174  105 PRO BBB CA  
2351  C C   . PRO B 106 ? 1.535 1.948 1.780 0.002  -0.081 0.173  105 PRO BBB C   
2352  O O   . PRO B 106 ? 1.504 1.898 1.734 0.018  -0.062 0.175  105 PRO BBB O   
2353  C CB  . PRO B 106 ? 1.605 2.097 1.895 0.031  -0.110 0.177  105 PRO BBB CB  
2354  C CG  . PRO B 106 ? 1.630 2.126 1.925 0.060  -0.091 0.185  105 PRO BBB CG  
2355  C CD  . PRO B 106 ? 1.600 2.121 1.929 0.043  -0.072 0.183  105 PRO BBB CD  
2356  N N   . MET B 107 ? 1.551 1.938 1.776 -0.017 -0.089 0.167  106 MET BBB N   
2357  C CA  . MET B 107 ? 1.576 1.913 1.759 -0.019 -0.080 0.162  106 MET BBB CA  
2358  C C   . MET B 107 ? 1.547 1.855 1.699 -0.001 -0.082 0.162  106 MET BBB C   
2359  O O   . MET B 107 ? 1.506 1.808 1.645 -0.001 -0.100 0.161  106 MET BBB O   
2360  C CB  . MET B 107 ? 1.598 1.920 1.772 -0.041 -0.090 0.156  106 MET BBB CB  
2361  C CG  . MET B 107 ? 1.611 1.945 1.803 -0.056 -0.081 0.159  106 MET BBB CG  
2362  S SD  . MET B 107 ? 1.628 1.958 1.826 -0.080 -0.094 0.156  106 MET BBB SD  
2363  C CE  . MET B 107 ? 1.630 1.949 1.823 -0.087 -0.074 0.162  106 MET BBB CE  
2364  N N   . ASP B 108 ? 1.553 1.841 1.690 0.015  -0.061 0.163  107 ASP BBB N   
2365  C CA  . ASP B 108 ? 1.587 1.839 1.689 0.037  -0.056 0.166  107 ASP BBB CA  
2366  C C   . ASP B 108 ? 1.531 1.732 1.593 0.027  -0.041 0.155  107 ASP BBB C   
2367  O O   . ASP B 108 ? 1.587 1.749 1.614 0.041  -0.032 0.156  107 ASP BBB O   
2368  C CB  . ASP B 108 ? 1.682 1.939 1.792 0.062  -0.039 0.174  107 ASP BBB CB  
2369  C CG  . ASP B 108 ? 1.731 1.987 1.852 0.058  -0.013 0.169  107 ASP BBB CG  
2370  O OD1 . ASP B 108 ? 1.746 2.045 1.904 0.051  -0.015 0.171  107 ASP BBB OD1 
2371  O OD2 . ASP B 108 ? 1.765 1.977 1.855 0.061  0.011  0.162  107 ASP BBB OD2 
2372  N N   . VAL B 109 ? 1.446 1.648 1.510 0.005  -0.039 0.143  108 VAL BBB N   
2373  C CA  . VAL B 109 ? 1.410 1.576 1.444 -0.006 -0.026 0.127  108 VAL BBB CA  
2374  C C   . VAL B 109 ? 1.354 1.533 1.394 -0.024 -0.041 0.118  108 VAL BBB C   
2375  O O   . VAL B 109 ? 1.341 1.548 1.405 -0.030 -0.046 0.121  108 VAL BBB O   
2376  C CB  . VAL B 109 ? 1.402 1.557 1.431 -0.007 0.002  0.116  108 VAL BBB CB  
2377  C CG1 . VAL B 109 ? 1.395 1.585 1.454 -0.004 0.006  0.121  108 VAL BBB CG1 
2378  C CG2 . VAL B 109 ? 1.388 1.531 1.401 -0.024 0.012  0.094  108 VAL BBB CG2 
2379  N N   . TRP B 110 ? 1.327 1.482 1.343 -0.031 -0.045 0.109  109 TRP BBB N   
2380  C CA  . TRP B 110 ? 1.306 1.466 1.323 -0.044 -0.060 0.101  109 TRP BBB CA  
2381  C C   . TRP B 110 ? 1.310 1.452 1.307 -0.051 -0.047 0.081  109 TRP BBB C   
2382  O O   . TRP B 110 ? 1.330 1.444 1.303 -0.051 -0.034 0.074  109 TRP BBB O   
2383  C CB  . TRP B 110 ? 1.325 1.481 1.338 -0.045 -0.082 0.108  109 TRP BBB CB  
2384  C CG  . TRP B 110 ? 1.327 1.513 1.369 -0.043 -0.098 0.121  109 TRP BBB CG  
2385  C CD1 . TRP B 110 ? 1.359 1.562 1.413 -0.030 -0.099 0.133  109 TRP BBB CD1 
2386  C CD2 . TRP B 110 ? 1.309 1.514 1.372 -0.056 -0.113 0.123  109 TRP BBB CD2 
2387  N NE1 . TRP B 110 ? 1.349 1.588 1.435 -0.035 -0.115 0.140  109 TRP BBB NE1 
2388  C CE2 . TRP B 110 ? 1.314 1.551 1.405 -0.054 -0.121 0.133  109 TRP BBB CE2 
2389  C CE3 . TRP B 110 ? 1.305 1.500 1.364 -0.068 -0.117 0.116  109 TRP BBB CE3 
2390  C CZ2 . TRP B 110 ? 1.296 1.555 1.414 -0.068 -0.132 0.135  109 TRP BBB CZ2 
2391  C CZ3 . TRP B 110 ? 1.305 1.513 1.385 -0.080 -0.127 0.121  109 TRP BBB CZ3 
2392  C CH2 . TRP B 110 ? 1.300 1.539 1.409 -0.083 -0.134 0.129  109 TRP BBB CH2 
2393  N N   . GLY B 111 ? 1.332 1.489 1.336 -0.057 -0.051 0.071  110 GLY BBB N   
2394  C CA  . GLY B 111 ? 1.385 1.537 1.376 -0.064 -0.045 0.048  110 GLY BBB CA  
2395  C C   . GLY B 111 ? 1.429 1.563 1.406 -0.067 -0.059 0.047  110 GLY BBB C   
2396  O O   . GLY B 111 ? 1.436 1.570 1.420 -0.067 -0.076 0.062  110 GLY BBB O   
2397  N N   . GLN B 112 ? 1.468 1.590 1.429 -0.073 -0.050 0.027  111 GLN BBB N   
2398  C CA  . GLN B 112 ? 1.487 1.588 1.431 -0.077 -0.060 0.024  111 GLN BBB CA  
2399  C C   . GLN B 112 ? 1.470 1.582 1.425 -0.076 -0.080 0.026  111 GLN BBB C   
2400  O O   . GLN B 112 ? 1.503 1.599 1.447 -0.079 -0.092 0.026  111 GLN BBB O   
2401  C CB  . GLN B 112 ? 1.513 1.600 1.437 -0.085 -0.041 0.000  111 GLN BBB CB  
2402  C CG  . GLN B 112 ? 1.489 1.604 1.427 -0.088 -0.034 -0.025 111 GLN BBB CG  
2403  C CD  . GLN B 112 ? 1.521 1.624 1.443 -0.100 -0.012 -0.051 111 GLN BBB CD  
2404  O OE1 . GLN B 112 ? 1.538 1.614 1.441 -0.108 0.009  -0.053 111 GLN BBB OE1 
2405  N NE2 . GLN B 112 ? 1.531 1.653 1.458 -0.101 -0.016 -0.072 111 GLN BBB NE2 
2406  N N   . GLY B 113 ? 1.455 1.590 1.427 -0.071 -0.082 0.027  112 GLY BBB N   
2407  C CA  . GLY B 113 ? 1.488 1.625 1.466 -0.067 -0.097 0.033  112 GLY BBB CA  
2408  C C   . GLY B 113 ? 1.530 1.676 1.503 -0.059 -0.096 0.013  112 GLY BBB C   
2409  O O   . GLY B 113 ? 1.535 1.682 1.500 -0.063 -0.087 -0.007 112 GLY BBB O   
2410  N N   . THR B 114 ? 1.588 1.741 1.564 -0.048 -0.103 0.019  113 THR BBB N   
2411  C CA  . THR B 114 ? 1.622 1.786 1.593 -0.033 -0.106 0.004  113 THR BBB CA  
2412  C C   . THR B 114 ? 1.645 1.776 1.605 -0.031 -0.118 0.011  113 THR BBB C   
2413  O O   . THR B 114 ? 1.661 1.772 1.621 -0.034 -0.123 0.032  113 THR BBB O   
2414  C CB  . THR B 114 ? 1.649 1.839 1.622 -0.017 -0.106 0.008  113 THR BBB CB  
2415  O OG1 . THR B 114 ? 1.611 1.829 1.595 -0.022 -0.094 0.001  113 THR BBB OG1 
2416  C CG2 . THR B 114 ? 1.660 1.869 1.627 0.004  -0.111 -0.008 113 THR BBB CG2 
2417  N N   . THR B 115 ? 1.650 1.775 1.603 -0.029 -0.120 -0.007 114 THR BBB N   
2418  C CA  . THR B 115 ? 1.691 1.782 1.631 -0.024 -0.128 -0.005 114 THR BBB CA  
2419  C C   . THR B 115 ? 1.711 1.807 1.645 0.003  -0.131 -0.006 114 THR BBB C   
2420  O O   . THR B 115 ? 1.727 1.858 1.665 0.018  -0.129 -0.027 114 THR BBB O   
2421  C CB  . THR B 115 ? 1.693 1.774 1.625 -0.032 -0.127 -0.025 114 THR BBB CB  
2422  O OG1 . THR B 115 ? 1.675 1.783 1.613 -0.039 -0.116 -0.042 114 THR BBB OG1 
2423  C CG2 . THR B 115 ? 1.705 1.751 1.628 -0.050 -0.133 -0.016 114 THR BBB CG2 
2424  N N   . VAL B 116 ? 1.722 1.784 1.645 0.009  -0.135 0.014  115 VAL BBB N   
2425  C CA  . VAL B 116 ? 1.745 1.796 1.651 0.039  -0.138 0.020  115 VAL BBB CA  
2426  C C   . VAL B 116 ? 1.767 1.765 1.655 0.040  -0.140 0.021  115 VAL BBB C   
2427  O O   . VAL B 116 ? 1.795 1.756 1.682 0.017  -0.138 0.033  115 VAL BBB O   
2428  C CB  . VAL B 116 ? 1.774 1.819 1.672 0.045  -0.134 0.045  115 VAL BBB CB  
2429  C CG1 . VAL B 116 ? 1.818 1.840 1.688 0.080  -0.136 0.055  115 VAL BBB CG1 
2430  C CG2 . VAL B 116 ? 1.742 1.836 1.656 0.043  -0.131 0.042  115 VAL BBB CG2 
2431  N N   . THR B 117 ? 1.753 1.752 1.631 0.066  -0.142 0.006  116 THR BBB N   
2432  C CA  . THR B 117 ? 1.773 1.719 1.631 0.072  -0.142 0.004  116 THR BBB CA  
2433  C C   . THR B 117 ? 1.785 1.712 1.619 0.114  -0.142 0.013  116 THR BBB C   
2434  O O   . THR B 117 ? 1.777 1.748 1.614 0.144  -0.147 -0.003 116 THR BBB O   
2435  C CB  . THR B 117 ? 1.758 1.718 1.626 0.061  -0.143 -0.024 116 THR BBB CB  
2436  O OG1 . THR B 117 ? 1.827 1.732 1.677 0.059  -0.141 -0.026 116 THR BBB OG1 
2437  C CG2 . THR B 117 ? 1.756 1.770 1.635 0.085  -0.143 -0.049 116 THR BBB CG2 
2438  N N   . VAL B 118 ? 1.800 1.665 1.609 0.116  -0.136 0.037  117 VAL BBB N   
2439  C CA  . VAL B 118 ? 1.870 1.697 1.643 0.156  -0.132 0.054  117 VAL BBB CA  
2440  C C   . VAL B 118 ? 1.938 1.704 1.689 0.167  -0.128 0.047  117 VAL BBB C   
2441  O O   . VAL B 118 ? 2.000 1.697 1.735 0.145  -0.117 0.060  117 VAL BBB O   
2442  C CB  . VAL B 118 ? 1.905 1.690 1.659 0.148  -0.122 0.085  117 VAL BBB CB  
2443  C CG1 . VAL B 118 ? 1.980 1.719 1.688 0.192  -0.116 0.106  117 VAL BBB CG1 
2444  C CG2 . VAL B 118 ? 1.857 1.698 1.634 0.132  -0.124 0.091  117 VAL BBB CG2 
2445  N N   . ALA B 119 ? 1.954 1.746 1.706 0.198  -0.134 0.026  118 ALA BBB N   
2446  C CA  . ALA B 119 ? 2.027 1.762 1.756 0.217  -0.129 0.019  118 ALA BBB CA  
2447  C C   . ALA B 119 ? 2.028 1.811 1.760 0.264  -0.138 -0.003 118 ALA BBB C   
2448  O O   . ALA B 119 ? 1.976 1.841 1.742 0.260  -0.146 -0.026 118 ALA BBB O   
2449  C CB  . ALA B 119 ? 2.019 1.728 1.760 0.175  -0.125 0.003  118 ALA BBB CB  
2450  N N   . SER B 120 ? 2.103 1.835 1.801 0.307  -0.134 0.003  119 SER BBB N   
2451  C CA  . SER B 120 ? 2.129 1.896 1.831 0.350  -0.140 -0.022 119 SER BBB CA  
2452  C C   . SER B 120 ? 2.100 1.881 1.830 0.317  -0.138 -0.054 119 SER BBB C   
2453  O O   . SER B 120 ? 2.073 1.801 1.799 0.273  -0.129 -0.049 119 SER BBB O   
2454  C CB  . SER B 120 ? 2.228 1.921 1.883 0.402  -0.134 -0.006 119 SER BBB CB  
2455  O OG  . SER B 120 ? 2.305 1.891 1.926 0.376  -0.116 0.018  119 SER BBB OG  
2456  N N   . THR B 121 ? 2.103 1.957 1.860 0.337  -0.144 -0.085 120 THR BBB N   
2457  C CA  . THR B 121 ? 2.092 1.978 1.879 0.305  -0.141 -0.118 120 THR BBB CA  
2458  C C   . THR B 121 ? 2.164 2.003 1.934 0.326  -0.133 -0.134 120 THR BBB C   
2459  O O   . THR B 121 ? 2.239 2.039 1.980 0.375  -0.133 -0.123 120 THR BBB O   
2460  C CB  . THR B 121 ? 2.033 2.027 1.861 0.308  -0.147 -0.148 120 THR BBB CB  
2461  O OG1 . THR B 121 ? 2.063 2.100 1.897 0.360  -0.152 -0.169 120 THR BBB OG1 
2462  C CG2 . THR B 121 ? 1.983 2.025 1.824 0.300  -0.155 -0.135 120 THR BBB CG2 
2463  N N   . LYS B 122 ? 2.147 1.987 1.930 0.292  -0.127 -0.157 121 LYS BBB N   
2464  C CA  . LYS B 122 ? 2.200 2.009 1.975 0.304  -0.118 -0.180 121 LYS BBB CA  
2465  C C   . LYS B 122 ? 2.162 2.009 1.960 0.261  -0.113 -0.209 121 LYS BBB C   
2466  O O   . LYS B 122 ? 2.146 1.975 1.943 0.213  -0.112 -0.199 121 LYS BBB O   
2467  C CB  . LYS B 122 ? 2.289 1.986 2.021 0.301  -0.109 -0.160 121 LYS BBB CB  
2468  C CG  . LYS B 122 ? 2.360 2.011 2.073 0.329  -0.098 -0.179 121 LYS BBB CG  
2469  C CD  . LYS B 122 ? 2.344 1.976 2.060 0.286  -0.089 -0.203 121 LYS BBB CD  
2470  C CE  . LYS B 122 ? 2.423 1.977 2.108 0.305  -0.076 -0.214 121 LYS BBB CE  
2471  N NZ  . LYS B 122 ? 2.442 2.034 2.137 0.362  -0.075 -0.236 121 LYS BBB NZ  
2472  N N   . GLY B 123 ? 2.159 2.061 1.979 0.279  -0.109 -0.243 122 GLY BBB N   
2473  C CA  . GLY B 123 ? 2.101 2.048 1.944 0.242  -0.100 -0.272 122 GLY BBB CA  
2474  C C   . GLY B 123 ? 2.119 2.000 1.937 0.212  -0.090 -0.280 122 GLY BBB C   
2475  O O   . GLY B 123 ? 2.191 2.010 1.984 0.232  -0.086 -0.279 122 GLY BBB O   
2476  N N   . PRO B 124 ? 2.038 1.930 1.859 0.165  -0.084 -0.289 123 PRO BBB N   
2477  C CA  . PRO B 124 ? 2.042 1.876 1.836 0.134  -0.077 -0.295 123 PRO BBB CA  
2478  C C   . PRO B 124 ? 2.043 1.884 1.836 0.146  -0.063 -0.331 123 PRO BBB C   
2479  O O   . PRO B 124 ? 2.004 1.914 1.824 0.154  -0.055 -0.355 123 PRO BBB O   
2480  C CB  . PRO B 124 ? 1.996 1.853 1.793 0.089  -0.076 -0.292 123 PRO BBB CB  
2481  C CG  . PRO B 124 ? 1.952 1.891 1.783 0.097  -0.073 -0.304 123 PRO BBB CG  
2482  C CD  . PRO B 124 ? 1.969 1.929 1.816 0.142  -0.083 -0.295 123 PRO BBB CD  
2483  N N   . SER B 125 ? 2.079 1.851 1.843 0.146  -0.057 -0.335 124 SER BBB N   
2484  C CA  . SER B 125 ? 2.104 1.871 1.859 0.143  -0.042 -0.369 124 SER BBB CA  
2485  C C   . SER B 125 ? 2.082 1.854 1.825 0.093  -0.037 -0.376 124 SER BBB C   
2486  O O   . SER B 125 ? 2.083 1.824 1.808 0.062  -0.047 -0.353 124 SER BBB O   
2487  C CB  . SER B 125 ? 2.176 1.863 1.900 0.158  -0.037 -0.372 124 SER BBB CB  
2488  O OG  . SER B 125 ? 2.219 1.916 1.955 0.212  -0.033 -0.382 124 SER BBB OG  
2489  N N   . VAL B 126 ? 2.071 1.882 1.820 0.086  -0.021 -0.407 125 VAL BBB N   
2490  C CA  . VAL B 126 ? 2.056 1.868 1.785 0.042  -0.012 -0.414 125 VAL BBB CA  
2491  C C   . VAL B 126 ? 2.092 1.875 1.796 0.038  0.005  -0.444 125 VAL BBB C   
2492  O O   . VAL B 126 ? 2.093 1.913 1.816 0.058  0.021  -0.473 125 VAL BBB O   
2493  C CB  . VAL B 126 ? 2.021 1.905 1.777 0.031  -0.002 -0.422 125 VAL BBB CB  
2494  C CG1 . VAL B 126 ? 2.029 1.902 1.755 -0.010 0.010  -0.426 125 VAL BBB CG1 
2495  C CG2 . VAL B 126 ? 1.984 1.898 1.766 0.038  -0.017 -0.396 125 VAL BBB CG2 
2496  N N   . PHE B 127 ? 2.111 1.834 1.774 0.011  0.000  -0.438 126 PHE BBB N   
2497  C CA  . PHE B 127 ? 2.157 1.844 1.786 0.000  0.014  -0.464 126 PHE BBB CA  
2498  C C   . PHE B 127 ? 2.149 1.838 1.745 -0.040 0.018  -0.465 126 PHE BBB C   
2499  O O   . PHE B 127 ? 2.109 1.799 1.699 -0.060 0.004  -0.439 126 PHE BBB O   
2500  C CB  . PHE B 127 ? 2.215 1.829 1.818 0.003  0.005  -0.460 126 PHE BBB CB  
2501  C CG  . PHE B 127 ? 2.232 1.830 1.858 0.044  0.001  -0.450 126 PHE BBB CG  
2502  C CD1 . PHE B 127 ? 2.238 1.863 1.888 0.085  0.013  -0.470 126 PHE BBB CD1 
2503  C CD2 . PHE B 127 ? 2.253 1.808 1.874 0.042  -0.015 -0.422 126 PHE BBB CD2 
2504  C CE1 . PHE B 127 ? 2.257 1.862 1.919 0.128  0.008  -0.459 126 PHE BBB CE1 
2505  C CE2 . PHE B 127 ? 2.271 1.802 1.903 0.081  -0.016 -0.411 126 PHE BBB CE2 
2506  C CZ  . PHE B 127 ? 2.274 1.827 1.923 0.126  -0.005 -0.428 126 PHE BBB CZ  
2507  N N   . PRO B 128 ? 2.178 1.867 1.751 -0.050 0.040  -0.493 127 PRO BBB N   
2508  C CA  . PRO B 128 ? 2.192 1.872 1.722 -0.084 0.046  -0.493 127 PRO BBB CA  
2509  C C   . PRO B 128 ? 2.259 1.881 1.740 -0.104 0.033  -0.492 127 PRO BBB C   
2510  O O   . PRO B 128 ? 2.274 1.859 1.754 -0.093 0.027  -0.500 127 PRO BBB O   
2511  C CB  . PRO B 128 ? 2.201 1.908 1.731 -0.083 0.077  -0.528 127 PRO BBB CB  
2512  C CG  . PRO B 128 ? 2.227 1.926 1.778 -0.052 0.083  -0.551 127 PRO BBB CG  
2513  C CD  . PRO B 128 ? 2.202 1.901 1.788 -0.026 0.060  -0.527 127 PRO BBB CD  
2514  N N   . LEU B 129 ? 2.284 1.899 1.723 -0.132 0.029  -0.482 128 LEU BBB N   
2515  C CA  . LEU B 129 ? 2.333 1.905 1.721 -0.153 0.016  -0.484 128 LEU BBB CA  
2516  C C   . LEU B 129 ? 2.360 1.927 1.693 -0.170 0.035  -0.500 128 LEU BBB C   
2517  O O   . LEU B 129 ? 2.338 1.914 1.644 -0.184 0.031  -0.481 128 LEU BBB O   
2518  C CB  . LEU B 129 ? 2.316 1.888 1.703 -0.166 -0.014 -0.451 128 LEU BBB CB  
2519  C CG  . LEU B 129 ? 2.285 1.859 1.720 -0.152 -0.030 -0.433 128 LEU BBB CG  
2520  C CD1 . LEU B 129 ? 2.242 1.828 1.679 -0.166 -0.055 -0.402 128 LEU BBB CD1 
2521  C CD2 . LEU B 129 ? 2.335 1.863 1.767 -0.149 -0.034 -0.449 128 LEU BBB CD2 
2522  N N   . ALA B 130 ? 2.409 1.960 1.725 -0.167 0.056  -0.533 129 ALA BBB N   
2523  C CA  . ALA B 130 ? 2.482 2.027 1.747 -0.181 0.081  -0.552 129 ALA BBB CA  
2524  C C   . ALA B 130 ? 2.557 2.070 1.754 -0.203 0.064  -0.547 129 ALA BBB C   
2525  O O   . ALA B 130 ? 2.601 2.088 1.788 -0.208 0.042  -0.550 129 ALA BBB O   
2526  C CB  . ALA B 130 ? 2.531 2.070 1.801 -0.170 0.107  -0.590 129 ALA BBB CB  
2527  N N   . PRO B 131 ? 2.584 2.095 1.728 -0.217 0.077  -0.542 130 PRO BBB N   
2528  C CA  . PRO B 131 ? 2.626 2.112 1.699 -0.233 0.058  -0.534 130 PRO BBB CA  
2529  C C   . PRO B 131 ? 2.678 2.132 1.693 -0.243 0.068  -0.567 130 PRO BBB C   
2530  O O   . PRO B 131 ? 2.646 2.094 1.674 -0.237 0.093  -0.596 130 PRO BBB O   
2531  C CB  . PRO B 131 ? 2.646 2.140 1.684 -0.238 0.074  -0.513 130 PRO BBB CB  
2532  C CG  . PRO B 131 ? 2.632 2.141 1.699 -0.233 0.116  -0.531 130 PRO BBB CG  
2533  C CD  . PRO B 131 ? 2.565 2.097 1.711 -0.217 0.111  -0.543 130 PRO BBB CD  
2534  N N   . SER B 132 ? 2.726 2.165 1.681 -0.255 0.045  -0.562 131 SER BBB N   
2535  C CA  . SER B 132 ? 2.815 2.226 1.696 -0.267 0.052  -0.589 131 SER BBB CA  
2536  C C   . SER B 132 ? 2.883 2.289 1.684 -0.273 0.045  -0.569 131 SER BBB C   
2537  O O   . SER B 132 ? 2.835 2.259 1.643 -0.268 0.024  -0.534 131 SER BBB O   
2538  C CB  A SER B 132 ? 2.831 2.226 1.713 -0.275 0.027  -0.610 131 SER BBB CB  
2539  C CB  B SER B 132 ? 2.821 2.217 1.704 -0.275 0.026  -0.610 131 SER BBB CB  
2540  O OG  A SER B 132 ? 2.796 2.209 1.692 -0.281 -0.013 -0.588 131 SER BBB OG  
2541  O OG  B SER B 132 ? 2.877 2.247 1.695 -0.286 0.036  -0.642 131 SER BBB OG  
2542  N N   . SER B 133 ? 2.978 2.358 1.703 -0.280 0.064  -0.590 132 SER BBB N   
2543  C CA  . SER B 133 ? 3.030 2.396 1.661 -0.283 0.061  -0.575 132 SER BBB CA  
2544  C C   . SER B 133 ? 3.074 2.417 1.633 -0.293 0.061  -0.609 132 SER BBB C   
2545  O O   . SER B 133 ? 3.012 2.354 1.599 -0.300 0.046  -0.637 132 SER BBB O   
2546  C CB  . SER B 133 ? 3.045 2.400 1.650 -0.279 0.101  -0.558 132 SER BBB CB  
2547  O OG  . SER B 133 ? 3.133 2.465 1.639 -0.278 0.099  -0.540 132 SER BBB OG  
2548  N N   . GLY B 138 ? 3.486 2.720 1.609 -0.264 0.099  -0.516 137 GLY BBB N   
2549  C CA  . GLY B 138 ? 3.379 2.646 1.610 -0.261 0.087  -0.497 137 GLY BBB CA  
2550  C C   . GLY B 138 ? 3.365 2.625 1.574 -0.244 0.083  -0.449 137 GLY BBB C   
2551  O O   . GLY B 138 ? 3.416 2.630 1.547 -0.239 0.121  -0.432 137 GLY BBB O   
2552  N N   . GLY B 139 ? 3.278 2.577 1.551 -0.234 0.042  -0.428 138 GLY BBB N   
2553  C CA  . GLY B 139 ? 3.246 2.544 1.507 -0.215 0.031  -0.383 138 GLY BBB CA  
2554  C C   . GLY B 139 ? 3.132 2.449 1.495 -0.218 0.043  -0.370 138 GLY BBB C   
2555  O O   . GLY B 139 ? 3.118 2.407 1.484 -0.224 0.091  -0.366 138 GLY BBB O   
2556  N N   . THR B 140 ? 3.050 2.414 1.494 -0.216 0.003  -0.366 139 THR BBB N   
2557  C CA  . THR B 140 ? 2.928 2.317 1.476 -0.219 0.008  -0.358 139 THR BBB CA  
2558  C C   . THR B 140 ? 2.888 2.302 1.514 -0.234 0.004  -0.394 139 THR BBB C   
2559  O O   . THR B 140 ? 2.961 2.382 1.573 -0.240 -0.020 -0.418 139 THR BBB O   
2560  C CB  . THR B 140 ? 2.850 2.270 1.430 -0.203 -0.029 -0.324 139 THR BBB CB  
2561  O OG1 . THR B 140 ? 2.688 2.130 1.365 -0.208 -0.021 -0.321 139 THR BBB OG1 
2562  C CG2 . THR B 140 ? 2.859 2.317 1.445 -0.201 -0.082 -0.331 139 THR BBB CG2 
2563  N N   . ALA B 141 ? 2.785 2.208 1.487 -0.238 0.028  -0.398 140 ALA BBB N   
2564  C CA  . ALA B 141 ? 2.720 2.166 1.504 -0.245 0.025  -0.426 140 ALA BBB CA  
2565  C C   . ALA B 141 ? 2.613 2.085 1.482 -0.240 0.029  -0.409 140 ALA BBB C   
2566  O O   . ALA B 141 ? 2.596 2.061 1.460 -0.238 0.057  -0.394 140 ALA BBB O   
2567  C CB  . ALA B 141 ? 2.761 2.188 1.531 -0.254 0.062  -0.461 140 ALA BBB CB  
2568  N N   . ALA B 142 ? 2.555 2.053 1.495 -0.238 0.004  -0.413 141 ALA BBB N   
2569  C CA  . ALA B 142 ? 2.469 1.996 1.488 -0.231 -0.003 -0.394 141 ALA BBB CA  
2570  C C   . ALA B 142 ? 2.444 1.983 1.531 -0.229 0.007  -0.418 141 ALA BBB C   
2571  O O   . ALA B 142 ? 2.476 2.001 1.556 -0.233 0.004  -0.445 141 ALA BBB O   
2572  C CB  . ALA B 142 ? 2.428 1.974 1.462 -0.228 -0.045 -0.371 141 ALA BBB CB  
2573  N N   . LEU B 143 ? 2.406 1.969 1.554 -0.220 0.018  -0.408 142 LEU BBB N   
2574  C CA  . LEU B 143 ? 2.369 1.949 1.583 -0.211 0.028  -0.427 142 LEU BBB CA  
2575  C C   . LEU B 143 ? 2.301 1.913 1.579 -0.201 0.014  -0.403 142 LEU BBB C   
2576  O O   . LEU B 143 ? 2.276 1.893 1.544 -0.203 0.005  -0.375 142 LEU BBB O   
2577  C CB  . LEU B 143 ? 2.379 1.964 1.591 -0.212 0.069  -0.452 142 LEU BBB CB  
2578  C CG  . LEU B 143 ? 2.354 1.950 1.559 -0.217 0.096  -0.440 142 LEU BBB CG  
2579  C CD1 . LEU B 143 ? 2.261 1.899 1.540 -0.208 0.100  -0.435 142 LEU BBB CD1 
2580  C CD2 . LEU B 143 ? 2.415 1.996 1.578 -0.228 0.137  -0.465 142 LEU BBB CD2 
2581  N N   . GLY B 144 ? 2.273 1.901 1.610 -0.188 0.014  -0.413 143 GLY BBB N   
2582  C CA  . GLY B 144 ? 2.209 1.865 1.603 -0.176 0.000  -0.392 143 GLY BBB CA  
2583  C C   . GLY B 144 ? 2.182 1.856 1.632 -0.156 0.006  -0.406 143 GLY BBB C   
2584  O O   . GLY B 144 ? 2.185 1.851 1.633 -0.149 0.022  -0.435 143 GLY BBB O   
2585  N N   . CYS B 145 ? 2.353 1.741 1.799 -0.007 -0.199 -0.202 144 CYS BBB N   
2586  C CA  . CYS B 145 ? 2.340 1.760 1.812 0.007  -0.189 -0.203 144 CYS BBB CA  
2587  C C   . CYS B 145 ? 2.308 1.724 1.769 0.023  -0.187 -0.216 144 CYS BBB C   
2588  O O   . CYS B 145 ? 2.311 1.711 1.757 0.023  -0.203 -0.226 144 CYS BBB O   
2589  C CB  . CYS B 145 ? 2.358 1.798 1.860 0.004  -0.213 -0.204 144 CYS BBB CB  
2590  S SG  . CYS B 145 ? 2.420 1.892 1.958 -0.012 -0.207 -0.183 144 CYS BBB SG  
2591  N N   . LEU B 146 ? 2.281 1.714 1.751 0.036  -0.166 -0.212 145 LEU BBB N   
2592  C CA  . LEU B 146 ? 2.262 1.698 1.729 0.050  -0.163 -0.219 145 LEU BBB CA  
2593  C C   . LEU B 146 ? 2.258 1.730 1.751 0.063  -0.169 -0.214 145 LEU BBB C   
2594  O O   . LEU B 146 ? 2.252 1.747 1.766 0.069  -0.156 -0.200 145 LEU BBB O   
2595  C CB  . LEU B 146 ? 2.267 1.683 1.717 0.053  -0.134 -0.217 145 LEU BBB CB  
2596  C CG  . LEU B 146 ? 2.261 1.673 1.707 0.062  -0.130 -0.221 145 LEU BBB CG  
2597  C CD1 . LEU B 146 ? 2.254 1.658 1.686 0.053  -0.150 -0.233 145 LEU BBB CD1 
2598  C CD2 . LEU B 146 ? 2.298 1.680 1.727 0.064  -0.101 -0.220 145 LEU BBB CD2 
2599  N N   . VAL B 147 ? 2.252 1.732 1.742 0.069  -0.187 -0.224 146 VAL BBB N   
2600  C CA  . VAL B 147 ? 2.239 1.753 1.743 0.081  -0.197 -0.222 146 VAL BBB CA  
2601  C C   . VAL B 147 ? 2.244 1.764 1.740 0.096  -0.183 -0.219 146 VAL BBB C   
2602  O O   . VAL B 147 ? 2.231 1.744 1.713 0.098  -0.189 -0.230 146 VAL BBB O   
2603  C CB  . VAL B 147 ? 2.263 1.776 1.761 0.077  -0.226 -0.238 146 VAL BBB CB  
2604  C CG1 . VAL B 147 ? 2.278 1.823 1.778 0.088  -0.239 -0.240 146 VAL BBB CG1 
2605  C CG2 . VAL B 147 ? 2.282 1.780 1.787 0.059  -0.240 -0.239 146 VAL BBB CG2 
2606  N N   . LYS B 148 ? 2.273 1.806 1.780 0.107  -0.164 -0.202 147 LYS BBB N   
2607  C CA  . LYS B 148 ? 2.301 1.827 1.802 0.118  -0.144 -0.193 147 LYS BBB CA  
2608  C C   . LYS B 148 ? 2.285 1.847 1.794 0.135  -0.147 -0.179 147 LYS BBB C   
2609  O O   . LYS B 148 ? 2.247 1.840 1.774 0.139  -0.156 -0.169 147 LYS BBB O   
2610  C CB  . LYS B 148 ? 2.346 1.843 1.848 0.118  -0.116 -0.184 147 LYS BBB CB  
2611  C CG  . LYS B 148 ? 2.391 1.861 1.880 0.122  -0.096 -0.180 147 LYS BBB CG  
2612  C CD  . LYS B 148 ? 2.435 1.872 1.924 0.128  -0.066 -0.170 147 LYS BBB CD  
2613  C CE  . LYS B 148 ? 2.466 1.870 1.944 0.131  -0.048 -0.164 147 LYS BBB CE  
2614  N NZ  . LYS B 148 ? 2.476 1.848 1.931 0.108  -0.051 -0.181 147 LYS BBB NZ  
2615  N N   . ASP B 149 ? 2.295 1.858 1.793 0.142  -0.140 -0.175 148 ASP BBB N   
2616  C CA  . ASP B 149 ? 2.312 1.904 1.811 0.159  -0.136 -0.155 148 ASP BBB CA  
2617  C C   . ASP B 149 ? 2.302 1.935 1.799 0.164  -0.162 -0.158 148 ASP BBB C   
2618  O O   . ASP B 149 ? 2.297 1.959 1.812 0.172  -0.167 -0.141 148 ASP BBB O   
2619  C CB  . ASP B 149 ? 2.340 1.922 1.856 0.171  -0.112 -0.130 148 ASP BBB CB  
2620  C CG  . ASP B 149 ? 2.369 1.901 1.877 0.167  -0.086 -0.128 148 ASP BBB CG  
2621  O OD1 . ASP B 149 ? 2.352 1.872 1.845 0.157  -0.086 -0.136 148 ASP BBB OD1 
2622  O OD2 . ASP B 149 ? 2.413 1.921 1.931 0.174  -0.066 -0.117 148 ASP BBB OD2 
2623  N N   . TYR B 150 ? 2.294 1.931 1.771 0.159  -0.180 -0.180 149 TYR BBB N   
2624  C CA  . TYR B 150 ? 2.289 1.956 1.750 0.162  -0.206 -0.191 149 TYR BBB CA  
2625  C C   . TYR B 150 ? 2.295 1.970 1.726 0.172  -0.205 -0.201 149 TYR BBB C   
2626  O O   . TYR B 150 ? 2.277 1.935 1.706 0.172  -0.188 -0.204 149 TYR BBB O   
2627  C CB  . TYR B 150 ? 2.287 1.939 1.751 0.146  -0.228 -0.214 149 TYR BBB CB  
2628  C CG  . TYR B 150 ? 2.303 1.923 1.755 0.141  -0.230 -0.238 149 TYR BBB CG  
2629  C CD1 . TYR B 150 ? 2.332 1.952 1.757 0.148  -0.242 -0.260 149 TYR BBB CD1 
2630  C CD2 . TYR B 150 ? 2.309 1.898 1.773 0.131  -0.220 -0.239 149 TYR BBB CD2 
2631  C CE1 . TYR B 150 ? 2.339 1.933 1.758 0.148  -0.243 -0.279 149 TYR BBB CE1 
2632  C CE2 . TYR B 150 ? 2.313 1.877 1.768 0.127  -0.225 -0.256 149 TYR BBB CE2 
2633  C CZ  . TYR B 150 ? 2.322 1.890 1.759 0.138  -0.236 -0.275 149 TYR BBB CZ  
2634  O OH  . TYR B 150 ? 2.321 1.867 1.755 0.139  -0.240 -0.290 149 TYR BBB OH  
2635  N N   . PHE B 151 ? 2.319 2.024 1.726 0.179  -0.222 -0.206 150 PHE BBB N   
2636  C CA  . PHE B 151 ? 2.344 2.065 1.714 0.193  -0.218 -0.213 150 PHE BBB CA  
2637  C C   . PHE B 151 ? 2.359 2.103 1.697 0.195  -0.245 -0.227 150 PHE BBB C   
2638  O O   . PHE B 151 ? 2.350 2.115 1.697 0.190  -0.263 -0.215 150 PHE BBB O   
2639  C CB  . PHE B 151 ? 2.373 2.111 1.744 0.204  -0.193 -0.180 150 PHE BBB CB  
2640  C CG  . PHE B 151 ? 2.410 2.162 1.753 0.215  -0.177 -0.181 150 PHE BBB CG  
2641  C CD1 . PHE B 151 ? 2.409 2.146 1.758 0.212  -0.166 -0.198 150 PHE BBB CD1 
2642  C CD2 . PHE B 151 ? 2.451 2.237 1.767 0.228  -0.172 -0.159 150 PHE BBB CD2 
2643  C CE1 . PHE B 151 ? 2.439 2.198 1.769 0.223  -0.148 -0.195 150 PHE BBB CE1 
2644  C CE2 . PHE B 151 ? 2.481 2.284 1.772 0.237  -0.153 -0.157 150 PHE BBB CE2 
2645  C CZ  . PHE B 151 ? 2.475 2.267 1.776 0.235  -0.140 -0.175 150 PHE BBB CZ  
2646  N N   . PRO B 152 ? 2.392 2.132 1.690 0.202  -0.251 -0.255 151 PRO BBB N   
2647  C CA  . PRO B 152 ? 2.380 2.097 1.676 0.208  -0.235 -0.273 151 PRO BBB CA  
2648  C C   . PRO B 152 ? 2.354 2.030 1.667 0.196  -0.250 -0.298 151 PRO BBB C   
2649  O O   . PRO B 152 ? 2.341 2.009 1.668 0.181  -0.270 -0.298 151 PRO BBB O   
2650  C CB  . PRO B 152 ? 2.444 2.177 1.688 0.225  -0.235 -0.294 151 PRO BBB CB  
2651  C CG  . PRO B 152 ? 2.486 2.225 1.700 0.218  -0.268 -0.306 151 PRO BBB CG  
2652  C CD  . PRO B 152 ? 2.453 2.212 1.703 0.206  -0.274 -0.272 151 PRO BBB CD  
2653  N N   . GLU B 153 ? 2.340 1.997 1.654 0.203  -0.241 -0.315 152 GLU BBB N   
2654  C CA  . GLU B 153 ? 2.347 1.962 1.669 0.197  -0.256 -0.340 152 GLU BBB CA  
2655  C C   . GLU B 153 ? 2.397 1.993 1.681 0.199  -0.280 -0.371 152 GLU BBB C   
2656  O O   . GLU B 153 ? 2.428 2.045 1.673 0.210  -0.282 -0.380 152 GLU BBB O   
2657  C CB  . GLU B 153 ? 2.343 1.954 1.674 0.211  -0.238 -0.346 152 GLU BBB CB  
2658  C CG  . GLU B 153 ? 2.295 1.903 1.666 0.200  -0.225 -0.324 152 GLU BBB CG  
2659  C CD  . GLU B 153 ? 2.294 1.867 1.683 0.195  -0.236 -0.336 152 GLU BBB CD  
2660  O OE1 . GLU B 153 ? 2.300 1.843 1.692 0.180  -0.254 -0.340 152 GLU BBB OE1 
2661  O OE2 . GLU B 153 ? 2.291 1.871 1.692 0.207  -0.226 -0.338 152 GLU BBB OE2 
2662  N N   . PRO B 154 ? 2.413 1.964 1.703 0.187  -0.301 -0.391 153 PRO BBB N   
2663  C CA  . PRO B 154 ? 2.381 1.908 1.711 0.172  -0.301 -0.379 153 PRO BBB CA  
2664  C C   . PRO B 154 ? 2.364 1.883 1.715 0.145  -0.319 -0.368 153 PRO BBB C   
2665  O O   . PRO B 154 ? 2.368 1.902 1.706 0.136  -0.336 -0.371 153 PRO BBB O   
2666  C CB  . PRO B 154 ? 2.427 1.907 1.744 0.182  -0.310 -0.408 153 PRO BBB CB  
2667  C CG  . PRO B 154 ? 2.496 1.961 1.768 0.186  -0.329 -0.438 153 PRO BBB CG  
2668  C CD  . PRO B 154 ? 2.483 2.000 1.735 0.188  -0.324 -0.426 153 PRO BBB CD  
2669  N N   . VAL B 155 ? 2.337 1.837 1.719 0.132  -0.316 -0.355 154 VAL BBB N   
2670  C CA  . VAL B 155 ? 2.335 1.825 1.741 0.106  -0.328 -0.343 154 VAL BBB CA  
2671  C C   . VAL B 155 ? 2.345 1.784 1.755 0.096  -0.340 -0.354 154 VAL BBB C   
2672  O O   . VAL B 155 ? 2.317 1.736 1.723 0.111  -0.332 -0.359 154 VAL BBB O   
2673  C CB  . VAL B 155 ? 2.311 1.827 1.747 0.100  -0.308 -0.312 154 VAL BBB CB  
2674  C CG1 . VAL B 155 ? 2.319 1.881 1.756 0.109  -0.298 -0.297 154 VAL BBB CG1 
2675  C CG2 . VAL B 155 ? 2.296 1.797 1.737 0.106  -0.288 -0.306 154 VAL BBB CG2 
2676  N N   . THR B 156 ? 2.376 1.799 1.797 0.071  -0.360 -0.353 155 THR BBB N   
2677  C CA  . THR B 156 ? 2.414 1.783 1.839 0.056  -0.374 -0.358 155 THR BBB CA  
2678  C C   . THR B 156 ? 2.369 1.747 1.826 0.030  -0.371 -0.331 155 THR BBB C   
2679  O O   . THR B 156 ? 2.336 1.755 1.811 0.018  -0.372 -0.318 155 THR BBB O   
2680  C CB  . THR B 156 ? 2.499 1.829 1.902 0.047  -0.403 -0.386 155 THR BBB CB  
2681  O OG1 . THR B 156 ? 2.508 1.869 1.922 0.023  -0.418 -0.380 155 THR BBB OG1 
2682  C CG2 . THR B 156 ? 2.538 1.858 1.903 0.075  -0.403 -0.416 155 THR BBB CG2 
2683  N N   . VAL B 157 ? 2.367 1.711 1.830 0.023  -0.368 -0.321 156 VAL BBB N   
2684  C CA  . VAL B 157 ? 2.358 1.709 1.844 0.000  -0.359 -0.294 156 VAL BBB CA  
2685  C C   . VAL B 157 ? 2.403 1.703 1.891 -0.020 -0.377 -0.292 156 VAL BBB C   
2686  O O   . VAL B 157 ? 2.455 1.707 1.924 -0.008 -0.388 -0.307 156 VAL BBB O   
2687  C CB  . VAL B 157 ? 2.337 1.699 1.822 0.012  -0.334 -0.279 156 VAL BBB CB  
2688  C CG1 . VAL B 157 ? 2.343 1.720 1.845 -0.007 -0.318 -0.253 156 VAL BBB CG1 
2689  C CG2 . VAL B 157 ? 2.314 1.710 1.792 0.034  -0.317 -0.284 156 VAL BBB CG2 
2690  N N   . SER B 158 ? 2.406 1.714 1.917 -0.049 -0.378 -0.271 157 SER BBB N   
2691  C CA  . SER B 158 ? 2.450 1.711 1.965 -0.073 -0.390 -0.259 157 SER BBB CA  
2692  C C   . SER B 158 ? 2.428 1.720 1.966 -0.093 -0.370 -0.226 157 SER BBB C   
2693  O O   . SER B 158 ? 2.384 1.732 1.938 -0.089 -0.351 -0.217 157 SER BBB O   
2694  C CB  . SER B 158 ? 2.503 1.732 2.022 -0.095 -0.420 -0.274 157 SER BBB CB  
2695  O OG  . SER B 158 ? 2.493 1.771 2.042 -0.120 -0.425 -0.264 157 SER BBB OG  
2696  N N   . TRP B 159 ? 2.460 1.716 1.996 -0.112 -0.372 -0.208 158 TRP BBB N   
2697  C CA  . TRP B 159 ? 2.452 1.731 1.998 -0.128 -0.348 -0.176 158 TRP BBB CA  
2698  C C   . TRP B 159 ? 2.488 1.758 2.060 -0.166 -0.358 -0.154 158 TRP BBB C   
2699  O O   . TRP B 159 ? 2.533 1.744 2.097 -0.178 -0.382 -0.157 158 TRP BBB O   
2700  C CB  . TRP B 159 ? 2.467 1.717 1.980 -0.114 -0.337 -0.168 158 TRP BBB CB  
2701  C CG  . TRP B 159 ? 2.424 1.698 1.920 -0.085 -0.320 -0.181 158 TRP BBB CG  
2702  C CD1 . TRP B 159 ? 2.409 1.669 1.888 -0.060 -0.330 -0.202 158 TRP BBB CD1 
2703  C CD2 . TRP B 159 ? 2.399 1.715 1.893 -0.080 -0.290 -0.172 158 TRP BBB CD2 
2704  N NE1 . TRP B 159 ? 2.360 1.651 1.830 -0.044 -0.309 -0.206 158 TRP BBB NE1 
2705  C CE2 . TRP B 159 ? 2.365 1.684 1.841 -0.055 -0.285 -0.189 158 TRP BBB CE2 
2706  C CE3 . TRP B 159 ? 2.411 1.759 1.917 -0.093 -0.265 -0.151 158 TRP BBB CE3 
2707  C CZ2 . TRP B 159 ? 2.351 1.696 1.818 -0.045 -0.258 -0.187 158 TRP BBB CZ2 
2708  C CZ3 . TRP B 159 ? 2.395 1.769 1.891 -0.078 -0.235 -0.151 158 TRP BBB CZ3 
2709  C CH2 . TRP B 159 ? 2.367 1.735 1.842 -0.056 -0.233 -0.170 158 TRP BBB CH2 
2710  N N   . ASN B 160 ? 2.467 1.795 2.072 -0.182 -0.339 -0.132 159 ASN BBB N   
2711  C CA  . ASN B 160 ? 2.503 1.845 2.145 -0.222 -0.344 -0.106 159 ASN BBB CA  
2712  C C   . ASN B 160 ? 2.521 1.844 2.181 -0.242 -0.382 -0.125 159 ASN BBB C   
2713  O O   . ASN B 160 ? 2.552 1.838 2.224 -0.276 -0.401 -0.114 159 ASN BBB O   
2714  C CB  . ASN B 160 ? 2.563 1.863 2.190 -0.241 -0.337 -0.079 159 ASN BBB CB  
2715  C CG  . ASN B 160 ? 2.553 1.889 2.169 -0.233 -0.297 -0.055 159 ASN BBB CG  
2716  O OD1 . ASN B 160 ? 2.507 1.865 2.103 -0.203 -0.277 -0.067 159 ASN BBB OD1 
2717  N ND2 . ASN B 160 ? 2.600 1.940 2.225 -0.261 -0.284 -0.020 159 ASN BBB ND2 
2718  N N   . SER B 161 ? 2.500 1.844 2.158 -0.222 -0.394 -0.153 160 SER BBB N   
2719  C CA  . SER B 161 ? 2.539 1.866 2.201 -0.237 -0.431 -0.179 160 SER BBB CA  
2720  C C   . SER B 161 ? 2.581 1.823 2.195 -0.219 -0.451 -0.212 160 SER BBB C   
2721  O O   . SER B 161 ? 2.628 1.853 2.229 -0.218 -0.476 -0.243 160 SER BBB O   
2722  C CB  . SER B 161 ? 2.581 1.917 2.284 -0.286 -0.450 -0.161 160 SER BBB CB  
2723  O OG  . SER B 161 ? 2.598 1.955 2.314 -0.300 -0.481 -0.182 160 SER BBB OG  
2724  N N   . GLY B 162 ? 2.570 1.764 2.159 -0.204 -0.439 -0.204 161 GLY BBB N   
2725  C CA  . GLY B 162 ? 2.610 1.726 2.161 -0.183 -0.454 -0.229 161 GLY BBB CA  
2726  C C   . GLY B 162 ? 2.678 1.727 2.223 -0.199 -0.460 -0.208 161 GLY BBB C   
2727  O O   . GLY B 162 ? 2.706 1.687 2.223 -0.179 -0.472 -0.223 161 GLY BBB O   
2728  N N   . ALA B 163 ? 2.712 1.780 2.283 -0.232 -0.451 -0.171 162 ALA BBB N   
2729  C CA  . ALA B 163 ? 2.784 1.796 2.349 -0.252 -0.452 -0.141 162 ALA BBB CA  
2730  C C   . ALA B 163 ? 2.762 1.797 2.308 -0.232 -0.424 -0.116 162 ALA BBB C   
2731  O O   . ALA B 163 ? 2.737 1.789 2.292 -0.256 -0.408 -0.079 162 ALA BBB O   
2732  C CB  . ALA B 163 ? 2.823 1.846 2.426 -0.302 -0.458 -0.115 162 ALA BBB CB  
2733  N N   . LEU B 164 ? 2.766 1.803 2.285 -0.192 -0.418 -0.136 163 LEU BBB N   
2734  C CA  . LEU B 164 ? 2.777 1.821 2.269 -0.172 -0.400 -0.119 163 LEU BBB CA  
2735  C C   . LEU B 164 ? 2.746 1.787 2.218 -0.130 -0.403 -0.148 163 LEU BBB C   
2736  O O   . LEU B 164 ? 2.655 1.751 2.127 -0.114 -0.386 -0.160 163 LEU BBB O   
2737  C CB  . LEU B 164 ? 2.750 1.863 2.248 -0.181 -0.368 -0.099 163 LEU BBB CB  
2738  C CG  . LEU B 164 ? 2.769 1.878 2.233 -0.177 -0.351 -0.073 163 LEU BBB CG  
2739  C CD1 . LEU B 164 ? 2.816 1.905 2.283 -0.211 -0.348 -0.034 163 LEU BBB CD1 
2740  C CD2 . LEU B 164 ? 2.715 1.883 2.169 -0.165 -0.320 -0.076 163 LEU BBB CD2 
2741  N N   . THR B 165 ? 2.802 1.782 2.261 -0.113 -0.423 -0.156 164 THR BBB N   
2742  C CA  . THR B 165 ? 2.781 1.755 2.225 -0.073 -0.427 -0.176 164 THR BBB CA  
2743  C C   . THR B 165 ? 2.790 1.750 2.216 -0.063 -0.427 -0.149 164 THR BBB C   
2744  O O   . THR B 165 ? 2.768 1.729 2.188 -0.031 -0.432 -0.159 164 THR BBB O   
2745  C CB  . THR B 165 ? 2.830 1.748 2.275 -0.055 -0.449 -0.204 164 THR BBB CB  
2746  O OG1 . THR B 165 ? 2.904 1.748 2.347 -0.069 -0.466 -0.185 164 THR BBB OG1 
2747  C CG2 . THR B 165 ? 2.822 1.753 2.276 -0.065 -0.453 -0.234 164 THR BBB CG2 
2748  N N   . SER B 166 ? 2.805 1.755 2.223 -0.090 -0.423 -0.114 165 SER BBB N   
2749  C CA  . SER B 166 ? 2.802 1.745 2.196 -0.088 -0.423 -0.082 165 SER BBB CA  
2750  C C   . SER B 166 ? 2.728 1.727 2.106 -0.070 -0.409 -0.089 165 SER BBB C   
2751  O O   . SER B 166 ? 2.676 1.714 2.039 -0.087 -0.387 -0.079 165 SER BBB O   
2752  C CB  . SER B 166 ? 2.821 1.758 2.207 -0.125 -0.413 -0.045 165 SER BBB CB  
2753  O OG  . SER B 166 ? 2.825 1.723 2.235 -0.150 -0.423 -0.042 165 SER BBB OG  
2754  N N   . GLY B 167 ? 2.696 1.698 2.078 -0.038 -0.419 -0.108 166 GLY BBB N   
2755  C CA  . GLY B 167 ? 2.658 1.705 2.027 -0.021 -0.413 -0.112 166 GLY BBB CA  
2756  C C   . GLY B 167 ? 2.598 1.696 1.974 -0.020 -0.393 -0.138 166 GLY BBB C   
2757  O O   . GLY B 167 ? 2.558 1.689 1.914 -0.031 -0.377 -0.133 166 GLY BBB O   
2758  N N   . VAL B 168 ? 2.595 1.697 1.994 -0.006 -0.393 -0.166 167 VAL BBB N   
2759  C CA  . VAL B 168 ? 2.554 1.701 1.962 -0.005 -0.374 -0.187 167 VAL BBB CA  
2760  C C   . VAL B 168 ? 2.528 1.698 1.946 0.024  -0.375 -0.210 167 VAL BBB C   
2761  O O   . VAL B 168 ? 2.549 1.696 1.978 0.043  -0.388 -0.224 167 VAL BBB O   
2762  C CB  . VAL B 168 ? 2.557 1.700 1.981 -0.019 -0.372 -0.196 167 VAL BBB CB  
2763  C CG1 . VAL B 168 ? 2.498 1.691 1.930 -0.020 -0.351 -0.208 167 VAL BBB CG1 
2764  C CG2 . VAL B 168 ? 2.609 1.727 2.032 -0.049 -0.374 -0.172 167 VAL BBB CG2 
2765  N N   . HIS B 169 ? 2.505 1.717 1.918 0.027  -0.361 -0.212 168 HIS BBB N   
2766  C CA  . HIS B 169 ? 2.487 1.731 1.912 0.050  -0.357 -0.229 168 HIS BBB CA  
2767  C C   . HIS B 169 ? 2.439 1.714 1.869 0.048  -0.338 -0.244 168 HIS BBB C   
2768  O O   . HIS B 169 ? 2.393 1.681 1.814 0.031  -0.321 -0.237 168 HIS BBB O   
2769  C CB  . HIS B 169 ? 2.509 1.776 1.927 0.050  -0.358 -0.218 168 HIS BBB CB  
2770  C CG  . HIS B 169 ? 2.592 1.836 2.000 0.047  -0.378 -0.197 168 HIS BBB CG  
2771  N ND1 . HIS B 169 ? 2.656 1.870 2.041 0.026  -0.381 -0.178 168 HIS BBB ND1 
2772  C CD2 . HIS B 169 ? 2.626 1.877 2.045 0.064  -0.396 -0.188 168 HIS BBB CD2 
2773  C CE1 . HIS B 169 ? 2.685 1.884 2.062 0.029  -0.400 -0.157 168 HIS BBB CE1 
2774  N NE2 . HIS B 169 ? 2.673 1.896 2.073 0.053  -0.411 -0.163 168 HIS BBB NE2 
2775  N N   . THR B 170 ? 2.451 1.735 1.894 0.067  -0.338 -0.263 169 THR BBB N   
2776  C CA  . THR B 170 ? 2.434 1.750 1.881 0.070  -0.322 -0.275 169 THR BBB CA  
2777  C C   . THR B 170 ? 2.392 1.738 1.846 0.092  -0.316 -0.285 169 THR BBB C   
2778  O O   . THR B 170 ? 2.408 1.748 1.867 0.114  -0.324 -0.298 169 THR BBB O   
2779  C CB  . THR B 170 ? 2.485 1.787 1.933 0.067  -0.330 -0.286 169 THR BBB CB  
2780  O OG1 . THR B 170 ? 2.527 1.819 1.976 0.041  -0.329 -0.271 169 THR BBB OG1 
2781  C CG2 . THR B 170 ? 2.467 1.803 1.917 0.077  -0.320 -0.299 169 THR BBB CG2 
2782  N N   . PHE B 171 ? 2.336 1.714 1.791 0.087  -0.299 -0.279 170 PHE BBB N   
2783  C CA  . PHE B 171 ? 2.305 1.715 1.771 0.100  -0.292 -0.280 170 PHE BBB CA  
2784  C C   . PHE B 171 ? 2.278 1.713 1.749 0.119  -0.282 -0.293 170 PHE BBB C   
2785  O O   . PHE B 171 ? 2.275 1.705 1.737 0.118  -0.280 -0.300 170 PHE BBB O   
2786  C CB  . PHE B 171 ? 2.296 1.720 1.757 0.081  -0.279 -0.269 170 PHE BBB CB  
2787  C CG  . PHE B 171 ? 2.327 1.729 1.774 0.063  -0.289 -0.258 170 PHE BBB CG  
2788  C CD1 . PHE B 171 ? 2.351 1.761 1.805 0.065  -0.304 -0.252 170 PHE BBB CD1 
2789  C CD2 . PHE B 171 ? 2.344 1.722 1.771 0.045  -0.283 -0.252 170 PHE BBB CD2 
2790  C CE1 . PHE B 171 ? 2.387 1.779 1.823 0.048  -0.316 -0.240 170 PHE BBB CE1 
2791  C CE2 . PHE B 171 ? 2.381 1.740 1.788 0.029  -0.291 -0.242 170 PHE BBB CE2 
2792  C CZ  . PHE B 171 ? 2.402 1.766 1.811 0.030  -0.309 -0.236 170 PHE BBB CZ  
2793  N N   . PRO B 172 ? 2.270 1.736 1.755 0.135  -0.276 -0.295 171 PRO BBB N   
2794  C CA  . PRO B 172 ? 2.263 1.760 1.749 0.152  -0.262 -0.303 171 PRO BBB CA  
2795  C C   . PRO B 172 ? 2.229 1.738 1.707 0.137  -0.246 -0.294 171 PRO BBB C   
2796  O O   . PRO B 172 ? 2.228 1.730 1.707 0.118  -0.241 -0.282 171 PRO BBB O   
2797  C CB  . PRO B 172 ? 2.264 1.800 1.773 0.164  -0.255 -0.298 171 PRO BBB CB  
2798  C CG  . PRO B 172 ? 2.281 1.802 1.803 0.164  -0.273 -0.293 171 PRO BBB CG  
2799  C CD  . PRO B 172 ? 2.282 1.761 1.785 0.140  -0.284 -0.287 171 PRO BBB CD  
2800  N N   . ALA B 173 ? 2.229 1.753 1.697 0.148  -0.238 -0.300 172 ALA BBB N   
2801  C CA  . ALA B 173 ? 2.221 1.761 1.685 0.141  -0.221 -0.287 172 ALA BBB CA  
2802  C C   . ALA B 173 ? 2.211 1.778 1.688 0.139  -0.204 -0.275 172 ALA BBB C   
2803  O O   . ALA B 173 ? 2.184 1.774 1.674 0.152  -0.203 -0.279 172 ALA BBB O   
2804  C CB  . ALA B 173 ? 2.254 1.806 1.701 0.153  -0.222 -0.294 172 ALA BBB CB  
2805  N N   . VAL B 174 ? 2.240 1.804 1.719 0.125  -0.190 -0.260 173 VAL BBB N   
2806  C CA  . VAL B 174 ? 2.282 1.866 1.773 0.118  -0.173 -0.247 173 VAL BBB CA  
2807  C C   . VAL B 174 ? 2.303 1.892 1.786 0.121  -0.156 -0.233 173 VAL BBB C   
2808  O O   . VAL B 174 ? 2.324 1.891 1.798 0.118  -0.156 -0.230 173 VAL BBB O   
2809  C CB  . VAL B 174 ? 2.293 1.856 1.791 0.093  -0.175 -0.242 173 VAL BBB CB  
2810  C CG1 . VAL B 174 ? 2.302 1.873 1.812 0.092  -0.193 -0.249 173 VAL BBB CG1 
2811  C CG2 . VAL B 174 ? 2.287 1.808 1.767 0.080  -0.174 -0.242 173 VAL BBB CG2 
2812  N N   . LEU B 175 ? 2.314 1.935 1.801 0.129  -0.141 -0.222 174 LEU BBB N   
2813  C CA  . LEU B 175 ? 2.322 1.950 1.799 0.135  -0.125 -0.204 174 LEU BBB CA  
2814  C C   . LEU B 175 ? 2.307 1.909 1.793 0.115  -0.110 -0.187 174 LEU BBB C   
2815  O O   . LEU B 175 ? 2.312 1.924 1.813 0.102  -0.101 -0.178 174 LEU BBB O   
2816  C CB  . LEU B 175 ? 2.348 2.021 1.822 0.151  -0.115 -0.198 174 LEU BBB CB  
2817  C CG  . LEU B 175 ? 2.374 2.060 1.836 0.157  -0.097 -0.174 174 LEU BBB CG  
2818  C CD1 . LEU B 175 ? 2.385 2.062 1.827 0.167  -0.106 -0.173 174 LEU BBB CD1 
2819  C CD2 . LEU B 175 ? 2.399 2.133 1.854 0.171  -0.084 -0.167 174 LEU BBB CD2 
2820  N N   . GLN B 176 ? 2.288 1.855 1.767 0.112  -0.107 -0.182 175 GLN BBB N   
2821  C CA  . GLN B 176 ? 2.305 1.834 1.785 0.097  -0.090 -0.169 175 GLN BBB CA  
2822  C C   . GLN B 176 ? 2.328 1.870 1.812 0.099  -0.071 -0.144 175 GLN BBB C   
2823  O O   . GLN B 176 ? 2.334 1.918 1.815 0.117  -0.071 -0.136 175 GLN BBB O   
2824  C CB  . GLN B 176 ? 2.313 1.812 1.786 0.105  -0.086 -0.166 175 GLN BBB CB  
2825  C CG  . GLN B 176 ? 2.295 1.769 1.763 0.095  -0.096 -0.184 175 GLN BBB CG  
2826  C CD  . GLN B 176 ? 2.281 1.751 1.750 0.109  -0.095 -0.181 175 GLN BBB CD  
2827  O OE1 . GLN B 176 ? 2.292 1.728 1.757 0.106  -0.082 -0.179 175 GLN BBB OE1 
2828  N NE2 . GLN B 176 ? 2.247 1.754 1.720 0.123  -0.109 -0.180 175 GLN BBB NE2 
2829  N N   . SER B 177 ? 2.357 1.860 1.844 0.082  -0.055 -0.133 176 SER BBB N   
2830  C CA  . SER B 177 ? 2.384 1.883 1.875 0.081  -0.034 -0.104 176 SER BBB CA  
2831  C C   . SER B 177 ? 2.369 1.884 1.851 0.110  -0.030 -0.085 176 SER BBB C   
2832  O O   . SER B 177 ? 2.371 1.918 1.851 0.119  -0.021 -0.063 176 SER BBB O   
2833  C CB  . SER B 177 ? 2.429 1.862 1.918 0.060  -0.020 -0.099 176 SER BBB CB  
2834  O OG  . SER B 177 ? 2.430 1.820 1.906 0.065  -0.021 -0.114 176 SER BBB OG  
2835  N N   . SER B 178 ? 2.345 1.846 1.822 0.124  -0.036 -0.093 177 SER BBB N   
2836  C CA  . SER B 178 ? 2.339 1.858 1.812 0.150  -0.037 -0.075 177 SER BBB CA  
2837  C C   . SER B 178 ? 2.315 1.894 1.778 0.164  -0.049 -0.071 177 SER BBB C   
2838  O O   . SER B 178 ? 2.333 1.933 1.789 0.183  -0.048 -0.048 177 SER BBB O   
2839  C CB  . SER B 178 ? 2.329 1.838 1.807 0.158  -0.047 -0.088 177 SER BBB CB  
2840  O OG  . SER B 178 ? 2.292 1.815 1.767 0.149  -0.067 -0.117 177 SER BBB OG  
2841  N N   . GLY B 179 ? 2.295 1.900 1.754 0.157  -0.059 -0.092 178 GLY BBB N   
2842  C CA  . GLY B 179 ? 2.296 1.952 1.737 0.172  -0.068 -0.096 178 GLY BBB CA  
2843  C C   . GLY B 179 ? 2.278 1.947 1.709 0.182  -0.093 -0.119 178 GLY BBB C   
2844  O O   . GLY B 179 ? 2.268 1.973 1.676 0.195  -0.103 -0.124 178 GLY BBB O   
2845  N N   . LEU B 180 ? 2.271 1.910 1.715 0.173  -0.102 -0.131 179 LEU BBB N   
2846  C CA  . LEU B 180 ? 2.262 1.905 1.703 0.175  -0.125 -0.153 179 LEU BBB CA  
2847  C C   . LEU B 180 ? 2.264 1.880 1.714 0.160  -0.132 -0.177 179 LEU BBB C   
2848  O O   . LEU B 180 ? 2.269 1.857 1.730 0.146  -0.120 -0.174 179 LEU BBB O   
2849  C CB  . LEU B 180 ? 2.240 1.877 1.694 0.179  -0.127 -0.138 179 LEU BBB CB  
2850  C CG  . LEU B 180 ? 2.252 1.905 1.707 0.194  -0.115 -0.105 179 LEU BBB CG  
2851  C CD1 . LEU B 180 ? 2.247 1.901 1.724 0.202  -0.117 -0.091 179 LEU BBB CD1 
2852  C CD2 . LEU B 180 ? 2.277 1.975 1.706 0.207  -0.126 -0.099 179 LEU BBB CD2 
2853  N N   . TYR B 181 ? 2.267 1.890 1.711 0.161  -0.153 -0.201 180 TYR BBB N   
2854  C CA  . TYR B 181 ? 2.252 1.852 1.701 0.149  -0.164 -0.221 180 TYR BBB CA  
2855  C C   . TYR B 181 ? 2.244 1.815 1.704 0.136  -0.166 -0.221 180 TYR BBB C   
2856  O O   . TYR B 181 ? 2.241 1.816 1.706 0.139  -0.166 -0.210 180 TYR BBB O   
2857  C CB  . TYR B 181 ? 2.253 1.862 1.689 0.158  -0.184 -0.245 180 TYR BBB CB  
2858  C CG  . TYR B 181 ? 2.270 1.906 1.691 0.174  -0.178 -0.250 180 TYR BBB CG  
2859  C CD1 . TYR B 181 ? 2.254 1.898 1.687 0.175  -0.167 -0.251 180 TYR BBB CD1 
2860  C CD2 . TYR B 181 ? 2.310 1.969 1.705 0.188  -0.183 -0.254 180 TYR BBB CD2 
2861  C CE1 . TYR B 181 ? 2.277 1.954 1.700 0.192  -0.157 -0.254 180 TYR BBB CE1 
2862  C CE2 . TYR B 181 ? 2.340 2.026 1.716 0.204  -0.174 -0.260 180 TYR BBB CE2 
2863  C CZ  . TYR B 181 ? 2.326 2.021 1.717 0.207  -0.159 -0.260 180 TYR BBB CZ  
2864  O OH  . TYR B 181 ? 2.363 2.090 1.737 0.226  -0.145 -0.264 180 TYR BBB OH  
2865  N N   . SER B 182 ? 2.251 1.798 1.715 0.123  -0.168 -0.230 181 SER BBB N   
2866  C CA  . SER B 182 ? 2.265 1.783 1.731 0.109  -0.172 -0.233 181 SER BBB CA  
2867  C C   . SER B 182 ? 2.263 1.768 1.726 0.102  -0.190 -0.249 181 SER BBB C   
2868  O O   . SER B 182 ? 2.251 1.767 1.716 0.107  -0.193 -0.255 181 SER BBB O   
2869  C CB  . SER B 182 ? 2.290 1.783 1.756 0.100  -0.152 -0.223 181 SER BBB CB  
2870  O OG  . SER B 182 ? 2.297 1.763 1.757 0.086  -0.154 -0.229 181 SER BBB OG  
2871  N N   . LEU B 183 ? 2.266 1.753 1.729 0.093  -0.200 -0.252 182 LEU BBB N   
2872  C CA  . LEU B 183 ? 2.278 1.749 1.738 0.089  -0.220 -0.263 182 LEU BBB CA  
2873  C C   . LEU B 183 ? 2.266 1.713 1.723 0.072  -0.222 -0.258 182 LEU BBB C   
2874  O O   . LEU B 183 ? 2.264 1.717 1.728 0.070  -0.219 -0.252 182 LEU BBB O   
2875  C CB  . LEU B 183 ? 2.314 1.795 1.772 0.101  -0.236 -0.275 182 LEU BBB CB  
2876  C CG  . LEU B 183 ? 2.362 1.818 1.818 0.099  -0.258 -0.287 182 LEU BBB CG  
2877  C CD1 . LEU B 183 ? 2.391 1.852 1.839 0.117  -0.269 -0.305 182 LEU BBB CD1 
2878  C CD2 . LEU B 183 ? 2.371 1.811 1.831 0.082  -0.266 -0.282 182 LEU BBB CD2 
2879  N N   . SER B 184 ? 2.274 1.701 1.722 0.062  -0.227 -0.258 183 SER BBB N   
2880  C CA  . SER B 184 ? 2.311 1.714 1.748 0.046  -0.227 -0.251 183 SER BBB CA  
2881  C C   . SER B 184 ? 2.337 1.724 1.776 0.043  -0.250 -0.254 183 SER BBB C   
2882  O O   . SER B 184 ? 2.377 1.764 1.820 0.054  -0.265 -0.263 183 SER BBB O   
2883  C CB  . SER B 184 ? 2.332 1.719 1.750 0.034  -0.220 -0.249 183 SER BBB CB  
2884  O OG  . SER B 184 ? 2.318 1.713 1.736 0.037  -0.202 -0.250 183 SER BBB OG  
2885  N N   . SER B 185 ? 2.337 1.710 1.774 0.029  -0.252 -0.245 184 SER BBB N   
2886  C CA  . SER B 185 ? 2.335 1.684 1.772 0.021  -0.272 -0.242 184 SER BBB CA  
2887  C C   . SER B 185 ? 2.361 1.693 1.783 0.002  -0.265 -0.226 184 SER BBB C   
2888  O O   . SER B 185 ? 2.372 1.718 1.796 -0.005 -0.245 -0.218 184 SER BBB O   
2889  C CB  . SER B 185 ? 2.326 1.678 1.780 0.020  -0.283 -0.247 184 SER BBB CB  
2890  O OG  . SER B 185 ? 2.323 1.643 1.776 0.007  -0.300 -0.241 184 SER BBB OG  
2891  N N   . VAL B 186 ? 2.401 1.707 1.807 -0.004 -0.280 -0.219 185 VAL BBB N   
2892  C CA  . VAL B 186 ? 2.432 1.723 1.812 -0.022 -0.273 -0.202 185 VAL BBB CA  
2893  C C   . VAL B 186 ? 2.460 1.720 1.838 -0.030 -0.294 -0.189 185 VAL BBB C   
2894  O O   . VAL B 186 ? 2.505 1.751 1.896 -0.017 -0.316 -0.196 185 VAL BBB O   
2895  C CB  . VAL B 186 ? 2.439 1.732 1.792 -0.022 -0.267 -0.205 185 VAL BBB CB  
2896  C CG1 . VAL B 186 ? 2.419 1.729 1.771 -0.018 -0.242 -0.215 185 VAL BBB CG1 
2897  C CG2 . VAL B 186 ? 2.442 1.735 1.802 -0.009 -0.291 -0.210 185 VAL BBB CG2 
2898  N N   . VAL B 187 ? 2.461 1.709 1.820 -0.049 -0.287 -0.169 186 VAL BBB N   
2899  C CA  . VAL B 187 ? 2.494 1.709 1.847 -0.060 -0.305 -0.149 186 VAL BBB CA  
2900  C C   . VAL B 187 ? 2.521 1.727 1.833 -0.075 -0.298 -0.128 186 VAL BBB C   
2901  O O   . VAL B 187 ? 2.530 1.754 1.823 -0.084 -0.271 -0.126 186 VAL BBB O   
2902  C CB  . VAL B 187 ? 2.517 1.728 1.897 -0.075 -0.304 -0.141 186 VAL BBB CB  
2903  C CG1 . VAL B 187 ? 2.497 1.743 1.885 -0.087 -0.274 -0.135 186 VAL BBB CG1 
2904  C CG2 . VAL B 187 ? 2.587 1.758 1.960 -0.092 -0.320 -0.116 186 VAL BBB CG2 
2905  N N   . THR B 188 ? 2.543 1.722 1.837 -0.075 -0.321 -0.113 187 THR BBB N   
2906  C CA  . THR B 188 ? 2.578 1.747 1.826 -0.089 -0.320 -0.090 187 THR BBB CA  
2907  C C   . THR B 188 ? 2.627 1.778 1.871 -0.110 -0.313 -0.062 187 THR BBB C   
2908  O O   . THR B 188 ? 2.649 1.773 1.922 -0.111 -0.330 -0.054 187 THR BBB O   
2909  C CB  . THR B 188 ? 2.590 1.744 1.827 -0.078 -0.352 -0.081 187 THR BBB CB  
2910  O OG1 . THR B 188 ? 2.517 1.686 1.787 -0.055 -0.363 -0.104 187 THR BBB OG1 
2911  C CG2 . THR B 188 ? 2.626 1.789 1.810 -0.088 -0.352 -0.071 187 THR BBB CG2 
2912  N N   . VAL B 189 ? 2.661 1.824 1.870 -0.127 -0.286 -0.050 188 VAL BBB N   
2913  C CA  . VAL B 189 ? 2.704 1.861 1.911 -0.149 -0.271 -0.020 188 VAL BBB CA  
2914  C C   . VAL B 189 ? 2.791 1.943 1.933 -0.162 -0.260 0.002  188 VAL BBB C   
2915  O O   . VAL B 189 ? 2.827 1.990 1.928 -0.157 -0.249 -0.013 188 VAL BBB O   
2916  C CB  . VAL B 189 ? 2.655 1.846 1.897 -0.155 -0.241 -0.028 188 VAL BBB CB  
2917  C CG1 . VAL B 189 ? 2.599 1.794 1.899 -0.146 -0.256 -0.047 188 VAL BBB CG1 
2918  C CG2 . VAL B 189 ? 2.645 1.865 1.862 -0.146 -0.208 -0.046 188 VAL BBB CG2 
2919  N N   . PRO B 190 ? 2.849 1.980 1.976 -0.181 -0.263 0.039  189 PRO BBB N   
2920  C CA  . PRO B 190 ? 2.922 2.050 1.980 -0.195 -0.250 0.064  189 PRO BBB CA  
2921  C C   . PRO B 190 ? 2.929 2.090 1.959 -0.199 -0.204 0.052  189 PRO BBB C   
2922  O O   . PRO B 190 ? 2.898 2.084 1.972 -0.200 -0.179 0.047  189 PRO BBB O   
2923  C CB  . PRO B 190 ? 2.967 2.072 2.033 -0.216 -0.254 0.108  189 PRO BBB CB  
2924  C CG  . PRO B 190 ? 2.937 2.013 2.063 -0.208 -0.287 0.104  189 PRO BBB CG  
2925  C CD  . PRO B 190 ? 2.852 1.954 2.021 -0.190 -0.282 0.060  189 PRO BBB CD  
2926  N N   . SER B 191 ? 2.970 2.129 1.926 -0.200 -0.195 0.048  190 SER BBB N   
2927  C CA  . SER B 191 ? 2.978 2.156 1.891 -0.200 -0.150 0.030  190 SER BBB CA  
2928  C C   . SER B 191 ? 2.945 2.152 1.895 -0.206 -0.110 0.045  190 SER BBB C   
2929  O O   . SER B 191 ? 2.906 2.138 1.899 -0.193 -0.087 0.023  190 SER BBB O   
2930  C CB  . SER B 191 ? 3.067 2.231 1.883 -0.210 -0.147 0.038  190 SER BBB CB  
2931  O OG  . SER B 191 ? 3.080 2.234 1.864 -0.202 -0.169 0.007  190 SER BBB OG  
2932  N N   . SER B 192 ? 2.958 2.164 1.899 -0.226 -0.102 0.086  191 SER BBB N   
2933  C CA  . SER B 192 ? 2.957 2.197 1.920 -0.237 -0.058 0.108  191 SER BBB CA  
2934  C C   . SER B 192 ? 2.893 2.155 1.956 -0.242 -0.065 0.115  191 SER BBB C   
2935  O O   . SER B 192 ? 2.875 2.170 1.970 -0.257 -0.037 0.142  191 SER BBB O   
2936  C CB  . SER B 192 ? 3.040 2.272 1.950 -0.259 -0.048 0.152  191 SER BBB CB  
2937  O OG  . SER B 192 ? 3.054 2.249 1.972 -0.271 -0.093 0.178  191 SER BBB OG  
2938  N N   . SER B 193 ? 2.861 2.108 1.970 -0.231 -0.102 0.092  192 SER BBB N   
2939  C CA  . SER B 193 ? 2.823 2.085 2.018 -0.235 -0.115 0.091  192 SER BBB CA  
2940  C C   . SER B 193 ? 2.797 2.114 2.035 -0.223 -0.080 0.074  192 SER BBB C   
2941  O O   . SER B 193 ? 2.768 2.117 2.070 -0.237 -0.074 0.089  192 SER BBB O   
2942  C CB  . SER B 193 ? 2.775 2.005 1.994 -0.223 -0.161 0.068  192 SER BBB CB  
2943  O OG  . SER B 193 ? 2.807 1.990 1.986 -0.226 -0.191 0.083  192 SER BBB OG  
2944  N N   . LEU B 194 ? 2.815 2.137 2.019 -0.200 -0.060 0.044  193 LEU BBB N   
2945  C CA  . LEU B 194 ? 2.787 2.151 2.027 -0.180 -0.030 0.024  193 LEU BBB CA  
2946  C C   . LEU B 194 ? 2.813 2.228 2.079 -0.188 0.016  0.051  193 LEU BBB C   
2947  O O   . LEU B 194 ? 2.765 2.228 2.101 -0.181 0.029  0.051  193 LEU BBB O   
2948  C CB  . LEU B 194 ? 2.807 2.153 1.989 -0.157 -0.014 -0.008 193 LEU BBB CB  
2949  C CG  . LEU B 194 ? 2.822 2.122 1.964 -0.153 -0.053 -0.030 193 LEU BBB CG  
2950  C CD1 . LEU B 194 ? 2.856 2.138 1.935 -0.139 -0.033 -0.058 193 LEU BBB CD1 
2951  C CD2 . LEU B 194 ? 2.762 2.064 1.964 -0.144 -0.087 -0.045 193 LEU BBB CD2 
2952  N N   . GLY B 195 ? 2.892 2.299 2.103 -0.202 0.039  0.075  194 GLY BBB N   
2953  C CA  . GLY B 195 ? 2.942 2.398 2.161 -0.207 0.090  0.102  194 GLY BBB CA  
2954  C C   . GLY B 195 ? 2.935 2.446 2.251 -0.225 0.091  0.130  194 GLY BBB C   
2955  O O   . GLY B 195 ? 2.944 2.514 2.292 -0.220 0.137  0.147  194 GLY BBB O   
2956  N N   . THR B 196 ? 2.941 2.434 2.303 -0.244 0.043  0.136  195 THR BBB N   
2957  C CA  . THR B 196 ? 2.928 2.466 2.384 -0.267 0.032  0.159  195 THR BBB CA  
2958  C C   . THR B 196 ? 2.853 2.371 2.351 -0.264 -0.018 0.132  195 THR BBB C   
2959  O O   . THR B 196 ? 2.799 2.361 2.349 -0.248 -0.015 0.116  195 THR BBB O   
2960  C CB  . THR B 196 ? 3.005 2.534 2.465 -0.308 0.026  0.203  195 THR BBB CB  
2961  O OG1 . THR B 196 ? 3.052 2.504 2.457 -0.314 -0.013 0.200  195 THR BBB OG1 
2962  C CG2 . THR B 196 ? 3.063 2.629 2.494 -0.314 0.080  0.236  195 THR BBB CG2 
2963  N N   . GLN B 197 ? 2.845 2.297 2.318 -0.276 -0.062 0.128  196 GLN BBB N   
2964  C CA  . GLN B 197 ? 2.791 2.216 2.300 -0.278 -0.111 0.106  196 GLN BBB CA  
2965  C C   . GLN B 197 ? 2.707 2.161 2.238 -0.247 -0.110 0.070  196 GLN BBB C   
2966  O O   . GLN B 197 ? 2.685 2.124 2.169 -0.219 -0.099 0.047  196 GLN BBB O   
2967  C CB  . GLN B 197 ? 2.826 2.173 2.284 -0.276 -0.147 0.098  196 GLN BBB CB  
2968  C CG  . GLN B 197 ? 2.812 2.126 2.298 -0.270 -0.191 0.070  196 GLN BBB CG  
2969  C CD  . GLN B 197 ? 2.841 2.158 2.387 -0.302 -0.213 0.082  196 GLN BBB CD  
2970  O OE1 . GLN B 197 ? 2.887 2.214 2.454 -0.334 -0.204 0.118  196 GLN BBB OE1 
2971  N NE2 . GLN B 197 ? 2.824 2.131 2.397 -0.294 -0.243 0.052  196 GLN BBB NE2 
2972  N N   . THR B 198 ? 2.659 2.153 2.259 -0.255 -0.123 0.068  197 THR BBB N   
2973  C CA  . THR B 198 ? 2.585 2.106 2.212 -0.229 -0.131 0.038  197 THR BBB CA  
2974  C C   . THR B 198 ? 2.571 2.031 2.161 -0.213 -0.166 0.004  197 THR BBB C   
2975  O O   . THR B 198 ? 2.591 1.997 2.165 -0.228 -0.196 0.006  197 THR BBB O   
2976  C CB  . THR B 198 ? 2.549 2.122 2.254 -0.248 -0.148 0.045  197 THR BBB CB  
2977  O OG1 . THR B 198 ? 2.561 2.195 2.309 -0.268 -0.118 0.082  197 THR BBB OG1 
2978  C CG2 . THR B 198 ? 2.497 2.107 2.227 -0.220 -0.151 0.022  197 THR BBB CG2 
2979  N N   . TYR B 199 ? 2.526 1.997 2.107 -0.181 -0.160 -0.022 198 TYR BBB N   
2980  C CA  . TYR B 199 ? 2.506 1.938 2.065 -0.162 -0.190 -0.054 198 TYR BBB CA  
2981  C C   . TYR B 199 ? 2.454 1.929 2.047 -0.143 -0.189 -0.071 198 TYR BBB C   
2982  O O   . TYR B 199 ? 2.435 1.929 2.017 -0.119 -0.163 -0.078 198 TYR BBB O   
2983  C CB  . TYR B 199 ? 2.527 1.918 2.023 -0.145 -0.182 -0.065 198 TYR BBB CB  
2984  C CG  . TYR B 199 ? 2.585 1.932 2.045 -0.163 -0.191 -0.048 198 TYR BBB CG  
2985  C CD1 . TYR B 199 ? 2.611 1.911 2.067 -0.170 -0.228 -0.051 198 TYR BBB CD1 
2986  C CD2 . TYR B 199 ? 2.626 1.977 2.052 -0.171 -0.161 -0.027 198 TYR BBB CD2 
2987  C CE1 . TYR B 199 ? 2.674 1.932 2.098 -0.184 -0.237 -0.029 198 TYR BBB CE1 
2988  C CE2 . TYR B 199 ? 2.687 1.999 2.075 -0.187 -0.171 -0.006 198 TYR BBB CE2 
2989  C CZ  . TYR B 199 ? 2.709 1.975 2.100 -0.194 -0.210 -0.005 198 TYR BBB CZ  
2990  O OH  . TYR B 199 ? 2.778 2.004 2.134 -0.207 -0.220 0.019  198 TYR BBB OH  
2991  N N   . ILE B 200 ? 2.442 1.930 2.074 -0.156 -0.219 -0.075 199 ILE BBB N   
2992  C CA  . ILE B 200 ? 2.403 1.925 2.061 -0.139 -0.230 -0.093 199 ILE BBB CA  
2993  C C   . ILE B 200 ? 2.399 1.872 2.022 -0.124 -0.257 -0.123 199 ILE BBB C   
2994  O O   . ILE B 200 ? 2.422 1.842 2.023 -0.136 -0.278 -0.128 199 ILE BBB O   
2995  C CB  . ILE B 200 ? 2.402 1.969 2.117 -0.165 -0.249 -0.080 199 ILE BBB CB  
2996  C CG1 . ILE B 200 ? 2.388 2.024 2.150 -0.172 -0.217 -0.048 199 ILE BBB CG1 
2997  C CG2 . ILE B 200 ? 2.383 1.970 2.110 -0.153 -0.274 -0.102 199 ILE BBB CG2 
2998  C CD1 . ILE B 200 ? 2.391 2.076 2.216 -0.206 -0.237 -0.029 199 ILE BBB CD1 
2999  N N   . CYS B 201 ? 2.377 1.869 1.997 -0.098 -0.256 -0.141 200 CYS BBB N   
3000  C CA  . CYS B 201 ? 2.403 1.863 1.998 -0.083 -0.280 -0.169 200 CYS BBB CA  
3001  C C   . CYS B 201 ? 2.395 1.892 2.015 -0.081 -0.298 -0.178 200 CYS BBB C   
3002  O O   . CYS B 201 ? 2.374 1.925 2.020 -0.072 -0.281 -0.166 200 CYS BBB O   
3003  C CB  . CYS B 201 ? 2.410 1.853 1.970 -0.057 -0.262 -0.179 200 CYS BBB CB  
3004  S SG  . CYS B 201 ? 2.408 1.889 1.973 -0.028 -0.250 -0.189 200 CYS BBB SG  
3005  N N   . ASN B 202 ? 2.432 1.900 2.041 -0.088 -0.330 -0.198 201 ASN BBB N   
3006  C CA  . ASN B 202 ? 2.455 1.950 2.076 -0.091 -0.355 -0.212 201 ASN BBB CA  
3007  C C   . ASN B 202 ? 2.447 1.928 2.032 -0.061 -0.358 -0.238 201 ASN BBB C   
3008  O O   . ASN B 202 ? 2.454 1.882 2.008 -0.053 -0.367 -0.256 201 ASN BBB O   
3009  C CB  . ASN B 202 ? 2.513 1.980 2.142 -0.124 -0.389 -0.219 201 ASN BBB CB  
3010  C CG  . ASN B 202 ? 2.530 1.998 2.189 -0.156 -0.384 -0.192 201 ASN BBB CG  
3011  O OD1 . ASN B 202 ? 2.553 1.979 2.197 -0.157 -0.372 -0.183 201 ASN BBB OD1 
3012  N ND2 . ASN B 202 ? 2.531 2.048 2.236 -0.183 -0.394 -0.176 201 ASN BBB ND2 
3013  N N   . VAL B 203 ? 2.432 1.962 2.024 -0.043 -0.351 -0.235 202 VAL BBB N   
3014  C CA  . VAL B 203 ? 2.443 1.969 2.002 -0.014 -0.346 -0.253 202 VAL BBB CA  
3015  C C   . VAL B 203 ? 2.465 2.023 2.020 -0.012 -0.368 -0.263 202 VAL BBB C   
3016  O O   . VAL B 203 ? 2.438 2.051 2.024 -0.016 -0.368 -0.243 202 VAL BBB O   
3017  C CB  . VAL B 203 ? 2.422 1.970 1.986 0.008  -0.311 -0.236 202 VAL BBB CB  
3018  C CG1 . VAL B 203 ? 2.419 1.965 1.954 0.034  -0.305 -0.250 202 VAL BBB CG1 
3019  C CG2 . VAL B 203 ? 2.418 1.937 1.979 0.003  -0.291 -0.227 202 VAL BBB CG2 
3020  N N   . ASN B 204 ? 2.526 2.054 2.042 -0.003 -0.385 -0.292 203 ASN BBB N   
3021  C CA  . ASN B 204 ? 2.560 2.109 2.056 -0.001 -0.408 -0.308 203 ASN BBB CA  
3022  C C   . ASN B 204 ? 2.526 2.081 1.987 0.032  -0.393 -0.319 203 ASN BBB C   
3023  O O   . ASN B 204 ? 2.516 2.032 1.956 0.047  -0.381 -0.333 203 ASN BBB O   
3024  C CB  . ASN B 204 ? 2.649 2.153 2.123 -0.022 -0.442 -0.337 203 ASN BBB CB  
3025  C CG  . ASN B 204 ? 2.689 2.177 2.198 -0.058 -0.455 -0.325 203 ASN BBB CG  
3026  O OD1 . ASN B 204 ? 2.690 2.224 2.244 -0.070 -0.445 -0.295 203 ASN BBB OD1 
3027  N ND2 . ASN B 204 ? 2.743 2.165 2.233 -0.073 -0.474 -0.348 203 ASN BBB ND2 
3028  N N   . HIS B 205 ? 2.495 2.101 1.952 0.042  -0.395 -0.310 204 HIS BBB N   
3029  C CA  . HIS B 205 ? 2.495 2.113 1.915 0.070  -0.383 -0.316 204 HIS BBB CA  
3030  C C   . HIS B 205 ? 2.557 2.193 1.943 0.065  -0.413 -0.334 204 HIS BBB C   
3031  O O   . HIS B 205 ? 2.560 2.245 1.966 0.054  -0.428 -0.315 204 HIS BBB O   
3032  C CB  . HIS B 205 ? 2.440 2.099 1.883 0.086  -0.355 -0.283 204 HIS BBB CB  
3033  C CG  . HIS B 205 ? 2.421 2.091 1.833 0.112  -0.338 -0.283 204 HIS BBB CG  
3034  N ND1 . HIS B 205 ? 2.398 2.113 1.812 0.126  -0.329 -0.258 204 HIS BBB ND1 
3035  C CD2 . HIS B 205 ? 2.418 2.063 1.800 0.127  -0.326 -0.301 204 HIS BBB CD2 
3036  C CE1 . HIS B 205 ? 2.393 2.108 1.777 0.145  -0.313 -0.260 204 HIS BBB CE1 
3037  N NE2 . HIS B 205 ? 2.403 2.078 1.769 0.147  -0.309 -0.287 204 HIS BBB NE2 
3038  N N   . LYS B 206 ? 2.622 2.222 1.958 0.075  -0.420 -0.369 205 LYS BBB N   
3039  C CA  . LYS B 206 ? 2.714 2.315 2.003 0.067  -0.452 -0.395 205 LYS BBB CA  
3040  C C   . LYS B 206 ? 2.705 2.371 1.979 0.082  -0.449 -0.375 205 LYS BBB C   
3041  O O   . LYS B 206 ? 2.727 2.433 2.005 0.065  -0.476 -0.366 205 LYS BBB O   
3042  C CB  . LYS B 206 ? 2.790 2.331 2.026 0.081  -0.453 -0.438 205 LYS BBB CB  
3043  C CG  . LYS B 206 ? 2.803 2.280 2.057 0.076  -0.448 -0.451 205 LYS BBB CG  
3044  C CD  . LYS B 206 ? 2.883 2.294 2.086 0.085  -0.459 -0.496 205 LYS BBB CD  
3045  C CE  . LYS B 206 ? 2.968 2.344 2.148 0.054  -0.499 -0.523 205 LYS BBB CE  
3046  N NZ  . LYS B 206 ? 3.052 2.347 2.185 0.064  -0.506 -0.568 205 LYS BBB NZ  
3047  N N   . PRO B 207 ? 2.669 2.348 1.927 0.111  -0.418 -0.364 206 PRO BBB N   
3048  C CA  . PRO B 207 ? 2.668 2.402 1.904 0.126  -0.414 -0.343 206 PRO BBB CA  
3049  C C   . PRO B 207 ? 2.627 2.418 1.906 0.115  -0.427 -0.305 206 PRO BBB C   
3050  O O   . PRO B 207 ? 2.688 2.523 1.942 0.117  -0.446 -0.297 206 PRO BBB O   
3051  C CB  . PRO B 207 ? 2.635 2.369 1.874 0.153  -0.373 -0.327 206 PRO BBB CB  
3052  C CG  . PRO B 207 ? 2.641 2.320 1.876 0.157  -0.362 -0.357 206 PRO BBB CG  
3053  C CD  . PRO B 207 ? 2.642 2.289 1.907 0.130  -0.385 -0.367 206 PRO BBB CD  
3054  N N   . SER B 208 ? 2.543 2.337 1.885 0.107  -0.415 -0.281 207 SER BBB N   
3055  C CA  . SER B 208 ? 2.509 2.358 1.904 0.102  -0.420 -0.241 207 SER BBB CA  
3056  C C   . SER B 208 ? 2.505 2.364 1.934 0.070  -0.451 -0.245 207 SER BBB C   
3057  O O   . SER B 208 ? 2.492 2.402 1.977 0.065  -0.453 -0.211 207 SER BBB O   
3058  C CB  . SER B 208 ? 2.455 2.302 1.892 0.118  -0.380 -0.211 207 SER BBB CB  
3059  O OG  . SER B 208 ? 2.423 2.228 1.888 0.105  -0.369 -0.221 207 SER BBB OG  
3060  N N   . ASN B 209 ? 2.513 2.329 1.916 0.048  -0.475 -0.283 208 ASN BBB N   
3061  C CA  . ASN B 209 ? 2.525 2.344 1.956 0.010  -0.510 -0.290 208 ASN BBB CA  
3062  C C   . ASN B 209 ? 2.465 2.317 1.974 0.002  -0.494 -0.253 208 ASN BBB C   
3063  O O   . ASN B 209 ? 2.441 2.355 1.992 -0.015 -0.516 -0.230 208 ASN BBB O   
3064  C CB  . ASN B 209 ? 2.586 2.451 1.991 -0.006 -0.553 -0.296 208 ASN BBB CB  
3065  C CG  . ASN B 209 ? 2.656 2.490 2.046 -0.046 -0.596 -0.330 208 ASN BBB CG  
3066  O OD1 . ASN B 209 ? 2.686 2.445 2.053 -0.054 -0.594 -0.362 208 ASN BBB OD1 
3067  N ND2 . ASN B 209 ? 2.692 2.582 2.090 -0.070 -0.636 -0.322 208 ASN BBB ND2 
3068  N N   . THR B 210 ? 2.437 2.253 1.963 0.014  -0.458 -0.246 209 THR BBB N   
3069  C CA  . THR B 210 ? 2.387 2.221 1.977 0.008  -0.436 -0.216 209 THR BBB CA  
3070  C C   . THR B 210 ? 2.386 2.156 1.975 -0.006 -0.425 -0.232 209 THR BBB C   
3071  O O   . THR B 210 ? 2.346 2.067 1.903 0.012  -0.404 -0.247 209 THR BBB O   
3072  C CB  . THR B 210 ? 2.332 2.189 1.940 0.041  -0.397 -0.186 209 THR BBB CB  
3073  O OG1 . THR B 210 ? 2.315 2.132 1.875 0.064  -0.378 -0.202 209 THR BBB OG1 
3074  C CG2 . THR B 210 ? 2.332 2.264 1.970 0.053  -0.404 -0.153 209 THR BBB CG2 
3075  N N   . LYS B 211 ? 2.426 2.201 2.054 -0.037 -0.438 -0.225 210 LYS BBB N   
3076  C CA  . LYS B 211 ? 2.453 2.182 2.095 -0.051 -0.424 -0.225 210 LYS BBB CA  
3077  C C   . LYS B 211 ? 2.424 2.186 2.108 -0.038 -0.386 -0.191 210 LYS BBB C   
3078  O O   . LYS B 211 ? 2.402 2.225 2.114 -0.023 -0.378 -0.168 210 LYS BBB O   
3079  C CB  . LYS B 211 ? 2.511 2.230 2.172 -0.094 -0.456 -0.231 210 LYS BBB CB  
3080  C CG  . LYS B 211 ? 2.519 2.199 2.199 -0.114 -0.443 -0.223 210 LYS BBB CG  
3081  C CD  . LYS B 211 ? 2.584 2.214 2.257 -0.152 -0.477 -0.242 210 LYS BBB CD  
3082  C CE  . LYS B 211 ? 2.612 2.293 2.323 -0.189 -0.512 -0.234 210 LYS BBB CE  
3083  N NZ  . LYS B 211 ? 2.585 2.316 2.364 -0.214 -0.501 -0.195 210 LYS BBB NZ  
3084  N N   . VAL B 212 ? 2.420 2.141 2.104 -0.041 -0.362 -0.189 211 VAL BBB N   
3085  C CA  . VAL B 212 ? 2.381 2.126 2.100 -0.034 -0.326 -0.160 211 VAL BBB CA  
3086  C C   . VAL B 212 ? 2.394 2.100 2.116 -0.058 -0.321 -0.159 211 VAL BBB C   
3087  O O   . VAL B 212 ? 2.421 2.064 2.101 -0.057 -0.321 -0.178 211 VAL BBB O   
3088  C CB  . VAL B 212 ? 2.363 2.093 2.060 0.000  -0.291 -0.158 211 VAL BBB CB  
3089  C CG1 . VAL B 212 ? 2.358 2.108 2.084 0.009  -0.253 -0.133 211 VAL BBB CG1 
3090  C CG2 . VAL B 212 ? 2.360 2.118 2.046 0.024  -0.296 -0.159 211 VAL BBB CG2 
3091  N N   . ASP B 213 ? 2.386 2.132 2.156 -0.079 -0.315 -0.133 212 ASP BBB N   
3092  C CA  . ASP B 213 ? 2.396 2.117 2.174 -0.102 -0.303 -0.123 212 ASP BBB CA  
3093  C C   . ASP B 213 ? 2.374 2.110 2.158 -0.081 -0.256 -0.103 212 ASP BBB C   
3094  O O   . ASP B 213 ? 2.357 2.153 2.191 -0.083 -0.238 -0.075 212 ASP BBB O   
3095  C CB  . ASP B 213 ? 2.419 2.175 2.245 -0.141 -0.325 -0.106 212 ASP BBB CB  
3096  C CG  . ASP B 213 ? 2.459 2.184 2.271 -0.168 -0.373 -0.130 212 ASP BBB CG  
3097  O OD1 . ASP B 213 ? 2.464 2.137 2.224 -0.152 -0.386 -0.161 212 ASP BBB OD1 
3098  O OD2 . ASP B 213 ? 2.489 2.241 2.340 -0.205 -0.396 -0.118 212 ASP BBB OD2 
3099  N N   . LYS B 214 ? 2.378 2.061 2.113 -0.061 -0.237 -0.117 213 LYS BBB N   
3100  C CA  . LYS B 214 ? 2.359 2.042 2.084 -0.039 -0.193 -0.107 213 LYS BBB CA  
3101  C C   . LYS B 214 ? 2.358 2.006 2.062 -0.055 -0.176 -0.100 213 LYS BBB C   
3102  O O   . LYS B 214 ? 2.340 1.930 1.999 -0.060 -0.187 -0.116 213 LYS BBB O   
3103  C CB  . LYS B 214 ? 2.366 2.015 2.050 -0.011 -0.185 -0.126 213 LYS BBB CB  
3104  C CG  . LYS B 214 ? 2.381 2.024 2.052 0.012  -0.142 -0.119 213 LYS BBB CG  
3105  C CD  . LYS B 214 ? 2.395 2.096 2.115 0.025  -0.116 -0.094 213 LYS BBB CD  
3106  C CE  . LYS B 214 ? 2.433 2.114 2.133 0.050  -0.071 -0.092 213 LYS BBB CE  
3107  N NZ  . LYS B 214 ? 2.456 2.192 2.205 0.063  -0.040 -0.066 213 LYS BBB NZ  
3108  N N   . LYS B 215 ? 2.357 2.044 2.093 -0.061 -0.149 -0.075 214 LYS BBB N   
3109  C CA  . LYS B 215 ? 2.386 2.051 2.101 -0.075 -0.125 -0.062 214 LYS BBB CA  
3110  C C   . LYS B 215 ? 2.381 2.001 2.038 -0.052 -0.098 -0.077 214 LYS BBB C   
3111  O O   . LYS B 215 ? 2.367 1.999 2.025 -0.024 -0.076 -0.082 214 LYS BBB O   
3112  C CB  . LYS B 215 ? 2.402 2.134 2.173 -0.083 -0.099 -0.031 214 LYS BBB CB  
3113  C CG  . LYS B 215 ? 2.442 2.165 2.189 -0.087 -0.059 -0.015 214 LYS BBB CG  
3114  C CD  . LYS B 215 ? 2.472 2.196 2.230 -0.125 -0.068 0.006  214 LYS BBB CD  
3115  C CE  . LYS B 215 ? 2.507 2.238 2.245 -0.125 -0.021 0.026  214 LYS BBB CE  
3116  N NZ  . LYS B 215 ? 2.545 2.262 2.279 -0.163 -0.029 0.048  214 LYS BBB NZ  
3117  N N   . VAL B 216 ? 2.384 1.952 1.992 -0.066 -0.101 -0.083 215 VAL BBB N   
3118  C CA  . VAL B 216 ? 2.383 1.906 1.929 -0.053 -0.078 -0.095 215 VAL BBB CA  
3119  C C   . VAL B 216 ? 2.421 1.945 1.947 -0.066 -0.049 -0.076 215 VAL BBB C   
3120  O O   . VAL B 216 ? 2.431 1.968 1.980 -0.091 -0.060 -0.056 215 VAL BBB O   
3121  C CB  . VAL B 216 ? 2.382 1.852 1.885 -0.057 -0.110 -0.115 215 VAL BBB CB  
3122  C CG1 . VAL B 216 ? 2.417 1.847 1.861 -0.048 -0.093 -0.129 215 VAL BBB CG1 
3123  C CG2 . VAL B 216 ? 2.348 1.821 1.872 -0.047 -0.139 -0.131 215 VAL BBB CG2 
3124  N N   . GLU B 217 ? 2.457 1.965 1.942 -0.050 -0.012 -0.082 216 GLU BBB N   
3125  C CA  . GLU B 217 ? 2.523 2.030 1.976 -0.059 0.021  -0.066 216 GLU BBB CA  
3126  C C   . GLU B 217 ? 2.564 2.029 1.947 -0.043 0.050  -0.086 216 GLU BBB C   
3127  O O   . GLU B 217 ? 2.584 2.032 1.960 -0.022 0.053  -0.108 216 GLU BBB O   
3128  C CB  . GLU B 217 ? 2.535 2.109 2.049 -0.057 0.052  -0.039 216 GLU BBB CB  
3129  C CG  . GLU B 217 ? 2.509 2.123 2.070 -0.026 0.071  -0.042 216 GLU BBB CG  
3130  C CD  . GLU B 217 ? 2.518 2.207 2.145 -0.020 0.103  -0.013 216 GLU BBB CD  
3131  O OE1 . GLU B 217 ? 2.506 2.243 2.191 -0.045 0.083  0.010  216 GLU BBB OE1 
3132  O OE2 . GLU B 217 ? 2.538 2.241 2.164 0.010  0.149  -0.013 216 GLU BBB OE2 
3133  N N   . PRO B 218 ? 2.600 2.041 1.924 -0.054 0.071  -0.081 217 PRO BBB N   
3134  C CA  . PRO B 218 ? 2.642 2.039 1.891 -0.041 0.098  -0.104 217 PRO BBB CA  
3135  C C   . PRO B 218 ? 2.652 2.067 1.914 -0.011 0.148  -0.109 217 PRO BBB C   
3136  O O   . PRO B 218 ? 2.621 2.093 1.947 -0.002 0.168  -0.087 217 PRO BBB O   
3137  C CB  . PRO B 218 ? 2.708 2.088 1.895 -0.063 0.107  -0.090 217 PRO BBB CB  
3138  C CG  . PRO B 218 ? 2.691 2.123 1.938 -0.079 0.108  -0.054 217 PRO BBB CG  
3139  C CD  . PRO B 218 ? 2.615 2.069 1.937 -0.081 0.068  -0.052 217 PRO BBB CD  
3140  N N   . LYS B 219 ? 2.704 2.068 1.907 0.004  0.166  -0.138 218 LYS BBB N   
3141  C CA  . LYS B 219 ? 2.761 2.122 1.968 0.038  0.214  -0.149 218 LYS BBB CA  
3142  C C   . LYS B 219 ? 2.852 2.205 2.005 0.045  0.267  -0.147 218 LYS BBB C   
3143  O O   . LYS B 219 ? 2.900 2.252 2.011 0.020  0.262  -0.137 218 LYS BBB O   
3144  C CB  . LYS B 219 ? 2.792 2.091 1.959 0.047  0.204  -0.182 218 LYS BBB CB  
3145  C CG  . LYS B 219 ? 2.817 2.109 2.011 0.083  0.237  -0.191 218 LYS BBB CG  
3146  C CD  . LYS B 219 ? 2.873 2.085 2.001 0.088  0.242  -0.226 218 LYS BBB CD  
3147  C CE  . LYS B 219 ? 2.833 2.020 1.950 0.064  0.190  -0.239 218 LYS BBB CE  
3148  N NZ  . LYS B 219 ? 2.740 1.969 1.936 0.072  0.163  -0.224 218 LYS BBB NZ  
3149  N N   . SER B 220 ? 2.877 2.229 2.035 0.080  0.317  -0.155 219 SER BBB N   
3150  C CA  . SER B 220 ? 2.964 2.286 2.050 0.094  0.374  -0.168 219 SER BBB CA  
3151  C C   . SER B 220 ? 3.000 2.261 2.054 0.127  0.403  -0.201 219 SER BBB C   
3152  O O   . SER B 220 ? 3.053 2.237 2.012 0.122  0.411  -0.235 219 SER BBB O   
3153  C CB  . SER B 220 ? 2.967 2.363 2.104 0.108  0.418  -0.134 219 SER BBB CB  
3154  O OG  . SER B 220 ? 3.055 2.424 2.107 0.111  0.465  -0.144 219 SER BBB OG  
3155  N N   . ASP C 1   ? 1.877 2.018 2.037 -0.306 0.191  0.406  1   ASP CCC N   
3156  C CA  . ASP C 1   ? 1.945 1.997 2.091 -0.336 0.177  0.416  1   ASP CCC CA  
3157  C C   . ASP C 1   ? 1.916 1.971 2.110 -0.346 0.134  0.381  1   ASP CCC C   
3158  O O   . ASP C 1   ? 1.957 1.947 2.153 -0.379 0.123  0.384  1   ASP CCC O   
3159  C CB  . ASP C 1   ? 2.011 2.057 2.186 -0.390 0.215  0.449  1   ASP CCC CB  
3160  C CG  . ASP C 1   ? 2.125 2.048 2.245 -0.414 0.215  0.471  1   ASP CCC CG  
3161  O OD1 . ASP C 1   ? 2.154 1.999 2.209 -0.379 0.186  0.463  1   ASP CCC OD1 
3162  O OD2 . ASP C 1   ? 2.181 2.086 2.321 -0.465 0.247  0.498  1   ASP CCC OD2 
3163  N N   . ILE C 2   ? 1.864 1.981 2.084 -0.318 0.111  0.350  2   ILE CCC N   
3164  C CA  . ILE C 2   ? 1.812 1.972 2.098 -0.330 0.080  0.318  2   ILE CCC CA  
3165  C C   . ILE C 2   ? 1.831 1.917 2.085 -0.322 0.042  0.298  2   ILE CCC C   
3166  O O   . ILE C 2   ? 1.872 1.894 2.056 -0.292 0.037  0.302  2   ILE CCC O   
3167  C CB  . ILE C 2   ? 1.714 1.958 2.025 -0.297 0.078  0.298  2   ILE CCC CB  
3168  C CG1 . ILE C 2   ? 1.719 2.037 2.060 -0.299 0.118  0.316  2   ILE CCC CG1 
3169  C CG2 . ILE C 2   ? 1.649 1.930 2.013 -0.302 0.044  0.268  2   ILE CCC CG2 
3170  C CD1 . ILE C 2   ? 1.661 2.040 2.007 -0.260 0.121  0.298  2   ILE CCC CD1 
3171  N N   . GLN C 3   ? 1.826 1.924 2.127 -0.345 0.015  0.274  3   GLN CCC N   
3172  C CA  . GLN C 3   ? 1.881 1.907 2.150 -0.339 -0.021 0.252  3   GLN CCC CA  
3173  C C   . GLN C 3   ? 1.851 1.929 2.171 -0.345 -0.052 0.219  3   GLN CCC C   
3174  O O   . GLN C 3   ? 1.833 1.980 2.222 -0.378 -0.050 0.219  3   GLN CCC O   
3175  C CB  . GLN C 3   ? 2.007 1.942 2.255 -0.378 -0.017 0.267  3   GLN CCC CB  
3176  C CG  . GLN C 3   ? 2.077 1.914 2.273 -0.366 -0.047 0.247  3   GLN CCC CG  
3177  C CD  . GLN C 3   ? 2.207 1.957 2.395 -0.417 -0.047 0.255  3   GLN CCC CD  
3178  O OE1 . GLN C 3   ? 2.259 2.002 2.460 -0.455 -0.018 0.284  3   GLN CCC OE1 
3179  N NE2 . GLN C 3   ? 2.276 1.955 2.438 -0.420 -0.077 0.230  3   GLN CCC NE2 
3180  N N   . LEU C 4   ? 1.852 1.900 2.136 -0.315 -0.079 0.194  4   LEU CCC N   
3181  C CA  . LEU C 4   ? 1.809 1.898 2.120 -0.307 -0.108 0.164  4   LEU CCC CA  
3182  C C   . LEU C 4   ? 1.869 1.885 2.153 -0.317 -0.139 0.141  4   LEU CCC C   
3183  O O   . LEU C 4   ? 1.930 1.860 2.154 -0.304 -0.139 0.144  4   LEU CCC O   
3184  C CB  . LEU C 4   ? 1.734 1.852 2.018 -0.259 -0.107 0.154  4   LEU CCC CB  
3185  C CG  . LEU C 4   ? 1.690 1.881 1.997 -0.246 -0.080 0.168  4   LEU CCC CG  
3186  C CD1 . LEU C 4   ? 1.640 1.845 1.915 -0.206 -0.081 0.154  4   LEU CCC CD1 
3187  C CD2 . LEU C 4   ? 1.674 1.943 2.053 -0.268 -0.079 0.169  4   LEU CCC CD2 
3188  N N   . THR C 5   ? 1.853 1.902 2.173 -0.335 -0.167 0.119  5   THR CCC N   
3189  C CA  . THR C 5   ? 1.876 1.864 2.166 -0.341 -0.202 0.089  5   THR CCC CA  
3190  C C   . THR C 5   ? 1.795 1.844 2.099 -0.320 -0.226 0.066  5   THR CCC C   
3191  O O   . THR C 5   ? 1.727 1.859 2.095 -0.338 -0.234 0.065  5   THR CCC O   
3192  C CB  . THR C 5   ? 1.964 1.916 2.278 -0.400 -0.215 0.086  5   THR CCC CB  
3193  O OG1 . THR C 5   ? 1.991 1.945 2.330 -0.430 -0.183 0.118  5   THR CCC OG1 
3194  C CG2 . THR C 5   ? 2.052 1.885 2.298 -0.403 -0.235 0.067  5   THR CCC CG2 
3195  N N   . GLN C 6   ? 1.787 1.800 2.035 -0.281 -0.236 0.049  6   GLN CCC N   
3196  C CA  . GLN C 6   ? 1.777 1.824 2.019 -0.258 -0.258 0.026  6   GLN CCC CA  
3197  C C   . GLN C 6   ? 1.858 1.862 2.083 -0.279 -0.296 -0.001 6   GLN CCC C   
3198  O O   . GLN C 6   ? 1.970 1.900 2.174 -0.305 -0.300 -0.004 6   GLN CCC O   
3199  C CB  . GLN C 6   ? 1.772 1.796 1.957 -0.211 -0.247 0.022  6   GLN CCC CB  
3200  C CG  . GLN C 6   ? 1.725 1.794 1.921 -0.190 -0.215 0.042  6   GLN CCC CG  
3201  C CD  . GLN C 6   ? 1.706 1.754 1.851 -0.154 -0.204 0.037  6   GLN CCC CD  
3202  O OE1 . GLN C 6   ? 1.711 1.738 1.836 -0.143 -0.186 0.047  6   GLN CCC OE1 
3203  N NE2 . GLN C 6   ? 1.699 1.758 1.824 -0.135 -0.213 0.021  6   GLN CCC NE2 
3204  N N   . SER C 7   ? 1.858 1.898 2.083 -0.268 -0.322 -0.020 7   SER CCC N   
3205  C CA  . SER C 7   ? 1.937 1.934 2.129 -0.279 -0.362 -0.051 7   SER CCC CA  
3206  C C   . SER C 7   ? 1.916 1.956 2.091 -0.247 -0.382 -0.065 7   SER CCC C   
3207  O O   . SER C 7   ? 1.885 2.007 2.104 -0.235 -0.376 -0.052 7   SER CCC O   
3208  C CB  . SER C 7   ? 1.996 2.005 2.238 -0.337 -0.386 -0.058 7   SER CCC CB  
3209  O OG  . SER C 7   ? 1.946 2.069 2.275 -0.353 -0.386 -0.044 7   SER CCC OG  
3210  N N   . PRO C 8   ? 1.956 1.937 2.059 -0.227 -0.402 -0.090 8   PRO CCC N   
3211  C CA  . PRO C 8   ? 2.036 1.914 2.078 -0.233 -0.408 -0.109 8   PRO CCC CA  
3212  C C   . PRO C 8   ? 2.022 1.854 2.021 -0.198 -0.369 -0.096 8   PRO CCC C   
3213  O O   . PRO C 8   ? 1.961 1.844 1.980 -0.176 -0.343 -0.076 8   PRO CCC O   
3214  C CB  . PRO C 8   ? 2.100 1.953 2.083 -0.219 -0.443 -0.140 8   PRO CCC CB  
3215  C CG  . PRO C 8   ? 2.028 1.945 2.010 -0.180 -0.435 -0.129 8   PRO CCC CG  
3216  C CD  . PRO C 8   ? 1.949 1.955 2.017 -0.192 -0.418 -0.101 8   PRO CCC CD  
3217  N N   . ASP C 9   ? 2.100 1.839 2.041 -0.192 -0.368 -0.109 9   ASP CCC N   
3218  C CA  . ASP C 9   ? 2.090 1.789 1.990 -0.153 -0.335 -0.101 9   ASP CCC CA  
3219  C C   . ASP C 9   ? 2.061 1.765 1.909 -0.110 -0.330 -0.114 9   ASP CCC C   
3220  O O   . ASP C 9   ? 1.975 1.706 1.822 -0.081 -0.299 -0.100 9   ASP CCC O   
3221  C CB  . ASP C 9   ? 2.206 1.802 2.063 -0.158 -0.335 -0.109 9   ASP CCC CB  
3222  C CG  . ASP C 9   ? 2.236 1.819 2.136 -0.196 -0.328 -0.087 9   ASP CCC CG  
3223  O OD1 . ASP C 9   ? 2.170 1.785 2.096 -0.184 -0.300 -0.059 9   ASP CCC OD1 
3224  O OD2 . ASP C 9   ? 2.325 1.864 2.229 -0.240 -0.351 -0.099 9   ASP CCC OD2 
3225  N N   . SER C 10  ? 2.110 1.788 1.915 -0.109 -0.358 -0.140 10  SER CCC N   
3226  C CA  . SER C 10  ? 2.102 1.775 1.846 -0.071 -0.354 -0.154 10  SER CCC CA  
3227  C C   . SER C 10  ? 2.070 1.796 1.824 -0.077 -0.379 -0.158 10  SER CCC C   
3228  O O   . SER C 10  ? 2.090 1.840 1.884 -0.110 -0.410 -0.162 10  SER CCC O   
3229  C CB  . SER C 10  ? 2.198 1.778 1.861 -0.055 -0.364 -0.183 10  SER CCC CB  
3230  O OG  . SER C 10  ? 2.218 1.794 1.818 -0.025 -0.364 -0.198 10  SER CCC OG  
3231  N N   . LEU C 11  ? 2.030 1.773 1.746 -0.045 -0.364 -0.155 11  LEU CCC N   
3232  C CA  . LEU C 11  ? 2.033 1.813 1.738 -0.039 -0.388 -0.158 11  LEU CCC CA  
3233  C C   . LEU C 11  ? 2.043 1.794 1.666 0.000  -0.371 -0.164 11  LEU CCC C   
3234  O O   . LEU C 11  ? 1.994 1.761 1.616 0.017  -0.331 -0.147 11  LEU CCC O   
3235  C CB  . LEU C 11  ? 1.981 1.841 1.760 -0.047 -0.377 -0.130 11  LEU CCC CB  
3236  C CG  . LEU C 11  ? 2.029 1.937 1.819 -0.043 -0.407 -0.130 11  LEU CCC CG  
3237  C CD1 . LEU C 11  ? 2.099 2.009 1.899 -0.068 -0.459 -0.152 11  LEU CCC CD1 
3238  C CD2 . LEU C 11  ? 1.960 1.942 1.826 -0.048 -0.392 -0.103 11  LEU CCC CD2 
3239  N N   . ALA C 12  ? 2.123 1.832 1.676 0.009  -0.401 -0.188 12  ALA CCC N   
3240  C CA  . ALA C 12  ? 2.162 1.837 1.624 0.045  -0.388 -0.195 12  ALA CCC CA  
3241  C C   . ALA C 12  ? 2.153 1.859 1.596 0.055  -0.415 -0.190 12  ALA CCC C   
3242  O O   . ALA C 12  ? 2.192 1.910 1.646 0.039  -0.465 -0.205 12  ALA CCC O   
3243  C CB  . ALA C 12  ? 2.271 1.868 1.654 0.055  -0.401 -0.227 12  ALA CCC CB  
3244  N N   . VAL C 13  ? 2.103 1.821 1.519 0.079  -0.385 -0.169 13  VAL CCC N   
3245  C CA  . VAL C 13  ? 2.096 1.842 1.498 0.095  -0.404 -0.156 13  VAL CCC CA  
3246  C C   . VAL C 13  ? 2.148 1.848 1.449 0.129  -0.376 -0.149 13  VAL CCC C   
3247  O O   . VAL C 13  ? 2.126 1.812 1.417 0.133  -0.325 -0.138 13  VAL CCC O   
3248  C CB  . VAL C 13  ? 1.998 1.810 1.488 0.085  -0.391 -0.129 13  VAL CCC CB  
3249  C CG1 . VAL C 13  ? 2.023 1.851 1.486 0.112  -0.398 -0.112 13  VAL CCC CG1 
3250  C CG2 . VAL C 13  ? 1.953 1.815 1.537 0.051  -0.420 -0.134 13  VAL CCC CG2 
3251  N N   . SER C 14  ? 2.214 1.896 1.444 0.153  -0.408 -0.154 14  SER CCC N   
3252  C CA  . SER C 14  ? 2.279 1.914 1.404 0.187  -0.384 -0.142 14  SER CCC CA  
3253  C C   . SER C 14  ? 2.229 1.883 1.378 0.193  -0.347 -0.108 14  SER CCC C   
3254  O O   . SER C 14  ? 2.181 1.886 1.397 0.190  -0.368 -0.096 14  SER CCC O   
3255  C CB  . SER C 14  ? 2.383 1.997 1.429 0.213  -0.435 -0.155 14  SER CCC CB  
3256  O OG  . SER C 14  ? 2.463 2.026 1.439 0.215  -0.452 -0.186 14  SER CCC OG  
3257  N N   . LEU C 15  ? 2.255 1.871 1.354 0.200  -0.292 -0.094 15  LEU CCC N   
3258  C CA  . LEU C 15  ? 2.255 1.868 1.359 0.201  -0.250 -0.064 15  LEU CCC CA  
3259  C C   . LEU C 15  ? 2.296 1.915 1.386 0.226  -0.281 -0.047 15  LEU CCC C   
3260  O O   . LEU C 15  ? 2.407 1.984 1.404 0.257  -0.301 -0.046 15  LEU CCC O   
3261  C CB  . LEU C 15  ? 2.336 1.890 1.347 0.210  -0.198 -0.054 15  LEU CCC CB  
3262  C CG  . LEU C 15  ? 2.306 1.876 1.355 0.185  -0.149 -0.059 15  LEU CCC CG  
3263  C CD1 . LEU C 15  ? 2.388 1.913 1.346 0.198  -0.118 -0.067 15  LEU CCC CD1 
3264  C CD2 . LEU C 15  ? 2.254 1.841 1.348 0.162  -0.107 -0.036 15  LEU CCC CD2 
3265  N N   . GLY C 16  ? 2.251 1.917 1.425 0.216  -0.284 -0.035 16  GLY CCC N   
3266  C CA  . GLY C 16  ? 2.318 1.990 1.481 0.246  -0.302 -0.015 16  GLY CCC CA  
3267  C C   . GLY C 16  ? 2.331 2.072 1.555 0.254  -0.364 -0.027 16  GLY CCC C   
3268  O O   . GLY C 16  ? 2.374 2.130 1.589 0.288  -0.385 -0.012 16  GLY CCC O   
3269  N N   . GLU C 17  ? 2.313 2.094 1.595 0.225  -0.392 -0.052 17  GLU CCC N   
3270  C CA  . GLU C 17  ? 2.299 2.160 1.666 0.215  -0.446 -0.064 17  GLU CCC CA  
3271  C C   . GLU C 17  ? 2.184 2.102 1.665 0.186  -0.424 -0.055 17  GLU CCC C   
3272  O O   . GLU C 17  ? 2.118 2.007 1.603 0.169  -0.375 -0.048 17  GLU CCC O   
3273  C CB  . GLU C 17  ? 2.352 2.215 1.716 0.194  -0.487 -0.097 17  GLU CCC CB  
3274  C CG  . GLU C 17  ? 2.494 2.288 1.733 0.220  -0.502 -0.110 17  GLU CCC CG  
3275  C CD  . GLU C 17  ? 2.611 2.415 1.791 0.261  -0.550 -0.108 17  GLU CCC CD  
3276  O OE1 . GLU C 17  ? 2.648 2.480 1.843 0.289  -0.548 -0.083 17  GLU CCC OE1 
3277  O OE2 . GLU C 17  ? 2.675 2.455 1.788 0.268  -0.591 -0.132 17  GLU CCC OE2 
3278  N N   . ARG C 18  ? 2.171 2.169 1.739 0.179  -0.457 -0.056 18  ARG CCC N   
3279  C CA  . ARG C 18  ? 2.085 2.143 1.762 0.151  -0.439 -0.047 18  ARG CCC CA  
3280  C C   . ARG C 18  ? 1.997 2.046 1.710 0.105  -0.433 -0.065 18  ARG CCC C   
3281  O O   . ARG C 18  ? 2.038 2.046 1.701 0.098  -0.453 -0.086 18  ARG CCC O   
3282  C CB  . ARG C 18  ? 2.120 2.274 1.878 0.158  -0.476 -0.044 18  ARG CCC CB  
3283  C CG  . ARG C 18  ? 2.056 2.273 1.915 0.139  -0.452 -0.030 18  ARG CCC CG  
3284  C CD  . ARG C 18  ? 2.062 2.386 2.005 0.147  -0.488 -0.027 18  ARG CCC CD  
3285  N NE  . ARG C 18  ? 2.134 2.468 2.031 0.204  -0.509 -0.017 18  ARG CCC NE  
3286  C CZ  . ARG C 18  ? 2.134 2.463 2.017 0.247  -0.481 0.007  18  ARG CCC CZ  
3287  N NH1 . ARG C 18  ? 2.072 2.391 1.984 0.237  -0.432 0.020  18  ARG CCC NH1 
3288  N NH2 . ARG C 18  ? 2.202 2.533 2.034 0.303  -0.504 0.016  18  ARG CCC NH2 
3289  N N   . ALA C 19  ? 1.883 1.961 1.670 0.079  -0.406 -0.056 19  ALA CCC N   
3290  C CA  . ALA C 19  ? 1.847 1.920 1.675 0.039  -0.400 -0.067 19  ALA CCC CA  
3291  C C   . ALA C 19  ? 1.788 1.924 1.712 0.017  -0.387 -0.053 19  ALA CCC C   
3292  O O   . ALA C 19  ? 1.755 1.896 1.688 0.028  -0.351 -0.034 19  ALA CCC O   
3293  C CB  . ALA C 19  ? 1.850 1.857 1.625 0.039  -0.361 -0.068 19  ALA CCC CB  
3294  N N   . THR C 20  ? 1.807 1.987 1.798 -0.016 -0.416 -0.062 20  THR CCC N   
3295  C CA  . THR C 20  ? 1.760 2.005 1.845 -0.041 -0.404 -0.047 20  THR CCC CA  
3296  C C   . THR C 20  ? 1.731 1.939 1.831 -0.078 -0.388 -0.051 20  THR CCC C   
3297  O O   . THR C 20  ? 1.734 1.886 1.795 -0.091 -0.405 -0.071 20  THR CCC O   
3298  C CB  . THR C 20  ? 1.782 2.116 1.938 -0.051 -0.443 -0.051 20  THR CCC CB  
3299  O OG1 . THR C 20  ? 1.880 2.198 2.006 -0.062 -0.490 -0.076 20  THR CCC OG1 
3300  C CG2 . THR C 20  ? 1.776 2.164 1.939 -0.007 -0.444 -0.036 20  THR CCC CG2 
3301  N N   . ILE C 21  ? 1.683 1.914 1.830 -0.090 -0.354 -0.032 21  ILE CCC N   
3302  C CA  . ILE C 21  ? 1.668 1.869 1.834 -0.122 -0.338 -0.029 21  ILE CCC CA  
3303  C C   . ILE C 21  ? 1.637 1.905 1.887 -0.147 -0.326 -0.011 21  ILE CCC C   
3304  O O   . ILE C 21  ? 1.604 1.914 1.875 -0.128 -0.301 0.006  21  ILE CCC O   
3305  C CB  . ILE C 21  ? 1.633 1.782 1.751 -0.105 -0.301 -0.022 21  ILE CCC CB  
3306  C CG1 . ILE C 21  ? 1.679 1.777 1.720 -0.078 -0.304 -0.037 21  ILE CCC CG1 
3307  C CG2 . ILE C 21  ? 1.629 1.742 1.756 -0.129 -0.290 -0.020 21  ILE CCC CG2 
3308  C CD1 . ILE C 21  ? 1.674 1.741 1.677 -0.062 -0.268 -0.030 21  ILE CCC CD1 
3309  N N   . ASN C 22  ? 1.649 1.921 1.939 -0.189 -0.342 -0.016 22  ASN CCC N   
3310  C CA  . ASN C 22  ? 1.607 1.940 1.978 -0.222 -0.330 0.001  22  ASN CCC CA  
3311  C C   . ASN C 22  ? 1.599 1.884 1.958 -0.233 -0.293 0.018  22  ASN CCC C   
3312  O O   . ASN C 22  ? 1.621 1.823 1.925 -0.233 -0.293 0.010  22  ASN CCC O   
3313  C CB  . ASN C 22  ? 1.644 2.003 2.064 -0.269 -0.365 -0.012 22  ASN CCC CB  
3314  C CG  . ASN C 22  ? 1.649 2.090 2.105 -0.259 -0.402 -0.024 22  ASN CCC CG  
3315  O OD1 . ASN C 22  ? 1.613 2.099 2.067 -0.215 -0.395 -0.016 22  ASN CCC OD1 
3316  N ND2 . ASN C 22  ? 1.704 2.164 2.189 -0.298 -0.442 -0.044 22  ASN CCC ND2 
3317  N N   . CYS C 23  ? 1.569 1.906 1.976 -0.239 -0.263 0.042  23  CYS CCC N   
3318  C CA  . CYS C 23  ? 1.574 1.878 1.973 -0.248 -0.227 0.062  23  CYS CCC CA  
3319  C C   . CYS C 23  ? 1.567 1.939 2.041 -0.279 -0.210 0.082  23  CYS CCC C   
3320  O O   . CYS C 23  ? 1.548 1.997 2.060 -0.261 -0.197 0.091  23  CYS CCC O   
3321  C CB  . CYS C 23  ? 1.568 1.863 1.925 -0.207 -0.200 0.070  23  CYS CCC CB  
3322  S SG  . CYS C 23  ? 1.605 1.889 1.956 -0.210 -0.158 0.097  23  CYS CCC SG  
3323  N N   . LYS C 24  ? 1.603 1.945 2.094 -0.325 -0.209 0.088  24  LYS CCC N   
3324  C CA  . LYS C 24  ? 1.601 2.007 2.166 -0.365 -0.191 0.108  24  LYS CCC CA  
3325  C C   . LYS C 24  ? 1.603 1.964 2.142 -0.370 -0.149 0.136  24  LYS CCC C   
3326  O O   . LYS C 24  ? 1.609 1.873 2.082 -0.365 -0.149 0.135  24  LYS CCC O   
3327  C CB  . LYS C 24  ? 1.658 2.062 2.264 -0.422 -0.220 0.095  24  LYS CCC CB  
3328  C CG  . LYS C 24  ? 1.681 2.172 2.378 -0.469 -0.202 0.114  24  LYS CCC CG  
3329  C CD  . LYS C 24  ? 1.762 2.249 2.500 -0.536 -0.230 0.100  24  LYS CCC CD  
3330  C CE  . LYS C 24  ? 1.790 2.336 2.605 -0.592 -0.199 0.125  24  LYS CCC CE  
3331  N NZ  . LYS C 24  ? 1.732 2.429 2.635 -0.576 -0.182 0.137  24  LYS CCC NZ  
3332  N N   . SER C 25  ? 1.597 2.029 2.183 -0.374 -0.116 0.159  25  SER CCC N   
3333  C CA  . SER C 25  ? 1.636 2.039 2.196 -0.376 -0.073 0.188  25  SER CCC CA  
3334  C C   . SER C 25  ? 1.696 2.131 2.315 -0.432 -0.052 0.209  25  SER CCC C   
3335  O O   . SER C 25  ? 1.695 2.232 2.398 -0.451 -0.054 0.208  25  SER CCC O   
3336  C CB  . SER C 25  ? 1.597 2.047 2.147 -0.331 -0.045 0.198  25  SER CCC CB  
3337  O OG  . SER C 25  ? 1.603 2.159 2.229 -0.339 -0.028 0.207  25  SER CCC OG  
3338  N N   . SER C 26  ? 1.753 2.106 2.331 -0.455 -0.031 0.230  26  SER CCC N   
3339  C CA  . SER C 26  ? 1.807 2.164 2.426 -0.515 -0.006 0.254  26  SER CCC CA  
3340  C C   . SER C 26  ? 1.762 2.217 2.429 -0.512 0.040  0.280  26  SER CCC C   
3341  O O   . SER C 26  ? 1.815 2.319 2.548 -0.564 0.061  0.296  26  SER CCC O   
3342  C CB  . SER C 26  ? 1.902 2.125 2.442 -0.530 0.005  0.271  26  SER CCC CB  
3343  O OG  . SER C 26  ? 1.901 2.063 2.356 -0.472 0.007  0.273  26  SER CCC OG  
3344  N N   . GLN C 27  ? 1.680 2.160 2.315 -0.455 0.056  0.283  27  GLN CCC N   
3345  C CA  . GLN C 27  ? 1.641 2.206 2.306 -0.439 0.101  0.304  27  GLN CCC CA  
3346  C C   . GLN C 27  ? 1.549 2.192 2.236 -0.388 0.089  0.284  27  GLN CCC C   
3347  O O   . GLN C 27  ? 1.506 2.104 2.148 -0.356 0.057  0.260  27  GLN CCC O   
3348  C CB  . GLN C 27  ? 1.672 2.164 2.250 -0.418 0.136  0.329  27  GLN CCC CB  
3349  C CG  . GLN C 27  ? 1.695 2.244 2.293 -0.424 0.191  0.360  27  GLN CCC CG  
3350  C CD  . GLN C 27  ? 1.770 2.230 2.282 -0.425 0.222  0.390  27  GLN CCC CD  
3351  O OE1 . GLN C 27  ? 1.776 2.147 2.203 -0.396 0.205  0.386  27  GLN CCC OE1 
3352  N NE2 . GLN C 27  ? 1.835 2.321 2.367 -0.456 0.269  0.423  27  GLN CCC NE2 
3353  N N   . SER C 28  ? 1.541 2.293 2.293 -0.380 0.117  0.293  28  SER CCC N   
3354  C CA  . SER C 28  ? 1.500 2.319 2.265 -0.324 0.113  0.278  28  SER CCC CA  
3355  C C   . SER C 28  ? 1.495 2.246 2.163 -0.275 0.131  0.278  28  SER CCC C   
3356  O O   . SER C 28  ? 1.525 2.228 2.144 -0.283 0.162  0.299  28  SER CCC O   
3357  C CB  . SER C 28  ? 1.512 2.462 2.366 -0.322 0.144  0.290  28  SER CCC CB  
3358  O OG  . SER C 28  ? 1.480 2.476 2.330 -0.260 0.144  0.277  28  SER CCC OG  
3359  N N   . VAL C 29  ? 1.463 2.209 2.102 -0.229 0.111  0.256  29  VAL CCC N   
3360  C CA  . VAL C 29  ? 1.467 2.145 2.013 -0.188 0.119  0.249  29  VAL CCC CA  
3361  C C   . VAL C 29  ? 1.470 2.200 2.018 -0.141 0.140  0.244  29  VAL CCC C   
3362  O O   . VAL C 29  ? 1.480 2.156 1.954 -0.107 0.141  0.232  29  VAL CCC O   
3363  C CB  . VAL C 29  ? 1.442 2.045 1.937 -0.181 0.078  0.227  29  VAL CCC CB  
3364  C CG1 . VAL C 29  ? 1.458 2.011 1.955 -0.222 0.056  0.229  29  VAL CCC CG1 
3365  C CG2 . VAL C 29  ? 1.415 2.049 1.935 -0.158 0.049  0.205  29  VAL CCC CG2 
3366  N N   . LEU C 30  ? 1.478 2.308 2.106 -0.139 0.157  0.253  30  LEU CCC N   
3367  C CA  . LEU C 30  ? 1.495 2.381 2.131 -0.086 0.179  0.249  30  LEU CCC CA  
3368  C C   . LEU C 30  ? 1.556 2.419 2.133 -0.067 0.228  0.262  30  LEU CCC C   
3369  O O   . LEU C 30  ? 1.588 2.469 2.181 -0.097 0.258  0.285  30  LEU CCC O   
3370  C CB  . LEU C 30  ? 1.484 2.499 2.236 -0.093 0.180  0.256  30  LEU CCC CB  
3371  C CG  . LEU C 30  ? 1.495 2.581 2.270 -0.032 0.195  0.251  30  LEU CCC CG  
3372  C CD1 . LEU C 30  ? 1.533 2.670 2.315 -0.013 0.254  0.270  30  LEU CCC CD1 
3373  C CD2 . LEU C 30  ? 1.495 2.496 2.181 0.018  0.177  0.230  30  LEU CCC CD2 
3374  N N   . TYR C 31  ? 1.603 2.419 2.106 -0.019 0.237  0.248  31  TYR CCC N   
3375  C CA  . TYR C 31  ? 1.675 2.472 2.115 0.010  0.283  0.254  31  TYR CCC CA  
3376  C C   . TYR C 31  ? 1.701 2.595 2.199 0.048  0.317  0.261  31  TYR CCC C   
3377  O O   . TYR C 31  ? 1.705 2.595 2.185 0.097  0.313  0.245  31  TYR CCC O   
3378  C CB  . TYR C 31  ? 1.714 2.409 2.046 0.039  0.273  0.232  31  TYR CCC CB  
3379  C CG  . TYR C 31  ? 1.758 2.376 2.007 0.019  0.278  0.234  31  TYR CCC CG  
3380  C CD1 . TYR C 31  ? 1.744 2.324 1.989 -0.019 0.247  0.237  31  TYR CCC CD1 
3381  C CD2 . TYR C 31  ? 1.806 2.388 1.975 0.044  0.311  0.232  31  TYR CCC CD2 
3382  C CE1 . TYR C 31  ? 1.745 2.263 1.916 -0.031 0.249  0.240  31  TYR CCC CE1 
3383  C CE2 . TYR C 31  ? 1.814 2.332 1.905 0.028  0.310  0.234  31  TYR CCC CE2 
3384  C CZ  . TYR C 31  ? 1.779 2.270 1.874 -0.008 0.278  0.238  31  TYR CCC CZ  
3385  O OH  . TYR C 31  ? 1.809 2.245 1.830 -0.017 0.275  0.241  31  TYR CCC OH  
3386  N N   . SER C 32  ? 1.720 2.699 2.287 0.026  0.350  0.285  32  SER CCC N   
3387  C CA  . SER C 32  ? 1.717 2.813 2.358 0.058  0.388  0.295  32  SER CCC CA  
3388  C C   . SER C 32  ? 1.747 2.803 2.309 0.129  0.411  0.281  32  SER CCC C   
3389  O O   . SER C 32  ? 1.735 2.850 2.339 0.176  0.409  0.273  32  SER CCC O   
3390  C CB  . SER C 32  ? 1.745 2.904 2.428 0.026  0.436  0.325  32  SER CCC CB  
3391  O OG  . SER C 32  ? 1.765 3.052 2.529 0.057  0.475  0.335  32  SER CCC OG  
3392  N N   . SER C 33  ? 1.776 2.731 2.224 0.137  0.430  0.276  33  SER CCC N   
3393  C CA  . SER C 33  ? 1.820 2.710 2.170 0.196  0.454  0.259  33  SER CCC CA  
3394  C C   . SER C 33  ? 1.820 2.688 2.165 0.238  0.423  0.236  33  SER CCC C   
3395  O O   . SER C 33  ? 1.859 2.782 2.230 0.293  0.446  0.236  33  SER CCC O   
3396  C CB  . SER C 33  ? 1.840 2.610 2.067 0.183  0.454  0.249  33  SER CCC CB  
3397  O OG  . SER C 33  ? 1.774 2.473 1.975 0.151  0.402  0.235  33  SER CCC OG  
3398  N N   . ILE C 34  ? 1.797 2.588 2.107 0.216  0.375  0.220  34  ILE CCC N   
3399  C CA  . ILE C 34  ? 1.792 2.544 2.084 0.250  0.344  0.201  34  ILE CCC CA  
3400  C C   . ILE C 34  ? 1.714 2.517 2.092 0.217  0.296  0.204  34  ILE CCC C   
3401  O O   . ILE C 34  ? 1.695 2.438 2.047 0.175  0.264  0.197  34  ILE CCC O   
3402  C CB  . ILE C 34  ? 1.826 2.438 1.992 0.255  0.334  0.177  34  ILE CCC CB  
3403  C CG1 . ILE C 34  ? 1.792 2.346 1.915 0.200  0.319  0.176  34  ILE CCC CG1 
3404  C CG2 . ILE C 34  ? 1.921 2.482 2.002 0.307  0.377  0.168  34  ILE CCC CG2 
3405  C CD1 . ILE C 34  ? 1.810 2.246 1.830 0.196  0.301  0.151  34  ILE CCC CD1 
3406  N N   . ASN C 35  ? 1.673 2.588 2.149 0.236  0.292  0.213  35  ASN CCC N   
3407  C CA  . ASN C 35  ? 1.595 2.578 2.164 0.203  0.248  0.215  35  ASN CCC CA  
3408  C C   . ASN C 35  ? 1.547 2.429 2.055 0.187  0.202  0.197  35  ASN CCC C   
3409  O O   . ASN C 35  ? 1.513 2.392 2.020 0.219  0.174  0.188  35  ASN CCC O   
3410  C CB  . ASN C 35  ? 1.609 2.710 2.264 0.249  0.245  0.219  35  ASN CCC CB  
3411  C CG  . ASN C 35  ? 1.569 2.767 2.333 0.210  0.203  0.223  35  ASN CCC CG  
3412  O OD1 . ASN C 35  ? 1.550 2.692 2.296 0.170  0.161  0.213  35  ASN CCC OD1 
3413  N ND2 . ASN C 35  ? 1.557 2.901 2.431 0.221  0.213  0.234  35  ASN CCC ND2 
3414  N N   . LYS C 36  ? 1.534 2.341 1.994 0.140  0.195  0.195  36  LYS CCC N   
3415  C CA  . LYS C 36  ? 1.525 2.247 1.937 0.116  0.155  0.180  36  LYS CCC CA  
3416  C C   . LYS C 36  ? 1.460 2.184 1.901 0.055  0.141  0.188  36  LYS CCC C   
3417  O O   . LYS C 36  ? 1.459 2.184 1.892 0.036  0.170  0.201  36  LYS CCC O   
3418  C CB  . LYS C 36  ? 1.600 2.207 1.898 0.130  0.165  0.166  36  LYS CCC CB  
3419  C CG  . LYS C 36  ? 1.704 2.277 1.948 0.187  0.185  0.157  36  LYS CCC CG  
3420  C CD  . LYS C 36  ? 1.745 2.314 1.995 0.218  0.157  0.149  36  LYS CCC CD  
3421  C CE  . LYS C 36  ? 1.845 2.361 2.028 0.279  0.179  0.142  36  LYS CCC CE  
3422  N NZ  . LYS C 36  ? 1.878 2.375 2.052 0.310  0.150  0.138  36  LYS CCC NZ  
3423  N N   . ASN C 37  ? 1.427 2.143 1.891 0.029  0.100  0.180  37  ASN CCC N   
3424  C CA  . ASN C 37  ? 1.435 2.129 1.912 -0.024 0.083  0.185  37  ASN CCC CA  
3425  C C   . ASN C 37  ? 1.436 2.029 1.822 -0.028 0.078  0.174  37  ASN CCC C   
3426  O O   . ASN C 37  ? 1.438 1.984 1.778 -0.006 0.062  0.158  37  ASN CCC O   
3427  C CB  . ASN C 37  ? 1.455 2.185 1.993 -0.048 0.042  0.179  37  ASN CCC CB  
3428  C CG  . ASN C 37  ? 1.502 2.342 2.142 -0.067 0.046  0.191  37  ASN CCC CG  
3429  O OD1 . ASN C 37  ? 1.537 2.445 2.230 -0.049 0.026  0.185  37  ASN CCC OD1 
3430  N ND2 . ASN C 37  ? 1.526 2.386 2.195 -0.103 0.072  0.210  37  ASN CCC ND2 
3431  N N   . TYR C 38  ? 1.440 2.003 1.802 -0.054 0.091  0.184  38  TYR CCC N   
3432  C CA  . TYR C 38  ? 1.438 1.922 1.721 -0.056 0.088  0.176  38  TYR CCC CA  
3433  C C   . TYR C 38  ? 1.430 1.880 1.715 -0.082 0.054  0.170  38  TYR CCC C   
3434  O O   . TYR C 38  ? 1.417 1.842 1.691 -0.105 0.054  0.180  38  TYR CCC O   
3435  C CB  . TYR C 38  ? 1.430 1.906 1.678 -0.059 0.121  0.191  38  TYR CCC CB  
3436  C CG  . TYR C 38  ? 1.439 1.905 1.638 -0.024 0.149  0.184  38  TYR CCC CG  
3437  C CD1 . TYR C 38  ? 1.448 1.956 1.675 0.006  0.162  0.182  38  TYR CCC CD1 
3438  C CD2 . TYR C 38  ? 1.460 1.874 1.580 -0.020 0.160  0.179  38  TYR CCC CD2 
3439  C CE1 . TYR C 38  ? 1.491 1.976 1.664 0.042  0.189  0.174  38  TYR CCC CE1 
3440  C CE2 . TYR C 38  ? 1.506 1.899 1.571 0.009  0.184  0.168  38  TYR CCC CE2 
3441  C CZ  . TYR C 38  ? 1.522 1.945 1.611 0.041  0.200  0.166  38  TYR CCC CZ  
3442  O OH  . TYR C 38  ? 1.562 1.952 1.588 0.074  0.226  0.154  38  TYR CCC OH  
3443  N N   . LEU C 39  ? 1.446 1.891 1.739 -0.074 0.027  0.154  39  LEU CCC N   
3444  C CA  . LEU C 39  ? 1.475 1.889 1.769 -0.093 -0.007 0.144  39  LEU CCC CA  
3445  C C   . LEU C 39  ? 1.444 1.815 1.687 -0.073 -0.020 0.124  39  LEU CCC C   
3446  O O   . LEU C 39  ? 1.443 1.819 1.673 -0.047 -0.013 0.119  39  LEU CCC O   
3447  C CB  . LEU C 39  ? 1.528 1.993 1.892 -0.107 -0.027 0.145  39  LEU CCC CB  
3448  C CG  . LEU C 39  ? 1.560 1.998 1.930 -0.126 -0.063 0.133  39  LEU CCC CG  
3449  C CD1 . LEU C 39  ? 1.563 1.982 1.903 -0.102 -0.085 0.114  39  LEU CCC CD1 
3450  C CD2 . LEU C 39  ? 1.582 1.958 1.915 -0.145 -0.065 0.134  39  LEU CCC CD2 
3451  N N   . ALA C 40  ? 1.421 1.747 1.632 -0.083 -0.035 0.115  40  ALA CCC N   
3452  C CA  . ALA C 40  ? 1.416 1.701 1.577 -0.071 -0.043 0.098  40  ALA CCC CA  
3453  C C   . ALA C 40  ? 1.425 1.689 1.586 -0.079 -0.070 0.088  40  ALA CCC C   
3454  O O   . ALA C 40  ? 1.429 1.699 1.621 -0.096 -0.083 0.093  40  ALA CCC O   
3455  C CB  . ALA C 40  ? 1.412 1.672 1.528 -0.072 -0.027 0.096  40  ALA CCC CB  
3456  N N   . TRP C 41  ? 1.439 1.673 1.561 -0.068 -0.075 0.074  41  TRP CCC N   
3457  C CA  . TRP C 41  ? 1.437 1.646 1.544 -0.069 -0.096 0.062  41  TRP CCC CA  
3458  C C   . TRP C 41  ? 1.448 1.627 1.509 -0.067 -0.087 0.052  41  TRP CCC C   
3459  O O   . TRP C 41  ? 1.455 1.624 1.487 -0.062 -0.070 0.049  41  TRP CCC O   
3460  C CB  . TRP C 41  ? 1.439 1.650 1.546 -0.054 -0.111 0.056  41  TRP CCC CB  
3461  C CG  . TRP C 41  ? 1.438 1.690 1.598 -0.060 -0.130 0.061  41  TRP CCC CG  
3462  C CD1 . TRP C 41  ? 1.451 1.750 1.648 -0.049 -0.126 0.070  41  TRP CCC CD1 
3463  C CD2 . TRP C 41  ? 1.428 1.679 1.612 -0.078 -0.155 0.055  41  TRP CCC CD2 
3464  N NE1 . TRP C 41  ? 1.434 1.774 1.685 -0.064 -0.149 0.070  41  TRP CCC NE1 
3465  C CE2 . TRP C 41  ? 1.434 1.738 1.674 -0.085 -0.168 0.061  41  TRP CCC CE2 
3466  C CE3 . TRP C 41  ? 1.442 1.652 1.603 -0.089 -0.168 0.045  41  TRP CCC CE3 
3467  C CZ2 . TRP C 41  ? 1.455 1.769 1.728 -0.109 -0.195 0.055  41  TRP CCC CZ2 
3468  C CZ3 . TRP C 41  ? 1.473 1.681 1.658 -0.108 -0.193 0.039  41  TRP CCC CZ3 
3469  C CH2 . TRP C 41  ? 1.478 1.736 1.719 -0.121 -0.207 0.043  41  TRP CCC CH2 
3470  N N   . TYR C 42  ? 1.440 1.608 1.497 -0.073 -0.096 0.047  42  TYR CCC N   
3471  C CA  . TYR C 42  ? 1.427 1.584 1.454 -0.072 -0.087 0.037  42  TYR CCC CA  
3472  C C   . TYR C 42  ? 1.440 1.576 1.449 -0.064 -0.099 0.025  42  TYR CCC C   
3473  O O   . TYR C 42  ? 1.461 1.584 1.481 -0.063 -0.118 0.024  42  TYR CCC O   
3474  C CB  . TYR C 42  ? 1.424 1.597 1.460 -0.076 -0.084 0.044  42  TYR CCC CB  
3475  C CG  . TYR C 42  ? 1.435 1.627 1.477 -0.081 -0.071 0.055  42  TYR CCC CG  
3476  C CD1 . TYR C 42  ? 1.460 1.661 1.479 -0.086 -0.057 0.049  42  TYR CCC CD1 
3477  C CD2 . TYR C 42  ? 1.437 1.635 1.503 -0.085 -0.071 0.070  42  TYR CCC CD2 
3478  C CE1 . TYR C 42  ? 1.479 1.692 1.492 -0.089 -0.046 0.056  42  TYR CCC CE1 
3479  C CE2 . TYR C 42  ? 1.445 1.658 1.508 -0.088 -0.056 0.080  42  TYR CCC CE2 
3480  C CZ  . TYR C 42  ? 1.481 1.699 1.514 -0.088 -0.044 0.073  42  TYR CCC CZ  
3481  O OH  . TYR C 42  ? 1.524 1.752 1.544 -0.089 -0.030 0.080  42  TYR CCC OH  
3482  N N   . GLN C 43  ? 1.438 1.564 1.414 -0.062 -0.087 0.016  43  GLN CCC N   
3483  C CA  . GLN C 43  ? 1.433 1.542 1.384 -0.053 -0.090 0.005  43  GLN CCC CA  
3484  C C   . GLN C 43  ? 1.426 1.559 1.380 -0.054 -0.078 0.001  43  GLN CCC C   
3485  O O   . GLN C 43  ? 1.413 1.571 1.373 -0.066 -0.064 0.003  43  GLN CCC O   
3486  C CB  . GLN C 43  ? 1.429 1.512 1.338 -0.050 -0.080 0.000  43  GLN CCC CB  
3487  C CG  . GLN C 43  ? 1.439 1.520 1.319 -0.051 -0.062 -0.009 43  GLN CCC CG  
3488  C CD  . GLN C 43  ? 1.460 1.506 1.291 -0.052 -0.046 -0.010 43  GLN CCC CD  
3489  O OE1 . GLN C 43  ? 1.456 1.505 1.271 -0.067 -0.021 -0.011 43  GLN CCC OE1 
3490  N NE2 . GLN C 43  ? 1.452 1.465 1.258 -0.036 -0.062 -0.008 43  GLN CCC NE2 
3491  N N   . GLN C 44  ? 1.432 1.559 1.382 -0.041 -0.085 -0.006 44  GLN CCC N   
3492  C CA  . GLN C 44  ? 1.441 1.602 1.397 -0.033 -0.074 -0.011 44  GLN CCC CA  
3493  C C   . GLN C 44  ? 1.481 1.628 1.409 -0.018 -0.067 -0.023 44  GLN CCC C   
3494  O O   . GLN C 44  ? 1.500 1.614 1.416 -0.001 -0.081 -0.029 44  GLN CCC O   
3495  C CB  . GLN C 44  ? 1.450 1.619 1.429 -0.022 -0.085 -0.004 44  GLN CCC CB  
3496  C CG  . GLN C 44  ? 1.480 1.682 1.463 -0.002 -0.079 -0.009 44  GLN CCC CG  
3497  C CD  . GLN C 44  ? 1.495 1.704 1.493 0.013  -0.090 0.002  44  GLN CCC CD  
3498  O OE1 . GLN C 44  ? 1.518 1.678 1.509 0.020  -0.103 0.009  44  GLN CCC OE1 
3499  N NE2 . GLN C 44  ? 1.492 1.762 1.508 0.017  -0.084 0.004  44  GLN CCC NE2 
3500  N N   . LYS C 45  ? 1.507 1.671 1.420 -0.028 -0.045 -0.028 45  LYS CCC N   
3501  C CA  . LYS C 45  ? 1.565 1.732 1.454 -0.013 -0.029 -0.039 45  LYS CCC CA  
3502  C C   . LYS C 45  ? 1.542 1.765 1.463 0.002  -0.025 -0.041 45  LYS CCC C   
3503  O O   . LYS C 45  ? 1.495 1.770 1.450 -0.011 -0.021 -0.037 45  LYS CCC O   
3504  C CB  . LYS C 45  ? 1.628 1.794 1.489 -0.033 -0.003 -0.040 45  LYS CCC CB  
3505  C CG  . LYS C 45  ? 1.690 1.791 1.499 -0.030 -0.007 -0.039 45  LYS CCC CG  
3506  C CD  . LYS C 45  ? 1.750 1.833 1.521 -0.049 0.021  -0.035 45  LYS CCC CD  
3507  C CE  . LYS C 45  ? 1.747 1.814 1.520 -0.070 0.021  -0.026 45  LYS CCC CE  
3508  N NZ  . LYS C 45  ? 1.783 1.818 1.511 -0.091 0.050  -0.023 45  LYS CCC NZ  
3509  N N   . PRO C 46  ? 1.575 1.785 1.484 0.034  -0.027 -0.049 46  PRO CCC N   
3510  C CA  . PRO C 46  ? 1.562 1.825 1.499 0.059  -0.023 -0.051 46  PRO CCC CA  
3511  C C   . PRO C 46  ? 1.535 1.890 1.508 0.046  0.000  -0.052 46  PRO CCC C   
3512  O O   . PRO C 46  ? 1.510 1.878 1.471 0.027  0.024  -0.057 46  PRO CCC O   
3513  C CB  . PRO C 46  ? 1.613 1.839 1.511 0.094  -0.018 -0.063 46  PRO CCC CB  
3514  C CG  . PRO C 46  ? 1.656 1.795 1.512 0.088  -0.037 -0.066 46  PRO CCC CG  
3515  C CD  . PRO C 46  ? 1.627 1.768 1.489 0.051  -0.037 -0.057 46  PRO CCC CD  
3516  N N   . GLY C 47  ? 1.531 1.948 1.545 0.056  -0.008 -0.048 47  GLY CCC N   
3517  C CA  . GLY C 47  ? 1.510 2.031 1.569 0.043  0.008  -0.051 47  GLY CCC CA  
3518  C C   . GLY C 47  ? 1.458 1.999 1.533 -0.001 0.002  -0.047 47  GLY CCC C   
3519  O O   . GLY C 47  ? 1.416 2.043 1.531 -0.012 0.003  -0.050 47  GLY CCC O   
3520  N N   . GLN C 48  ? 1.470 1.935 1.513 -0.021 -0.004 -0.042 48  GLN CCC N   
3521  C CA  . GLN C 48  ? 1.479 1.940 1.523 -0.060 -0.007 -0.039 48  GLN CCC CA  
3522  C C   . GLN C 48  ? 1.422 1.860 1.469 -0.048 -0.031 -0.027 48  GLN CCC C   
3523  O O   . GLN C 48  ? 1.427 1.833 1.469 -0.017 -0.045 -0.021 48  GLN CCC O   
3524  C CB  . GLN C 48  ? 1.553 1.944 1.556 -0.082 0.006  -0.039 48  GLN CCC CB  
3525  C CG  . GLN C 48  ? 1.603 2.000 1.589 -0.092 0.034  -0.046 48  GLN CCC CG  
3526  C CD  . GLN C 48  ? 1.655 1.971 1.588 -0.105 0.043  -0.043 48  GLN CCC CD  
3527  O OE1 . GLN C 48  ? 1.683 1.947 1.600 -0.105 0.028  -0.037 48  GLN CCC OE1 
3528  N NE2 . GLN C 48  ? 1.701 2.009 1.607 -0.112 0.069  -0.047 48  GLN CCC NE2 
3529  N N   . PRO C 49  ? 1.366 1.812 1.415 -0.074 -0.035 -0.025 49  PRO CCC N   
3530  C CA  . PRO C 49  ? 1.345 1.756 1.388 -0.067 -0.052 -0.012 49  PRO CCC CA  
3531  C C   . PRO C 49  ? 1.356 1.693 1.373 -0.073 -0.050 -0.007 49  PRO CCC C   
3532  O O   . PRO C 49  ? 1.382 1.696 1.383 -0.082 -0.037 -0.014 49  PRO CCC O   
3533  C CB  . PRO C 49  ? 1.341 1.789 1.387 -0.094 -0.052 -0.015 49  PRO CCC CB  
3534  C CG  . PRO C 49  ? 1.356 1.814 1.395 -0.127 -0.032 -0.029 49  PRO CCC CG  
3535  C CD  . PRO C 49  ? 1.366 1.850 1.419 -0.113 -0.022 -0.035 49  PRO CCC CD  
3536  N N   . PRO C 50  ? 1.355 1.660 1.371 -0.067 -0.061 0.005  50  PRO CCC N   
3537  C CA  . PRO C 50  ? 1.363 1.617 1.366 -0.074 -0.061 0.010  50  PRO CCC CA  
3538  C C   . PRO C 50  ? 1.383 1.627 1.367 -0.096 -0.046 0.006  50  PRO CCC C   
3539  O O   . PRO C 50  ? 1.368 1.636 1.350 -0.111 -0.041 0.003  50  PRO CCC O   
3540  C CB  . PRO C 50  ? 1.345 1.586 1.359 -0.068 -0.072 0.025  50  PRO CCC CB  
3541  C CG  . PRO C 50  ? 1.361 1.620 1.384 -0.048 -0.081 0.029  50  PRO CCC CG  
3542  C CD  . PRO C 50  ? 1.359 1.674 1.387 -0.051 -0.075 0.018  50  PRO CCC CD  
3543  N N   . LYS C 51  ? 1.417 1.621 1.382 -0.096 -0.042 0.005  51  LYS CCC N   
3544  C CA  . LYS C 51  ? 1.472 1.646 1.409 -0.108 -0.028 0.003  51  LYS CCC CA  
3545  C C   . LYS C 51  ? 1.498 1.653 1.442 -0.096 -0.036 0.014  51  LYS CCC C   
3546  O O   . LYS C 51  ? 1.472 1.624 1.435 -0.083 -0.051 0.019  51  LYS CCC O   
3547  C CB  . LYS C 51  ? 1.515 1.657 1.420 -0.109 -0.018 -0.003 51  LYS CCC CB  
3548  C CG  . LYS C 51  ? 1.565 1.661 1.428 -0.120 0.000  -0.004 51  LYS CCC CG  
3549  C CD  . LYS C 51  ? 1.631 1.694 1.455 -0.125 0.015  -0.009 51  LYS CCC CD  
3550  C CE  . LYS C 51  ? 1.716 1.711 1.485 -0.127 0.031  -0.005 51  LYS CCC CE  
3551  N NZ  . LYS C 51  ? 1.776 1.756 1.522 -0.160 0.053  -0.013 51  LYS CCC NZ  
3552  N N   . LEU C 52  ? 1.550 1.696 1.482 -0.102 -0.025 0.017  52  LEU CCC N   
3553  C CA  . LEU C 52  ? 1.555 1.691 1.495 -0.088 -0.026 0.027  52  LEU CCC CA  
3554  C C   . LEU C 52  ? 1.586 1.684 1.500 -0.076 -0.023 0.026  52  LEU CCC C   
3555  O O   . LEU C 52  ? 1.622 1.683 1.492 -0.083 -0.008 0.019  52  LEU CCC O   
3556  C CB  . LEU C 52  ? 1.576 1.712 1.501 -0.094 -0.011 0.028  52  LEU CCC CB  
3557  C CG  . LEU C 52  ? 1.592 1.729 1.528 -0.078 -0.006 0.039  52  LEU CCC CG  
3558  C CD1 . LEU C 52  ? 1.551 1.726 1.536 -0.075 -0.018 0.053  52  LEU CCC CD1 
3559  C CD2 . LEU C 52  ? 1.632 1.754 1.534 -0.080 0.013  0.035  52  LEU CCC CD2 
3560  N N   . LEU C 53  ? 1.569 1.674 1.506 -0.059 -0.039 0.033  53  LEU CCC N   
3561  C CA  . LEU C 53  ? 1.615 1.692 1.529 -0.039 -0.043 0.034  53  LEU CCC CA  
3562  C C   . LEU C 53  ? 1.636 1.723 1.563 -0.020 -0.038 0.044  53  LEU CCC C   
3563  O O   . LEU C 53  ? 1.697 1.745 1.582 -0.004 -0.025 0.044  53  LEU CCC O   
3564  C CB  . LEU C 53  ? 1.624 1.711 1.556 -0.032 -0.068 0.033  53  LEU CCC CB  
3565  C CG  . LEU C 53  ? 1.640 1.714 1.554 -0.042 -0.071 0.023  53  LEU CCC CG  
3566  C CD1 . LEU C 53  ? 1.642 1.720 1.569 -0.034 -0.097 0.019  53  LEU CCC CD1 
3567  C CD2 . LEU C 53  ? 1.694 1.726 1.550 -0.042 -0.052 0.018  53  LEU CCC CD2 
3568  N N   . ILE C 54  ? 1.586 1.721 1.566 -0.022 -0.045 0.052  54  ILE CCC N   
3569  C CA  . ILE C 54  ? 1.557 1.721 1.564 -0.002 -0.040 0.062  54  ILE CCC CA  
3570  C C   . ILE C 54  ? 1.495 1.695 1.535 -0.014 -0.027 0.070  54  ILE CCC C   
3571  O O   . ILE C 54  ? 1.485 1.703 1.552 -0.035 -0.036 0.073  54  ILE CCC O   
3572  C CB  . ILE C 54  ? 1.565 1.762 1.610 0.011  -0.066 0.065  54  ILE CCC CB  
3573  C CG1 . ILE C 54  ? 1.636 1.790 1.632 0.035  -0.073 0.061  54  ILE CCC CG1 
3574  C CG2 . ILE C 54  ? 1.568 1.824 1.668 0.023  -0.063 0.077  54  ILE CCC CG2 
3575  C CD1 . ILE C 54  ? 1.668 1.856 1.693 0.051  -0.104 0.062  54  ILE CCC CD1 
3576  N N   . TYR C 55  ? 1.451 1.655 1.483 0.003  -0.005 0.075  55  TYR CCC N   
3577  C CA  . TYR C 55  ? 1.423 1.661 1.480 -0.002 0.012  0.086  55  TYR CCC CA  
3578  C C   . TYR C 55  ? 1.447 1.731 1.542 0.025  0.021  0.096  55  TYR CCC C   
3579  O O   . TYR C 55  ? 1.473 1.755 1.567 0.050  0.011  0.094  55  TYR CCC O   
3580  C CB  . TYR C 55  ? 1.428 1.626 1.427 -0.008 0.033  0.078  55  TYR CCC CB  
3581  C CG  . TYR C 55  ? 1.468 1.617 1.411 0.015  0.052  0.069  55  TYR CCC CG  
3582  C CD1 . TYR C 55  ? 1.493 1.582 1.383 0.011  0.050  0.056  55  TYR CCC CD1 
3583  C CD2 . TYR C 55  ? 1.515 1.671 1.450 0.040  0.075  0.074  55  TYR CCC CD2 
3584  C CE1 . TYR C 55  ? 1.573 1.600 1.401 0.030  0.069  0.049  55  TYR CCC CE1 
3585  C CE2 . TYR C 55  ? 1.574 1.672 1.448 0.065  0.094  0.066  55  TYR CCC CE2 
3586  C CZ  . TYR C 55  ? 1.606 1.632 1.423 0.059  0.090  0.053  55  TYR CCC CZ  
3587  O OH  . TYR C 55  ? 1.681 1.633 1.428 0.081  0.110  0.045  55  TYR CCC OH  
3588  N N   . TRP C 56  ? 1.480 1.806 1.606 0.023  0.040  0.108  56  TRP CCC N   
3589  C CA  . TRP C 56  ? 1.493 1.891 1.681 0.041  0.049  0.122  56  TRP CCC CA  
3590  C C   . TRP C 56  ? 1.435 1.869 1.670 0.048  0.018  0.120  56  TRP CCC C   
3591  O O   . TRP C 56  ? 1.417 1.879 1.665 0.084  0.019  0.122  56  TRP CCC O   
3592  C CB  . TRP C 56  ? 1.591 1.985 1.750 0.080  0.081  0.123  56  TRP CCC CB  
3593  C CG  . TRP C 56  ? 1.670 2.021 1.769 0.076  0.109  0.120  56  TRP CCC CG  
3594  C CD1 . TRP C 56  ? 1.681 2.021 1.765 0.044  0.111  0.122  56  TRP CCC CD1 
3595  C CD2 . TRP C 56  ? 1.748 2.056 1.784 0.109  0.138  0.113  56  TRP CCC CD2 
3596  N NE1 . TRP C 56  ? 1.748 2.046 1.767 0.052  0.136  0.115  56  TRP CCC NE1 
3597  C CE2 . TRP C 56  ? 1.805 2.080 1.792 0.090  0.154  0.108  56  TRP CCC CE2 
3598  C CE3 . TRP C 56  ? 1.786 2.075 1.797 0.155  0.151  0.109  56  TRP CCC CE3 
3599  C CZ2 . TRP C 56  ? 1.882 2.104 1.794 0.111  0.181  0.097  56  TRP CCC CZ2 
3600  C CZ3 . TRP C 56  ? 1.881 2.110 1.816 0.178  0.181  0.099  56  TRP CCC CZ3 
3601  C CH2 . TRP C 56  ? 1.916 2.112 1.802 0.154  0.196  0.092  56  TRP CCC CH2 
3602  N N   . ALA C 57  ? 1.391 1.819 1.643 0.017  -0.010 0.116  57  ALA CCC N   
3603  C CA  . ALA C 57  ? 1.366 1.836 1.670 0.009  -0.044 0.114  57  ALA CCC CA  
3604  C C   . ALA C 57  ? 1.361 1.803 1.631 0.038  -0.065 0.103  57  ALA CCC C   
3605  O O   . ALA C 57  ? 1.300 1.749 1.586 0.026  -0.099 0.096  57  ALA CCC O   
3606  C CB  . ALA C 57  ? 1.375 1.938 1.761 0.010  -0.039 0.127  57  ALA CCC CB  
3607  N N   . SER C 58  ? 1.406 1.811 1.622 0.074  -0.047 0.102  58  SER CCC N   
3608  C CA  . SER C 58  ? 1.468 1.851 1.650 0.114  -0.061 0.098  58  SER CCC CA  
3609  C C   . SER C 58  ? 1.529 1.817 1.617 0.134  -0.039 0.093  58  SER CCC C   
3610  O O   . SER C 58  ? 1.566 1.811 1.608 0.158  -0.052 0.090  58  SER CCC O   
3611  C CB  . SER C 58  ? 1.487 1.949 1.724 0.149  -0.062 0.108  58  SER CCC CB  
3612  O OG  . SER C 58  ? 1.514 1.984 1.748 0.167  -0.024 0.115  58  SER CCC OG  
3613  N N   . THR C 59  ? 1.568 1.820 1.623 0.125  -0.008 0.092  59  THR CCC N   
3614  C CA  . THR C 59  ? 1.634 1.790 1.597 0.136  0.015  0.084  59  THR CCC CA  
3615  C C   . THR C 59  ? 1.609 1.712 1.532 0.100  0.006  0.073  59  THR CCC C   
3616  O O   . THR C 59  ? 1.553 1.684 1.508 0.065  0.000  0.071  59  THR CCC O   
3617  C CB  . THR C 59  ? 1.682 1.824 1.623 0.137  0.048  0.083  59  THR CCC CB  
3618  O OG1 . THR C 59  ? 1.694 1.916 1.699 0.155  0.056  0.094  59  THR CCC OG1 
3619  C CG2 . THR C 59  ? 1.770 1.820 1.623 0.164  0.071  0.076  59  THR CCC CG2 
3620  N N   . ARG C 60  ? 1.650 1.679 1.505 0.109  0.009  0.068  60  ARG CCC N   
3621  C CA  . ARG C 60  ? 1.652 1.637 1.471 0.076  0.005  0.058  60  ARG CCC CA  
3622  C C   . ARG C 60  ? 1.674 1.613 1.449 0.048  0.030  0.048  60  ARG CCC C   
3623  O O   . ARG C 60  ? 1.721 1.615 1.453 0.063  0.052  0.046  60  ARG CCC O   
3624  C CB  . ARG C 60  ? 1.714 1.642 1.478 0.096  -0.001 0.060  60  ARG CCC CB  
3625  C CG  . ARG C 60  ? 1.716 1.689 1.514 0.128  -0.030 0.068  60  ARG CCC CG  
3626  C CD  . ARG C 60  ? 1.756 1.690 1.510 0.133  -0.046 0.067  60  ARG CCC CD  
3627  N NE  . ARG C 60  ? 1.853 1.688 1.514 0.144  -0.023 0.069  60  ARG CCC NE  
3628  C CZ  . ARG C 60  ? 1.954 1.743 1.567 0.188  -0.015 0.079  60  ARG CCC CZ  
3629  N NH1 . ARG C 60  ? 1.959 1.807 1.618 0.229  -0.029 0.086  60  ARG CCC NH1 
3630  N NH2 . ARG C 60  ? 2.049 1.732 1.569 0.193  0.009  0.081  60  ARG CCC NH2 
3631  N N   . GLU C 61  ? 1.660 1.609 1.444 0.010  0.026  0.040  61  GLU CCC N   
3632  C CA  . GLU C 61  ? 1.730 1.645 1.475 -0.023 0.044  0.027  61  GLU CCC CA  
3633  C C   . GLU C 61  ? 1.808 1.644 1.484 -0.031 0.058  0.021  61  GLU CCC C   
3634  O O   . GLU C 61  ? 1.798 1.618 1.463 -0.016 0.049  0.027  61  GLU CCC O   
3635  C CB  . GLU C 61  ? 1.714 1.685 1.503 -0.053 0.032  0.022  61  GLU CCC CB  
3636  C CG  . GLU C 61  ? 1.788 1.746 1.549 -0.088 0.044  0.008  61  GLU CCC CG  
3637  C CD  . GLU C 61  ? 1.847 1.795 1.586 -0.092 0.057  0.003  61  GLU CCC CD  
3638  O OE1 . GLU C 61  ? 1.932 1.817 1.618 -0.081 0.075  -0.001 61  GLU CCC OE1 
3639  O OE2 . GLU C 61  ? 1.830 1.827 1.599 -0.102 0.050  0.003  61  GLU CCC OE2 
3640  N N   . SER C 62  ? 1.900 1.683 1.524 -0.055 0.079  0.009  62  SER CCC N   
3641  C CA  . SER C 62  ? 1.973 1.677 1.529 -0.077 0.097  0.002  62  SER CCC CA  
3642  C C   . SER C 62  ? 1.901 1.641 1.483 -0.102 0.088  0.001  62  SER CCC C   
3643  O O   . SER C 62  ? 1.789 1.606 1.429 -0.119 0.075  -0.003 62  SER CCC O   
3644  C CB  . SER C 62  ? 2.068 1.728 1.581 -0.113 0.116  -0.015 62  SER CCC CB  
3645  O OG  . SER C 62  ? 2.020 1.756 1.583 -0.138 0.105  -0.024 62  SER CCC OG  
3646  N N   . GLY C 63  ? 1.956 1.640 1.492 -0.097 0.097  0.007  63  GLY CCC N   
3647  C CA  . GLY C 63  ? 1.944 1.647 1.486 -0.120 0.098  0.006  63  GLY CCC CA  
3648  C C   . GLY C 63  ? 1.868 1.617 1.447 -0.088 0.073  0.015  63  GLY CCC C   
3649  O O   . GLY C 63  ? 1.821 1.607 1.421 -0.103 0.069  0.011  63  GLY CCC O   
3650  N N   . VAL C 64  ? 1.825 1.572 1.410 -0.047 0.056  0.025  64  VAL CCC N   
3651  C CA  . VAL C 64  ? 1.742 1.539 1.369 -0.019 0.026  0.031  64  VAL CCC CA  
3652  C C   . VAL C 64  ? 1.799 1.543 1.374 0.020  0.021  0.042  64  VAL CCC C   
3653  O O   . VAL C 64  ? 1.810 1.519 1.359 0.047  0.027  0.050  64  VAL CCC O   
3654  C CB  . VAL C 64  ? 1.666 1.531 1.363 -0.009 0.008  0.033  64  VAL CCC CB  
3655  C CG1 . VAL C 64  ? 1.621 1.533 1.361 0.011  -0.024 0.037  64  VAL CCC CG1 
3656  C CG2 . VAL C 64  ? 1.629 1.539 1.367 -0.041 0.012  0.024  64  VAL CCC CG2 
3657  N N   . PRO C 65  ? 1.857 1.594 1.411 0.029  0.009  0.044  65  PRO CCC N   
3658  C CA  . PRO C 65  ? 1.962 1.649 1.458 0.070  -0.001 0.056  65  PRO CCC CA  
3659  C C   . PRO C 65  ? 1.964 1.693 1.499 0.112  -0.029 0.063  65  PRO CCC C   
3660  O O   . PRO C 65  ? 1.887 1.691 1.500 0.104  -0.044 0.058  65  PRO CCC O   
3661  C CB  . PRO C 65  ? 1.972 1.668 1.455 0.068  -0.014 0.053  65  PRO CCC CB  
3662  C CG  . PRO C 65  ? 1.924 1.644 1.432 0.023  0.005  0.041  65  PRO CCC CG  
3663  C CD  . PRO C 65  ? 1.840 1.612 1.416 0.005  0.005  0.035  65  PRO CCC CD  
3664  N N   . ASP C 66  ? 2.064 1.744 1.540 0.155  -0.034 0.075  66  ASP CCC N   
3665  C CA  . ASP C 66  ? 2.069 1.790 1.573 0.204  -0.061 0.084  66  ASP CCC CA  
3666  C C   . ASP C 66  ? 1.990 1.800 1.563 0.205  -0.104 0.077  66  ASP CCC C   
3667  O O   . ASP C 66  ? 1.945 1.832 1.590 0.220  -0.125 0.078  66  ASP CCC O   
3668  C CB  . ASP C 66  ? 2.203 1.845 1.616 0.254  -0.060 0.099  66  ASP CCC CB  
3669  C CG  . ASP C 66  ? 2.316 1.835 1.627 0.244  -0.017 0.105  66  ASP CCC CG  
3670  O OD1 . ASP C 66  ? 2.361 1.834 1.623 0.218  -0.005 0.104  66  ASP CCC OD1 
3671  O OD2 . ASP C 66  ? 2.377 1.843 1.657 0.260  0.006  0.111  66  ASP CCC OD2 
3672  N N   . ARG C 67  ? 1.967 1.765 1.515 0.187  -0.114 0.070  67  ARG CCC N   
3673  C CA  . ARG C 67  ? 1.913 1.772 1.502 0.189  -0.157 0.060  67  ARG CCC CA  
3674  C C   . ARG C 67  ? 1.768 1.710 1.459 0.158  -0.169 0.051  67  ARG CCC C   
3675  O O   . ARG C 67  ? 1.714 1.715 1.453 0.160  -0.207 0.044  67  ARG CCC O   
3676  C CB  . ARG C 67  ? 1.970 1.782 1.497 0.177  -0.157 0.053  67  ARG CCC CB  
3677  C CG  . ARG C 67  ? 1.937 1.731 1.464 0.135  -0.123 0.045  67  ARG CCC CG  
3678  C CD  . ARG C 67  ? 1.970 1.738 1.449 0.129  -0.128 0.036  67  ARG CCC CD  
3679  N NE  . ARG C 67  ? 1.952 1.713 1.433 0.094  -0.094 0.029  67  ARG CCC NE  
3680  C CZ  . ARG C 67  ? 2.022 1.730 1.449 0.080  -0.054 0.036  67  ARG CCC CZ  
3681  N NH1 . ARG C 67  ? 2.116 1.756 1.471 0.099  -0.039 0.051  67  ARG CCC NH1 
3682  N NH2 . ARG C 67  ? 2.014 1.736 1.458 0.047  -0.028 0.028  67  ARG CCC NH2 
3683  N N   . PHE C 68  ? 1.707 1.651 1.425 0.129  -0.140 0.050  68  PHE CCC N   
3684  C CA  . PHE C 68  ? 1.635 1.648 1.440 0.103  -0.144 0.046  68  PHE CCC CA  
3685  C C   . PHE C 68  ? 1.624 1.684 1.476 0.124  -0.145 0.056  68  PHE CCC C   
3686  O O   . PHE C 68  ? 1.646 1.669 1.461 0.145  -0.120 0.064  68  PHE CCC O   
3687  C CB  . PHE C 68  ? 1.595 1.591 1.401 0.069  -0.114 0.041  68  PHE CCC CB  
3688  C CG  . PHE C 68  ? 1.582 1.562 1.371 0.047  -0.115 0.030  68  PHE CCC CG  
3689  C CD1 . PHE C 68  ? 1.538 1.558 1.376 0.029  -0.134 0.023  68  PHE CCC CD1 
3690  C CD2 . PHE C 68  ? 1.636 1.559 1.356 0.045  -0.094 0.029  68  PHE CCC CD2 
3691  C CE1 . PHE C 68  ? 1.554 1.557 1.373 0.016  -0.133 0.012  68  PHE CCC CE1 
3692  C CE2 . PHE C 68  ? 1.642 1.559 1.350 0.029  -0.092 0.019  68  PHE CCC CE2 
3693  C CZ  . PHE C 68  ? 1.602 1.560 1.360 0.018  -0.111 0.010  68  PHE CCC CZ  
3694  N N   . SER C 69  ? 1.583 1.721 1.513 0.118  -0.170 0.054  69  SER CCC N   
3695  C CA  . SER C 69  ? 1.573 1.779 1.564 0.136  -0.170 0.064  69  SER CCC CA  
3696  C C   . SER C 69  ? 1.521 1.805 1.602 0.103  -0.187 0.061  69  SER CCC C   
3697  O O   . SER C 69  ? 1.523 1.821 1.619 0.086  -0.219 0.051  69  SER CCC O   
3698  C CB  . SER C 69  ? 1.634 1.856 1.612 0.183  -0.191 0.070  69  SER CCC CB  
3699  O OG  . SER C 69  ? 1.661 1.901 1.639 0.182  -0.232 0.061  69  SER CCC OG  
3700  N N   . GLY C 70  ? 1.487 1.812 1.618 0.093  -0.165 0.069  70  GLY CCC N   
3701  C CA  . GLY C 70  ? 1.453 1.846 1.665 0.060  -0.172 0.071  70  GLY CCC CA  
3702  C C   . GLY C 70  ? 1.453 1.936 1.735 0.079  -0.175 0.081  70  GLY CCC C   
3703  O O   . GLY C 70  ? 1.446 1.929 1.709 0.120  -0.157 0.089  70  GLY CCC O   
3704  N N   . SER C 71  ? 1.467 2.023 1.827 0.051  -0.198 0.080  71  SER CCC N   
3705  C CA  . SER C 71  ? 1.492 2.158 1.942 0.056  -0.198 0.090  71  SER CCC CA  
3706  C C   . SER C 71  ? 1.478 2.179 1.991 0.001  -0.189 0.094  71  SER CCC C   
3707  O O   . SER C 71  ? 1.483 2.115 1.960 -0.031 -0.187 0.089  71  SER CCC O   
3708  C CB  . SER C 71  ? 1.527 2.259 2.013 0.074  -0.242 0.083  71  SER CCC CB  
3709  O OG  . SER C 71  ? 1.540 2.257 2.027 0.035  -0.280 0.067  71  SER CCC OG  
3710  N N   . GLY C 72  ? 1.465 2.267 2.065 -0.006 -0.179 0.106  72  GLY CCC N   
3711  C CA  . GLY C 72  ? 1.443 2.277 2.103 -0.060 -0.166 0.114  72  GLY CCC CA  
3712  C C   . GLY C 72  ? 1.432 2.370 2.172 -0.056 -0.136 0.132  72  GLY CCC C   
3713  O O   . GLY C 72  ? 1.413 2.359 2.133 -0.010 -0.105 0.141  72  GLY CCC O   
3714  N N   . SER C 73  ? 1.438 2.446 2.261 -0.107 -0.142 0.136  73  SER CCC N   
3715  C CA  . SER C 73  ? 1.430 2.560 2.351 -0.117 -0.115 0.153  73  SER CCC CA  
3716  C C   . SER C 73  ? 1.430 2.542 2.373 -0.181 -0.090 0.166  73  SER CCC C   
3717  O O   . SER C 73  ? 1.452 2.597 2.454 -0.237 -0.113 0.162  73  SER CCC O   
3718  C CB  . SER C 73  ? 1.435 2.689 2.449 -0.118 -0.154 0.145  73  SER CCC CB  
3719  O OG  . SER C 73  ? 1.422 2.808 2.543 -0.135 -0.128 0.161  73  SER CCC OG  
3720  N N   . GLY C 74  ? 1.413 2.462 2.300 -0.173 -0.046 0.181  74  GLY CCC N   
3721  C CA  . GLY C 74  ? 1.432 2.472 2.335 -0.220 -0.009 0.201  74  GLY CCC CA  
3722  C C   . GLY C 74  ? 1.449 2.378 2.298 -0.263 -0.024 0.198  74  GLY CCC C   
3723  O O   . GLY C 74  ? 1.430 2.275 2.203 -0.253 0.000  0.206  74  GLY CCC O   
3724  N N   . THR C 75  ? 1.485 2.417 2.371 -0.309 -0.061 0.186  75  THR CCC N   
3725  C CA  . THR C 75  ? 1.521 2.347 2.362 -0.354 -0.075 0.182  75  THR CCC CA  
3726  C C   . THR C 75  ? 1.531 2.295 2.325 -0.343 -0.126 0.153  75  THR CCC C   
3727  O O   . THR C 75  ? 1.540 2.205 2.280 -0.366 -0.137 0.147  75  THR CCC O   
3728  C CB  . THR C 75  ? 1.566 2.429 2.480 -0.425 -0.073 0.191  75  THR CCC CB  
3729  O OG1 . THR C 75  ? 1.566 2.515 2.555 -0.445 -0.114 0.172  75  THR CCC OG1 
3730  C CG2 . THR C 75  ? 1.580 2.510 2.542 -0.440 -0.019 0.222  75  THR CCC CG2 
3731  N N   . ASP C 76  ? 1.533 2.351 2.340 -0.305 -0.152 0.137  76  ASP CCC N   
3732  C CA  . ASP C 76  ? 1.542 2.318 2.310 -0.292 -0.200 0.110  76  ASP CCC CA  
3733  C C   . ASP C 76  ? 1.504 2.260 2.212 -0.226 -0.198 0.105  76  ASP CCC C   
3734  O O   . ASP C 76  ? 1.478 2.313 2.221 -0.192 -0.188 0.112  76  ASP CCC O   
3735  C CB  . ASP C 76  ? 1.569 2.438 2.414 -0.315 -0.242 0.095  76  ASP CCC CB  
3736  C CG  . ASP C 76  ? 1.655 2.522 2.546 -0.389 -0.253 0.092  76  ASP CCC CG  
3737  O OD1 . ASP C 76  ? 1.704 2.457 2.530 -0.412 -0.262 0.083  76  ASP CCC OD1 
3738  O OD2 . ASP C 76  ? 1.715 2.692 2.704 -0.423 -0.252 0.099  76  ASP CCC OD2 
3739  N N   . PHE C 77  ? 1.504 2.158 2.125 -0.211 -0.206 0.093  77  PHE CCC N   
3740  C CA  . PHE C 77  ? 1.492 2.106 2.044 -0.158 -0.201 0.088  77  PHE CCC CA  
3741  C C   . PHE C 77  ? 1.494 2.044 1.988 -0.151 -0.237 0.066  77  PHE CCC C   
3742  O O   . PHE C 77  ? 1.486 1.984 1.964 -0.183 -0.253 0.056  77  PHE CCC O   
3743  C CB  . PHE C 77  ? 1.503 2.060 2.003 -0.147 -0.162 0.101  77  PHE CCC CB  
3744  C CG  . PHE C 77  ? 1.524 2.133 2.069 -0.154 -0.124 0.122  77  PHE CCC CG  
3745  C CD1 . PHE C 77  ? 1.532 2.196 2.093 -0.119 -0.103 0.130  77  PHE CCC CD1 
3746  C CD2 . PHE C 77  ? 1.559 2.157 2.124 -0.196 -0.110 0.135  77  PHE CCC CD2 
3747  C CE1 . PHE C 77  ? 1.539 2.253 2.138 -0.123 -0.066 0.150  77  PHE CCC CE1 
3748  C CE2 . PHE C 77  ? 1.570 2.217 2.173 -0.203 -0.073 0.157  77  PHE CCC CE2 
3749  C CZ  . PHE C 77  ? 1.558 2.266 2.178 -0.166 -0.050 0.164  77  PHE CCC CZ  
3750  N N   . THR C 78  ? 1.490 2.036 1.945 -0.108 -0.246 0.059  78  THR CCC N   
3751  C CA  . THR C 78  ? 1.514 2.003 1.906 -0.094 -0.276 0.040  78  THR CCC CA  
3752  C C   . THR C 78  ? 1.528 1.961 1.844 -0.053 -0.255 0.042  78  THR CCC C   
3753  O O   . THR C 78  ? 1.522 1.979 1.840 -0.024 -0.233 0.054  78  THR CCC O   
3754  C CB  . THR C 78  ? 1.539 2.086 1.959 -0.084 -0.319 0.029  78  THR CCC CB  
3755  O OG1 . THR C 78  ? 1.553 2.177 2.062 -0.124 -0.332 0.030  78  THR CCC OG1 
3756  C CG2 . THR C 78  ? 1.580 2.065 1.935 -0.082 -0.353 0.007  78  THR CCC CG2 
3757  N N   . LEU C 79  ? 1.563 1.920 1.812 -0.053 -0.260 0.030  79  LEU CCC N   
3758  C CA  . LEU C 79  ? 1.566 1.864 1.737 -0.023 -0.244 0.028  79  LEU CCC CA  
3759  C C   . LEU C 79  ? 1.590 1.866 1.716 -0.004 -0.276 0.015  79  LEU CCC C   
3760  O O   . LEU C 79  ? 1.624 1.878 1.739 -0.023 -0.301 -0.001 79  LEU CCC O   
3761  C CB  . LEU C 79  ? 1.558 1.799 1.692 -0.037 -0.222 0.026  79  LEU CCC CB  
3762  C CG  . LEU C 79  ? 1.569 1.755 1.630 -0.017 -0.205 0.023  79  LEU CCC CG  
3763  C CD1 . LEU C 79  ? 1.574 1.762 1.616 0.010  -0.186 0.033  79  LEU CCC CD1 
3764  C CD2 . LEU C 79  ? 1.551 1.707 1.595 -0.032 -0.180 0.022  79  LEU CCC CD2 
3765  N N   . THR C 80  ? 1.585 1.859 1.676 0.033  -0.275 0.020  80  THR CCC N   
3766  C CA  . THR C 80  ? 1.639 1.890 1.676 0.059  -0.305 0.011  80  THR CCC CA  
3767  C C   . THR C 80  ? 1.671 1.842 1.617 0.081  -0.278 0.015  80  THR CCC C   
3768  O O   . THR C 80  ? 1.664 1.823 1.596 0.099  -0.248 0.028  80  THR CCC O   
3769  C CB  . THR C 80  ? 1.660 1.981 1.735 0.087  -0.331 0.017  80  THR CCC CB  
3770  O OG1 . THR C 80  ? 1.592 1.995 1.765 0.059  -0.337 0.020  80  THR CCC OG1 
3771  C CG2 . THR C 80  ? 1.726 2.044 1.762 0.104  -0.376 0.004  80  THR CCC CG2 
3772  N N   . ILE C 81  ? 1.711 1.831 1.598 0.079  -0.287 0.002  81  ILE CCC N   
3773  C CA  . ILE C 81  ? 1.745 1.789 1.541 0.095  -0.262 0.004  81  ILE CCC CA  
3774  C C   . ILE C 81  ? 1.813 1.832 1.544 0.128  -0.289 0.002  81  ILE CCC C   
3775  O O   . ILE C 81  ? 1.861 1.847 1.544 0.125  -0.303 -0.012 81  ILE CCC O   
3776  C CB  . ILE C 81  ? 1.724 1.733 1.501 0.069  -0.246 -0.008 81  ILE CCC CB  
3777  C CG1 . ILE C 81  ? 1.635 1.676 1.480 0.038  -0.234 -0.008 81  ILE CCC CG1 
3778  C CG2 . ILE C 81  ? 1.763 1.710 1.464 0.078  -0.210 -0.003 81  ILE CCC CG2 
3779  C CD1 . ILE C 81  ? 1.617 1.629 1.446 0.022  -0.221 -0.019 81  ILE CCC CD1 
3780  N N   . SER C 82  ? 1.842 1.875 1.564 0.163  -0.297 0.015  82  SER CCC N   
3781  C CA  . SER C 82  ? 1.953 1.954 1.598 0.203  -0.321 0.017  82  SER CCC CA  
3782  C C   . SER C 82  ? 2.016 1.922 1.559 0.205  -0.288 0.020  82  SER CCC C   
3783  O O   . SER C 82  ? 1.989 1.864 1.529 0.187  -0.244 0.026  82  SER CCC O   
3784  C CB  . SER C 82  ? 2.000 2.025 1.648 0.247  -0.329 0.035  82  SER CCC CB  
3785  O OG  . SER C 82  ? 2.049 2.006 1.641 0.264  -0.284 0.052  82  SER CCC OG  
3786  N N   . SER C 83  ? 2.101 1.967 1.567 0.224  -0.308 0.013  83  SER CCC N   
3787  C CA  . SER C 83  ? 2.163 1.940 1.523 0.229  -0.275 0.018  83  SER CCC CA  
3788  C C   . SER C 83  ? 2.087 1.852 1.466 0.188  -0.237 0.009  83  SER CCC C   
3789  O O   . SER C 83  ? 2.064 1.791 1.421 0.177  -0.192 0.021  83  SER CCC O   
3790  C CB  . SER C 83  ? 2.243 1.959 1.538 0.258  -0.245 0.042  83  SER CCC CB  
3791  O OG  . SER C 83  ? 2.344 2.071 1.616 0.305  -0.280 0.052  83  SER CCC OG  
3792  N N   . LEU C 84  ? 2.048 1.843 1.465 0.166  -0.257 -0.012 84  LEU CCC N   
3793  C CA  . LEU C 84  ? 1.997 1.789 1.437 0.134  -0.225 -0.021 84  LEU CCC CA  
3794  C C   . LEU C 84  ? 2.076 1.806 1.431 0.138  -0.183 -0.015 84  LEU CCC C   
3795  O O   . LEU C 84  ? 2.201 1.884 1.469 0.165  -0.190 -0.012 84  LEU CCC O   
3796  C CB  . LEU C 84  ? 1.972 1.782 1.437 0.121  -0.255 -0.045 84  LEU CCC CB  
3797  C CG  . LEU C 84  ? 1.905 1.719 1.401 0.096  -0.227 -0.053 84  LEU CCC CG  
3798  C CD1 . LEU C 84  ? 1.815 1.676 1.397 0.074  -0.213 -0.043 84  LEU CCC CD1 
3799  C CD2 . LEU C 84  ? 1.925 1.732 1.420 0.092  -0.255 -0.077 84  LEU CCC CD2 
3800  N N   . GLN C 85  ? 2.048 1.782 1.425 0.113  -0.141 -0.013 85  GLN CCC N   
3801  C CA  . GLN C 85  ? 2.127 1.815 1.438 0.108  -0.094 -0.006 85  GLN CCC CA  
3802  C C   . GLN C 85  ? 2.085 1.800 1.424 0.088  -0.073 -0.021 85  GLN CCC C   
3803  O O   . GLN C 85  ? 1.999 1.760 1.408 0.079  -0.093 -0.032 85  GLN CCC O   
3804  C CB  . GLN C 85  ? 2.153 1.821 1.459 0.095  -0.059 0.012  85  GLN CCC CB  
3805  C CG  . GLN C 85  ? 2.236 1.858 1.490 0.124  -0.071 0.029  85  GLN CCC CG  
3806  C CD  . GLN C 85  ? 2.374 1.922 1.514 0.152  -0.065 0.039  85  GLN CCC CD  
3807  O OE1 . GLN C 85  ? 2.465 1.953 1.543 0.167  -0.049 0.058  85  GLN CCC OE1 
3808  N NE2 . GLN C 85  ? 2.401 1.947 1.506 0.161  -0.077 0.026  85  GLN CCC NE2 
3809  N N   . ALA C 86  ? 2.144 1.832 1.428 0.085  -0.033 -0.018 86  ALA CCC N   
3810  C CA  . ALA C 86  ? 2.145 1.865 1.453 0.070  -0.001 -0.028 86  ALA CCC CA  
3811  C C   . ALA C 86  ? 2.086 1.872 1.495 0.047  -0.004 -0.032 86  ALA CCC C   
3812  O O   . ALA C 86  ? 2.048 1.861 1.497 0.053  -0.027 -0.046 86  ALA CCC O   
3813  C CB  . ALA C 86  ? 2.198 1.894 1.455 0.056  0.052  -0.016 86  ALA CCC CB  
3814  N N   . GLU C 87  ? 2.096 1.896 1.534 0.022  0.018  -0.020 87  GLU CCC N   
3815  C CA  . GLU C 87  ? 2.005 1.867 1.524 -0.003 0.027  -0.023 87  GLU CCC CA  
3816  C C   . GLU C 87  ? 1.863 1.750 1.442 0.000  -0.011 -0.024 87  GLU CCC C   
3817  O O   . GLU C 87  ? 1.775 1.707 1.413 -0.018 -0.006 -0.024 87  GLU CCC O   
3818  C CB  . GLU C 87  ? 2.086 1.946 1.602 -0.035 0.063  -0.013 87  GLU CCC CB  
3819  C CG  . GLU C 87  ? 2.168 1.967 1.641 -0.033 0.062  0.001  87  GLU CCC CG  
3820  C CD  . GLU C 87  ? 2.209 1.995 1.679 -0.068 0.094  0.008  87  GLU CCC CD  
3821  O OE1 . GLU C 87  ? 2.162 2.005 1.692 -0.096 0.103  0.000  87  GLU CCC OE1 
3822  O OE2 . GLU C 87  ? 2.297 2.009 1.699 -0.067 0.110  0.020  87  GLU CCC OE2 
3823  N N   . ASP C 88  ? 1.828 1.691 1.392 0.021  -0.046 -0.026 88  ASP CCC N   
3824  C CA  . ASP C 88  ? 1.769 1.659 1.393 0.021  -0.081 -0.026 88  ASP CCC CA  
3825  C C   . ASP C 88  ? 1.743 1.652 1.398 0.023  -0.100 -0.040 88  ASP CCC C   
3826  O O   . ASP C 88  ? 1.688 1.621 1.397 0.016  -0.122 -0.040 88  ASP CCC O   
3827  C CB  . ASP C 88  ? 1.797 1.665 1.398 0.039  -0.112 -0.023 88  ASP CCC CB  
3828  C CG  . ASP C 88  ? 1.829 1.675 1.404 0.044  -0.099 -0.007 88  ASP CCC CG  
3829  O OD1 . ASP C 88  ? 1.802 1.661 1.406 0.027  -0.077 0.001  88  ASP CCC OD1 
3830  O OD2 . ASP C 88  ? 1.915 1.724 1.435 0.068  -0.111 -0.002 88  ASP CCC OD2 
3831  N N   . VAL C 89  ? 1.784 1.679 1.403 0.034  -0.089 -0.052 89  VAL CCC N   
3832  C CA  . VAL C 89  ? 1.797 1.697 1.435 0.042  -0.101 -0.066 89  VAL CCC CA  
3833  C C   . VAL C 89  ? 1.745 1.693 1.448 0.028  -0.089 -0.060 89  VAL CCC C   
3834  O O   . VAL C 89  ? 1.719 1.699 1.433 0.019  -0.057 -0.054 89  VAL CCC O   
3835  C CB  . VAL C 89  ? 1.859 1.736 1.441 0.061  -0.083 -0.079 89  VAL CCC CB  
3836  C CG1 . VAL C 89  ? 1.877 1.754 1.474 0.075  -0.090 -0.093 89  VAL CCC CG1 
3837  C CG2 . VAL C 89  ? 1.926 1.751 1.431 0.078  -0.097 -0.085 89  VAL CCC CG2 
3838  N N   . ALA C 90  ? 1.715 1.668 1.459 0.025  -0.113 -0.061 90  ALA CCC N   
3839  C CA  . ALA C 90  ? 1.659 1.649 1.458 0.016  -0.107 -0.053 90  ALA CCC CA  
3840  C C   . ALA C 90  ? 1.651 1.626 1.479 0.011  -0.136 -0.052 90  ALA CCC C   
3841  O O   . ALA C 90  ? 1.634 1.578 1.447 0.009  -0.162 -0.059 90  ALA CCC O   
3842  C CB  . ALA C 90  ? 1.622 1.650 1.448 -0.002 -0.089 -0.040 90  ALA CCC CB  
3843  N N   . VAL C 91  ? 1.631 1.629 1.498 0.006  -0.133 -0.043 91  VAL CCC N   
3844  C CA  . VAL C 91  ? 1.608 1.596 1.508 -0.006 -0.152 -0.035 91  VAL CCC CA  
3845  C C   . VAL C 91  ? 1.551 1.574 1.487 -0.026 -0.150 -0.020 91  VAL CCC C   
3846  O O   . VAL C 91  ? 1.514 1.570 1.455 -0.029 -0.129 -0.014 91  VAL CCC O   
3847  C CB  . VAL C 91  ? 1.636 1.625 1.549 0.004  -0.145 -0.029 91  VAL CCC CB  
3848  C CG1 . VAL C 91  ? 1.664 1.614 1.589 -0.007 -0.165 -0.024 91  VAL CCC CG1 
3849  C CG2 . VAL C 91  ? 1.689 1.669 1.571 0.034  -0.134 -0.042 91  VAL CCC CG2 
3850  N N   . TYR C 92  ? 1.539 1.556 1.498 -0.041 -0.169 -0.016 92  TYR CCC N   
3851  C CA  . TYR C 92  ? 1.491 1.544 1.486 -0.055 -0.166 -0.002 92  TYR CCC CA  
3852  C C   . TYR C 92  ? 1.498 1.556 1.532 -0.072 -0.170 0.011  92  TYR CCC C   
3853  O O   . TYR C 92  ? 1.555 1.584 1.594 -0.082 -0.189 0.006  92  TYR CCC O   
3854  C CB  . TYR C 92  ? 1.500 1.555 1.491 -0.055 -0.183 -0.007 92  TYR CCC CB  
3855  C CG  . TYR C 92  ? 1.516 1.560 1.461 -0.038 -0.173 -0.013 92  TYR CCC CG  
3856  C CD1 . TYR C 92  ? 1.586 1.597 1.484 -0.026 -0.178 -0.027 92  TYR CCC CD1 
3857  C CD2 . TYR C 92  ? 1.500 1.562 1.444 -0.035 -0.156 -0.003 92  TYR CCC CD2 
3858  C CE1 . TYR C 92  ? 1.626 1.622 1.477 -0.013 -0.164 -0.030 92  TYR CCC CE1 
3859  C CE2 . TYR C 92  ? 1.547 1.587 1.442 -0.023 -0.143 -0.007 92  TYR CCC CE2 
3860  C CZ  . TYR C 92  ? 1.602 1.611 1.451 -0.013 -0.146 -0.019 92  TYR CCC CZ  
3861  O OH  . TYR C 92  ? 1.633 1.617 1.429 -0.003 -0.129 -0.019 92  TYR CCC OH  
3862  N N   . TYR C 93  ? 1.484 1.571 1.537 -0.076 -0.152 0.026  93  TYR CCC N   
3863  C CA  . TYR C 93  ? 1.489 1.584 1.573 -0.091 -0.148 0.044  93  TYR CCC CA  
3864  C C   . TYR C 93  ? 1.459 1.596 1.575 -0.100 -0.139 0.055  93  TYR CCC C   
3865  O O   . TYR C 93  ? 1.433 1.589 1.537 -0.089 -0.127 0.053  93  TYR CCC O   
3866  C CB  . TYR C 93  ? 1.482 1.574 1.553 -0.081 -0.134 0.053  93  TYR CCC CB  
3867  C CG  . TYR C 93  ? 1.502 1.564 1.543 -0.062 -0.139 0.042  93  TYR CCC CG  
3868  C CD1 . TYR C 93  ? 1.511 1.590 1.533 -0.046 -0.131 0.030  93  TYR CCC CD1 
3869  C CD2 . TYR C 93  ? 1.548 1.562 1.578 -0.059 -0.148 0.045  93  TYR CCC CD2 
3870  C CE1 . TYR C 93  ? 1.555 1.619 1.554 -0.025 -0.131 0.020  93  TYR CCC CE1 
3871  C CE2 . TYR C 93  ? 1.609 1.596 1.609 -0.033 -0.150 0.035  93  TYR CCC CE2 
3872  C CZ  . TYR C 93  ? 1.603 1.620 1.590 -0.014 -0.141 0.022  93  TYR CCC CZ  
3873  O OH  . TYR C 93  ? 1.626 1.627 1.588 0.015  -0.140 0.012  93  TYR CCC OH  
3874  N N   . CYS C 94  ? 1.472 1.621 1.625 -0.119 -0.143 0.066  94  CYS CCC N   
3875  C CA  . CYS C 94  ? 1.476 1.671 1.663 -0.125 -0.126 0.082  94  CYS CCC CA  
3876  C C   . CYS C 94  ? 1.506 1.696 1.692 -0.132 -0.107 0.100  94  CYS CCC C   
3877  O O   . CYS C 94  ? 1.550 1.701 1.726 -0.141 -0.113 0.105  94  CYS CCC O   
3878  C CB  . CYS C 94  ? 1.498 1.727 1.735 -0.143 -0.140 0.083  94  CYS CCC CB  
3879  S SG  . CYS C 94  ? 1.587 1.787 1.848 -0.179 -0.152 0.089  94  CYS CCC SG  
3880  N N   . GLN C 95  ? 1.496 1.716 1.682 -0.126 -0.085 0.111  95  GLN CCC N   
3881  C CA  . GLN C 95  ? 1.506 1.725 1.680 -0.129 -0.065 0.129  95  GLN CCC CA  
3882  C C   . GLN C 95  ? 1.499 1.760 1.703 -0.134 -0.043 0.144  95  GLN CCC C   
3883  O O   . GLN C 95  ? 1.505 1.793 1.713 -0.121 -0.038 0.136  95  GLN CCC O   
3884  C CB  . GLN C 95  ? 1.516 1.729 1.646 -0.111 -0.058 0.123  95  GLN CCC CB  
3885  C CG  . GLN C 95  ? 1.568 1.780 1.676 -0.109 -0.042 0.140  95  GLN CCC CG  
3886  C CD  . GLN C 95  ? 1.585 1.815 1.663 -0.098 -0.028 0.134  95  GLN CCC CD  
3887  O OE1 . GLN C 95  ? 1.621 1.849 1.667 -0.091 -0.032 0.127  95  GLN CCC OE1 
3888  N NE2 . GLN C 95  ? 1.571 1.822 1.659 -0.098 -0.012 0.134  95  GLN CCC NE2 
3889  N N   . GLN C 96  ? 1.517 1.781 1.736 -0.151 -0.029 0.165  96  GLN CCC N   
3890  C CA  . GLN C 96  ? 1.508 1.815 1.748 -0.153 0.000  0.181  96  GLN CCC CA  
3891  C C   . GLN C 96  ? 1.530 1.824 1.716 -0.136 0.019  0.188  96  GLN CCC C   
3892  O O   . GLN C 96  ? 1.563 1.818 1.709 -0.133 0.012  0.191  96  GLN CCC O   
3893  C CB  . GLN C 96  ? 1.525 1.843 1.807 -0.184 0.010  0.202  96  GLN CCC CB  
3894  C CG  . GLN C 96  ? 1.556 1.822 1.800 -0.194 0.019  0.222  96  GLN CCC CG  
3895  C CD  . GLN C 96  ? 1.568 1.841 1.776 -0.181 0.051  0.241  96  GLN CCC CD  
3896  O OE1 . GLN C 96  ? 1.537 1.859 1.760 -0.173 0.073  0.243  96  GLN CCC OE1 
3897  N NE2 . GLN C 96  ? 1.632 1.855 1.786 -0.175 0.052  0.254  96  GLN CCC NE2 
3898  N N   . TYR C 97  ? 1.537 1.862 1.718 -0.122 0.042  0.188  97  TYR CCC N   
3899  C CA  . TYR C 97  ? 1.564 1.877 1.689 -0.109 0.063  0.193  97  TYR CCC CA  
3900  C C   . TYR C 97  ? 1.587 1.938 1.727 -0.105 0.097  0.209  97  TYR CCC C   
3901  O O   . TYR C 97  ? 1.625 1.975 1.723 -0.085 0.115  0.202  97  TYR CCC O   
3902  C CB  . TYR C 97  ? 1.536 1.831 1.616 -0.092 0.052  0.169  97  TYR CCC CB  
3903  C CG  . TYR C 97  ? 1.515 1.823 1.606 -0.079 0.055  0.153  97  TYR CCC CG  
3904  C CD1 . TYR C 97  ? 1.480 1.790 1.602 -0.080 0.034  0.141  97  TYR CCC CD1 
3905  C CD2 . TYR C 97  ? 1.543 1.855 1.606 -0.062 0.079  0.149  97  TYR CCC CD2 
3906  C CE1 . TYR C 97  ? 1.467 1.782 1.590 -0.062 0.036  0.130  97  TYR CCC CE1 
3907  C CE2 . TYR C 97  ? 1.541 1.853 1.604 -0.044 0.083  0.136  97  TYR CCC CE2 
3908  C CZ  . TYR C 97  ? 1.488 1.802 1.582 -0.043 0.061  0.128  97  TYR CCC CZ  
3909  O OH  . TYR C 97  ? 1.443 1.751 1.528 -0.020 0.066  0.118  97  TYR CCC OH  
3910  N N   . TYR C 98  ? 1.573 1.957 1.770 -0.124 0.108  0.227  98  TYR CCC N   
3911  C CA  . TYR C 98  ? 1.594 2.022 1.812 -0.125 0.147  0.247  98  TYR CCC CA  
3912  C C   . TYR C 98  ? 1.648 2.042 1.803 -0.124 0.169  0.266  98  TYR CCC C   
3913  O O   . TYR C 98  ? 1.706 2.117 1.833 -0.107 0.201  0.273  98  TYR CCC O   
3914  C CB  . TYR C 98  ? 1.580 2.059 1.883 -0.154 0.152  0.262  98  TYR CCC CB  
3915  C CG  . TYR C 98  ? 1.600 2.137 1.933 -0.156 0.196  0.284  98  TYR CCC CG  
3916  C CD1 . TYR C 98  ? 1.566 2.169 1.934 -0.130 0.213  0.277  98  TYR CCC CD1 
3917  C CD2 . TYR C 98  ? 1.658 2.183 1.979 -0.180 0.224  0.313  98  TYR CCC CD2 
3918  C CE1 . TYR C 98  ? 1.584 2.249 1.981 -0.127 0.258  0.297  98  TYR CCC CE1 
3919  C CE2 . TYR C 98  ? 1.687 2.269 2.034 -0.182 0.270  0.334  98  TYR CCC CE2 
3920  C CZ  . TYR C 98  ? 1.653 2.310 2.041 -0.154 0.288  0.325  98  TYR CCC CZ  
3921  O OH  . TYR C 98  ? 1.703 2.424 2.120 -0.152 0.337  0.346  98  TYR CCC OH  
3922  N N   . SER C 99  ? 1.649 1.993 1.777 -0.138 0.151  0.275  99  SER CCC N   
3923  C CA  . SER C 99  ? 1.720 2.025 1.781 -0.135 0.166  0.296  99  SER CCC CA  
3924  C C   . SER C 99  ? 1.708 1.957 1.736 -0.135 0.134  0.295  99  SER CCC C   
3925  O O   . SER C 99  ? 1.657 1.894 1.723 -0.148 0.109  0.286  99  SER CCC O   
3926  C CB  . SER C 99  ? 1.795 2.113 1.877 -0.157 0.203  0.330  99  SER CCC CB  
3927  O OG  . SER C 99  ? 1.817 2.110 1.936 -0.189 0.191  0.343  99  SER CCC OG  
3928  N N   . THR C 100 ? 1.756 1.971 1.710 -0.119 0.135  0.305  100 THR CCC N   
3929  C CA  . THR C 100 ? 1.778 1.942 1.694 -0.111 0.110  0.312  100 THR CCC CA  
3930  C C   . THR C 100 ? 1.848 1.971 1.776 -0.134 0.121  0.343  100 THR CCC C   
3931  O O   . THR C 100 ? 1.879 2.010 1.817 -0.153 0.156  0.366  100 THR CCC O   
3932  C CB  . THR C 100 ? 1.795 1.946 1.630 -0.084 0.106  0.315  100 THR CCC CB  
3933  O OG1 . THR C 100 ? 1.838 1.979 1.633 -0.085 0.141  0.344  100 THR CCC OG1 
3934  C CG2 . THR C 100 ? 1.743 1.928 1.565 -0.070 0.094  0.281  100 THR CCC CG2 
3935  N N   . PRO C 101 ? 1.893 1.967 1.820 -0.136 0.096  0.342  101 PRO CCC N   
3936  C CA  . PRO C 101 ? 1.868 1.940 1.789 -0.114 0.060  0.315  101 PRO CCC CA  
3937  C C   . PRO C 101 ? 1.806 1.915 1.793 -0.127 0.046  0.286  101 PRO CCC C   
3938  O O   . PRO C 101 ? 1.810 1.911 1.841 -0.154 0.048  0.289  101 PRO CCC O   
3939  C CB  . PRO C 101 ? 1.924 1.924 1.815 -0.107 0.045  0.330  101 PRO CCC CB  
3940  C CG  . PRO C 101 ? 1.974 1.939 1.889 -0.144 0.068  0.355  101 PRO CCC CG  
3941  C CD  . PRO C 101 ? 1.965 1.978 1.893 -0.160 0.104  0.369  101 PRO CCC CD  
3942  N N   . TYR C 102 ? 1.770 1.916 1.757 -0.111 0.033  0.258  102 TYR CCC N   
3943  C CA  . TYR C 102 ? 1.724 1.891 1.756 -0.116 0.015  0.230  102 TYR CCC CA  
3944  C C   . TYR C 102 ? 1.743 1.866 1.788 -0.123 -0.006 0.229  102 TYR CCC C   
3945  O O   . TYR C 102 ? 1.793 1.874 1.799 -0.109 -0.013 0.240  102 TYR CCC O   
3946  C CB  . TYR C 102 ? 1.698 1.887 1.709 -0.097 0.001  0.204  102 TYR CCC CB  
3947  C CG  . TYR C 102 ? 1.705 1.924 1.695 -0.091 0.018  0.197  102 TYR CCC CG  
3948  C CD1 . TYR C 102 ? 1.715 1.943 1.693 -0.094 0.045  0.214  102 TYR CCC CD1 
3949  C CD2 . TYR C 102 ? 1.720 1.952 1.693 -0.083 0.006  0.171  102 TYR CCC CD2 
3950  C CE1 . TYR C 102 ? 1.726 1.971 1.674 -0.084 0.060  0.204  102 TYR CCC CE1 
3951  C CE2 . TYR C 102 ? 1.732 1.977 1.675 -0.079 0.020  0.161  102 TYR CCC CE2 
3952  C CZ  . TYR C 102 ? 1.736 1.985 1.663 -0.078 0.046  0.176  102 TYR CCC CZ  
3953  O OH  . TYR C 102 ? 1.760 2.011 1.648 -0.071 0.059  0.162  102 TYR CCC OH  
3954  N N   . THR C 103 ? 1.711 1.840 1.802 -0.142 -0.015 0.217  103 THR CCC N   
3955  C CA  . THR C 103 ? 1.709 1.789 1.806 -0.150 -0.036 0.211  103 THR CCC CA  
3956  C C   . THR C 103 ? 1.643 1.743 1.768 -0.150 -0.056 0.182  103 THR CCC C   
3957  O O   . THR C 103 ? 1.596 1.745 1.755 -0.157 -0.051 0.175  103 THR CCC O   
3958  C CB  . THR C 103 ? 1.759 1.807 1.877 -0.184 -0.026 0.231  103 THR CCC CB  
3959  O OG1 . THR C 103 ? 1.700 1.808 1.874 -0.208 -0.012 0.233  103 THR CCC OG1 
3960  C CG2 . THR C 103 ? 1.834 1.838 1.907 -0.181 -0.007 0.263  103 THR CCC CG2 
3961  N N   . PHE C 104 ? 1.649 1.712 1.754 -0.137 -0.076 0.167  104 PHE CCC N   
3962  C CA  . PHE C 104 ? 1.632 1.702 1.750 -0.134 -0.095 0.140  104 PHE CCC CA  
3963  C C   . PHE C 104 ? 1.679 1.705 1.810 -0.156 -0.112 0.135  104 PHE CCC C   
3964  O O   . PHE C 104 ? 1.738 1.714 1.857 -0.169 -0.108 0.151  104 PHE CCC O   
3965  C CB  . PHE C 104 ? 1.650 1.710 1.733 -0.104 -0.104 0.125  104 PHE CCC CB  
3966  C CG  . PHE C 104 ? 1.636 1.741 1.707 -0.087 -0.094 0.123  104 PHE CCC CG  
3967  C CD1 . PHE C 104 ? 1.596 1.736 1.674 -0.087 -0.092 0.107  104 PHE CCC CD1 
3968  C CD2 . PHE C 104 ? 1.683 1.789 1.727 -0.073 -0.087 0.137  104 PHE CCC CD2 
3969  C CE1 . PHE C 104 ? 1.584 1.755 1.646 -0.079 -0.083 0.102  104 PHE CCC CE1 
3970  C CE2 . PHE C 104 ? 1.645 1.795 1.677 -0.063 -0.081 0.131  104 PHE CCC CE2 
3971  C CZ  . PHE C 104 ? 1.593 1.773 1.634 -0.069 -0.078 0.112  104 PHE CCC CZ  
3972  N N   . GLY C 105 ? 1.654 1.693 1.801 -0.160 -0.129 0.113  105 GLY CCC N   
3973  C CA  . GLY C 105 ? 1.680 1.673 1.827 -0.177 -0.152 0.098  105 GLY CCC CA  
3974  C C   . GLY C 105 ? 1.706 1.641 1.801 -0.150 -0.163 0.084  105 GLY CCC C   
3975  O O   . GLY C 105 ? 1.682 1.631 1.754 -0.119 -0.152 0.085  105 GLY CCC O   
3976  N N   . GLN C 106 ? 1.757 1.631 1.834 -0.160 -0.182 0.069  106 GLN CCC N   
3977  C CA  . GLN C 106 ? 1.824 1.628 1.846 -0.131 -0.189 0.055  106 GLN CCC CA  
3978  C C   . GLN C 106 ? 1.773 1.602 1.777 -0.103 -0.195 0.032  106 GLN CCC C   
3979  O O   . GLN C 106 ? 1.793 1.581 1.754 -0.073 -0.196 0.021  106 GLN CCC O   
3980  C CB  . GLN C 106 ? 1.961 1.678 1.961 -0.156 -0.206 0.046  106 GLN CCC CB  
3981  C CG  . GLN C 106 ? 1.999 1.720 2.012 -0.180 -0.232 0.019  106 GLN CCC CG  
3982  C CD  . GLN C 106 ? 1.980 1.766 2.058 -0.223 -0.238 0.026  106 GLN CCC CD  
3983  O OE1 . GLN C 106 ? 2.002 1.811 2.115 -0.245 -0.221 0.051  106 GLN CCC OE1 
3984  N NE2 . GLN C 106 ? 1.954 1.772 2.047 -0.233 -0.263 0.005  106 GLN CCC NE2 
3985  N N   . GLY C 107 ? 1.707 1.599 1.740 -0.111 -0.197 0.027  107 GLY CCC N   
3986  C CA  . GLY C 107 ? 1.672 1.587 1.684 -0.088 -0.198 0.009  107 GLY CCC CA  
3987  C C   . GLY C 107 ? 1.703 1.593 1.699 -0.095 -0.223 -0.013 107 GLY CCC C   
3988  O O   . GLY C 107 ? 1.754 1.595 1.747 -0.116 -0.241 -0.020 107 GLY CCC O   
3989  N N   . THR C 108 ? 1.690 1.607 1.672 -0.081 -0.225 -0.024 108 THR CCC N   
3990  C CA  . THR C 108 ? 1.735 1.630 1.687 -0.080 -0.249 -0.046 108 THR CCC CA  
3991  C C   . THR C 108 ? 1.764 1.650 1.665 -0.048 -0.237 -0.058 108 THR CCC C   
3992  O O   . THR C 108 ? 1.738 1.667 1.645 -0.039 -0.218 -0.049 108 THR CCC O   
3993  C CB  . THR C 108 ? 1.694 1.640 1.684 -0.097 -0.264 -0.043 108 THR CCC CB  
3994  O OG1 . THR C 108 ? 1.647 1.614 1.692 -0.128 -0.269 -0.030 108 THR CCC OG1 
3995  C CG2 . THR C 108 ? 1.759 1.688 1.718 -0.095 -0.295 -0.065 108 THR CCC CG2 
3996  N N   . LYS C 109 ? 1.830 1.660 1.679 -0.032 -0.244 -0.077 109 LYS CCC N   
3997  C CA  . LYS C 109 ? 1.848 1.670 1.645 -0.002 -0.229 -0.089 109 LYS CCC CA  
3998  C C   . LYS C 109 ? 1.851 1.678 1.625 -0.005 -0.248 -0.098 109 LYS CCC C   
3999  O O   . LYS C 109 ? 1.893 1.699 1.667 -0.022 -0.281 -0.109 109 LYS CCC O   
4000  C CB  . LYS C 109 ? 1.929 1.689 1.675 0.022  -0.227 -0.107 109 LYS CCC CB  
4001  C CG  . LYS C 109 ? 1.977 1.740 1.677 0.055  -0.203 -0.116 109 LYS CCC CG  
4002  C CD  . LYS C 109 ? 1.979 1.802 1.709 0.067  -0.168 -0.100 109 LYS CCC CD  
4003  C CE  . LYS C 109 ? 2.011 1.861 1.712 0.084  -0.141 -0.104 109 LYS CCC CE  
4004  N NZ  . LYS C 109 ? 1.929 1.851 1.672 0.078  -0.113 -0.088 109 LYS CCC NZ  
4005  N N   . VAL C 110 ? 1.798 1.652 1.555 0.009  -0.228 -0.092 110 VAL CCC N   
4006  C CA  . VAL C 110 ? 1.815 1.664 1.531 0.017  -0.241 -0.098 110 VAL CCC CA  
4007  C C   . VAL C 110 ? 1.846 1.668 1.494 0.042  -0.217 -0.106 110 VAL CCC C   
4008  O O   . VAL C 110 ? 1.801 1.649 1.457 0.047  -0.182 -0.095 110 VAL CCC O   
4009  C CB  . VAL C 110 ? 1.766 1.661 1.515 0.010  -0.235 -0.079 110 VAL CCC CB  
4010  C CG1 . VAL C 110 ? 1.796 1.678 1.491 0.027  -0.242 -0.080 110 VAL CCC CG1 
4011  C CG2 . VAL C 110 ? 1.752 1.681 1.567 -0.012 -0.258 -0.071 110 VAL CCC CG2 
4012  N N   . GLU C 111 ? 1.938 1.712 1.522 0.056  -0.237 -0.126 111 GLU CCC N   
4013  C CA  . GLU C 111 ? 2.003 1.744 1.511 0.083  -0.214 -0.137 111 GLU CCC CA  
4014  C C   . GLU C 111 ? 2.032 1.749 1.475 0.093  -0.233 -0.142 111 GLU CCC C   
4015  O O   . GLU C 111 ? 1.992 1.712 1.449 0.082  -0.274 -0.146 111 GLU CCC O   
4016  C CB  . GLU C 111 ? 2.084 1.781 1.564 0.097  -0.215 -0.157 111 GLU CCC CB  
4017  C CG  . GLU C 111 ? 2.074 1.797 1.609 0.097  -0.192 -0.148 111 GLU CCC CG  
4018  C CD  . GLU C 111 ? 2.160 1.848 1.658 0.126  -0.174 -0.164 111 GLU CCC CD  
4019  O OE1 . GLU C 111 ? 2.237 1.859 1.698 0.133  -0.199 -0.184 111 GLU CCC OE1 
4020  O OE2 . GLU C 111 ? 2.146 1.875 1.656 0.144  -0.136 -0.156 111 GLU CCC OE2 
4021  N N   . ILE C 112 ? 2.071 1.769 1.448 0.114  -0.203 -0.140 112 ILE CCC N   
4022  C CA  . ILE C 112 ? 2.152 1.820 1.450 0.131  -0.212 -0.139 112 ILE CCC CA  
4023  C C   . ILE C 112 ? 2.257 1.869 1.477 0.148  -0.240 -0.167 112 ILE CCC C   
4024  O O   . ILE C 112 ? 2.309 1.890 1.480 0.166  -0.214 -0.179 112 ILE CCC O   
4025  C CB  . ILE C 112 ? 2.177 1.843 1.433 0.141  -0.160 -0.123 112 ILE CCC CB  
4026  C CG1 . ILE C 112 ? 2.120 1.831 1.439 0.120  -0.136 -0.098 112 ILE CCC CG1 
4027  C CG2 . ILE C 112 ? 2.272 1.889 1.424 0.164  -0.164 -0.123 112 ILE CCC CG2 
4028  C CD1 . ILE C 112 ? 2.132 1.841 1.450 0.120  -0.159 -0.083 112 ILE CCC CD1 
4029  N N   . LYS C 113 ? 2.321 1.922 1.527 0.145  -0.292 -0.177 113 LYS CCC N   
4030  C CA  . LYS C 113 ? 2.440 1.983 1.558 0.161  -0.326 -0.206 113 LYS CCC CA  
4031  C C   . LYS C 113 ? 2.497 2.004 1.509 0.193  -0.303 -0.201 113 LYS CCC C   
4032  O O   . LYS C 113 ? 2.460 1.985 1.464 0.199  -0.300 -0.178 113 LYS CCC O   
4033  C CB  . LYS C 113 ? 2.473 2.031 1.615 0.144  -0.391 -0.219 113 LYS CCC CB  
4034  C CG  . LYS C 113 ? 2.594 2.092 1.657 0.149  -0.433 -0.256 113 LYS CCC CG  
4035  C CD  . LYS C 113 ? 2.598 2.100 1.720 0.113  -0.480 -0.278 113 LYS CCC CD  
4036  C CE  . LYS C 113 ? 2.564 2.140 1.762 0.090  -0.522 -0.267 113 LYS CCC CE  
4037  N NZ  . LYS C 113 ? 2.607 2.183 1.847 0.050  -0.572 -0.293 113 LYS CCC NZ  
4038  N N   . ARG C 114 ? 2.407 1.976 1.625 0.183  -0.320 -0.323 114 ARG CCC N   
4039  C CA  . ARG C 114 ? 2.482 1.962 1.624 0.185  -0.331 -0.319 114 ARG CCC CA  
4040  C C   . ARG C 114 ? 2.490 1.969 1.632 0.180  -0.346 -0.320 114 ARG CCC C   
4041  O O   . ARG C 114 ? 2.440 1.989 1.650 0.167  -0.347 -0.326 114 ARG CCC O   
4042  C CB  . ARG C 114 ? 2.489 1.916 1.604 0.155  -0.309 -0.305 114 ARG CCC CB  
4043  C CG  . ARG C 114 ? 2.443 1.908 1.604 0.117  -0.288 -0.296 114 ARG CCC CG  
4044  C CD  . ARG C 114 ? 2.476 1.877 1.607 0.090  -0.272 -0.284 114 ARG CCC CD  
4045  N NE  . ARG C 114 ? 2.531 1.879 1.613 0.095  -0.275 -0.278 114 ARG CCC NE  
4046  C CZ  . ARG C 114 ? 2.574 1.851 1.616 0.082  -0.256 -0.265 114 ARG CCC CZ  
4047  N NH1 . ARG C 114 ? 2.564 1.819 1.622 0.058  -0.236 -0.258 114 ARG CCC NH1 
4048  N NH2 . ARG C 114 ? 2.640 1.866 1.624 0.094  -0.256 -0.258 114 ARG CCC NH2 
4049  N N   . THR C 115 ? 2.551 1.946 1.614 0.191  -0.353 -0.315 115 THR CCC N   
4050  C CA  . THR C 115 ? 2.591 1.959 1.622 0.194  -0.367 -0.317 115 THR CCC CA  
4051  C C   . THR C 115 ? 2.485 1.893 1.567 0.153  -0.347 -0.310 115 THR CCC C   
4052  O O   . THR C 115 ? 2.409 1.816 1.507 0.123  -0.317 -0.297 115 THR CCC O   
4053  C CB  . THR C 115 ? 2.712 1.967 1.635 0.209  -0.361 -0.303 115 THR CCC CB  
4054  O OG1 . THR C 115 ? 2.724 1.945 1.641 0.172  -0.321 -0.283 115 THR CCC OG1 
4055  C CG2 . THR C 115 ? 2.780 1.985 1.652 0.243  -0.372 -0.304 115 THR CCC CG2 
4056  N N   . VAL C 116 ? 2.470 1.910 1.579 0.154  -0.368 -0.323 116 VAL CCC N   
4057  C CA  . VAL C 116 ? 2.421 1.885 1.568 0.120  -0.354 -0.319 116 VAL CCC CA  
4058  C C   . VAL C 116 ? 2.456 1.845 1.536 0.103  -0.322 -0.298 116 VAL CCC C   
4059  O O   . VAL C 116 ? 2.558 1.868 1.555 0.124  -0.320 -0.291 116 VAL CCC O   
4060  C CB  . VAL C 116 ? 2.425 1.905 1.585 0.131  -0.390 -0.339 116 VAL CCC CB  
4061  C CG1 . VAL C 116 ? 2.345 1.863 1.564 0.094  -0.376 -0.337 116 VAL CCC CG1 
4062  C CG2 . VAL C 116 ? 2.424 1.964 1.643 0.157  -0.429 -0.363 116 VAL CCC CG2 
4063  N N   . ALA C 117 ? 2.393 1.803 1.511 0.068  -0.296 -0.289 117 ALA CCC N   
4064  C CA  . ALA C 117 ? 2.412 1.764 1.489 0.050  -0.262 -0.270 117 ALA CCC CA  
4065  C C   . ALA C 117 ? 2.344 1.730 1.467 0.019  -0.246 -0.267 117 ALA CCC C   
4066  O O   . ALA C 117 ? 2.253 1.702 1.446 0.000  -0.241 -0.267 117 ALA CCC O   
4067  C CB  . ALA C 117 ? 2.416 1.751 1.496 0.040  -0.241 -0.259 117 ALA CCC CB  
4068  N N   . ALA C 118 ? 2.388 1.727 1.465 0.020  -0.236 -0.262 118 ALA CCC N   
4069  C CA  . ALA C 118 ? 2.331 1.689 1.438 -0.003 -0.223 -0.261 118 ALA CCC CA  
4070  C C   . ALA C 118 ? 2.272 1.629 1.406 -0.030 -0.184 -0.243 118 ALA CCC C   
4071  O O   . ALA C 118 ? 2.257 1.575 1.368 -0.030 -0.165 -0.232 118 ALA CCC O   
4072  C CB  . ALA C 118 ? 2.408 1.707 1.443 0.017  -0.229 -0.265 118 ALA CCC CB  
4073  N N   . PRO C 119 ? 2.230 1.628 1.418 -0.053 -0.174 -0.242 119 PRO CCC N   
4074  C CA  . PRO C 119 ? 2.216 1.625 1.443 -0.076 -0.146 -0.231 119 PRO CCC CA  
4075  C C   . PRO C 119 ? 2.268 1.635 1.473 -0.083 -0.115 -0.220 119 PRO CCC C   
4076  O O   . PRO C 119 ? 2.320 1.672 1.498 -0.076 -0.117 -0.224 119 PRO CCC O   
4077  C CB  . PRO C 119 ? 2.148 1.622 1.439 -0.091 -0.155 -0.236 119 PRO CCC CB  
4078  C CG  . PRO C 119 ? 2.155 1.634 1.438 -0.083 -0.175 -0.247 119 PRO CCC CG  
4079  C CD  . PRO C 119 ? 2.212 1.647 1.432 -0.057 -0.193 -0.254 119 PRO CCC CD  
4080  N N   . SER C 120 ? 2.302 1.652 1.524 -0.095 -0.087 -0.209 120 SER CCC N   
4081  C CA  . SER C 120 ? 2.355 1.674 1.578 -0.104 -0.048 -0.196 120 SER CCC CA  
4082  C C   . SER C 120 ? 2.289 1.659 1.578 -0.122 -0.045 -0.199 120 SER CCC C   
4083  O O   . SER C 120 ? 2.257 1.661 1.608 -0.137 -0.045 -0.200 120 SER CCC O   
4084  C CB  . SER C 120 ? 2.416 1.702 1.652 -0.112 -0.021 -0.184 120 SER CCC CB  
4085  O OG  . SER C 120 ? 2.519 1.747 1.685 -0.092 -0.021 -0.179 120 SER CCC OG  
4086  N N   . VAL C 121 ? 2.283 1.653 1.554 -0.117 -0.046 -0.202 121 VAL CCC N   
4087  C CA  . VAL C 121 ? 2.218 1.630 1.542 -0.130 -0.045 -0.205 121 VAL CCC CA  
4088  C C   . VAL C 121 ? 2.234 1.634 1.584 -0.137 -0.008 -0.195 121 VAL CCC C   
4089  O O   . VAL C 121 ? 2.301 1.651 1.606 -0.127 0.022  -0.186 121 VAL CCC O   
4090  C CB  . VAL C 121 ? 2.206 1.620 1.507 -0.123 -0.064 -0.214 121 VAL CCC CB  
4091  C CG1 . VAL C 121 ? 2.164 1.609 1.514 -0.135 -0.059 -0.215 121 VAL CCC CG1 
4092  C CG2 . VAL C 121 ? 2.189 1.627 1.490 -0.119 -0.099 -0.225 121 VAL CCC CG2 
4093  N N   . PHE C 122 ? 2.183 1.627 1.602 -0.151 -0.009 -0.198 122 PHE CCC N   
4094  C CA  . PHE C 122 ? 2.183 1.635 1.654 -0.158 0.020  -0.193 122 PHE CCC CA  
4095  C C   . PHE C 122 ? 2.148 1.641 1.657 -0.161 0.003  -0.200 122 PHE CCC C   
4096  O O   . PHE C 122 ? 2.117 1.640 1.637 -0.163 -0.027 -0.205 122 PHE CCC O   
4097  C CB  . PHE C 122 ? 2.165 1.627 1.696 -0.171 0.029  -0.192 122 PHE CCC CB  
4098  C CG  . PHE C 122 ? 2.220 1.632 1.726 -0.170 0.066  -0.179 122 PHE CCC CG  
4099  C CD1 . PHE C 122 ? 2.293 1.677 1.799 -0.167 0.113  -0.166 122 PHE CCC CD1 
4100  C CD2 . PHE C 122 ? 2.224 1.609 1.700 -0.169 0.056  -0.177 122 PHE CCC CD2 
4101  C CE1 . PHE C 122 ? 2.382 1.711 1.857 -0.164 0.155  -0.149 122 PHE CCC CE1 
4102  C CE2 . PHE C 122 ? 2.329 1.657 1.775 -0.167 0.093  -0.162 122 PHE CCC CE2 
4103  C CZ  . PHE C 122 ? 2.414 1.711 1.857 -0.164 0.145  -0.146 122 PHE CCC CZ  
4104  N N   . ILE C 123 ? 2.155 1.646 1.679 -0.158 0.025  -0.197 123 ILE CCC N   
4105  C CA  . ILE C 123 ? 2.103 1.627 1.664 -0.157 0.011  -0.203 123 ILE CCC CA  
4106  C C   . ILE C 123 ? 2.079 1.629 1.717 -0.161 0.028  -0.203 123 ILE CCC C   
4107  O O   . ILE C 123 ? 2.090 1.625 1.747 -0.163 0.063  -0.197 123 ILE CCC O   
4108  C CB  . ILE C 123 ? 2.114 1.613 1.629 -0.147 0.013  -0.204 123 ILE CCC CB  
4109  C CG1 . ILE C 123 ? 2.079 1.604 1.618 -0.148 -0.008 -0.207 123 ILE CCC CG1 
4110  C CG2 . ILE C 123 ? 2.163 1.633 1.667 -0.137 0.051  -0.199 123 ILE CCC CG2 
4111  C CD1 . ILE C 123 ? 2.103 1.601 1.601 -0.143 -0.016 -0.210 123 ILE CCC CD1 
4112  N N   . PHE C 124 ? 2.062 1.648 1.744 -0.159 0.004  -0.211 124 PHE CCC N   
4113  C CA  . PHE C 124 ? 2.075 1.695 1.842 -0.158 0.006  -0.218 124 PHE CCC CA  
4114  C C   . PHE C 124 ? 2.057 1.689 1.831 -0.145 -0.004 -0.220 124 PHE CCC C   
4115  O O   . PHE C 124 ? 2.019 1.654 1.764 -0.138 -0.032 -0.221 124 PHE CCC O   
4116  C CB  . PHE C 124 ? 2.090 1.737 1.898 -0.163 -0.027 -0.228 124 PHE CCC CB  
4117  C CG  . PHE C 124 ? 2.113 1.745 1.926 -0.176 -0.017 -0.227 124 PHE CCC CG  
4118  C CD1 . PHE C 124 ? 2.141 1.767 2.006 -0.187 0.020  -0.223 124 PHE CCC CD1 
4119  C CD2 . PHE C 124 ? 2.123 1.745 1.890 -0.177 -0.040 -0.229 124 PHE CCC CD2 
4120  C CE1 . PHE C 124 ? 2.183 1.785 2.049 -0.199 0.032  -0.219 124 PHE CCC CE1 
4121  C CE2 . PHE C 124 ? 2.159 1.760 1.927 -0.187 -0.032 -0.227 124 PHE CCC CE2 
4122  C CZ  . PHE C 124 ? 2.191 1.779 2.006 -0.199 0.004  -0.222 124 PHE CCC CZ  
4123  N N   . PRO C 125 ? 2.070 1.710 1.887 -0.138 0.021  -0.221 125 PRO CCC N   
4124  C CA  . PRO C 125 ? 2.070 1.721 1.900 -0.122 0.009  -0.225 125 PRO CCC CA  
4125  C C   . PRO C 125 ? 2.047 1.738 1.935 -0.115 -0.029 -0.238 125 PRO CCC C   
4126  O O   . PRO C 125 ? 2.039 1.747 1.958 -0.124 -0.046 -0.245 125 PRO CCC O   
4127  C CB  . PRO C 125 ? 2.099 1.750 1.967 -0.115 0.051  -0.223 125 PRO CCC CB  
4128  C CG  . PRO C 125 ? 2.100 1.761 2.019 -0.130 0.079  -0.221 125 PRO CCC CG  
4129  C CD  . PRO C 125 ? 2.097 1.734 1.955 -0.144 0.066  -0.217 125 PRO CCC CD  
4130  N N   . PRO C 126 ? 2.052 1.751 1.948 -0.095 -0.048 -0.242 126 PRO CCC N   
4131  C CA  . PRO C 126 ? 2.042 1.776 1.996 -0.080 -0.085 -0.257 126 PRO CCC CA  
4132  C C   . PRO C 126 ? 2.017 1.793 2.085 -0.082 -0.073 -0.271 126 PRO CCC C   
4133  O O   . PRO C 126 ? 1.986 1.758 2.075 -0.089 -0.028 -0.264 126 PRO CCC O   
4134  C CB  . PRO C 126 ? 2.066 1.784 1.979 -0.055 -0.102 -0.254 126 PRO CCC CB  
4135  C CG  . PRO C 126 ? 2.074 1.759 1.946 -0.058 -0.065 -0.241 126 PRO CCC CG  
4136  C CD  . PRO C 126 ? 2.068 1.736 1.912 -0.083 -0.038 -0.233 126 PRO CCC CD  
4137  N N   . SER C 127 ? 2.003 1.814 2.142 -0.076 -0.112 -0.292 127 SER CCC N   
4138  C CA  . SER C 127 ? 1.985 1.847 2.259 -0.076 -0.111 -0.311 127 SER CCC CA  
4139  C C   . SER C 127 ? 1.992 1.871 2.295 -0.047 -0.116 -0.316 127 SER CCC C   
4140  O O   . SER C 127 ? 2.008 1.858 2.227 -0.024 -0.139 -0.311 127 SER CCC O   
4141  C CB  . SER C 127 ? 1.978 1.868 2.315 -0.075 -0.162 -0.336 127 SER CCC CB  
4142  O OG  . SER C 127 ? 1.996 1.873 2.267 -0.045 -0.217 -0.345 127 SER CCC OG  
4143  N N   . ASP C 128 ? 1.992 1.913 2.411 -0.047 -0.092 -0.326 128 ASP CCC N   
4144  C CA  . ASP C 128 ? 2.016 1.963 2.484 -0.015 -0.104 -0.337 128 ASP CCC CA  
4145  C C   . ASP C 128 ? 2.027 1.996 2.518 0.012  -0.180 -0.363 128 ASP CCC C   
4146  O O   . ASP C 128 ? 2.057 2.007 2.489 0.046  -0.208 -0.363 128 ASP CCC O   
4147  C CB  . ASP C 128 ? 2.024 2.020 2.626 -0.021 -0.057 -0.342 128 ASP CCC CB  
4148  C CG  . ASP C 128 ? 2.059 2.028 2.616 -0.010 0.002  -0.322 128 ASP CCC CG  
4149  O OD1 . ASP C 128 ? 2.071 1.980 2.495 -0.011 0.015  -0.303 128 ASP CCC OD1 
4150  O OD2 . ASP C 128 ? 2.084 2.095 2.746 0.000  0.033  -0.329 128 ASP CCC OD2 
4151  N N   . GLU C 129 ? 2.006 2.003 2.568 0.000  -0.214 -0.385 129 GLU CCC N   
4152  C CA  . GLU C 129 ? 2.005 2.015 2.578 0.028  -0.294 -0.414 129 GLU CCC CA  
4153  C C   . GLU C 129 ? 2.009 1.959 2.419 0.057  -0.320 -0.398 129 GLU CCC C   
4154  O O   . GLU C 129 ? 2.025 1.972 2.416 0.098  -0.358 -0.408 129 GLU CCC O   
4155  C CB  . GLU C 129 ? 2.016 2.041 2.643 0.005  -0.321 -0.433 129 GLU CCC CB  
4156  C CG  . GLU C 129 ? 2.080 2.129 2.757 0.037  -0.407 -0.474 129 GLU CCC CG  
4157  C CD  . GLU C 129 ? 2.116 2.164 2.821 0.020  -0.445 -0.497 129 GLU CCC CD  
4158  O OE1 . GLU C 129 ? 2.146 2.163 2.795 -0.012 -0.408 -0.476 129 GLU CCC OE1 
4159  O OE2 . GLU C 129 ? 2.137 2.213 2.918 0.042  -0.516 -0.538 129 GLU CCC OE2 
4160  N N   . GLN C 130 ? 1.983 1.887 2.284 0.036  -0.295 -0.374 130 GLN CCC N   
4161  C CA  . GLN C 130 ? 2.004 1.851 2.159 0.057  -0.310 -0.355 130 GLN CCC CA  
4162  C C   . GLN C 130 ? 2.039 1.858 2.139 0.080  -0.294 -0.338 130 GLN CCC C   
4163  O O   . GLN C 130 ? 2.080 1.864 2.099 0.114  -0.325 -0.334 130 GLN CCC O   
4164  C CB  . GLN C 130 ? 1.967 1.780 2.040 0.026  -0.276 -0.331 130 GLN CCC CB  
4165  C CG  . GLN C 130 ? 1.985 1.745 1.926 0.043  -0.280 -0.309 130 GLN CCC CG  
4166  C CD  . GLN C 130 ? 1.964 1.700 1.841 0.015  -0.253 -0.290 130 GLN CCC CD  
4167  O OE1 . GLN C 130 ? 1.917 1.666 1.831 -0.017 -0.227 -0.290 130 GLN CCC OE1 
4168  N NE2 . GLN C 130 ? 1.991 1.688 1.769 0.030  -0.258 -0.274 130 GLN CCC NE2 
4169  N N   . LEU C 131 ? 2.039 1.864 2.170 0.063  -0.244 -0.326 131 LEU CCC N   
4170  C CA  . LEU C 131 ? 2.080 1.870 2.153 0.081  -0.224 -0.309 131 LEU CCC CA  
4171  C C   . LEU C 131 ? 2.143 1.940 2.236 0.128  -0.269 -0.325 131 LEU CCC C   
4172  O O   . LEU C 131 ? 2.204 1.951 2.204 0.154  -0.279 -0.311 131 LEU CCC O   
4173  C CB  . LEU C 131 ? 2.055 1.855 2.173 0.062  -0.168 -0.302 131 LEU CCC CB  
4174  C CG  . LEU C 131 ? 2.034 1.801 2.088 0.027  -0.125 -0.282 131 LEU CCC CG  
4175  C CD1 . LEU C 131 ? 2.028 1.806 2.130 0.013  -0.072 -0.279 131 LEU CCC CD1 
4176  C CD2 . LEU C 131 ? 2.060 1.765 2.000 0.032  -0.122 -0.262 131 LEU CCC CD2 
4177  N N   . LYS C 132 ? 2.158 2.016 2.373 0.139  -0.295 -0.355 132 LYS CCC N   
4178  C CA  . LYS C 132 ? 2.234 2.110 2.488 0.189  -0.346 -0.377 132 LYS CCC CA  
4179  C C   . LYS C 132 ? 2.307 2.141 2.461 0.224  -0.404 -0.380 132 LYS CCC C   
4180  O O   . LYS C 132 ? 2.375 2.186 2.492 0.272  -0.437 -0.384 132 LYS CCC O   
4181  C CB  . LYS C 132 ? 2.227 2.185 2.652 0.186  -0.365 -0.412 132 LYS CCC CB  
4182  C CG  . LYS C 132 ? 2.208 2.206 2.736 0.163  -0.303 -0.408 132 LYS CCC CG  
4183  C CD  . LYS C 132 ? 2.207 2.290 2.922 0.156  -0.314 -0.441 132 LYS CCC CD  
4184  C CE  . LYS C 132 ? 2.191 2.296 2.959 0.118  -0.322 -0.451 132 LYS CCC CE  
4185  N NZ  . LYS C 132 ? 2.180 2.365 3.147 0.104  -0.321 -0.479 132 LYS CCC NZ  
4186  N N   . SER C 133 ? 2.326 2.144 2.431 0.206  -0.414 -0.377 133 SER CCC N   
4187  C CA  . SER C 133 ? 2.416 2.190 2.415 0.242  -0.463 -0.379 133 SER CCC CA  
4188  C C   . SER C 133 ? 2.470 2.167 2.327 0.265  -0.443 -0.343 133 SER CCC C   
4189  O O   . SER C 133 ? 2.578 2.236 2.360 0.317  -0.485 -0.346 133 SER CCC O   
4190  C CB  . SER C 133 ? 2.423 2.195 2.399 0.215  -0.467 -0.381 133 SER CCC CB  
4191  O OG  . SER C 133 ? 2.428 2.155 2.304 0.189  -0.417 -0.344 133 SER CCC OG  
4192  N N   . GLY C 134 ? 2.408 2.082 2.230 0.229  -0.382 -0.312 134 GLY CCC N   
4193  C CA  . GLY C 134 ? 2.428 2.029 2.134 0.240  -0.355 -0.277 134 GLY CCC CA  
4194  C C   . GLY C 134 ? 2.368 1.947 2.029 0.193  -0.304 -0.250 134 GLY CCC C   
4195  O O   . GLY C 134 ? 2.371 1.917 2.003 0.179  -0.267 -0.229 134 GLY CCC O   
4196  N N   . THR C 135 ? 2.331 1.925 1.986 0.172  -0.307 -0.253 135 THR CCC N   
4197  C CA  . THR C 135 ? 2.286 1.867 1.909 0.129  -0.265 -0.232 135 THR CCC CA  
4198  C C   . THR C 135 ? 2.203 1.830 1.913 0.088  -0.240 -0.243 135 THR CCC C   
4199  O O   . THR C 135 ? 2.164 1.834 1.962 0.092  -0.253 -0.266 135 THR CCC O   
4200  C CB  . THR C 135 ? 2.305 1.877 1.873 0.132  -0.278 -0.228 135 THR CCC CB  
4201  O OG1 . THR C 135 ? 2.303 1.913 1.922 0.145  -0.322 -0.260 135 THR CCC OG1 
4202  C CG2 . THR C 135 ? 2.378 1.889 1.837 0.167  -0.280 -0.205 135 THR CCC CG2 
4203  N N   . ALA C 136 ? 2.180 1.794 1.866 0.053  -0.204 -0.227 136 ALA CCC N   
4204  C CA  . ALA C 136 ? 2.145 1.787 1.884 0.017  -0.176 -0.233 136 ALA CCC CA  
4205  C C   . ALA C 136 ? 2.136 1.766 1.831 -0.009 -0.162 -0.221 136 ALA CCC C   
4206  O O   . ALA C 136 ? 2.154 1.749 1.790 -0.015 -0.147 -0.202 136 ALA CCC O   
4207  C CB  . ALA C 136 ? 2.152 1.777 1.896 0.010  -0.144 -0.226 136 ALA CCC CB  
4208  N N   . SER C 137 ? 2.110 1.769 1.840 -0.024 -0.168 -0.233 137 SER CCC N   
4209  C CA  . SER C 137 ? 2.076 1.728 1.769 -0.043 -0.161 -0.226 137 SER CCC CA  
4210  C C   . SER C 137 ? 2.054 1.713 1.774 -0.073 -0.131 -0.226 137 SER CCC C   
4211  O O   . SER C 137 ? 2.048 1.730 1.830 -0.080 -0.127 -0.238 137 SER CCC O   
4212  C CB  . SER C 137 ? 2.058 1.724 1.752 -0.032 -0.193 -0.239 137 SER CCC CB  
4213  O OG  . SER C 137 ? 2.081 1.726 1.718 0.000  -0.215 -0.233 137 SER CCC OG  
4214  N N   . VAL C 138 ? 2.072 1.708 1.745 -0.088 -0.112 -0.213 138 VAL CCC N   
4215  C CA  . VAL C 138 ? 2.098 1.727 1.770 -0.110 -0.088 -0.212 138 VAL CCC CA  
4216  C C   . VAL C 138 ? 2.105 1.737 1.754 -0.120 -0.095 -0.211 138 VAL CCC C   
4217  O O   . VAL C 138 ? 2.141 1.764 1.751 -0.119 -0.100 -0.202 138 VAL CCC O   
4218  C CB  . VAL C 138 ? 2.139 1.737 1.776 -0.115 -0.070 -0.204 138 VAL CCC CB  
4219  C CG1 . VAL C 138 ? 2.151 1.735 1.777 -0.128 -0.049 -0.206 138 VAL CCC CG1 
4220  C CG2 . VAL C 138 ? 2.174 1.764 1.826 -0.100 -0.066 -0.205 138 VAL CCC CG2 
4221  N N   . VAL C 139 ? 2.101 1.744 1.776 -0.129 -0.093 -0.219 139 VAL CCC N   
4222  C CA  . VAL C 139 ? 2.095 1.737 1.748 -0.135 -0.102 -0.219 139 VAL CCC CA  
4223  C C   . VAL C 139 ? 2.052 1.674 1.680 -0.149 -0.080 -0.215 139 VAL CCC C   
4224  O O   . VAL C 139 ? 2.026 1.635 1.666 -0.154 -0.058 -0.214 139 VAL CCC O   
4225  C CB  . VAL C 139 ? 2.136 1.796 1.833 -0.134 -0.119 -0.233 139 VAL CCC CB  
4226  C CG1 . VAL C 139 ? 2.150 1.805 1.815 -0.133 -0.134 -0.235 139 VAL CCC CG1 
4227  C CG2 . VAL C 139 ? 2.166 1.844 1.896 -0.116 -0.145 -0.244 139 VAL CCC CG2 
4228  N N   . CYS C 140 ? 2.040 1.656 1.629 -0.151 -0.087 -0.211 140 CYS CCC N   
4229  C CA  . CYS C 140 ? 2.066 1.660 1.623 -0.157 -0.078 -0.210 140 CYS CCC CA  
4230  C C   . CYS C 140 ? 2.065 1.664 1.613 -0.156 -0.091 -0.213 140 CYS CCC C   
4231  O O   . CYS C 140 ? 2.055 1.673 1.603 -0.149 -0.107 -0.214 140 CYS CCC O   
4232  C CB  . CYS C 140 ? 2.095 1.681 1.623 -0.158 -0.081 -0.207 140 CYS CCC CB  
4233  S SG  . CYS C 140 ? 2.168 1.721 1.652 -0.159 -0.077 -0.211 140 CYS CCC SG  
4234  N N   . LEU C 141 ? 2.089 1.666 1.624 -0.160 -0.081 -0.214 141 LEU CCC N   
4235  C CA  . LEU C 141 ? 2.084 1.657 1.614 -0.158 -0.091 -0.218 141 LEU CCC CA  
4236  C C   . LEU C 141 ? 2.072 1.618 1.553 -0.154 -0.089 -0.216 141 LEU CCC C   
4237  O O   . LEU C 141 ? 2.116 1.629 1.573 -0.155 -0.070 -0.211 141 LEU CCC O   
4238  C CB  . LEU C 141 ? 2.102 1.668 1.676 -0.166 -0.080 -0.221 141 LEU CCC CB  
4239  C CG  . LEU C 141 ? 2.118 1.662 1.689 -0.169 -0.081 -0.224 141 LEU CCC CG  
4240  C CD1 . LEU C 141 ? 2.108 1.666 1.667 -0.159 -0.112 -0.233 141 LEU CCC CD1 
4241  C CD2 . LEU C 141 ? 2.126 1.665 1.761 -0.182 -0.066 -0.226 141 LEU CCC CD2 
4242  N N   . LEU C 142 ? 2.022 1.580 1.485 -0.146 -0.107 -0.219 142 LEU CCC N   
4243  C CA  . LEU C 142 ? 2.031 1.568 1.452 -0.137 -0.114 -0.220 142 LEU CCC CA  
4244  C C   . LEU C 142 ? 2.046 1.569 1.461 -0.132 -0.120 -0.223 142 LEU CCC C   
4245  O O   . LEU C 142 ? 2.058 1.605 1.482 -0.125 -0.136 -0.229 142 LEU CCC O   
4246  C CB  . LEU C 142 ? 2.007 1.573 1.427 -0.131 -0.130 -0.223 142 LEU CCC CB  
4247  C CG  . LEU C 142 ? 2.005 1.578 1.432 -0.136 -0.129 -0.223 142 LEU CCC CG  
4248  C CD1 . LEU C 142 ? 1.989 1.575 1.446 -0.146 -0.118 -0.218 142 LEU CCC CD1 
4249  C CD2 . LEU C 142 ? 1.991 1.595 1.434 -0.133 -0.144 -0.227 142 LEU CCC CD2 
4250  N N   . ASN C 143 ? 2.070 1.550 1.467 -0.134 -0.104 -0.219 143 ASN CCC N   
4251  C CA  . ASN C 143 ? 2.091 1.547 1.489 -0.133 -0.108 -0.222 143 ASN CCC CA  
4252  C C   . ASN C 143 ? 2.140 1.568 1.483 -0.115 -0.118 -0.223 143 ASN CCC C   
4253  O O   . ASN C 143 ? 2.174 1.575 1.471 -0.106 -0.112 -0.218 143 ASN CCC O   
4254  C CB  . ASN C 143 ? 2.115 1.537 1.538 -0.147 -0.080 -0.215 143 ASN CCC CB  
4255  C CG  . ASN C 143 ? 2.137 1.552 1.599 -0.154 -0.089 -0.223 143 ASN CCC CG  
4256  O OD1 . ASN C 143 ? 2.111 1.560 1.602 -0.152 -0.116 -0.237 143 ASN CCC OD1 
4257  N ND2 . ASN C 143 ? 2.202 1.565 1.658 -0.160 -0.068 -0.215 143 ASN CCC ND2 
4258  N N   . ASN C 144 ? 2.190 1.622 1.532 -0.106 -0.137 -0.231 144 ASN CCC N   
4259  C CA  . ASN C 144 ? 2.262 1.660 1.556 -0.086 -0.148 -0.233 144 ASN CCC CA  
4260  C C   . ASN C 144 ? 2.264 1.670 1.521 -0.069 -0.159 -0.233 144 ASN CCC C   
4261  O O   . ASN C 144 ? 2.306 1.671 1.521 -0.064 -0.148 -0.227 144 ASN CCC O   
4262  C CB  . ASN C 144 ? 2.347 1.676 1.616 -0.090 -0.127 -0.223 144 ASN CCC CB  
4263  C CG  . ASN C 144 ? 2.371 1.692 1.695 -0.110 -0.120 -0.226 144 ASN CCC CG  
4264  O OD1 . ASN C 144 ? 2.421 1.709 1.766 -0.127 -0.091 -0.216 144 ASN CCC OD1 
4265  N ND2 . ASN C 144 ? 2.360 1.709 1.710 -0.106 -0.147 -0.242 144 ASN CCC ND2 
4266  N N   . PHE C 145 ? 2.238 1.693 1.510 -0.058 -0.179 -0.242 145 PHE CCC N   
4267  C CA  . PHE C 145 ? 2.246 1.720 1.505 -0.042 -0.195 -0.248 145 PHE CCC CA  
4268  C C   . PHE C 145 ? 2.219 1.738 1.499 -0.025 -0.212 -0.257 145 PHE CCC C   
4269  O O   . PHE C 145 ? 2.192 1.733 1.493 -0.026 -0.208 -0.257 145 PHE CCC O   
4270  C CB  . PHE C 145 ? 2.216 1.719 1.503 -0.057 -0.191 -0.247 145 PHE CCC CB  
4271  C CG  . PHE C 145 ? 2.141 1.698 1.483 -0.071 -0.184 -0.245 145 PHE CCC CG  
4272  C CD1 . PHE C 145 ? 2.112 1.666 1.471 -0.087 -0.168 -0.238 145 PHE CCC CD1 
4273  C CD2 . PHE C 145 ? 2.113 1.721 1.491 -0.066 -0.192 -0.249 145 PHE CCC CD2 
4274  C CE1 . PHE C 145 ? 2.085 1.679 1.481 -0.094 -0.165 -0.236 145 PHE CCC CE1 
4275  C CE2 . PHE C 145 ? 2.089 1.734 1.504 -0.075 -0.180 -0.243 145 PHE CCC CE2 
4276  C CZ  . PHE C 145 ? 2.080 1.715 1.497 -0.087 -0.168 -0.236 145 PHE CCC CZ  
4277  N N   . TYR C 146 ? 2.223 1.752 1.495 -0.006 -0.231 -0.266 146 TYR CCC N   
4278  C CA  . TYR C 146 ? 2.196 1.777 1.501 0.013  -0.245 -0.275 146 TYR CCC CA  
4279  C C   . TYR C 146 ? 2.202 1.811 1.532 0.019  -0.265 -0.286 146 TYR CCC C   
4280  O O   . TYR C 146 ? 2.281 1.846 1.566 0.029  -0.281 -0.291 146 TYR CCC O   
4281  C CB  . TYR C 146 ? 2.228 1.781 1.494 0.040  -0.256 -0.280 146 TYR CCC CB  
4282  C CG  . TYR C 146 ? 2.207 1.817 1.511 0.061  -0.263 -0.289 146 TYR CCC CG  
4283  C CD1 . TYR C 146 ? 2.168 1.808 1.493 0.061  -0.247 -0.285 146 TYR CCC CD1 
4284  C CD2 . TYR C 146 ? 2.227 1.864 1.549 0.084  -0.286 -0.301 146 TYR CCC CD2 
4285  C CE1 . TYR C 146 ? 2.153 1.845 1.512 0.083  -0.245 -0.289 146 TYR CCC CE1 
4286  C CE2 . TYR C 146 ? 2.207 1.904 1.578 0.103  -0.286 -0.308 146 TYR CCC CE2 
4287  C CZ  . TYR C 146 ? 2.168 1.892 1.556 0.102  -0.261 -0.300 146 TYR CCC CZ  
4288  O OH  . TYR C 146 ? 2.161 1.942 1.593 0.123  -0.252 -0.303 146 TYR CCC OH  
4289  N N   . PRO C 147 ? 2.167 1.844 1.569 0.016  -0.265 -0.290 147 PRO CCC N   
4290  C CA  . PRO C 147 ? 2.157 1.881 1.600 0.013  -0.243 -0.282 147 PRO CCC CA  
4291  C C   . PRO C 147 ? 2.147 1.878 1.607 -0.014 -0.217 -0.268 147 PRO CCC C   
4292  O O   . PRO C 147 ? 2.120 1.818 1.559 -0.031 -0.215 -0.264 147 PRO CCC O   
4293  C CB  . PRO C 147 ? 2.149 1.938 1.666 0.022  -0.251 -0.292 147 PRO CCC CB  
4294  C CG  . PRO C 147 ? 2.140 1.927 1.680 0.009  -0.272 -0.302 147 PRO CCC CG  
4295  C CD  . PRO C 147 ? 2.177 1.887 1.627 0.016  -0.287 -0.304 147 PRO CCC CD  
4296  N N   . ARG C 148 ? 2.166 1.936 1.656 -0.011 -0.196 -0.259 148 ARG CCC N   
4297  C CA  . ARG C 148 ? 2.182 1.956 1.679 -0.027 -0.172 -0.244 148 ARG CCC CA  
4298  C C   . ARG C 148 ? 2.152 1.942 1.695 -0.053 -0.166 -0.240 148 ARG CCC C   
4299  O O   . ARG C 148 ? 2.111 1.877 1.639 -0.069 -0.160 -0.233 148 ARG CCC O   
4300  C CB  . ARG C 148 ? 2.234 2.041 1.743 -0.010 -0.149 -0.235 148 ARG CCC CB  
4301  C CG  . ARG C 148 ? 2.278 2.067 1.755 -0.009 -0.133 -0.224 148 ARG CCC CG  
4302  C CD  . ARG C 148 ? 2.361 2.158 1.811 0.023  -0.120 -0.221 148 ARG CCC CD  
4303  N NE  . ARG C 148 ? 2.426 2.185 1.818 0.035  -0.126 -0.223 148 ARG CCC NE  
4304  C CZ  . ARG C 148 ? 2.459 2.210 1.837 0.033  -0.114 -0.212 148 ARG CCC CZ  
4305  N NH1 . ARG C 148 ? 2.458 2.231 1.874 0.017  -0.090 -0.195 148 ARG CCC NH1 
4306  N NH2 . ARG C 148 ? 2.482 2.199 1.810 0.049  -0.129 -0.219 148 ARG CCC NH2 
4307  N N   . GLU C 149 ? 2.180 2.012 1.785 -0.054 -0.169 -0.245 149 GLU CCC N   
4308  C CA  . GLU C 149 ? 2.192 2.046 1.858 -0.078 -0.162 -0.242 149 GLU CCC CA  
4309  C C   . GLU C 149 ? 2.158 1.968 1.793 -0.092 -0.184 -0.252 149 GLU CCC C   
4310  O O   . GLU C 149 ? 2.178 1.981 1.815 -0.086 -0.214 -0.270 149 GLU CCC O   
4311  C CB  . GLU C 149 ? 2.253 2.161 2.005 -0.077 -0.167 -0.252 149 GLU CCC CB  
4312  C CG  . GLU C 149 ? 2.322 2.273 2.099 -0.056 -0.144 -0.244 149 GLU CCC CG  
4313  C CD  . GLU C 149 ? 2.395 2.345 2.143 -0.026 -0.169 -0.260 149 GLU CCC CD  
4314  O OE1 . GLU C 149 ? 2.417 2.390 2.209 -0.020 -0.199 -0.280 149 GLU CCC OE1 
4315  O OE2 . GLU C 149 ? 2.436 2.359 2.115 -0.006 -0.163 -0.255 149 GLU CCC OE2 
4316  N N   . ALA C 150 ? 2.111 1.891 1.715 -0.104 -0.170 -0.240 150 ALA CCC N   
4317  C CA  . ALA C 150 ? 2.100 1.841 1.678 -0.117 -0.179 -0.245 150 ALA CCC CA  
4318  C C   . ALA C 150 ? 2.078 1.825 1.691 -0.137 -0.161 -0.234 150 ALA CCC C   
4319  O O   . ALA C 150 ? 2.095 1.849 1.706 -0.138 -0.137 -0.217 150 ALA CCC O   
4320  C CB  . ALA C 150 ? 2.108 1.806 1.621 -0.111 -0.176 -0.242 150 ALA CCC CB  
4321  N N   . LYS C 151 ? 2.056 1.796 1.695 -0.150 -0.175 -0.245 151 LYS CCC N   
4322  C CA  . LYS C 151 ? 2.026 1.760 1.695 -0.169 -0.161 -0.237 151 LYS CCC CA  
4323  C C   . LYS C 151 ? 2.000 1.688 1.611 -0.170 -0.159 -0.235 151 LYS CCC C   
4324  O O   . LYS C 151 ? 2.003 1.658 1.573 -0.163 -0.177 -0.249 151 LYS CCC O   
4325  C CB  . LYS C 151 ? 2.050 1.795 1.780 -0.182 -0.181 -0.253 151 LYS CCC CB  
4326  C CG  . LYS C 151 ? 2.073 1.799 1.830 -0.202 -0.172 -0.248 151 LYS CCC CG  
4327  C CD  . LYS C 151 ? 2.116 1.845 1.934 -0.215 -0.201 -0.272 151 LYS CCC CD  
4328  C CE  . LYS C 151 ? 2.159 1.843 1.967 -0.227 -0.206 -0.277 151 LYS CCC CE  
4329  N NZ  . LYS C 151 ? 2.198 1.874 2.052 -0.234 -0.247 -0.309 151 LYS CCC NZ  
4330  N N   . VAL C 152 ? 1.976 1.660 1.581 -0.174 -0.135 -0.218 152 VAL CCC N   
4331  C CA  . VAL C 152 ? 1.991 1.640 1.563 -0.176 -0.130 -0.215 152 VAL CCC CA  
4332  C C   . VAL C 152 ? 2.025 1.667 1.628 -0.189 -0.120 -0.208 152 VAL CCC C   
4333  O O   . VAL C 152 ? 2.049 1.711 1.681 -0.193 -0.103 -0.193 152 VAL CCC O   
4334  C CB  . VAL C 152 ? 1.965 1.612 1.511 -0.167 -0.117 -0.205 152 VAL CCC CB  
4335  C CG1 . VAL C 152 ? 1.957 1.578 1.488 -0.168 -0.110 -0.203 152 VAL CCC CG1 
4336  C CG2 . VAL C 152 ? 1.970 1.616 1.489 -0.156 -0.126 -0.212 152 VAL CCC CG2 
4337  N N   . GLN C 153 ? 2.068 1.677 1.659 -0.194 -0.128 -0.219 153 GLN CCC N   
4338  C CA  . GLN C 153 ? 2.091 1.682 1.704 -0.205 -0.119 -0.213 153 GLN CCC CA  
4339  C C   . GLN C 153 ? 2.093 1.649 1.666 -0.197 -0.116 -0.215 153 GLN CCC C   
4340  O O   . GLN C 153 ? 2.094 1.629 1.629 -0.188 -0.125 -0.229 153 GLN CCC O   
4341  C CB  . GLN C 153 ? 2.125 1.713 1.783 -0.219 -0.136 -0.227 153 GLN CCC CB  
4342  C CG  . GLN C 153 ? 2.170 1.736 1.855 -0.232 -0.124 -0.218 153 GLN CCC CG  
4343  C CD  . GLN C 153 ? 2.188 1.772 1.951 -0.252 -0.121 -0.215 153 GLN CCC CD  
4344  O OE1 . GLN C 153 ? 2.195 1.804 2.002 -0.259 -0.141 -0.232 153 GLN CCC OE1 
4345  N NE2 . GLN C 153 ? 2.198 1.770 1.984 -0.262 -0.094 -0.193 153 GLN CCC NE2 
4346  N N   . TRP C 154 ? 2.078 1.625 1.657 -0.198 -0.100 -0.201 154 TRP CCC N   
4347  C CA  . TRP C 154 ? 2.076 1.593 1.630 -0.189 -0.094 -0.203 154 TRP CCC CA  
4348  C C   . TRP C 154 ? 2.124 1.603 1.680 -0.195 -0.102 -0.214 154 TRP CCC C   
4349  O O   . TRP C 154 ? 2.149 1.627 1.742 -0.210 -0.103 -0.210 154 TRP CCC O   
4350  C CB  . TRP C 154 ? 2.036 1.561 1.593 -0.181 -0.079 -0.185 154 TRP CCC CB  
4351  C CG  . TRP C 154 ? 1.986 1.540 1.536 -0.171 -0.078 -0.181 154 TRP CCC CG  
4352  C CD1 . TRP C 154 ? 1.978 1.557 1.532 -0.169 -0.077 -0.172 154 TRP CCC CD1 
4353  C CD2 . TRP C 154 ? 1.968 1.526 1.508 -0.162 -0.077 -0.187 154 TRP CCC CD2 
4354  N NE1 . TRP C 154 ? 1.968 1.563 1.512 -0.158 -0.082 -0.175 154 TRP CCC NE1 
4355  C CE2 . TRP C 154 ? 1.958 1.542 1.500 -0.156 -0.082 -0.184 154 TRP CCC CE2 
4356  C CE3 . TRP C 154 ? 1.986 1.529 1.523 -0.157 -0.071 -0.195 154 TRP CCC CE3 
4357  C CZ2 . TRP C 154 ? 1.957 1.552 1.506 -0.149 -0.084 -0.191 154 TRP CCC CZ2 
4358  C CZ3 . TRP C 154 ? 1.989 1.547 1.536 -0.150 -0.067 -0.198 154 TRP CCC CZ3 
4359  C CH2 . TRP C 154 ? 1.976 1.558 1.533 -0.149 -0.075 -0.197 154 TRP CCC CH2 
4360  N N   . LYS C 155 ? 2.147 1.595 1.668 -0.184 -0.105 -0.227 155 LYS CCC N   
4361  C CA  . LYS C 155 ? 2.194 1.596 1.703 -0.182 -0.110 -0.238 155 LYS CCC CA  
4362  C C   . LYS C 155 ? 2.174 1.564 1.665 -0.166 -0.090 -0.230 155 LYS CCC C   
4363  O O   . LYS C 155 ? 2.148 1.555 1.625 -0.155 -0.077 -0.227 155 LYS CCC O   
4364  C CB  . LYS C 155 ? 2.269 1.638 1.739 -0.173 -0.131 -0.263 155 LYS CCC CB  
4365  C CG  . LYS C 155 ? 2.295 1.679 1.784 -0.183 -0.158 -0.277 155 LYS CCC CG  
4366  C CD  . LYS C 155 ? 2.376 1.721 1.809 -0.165 -0.183 -0.303 155 LYS CCC CD  
4367  C CE  . LYS C 155 ? 2.389 1.751 1.849 -0.171 -0.218 -0.321 155 LYS CCC CE  
4368  N NZ  . LYS C 155 ? 2.457 1.769 1.856 -0.148 -0.253 -0.352 155 LYS CCC NZ  
4369  N N   . VAL C 156 ? 2.176 1.540 1.677 -0.166 -0.087 -0.226 156 VAL CCC N   
4370  C CA  . VAL C 156 ? 2.186 1.532 1.671 -0.147 -0.073 -0.224 156 VAL CCC CA  
4371  C C   . VAL C 156 ? 2.246 1.535 1.708 -0.142 -0.082 -0.240 156 VAL CCC C   
4372  O O   . VAL C 156 ? 2.285 1.550 1.767 -0.154 -0.091 -0.238 156 VAL CCC O   
4373  C CB  . VAL C 156 ? 2.162 1.525 1.670 -0.143 -0.063 -0.203 156 VAL CCC CB  
4374  C CG1 . VAL C 156 ? 2.181 1.523 1.681 -0.122 -0.054 -0.202 156 VAL CCC CG1 
4375  C CG2 . VAL C 156 ? 2.119 1.532 1.640 -0.143 -0.060 -0.193 156 VAL CCC CG2 
4376  N N   . ASP C 157 ? 2.280 1.543 1.699 -0.123 -0.079 -0.256 157 ASP CCC N   
4377  C CA  . ASP C 157 ? 2.358 1.559 1.739 -0.113 -0.094 -0.278 157 ASP CCC CA  
4378  C C   . ASP C 157 ? 2.383 1.571 1.774 -0.132 -0.127 -0.295 157 ASP CCC C   
4379  O O   . ASP C 157 ? 2.400 1.554 1.811 -0.143 -0.145 -0.304 157 ASP CCC O   
4380  C CB  . ASP C 157 ? 2.382 1.550 1.771 -0.105 -0.088 -0.274 157 ASP CCC CB  
4381  C CG  . ASP C 157 ? 2.355 1.545 1.749 -0.085 -0.061 -0.260 157 ASP CCC CG  
4382  O OD1 . ASP C 157 ? 2.327 1.547 1.714 -0.073 -0.042 -0.258 157 ASP CCC OD1 
4383  O OD2 . ASP C 157 ? 2.359 1.534 1.769 -0.080 -0.058 -0.251 157 ASP CCC OD2 
4384  N N   . ASN C 158 ? 2.392 1.607 1.775 -0.135 -0.135 -0.299 158 ASN CCC N   
4385  C CA  . ASN C 158 ? 2.425 1.639 1.824 -0.149 -0.171 -0.317 158 ASN CCC CA  
4386  C C   . ASN C 158 ? 2.423 1.645 1.896 -0.178 -0.181 -0.313 158 ASN CCC C   
4387  O O   . ASN C 158 ? 2.475 1.661 1.964 -0.186 -0.212 -0.337 158 ASN CCC O   
4388  C CB  . ASN C 158 ? 2.527 1.681 1.861 -0.127 -0.200 -0.351 158 ASN CCC CB  
4389  C CG  . ASN C 158 ? 2.575 1.722 1.835 -0.100 -0.190 -0.353 158 ASN CCC CG  
4390  O OD1 . ASN C 158 ? 2.507 1.699 1.780 -0.106 -0.176 -0.336 158 ASN CCC OD1 
4391  N ND2 . ASN C 158 ? 2.682 1.766 1.860 -0.067 -0.198 -0.373 158 ASN CCC ND2 
4392  N N   . ALA C 159 ? 2.388 1.649 1.902 -0.191 -0.155 -0.283 159 ALA CCC N   
4393  C CA  . ALA C 159 ? 2.391 1.663 1.973 -0.217 -0.149 -0.267 159 ALA CCC CA  
4394  C C   . ALA C 159 ? 2.334 1.664 1.940 -0.223 -0.126 -0.239 159 ALA CCC C   
4395  O O   . ALA C 159 ? 2.313 1.657 1.891 -0.208 -0.106 -0.223 159 ALA CCC O   
4396  C CB  . ALA C 159 ? 2.430 1.659 2.008 -0.213 -0.135 -0.257 159 ALA CCC CB  
4397  N N   . LEU C 160 ? 2.320 1.682 1.980 -0.243 -0.131 -0.237 160 LEU CCC N   
4398  C CA  . LEU C 160 ? 2.284 1.700 1.959 -0.245 -0.113 -0.216 160 LEU CCC CA  
4399  C C   . LEU C 160 ? 2.287 1.702 1.955 -0.239 -0.081 -0.185 160 LEU CCC C   
4400  O O   . LEU C 160 ? 2.322 1.710 2.019 -0.251 -0.068 -0.171 160 LEU CCC O   
4401  C CB  . LEU C 160 ? 2.290 1.738 2.033 -0.266 -0.121 -0.220 160 LEU CCC CB  
4402  C CG  . LEU C 160 ? 2.329 1.777 2.082 -0.267 -0.161 -0.256 160 LEU CCC CG  
4403  C CD1 . LEU C 160 ? 2.326 1.813 2.169 -0.289 -0.169 -0.261 160 LEU CCC CD1 
4404  C CD2 . LEU C 160 ? 2.327 1.786 2.014 -0.244 -0.171 -0.265 160 LEU CCC CD2 
4405  N N   . GLN C 161 ? 2.270 1.708 1.901 -0.220 -0.071 -0.174 161 GLN CCC N   
4406  C CA  . GLN C 161 ? 2.268 1.711 1.887 -0.208 -0.048 -0.146 161 GLN CCC CA  
4407  C C   . GLN C 161 ? 2.250 1.732 1.889 -0.213 -0.036 -0.133 161 GLN CCC C   
4408  O O   . GLN C 161 ? 2.197 1.711 1.848 -0.218 -0.050 -0.147 161 GLN CCC O   
4409  C CB  . GLN C 161 ? 2.243 1.688 1.820 -0.184 -0.051 -0.148 161 GLN CCC CB  
4410  C CG  . GLN C 161 ? 2.253 1.660 1.815 -0.175 -0.055 -0.157 161 GLN CCC CG  
4411  C CD  . GLN C 161 ? 2.288 1.658 1.844 -0.167 -0.043 -0.139 161 GLN CCC CD  
4412  O OE1 . GLN C 161 ? 2.306 1.672 1.867 -0.170 -0.027 -0.117 161 GLN CCC OE1 
4413  N NE2 . GLN C 161 ? 2.301 1.638 1.840 -0.154 -0.046 -0.147 161 GLN CCC NE2 
4414  N N   . SER C 162 ? 2.288 1.761 1.925 -0.208 -0.010 -0.105 162 SER CCC N   
4415  C CA  . SER C 162 ? 2.287 1.786 1.951 -0.213 0.012  -0.087 162 SER CCC CA  
4416  C C   . SER C 162 ? 2.307 1.781 1.930 -0.191 0.043  -0.054 162 SER CCC C   
4417  O O   . SER C 162 ? 2.337 1.767 1.964 -0.195 0.062  -0.036 162 SER CCC O   
4418  C CB  . SER C 162 ? 2.312 1.813 2.050 -0.243 0.018  -0.090 162 SER CCC CB  
4419  O OG  . SER C 162 ? 2.350 1.877 2.125 -0.248 0.048  -0.070 162 SER CCC OG  
4420  N N   . GLY C 163 ? 2.287 1.781 1.865 -0.165 0.045  -0.047 163 GLY CCC N   
4421  C CA  . GLY C 163 ? 2.338 1.804 1.858 -0.134 0.069  -0.019 163 GLY CCC CA  
4422  C C   . GLY C 163 ? 2.333 1.793 1.791 -0.100 0.041  -0.029 163 GLY CCC C   
4423  O O   . GLY C 163 ? 2.383 1.826 1.782 -0.066 0.049  -0.013 163 GLY CCC O   
4424  N N   . ASN C 164 ? 2.293 1.764 1.765 -0.107 0.010  -0.055 164 ASN CCC N   
4425  C CA  . ASN C 164 ? 2.298 1.769 1.738 -0.081 -0.018 -0.070 164 ASN CCC CA  
4426  C C   . ASN C 164 ? 2.240 1.755 1.698 -0.086 -0.041 -0.095 164 ASN CCC C   
4427  O O   . ASN C 164 ? 2.215 1.738 1.670 -0.072 -0.064 -0.111 164 ASN CCC O   
4428  C CB  . ASN C 164 ? 2.307 1.752 1.756 -0.082 -0.025 -0.076 164 ASN CCC CB  
4429  C CG  . ASN C 164 ? 2.292 1.736 1.786 -0.115 -0.023 -0.087 164 ASN CCC CG  
4430  O OD1 . ASN C 164 ? 2.253 1.727 1.774 -0.135 -0.028 -0.101 164 ASN CCC OD1 
4431  N ND2 . ASN C 164 ? 2.339 1.743 1.835 -0.118 -0.017 -0.083 164 ASN CCC ND2 
4432  N N   . SER C 165 ? 2.203 1.745 1.683 -0.104 -0.035 -0.098 165 SER CCC N   
4433  C CA  . SER C 165 ? 2.147 1.722 1.635 -0.107 -0.054 -0.118 165 SER CCC CA  
4434  C C   . SER C 165 ? 2.158 1.745 1.616 -0.087 -0.051 -0.111 165 SER CCC C   
4435  O O   . SER C 165 ? 2.198 1.770 1.635 -0.077 -0.027 -0.088 165 SER CCC O   
4436  C CB  . SER C 165 ? 2.110 1.701 1.634 -0.134 -0.055 -0.131 165 SER CCC CB  
4437  O OG  . SER C 165 ? 2.101 1.708 1.641 -0.143 -0.042 -0.122 165 SER CCC OG  
4438  N N   . GLN C 166 ? 2.122 1.729 1.576 -0.081 -0.071 -0.129 166 GLN CCC N   
4439  C CA  . GLN C 166 ? 2.136 1.751 1.556 -0.059 -0.074 -0.128 166 GLN CCC CA  
4440  C C   . GLN C 166 ? 2.113 1.751 1.551 -0.068 -0.093 -0.149 166 GLN CCC C   
4441  O O   . GLN C 166 ? 2.092 1.731 1.545 -0.072 -0.114 -0.166 166 GLN CCC O   
4442  C CB  . GLN C 166 ? 2.158 1.753 1.529 -0.022 -0.090 -0.129 166 GLN CCC CB  
4443  C CG  . GLN C 166 ? 2.201 1.767 1.518 0.005  -0.065 -0.102 166 GLN CCC CG  
4444  C CD  . GLN C 166 ? 2.251 1.788 1.508 0.047  -0.090 -0.107 166 GLN CCC CD  
4445  O OE1 . GLN C 166 ? 2.230 1.776 1.481 0.062  -0.127 -0.132 166 GLN CCC OE1 
4446  N NE2 . GLN C 166 ? 2.320 1.819 1.534 0.068  -0.073 -0.084 166 GLN CCC NE2 
4447  N N   . GLU C 167 ? 2.143 1.798 1.584 -0.071 -0.083 -0.147 167 GLU CCC N   
4448  C CA  . GLU C 167 ? 2.150 1.819 1.601 -0.078 -0.098 -0.164 167 GLU CCC CA  
4449  C C   . GLU C 167 ? 2.163 1.827 1.574 -0.049 -0.114 -0.173 167 GLU CCC C   
4450  O O   . GLU C 167 ? 2.189 1.846 1.561 -0.023 -0.104 -0.161 167 GLU CCC O   
4451  C CB  . GLU C 167 ? 2.162 1.852 1.639 -0.092 -0.085 -0.161 167 GLU CCC CB  
4452  C CG  . GLU C 167 ? 2.163 1.852 1.678 -0.118 -0.081 -0.161 167 GLU CCC CG  
4453  C CD  . GLU C 167 ? 2.160 1.870 1.708 -0.131 -0.079 -0.166 167 GLU CCC CD  
4454  O OE1 . GLU C 167 ? 2.152 1.878 1.695 -0.120 -0.083 -0.170 167 GLU CCC OE1 
4455  O OE2 . GLU C 167 ? 2.157 1.864 1.736 -0.149 -0.078 -0.167 167 GLU CCC OE2 
4456  N N   . SER C 168 ? 2.143 1.806 1.561 -0.053 -0.137 -0.193 168 SER CCC N   
4457  C CA  . SER C 168 ? 2.170 1.825 1.557 -0.029 -0.158 -0.207 168 SER CCC CA  
4458  C C   . SER C 168 ? 2.150 1.808 1.553 -0.043 -0.165 -0.219 168 SER CCC C   
4459  O O   . SER C 168 ? 2.121 1.774 1.556 -0.065 -0.169 -0.226 168 SER CCC O   
4460  C CB  . SER C 168 ? 2.203 1.844 1.586 -0.016 -0.186 -0.222 168 SER CCC CB  
4461  O OG  . SER C 168 ? 2.267 1.893 1.611 0.013  -0.210 -0.238 168 SER CCC OG  
4462  N N   . VAL C 169 ? 2.171 1.832 1.549 -0.026 -0.164 -0.220 169 VAL CCC N   
4463  C CA  . VAL C 169 ? 2.147 1.809 1.532 -0.033 -0.167 -0.228 169 VAL CCC CA  
4464  C C   . VAL C 169 ? 2.151 1.793 1.506 -0.011 -0.190 -0.246 169 VAL CCC C   
4465  O O   . VAL C 169 ? 2.186 1.826 1.502 0.019  -0.191 -0.246 169 VAL CCC O   
4466  C CB  . VAL C 169 ? 2.167 1.857 1.559 -0.030 -0.145 -0.216 169 VAL CCC CB  
4467  C CG1 . VAL C 169 ? 2.172 1.861 1.566 -0.030 -0.154 -0.225 169 VAL CCC CG1 
4468  C CG2 . VAL C 169 ? 2.160 1.866 1.587 -0.051 -0.126 -0.202 169 VAL CCC CG2 
4469  N N   . THR C 170 ? 2.119 1.740 1.488 -0.024 -0.205 -0.259 170 THR CCC N   
4470  C CA  . THR C 170 ? 2.172 1.765 1.519 -0.008 -0.229 -0.278 170 THR CCC CA  
4471  C C   . THR C 170 ? 2.196 1.794 1.512 0.012  -0.223 -0.276 170 THR CCC C   
4472  O O   . THR C 170 ? 2.175 1.792 1.506 0.001  -0.206 -0.264 170 THR CCC O   
4473  C CB  . THR C 170 ? 2.164 1.729 1.543 -0.032 -0.240 -0.288 170 THR CCC CB  
4474  O OG1 . THR C 170 ? 2.157 1.714 1.532 -0.041 -0.225 -0.280 170 THR CCC OG1 
4475  C CG2 . THR C 170 ? 2.130 1.700 1.556 -0.056 -0.235 -0.286 170 THR CCC CG2 
4476  N N   . GLU C 171 ? 2.251 1.833 1.528 0.043  -0.239 -0.289 171 GLU CCC N   
4477  C CA  . GLU C 171 ? 2.264 1.847 1.512 0.067  -0.235 -0.291 171 GLU CCC CA  
4478  C C   . GLU C 171 ? 2.215 1.773 1.475 0.051  -0.243 -0.297 171 GLU CCC C   
4479  O O   . GLU C 171 ? 2.183 1.718 1.469 0.024  -0.250 -0.300 171 GLU CCC O   
4480  C CB  . GLU C 171 ? 2.350 1.910 1.544 0.107  -0.252 -0.307 171 GLU CCC CB  
4481  C CG  . GLU C 171 ? 2.388 1.965 1.548 0.134  -0.236 -0.295 171 GLU CCC CG  
4482  C CD  . GLU C 171 ? 2.387 2.011 1.567 0.133  -0.193 -0.270 171 GLU CCC CD  
4483  O OE1 . GLU C 171 ? 2.400 2.038 1.571 0.154  -0.180 -0.269 171 GLU CCC OE1 
4484  O OE2 . GLU C 171 ? 2.384 2.031 1.598 0.110  -0.175 -0.253 171 GLU CCC OE2 
4485  N N   . GLN C 172 ? 2.187 1.748 1.430 0.070  -0.240 -0.298 172 GLN CCC N   
4486  C CA  . GLN C 172 ? 2.175 1.705 1.416 0.062  -0.248 -0.301 172 GLN CCC CA  
4487  C C   . GLN C 172 ? 2.178 1.650 1.412 0.052  -0.268 -0.315 172 GLN CCC C   
4488  O O   . GLN C 172 ? 2.186 1.645 1.406 0.067  -0.286 -0.330 172 GLN CCC O   
4489  C CB  . GLN C 172 ? 2.202 1.740 1.419 0.093  -0.249 -0.305 172 GLN CCC CB  
4490  C CG  . GLN C 172 ? 2.167 1.743 1.412 0.087  -0.236 -0.294 172 GLN CCC CG  
4491  C CD  . GLN C 172 ? 2.198 1.784 1.430 0.120  -0.242 -0.300 172 GLN CCC CD  
4492  O OE1 . GLN C 172 ? 2.251 1.808 1.446 0.147  -0.254 -0.312 172 GLN CCC OE1 
4493  N NE2 . GLN C 172 ? 2.194 1.821 1.460 0.120  -0.237 -0.295 172 GLN CCC NE2 
4494  N N   . ASP C 173 ? 2.170 1.607 1.415 0.030  -0.264 -0.311 173 ASP CCC N   
4495  C CA  . ASP C 173 ? 2.193 1.578 1.456 0.010  -0.274 -0.319 173 ASP CCC CA  
4496  C C   . ASP C 173 ? 2.258 1.593 1.489 0.031  -0.296 -0.336 173 ASP CCC C   
4497  O O   . ASP C 173 ? 2.242 1.569 1.434 0.055  -0.296 -0.334 173 ASP CCC O   
4498  C CB  . ASP C 173 ? 2.190 1.548 1.470 -0.019 -0.252 -0.303 173 ASP CCC CB  
4499  C CG  . ASP C 173 ? 2.233 1.536 1.542 -0.040 -0.253 -0.309 173 ASP CCC CG  
4500  O OD1 . ASP C 173 ? 2.245 1.554 1.593 -0.047 -0.271 -0.325 173 ASP CCC OD1 
4501  O OD2 . ASP C 173 ? 2.277 1.529 1.571 -0.048 -0.236 -0.297 173 ASP CCC OD2 
4502  N N   . SER C 174 ? 2.326 1.629 1.580 0.023  -0.316 -0.354 174 SER CCC N   
4503  C CA  . SER C 174 ? 2.413 1.656 1.650 0.036  -0.343 -0.376 174 SER CCC CA  
4504  C C   . SER C 174 ? 2.478 1.664 1.693 0.032  -0.329 -0.364 174 SER CCC C   
4505  O O   . SER C 174 ? 2.526 1.667 1.704 0.056  -0.347 -0.378 174 SER CCC O   
4506  C CB  . SER C 174 ? 2.417 1.639 1.710 0.014  -0.365 -0.396 174 SER CCC CB  
4507  O OG  . SER C 174 ? 2.331 1.606 1.661 0.003  -0.364 -0.395 174 SER CCC OG  
4508  N N   . LYS C 175 ? 2.485 1.668 1.714 0.007  -0.298 -0.340 175 LYS CCC N   
4509  C CA  . LYS C 175 ? 2.550 1.667 1.754 0.002  -0.279 -0.325 175 LYS CCC CA  
4510  C C   . LYS C 175 ? 2.544 1.680 1.698 0.022  -0.266 -0.307 175 LYS CCC C   
4511  O O   . LYS C 175 ? 2.631 1.735 1.732 0.052  -0.276 -0.310 175 LYS CCC O   
4512  C CB  . LYS C 175 ? 2.572 1.658 1.830 -0.039 -0.252 -0.311 175 LYS CCC CB  
4513  C CG  . LYS C 175 ? 2.595 1.671 1.927 -0.063 -0.269 -0.332 175 LYS CCC CG  
4514  C CD  . LYS C 175 ? 2.598 1.669 2.006 -0.104 -0.239 -0.319 175 LYS CCC CD  
4515  C CE  . LYS C 175 ? 2.601 1.680 2.099 -0.126 -0.265 -0.346 175 LYS CCC CE  
4516  N NZ  . LYS C 175 ? 2.673 1.690 2.172 -0.119 -0.294 -0.369 175 LYS CCC NZ  
4517  N N   . ASP C 176 ? 2.491 1.674 1.661 0.009  -0.248 -0.293 176 ASP CCC N   
4518  C CA  . ASP C 176 ? 2.524 1.710 1.654 0.021  -0.235 -0.278 176 ASP CCC CA  
4519  C C   . ASP C 176 ? 2.455 1.719 1.588 0.040  -0.247 -0.283 176 ASP CCC C   
4520  O O   . ASP C 176 ? 2.428 1.703 1.542 0.049  -0.244 -0.275 176 ASP CCC O   
4521  C CB  . ASP C 176 ? 2.570 1.739 1.712 -0.006 -0.205 -0.258 176 ASP CCC CB  
4522  C CG  . ASP C 176 ? 2.538 1.772 1.731 -0.028 -0.197 -0.258 176 ASP CCC CG  
4523  O OD1 . ASP C 176 ? 2.509 1.804 1.725 -0.021 -0.214 -0.269 176 ASP CCC OD1 
4524  O OD2 . ASP C 176 ? 2.594 1.816 1.800 -0.049 -0.172 -0.244 176 ASP CCC OD2 
4525  N N   . SER C 177 ? 2.424 1.737 1.582 0.047  -0.259 -0.296 177 SER CCC N   
4526  C CA  . SER C 177 ? 2.368 1.753 1.537 0.067  -0.263 -0.299 177 SER CCC CA  
4527  C C   . SER C 177 ? 2.287 1.719 1.487 0.047  -0.249 -0.287 177 SER CCC C   
4528  O O   . SER C 177 ? 2.238 1.716 1.449 0.061  -0.250 -0.287 177 SER CCC O   
4529  C CB  . SER C 177 ? 2.407 1.789 1.543 0.102  -0.275 -0.304 177 SER CCC CB  
4530  O OG  . SER C 177 ? 2.480 1.805 1.579 0.121  -0.289 -0.315 177 SER CCC OG  
4531  N N   . THR C 178 ? 2.275 1.696 1.497 0.017  -0.235 -0.279 178 THR CCC N   
4532  C CA  . THR C 178 ? 2.243 1.702 1.494 -0.003 -0.222 -0.270 178 THR CCC CA  
4533  C C   . THR C 178 ? 2.195 1.694 1.483 -0.015 -0.217 -0.270 178 THR CCC C   
4534  O O   . THR C 178 ? 2.209 1.694 1.498 -0.012 -0.226 -0.279 178 THR CCC O   
4535  C CB  . THR C 178 ? 2.260 1.676 1.502 -0.024 -0.206 -0.259 178 THR CCC CB  
4536  O OG1 . THR C 178 ? 2.253 1.646 1.520 -0.044 -0.197 -0.258 178 THR CCC OG1 
4537  C CG2 . THR C 178 ? 2.319 1.677 1.507 -0.008 -0.208 -0.255 178 THR CCC CG2 
4538  N N   . TYR C 179 ? 2.147 1.689 1.461 -0.025 -0.207 -0.263 179 TYR CCC N   
4539  C CA  . TYR C 179 ? 2.109 1.679 1.451 -0.037 -0.200 -0.259 179 TYR CCC CA  
4540  C C   . TYR C 179 ? 2.083 1.635 1.443 -0.063 -0.189 -0.253 179 TYR CCC C   
4541  O O   . TYR C 179 ? 2.111 1.632 1.456 -0.070 -0.183 -0.249 179 TYR CCC O   
4542  C CB  . TYR C 179 ? 2.095 1.717 1.457 -0.032 -0.191 -0.253 179 TYR CCC CB  
4543  C CG  . TYR C 179 ? 2.128 1.775 1.483 -0.005 -0.194 -0.256 179 TYR CCC CG  
4544  C CD1 . TYR C 179 ? 2.156 1.806 1.492 0.017  -0.194 -0.260 179 TYR CCC CD1 
4545  C CD2 . TYR C 179 ? 2.145 1.811 1.514 0.001  -0.197 -0.258 179 TYR CCC CD2 
4546  C CE1 . TYR C 179 ? 2.180 1.854 1.510 0.045  -0.191 -0.262 179 TYR CCC CE1 
4547  C CE2 . TYR C 179 ? 2.177 1.874 1.552 0.027  -0.197 -0.262 179 TYR CCC CE2 
4548  C CZ  . TYR C 179 ? 2.189 1.890 1.545 0.049  -0.190 -0.262 179 TYR CCC CZ  
4549  O OH  . TYR C 179 ? 2.203 1.935 1.565 0.077  -0.185 -0.265 179 TYR CCC OH  
4550  N N   . SER C 180 ? 2.048 1.616 1.435 -0.073 -0.185 -0.252 180 SER CCC N   
4551  C CA  . SER C 180 ? 2.021 1.587 1.434 -0.095 -0.172 -0.246 180 SER CCC CA  
4552  C C   . SER C 180 ? 2.006 1.607 1.436 -0.095 -0.170 -0.241 180 SER CCC C   
4553  O O   . SER C 180 ? 2.021 1.641 1.440 -0.077 -0.177 -0.243 180 SER CCC O   
4554  C CB  . SER C 180 ? 2.017 1.555 1.453 -0.107 -0.172 -0.251 180 SER CCC CB  
4555  O OG  . SER C 180 ? 2.032 1.529 1.447 -0.106 -0.171 -0.253 180 SER CCC OG  
4556  N N   . LEU C 181 ? 2.000 1.607 1.452 -0.110 -0.158 -0.235 181 LEU CCC N   
4557  C CA  . LEU C 181 ? 1.991 1.624 1.454 -0.109 -0.152 -0.227 181 LEU CCC CA  
4558  C C   . LEU C 181 ? 1.977 1.606 1.467 -0.120 -0.147 -0.226 181 LEU CCC C   
4559  O O   . LEU C 181 ? 1.971 1.583 1.471 -0.133 -0.136 -0.226 181 LEU CCC O   
4560  C CB  . LEU C 181 ? 1.990 1.636 1.452 -0.113 -0.143 -0.220 181 LEU CCC CB  
4561  C CG  . LEU C 181 ? 1.998 1.668 1.473 -0.111 -0.134 -0.209 181 LEU CCC CG  
4562  C CD1 . LEU C 181 ? 1.991 1.681 1.480 -0.113 -0.130 -0.207 181 LEU CCC CD1 
4563  C CD2 . LEU C 181 ? 1.998 1.661 1.487 -0.123 -0.126 -0.204 181 LEU CCC CD2 
4564  N N   . SER C 182 ? 1.984 1.625 1.479 -0.111 -0.153 -0.225 182 SER CCC N   
4565  C CA  . SER C 182 ? 2.001 1.643 1.522 -0.117 -0.150 -0.224 182 SER CCC CA  
4566  C C   . SER C 182 ? 2.026 1.676 1.535 -0.111 -0.140 -0.210 182 SER CCC C   
4567  O O   . SER C 182 ? 2.066 1.720 1.553 -0.092 -0.147 -0.207 182 SER CCC O   
4568  C CB  . SER C 182 ? 2.019 1.663 1.562 -0.107 -0.171 -0.238 182 SER CCC CB  
4569  O OG  . SER C 182 ? 2.031 1.681 1.559 -0.087 -0.182 -0.235 182 SER CCC OG  
4570  N N   . SER C 183 ? 2.041 1.688 1.558 -0.125 -0.125 -0.203 183 SER CCC N   
4571  C CA  . SER C 183 ? 2.064 1.710 1.581 -0.125 -0.114 -0.191 183 SER CCC CA  
4572  C C   . SER C 183 ? 2.052 1.691 1.586 -0.122 -0.116 -0.193 183 SER CCC C   
4573  O O   . SER C 183 ? 2.014 1.647 1.567 -0.133 -0.111 -0.199 183 SER CCC O   
4574  C CB  . SER C 183 ? 2.077 1.719 1.599 -0.140 -0.103 -0.186 183 SER CCC CB  
4575  O OG  . SER C 183 ? 2.111 1.750 1.637 -0.140 -0.092 -0.173 183 SER CCC OG  
4576  N N   . THR C 184 ? 2.076 1.714 1.598 -0.104 -0.123 -0.189 184 THR CCC N   
4577  C CA  . THR C 184 ? 2.087 1.721 1.627 -0.095 -0.130 -0.192 184 THR CCC CA  
4578  C C   . THR C 184 ? 2.093 1.709 1.617 -0.093 -0.115 -0.176 184 THR CCC C   
4579  O O   . THR C 184 ? 2.085 1.692 1.579 -0.086 -0.106 -0.161 184 THR CCC O   
4580  C CB  . THR C 184 ? 2.137 1.776 1.672 -0.070 -0.158 -0.203 184 THR CCC CB  
4581  O OG1 . THR C 184 ? 2.134 1.783 1.680 -0.073 -0.171 -0.218 184 THR CCC OG1 
4582  C CG2 . THR C 184 ? 2.143 1.786 1.714 -0.061 -0.172 -0.214 184 THR CCC CG2 
4583  N N   . LEU C 185 ? 2.095 1.702 1.640 -0.100 -0.108 -0.178 185 LEU CCC N   
4584  C CA  . LEU C 185 ? 2.101 1.683 1.635 -0.098 -0.097 -0.165 185 LEU CCC CA  
4585  C C   . LEU C 185 ? 2.143 1.721 1.681 -0.074 -0.110 -0.169 185 LEU CCC C   
4586  O O   . LEU C 185 ? 2.132 1.725 1.707 -0.074 -0.116 -0.183 185 LEU CCC O   
4587  C CB  . LEU C 185 ? 2.062 1.633 1.611 -0.118 -0.084 -0.170 185 LEU CCC CB  
4588  C CG  . LEU C 185 ? 2.078 1.617 1.620 -0.119 -0.074 -0.161 185 LEU CCC CG  
4589  C CD1 . LEU C 185 ? 2.095 1.622 1.628 -0.130 -0.065 -0.147 185 LEU CCC CD1 
4590  C CD2 . LEU C 185 ? 2.066 1.590 1.616 -0.127 -0.068 -0.173 185 LEU CCC CD2 
4591  N N   . THR C 186 ? 2.192 1.749 1.693 -0.051 -0.113 -0.155 186 THR CCC N   
4592  C CA  . THR C 186 ? 2.229 1.774 1.722 -0.020 -0.132 -0.158 186 THR CCC CA  
4593  C C   . THR C 186 ? 2.241 1.749 1.718 -0.017 -0.115 -0.142 186 THR CCC C   
4594  O O   . THR C 186 ? 2.218 1.702 1.674 -0.031 -0.092 -0.123 186 THR CCC O   
4595  C CB  . THR C 186 ? 2.290 1.828 1.737 0.013  -0.152 -0.156 186 THR CCC CB  
4596  O OG1 . THR C 186 ? 2.264 1.833 1.730 0.009  -0.170 -0.174 186 THR CCC OG1 
4597  C CG2 . THR C 186 ? 2.342 1.866 1.776 0.052  -0.180 -0.163 186 THR CCC CG2 
4598  N N   . LEU C 187 ? 2.264 1.769 1.759 0.000  -0.127 -0.152 187 LEU CCC N   
4599  C CA  . LEU C 187 ? 2.326 1.788 1.801 0.013  -0.117 -0.139 187 LEU CCC CA  
4600  C C   . LEU C 187 ? 2.366 1.836 1.861 0.045  -0.142 -0.154 187 LEU CCC C   
4601  O O   . LEU C 187 ? 2.361 1.876 1.906 0.048  -0.162 -0.176 187 LEU CCC O   
4602  C CB  . LEU C 187 ? 2.296 1.745 1.790 -0.018 -0.094 -0.138 187 LEU CCC CB  
4603  C CG  . LEU C 187 ? 2.263 1.742 1.806 -0.029 -0.094 -0.160 187 LEU CCC CG  
4604  C CD1 . LEU C 187 ? 2.294 1.739 1.835 -0.037 -0.077 -0.160 187 LEU CCC CD1 
4605  C CD2 . LEU C 187 ? 2.215 1.728 1.779 -0.054 -0.090 -0.169 187 LEU CCC CD2 
4606  N N   . SER C 188 ? 2.411 1.837 1.874 0.068  -0.140 -0.142 188 SER CCC N   
4607  C CA  . SER C 188 ? 2.430 1.858 1.910 0.105  -0.165 -0.155 188 SER CCC CA  
4608  C C   . SER C 188 ? 2.387 1.852 1.942 0.089  -0.158 -0.176 188 SER CCC C   
4609  O O   . SER C 188 ? 2.376 1.829 1.934 0.059  -0.129 -0.171 188 SER CCC O   
4610  C CB  . SER C 188 ? 2.500 1.862 1.921 0.131  -0.159 -0.135 188 SER CCC CB  
4611  O OG  . SER C 188 ? 2.478 1.807 1.899 0.104  -0.128 -0.123 188 SER CCC OG  
4612  N N   . LYS C 189 ? 2.386 1.892 1.999 0.111  -0.182 -0.199 189 LYS CCC N   
4613  C CA  . LYS C 189 ? 2.349 1.890 2.038 0.106  -0.169 -0.216 189 LYS CCC CA  
4614  C C   . LYS C 189 ? 2.368 1.858 2.022 0.108  -0.145 -0.204 189 LYS CCC C   
4615  O O   . LYS C 189 ? 2.355 1.848 2.029 0.086  -0.116 -0.207 189 LYS CCC O   
4616  C CB  . LYS C 189 ? 2.359 1.945 2.118 0.139  -0.203 -0.240 189 LYS CCC CB  
4617  C CG  . LYS C 189 ? 2.336 1.961 2.182 0.139  -0.184 -0.256 189 LYS CCC CG  
4618  C CD  . LYS C 189 ? 2.388 1.983 2.222 0.172  -0.182 -0.254 189 LYS CCC CD  
4619  C CE  . LYS C 189 ? 2.373 2.017 2.305 0.179  -0.165 -0.273 189 LYS CCC CE  
4620  N NZ  . LYS C 189 ? 2.370 2.075 2.395 0.208  -0.204 -0.298 189 LYS CCC NZ  
4621  N N   . ALA C 190 ? 2.413 1.852 2.011 0.137  -0.156 -0.190 190 ALA CCC N   
4622  C CA  . ALA C 190 ? 2.469 1.844 2.023 0.140  -0.137 -0.177 190 ALA CCC CA  
4623  C C   . ALA C 190 ? 2.439 1.793 1.978 0.097  -0.106 -0.169 190 ALA CCC C   
4624  O O   . ALA C 190 ? 2.452 1.802 2.010 0.089  -0.089 -0.180 190 ALA CCC O   
4625  C CB  . ALA C 190 ? 2.554 1.867 2.034 0.167  -0.148 -0.155 190 ALA CCC CB  
4626  N N   . ASP C 191 ? 2.406 1.749 1.913 0.073  -0.101 -0.154 191 ASP CCC N   
4627  C CA  . ASP C 191 ? 2.384 1.704 1.878 0.034  -0.079 -0.147 191 ASP CCC CA  
4628  C C   . ASP C 191 ? 2.325 1.691 1.859 0.011  -0.071 -0.166 191 ASP CCC C   
4629  O O   . ASP C 191 ? 2.310 1.653 1.834 -0.011 -0.057 -0.170 191 ASP CCC O   
4630  C CB  . ASP C 191 ? 2.380 1.683 1.841 0.019  -0.074 -0.126 191 ASP CCC CB  
4631  C CG  . ASP C 191 ? 2.451 1.692 1.862 0.039  -0.069 -0.100 191 ASP CCC CG  
4632  O OD1 . ASP C 191 ? 2.477 1.668 1.876 0.048  -0.064 -0.098 191 ASP CCC OD1 
4633  O OD2 . ASP C 191 ? 2.477 1.712 1.854 0.048  -0.068 -0.083 191 ASP CCC OD2 
4634  N N   . TYR C 192 ? 2.305 1.728 1.880 0.017  -0.080 -0.178 192 TYR CCC N   
4635  C CA  . TYR C 192 ? 2.285 1.747 1.897 -0.002 -0.067 -0.192 192 TYR CCC CA  
4636  C C   . TYR C 192 ? 2.343 1.795 1.970 0.007  -0.048 -0.204 192 TYR CCC C   
4637  O O   . TYR C 192 ? 2.360 1.806 1.980 -0.009 -0.029 -0.209 192 TYR CCC O   
4638  C CB  . TYR C 192 ? 2.228 1.748 1.890 0.002  -0.081 -0.202 192 TYR CCC CB  
4639  C CG  . TYR C 192 ? 2.179 1.731 1.881 -0.017 -0.061 -0.213 192 TYR CCC CG  
4640  C CD1 . TYR C 192 ? 2.151 1.699 1.829 -0.043 -0.052 -0.209 192 TYR CCC CD1 
4641  C CD2 . TYR C 192 ? 2.171 1.753 1.935 -0.005 -0.049 -0.225 192 TYR CCC CD2 
4642  C CE1 . TYR C 192 ? 2.129 1.695 1.832 -0.056 -0.031 -0.215 192 TYR CCC CE1 
4643  C CE2 . TYR C 192 ? 2.142 1.746 1.939 -0.021 -0.022 -0.230 192 TYR CCC CE2 
4644  C CZ  . TYR C 192 ? 2.118 1.709 1.878 -0.046 -0.013 -0.224 192 TYR CCC CZ  
4645  O OH  . TYR C 192 ? 2.082 1.683 1.863 -0.057 0.016  -0.226 192 TYR CCC OH  
4646  N N   . GLU C 193 ? 2.415 1.863 2.059 0.037  -0.053 -0.207 193 GLU CCC N   
4647  C CA  . GLU C 193 ? 2.479 1.919 2.139 0.054  -0.033 -0.219 193 GLU CCC CA  
4648  C C   . GLU C 193 ? 2.557 1.925 2.154 0.051  -0.024 -0.215 193 GLU CCC C   
4649  O O   . GLU C 193 ? 2.644 1.995 2.238 0.064  -0.004 -0.226 193 GLU CCC O   
4650  C CB  . GLU C 193 ? 2.519 1.984 2.226 0.091  -0.046 -0.226 193 GLU CCC CB  
4651  C CG  . GLU C 193 ? 2.508 2.047 2.300 0.093  -0.053 -0.238 193 GLU CCC CG  
4652  C CD  . GLU C 193 ? 2.568 2.145 2.434 0.128  -0.057 -0.253 193 GLU CCC CD  
4653  O OE1 . GLU C 193 ? 2.655 2.199 2.496 0.159  -0.069 -0.252 193 GLU CCC OE1 
4654  O OE2 . GLU C 193 ? 2.575 2.213 2.529 0.124  -0.046 -0.265 193 GLU CCC OE2 
4655  N N   . LYS C 194 ? 2.563 1.891 2.118 0.035  -0.036 -0.203 194 LYS CCC N   
4656  C CA  . LYS C 194 ? 2.592 1.849 2.099 0.027  -0.033 -0.202 194 LYS CCC CA  
4657  C C   . LYS C 194 ? 2.542 1.791 2.032 0.004  -0.024 -0.213 194 LYS CCC C   
4658  O O   . LYS C 194 ? 2.589 1.794 2.051 0.013  -0.017 -0.226 194 LYS CCC O   
4659  C CB  . LYS C 194 ? 2.633 1.852 2.115 0.017  -0.045 -0.182 194 LYS CCC CB  
4660  C CG  . LYS C 194 ? 2.702 1.883 2.168 0.049  -0.051 -0.172 194 LYS CCC CG  
4661  C CD  . LYS C 194 ? 2.742 1.898 2.182 0.048  -0.057 -0.146 194 LYS CCC CD  
4662  C CE  . LYS C 194 ? 2.770 1.883 2.195 0.012  -0.047 -0.133 194 LYS CCC CE  
4663  N NZ  . LYS C 194 ? 2.813 1.895 2.211 0.016  -0.041 -0.103 194 LYS CCC NZ  
4664  N N   . HIS C 195 ? 2.452 1.736 1.952 -0.021 -0.027 -0.210 195 HIS CCC N   
4665  C CA  . HIS C 195 ? 2.423 1.700 1.902 -0.040 -0.024 -0.220 195 HIS CCC CA  
4666  C C   . HIS C 195 ? 2.373 1.684 1.863 -0.030 -0.003 -0.228 195 HIS CCC C   
4667  O O   . HIS C 195 ? 2.295 1.651 1.829 -0.019 0.004  -0.224 195 HIS CCC O   
4668  C CB  . HIS C 195 ? 2.401 1.693 1.885 -0.069 -0.037 -0.211 195 HIS CCC CB  
4669  C CG  . HIS C 195 ? 2.424 1.690 1.909 -0.078 -0.045 -0.196 195 HIS CCC CG  
4670  N ND1 . HIS C 195 ? 2.481 1.687 1.950 -0.078 -0.049 -0.199 195 HIS CCC ND1 
4671  C CD2 . HIS C 195 ? 2.401 1.687 1.898 -0.084 -0.048 -0.177 195 HIS CCC CD2 
4672  C CE1 . HIS C 195 ? 2.493 1.682 1.969 -0.088 -0.049 -0.179 195 HIS CCC CE1 
4673  N NE2 . HIS C 195 ? 2.453 1.690 1.941 -0.089 -0.047 -0.165 195 HIS CCC NE2 
4674  N N   . LYS C 196 ? 2.408 1.695 1.860 -0.033 0.006  -0.239 196 LYS CCC N   
4675  C CA  . LYS C 196 ? 2.410 1.717 1.864 -0.020 0.035  -0.243 196 LYS CCC CA  
4676  C C   . LYS C 196 ? 2.374 1.692 1.810 -0.038 0.036  -0.242 196 LYS CCC C   
4677  O O   . LYS C 196 ? 2.354 1.708 1.820 -0.038 0.058  -0.236 196 LYS CCC O   
4678  C CB  . LYS C 196 ? 2.489 1.746 1.896 0.008  0.056  -0.255 196 LYS CCC CB  
4679  C CG  . LYS C 196 ? 2.500 1.784 1.951 0.034  0.087  -0.253 196 LYS CCC CG  
4680  C CD  . LYS C 196 ? 2.563 1.797 1.979 0.065  0.096  -0.263 196 LYS CCC CD  
4681  C CE  . LYS C 196 ? 2.545 1.818 2.027 0.088  0.115  -0.260 196 LYS CCC CE  
4682  N NZ  . LYS C 196 ? 2.626 1.847 2.072 0.120  0.116  -0.271 196 LYS CCC NZ  
4683  N N   . VAL C 197 ? 2.366 1.656 1.765 -0.053 0.011  -0.248 197 VAL CCC N   
4684  C CA  . VAL C 197 ? 2.344 1.638 1.718 -0.064 0.008  -0.249 197 VAL CCC CA  
4685  C C   . VAL C 197 ? 2.291 1.628 1.705 -0.090 -0.013 -0.240 197 VAL CCC C   
4686  O O   . VAL C 197 ? 2.308 1.633 1.723 -0.104 -0.038 -0.243 197 VAL CCC O   
4687  C CB  . VAL C 197 ? 2.392 1.626 1.697 -0.057 -0.010 -0.267 197 VAL CCC CB  
4688  C CG1 . VAL C 197 ? 2.379 1.616 1.657 -0.064 -0.020 -0.270 197 VAL CCC CG1 
4689  C CG2 . VAL C 197 ? 2.473 1.657 1.722 -0.024 0.013  -0.277 197 VAL CCC CG2 
4690  N N   . TYR C 198 ? 2.243 1.624 1.688 -0.096 -0.002 -0.230 198 TYR CCC N   
4691  C CA  . TYR C 198 ? 2.175 1.596 1.651 -0.115 -0.019 -0.222 198 TYR CCC CA  
4692  C C   . TYR C 198 ? 2.158 1.577 1.607 -0.121 -0.021 -0.225 198 TYR CCC C   
4693  O O   . TYR C 198 ? 2.170 1.584 1.607 -0.113 0.001  -0.224 198 TYR CCC O   
4694  C CB  . TYR C 198 ? 2.137 1.602 1.665 -0.113 -0.012 -0.214 198 TYR CCC CB  
4695  C CG  . TYR C 198 ? 2.148 1.615 1.698 -0.102 -0.018 -0.211 198 TYR CCC CG  
4696  C CD1 . TYR C 198 ? 2.189 1.647 1.750 -0.084 -0.002 -0.215 198 TYR CCC CD1 
4697  C CD2 . TYR C 198 ? 2.145 1.618 1.699 -0.107 -0.037 -0.202 198 TYR CCC CD2 
4698  C CE1 . TYR C 198 ? 2.219 1.673 1.794 -0.071 -0.011 -0.212 198 TYR CCC CE1 
4699  C CE2 . TYR C 198 ? 2.183 1.645 1.743 -0.094 -0.041 -0.197 198 TYR CCC CE2 
4700  C CZ  . TYR C 198 ? 2.221 1.673 1.791 -0.075 -0.031 -0.203 198 TYR CCC CZ  
4701  O OH  . TYR C 198 ? 2.272 1.710 1.845 -0.058 -0.038 -0.198 198 TYR CCC OH  
4702  N N   . ALA C 199 ? 2.131 1.553 1.575 -0.134 -0.045 -0.227 199 ALA CCC N   
4703  C CA  . ALA C 199 ? 2.150 1.563 1.561 -0.135 -0.055 -0.234 199 ALA CCC CA  
4704  C C   . ALA C 199 ? 2.105 1.556 1.546 -0.150 -0.072 -0.229 199 ALA CCC C   
4705  O O   . ALA C 199 ? 2.038 1.512 1.515 -0.159 -0.076 -0.221 199 ALA CCC O   
4706  C CB  . ALA C 199 ? 2.220 1.587 1.587 -0.128 -0.072 -0.251 199 ALA CCC CB  
4707  N N   . CYS C 200 ? 2.151 1.603 1.571 -0.149 -0.078 -0.232 200 CYS CCC N   
4708  C CA  . CYS C 200 ? 2.139 1.626 1.581 -0.157 -0.090 -0.228 200 CYS CCC CA  
4709  C C   . CYS C 200 ? 2.137 1.608 1.548 -0.153 -0.111 -0.241 200 CYS CCC C   
4710  O O   . CYS C 200 ? 2.125 1.575 1.494 -0.141 -0.107 -0.242 200 CYS CCC O   
4711  C CB  . CYS C 200 ? 2.167 1.673 1.619 -0.156 -0.075 -0.219 200 CYS CCC CB  
4712  S SG  . CYS C 200 ? 2.214 1.761 1.691 -0.162 -0.089 -0.214 200 CYS CCC SG  
4713  N N   . GLU C 201 ? 2.135 1.615 1.571 -0.161 -0.134 -0.250 201 GLU CCC N   
4714  C CA  . GLU C 201 ? 2.174 1.647 1.598 -0.155 -0.164 -0.268 201 GLU CCC CA  
4715  C C   . GLU C 201 ? 2.135 1.650 1.588 -0.159 -0.170 -0.263 201 GLU CCC C   
4716  O O   . GLU C 201 ? 2.136 1.690 1.642 -0.172 -0.161 -0.251 201 GLU CCC O   
4717  C CB  . GLU C 201 ? 2.206 1.671 1.663 -0.165 -0.186 -0.283 201 GLU CCC CB  
4718  C CG  . GLU C 201 ? 2.254 1.698 1.694 -0.154 -0.226 -0.311 201 GLU CCC CG  
4719  C CD  . GLU C 201 ? 2.275 1.720 1.772 -0.168 -0.254 -0.330 201 GLU CCC CD  
4720  O OE1 . GLU C 201 ? 2.240 1.726 1.817 -0.192 -0.244 -0.318 201 GLU CCC OE1 
4721  O OE2 . GLU C 201 ? 2.326 1.726 1.788 -0.155 -0.285 -0.356 201 GLU CCC OE2 
4722  N N   . VAL C 202 ? 2.134 1.637 1.548 -0.144 -0.182 -0.270 202 VAL CCC N   
4723  C CA  . VAL C 202 ? 2.087 1.625 1.517 -0.141 -0.186 -0.266 202 VAL CCC CA  
4724  C C   . VAL C 202 ? 2.128 1.666 1.555 -0.128 -0.221 -0.286 202 VAL CCC C   
4725  O O   . VAL C 202 ? 2.203 1.694 1.562 -0.107 -0.235 -0.297 202 VAL CCC O   
4726  C CB  . VAL C 202 ? 2.073 1.591 1.460 -0.132 -0.166 -0.254 202 VAL CCC CB  
4727  C CG1 . VAL C 202 ? 2.060 1.604 1.456 -0.126 -0.173 -0.253 202 VAL CCC CG1 
4728  C CG2 . VAL C 202 ? 2.037 1.561 1.440 -0.143 -0.138 -0.239 202 VAL CCC CG2 
4729  N N   . THR C 203 ? 2.108 1.695 1.605 -0.138 -0.234 -0.291 203 THR CCC N   
4730  C CA  . THR C 203 ? 2.151 1.754 1.670 -0.126 -0.271 -0.313 203 THR CCC CA  
4731  C C   . THR C 203 ? 2.154 1.792 1.684 -0.117 -0.265 -0.304 203 THR CCC C   
4732  O O   . THR C 203 ? 2.135 1.825 1.733 -0.129 -0.250 -0.295 203 THR CCC O   
4733  C CB  . THR C 203 ? 2.139 1.777 1.748 -0.144 -0.288 -0.326 203 THR CCC CB  
4734  O OG1 . THR C 203 ? 2.176 1.769 1.761 -0.145 -0.306 -0.342 203 THR CCC OG1 
4735  C CG2 . THR C 203 ? 2.142 1.820 1.809 -0.136 -0.322 -0.347 203 THR CCC CG2 
4736  N N   . HIS C 204 ? 2.214 1.820 1.675 -0.094 -0.272 -0.306 204 HIS CCC N   
4737  C CA  . HIS C 204 ? 2.226 1.853 1.686 -0.080 -0.273 -0.303 204 HIS CCC CA  
4738  C C   . HIS C 204 ? 2.278 1.899 1.724 -0.054 -0.314 -0.326 204 HIS CCC C   
4739  O O   . HIS C 204 ? 2.325 1.896 1.714 -0.038 -0.338 -0.340 204 HIS CCC O   
4740  C CB  . HIS C 204 ? 2.248 1.838 1.644 -0.074 -0.248 -0.286 204 HIS CCC CB  
4741  C CG  . HIS C 204 ? 2.248 1.855 1.644 -0.061 -0.248 -0.283 204 HIS CCC CG  
4742  N ND1 . HIS C 204 ? 2.294 1.856 1.624 -0.040 -0.254 -0.283 204 HIS CCC ND1 
4743  C CD2 . HIS C 204 ? 2.218 1.880 1.669 -0.063 -0.243 -0.280 204 HIS CCC CD2 
4744  C CE1 . HIS C 204 ? 2.294 1.883 1.641 -0.030 -0.255 -0.282 204 HIS CCC CE1 
4745  N NE2 . HIS C 204 ? 2.255 1.906 1.673 -0.042 -0.248 -0.281 204 HIS CCC NE2 
4746  N N   . GLN C 205 ? 2.278 1.946 1.769 -0.044 -0.322 -0.330 205 GLN CCC N   
4747  C CA  . GLN C 205 ? 2.345 2.019 1.837 -0.015 -0.365 -0.353 205 GLN CCC CA  
4748  C C   . GLN C 205 ? 2.438 2.031 1.812 0.016  -0.382 -0.357 205 GLN CCC C   
4749  O O   . GLN C 205 ? 2.503 2.076 1.853 0.043  -0.426 -0.382 205 GLN CCC O   
4750  C CB  . GLN C 205 ? 2.318 2.046 1.858 -0.006 -0.358 -0.350 205 GLN CCC CB  
4751  C CG  . GLN C 205 ? 2.363 2.113 1.929 0.024  -0.404 -0.377 205 GLN CCC CG  
4752  C CD  . GLN C 205 ? 2.398 2.133 1.913 0.055  -0.405 -0.373 205 GLN CCC CD  
4753  O OE1 . GLN C 205 ? 2.376 2.125 1.892 0.049  -0.371 -0.354 205 GLN CCC OE1 
4754  N NE2 . GLN C 205 ? 2.471 2.170 1.933 0.091  -0.448 -0.392 205 GLN CCC NE2 
4755  N N   . GLY C 206 ? 2.464 2.011 1.770 0.013  -0.347 -0.334 206 GLY CCC N   
4756  C CA  . GLY C 206 ? 2.553 2.013 1.745 0.039  -0.347 -0.329 206 GLY CCC CA  
4757  C C   . GLY C 206 ? 2.616 2.022 1.750 0.048  -0.360 -0.339 206 GLY CCC C   
4758  O O   . GLY C 206 ? 2.725 2.070 1.772 0.085  -0.385 -0.349 206 GLY CCC O   
4759  N N   . LEU C 207 ? 2.581 2.005 1.754 0.021  -0.346 -0.337 207 LEU CCC N   
4760  C CA  . LEU C 207 ? 2.649 2.015 1.760 0.030  -0.350 -0.345 207 LEU CCC CA  
4761  C C   . LEU C 207 ? 2.666 2.051 1.814 0.039  -0.404 -0.378 207 LEU CCC C   
4762  O O   . LEU C 207 ? 2.586 2.036 1.840 0.009  -0.408 -0.385 207 LEU CCC O   
4763  C CB  . LEU C 207 ? 2.626 1.998 1.762 -0.002 -0.307 -0.325 207 LEU CCC CB  
4764  C CG  . LEU C 207 ? 2.652 1.991 1.746 -0.007 -0.258 -0.297 207 LEU CCC CG  
4765  C CD1 . LEU C 207 ? 2.585 1.961 1.741 -0.041 -0.223 -0.282 207 LEU CCC CD1 
4766  C CD2 . LEU C 207 ? 2.762 2.010 1.742 0.022  -0.245 -0.292 207 LEU CCC CD2 
4767  N N   . SER C 208 ? 2.760 2.083 1.822 0.080  -0.444 -0.400 208 SER CCC N   
4768  C CA  . SER C 208 ? 2.790 2.113 1.870 0.096  -0.506 -0.439 208 SER CCC CA  
4769  C C   . SER C 208 ? 2.732 2.073 1.871 0.063  -0.498 -0.444 208 SER CCC C   
4770  O O   . SER C 208 ? 2.636 2.052 1.902 0.032  -0.509 -0.454 208 SER CCC O   
4771  C CB  . SER C 208 ? 2.916 2.143 1.855 0.150  -0.539 -0.456 208 SER CCC CB  
4772  O OG  . SER C 208 ? 2.964 2.113 1.790 0.159  -0.487 -0.427 208 SER CCC OG  
4773  N N   . SER C 209 ? 2.760 2.032 1.810 0.071  -0.473 -0.435 209 SER CCC N   
4774  C CA  . SER C 209 ? 2.715 1.989 1.800 0.045  -0.460 -0.437 209 SER CCC CA  
4775  C C   . SER C 209 ? 2.600 1.907 1.726 0.008  -0.395 -0.399 209 SER CCC C   
4776  O O   . SER C 209 ? 2.599 1.881 1.668 0.014  -0.354 -0.373 209 SER CCC O   
4777  C CB  . SER C 209 ? 2.838 2.019 1.802 0.080  -0.471 -0.450 209 SER CCC CB  
4778  O OG  . SER C 209 ? 2.841 2.023 1.847 0.061  -0.482 -0.466 209 SER CCC OG  
4779  N N   . PRO C 210 ? 2.498 1.859 1.726 -0.030 -0.384 -0.396 210 PRO CCC N   
4780  C CA  . PRO C 210 ? 2.405 1.794 1.668 -0.059 -0.329 -0.363 210 PRO CCC CA  
4781  C C   . PRO C 210 ? 2.429 1.761 1.605 -0.048 -0.289 -0.345 210 PRO CCC C   
4782  O O   . PRO C 210 ? 2.520 1.788 1.619 -0.024 -0.299 -0.357 210 PRO CCC O   
4783  C CB  . PRO C 210 ? 2.363 1.784 1.712 -0.089 -0.333 -0.370 210 PRO CCC CB  
4784  C CG  . PRO C 210 ? 2.397 1.843 1.807 -0.087 -0.386 -0.401 210 PRO CCC CG  
4785  C CD  . PRO C 210 ? 2.488 1.882 1.805 -0.045 -0.425 -0.424 210 PRO CCC CD  
4786  N N   . VAL C 211 ? 2.372 1.726 1.567 -0.064 -0.245 -0.317 211 VAL CCC N   
4787  C CA  . VAL C 211 ? 2.402 1.716 1.541 -0.058 -0.200 -0.296 211 VAL CCC CA  
4788  C C   . VAL C 211 ? 2.382 1.724 1.578 -0.083 -0.173 -0.285 211 VAL CCC C   
4789  O O   . VAL C 211 ? 2.360 1.757 1.627 -0.105 -0.166 -0.274 211 VAL CCC O   
4790  C CB  . VAL C 211 ? 2.362 1.676 1.486 -0.056 -0.175 -0.277 211 VAL CCC CB  
4791  C CG1 . VAL C 211 ? 2.331 1.629 1.449 -0.063 -0.125 -0.255 211 VAL CCC CG1 
4792  C CG2 . VAL C 211 ? 2.459 1.721 1.499 -0.023 -0.194 -0.284 211 VAL CCC CG2 
4793  N N   . THR C 212 ? 2.438 1.738 1.595 -0.073 -0.157 -0.286 212 THR CCC N   
4794  C CA  . THR C 212 ? 2.388 1.706 1.589 -0.090 -0.129 -0.275 212 THR CCC CA  
4795  C C   . THR C 212 ? 2.400 1.694 1.570 -0.081 -0.083 -0.256 212 THR CCC C   
4796  O O   . THR C 212 ? 2.469 1.704 1.559 -0.055 -0.069 -0.257 212 THR CCC O   
4797  C CB  . THR C 212 ? 2.424 1.716 1.617 -0.086 -0.147 -0.292 212 THR CCC CB  
4798  O OG1 . THR C 212 ? 2.430 1.738 1.656 -0.093 -0.192 -0.312 212 THR CCC OG1 
4799  C CG2 . THR C 212 ? 2.370 1.686 1.616 -0.103 -0.125 -0.281 212 THR CCC CG2 
4800  N N   . LYS C 213 ? 2.349 1.686 1.583 -0.100 -0.059 -0.241 213 LYS CCC N   
4801  C CA  . LYS C 213 ? 2.388 1.718 1.629 -0.098 -0.014 -0.226 213 LYS CCC CA  
4802  C C   . LYS C 213 ? 2.332 1.692 1.630 -0.108 -0.008 -0.225 213 LYS CCC C   
4803  O O   . LYS C 213 ? 2.301 1.703 1.649 -0.124 -0.030 -0.226 213 LYS CCC O   
4804  C CB  . LYS C 213 ? 2.415 1.768 1.688 -0.109 -0.001 -0.213 213 LYS CCC CB  
4805  C CG  . LYS C 213 ? 2.528 1.837 1.735 -0.094 0.003  -0.210 213 LYS CCC CG  
4806  C CD  . LYS C 213 ? 2.616 1.882 1.794 -0.084 0.054  -0.193 213 LYS CCC CD  
4807  C CE  . LYS C 213 ? 2.594 1.894 1.851 -0.105 0.079  -0.181 213 LYS CCC CE  
4808  N NZ  . LYS C 213 ? 2.677 1.928 1.902 -0.098 0.122  -0.163 213 LYS CCC NZ  
4809  N N   . SER C 214 ? 2.361 1.698 1.648 -0.096 0.023  -0.221 214 SER CCC N   
4810  C CA  . SER C 214 ? 2.358 1.710 1.683 -0.097 0.027  -0.223 214 SER CCC CA  
4811  C C   . SER C 214 ? 2.378 1.726 1.719 -0.086 0.073  -0.214 214 SER CCC C   
4812  O O   . SER C 214 ? 2.411 1.730 1.719 -0.076 0.106  -0.206 214 SER CCC O   
4813  C CB  . SER C 214 ? 2.414 1.729 1.694 -0.087 0.003  -0.239 214 SER CCC CB  
4814  O OG  . SER C 214 ? 2.506 1.762 1.712 -0.060 0.024  -0.244 214 SER CCC OG  
4815  N N   . PHE C 215 ? 2.379 1.752 1.771 -0.087 0.077  -0.215 215 PHE CCC N   
4816  C CA  . PHE C 215 ? 2.436 1.809 1.854 -0.073 0.117  -0.210 215 PHE CCC CA  
4817  C C   . PHE C 215 ? 2.465 1.829 1.881 -0.061 0.106  -0.219 215 PHE CCC C   
4818  O O   . PHE C 215 ? 2.421 1.804 1.862 -0.073 0.072  -0.223 215 PHE CCC O   
4819  C CB  . PHE C 215 ? 2.397 1.828 1.912 -0.086 0.132  -0.202 215 PHE CCC CB  
4820  C CG  . PHE C 215 ? 2.337 1.816 1.913 -0.098 0.096  -0.207 215 PHE CCC CG  
4821  C CD1 . PHE C 215 ? 2.295 1.794 1.874 -0.114 0.062  -0.208 215 PHE CCC CD1 
4822  C CD2 . PHE C 215 ? 2.335 1.837 1.959 -0.088 0.096  -0.211 215 PHE CCC CD2 
4823  C CE1 . PHE C 215 ? 2.264 1.797 1.882 -0.118 0.032  -0.210 215 PHE CCC CE1 
4824  C CE2 . PHE C 215 ? 2.295 1.830 1.958 -0.092 0.062  -0.214 215 PHE CCC CE2 
4825  C CZ  . PHE C 215 ? 2.260 1.808 1.917 -0.106 0.032  -0.213 215 PHE CCC CZ  
4826  N N   . ASN C 216 ? 2.560 1.888 1.943 -0.037 0.138  -0.221 216 ASN CCC N   
4827  C CA  . ASN C 216 ? 2.617 1.942 2.015 -0.022 0.139  -0.228 216 ASN CCC CA  
4828  C C   . ASN C 216 ? 2.596 1.985 2.098 -0.026 0.155  -0.220 216 ASN CCC C   
4829  O O   . ASN C 216 ? 2.614 2.033 2.162 -0.035 0.181  -0.211 216 ASN CCC O   
4830  C CB  . ASN C 216 ? 2.725 1.987 2.047 0.011  0.167  -0.234 216 ASN CCC CB  
4831  C CG  . ASN C 216 ? 2.806 2.002 2.023 0.020  0.144  -0.246 216 ASN CCC CG  
4832  O OD1 . ASN C 216 ? 2.796 1.991 1.992 0.007  0.131  -0.243 216 ASN CCC OD1 
4833  N ND2 . ASN C 216 ? 2.901 2.040 2.053 0.044  0.133  -0.262 216 ASN CCC ND2 
4834  N N   . ARG C 217 ? 2.586 1.992 2.125 -0.020 0.137  -0.225 217 ARG CCC N   
4835  C CA  . ARG C 217 ? 2.539 2.006 2.177 -0.020 0.138  -0.224 217 ARG CCC CA  
4836  C C   . ARG C 217 ? 2.607 2.089 2.292 -0.001 0.189  -0.222 217 ARG CCC C   
4837  O O   . ARG C 217 ? 2.672 2.108 2.299 0.021  0.219  -0.223 217 ARG CCC O   
4838  C CB  . ARG C 217 ? 2.507 1.974 2.152 -0.011 0.104  -0.229 217 ARG CCC CB  
4839  C CG  . ARG C 217 ? 2.453 1.979 2.185 -0.010 0.086  -0.230 217 ARG CCC CG  
4840  C CD  . ARG C 217 ? 2.433 1.949 2.146 -0.008 0.045  -0.229 217 ARG CCC CD  
4841  N NE  . ARG C 217 ? 2.472 1.934 2.131 0.007  0.045  -0.231 217 ARG CCC NE  
4842  C CZ  . ARG C 217 ? 2.490 1.947 2.166 0.034  0.049  -0.236 217 ARG CCC CZ  
4843  N NH1 . ARG C 217 ? 2.465 1.974 2.220 0.050  0.053  -0.240 217 ARG CCC NH1 
4844  N NH2 . ARG C 217 ? 2.538 1.935 2.157 0.046  0.047  -0.238 217 ARG CCC NH2 
4845  N N   . GLY C 218 ? 2.623 2.168 2.412 -0.009 0.199  -0.221 218 GLY CCC N   
4846  C CA  . GLY C 218 ? 2.690 2.265 2.557 0.003  0.251  -0.218 218 GLY CCC CA  
4847  C C   . GLY C 218 ? 2.754 2.324 2.628 -0.013 0.294  -0.205 218 GLY CCC C   
4848  O O   . GLY C 218 ? 2.839 2.428 2.777 -0.005 0.350  -0.198 218 GLY CCC O   
4849  N N   . GLU C 219 ? 2.729 2.276 2.546 -0.034 0.272  -0.201 219 GLU CCC N   
4850  C CA  . GLU C 219 ? 2.706 2.231 2.503 -0.046 0.309  -0.187 219 GLU CCC CA  
4851  C C   . GLU C 219 ? 2.591 2.133 2.397 -0.074 0.264  -0.189 219 GLU CCC C   
4852  O O   . GLU C 219 ? 2.541 2.081 2.363 -0.090 0.283  -0.180 219 GLU CCC O   
4853  C CB  . GLU C 219 ? 2.789 2.232 2.450 -0.025 0.335  -0.179 219 GLU CCC CB  
4854  C CG  . GLU C 219 ? 2.855 2.270 2.491 0.009  0.386  -0.177 219 GLU CCC CG  
4855  C CD  . GLU C 219 ? 2.859 2.250 2.442 0.030  0.354  -0.192 219 GLU CCC CD  
4856  O OE1 . GLU C 219 ? 2.859 2.210 2.357 0.028  0.308  -0.201 219 GLU CCC OE1 
4857  O OE2 . GLU C 219 ? 2.846 2.259 2.480 0.050  0.374  -0.196 219 GLU CCC OE2 
4858  N N   . GLN D 1   ? 3.412 3.919 2.395 -0.256 0.064  -0.408 1   GLN DDD N   
4859  C CA  . GLN D 1   ? 3.412 3.920 2.384 -0.268 0.048  -0.415 1   GLN DDD CA  
4860  C C   . GLN D 1   ? 3.435 3.957 2.371 -0.278 0.034  -0.425 1   GLN DDD C   
4861  O O   . GLN D 1   ? 3.436 3.968 2.371 -0.278 0.030  -0.432 1   GLN DDD O   
4862  C CB  . GLN D 1   ? 3.391 3.894 2.402 -0.274 0.038  -0.424 1   GLN DDD CB  
4863  C CG  . GLN D 1   ? 3.381 3.879 2.380 -0.281 0.025  -0.428 1   GLN DDD CG  
4864  C CD  . GLN D 1   ? 3.371 3.866 2.401 -0.283 0.009  -0.442 1   GLN DDD CD  
4865  O OE1 . GLN D 1   ? 3.368 3.865 2.377 -0.286 -0.009 -0.453 1   GLN DDD OE1 
4866  N NE2 . GLN D 1   ? 3.361 3.851 2.444 -0.278 0.015  -0.444 1   GLN DDD NE2 
4867  N N   . VAL D 2   ? 3.467 3.987 2.377 -0.285 0.028  -0.428 2   VAL DDD N   
4868  C CA  . VAL D 2   ? 3.487 4.014 2.366 -0.295 0.019  -0.438 2   VAL DDD CA  
4869  C C   . VAL D 2   ? 3.493 4.013 2.375 -0.302 0.007  -0.447 2   VAL DDD C   
4870  O O   . VAL D 2   ? 3.494 4.001 2.388 -0.301 0.001  -0.446 2   VAL DDD O   
4871  C CB  . VAL D 2   ? 3.504 4.027 2.359 -0.299 0.021  -0.438 2   VAL DDD CB  
4872  C CG1 . VAL D 2   ? 3.517 4.043 2.347 -0.311 0.017  -0.449 2   VAL DDD CG1 
4873  C CG2 . VAL D 2   ? 3.505 4.034 2.352 -0.289 0.029  -0.432 2   VAL DDD CG2 
4874  N N   . GLN D 3   ? 3.502 4.029 2.372 -0.307 0.003  -0.455 3   GLN DDD N   
4875  C CA  . GLN D 3   ? 3.526 4.044 2.389 -0.310 -0.008 -0.464 3   GLN DDD CA  
4876  C C   . GLN D 3   ? 3.554 4.070 2.382 -0.318 -0.005 -0.471 3   GLN DDD C   
4877  O O   . GLN D 3   ? 3.540 4.072 2.368 -0.321 0.002  -0.474 3   GLN DDD O   
4878  C CB  . GLN D 3   ? 3.518 4.043 2.410 -0.304 -0.014 -0.468 3   GLN DDD CB  
4879  C CG  . GLN D 3   ? 3.515 4.032 2.444 -0.297 -0.021 -0.468 3   GLN DDD CG  
4880  C CD  . GLN D 3   ? 3.502 4.029 2.475 -0.292 -0.012 -0.464 3   GLN DDD CD  
4881  O OE1 . GLN D 3   ? 3.498 4.033 2.469 -0.290 0.002  -0.455 3   GLN DDD OE1 
4882  N NE2 . GLN D 3   ? 3.495 4.019 2.511 -0.287 -0.019 -0.471 3   GLN DDD NE2 
4883  N N   . LEU D 4   ? 3.602 4.097 2.403 -0.320 -0.008 -0.474 4   LEU DDD N   
4884  C CA  . LEU D 4   ? 3.646 4.129 2.413 -0.327 0.000  -0.480 4   LEU DDD CA  
4885  C C   . LEU D 4   ? 3.686 4.157 2.443 -0.321 -0.009 -0.486 4   LEU DDD C   
4886  O O   . LEU D 4   ? 3.698 4.161 2.463 -0.311 -0.024 -0.487 4   LEU DDD O   
4887  C CB  . LEU D 4   ? 3.667 4.127 2.405 -0.329 0.006  -0.477 4   LEU DDD CB  
4888  C CG  . LEU D 4   ? 3.653 4.122 2.403 -0.333 0.011  -0.471 4   LEU DDD CG  
4889  C CD1 . LEU D 4   ? 3.681 4.127 2.400 -0.337 0.019  -0.470 4   LEU DDD CD1 
4890  C CD2 . LEU D 4   ? 3.630 4.126 2.397 -0.337 0.019  -0.474 4   LEU DDD CD2 
4891  N N   . VAL D 5   ? 3.719 4.192 2.463 -0.326 -0.001 -0.492 5   VAL DDD N   
4892  C CA  . VAL D 5   ? 3.753 4.213 2.481 -0.319 -0.008 -0.498 5   VAL DDD CA  
4893  C C   . VAL D 5   ? 3.816 4.253 2.505 -0.324 0.010  -0.501 5   VAL DDD C   
4894  O O   . VAL D 5   ? 3.805 4.257 2.503 -0.334 0.023  -0.506 5   VAL DDD O   
4895  C CB  . VAL D 5   ? 3.711 4.198 2.473 -0.318 -0.014 -0.501 5   VAL DDD CB  
4896  C CG1 . VAL D 5   ? 3.723 4.196 2.468 -0.311 -0.022 -0.508 5   VAL DDD CG1 
4897  C CG2 . VAL D 5   ? 3.681 4.185 2.484 -0.313 -0.025 -0.497 5   VAL DDD CG2 
4898  N N   . GLU D 6   ? 3.899 4.299 2.545 -0.315 0.010  -0.500 6   GLU DDD N   
4899  C CA  . GLU D 6   ? 3.976 4.342 2.576 -0.315 0.032  -0.502 6   GLU DDD CA  
4900  C C   . GLU D 6   ? 3.984 4.347 2.576 -0.309 0.029  -0.508 6   GLU DDD C   
4901  O O   . GLU D 6   ? 3.981 4.361 2.595 -0.301 0.006  -0.511 6   GLU DDD O   
4902  C CB  . GLU D 6   ? 4.054 4.375 2.603 -0.301 0.032  -0.498 6   GLU DDD CB  
4903  C CG  . GLU D 6   ? 4.075 4.394 2.626 -0.307 0.038  -0.492 6   GLU DDD CG  
4904  C CD  . GLU D 6   ? 4.075 4.410 2.652 -0.300 0.012  -0.489 6   GLU DDD CD  
4905  O OE1 . GLU D 6   ? 4.061 4.422 2.675 -0.297 -0.006 -0.493 6   GLU DDD OE1 
4906  O OE2 . GLU D 6   ? 4.113 4.432 2.676 -0.297 0.013  -0.485 6   GLU DDD OE2 
4907  N N   . SER D 7   ? 3.991 4.333 2.556 -0.314 0.054  -0.510 7   SER DDD N   
4908  C CA  . SER D 7   ? 3.985 4.311 2.527 -0.306 0.057  -0.514 7   SER DDD CA  
4909  C C   . SER D 7   ? 4.006 4.296 2.512 -0.312 0.094  -0.514 7   SER DDD C   
4910  O O   . SER D 7   ? 3.999 4.286 2.512 -0.325 0.115  -0.513 7   SER DDD O   
4911  C CB  . SER D 7   ? 3.938 4.308 2.528 -0.315 0.047  -0.520 7   SER DDD CB  
4912  O OG  . SER D 7   ? 3.907 4.310 2.536 -0.334 0.059  -0.523 7   SER DDD OG  
4913  N N   . GLY D 8   ? 4.025 4.287 2.496 -0.301 0.102  -0.516 8   GLY DDD N   
4914  C CA  . GLY D 8   ? 4.068 4.288 2.503 -0.304 0.142  -0.515 8   GLY DDD CA  
4915  C C   . GLY D 8   ? 4.132 4.287 2.492 -0.280 0.153  -0.507 8   GLY DDD C   
4916  O O   . GLY D 8   ? 4.192 4.302 2.516 -0.280 0.192  -0.504 8   GLY DDD O   
4917  N N   . GLY D 9   ? 4.122 4.269 2.459 -0.260 0.121  -0.504 9   GLY DDD N   
4918  C CA  . GLY D 9   ? 4.181 4.265 2.439 -0.229 0.122  -0.498 9   GLY DDD CA  
4919  C C   . GLY D 9   ? 4.218 4.266 2.424 -0.205 0.122  -0.500 9   GLY DDD C   
4920  O O   . GLY D 9   ? 4.169 4.252 2.410 -0.210 0.105  -0.508 9   GLY DDD O   
4921  N N   . GLY D 10  ? 4.296 4.274 2.419 -0.178 0.142  -0.494 10  GLY DDD N   
4922  C CA  . GLY D 10  ? 4.358 4.289 2.416 -0.148 0.143  -0.495 10  GLY DDD CA  
4923  C C   . GLY D 10  ? 4.452 4.298 2.417 -0.125 0.185  -0.484 10  GLY DDD C   
4924  O O   . GLY D 10  ? 4.478 4.296 2.416 -0.120 0.196  -0.476 10  GLY DDD O   
4925  N N   . LEU D 11  ? 4.501 4.306 2.420 -0.112 0.209  -0.482 11  LEU DDD N   
4926  C CA  . LEU D 11  ? 4.616 4.327 2.429 -0.078 0.247  -0.471 11  LEU DDD CA  
4927  C C   . LEU D 11  ? 4.645 4.332 2.470 -0.105 0.314  -0.463 11  LEU DDD C   
4928  O O   . LEU D 11  ? 4.589 4.327 2.488 -0.139 0.322  -0.470 11  LEU DDD O   
4929  C CB  . LEU D 11  ? 4.652 4.339 2.414 -0.044 0.226  -0.476 11  LEU DDD CB  
4930  C CG  . LEU D 11  ? 4.765 4.362 2.404 0.013  0.228  -0.471 11  LEU DDD CG  
4931  C CD1 . LEU D 11  ? 4.770 4.368 2.386 0.040  0.182  -0.477 11  LEU DDD CD1 
4932  C CD2 . LEU D 11  ? 4.801 4.383 2.402 0.041  0.211  -0.479 11  LEU DDD CD2 
4933  N N   . MET D 12  ? 4.740 4.353 2.499 -0.091 0.361  -0.450 12  MET DDD N   
4934  C CA  . MET D 12  ? 4.771 4.354 2.544 -0.116 0.431  -0.444 12  MET DDD CA  
4935  C C   . MET D 12  ? 4.879 4.355 2.546 -0.083 0.482  -0.428 12  MET DDD C   
4936  O O   . MET D 12  ? 4.909 4.362 2.543 -0.070 0.477  -0.421 12  MET DDD O   
4937  C CB  . MET D 12  ? 4.710 4.353 2.580 -0.162 0.440  -0.450 12  MET DDD CB  
4938  C CG  . MET D 12  ? 4.628 4.350 2.602 -0.202 0.433  -0.465 12  MET DDD CG  
4939  S SD  . MET D 12  ? 4.674 4.367 2.636 -0.202 0.472  -0.467 12  MET DDD SD  
4940  C CE  . MET D 12  ? 4.746 4.369 2.695 -0.213 0.559  -0.461 12  MET DDD CE  
4941  N N   . GLN D 13  ? 4.931 4.344 2.549 -0.071 0.532  -0.421 13  GLN DDD N   
4942  C CA  . GLN D 13  ? 5.037 4.340 2.553 -0.040 0.594  -0.404 13  GLN DDD CA  
4943  C C   . GLN D 13  ? 5.012 4.315 2.579 -0.074 0.641  -0.401 13  GLN DDD C   
4944  O O   . GLN D 13  ? 4.944 4.301 2.613 -0.121 0.663  -0.412 13  GLN DDD O   
4945  C CB  . GLN D 13  ? 5.106 4.343 2.564 -0.020 0.639  -0.398 13  GLN DDD CB  
4946  C CG  . GLN D 13  ? 5.055 4.320 2.603 -0.066 0.689  -0.405 13  GLN DDD CG  
4947  C CD  . GLN D 13  ? 5.132 4.327 2.616 -0.043 0.733  -0.398 13  GLN DDD CD  
4948  O OE1 . GLN D 13  ? 5.226 4.338 2.588 0.009  0.738  -0.385 13  GLN DDD OE1 
4949  N NE2 . GLN D 13  ? 5.085 4.312 2.649 -0.080 0.766  -0.408 13  GLN DDD NE2 
4950  N N   . ALA D 14  ? 5.053 4.304 2.556 -0.051 0.649  -0.389 14  ALA DDD N   
4951  C CA  . ALA D 14  ? 5.031 4.278 2.571 -0.077 0.686  -0.386 14  ALA DDD CA  
4952  C C   . ALA D 14  ? 5.047 4.273 2.638 -0.109 0.765  -0.388 14  ALA DDD C   
4953  O O   . ALA D 14  ? 5.147 4.294 2.672 -0.087 0.816  -0.378 14  ALA DDD O   
4954  C CB  . ALA D 14  ? 5.121 4.283 2.551 -0.033 0.698  -0.369 14  ALA DDD CB  
4955  N N   . GLY D 15  ? 4.962 4.254 2.667 -0.158 0.774  -0.402 15  GLY DDD N   
4956  C CA  . GLY D 15  ? 4.961 4.253 2.743 -0.195 0.840  -0.413 15  GLY DDD CA  
4957  C C   . GLY D 15  ? 4.868 4.252 2.756 -0.230 0.813  -0.435 15  GLY DDD C   
4958  O O   . GLY D 15  ? 4.831 4.244 2.813 -0.268 0.852  -0.451 15  GLY DDD O   
4959  N N   . GLY D 16  ? 4.836 4.264 2.713 -0.218 0.749  -0.437 16  GLY DDD N   
4960  C CA  . GLY D 16  ? 4.739 4.263 2.714 -0.249 0.710  -0.457 16  GLY DDD CA  
4961  C C   . GLY D 16  ? 4.642 4.254 2.712 -0.281 0.673  -0.471 16  GLY DDD C   
4962  O O   . GLY D 16  ? 4.654 4.250 2.736 -0.291 0.699  -0.470 16  GLY DDD O   
4963  N N   . SER D 17  ? 4.553 4.251 2.686 -0.296 0.616  -0.484 17  SER DDD N   
4964  C CA  . SER D 17  ? 4.462 4.242 2.671 -0.320 0.572  -0.495 17  SER DDD CA  
4965  C C   . SER D 17  ? 4.397 4.239 2.619 -0.313 0.502  -0.497 17  SER DDD C   
4966  O O   . SER D 17  ? 4.387 4.227 2.590 -0.303 0.491  -0.497 17  SER DDD O   
4967  C CB  . SER D 17  ? 4.412 4.241 2.726 -0.359 0.598  -0.518 17  SER DDD CB  
4968  O OG  . SER D 17  ? 4.339 4.235 2.714 -0.376 0.560  -0.527 17  SER DDD OG  
4969  N N   . LEU D 18  ? 4.356 4.248 2.609 -0.320 0.459  -0.499 18  LEU DDD N   
4970  C CA  . LEU D 18  ? 4.298 4.254 2.577 -0.318 0.396  -0.502 18  LEU DDD CA  
4971  C C   . LEU D 18  ? 4.227 4.254 2.588 -0.344 0.374  -0.513 18  LEU DDD C   
4972  O O   . LEU D 18  ? 4.240 4.257 2.607 -0.351 0.390  -0.512 18  LEU DDD O   
4973  C CB  . LEU D 18  ? 4.330 4.253 2.533 -0.283 0.363  -0.488 18  LEU DDD CB  
4974  C CG  . LEU D 18  ? 4.279 4.245 2.491 -0.272 0.306  -0.490 18  LEU DDD CG  
4975  C CD1 . LEU D 18  ? 4.243 4.241 2.495 -0.284 0.306  -0.500 18  LEU DDD CD1 
4976  C CD2 . LEU D 18  ? 4.340 4.253 2.465 -0.231 0.286  -0.481 18  LEU DDD CD2 
4977  N N   . ARG D 19  ? 4.159 4.252 2.578 -0.355 0.340  -0.524 19  ARG DDD N   
4978  C CA  . ARG D 19  ? 4.085 4.246 2.576 -0.375 0.314  -0.534 19  ARG DDD CA  
4979  C C   . ARG D 19  ? 4.083 4.271 2.564 -0.361 0.263  -0.526 19  ARG DDD C   
4980  O O   . ARG D 19  ? 4.093 4.278 2.550 -0.345 0.241  -0.521 19  ARG DDD O   
4981  C CB  . ARG D 19  ? 4.012 4.223 2.570 -0.394 0.317  -0.553 19  ARG DDD CB  
4982  C CG  . ARG D 19  ? 3.916 4.193 2.544 -0.410 0.293  -0.567 19  ARG DDD CG  
4983  C CD  . ARG D 19  ? 3.868 4.186 2.554 -0.424 0.296  -0.588 19  ARG DDD CD  
4984  N NE  . ARG D 19  ? 3.797 4.175 2.546 -0.435 0.275  -0.604 19  ARG DDD NE  
4985  C CZ  . ARG D 19  ? 3.763 4.183 2.570 -0.446 0.275  -0.627 19  ARG DDD CZ  
4986  N NH1 . ARG D 19  ? 3.778 4.189 2.595 -0.451 0.296  -0.636 19  ARG DDD NH1 
4987  N NH2 . ARG D 19  ? 3.720 4.190 2.575 -0.450 0.253  -0.641 19  ARG DDD NH2 
4988  N N   . LEU D 20  ? 4.087 4.298 2.589 -0.366 0.246  -0.524 20  LEU DDD N   
4989  C CA  . LEU D 20  ? 4.068 4.307 2.573 -0.355 0.201  -0.517 20  LEU DDD CA  
4990  C C   . LEU D 20  ? 4.017 4.320 2.591 -0.371 0.183  -0.527 20  LEU DDD C   
4991  O O   . LEU D 20  ? 4.016 4.333 2.623 -0.388 0.203  -0.536 20  LEU DDD O   
4992  C CB  . LEU D 20  ? 4.096 4.300 2.558 -0.342 0.198  -0.505 20  LEU DDD CB  
4993  C CG  . LEU D 20  ? 4.147 4.296 2.536 -0.314 0.194  -0.495 20  LEU DDD CG  
4994  C CD1 . LEU D 20  ? 4.206 4.294 2.540 -0.306 0.226  -0.487 20  LEU DDD CD1 
4995  C CD2 . LEU D 20  ? 4.123 4.288 2.508 -0.298 0.149  -0.492 20  LEU DDD CD2 
4996  N N   . SER D 21  ? 3.985 4.322 2.578 -0.365 0.149  -0.525 21  SER DDD N   
4997  C CA  . SER D 21  ? 3.924 4.317 2.573 -0.375 0.131  -0.532 21  SER DDD CA  
4998  C C   . SER D 21  ? 3.900 4.308 2.554 -0.365 0.101  -0.523 21  SER DDD C   
4999  O O   . SER D 21  ? 3.904 4.307 2.546 -0.352 0.081  -0.517 21  SER DDD O   
5000  C CB  . SER D 21  ? 3.901 4.318 2.572 -0.377 0.127  -0.541 21  SER DDD CB  
5001  O OG  . SER D 21  ? 3.936 4.326 2.591 -0.381 0.155  -0.547 21  SER DDD OG  
5002  N N   . CYS D 22  ? 3.879 4.304 2.553 -0.370 0.098  -0.522 22  CYS DDD N   
5003  C CA  . CYS D 22  ? 3.845 4.285 2.530 -0.362 0.074  -0.513 22  CYS DDD CA  
5004  C C   . CYS D 22  ? 3.795 4.279 2.524 -0.365 0.065  -0.518 22  CYS DDD C   
5005  O O   . CYS D 22  ? 3.773 4.274 2.520 -0.373 0.073  -0.526 22  CYS DDD O   
5006  C CB  . CYS D 22  ? 3.855 4.275 2.523 -0.362 0.079  -0.506 22  CYS DDD CB  
5007  S SG  . CYS D 22  ? 3.817 4.260 2.509 -0.355 0.056  -0.497 22  CYS DDD SG  
5008  N N   . ALA D 23  ? 3.765 4.266 2.508 -0.358 0.048  -0.515 23  ALA DDD N   
5009  C CA  . ALA D 23  ? 3.719 4.255 2.496 -0.355 0.039  -0.517 23  ALA DDD CA  
5010  C C   . ALA D 23  ? 3.702 4.243 2.489 -0.347 0.028  -0.506 23  ALA DDD C   
5011  O O   . ALA D 23  ? 3.702 4.227 2.482 -0.341 0.019  -0.498 23  ALA DDD O   
5012  C CB  . ALA D 23  ? 3.707 4.253 2.493 -0.351 0.031  -0.519 23  ALA DDD CB  
5013  N N   . VAL D 24  ? 3.694 4.255 2.495 -0.346 0.029  -0.509 24  VAL DDD N   
5014  C CA  . VAL D 24  ? 3.679 4.243 2.488 -0.337 0.023  -0.498 24  VAL DDD CA  
5015  C C   . VAL D 24  ? 3.641 4.224 2.468 -0.325 0.018  -0.495 24  VAL DDD C   
5016  O O   . VAL D 24  ? 3.635 4.238 2.468 -0.324 0.020  -0.507 24  VAL DDD O   
5017  C CB  . VAL D 24  ? 3.697 4.262 2.501 -0.341 0.030  -0.502 24  VAL DDD CB  
5018  C CG1 . VAL D 24  ? 3.696 4.256 2.500 -0.333 0.026  -0.489 24  VAL DDD CG1 
5019  C CG2 . VAL D 24  ? 3.723 4.269 2.509 -0.354 0.041  -0.507 24  VAL DDD CG2 
5020  N N   . SER D 25  ? 3.609 4.186 2.446 -0.316 0.014  -0.483 25  SER DDD N   
5021  C CA  . SER D 25  ? 3.589 4.176 2.441 -0.302 0.015  -0.476 25  SER DDD CA  
5022  C C   . SER D 25  ? 3.590 4.166 2.447 -0.293 0.019  -0.463 25  SER DDD C   
5023  O O   . SER D 25  ? 3.586 4.147 2.453 -0.296 0.018  -0.456 25  SER DDD O   
5024  C CB  . SER D 25  ? 3.577 4.165 2.445 -0.299 0.013  -0.475 25  SER DDD CB  
5025  O OG  . SER D 25  ? 3.574 4.148 2.456 -0.301 0.009  -0.469 25  SER DDD OG  
5026  N N   . GLY D 26  ? 3.592 4.174 2.441 -0.280 0.024  -0.460 26  GLY DDD N   
5027  C CA  . GLY D 26  ? 3.587 4.155 2.435 -0.268 0.031  -0.447 26  GLY DDD CA  
5028  C C   . GLY D 26  ? 3.583 4.159 2.410 -0.256 0.032  -0.452 26  GLY DDD C   
5029  O O   . GLY D 26  ? 3.587 4.181 2.407 -0.251 0.027  -0.465 26  GLY DDD O   
5030  N N   . ARG D 27  ? 3.576 4.140 2.395 -0.250 0.036  -0.443 27  ARG DDD N   
5031  C CA  . ARG D 27  ? 3.588 4.159 2.386 -0.237 0.034  -0.450 27  ARG DDD CA  
5032  C C   . ARG D 27  ? 3.589 4.177 2.386 -0.254 0.025  -0.470 27  ARG DDD C   
5033  O O   . ARG D 27  ? 3.597 4.179 2.392 -0.265 0.026  -0.470 27  ARG DDD O   
5034  C CB  . ARG D 27  ? 3.587 4.139 2.377 -0.230 0.041  -0.435 27  ARG DDD CB  
5035  C CG  . ARG D 27  ? 3.593 4.124 2.386 -0.211 0.056  -0.415 27  ARG DDD CG  
5036  C CD  . ARG D 27  ? 3.601 4.114 2.381 -0.199 0.065  -0.404 27  ARG DDD CD  
5037  N NE  . ARG D 27  ? 3.610 4.097 2.398 -0.185 0.085  -0.384 27  ARG DDD NE  
5038  C CZ  . ARG D 27  ? 3.629 4.094 2.400 -0.165 0.099  -0.370 27  ARG DDD CZ  
5039  N NH1 . ARG D 27  ? 3.642 4.110 2.384 -0.156 0.091  -0.375 27  ARG DDD NH1 
5040  N NH2 . ARG D 27  ? 3.640 4.079 2.424 -0.153 0.122  -0.352 27  ARG DDD NH2 
5041  N N   . THR D 28  ? 3.586 4.193 2.386 -0.255 0.019  -0.488 28  THR DDD N   
5042  C CA  . THR D 28  ? 3.573 4.197 2.380 -0.270 0.015  -0.511 28  THR DDD CA  
5043  C C   . THR D 28  ? 3.586 4.218 2.389 -0.263 0.012  -0.523 28  THR DDD C   
5044  O O   . THR D 28  ? 3.580 4.216 2.392 -0.281 0.014  -0.536 28  THR DDD O   
5045  C CB  . THR D 28  ? 3.557 4.202 2.375 -0.269 0.010  -0.529 28  THR DDD CB  
5046  O OG1 . THR D 28  ? 3.546 4.185 2.370 -0.279 0.013  -0.520 28  THR DDD OG1 
5047  C CG2 . THR D 28  ? 3.544 4.207 2.377 -0.282 0.009  -0.556 28  THR DDD CG2 
5048  N N   . PHE D 29  ? 3.602 4.235 2.389 -0.237 0.007  -0.521 29  PHE DDD N   
5049  C CA  . PHE D 29  ? 3.608 4.252 2.388 -0.222 -0.001 -0.538 29  PHE DDD CA  
5050  C C   . PHE D 29  ? 3.622 4.255 2.403 -0.237 0.004  -0.532 29  PHE DDD C   
5051  O O   . PHE D 29  ? 3.620 4.267 2.410 -0.240 0.000  -0.554 29  PHE DDD O   
5052  C CB  . PHE D 29  ? 3.608 4.244 2.361 -0.185 -0.004 -0.529 29  PHE DDD CB  
5053  C CG  . PHE D 29  ? 3.599 4.205 2.333 -0.177 0.007  -0.500 29  PHE DDD CG  
5054  C CD1 . PHE D 29  ? 3.598 4.197 2.321 -0.172 0.007  -0.499 29  PHE DDD CD1 
5055  C CD2 . PHE D 29  ? 3.586 4.172 2.317 -0.173 0.020  -0.475 29  PHE DDD CD2 
5056  C CE1 . PHE D 29  ? 3.599 4.170 2.308 -0.165 0.019  -0.472 29  PHE DDD CE1 
5057  C CE2 . PHE D 29  ? 3.590 4.149 2.313 -0.166 0.033  -0.451 29  PHE DDD CE2 
5058  C CZ  . PHE D 29  ? 3.598 4.149 2.308 -0.162 0.033  -0.449 29  PHE DDD CZ  
5059  N N   . SER D 30  ? 3.637 4.246 2.412 -0.245 0.014  -0.507 30  SER DDD N   
5060  C CA  . SER D 30  ? 3.643 4.237 2.414 -0.255 0.019  -0.497 30  SER DDD CA  
5061  C C   . SER D 30  ? 3.634 4.224 2.416 -0.283 0.024  -0.502 30  SER DDD C   
5062  O O   . SER D 30  ? 3.641 4.219 2.419 -0.292 0.028  -0.495 30  SER DDD O   
5063  C CB  . SER D 30  ? 3.651 4.221 2.413 -0.246 0.026  -0.469 30  SER DDD CB  
5064  O OG  . SER D 30  ? 3.648 4.213 2.418 -0.246 0.029  -0.459 30  SER DDD OG  
5065  N N   . THR D 31  ? 3.623 4.222 2.418 -0.296 0.025  -0.514 31  THR DDD N   
5066  C CA  . THR D 31  ? 3.617 4.206 2.416 -0.320 0.034  -0.519 31  THR DDD CA  
5067  C C   . THR D 31  ? 3.616 4.212 2.424 -0.329 0.039  -0.537 31  THR DDD C   
5068  O O   . THR D 31  ? 3.605 4.225 2.432 -0.324 0.035  -0.561 31  THR DDD O   
5069  C CB  . THR D 31  ? 3.611 4.208 2.421 -0.329 0.037  -0.528 31  THR DDD CB  
5070  O OG1 . THR D 31  ? 3.609 4.202 2.414 -0.320 0.031  -0.514 31  THR DDD OG1 
5071  C CG2 . THR D 31  ? 3.614 4.191 2.419 -0.349 0.049  -0.529 31  THR DDD CG2 
5072  N N   . ALA D 32  ? 3.620 4.196 2.419 -0.339 0.047  -0.528 32  ALA DDD N   
5073  C CA  . ALA D 32  ? 3.627 4.203 2.436 -0.350 0.056  -0.544 32  ALA DDD CA  
5074  C C   . ALA D 32  ? 3.637 4.204 2.454 -0.370 0.074  -0.555 32  ALA DDD C   
5075  O O   . ALA D 32  ? 3.631 4.216 2.477 -0.376 0.080  -0.581 32  ALA DDD O   
5076  C CB  . ALA D 32  ? 3.633 4.188 2.424 -0.352 0.059  -0.527 32  ALA DDD CB  
5077  N N   . ALA D 33  ? 3.653 4.191 2.447 -0.377 0.081  -0.537 33  ALA DDD N   
5078  C CA  . ALA D 33  ? 3.683 4.198 2.470 -0.392 0.101  -0.541 33  ALA DDD CA  
5079  C C   . ALA D 33  ? 3.709 4.203 2.471 -0.389 0.097  -0.524 33  ALA DDD C   
5080  O O   . ALA D 33  ? 3.706 4.198 2.457 -0.378 0.082  -0.507 33  ALA DDD O   
5081  C CB  . ALA D 33  ? 3.695 4.184 2.469 -0.400 0.117  -0.537 33  ALA DDD CB  
5082  N N   . MET D 34  ? 3.752 4.233 2.510 -0.396 0.112  -0.530 34  MET DDD N   
5083  C CA  . MET D 34  ? 3.781 4.236 2.509 -0.393 0.112  -0.517 34  MET DDD CA  
5084  C C   . MET D 34  ? 3.816 4.227 2.511 -0.398 0.134  -0.513 34  MET DDD C   
5085  O O   . MET D 34  ? 3.818 4.224 2.526 -0.410 0.158  -0.526 34  MET DDD O   
5086  C CB  . MET D 34  ? 3.789 4.258 2.530 -0.394 0.112  -0.527 34  MET DDD CB  
5087  C CG  . MET D 34  ? 3.767 4.274 2.535 -0.386 0.092  -0.531 34  MET DDD CG  
5088  S SD  . MET D 34  ? 3.769 4.275 2.525 -0.371 0.069  -0.509 34  MET DDD SD  
5089  C CE  . MET D 34  ? 3.779 4.259 2.511 -0.370 0.069  -0.503 34  MET DDD CE  
5090  N N   . GLY D 35  ? 3.842 4.221 2.498 -0.388 0.128  -0.498 35  GLY DDD N   
5091  C CA  . GLY D 35  ? 3.899 4.229 2.511 -0.387 0.148  -0.491 35  GLY DDD CA  
5092  C C   . GLY D 35  ? 3.933 4.234 2.507 -0.374 0.144  -0.485 35  GLY DDD C   
5093  O O   . GLY D 35  ? 3.926 4.244 2.507 -0.365 0.118  -0.481 35  GLY DDD O   
5094  N N   . TRP D 36  ? 3.973 4.232 2.512 -0.373 0.171  -0.484 36  TRP DDD N   
5095  C CA  . TRP D 36  ? 4.007 4.226 2.494 -0.355 0.169  -0.477 36  TRP DDD CA  
5096  C C   . TRP D 36  ? 4.054 4.226 2.486 -0.339 0.170  -0.466 36  TRP DDD C   
5097  O O   . TRP D 36  ? 4.076 4.226 2.498 -0.346 0.195  -0.464 36  TRP DDD O   
5098  C CB  . TRP D 36  ? 4.029 4.227 2.506 -0.360 0.200  -0.484 36  TRP DDD CB  
5099  C CG  . TRP D 36  ? 3.982 4.223 2.503 -0.370 0.191  -0.495 36  TRP DDD CG  
5100  C CD1 . TRP D 36  ? 3.941 4.218 2.515 -0.388 0.203  -0.509 36  TRP DDD CD1 
5101  C CD2 . TRP D 36  ? 3.972 4.225 2.490 -0.359 0.167  -0.493 36  TRP DDD CD2 
5102  N NE1 . TRP D 36  ? 3.909 4.218 2.509 -0.389 0.188  -0.516 36  TRP DDD NE1 
5103  C CE2 . TRP D 36  ? 3.928 4.223 2.495 -0.372 0.167  -0.506 36  TRP DDD CE2 
5104  C CE3 . TRP D 36  ? 3.996 4.230 2.477 -0.338 0.144  -0.486 36  TRP DDD CE3 
5105  C CZ2 . TRP D 36  ? 3.913 4.229 2.491 -0.367 0.148  -0.507 36  TRP DDD CZ2 
5106  C CZ3 . TRP D 36  ? 3.975 4.230 2.471 -0.333 0.124  -0.489 36  TRP DDD CZ3 
5107  C CH2 . TRP D 36  ? 3.935 4.231 2.478 -0.348 0.127  -0.499 36  TRP DDD CH2 
5108  N N   . PHE D 37  ? 4.064 4.223 2.467 -0.318 0.142  -0.461 37  PHE DDD N   
5109  C CA  . PHE D 37  ? 4.110 4.220 2.453 -0.295 0.137  -0.453 37  PHE DDD CA  
5110  C C   . PHE D 37  ? 4.170 4.244 2.462 -0.271 0.130  -0.453 37  PHE DDD C   
5111  O O   . PHE D 37  ? 4.157 4.260 2.474 -0.271 0.112  -0.459 37  PHE DDD O   
5112  C CB  . PHE D 37  ? 4.055 4.188 2.417 -0.289 0.103  -0.451 37  PHE DDD CB  
5113  C CG  . PHE D 37  ? 3.995 4.152 2.393 -0.307 0.109  -0.448 37  PHE DDD CG  
5114  C CD1 . PHE D 37  ? 3.924 4.131 2.381 -0.327 0.109  -0.453 37  PHE DDD CD1 
5115  C CD2 . PHE D 37  ? 4.003 4.132 2.372 -0.301 0.114  -0.442 37  PHE DDD CD2 
5116  C CE1 . PHE D 37  ? 3.882 4.110 2.369 -0.340 0.113  -0.452 37  PHE DDD CE1 
5117  C CE2 . PHE D 37  ? 3.954 4.107 2.356 -0.317 0.119  -0.440 37  PHE DDD CE2 
5118  C CZ  . PHE D 37  ? 3.899 4.101 2.360 -0.336 0.118  -0.446 37  PHE DDD CZ  
5119  N N   . ARG D 38  ? 4.236 4.249 2.456 -0.249 0.144  -0.447 38  ARG DDD N   
5120  C CA  . ARG D 38  ? 4.273 4.243 2.430 -0.217 0.134  -0.448 38  ARG DDD CA  
5121  C C   . ARG D 38  ? 4.324 4.257 2.428 -0.186 0.112  -0.446 38  ARG DDD C   
5122  O O   . ARG D 38  ? 4.354 4.268 2.442 -0.188 0.126  -0.439 38  ARG DDD O   
5123  C CB  . ARG D 38  ? 4.307 4.226 2.416 -0.214 0.179  -0.444 38  ARG DDD CB  
5124  C CG  . ARG D 38  ? 4.353 4.211 2.405 -0.207 0.218  -0.434 38  ARG DDD CG  
5125  C CD  . ARG D 38  ? 4.386 4.200 2.409 -0.212 0.270  -0.430 38  ARG DDD CD  
5126  N NE  . ARG D 38  ? 4.436 4.190 2.412 -0.207 0.314  -0.420 38  ARG DDD NE  
5127  C CZ  . ARG D 38  ? 4.482 4.188 2.434 -0.212 0.370  -0.416 38  ARG DDD CZ  
5128  N NH1 . ARG D 38  ? 4.477 4.189 2.447 -0.220 0.387  -0.421 38  ARG DDD NH1 
5129  N NH2 . ARG D 38  ? 4.537 4.188 2.448 -0.207 0.410  -0.407 38  ARG DDD NH2 
5130  N N   . GLN D 39  ? 4.337 4.264 2.418 -0.157 0.076  -0.455 39  GLN DDD N   
5131  C CA  . GLN D 39  ? 4.393 4.277 2.412 -0.118 0.052  -0.458 39  GLN DDD CA  
5132  C C   . GLN D 39  ? 4.481 4.305 2.417 -0.083 0.059  -0.459 39  GLN DDD C   
5133  O O   . GLN D 39  ? 4.484 4.327 2.434 -0.076 0.038  -0.469 39  GLN DDD O   
5134  C CB  . GLN D 39  ? 4.339 4.269 2.411 -0.111 0.000  -0.473 39  GLN DDD CB  
5135  C CG  . GLN D 39  ? 4.398 4.289 2.413 -0.067 -0.032 -0.483 39  GLN DDD CG  
5136  C CD  . GLN D 39  ? 4.344 4.276 2.419 -0.071 -0.067 -0.492 39  GLN DDD CD  
5137  O OE1 . GLN D 39  ? 4.274 4.264 2.430 -0.089 -0.086 -0.500 39  GLN DDD OE1 
5138  N NE2 . GLN D 39  ? 4.378 4.278 2.412 -0.052 -0.071 -0.491 39  GLN DDD NE2 
5139  N N   . ALA D 40  ? 4.560 4.313 2.410 -0.061 0.089  -0.449 40  ALA DDD N   
5140  C CA  . ALA D 40  ? 4.648 4.328 2.400 -0.020 0.099  -0.447 40  ALA DDD CA  
5141  C C   . ALA D 40  ? 4.672 4.338 2.385 0.026  0.046  -0.463 40  ALA DDD C   
5142  O O   . ALA D 40  ? 4.628 4.332 2.386 0.024  0.010  -0.472 40  ALA DDD O   
5143  C CB  . ALA D 40  ? 4.728 4.333 2.403 -0.012 0.153  -0.430 40  ALA DDD CB  
5144  N N   . PRO D 41  ? 4.739 4.352 2.370 0.070  0.038  -0.468 41  PRO DDD N   
5145  C CA  . PRO D 41  ? 4.782 4.374 2.368 0.120  -0.013 -0.487 41  PRO DDD CA  
5146  C C   . PRO D 41  ? 4.829 4.374 2.356 0.142  -0.007 -0.480 41  PRO DDD C   
5147  O O   . PRO D 41  ? 4.886 4.370 2.346 0.145  0.043  -0.460 41  PRO DDD O   
5148  C CB  . PRO D 41  ? 4.872 4.405 2.370 0.162  -0.009 -0.490 41  PRO DDD CB  
5149  C CG  . PRO D 41  ? 4.904 4.396 2.367 0.141  0.060  -0.465 41  PRO DDD CG  
5150  C CD  . PRO D 41  ? 4.792 4.359 2.369 0.077  0.077  -0.459 41  PRO DDD CD  
5151  N N   . GLY D 42  ? 4.799 4.375 2.360 0.154  -0.055 -0.497 42  GLY DDD N   
5152  C CA  . GLY D 42  ? 4.854 4.387 2.358 0.182  -0.061 -0.495 42  GLY DDD CA  
5153  C C   . GLY D 42  ? 4.801 4.356 2.350 0.139  -0.031 -0.478 42  GLY DDD C   
5154  O O   . GLY D 42  ? 4.822 4.357 2.345 0.157  -0.043 -0.479 42  GLY DDD O   
5155  N N   . LYS D 43  ? 3.978 4.321 2.104 -0.286 0.069  -0.317 43  LYS DDD N   
5156  C CA  . LYS D 43  ? 3.947 4.290 2.093 -0.265 0.059  -0.301 43  LYS DDD CA  
5157  C C   . LYS D 43  ? 3.912 4.252 2.101 -0.232 0.057  -0.298 43  LYS DDD C   
5158  O O   . LYS D 43  ? 3.903 4.244 2.113 -0.224 0.072  -0.316 43  LYS DDD O   
5159  C CB  . LYS D 43  ? 3.942 4.298 2.092 -0.270 0.075  -0.312 43  LYS DDD CB  
5160  C CG  . LYS D 43  ? 3.953 4.311 2.068 -0.293 0.067  -0.301 43  LYS DDD CG  
5161  C CD  . LYS D 43  ? 3.946 4.318 2.066 -0.297 0.085  -0.314 43  LYS DDD CD  
5162  C CE  . LYS D 43  ? 3.954 4.327 2.044 -0.315 0.074  -0.298 43  LYS DDD CE  
5163  N NZ  . LYS D 43  ? 3.923 4.291 2.032 -0.294 0.059  -0.279 43  LYS DDD NZ  
5164  N N   . GLU D 44  ? 3.894 4.229 2.097 -0.214 0.040  -0.277 44  GLU DDD N   
5165  C CA  . GLU D 44  ? 3.866 4.200 2.111 -0.181 0.037  -0.272 44  GLU DDD CA  
5166  C C   . GLU D 44  ? 3.853 4.197 2.127 -0.169 0.057  -0.288 44  GLU DDD C   
5167  O O   . GLU D 44  ? 3.863 4.214 2.126 -0.180 0.065  -0.293 44  GLU DDD O   
5168  C CB  . GLU D 44  ? 3.850 4.179 2.097 -0.168 0.013  -0.246 44  GLU DDD CB  
5169  C CG  . GLU D 44  ? 3.875 4.194 2.090 -0.183 -0.009 -0.230 44  GLU DDD CG  
5170  C CD  . GLU D 44  ? 3.893 4.206 2.105 -0.184 -0.012 -0.232 44  GLU DDD CD  
5171  O OE1 . GLU D 44  ? 3.884 4.197 2.126 -0.161 -0.016 -0.228 44  GLU DDD OE1 
5172  O OE2 . GLU D 44  ? 3.922 4.232 2.102 -0.209 -0.012 -0.236 44  GLU DDD OE2 
5173  N N   . ARG D 45  ? 3.832 4.177 2.143 -0.147 0.065  -0.296 45  ARG DDD N   
5174  C CA  . ARG D 45  ? 3.815 4.169 2.158 -0.134 0.085  -0.313 45  ARG DDD CA  
5175  C C   . ARG D 45  ? 3.800 4.157 2.157 -0.118 0.079  -0.300 45  ARG DDD C   
5176  O O   . ARG D 45  ? 3.782 4.135 2.151 -0.101 0.061  -0.281 45  ARG DDD O   
5177  C CB  . ARG D 45  ? 3.784 4.136 2.160 -0.117 0.094  -0.325 45  ARG DDD CB  
5178  C CG  . ARG D 45  ? 3.727 4.081 2.144 -0.087 0.089  -0.316 45  ARG DDD CG  
5179  C CD  . ARG D 45  ? 3.697 4.044 2.115 -0.075 0.066  -0.293 45  ARG DDD CD  
5180  N NE  . ARG D 45  ? 3.669 4.018 2.093 -0.062 0.056  -0.276 45  ARG DDD NE  
5181  C CZ  . ARG D 45  ? 3.632 3.985 2.090 -0.037 0.052  -0.268 45  ARG DDD CZ  
5182  N NH1 . ARG D 45  ? 3.616 3.969 2.105 -0.021 0.056  -0.274 45  ARG DDD NH1 
5183  N NH2 . ARG D 45  ? 3.615 3.970 2.076 -0.028 0.042  -0.254 45  ARG DDD NH2 
5184  N N   . GLU D 46  ? 3.811 4.177 2.166 -0.125 0.092  -0.309 46  GLU DDD N   
5185  C CA  . GLU D 46  ? 3.797 4.167 2.158 -0.116 0.086  -0.297 46  GLU DDD CA  
5186  C C   . GLU D 46  ? 3.798 4.176 2.197 -0.097 0.103  -0.310 46  GLU DDD C   
5187  O O   . GLU D 46  ? 3.809 4.192 2.223 -0.098 0.121  -0.331 46  GLU DDD O   
5188  C CB  . GLU D 46  ? 3.809 4.183 2.133 -0.143 0.086  -0.296 46  GLU DDD CB  
5189  C CG  . GLU D 46  ? 3.821 4.205 2.138 -0.160 0.110  -0.321 46  GLU DDD CG  
5190  C CD  . GLU D 46  ? 3.847 4.233 2.118 -0.194 0.111  -0.323 46  GLU DDD CD  
5191  O OE1 . GLU D 46  ? 3.852 4.250 2.116 -0.207 0.126  -0.337 46  GLU DDD OE1 
5192  O OE2 . GLU D 46  ? 3.847 4.224 2.090 -0.207 0.096  -0.311 46  GLU DDD OE2 
5193  N N   . PHE D 47  ? 3.798 4.179 2.214 -0.081 0.097  -0.298 47  PHE DDD N   
5194  C CA  . PHE D 47  ? 3.788 4.177 2.239 -0.063 0.111  -0.307 47  PHE DDD CA  
5195  C C   . PHE D 47  ? 3.811 4.210 2.252 -0.081 0.131  -0.327 47  PHE DDD C   
5196  O O   . PHE D 47  ? 3.837 4.237 2.242 -0.104 0.129  -0.325 47  PHE DDD O   
5197  C CB  . PHE D 47  ? 3.768 4.157 2.231 -0.046 0.097  -0.287 47  PHE DDD CB  
5198  C CG  . PHE D 47  ? 3.759 4.157 2.256 -0.029 0.110  -0.295 47  PHE DDD CG  
5199  C CD1 . PHE D 47  ? 3.747 4.146 2.281 -0.010 0.120  -0.305 47  PHE DDD CD1 
5200  C CD2 . PHE D 47  ? 3.767 4.170 2.258 -0.032 0.111  -0.291 47  PHE DDD CD2 
5201  C CE1 . PHE D 47  ? 3.735 4.142 2.300 0.006  0.131  -0.312 47  PHE DDD CE1 
5202  C CE2 . PHE D 47  ? 3.753 4.164 2.276 -0.016 0.123  -0.298 47  PHE DDD CE2 
5203  C CZ  . PHE D 47  ? 3.737 4.150 2.297 0.003  0.133  -0.309 47  PHE DDD CZ  
5204  N N   . VAL D 48  ? 3.800 4.207 2.273 -0.070 0.150  -0.346 48  VAL DDD N   
5205  C CA  . VAL D 48  ? 3.811 4.230 2.281 -0.083 0.171  -0.368 48  VAL DDD CA  
5206  C C   . VAL D 48  ? 3.776 4.203 2.276 -0.065 0.178  -0.368 48  VAL DDD C   
5207  O O   . VAL D 48  ? 3.768 4.201 2.253 -0.074 0.178  -0.363 48  VAL DDD O   
5208  C CB  . VAL D 48  ? 3.831 4.254 2.312 -0.088 0.189  -0.394 48  VAL DDD CB  
5209  C CG1 . VAL D 48  ? 3.847 4.284 2.332 -0.099 0.212  -0.418 48  VAL DDD CG1 
5210  C CG2 . VAL D 48  ? 3.864 4.280 2.315 -0.107 0.184  -0.395 48  VAL DDD CG2 
5211  N N   . ALA D 49  ? 3.748 4.174 2.289 -0.041 0.182  -0.373 49  ALA DDD N   
5212  C CA  . ALA D 49  ? 3.723 4.156 2.298 -0.022 0.189  -0.374 49  ALA DDD CA  
5213  C C   . ALA D 49  ? 3.690 4.118 2.304 0.006  0.184  -0.369 49  ALA DDD C   
5214  O O   . ALA D 49  ? 3.717 4.138 2.335 0.007  0.182  -0.373 49  ALA DDD O   
5215  C CB  . ALA D 49  ? 3.732 4.178 2.316 -0.030 0.213  -0.400 49  ALA DDD CB  
5216  N N   . ALA D 50  ? 3.631 4.061 2.270 0.026  0.180  -0.358 50  ALA DDD N   
5217  C CA  . ALA D 50  ? 3.569 3.996 2.249 0.053  0.177  -0.355 50  ALA DDD CA  
5218  C C   . ALA D 50  ? 3.527 3.963 2.238 0.066  0.190  -0.363 50  ALA DDD C   
5219  O O   . ALA D 50  ? 3.509 3.953 2.207 0.057  0.195  -0.364 50  ALA DDD O   
5220  C CB  . ALA D 50  ? 3.554 3.975 2.233 0.065  0.155  -0.329 50  ALA DDD CB  
5221  N N   . ILE D 51  ? 3.495 3.932 2.246 0.085  0.195  -0.369 51  ILE DDD N   
5222  C CA  . ILE D 51  ? 3.472 3.917 2.258 0.100  0.206  -0.377 51  ILE DDD CA  
5223  C C   . ILE D 51  ? 3.432 3.873 2.253 0.126  0.197  -0.364 51  ILE DDD C   
5224  O O   . ILE D 51  ? 3.441 3.875 2.273 0.131  0.193  -0.365 51  ILE DDD O   
5225  C CB  . ILE D 51  ? 3.486 3.937 2.287 0.094  0.228  -0.406 51  ILE DDD CB  
5226  C CG1 . ILE D 51  ? 3.468 3.928 2.303 0.108  0.239  -0.414 51  ILE DDD CG1 
5227  C CG2 . ILE D 51  ? 3.493 3.936 2.309 0.098  0.229  -0.416 51  ILE DDD CG2 
5228  C CD1 . ILE D 51  ? 3.487 3.955 2.330 0.098  0.261  -0.444 51  ILE DDD CD1 
5229  N N   . ARG D 52  ? 3.382 3.828 2.221 0.141  0.193  -0.353 52  ARG DDD N   
5230  C CA  . ARG D 52  ? 3.325 3.770 2.200 0.166  0.185  -0.342 52  ARG DDD CA  
5231  C C   . ARG D 52  ? 3.319 3.766 2.232 0.175  0.200  -0.361 52  ARG DDD C   
5232  O O   . ARG D 52  ? 3.328 3.782 2.248 0.170  0.216  -0.378 52  ARG DDD O   
5233  C CB  . ARG D 52  ? 3.278 3.728 2.159 0.178  0.178  -0.326 52  ARG DDD CB  
5234  C CG  . ARG D 52  ? 3.223 3.672 2.131 0.200  0.164  -0.309 52  ARG DDD CG  
5235  C CD  . ARG D 52  ? 3.185 3.640 2.104 0.213  0.159  -0.296 52  ARG DDD CD  
5236  N NE  . ARG D 52  ? 3.179 3.634 2.065 0.205  0.147  -0.282 52  ARG DDD NE  
5237  C CZ  . ARG D 52  ? 3.174 3.624 2.042 0.205  0.130  -0.265 52  ARG DDD CZ  
5238  N NH1 . ARG D 52  ? 3.165 3.612 2.043 0.212  0.122  -0.260 52  ARG DDD NH1 
5239  N NH2 . ARG D 52  ? 3.182 3.631 2.023 0.197  0.119  -0.254 52  ARG DDD NH2 
5240  N N   . TRP D 53  ? 3.307 3.749 2.243 0.187  0.194  -0.359 53  TRP DDD N   
5241  C CA  . TRP D 53  ? 3.299 3.740 2.273 0.197  0.205  -0.375 53  TRP DDD CA  
5242  C C   . TRP D 53  ? 3.275 3.723 2.278 0.211  0.212  -0.376 53  TRP DDD C   
5243  O O   . TRP D 53  ? 3.285 3.738 2.307 0.210  0.228  -0.397 53  TRP DDD O   
5244  C CB  . TRP D 53  ? 3.286 3.720 2.279 0.208  0.193  -0.365 53  TRP DDD CB  
5245  C CG  . TRP D 53  ? 3.288 3.717 2.304 0.208  0.203  -0.385 53  TRP DDD CG  
5246  C CD1 . TRP D 53  ? 3.269 3.695 2.325 0.224  0.202  -0.387 53  TRP DDD CD1 
5247  C CD2 . TRP D 53  ? 3.310 3.735 2.310 0.191  0.213  -0.405 53  TRP DDD CD2 
5248  N NE1 . TRP D 53  ? 3.278 3.699 2.345 0.218  0.211  -0.407 53  TRP DDD NE1 
5249  C CE2 . TRP D 53  ? 3.308 3.729 2.341 0.198  0.218  -0.419 53  TRP DDD CE2 
5250  C CE3 . TRP D 53  ? 3.334 3.761 2.296 0.169  0.218  -0.413 53  TRP DDD CE3 
5251  C CZ2 . TRP D 53  ? 3.337 3.754 2.366 0.186  0.228  -0.442 53  TRP DDD CZ2 
5252  C CZ3 . TRP D 53  ? 3.362 3.785 2.318 0.156  0.229  -0.435 53  TRP DDD CZ3 
5253  C CH2 . TRP D 53  ? 3.364 3.782 2.354 0.165  0.234  -0.450 53  TRP DDD CH2 
5254  N N   . SER D 54  ? 3.233 3.685 2.242 0.224  0.200  -0.355 54  SER DDD N   
5255  C CA  . SER D 54  ? 3.201 3.660 2.240 0.240  0.203  -0.352 54  SER DDD CA  
5256  C C   . SER D 54  ? 3.202 3.668 2.220 0.232  0.208  -0.352 54  SER DDD C   
5257  O O   . SER D 54  ? 3.191 3.660 2.209 0.242  0.198  -0.334 54  SER DDD O   
5258  C CB  . SER D 54  ? 3.169 3.627 2.226 0.258  0.188  -0.331 54  SER DDD CB  
5259  O OG  . SER D 54  ? 3.146 3.611 2.222 0.272  0.188  -0.323 54  SER DDD OG  
5260  N N   . GLY D 55  ? 3.218 3.687 2.221 0.216  0.223  -0.371 55  GLY DDD N   
5261  C CA  . GLY D 55  ? 3.218 3.695 2.207 0.208  0.230  -0.373 55  GLY DDD CA  
5262  C C   . GLY D 55  ? 3.248 3.729 2.206 0.184  0.243  -0.390 55  GLY DDD C   
5263  O O   . GLY D 55  ? 3.249 3.738 2.203 0.178  0.253  -0.398 55  GLY DDD O   
5264  N N   . GLY D 56  ? 3.274 3.748 2.211 0.171  0.241  -0.396 56  GLY DDD N   
5265  C CA  . GLY D 56  ? 3.306 3.784 2.216 0.147  0.254  -0.414 56  GLY DDD CA  
5266  C C   . GLY D 56  ? 3.317 3.798 2.186 0.130  0.249  -0.405 56  GLY DDD C   
5267  O O   . GLY D 56  ? 3.335 3.822 2.180 0.109  0.260  -0.420 56  GLY DDD O   
5268  N N   . SER D 57  ? 3.300 3.778 2.161 0.138  0.233  -0.381 57  SER DDD N   
5269  C CA  . SER D 57  ? 3.311 3.789 2.132 0.122  0.224  -0.367 57  SER DDD CA  
5270  C C   . SER D 57  ? 3.339 3.808 2.127 0.107  0.215  -0.364 57  SER DDD C   
5271  O O   . SER D 57  ? 3.337 3.798 2.133 0.117  0.203  -0.353 57  SER DDD O   
5272  C CB  . SER D 57  ? 3.276 3.752 2.101 0.137  0.208  -0.343 57  SER DDD CB  
5273  O OG  . SER D 57  ? 3.232 3.707 2.096 0.162  0.204  -0.338 57  SER DDD OG  
5274  N N   . ALA D 58  ? 3.369 3.842 2.125 0.082  0.222  -0.374 58  ALA DDD N   
5275  C CA  . ALA D 58  ? 3.395 3.861 2.117 0.064  0.216  -0.373 58  ALA DDD CA  
5276  C C   . ALA D 58  ? 3.404 3.865 2.089 0.052  0.199  -0.352 58  ALA DDD C   
5277  O O   . ALA D 58  ? 3.392 3.858 2.072 0.052  0.198  -0.344 58  ALA DDD O   
5278  C CB  . ALA D 58  ? 3.430 3.903 2.140 0.043  0.235  -0.398 58  ALA DDD CB  
5279  N N   . TYR D 59  ? 3.422 3.874 2.082 0.043  0.187  -0.344 59  TYR DDD N   
5280  C CA  . TYR D 59  ? 3.450 3.896 2.071 0.028  0.170  -0.326 59  TYR DDD CA  
5281  C C   . TYR D 59  ? 3.519 3.965 2.105 0.001  0.175  -0.336 59  TYR DDD C   
5282  O O   . TYR D 59  ? 3.539 3.976 2.113 -0.003 0.165  -0.331 59  TYR DDD O   
5283  C CB  . TYR D 59  ? 3.417 3.853 2.039 0.042  0.148  -0.303 59  TYR DDD CB  
5284  C CG  . TYR D 59  ? 3.416 3.847 2.004 0.029  0.129  -0.284 59  TYR DDD CG  
5285  C CD1 . TYR D 59  ? 3.423 3.859 1.992 0.016  0.131  -0.282 59  TYR DDD CD1 
5286  C CD2 . TYR D 59  ? 3.411 3.832 1.986 0.031  0.110  -0.268 59  TYR DDD CD2 
5287  C CE1 . TYR D 59  ? 3.436 3.866 1.974 0.005  0.113  -0.264 59  TYR DDD CE1 
5288  C CE2 . TYR D 59  ? 3.422 3.837 1.967 0.020  0.092  -0.251 59  TYR DDD CE2 
5289  C CZ  . TYR D 59  ? 3.436 3.855 1.963 0.007  0.093  -0.248 59  TYR DDD CZ  
5290  O OH  . TYR D 59  ? 3.450 3.862 1.948 -0.004 0.074  -0.231 59  TYR DDD OH  
5291  N N   . TYR D 60  ? 3.573 4.029 2.143 -0.019 0.189  -0.350 60  TYR DDD N   
5292  C CA  . TYR D 60  ? 3.624 4.082 2.156 -0.048 0.194  -0.360 60  TYR DDD CA  
5293  C C   . TYR D 60  ? 3.625 4.072 2.121 -0.061 0.172  -0.337 60  TYR DDD C   
5294  O O   . TYR D 60  ? 3.591 4.036 2.081 -0.056 0.158  -0.319 60  TYR DDD O   
5295  C CB  . TYR D 60  ? 3.666 4.139 2.193 -0.063 0.214  -0.378 60  TYR DDD CB  
5296  C CG  . TYR D 60  ? 3.693 4.174 2.246 -0.059 0.235  -0.406 60  TYR DDD CG  
5297  C CD1 . TYR D 60  ? 3.672 4.154 2.270 -0.033 0.242  -0.412 60  TYR DDD CD1 
5298  C CD2 . TYR D 60  ? 3.750 4.236 2.283 -0.081 0.247  -0.425 60  TYR DDD CD2 
5299  C CE1 . TYR D 60  ? 3.693 4.181 2.316 -0.029 0.260  -0.437 60  TYR DDD CE1 
5300  C CE2 . TYR D 60  ? 3.772 4.265 2.329 -0.077 0.266  -0.451 60  TYR DDD CE2 
5301  C CZ  . TYR D 60  ? 3.748 4.242 2.351 -0.051 0.272  -0.457 60  TYR DDD CZ  
5302  O OH  . TYR D 60  ? 3.786 4.286 2.415 -0.047 0.289  -0.483 60  TYR DDD OH  
5303  N N   . ALA D 61  ? 3.647 4.088 2.120 -0.075 0.168  -0.339 61  ALA DDD N   
5304  C CA  . ALA D 61  ? 3.669 4.100 2.104 -0.090 0.148  -0.321 61  ALA DDD CA  
5305  C C   . ALA D 61  ? 3.707 4.145 2.105 -0.119 0.152  -0.323 61  ALA DDD C   
5306  O O   . ALA D 61  ? 3.736 4.187 2.136 -0.130 0.172  -0.343 61  ALA DDD O   
5307  C CB  . ALA D 61  ? 3.678 4.102 2.104 -0.096 0.145  -0.324 61  ALA DDD CB  
5308  N N   . ASP D 62  ? 3.712 4.142 2.079 -0.132 0.132  -0.303 62  ASP DDD N   
5309  C CA  . ASP D 62  ? 3.726 4.160 2.060 -0.156 0.128  -0.296 62  ASP DDD CA  
5310  C C   . ASP D 62  ? 3.771 4.216 2.077 -0.186 0.144  -0.315 62  ASP DDD C   
5311  O O   . ASP D 62  ? 3.790 4.246 2.083 -0.202 0.153  -0.320 62  ASP DDD O   
5312  C CB  . ASP D 62  ? 3.716 4.136 2.025 -0.161 0.100  -0.269 62  ASP DDD CB  
5313  C CG  . ASP D 62  ? 3.672 4.081 2.006 -0.133 0.083  -0.254 62  ASP DDD CG  
5314  O OD1 . ASP D 62  ? 3.647 4.053 1.997 -0.121 0.086  -0.260 62  ASP DDD OD1 
5315  O OD2 . ASP D 62  ? 3.650 4.053 1.987 -0.123 0.066  -0.235 62  ASP DDD OD2 
5316  N N   . SER D 63  ? 3.788 4.230 2.085 -0.194 0.148  -0.325 63  SER DDD N   
5317  C CA  . SER D 63  ? 3.821 4.272 2.086 -0.225 0.161  -0.342 63  SER DDD CA  
5318  C C   . SER D 63  ? 3.835 4.301 2.123 -0.224 0.190  -0.372 63  SER DDD C   
5319  O O   . SER D 63  ? 3.863 4.341 2.127 -0.249 0.203  -0.389 63  SER DDD O   
5320  C CB  . SER D 63  ? 3.824 4.265 2.068 -0.236 0.151  -0.337 63  SER DDD CB  
5321  O OG  . SER D 63  ? 3.787 4.217 2.060 -0.211 0.146  -0.335 63  SER DDD OG  
5322  N N   . VAL D 64  ? 3.821 4.290 2.153 -0.195 0.198  -0.379 64  VAL DDD N   
5323  C CA  . VAL D 64  ? 3.823 4.305 2.182 -0.190 0.224  -0.408 64  VAL DDD CA  
5324  C C   . VAL D 64  ? 3.790 4.283 2.172 -0.179 0.232  -0.410 64  VAL DDD C   
5325  O O   . VAL D 64  ? 3.785 4.293 2.184 -0.180 0.254  -0.435 64  VAL DDD O   
5326  C CB  . VAL D 64  ? 3.821 4.296 2.214 -0.168 0.227  -0.418 64  VAL DDD CB  
5327  C CG1 . VAL D 64  ? 3.841 4.307 2.212 -0.180 0.220  -0.417 64  VAL DDD CG1 
5328  C CG2 . VAL D 64  ? 3.789 4.253 2.215 -0.136 0.215  -0.400 64  VAL DDD CG2 
5329  N N   . LYS D 65  ? 3.753 4.239 2.137 -0.167 0.216  -0.387 65  LYS DDD N   
5330  C CA  . LYS D 65  ? 3.720 4.215 2.124 -0.157 0.222  -0.386 65  LYS DDD CA  
5331  C C   . LYS D 65  ? 3.746 4.261 2.132 -0.182 0.241  -0.405 65  LYS DDD C   
5332  O O   . LYS D 65  ? 3.767 4.284 2.113 -0.209 0.236  -0.399 65  LYS DDD O   
5333  C CB  . LYS D 65  ? 3.691 4.175 2.084 -0.151 0.199  -0.356 65  LYS DDD CB  
5334  C CG  . LYS D 65  ? 3.636 4.119 2.067 -0.121 0.196  -0.348 65  LYS DDD CG  
5335  C CD  . LYS D 65  ? 3.603 4.071 2.032 -0.108 0.170  -0.320 65  LYS DDD CD  
5336  C CE  . LYS D 65  ? 3.550 4.015 2.021 -0.075 0.167  -0.313 65  LYS DDD CE  
5337  N NZ  . LYS D 65  ? 3.524 3.974 2.000 -0.059 0.145  -0.294 65  LYS DDD NZ  
5338  N N   . GLY D 66  ? 3.745 4.273 2.161 -0.173 0.263  -0.429 66  GLY DDD N   
5339  C CA  . GLY D 66  ? 3.774 4.325 2.181 -0.193 0.283  -0.449 66  GLY DDD CA  
5340  C C   . GLY D 66  ? 3.816 4.378 2.221 -0.207 0.303  -0.478 66  GLY DDD C   
5341  O O   . GLY D 66  ? 3.825 4.407 2.220 -0.226 0.320  -0.497 66  GLY DDD O   
5342  N N   . ARG D 67  ? 3.854 4.404 2.266 -0.199 0.299  -0.482 67  ARG DDD N   
5343  C CA  . ARG D 67  ? 3.914 4.473 2.325 -0.212 0.316  -0.510 67  ARG DDD CA  
5344  C C   . ARG D 67  ? 3.907 4.459 2.363 -0.184 0.323  -0.523 67  ARG DDD C   
5345  O O   . ARG D 67  ? 3.911 4.476 2.391 -0.181 0.343  -0.550 67  ARG DDD O   
5346  C CB  . ARG D 67  ? 3.961 4.512 2.328 -0.236 0.305  -0.502 67  ARG DDD CB  
5347  C CG  . ARG D 67  ? 3.997 4.553 2.319 -0.263 0.296  -0.487 67  ARG DDD CG  
5348  C CD  . ARG D 67  ? 4.040 4.593 2.318 -0.292 0.290  -0.484 67  ARG DDD CD  
5349  N NE  . ARG D 67  ? 4.040 4.572 2.318 -0.281 0.272  -0.469 67  ARG DDD NE  
5350  C CZ  . ARG D 67  ? 4.063 4.591 2.342 -0.283 0.277  -0.483 67  ARG DDD CZ  
5351  N NH1 . ARG D 67  ? 4.093 4.636 2.372 -0.296 0.298  -0.512 67  ARG DDD NH1 
5352  N NH2 . ARG D 67  ? 4.056 4.564 2.335 -0.272 0.259  -0.466 67  ARG DDD NH2 
5353  N N   . PHE D 68  ? 3.901 4.433 2.370 -0.164 0.305  -0.504 68  PHE DDD N   
5354  C CA  . PHE D 68  ? 3.892 4.415 2.400 -0.139 0.308  -0.513 68  PHE DDD CA  
5355  C C   . PHE D 68  ? 3.869 4.396 2.422 -0.112 0.313  -0.514 68  PHE DDD C   
5356  O O   . PHE D 68  ? 3.860 4.393 2.408 -0.113 0.312  -0.505 68  PHE DDD O   
5357  C CB  . PHE D 68  ? 3.888 4.391 2.387 -0.133 0.287  -0.492 68  PHE DDD CB  
5358  C CG  . PHE D 68  ? 3.921 4.421 2.383 -0.157 0.284  -0.496 68  PHE DDD CG  
5359  C CD1 . PHE D 68  ? 3.952 4.467 2.385 -0.186 0.298  -0.513 68  PHE DDD CD1 
5360  C CD2 . PHE D 68  ? 3.919 4.402 2.374 -0.152 0.268  -0.481 68  PHE DDD CD2 
5361  C CE1 . PHE D 68  ? 3.978 4.491 2.376 -0.209 0.295  -0.516 68  PHE DDD CE1 
5362  C CE2 . PHE D 68  ? 3.946 4.426 2.367 -0.175 0.265  -0.484 68  PHE DDD CE2 
5363  C CZ  . PHE D 68  ? 3.977 4.472 2.369 -0.203 0.279  -0.501 68  PHE DDD CZ  
5364  N N   . THR D 69  ? 3.866 4.389 2.460 -0.091 0.319  -0.527 69  THR DDD N   
5365  C CA  . THR D 69  ? 3.840 4.361 2.478 -0.061 0.320  -0.523 69  THR DDD CA  
5366  C C   . THR D 69  ? 3.825 4.332 2.495 -0.039 0.313  -0.521 69  THR DDD C   
5367  O O   . THR D 69  ? 3.831 4.340 2.520 -0.038 0.325  -0.545 69  THR DDD O   
5368  C CB  . THR D 69  ? 3.835 4.374 2.499 -0.059 0.341  -0.547 69  THR DDD CB  
5369  O OG1 . THR D 69  ? 3.852 4.407 2.485 -0.083 0.348  -0.551 69  THR DDD OG1 
5370  C CG2 . THR D 69  ? 3.801 4.338 2.504 -0.032 0.338  -0.537 69  THR DDD CG2 
5371  N N   . ILE D 70  ? 3.798 4.291 2.474 -0.022 0.294  -0.495 70  ILE DDD N   
5372  C CA  . ILE D 70  ? 3.762 4.242 2.471 0.002  0.285  -0.488 70  ILE DDD CA  
5373  C C   . ILE D 70  ? 3.710 4.196 2.464 0.024  0.293  -0.494 70  ILE DDD C   
5374  O O   . ILE D 70  ? 3.685 4.177 2.440 0.028  0.293  -0.485 70  ILE DDD O   
5375  C CB  . ILE D 70  ? 3.765 4.232 2.461 0.009  0.262  -0.458 70  ILE DDD CB  
5376  C CG1 . ILE D 70  ? 3.766 4.221 2.488 0.026  0.255  -0.456 70  ILE DDD CG1 
5377  C CG2 . ILE D 70  ? 3.746 4.213 2.445 0.020  0.251  -0.437 70  ILE DDD CG2 
5378  C CD1 . ILE D 70  ? 3.765 4.208 2.474 0.032  0.232  -0.428 70  ILE DDD CD1 
5379  N N   . SER D 71  ? 3.682 4.164 2.471 0.038  0.299  -0.508 71  SER DDD N   
5380  C CA  . SER D 71  ? 3.646 4.132 2.482 0.060  0.306  -0.516 71  SER DDD CA  
5381  C C   . SER D 71  ? 3.619 4.093 2.485 0.076  0.301  -0.518 71  SER DDD C   
5382  O O   . SER D 71  ? 3.637 4.105 2.488 0.065  0.299  -0.523 71  SER DDD O   
5383  C CB  . SER D 71  ? 3.665 4.167 2.512 0.052  0.328  -0.544 71  SER DDD CB  
5384  O OG  . SER D 71  ? 3.697 4.200 2.536 0.038  0.338  -0.568 71  SER DDD OG  
5385  N N   . ARG D 72  ? 3.576 4.048 2.483 0.099  0.299  -0.513 72  ARG DDD N   
5386  C CA  . ARG D 72  ? 3.560 4.021 2.499 0.115  0.293  -0.513 72  ARG DDD CA  
5387  C C   . ARG D 72  ? 3.534 3.999 2.520 0.132  0.303  -0.529 72  ARG DDD C   
5388  O O   . ARG D 72  ? 3.505 3.979 2.502 0.137  0.310  -0.530 72  ARG DDD O   
5389  C CB  . ARG D 72  ? 3.549 3.999 2.485 0.128  0.272  -0.483 72  ARG DDD CB  
5390  C CG  . ARG D 72  ? 3.527 3.982 2.474 0.142  0.265  -0.464 72  ARG DDD CG  
5391  C CD  . ARG D 72  ? 3.502 3.955 2.496 0.166  0.263  -0.461 72  ARG DDD CD  
5392  N NE  . ARG D 72  ? 3.475 3.932 2.481 0.180  0.257  -0.444 72  ARG DDD NE  
5393  C CZ  . ARG D 72  ? 3.472 3.940 2.488 0.182  0.269  -0.452 72  ARG DDD CZ  
5394  N NH1 . ARG D 72  ? 3.494 3.969 2.509 0.170  0.286  -0.477 72  ARG DDD NH1 
5395  N NH2 . ARG D 72  ? 3.450 3.921 2.477 0.195  0.262  -0.436 72  ARG DDD NH2 
5396  N N   . ASP D 73  ? 3.537 3.995 2.550 0.138  0.305  -0.543 73  ASP DDD N   
5397  C CA  . ASP D 73  ? 3.532 3.990 2.594 0.155  0.312  -0.557 73  ASP DDD CA  
5398  C C   . ASP D 73  ? 3.519 3.965 2.607 0.174  0.296  -0.539 73  ASP DDD C   
5399  O O   . ASP D 73  ? 3.544 3.980 2.632 0.171  0.291  -0.542 73  ASP DDD O   
5400  C CB  . ASP D 73  ? 3.555 4.017 2.627 0.146  0.328  -0.591 73  ASP DDD CB  
5401  C CG  . ASP D 73  ? 3.543 4.006 2.667 0.163  0.336  -0.608 73  ASP DDD CG  
5402  O OD1 . ASP D 73  ? 3.509 3.969 2.661 0.181  0.329  -0.594 73  ASP DDD OD1 
5403  O OD2 . ASP D 73  ? 3.565 4.031 2.701 0.156  0.348  -0.637 73  ASP DDD OD2 
5404  N N   . LYS D 74  ? 3.491 3.937 2.599 0.191  0.288  -0.520 74  LYS DDD N   
5405  C CA  . LYS D 74  ? 3.459 3.895 2.586 0.208  0.271  -0.497 74  LYS DDD CA  
5406  C C   . LYS D 74  ? 3.463 3.891 2.629 0.218  0.272  -0.511 74  LYS DDD C   
5407  O O   . LYS D 74  ? 3.467 3.884 2.636 0.222  0.258  -0.498 74  LYS DDD O   
5408  C CB  . LYS D 74  ? 3.413 3.854 2.556 0.224  0.265  -0.478 74  LYS DDD CB  
5409  C CG  . LYS D 74  ? 3.393 3.838 2.500 0.219  0.257  -0.458 74  LYS DDD CG  
5410  C CD  . LYS D 74  ? 3.346 3.797 2.471 0.236  0.250  -0.438 74  LYS DDD CD  
5411  C CE  . LYS D 74  ? 3.312 3.756 2.448 0.249  0.232  -0.415 74  LYS DDD CE  
5412  N NZ  . LYS D 74  ? 3.277 3.727 2.423 0.263  0.224  -0.395 74  LYS DDD NZ  
5413  N N   . ALA D 75  ? 3.463 3.895 2.657 0.220  0.286  -0.536 75  ALA DDD N   
5414  C CA  . ALA D 75  ? 3.457 3.882 2.693 0.230  0.287  -0.551 75  ALA DDD CA  
5415  C C   . ALA D 75  ? 3.482 3.898 2.703 0.216  0.288  -0.565 75  ALA DDD C   
5416  O O   . ALA D 75  ? 3.471 3.876 2.719 0.224  0.281  -0.567 75  ALA DDD O   
5417  C CB  . ALA D 75  ? 3.456 3.890 2.722 0.234  0.303  -0.576 75  ALA DDD CB  
5418  N N   . LYS D 76  ? 3.512 3.933 2.692 0.197  0.295  -0.573 76  LYS DDD N   
5419  C CA  . LYS D 76  ? 3.545 3.960 2.705 0.181  0.297  -0.587 76  LYS DDD CA  
5420  C C   . LYS D 76  ? 3.552 3.959 2.677 0.174  0.281  -0.563 76  LYS DDD C   
5421  O O   . LYS D 76  ? 3.577 3.977 2.685 0.162  0.280  -0.571 76  LYS DDD O   
5422  C CB  . LYS D 76  ? 3.567 3.994 2.705 0.162  0.315  -0.614 76  LYS DDD CB  
5423  C CG  . LYS D 76  ? 3.572 4.005 2.745 0.165  0.331  -0.647 76  LYS DDD CG  
5424  C CD  . LYS D 76  ? 3.594 4.039 2.742 0.145  0.349  -0.675 76  LYS DDD CD  
5425  C CE  . LYS D 76  ? 3.608 4.057 2.792 0.147  0.363  -0.710 76  LYS DDD CE  
5426  N NZ  . LYS D 76  ? 3.591 4.042 2.823 0.168  0.365  -0.712 76  LYS DDD NZ  
5427  N N   . ASN D 77  ? 3.538 3.946 2.652 0.181  0.270  -0.535 77  ASN DDD N   
5428  C CA  . ASN D 77  ? 3.542 3.945 2.624 0.176  0.254  -0.510 77  ASN DDD CA  
5429  C C   . ASN D 77  ? 3.590 3.995 2.627 0.153  0.259  -0.519 77  ASN DDD C   
5430  O O   . ASN D 77  ? 3.617 4.013 2.633 0.145  0.250  -0.511 77  ASN DDD O   
5431  C CB  . ASN D 77  ? 3.524 3.914 2.624 0.185  0.240  -0.500 77  ASN DDD CB  
5432  C CG  . ASN D 77  ? 3.486 3.875 2.624 0.207  0.231  -0.484 77  ASN DDD CG  
5433  O OD1 . ASN D 77  ? 3.460 3.856 2.598 0.215  0.229  -0.470 77  ASN DDD OD1 
5434  N ND2 . ASN D 77  ? 3.477 3.857 2.648 0.216  0.226  -0.487 77  ASN DDD ND2 
5435  N N   . THR D 78  ? 3.614 4.029 2.636 0.141  0.274  -0.535 78  THR DDD N   
5436  C CA  . THR D 78  ? 3.644 4.064 2.625 0.117  0.282  -0.546 78  THR DDD CA  
5437  C C   . THR D 78  ? 3.641 4.069 2.590 0.110  0.281  -0.532 78  THR DDD C   
5438  O O   . THR D 78  ? 3.607 4.043 2.574 0.120  0.284  -0.529 78  THR DDD O   
5439  C CB  . THR D 78  ? 3.676 4.103 2.668 0.109  0.301  -0.581 78  THR DDD CB  
5440  O OG1 . THR D 78  ? 3.676 4.094 2.708 0.121  0.301  -0.593 78  THR DDD OG1 
5441  C CG2 . THR D 78  ? 3.715 4.145 2.667 0.084  0.308  -0.595 78  THR DDD CG2 
5442  N N   . VAL D 79  ? 3.676 4.103 2.582 0.092  0.275  -0.524 79  VAL DDD N   
5443  C CA  . VAL D 79  ? 3.709 4.145 2.579 0.078  0.276  -0.515 79  VAL DDD CA  
5444  C C   . VAL D 79  ? 3.766 4.208 2.605 0.053  0.289  -0.537 79  VAL DDD C   
5445  O O   . VAL D 79  ? 3.806 4.243 2.639 0.045  0.290  -0.547 79  VAL DDD O   
5446  C CB  . VAL D 79  ? 3.705 4.134 2.549 0.079  0.256  -0.484 79  VAL DDD CB  
5447  C CG1 . VAL D 79  ? 3.718 4.137 2.541 0.069  0.246  -0.479 79  VAL DDD CG1 
5448  C CG2 . VAL D 79  ? 3.717 4.153 2.528 0.067  0.255  -0.474 79  VAL DDD CG2 
5449  N N   . TYR D 80  ? 3.781 4.237 2.605 0.042  0.300  -0.544 80  TYR DDD N   
5450  C CA  . TYR D 80  ? 3.808 4.275 2.605 0.017  0.315  -0.567 80  TYR DDD CA  
5451  C C   . TYR D 80  ? 3.840 4.311 2.590 -0.002 0.309  -0.550 80  TYR DDD C   
5452  O O   . TYR D 80  ? 3.818 4.290 2.567 0.006  0.301  -0.530 80  TYR DDD O   
5453  C CB  . TYR D 80  ? 3.788 4.270 2.610 0.018  0.335  -0.593 80  TYR DDD CB  
5454  C CG  . TYR D 80  ? 3.753 4.231 2.624 0.037  0.342  -0.610 80  TYR DDD CG  
5455  C CD1 . TYR D 80  ? 3.756 4.230 2.635 0.033  0.347  -0.631 80  TYR DDD CD1 
5456  C CD2 . TYR D 80  ? 3.708 4.187 2.617 0.060  0.341  -0.605 80  TYR DDD CD2 
5457  C CE1 . TYR D 80  ? 3.732 4.202 2.657 0.050  0.351  -0.646 80  TYR DDD CE1 
5458  C CE2 . TYR D 80  ? 3.681 4.156 2.636 0.077  0.346  -0.620 80  TYR DDD CE2 
5459  C CZ  . TYR D 80  ? 3.694 4.164 2.658 0.072  0.350  -0.640 80  TYR DDD CZ  
5460  O OH  . TYR D 80  ? 3.660 4.125 2.670 0.089  0.353  -0.654 80  TYR DDD OH  
5461  N N   . LEU D 81  ? 3.895 4.367 2.607 -0.026 0.311  -0.558 81  LEU DDD N   
5462  C CA  . LEU D 81  ? 3.924 4.403 2.590 -0.049 0.309  -0.549 81  LEU DDD CA  
5463  C C   . LEU D 81  ? 3.969 4.465 2.623 -0.071 0.330  -0.577 81  LEU DDD C   
5464  O O   . LEU D 81  ? 4.009 4.507 2.655 -0.083 0.337  -0.596 81  LEU DDD O   
5465  C CB  . LEU D 81  ? 3.922 4.389 2.553 -0.061 0.293  -0.531 81  LEU DDD CB  
5466  C CG  . LEU D 81  ? 3.923 4.393 2.508 -0.082 0.285  -0.515 81  LEU DDD CG  
5467  C CD1 . LEU D 81  ? 3.897 4.365 2.488 -0.068 0.273  -0.491 81  LEU DDD CD1 
5468  C CD2 . LEU D 81  ? 3.928 4.387 2.480 -0.096 0.270  -0.502 81  LEU DDD CD2 
5469  N N   . GLN D 82  ? 3.970 4.481 2.625 -0.074 0.339  -0.581 82  GLN DDD N   
5470  C CA  . GLN D 82  ? 3.993 4.524 2.630 -0.097 0.358  -0.605 82  GLN DDD CA  
5471  C C   . GLN D 82  ? 4.035 4.568 2.619 -0.123 0.350  -0.591 82  GLN DDD C   
5472  O O   . GLN D 82  ? 4.023 4.550 2.592 -0.121 0.336  -0.565 82  GLN DDD O   
5473  C CB  . GLN D 82  ? 3.956 4.501 2.617 -0.088 0.371  -0.614 82  GLN DDD CB  
5474  C CG  . GLN D 82  ? 3.958 4.527 2.614 -0.107 0.393  -0.646 82  GLN DDD CG  
5475  C CD  . GLN D 82  ? 3.952 4.522 2.626 -0.108 0.405  -0.675 82  GLN DDD CD  
5476  O OE1 . GLN D 82  ? 3.912 4.475 2.628 -0.085 0.407  -0.683 82  GLN DDD OE1 
5477  N NE2 . GLN D 82  ? 3.973 4.551 2.614 -0.134 0.413  -0.690 82  GLN DDD NE2 
5478  N N   . MET D 83  ? 4.088 4.627 2.643 -0.148 0.357  -0.607 83  MET DDD N   
5479  C CA  . MET D 83  ? 4.130 4.669 2.632 -0.175 0.349  -0.593 83  MET DDD CA  
5480  C C   . MET D 83  ? 4.170 4.733 2.651 -0.202 0.367  -0.614 83  MET DDD C   
5481  O O   . MET D 83  ? 4.202 4.773 2.669 -0.219 0.379  -0.637 83  MET DDD O   
5482  C CB  . MET D 83  ? 4.157 4.683 2.640 -0.184 0.340  -0.591 83  MET DDD CB  
5483  C CG  . MET D 83  ? 4.138 4.643 2.642 -0.159 0.322  -0.570 83  MET DDD CG  
5484  S SD  . MET D 83  ? 4.166 4.657 2.655 -0.167 0.315  -0.573 83  MET DDD SD  
5485  C CE  . MET D 83  ? 4.195 4.684 2.624 -0.197 0.300  -0.552 83  MET DDD CE  
5486  N N   . ASN D 84  ? 4.179 4.753 2.657 -0.204 0.370  -0.608 84  ASN DDD N   
5487  C CA  . ASN D 84  ? 4.206 4.803 2.660 -0.229 0.385  -0.624 84  ASN DDD CA  
5488  C C   . ASN D 84  ? 4.220 4.817 2.619 -0.259 0.374  -0.608 84  ASN DDD C   
5489  O O   . ASN D 84  ? 4.230 4.807 2.615 -0.255 0.352  -0.579 84  ASN DDD O   
5490  C CB  . ASN D 84  ? 4.195 4.805 2.669 -0.220 0.391  -0.622 84  ASN DDD CB  
5491  C CG  . ASN D 84  ? 4.166 4.773 2.695 -0.188 0.398  -0.632 84  ASN DDD CG  
5492  O OD1 . ASN D 84  ? 4.174 4.785 2.728 -0.181 0.412  -0.658 84  ASN DDD OD1 
5493  N ND2 . ASN D 84  ? 4.131 4.731 2.678 -0.168 0.388  -0.611 84  ASN DDD ND2 
5494  N N   . SER D 85  ? 4.219 4.836 2.590 -0.289 0.388  -0.625 85  SER DDD N   
5495  C CA  . SER D 85  ? 4.226 4.848 2.544 -0.321 0.379  -0.611 85  SER DDD CA  
5496  C C   . SER D 85  ? 4.229 4.830 2.521 -0.328 0.361  -0.594 85  SER DDD C   
5497  O O   . SER D 85  ? 4.242 4.833 2.501 -0.339 0.342  -0.567 85  SER DDD O   
5498  C CB  . SER D 85  ? 4.203 4.824 2.508 -0.322 0.367  -0.585 85  SER DDD CB  
5499  O OG  . SER D 85  ? 4.179 4.819 2.507 -0.316 0.383  -0.599 85  SER DDD OG  
5500  N N   . LEU D 86  ? 4.212 4.807 2.518 -0.321 0.366  -0.610 86  LEU DDD N   
5501  C CA  . LEU D 86  ? 4.190 4.764 2.478 -0.322 0.348  -0.594 86  LEU DDD CA  
5502  C C   . LEU D 86  ? 4.211 4.786 2.444 -0.356 0.338  -0.580 86  LEU DDD C   
5503  O O   . LEU D 86  ? 4.261 4.858 2.470 -0.383 0.353  -0.599 86  LEU DDD O   
5504  C CB  . LEU D 86  ? 4.182 4.754 2.488 -0.318 0.358  -0.619 86  LEU DDD CB  
5505  C CG  . LEU D 86  ? 4.140 4.711 2.499 -0.288 0.370  -0.638 86  LEU DDD CG  
5506  C CD1 . LEU D 86  ? 4.152 4.749 2.525 -0.297 0.396  -0.672 86  LEU DDD CD1 
5507  C CD2 . LEU D 86  ? 4.123 4.679 2.499 -0.277 0.366  -0.644 86  LEU DDD CD2 
5508  N N   . LYS D 87  ? 4.163 4.719 2.378 -0.354 0.314  -0.549 87  LYS DDD N   
5509  C CA  . LYS D 87  ? 4.155 4.706 2.318 -0.383 0.299  -0.531 87  LYS DDD CA  
5510  C C   . LYS D 87  ? 4.161 4.701 2.313 -0.388 0.294  -0.535 87  LYS DDD C   
5511  O O   . LYS D 87  ? 4.154 4.687 2.341 -0.366 0.299  -0.546 87  LYS DDD O   
5512  C CB  . LYS D 87  ? 4.107 4.642 2.261 -0.375 0.274  -0.495 87  LYS DDD CB  
5513  C CG  . LYS D 87  ? 4.079 4.623 2.227 -0.380 0.273  -0.485 87  LYS DDD CG  
5514  C CD  . LYS D 87  ? 4.059 4.588 2.182 -0.384 0.246  -0.450 87  LYS DDD CD  
5515  C CE  . LYS D 87  ? 4.027 4.555 2.167 -0.369 0.240  -0.435 87  LYS DDD CE  
5516  N NZ  . LYS D 87  ? 4.013 4.520 2.140 -0.362 0.211  -0.401 87  LYS DDD NZ  
5517  N N   . TYR D 88  ? 4.170 4.709 2.277 -0.417 0.285  -0.526 88  TYR DDD N   
5518  C CA  . TYR D 88  ? 4.163 4.689 2.253 -0.425 0.277  -0.526 88  TYR DDD CA  
5519  C C   . TYR D 88  ? 4.162 4.663 2.266 -0.401 0.254  -0.499 88  TYR DDD C   
5520  O O   . TYR D 88  ? 4.168 4.658 2.278 -0.395 0.251  -0.503 88  TYR DDD O   
5521  C CB  . TYR D 88  ? 4.157 4.690 2.194 -0.464 0.272  -0.521 88  TYR DDD CB  
5522  C CG  . TYR D 88  ? 4.148 4.704 2.169 -0.490 0.296  -0.553 88  TYR DDD CG  
5523  C CD1 . TYR D 88  ? 4.127 4.690 2.173 -0.482 0.314  -0.583 88  TYR DDD CD1 
5524  C CD2 . TYR D 88  ? 4.158 4.732 2.140 -0.523 0.300  -0.554 88  TYR DDD CD2 
5525  C CE1 . TYR D 88  ? 4.148 4.734 2.181 -0.505 0.335  -0.613 88  TYR DDD CE1 
5526  C CE2 . TYR D 88  ? 4.179 4.778 2.147 -0.548 0.321  -0.583 88  TYR DDD CE2 
5527  C CZ  . TYR D 88  ? 4.175 4.780 2.169 -0.538 0.339  -0.614 88  TYR DDD CZ  
5528  O OH  . TYR D 88  ? 4.202 4.832 2.181 -0.563 0.361  -0.644 88  TYR DDD OH  
5529  N N   . GLU D 89  ? 4.162 4.654 2.271 -0.388 0.238  -0.474 89  GLU DDD N   
5530  C CA  . GLU D 89  ? 4.143 4.612 2.266 -0.364 0.215  -0.447 89  GLU DDD CA  
5531  C C   . GLU D 89  ? 4.136 4.600 2.309 -0.329 0.222  -0.457 89  GLU DDD C   
5532  O O   . GLU D 89  ? 4.115 4.562 2.302 -0.310 0.206  -0.439 89  GLU DDD O   
5533  C CB  . GLU D 89  ? 4.112 4.576 2.228 -0.360 0.198  -0.420 89  GLU DDD CB  
5534  C CG  . GLU D 89  ? 4.123 4.577 2.195 -0.382 0.175  -0.396 89  GLU DDD CG  
5535  C CD  . GLU D 89  ? 4.166 4.630 2.194 -0.420 0.182  -0.406 89  GLU DDD CD  
5536  O OE1 . GLU D 89  ? 4.185 4.639 2.181 -0.437 0.165  -0.391 89  GLU DDD OE1 
5537  O OE2 . GLU D 89  ? 4.182 4.666 2.209 -0.434 0.204  -0.430 89  GLU DDD OE2 
5538  N N   . ASP D 90  ? 4.165 4.644 2.365 -0.323 0.245  -0.483 90  ASP DDD N   
5539  C CA  . ASP D 90  ? 4.146 4.622 2.396 -0.291 0.253  -0.494 90  ASP DDD CA  
5540  C C   . ASP D 90  ? 4.146 4.615 2.404 -0.289 0.257  -0.508 90  ASP DDD C   
5541  O O   . ASP D 90  ? 4.123 4.585 2.419 -0.263 0.259  -0.513 90  ASP DDD O   
5542  C CB  . ASP D 90  ? 4.158 4.652 2.433 -0.286 0.276  -0.518 90  ASP DDD CB  
5543  C CG  . ASP D 90  ? 4.161 4.662 2.438 -0.283 0.274  -0.505 90  ASP DDD CG  
5544  O OD1 . ASP D 90  ? 4.168 4.657 2.431 -0.280 0.253  -0.477 90  ASP DDD OD1 
5545  O OD2 . ASP D 90  ? 4.177 4.695 2.468 -0.284 0.292  -0.524 90  ASP DDD OD2 
5546  N N   . THR D 91  ? 4.167 4.636 2.388 -0.316 0.257  -0.514 91  THR DDD N   
5547  C CA  . THR D 91  ? 4.165 4.627 2.390 -0.316 0.258  -0.525 91  THR DDD CA  
5548  C C   . THR D 91  ? 4.145 4.585 2.380 -0.296 0.236  -0.500 91  THR DDD C   
5549  O O   . THR D 91  ? 4.146 4.577 2.351 -0.305 0.217  -0.476 91  THR DDD O   
5550  C CB  . THR D 91  ? 4.190 4.657 2.370 -0.350 0.260  -0.533 91  THR DDD CB  
5551  O OG1 . THR D 91  ? 4.203 4.691 2.377 -0.368 0.283  -0.561 91  THR DDD OG1 
5552  C CG2 . THR D 91  ? 4.191 4.647 2.372 -0.349 0.257  -0.539 91  THR DDD CG2 
5553  N N   . ALA D 92  ? 4.126 4.560 2.402 -0.269 0.238  -0.506 92  ALA DDD N   
5554  C CA  . ALA D 92  ? 4.109 4.525 2.402 -0.247 0.219  -0.483 92  ALA DDD CA  
5555  C C   . ALA D 92  ? 4.101 4.512 2.436 -0.224 0.227  -0.498 92  ALA DDD C   
5556  O O   . ALA D 92  ? 4.109 4.530 2.461 -0.226 0.247  -0.526 92  ALA DDD O   
5557  C CB  . ALA D 92  ? 4.084 4.497 2.385 -0.231 0.206  -0.460 92  ALA DDD CB  
5558  N N   . VAL D 93  ? 4.089 4.486 2.442 -0.204 0.211  -0.480 93  VAL DDD N   
5559  C CA  . VAL D 93  ? 4.061 4.452 2.460 -0.177 0.214  -0.487 93  VAL DDD CA  
5560  C C   . VAL D 93  ? 4.026 4.418 2.454 -0.153 0.209  -0.473 93  VAL DDD C   
5561  O O   . VAL D 93  ? 3.995 4.380 2.414 -0.146 0.191  -0.446 93  VAL DDD O   
5562  C CB  . VAL D 93  ? 4.049 4.426 2.450 -0.171 0.200  -0.477 93  VAL DDD CB  
5563  C CG1 . VAL D 93  ? 4.011 4.383 2.458 -0.145 0.202  -0.483 93  VAL DDD CG1 
5564  C CG2 . VAL D 93  ? 4.085 4.461 2.456 -0.196 0.205  -0.491 93  VAL DDD CG2 
5565  N N   . TYR D 94  ? 4.023 4.424 2.485 -0.140 0.225  -0.490 94  TYR DDD N   
5566  C CA  . TYR D 94  ? 3.997 4.400 2.490 -0.117 0.223  -0.480 94  TYR DDD CA  
5567  C C   . TYR D 94  ? 3.968 4.362 2.500 -0.091 0.216  -0.474 94  TYR DDD C   
5568  O O   . TYR D 94  ? 3.977 4.368 2.532 -0.086 0.226  -0.494 94  TYR DDD O   
5569  C CB  . TYR D 94  ? 4.005 4.423 2.509 -0.120 0.244  -0.502 94  TYR DDD CB  
5570  C CG  . TYR D 94  ? 4.024 4.453 2.491 -0.143 0.247  -0.500 94  TYR DDD CG  
5571  C CD1 . TYR D 94  ? 4.063 4.495 2.491 -0.171 0.251  -0.510 94  TYR DDD CD1 
5572  C CD2 . TYR D 94  ? 4.009 4.443 2.476 -0.138 0.243  -0.486 94  TYR DDD CD2 
5573  C CE1 . TYR D 94  ? 4.088 4.529 2.481 -0.194 0.252  -0.506 94  TYR DDD CE1 
5574  C CE2 . TYR D 94  ? 4.028 4.470 2.460 -0.160 0.244  -0.483 94  TYR DDD CE2 
5575  C CZ  . TYR D 94  ? 4.069 4.516 2.463 -0.189 0.248  -0.492 94  TYR DDD CZ  
5576  O OH  . TYR D 94  ? 4.099 4.554 2.458 -0.212 0.249  -0.488 94  TYR DDD OH  
5577  N N   . TYR D 95  ? 3.933 4.320 2.470 -0.075 0.199  -0.448 95  TYR DDD N   
5578  C CA  . TYR D 95  ? 3.889 4.268 2.461 -0.050 0.189  -0.436 95  TYR DDD CA  
5579  C C   . TYR D 95  ? 3.851 4.235 2.453 -0.029 0.190  -0.430 95  TYR DDD C   
5580  O O   . TYR D 95  ? 3.831 4.219 2.419 -0.029 0.182  -0.413 95  TYR DDD O   
5581  C CB  . TYR D 95  ? 3.876 4.245 2.430 -0.048 0.167  -0.410 95  TYR DDD CB  
5582  C CG  . TYR D 95  ? 3.898 4.261 2.422 -0.068 0.162  -0.412 95  TYR DDD CG  
5583  C CD1 . TYR D 95  ? 3.890 4.245 2.427 -0.064 0.161  -0.419 95  TYR DDD CD1 
5584  C CD2 . TYR D 95  ? 3.918 4.282 2.399 -0.091 0.158  -0.407 95  TYR DDD CD2 
5585  C CE1 . TYR D 95  ? 3.905 4.254 2.414 -0.081 0.156  -0.420 95  TYR DDD CE1 
5586  C CE2 . TYR D 95  ? 3.928 4.285 2.380 -0.109 0.153  -0.409 95  TYR DDD CE2 
5587  C CZ  . TYR D 95  ? 3.922 4.272 2.388 -0.104 0.153  -0.415 95  TYR DDD CZ  
5588  O OH  . TYR D 95  ? 3.929 4.273 2.366 -0.122 0.148  -0.417 95  TYR DDD OH  
5589  N N   . CYS D 96  ? 3.830 4.216 2.473 -0.012 0.199  -0.442 96  CYS DDD N   
5590  C CA  . CYS D 96  ? 3.792 4.180 2.470 0.012  0.197  -0.433 96  CYS DDD CA  
5591  C C   . CYS D 96  ? 3.776 4.156 2.466 0.029  0.178  -0.410 96  CYS DDD C   
5592  O O   . CYS D 96  ? 3.778 4.150 2.467 0.027  0.172  -0.409 96  CYS DDD O   
5593  C CB  . CYS D 96  ? 3.776 4.169 2.493 0.022  0.214  -0.456 96  CYS DDD CB  
5594  S SG  . CYS D 96  ? 3.757 4.139 2.511 0.039  0.210  -0.459 96  CYS DDD SG  
5595  N N   . ALA D 97  ? 3.758 4.141 2.460 0.044  0.170  -0.392 97  ALA DDD N   
5596  C CA  . ALA D 97  ? 3.720 4.099 2.433 0.061  0.151  -0.368 97  ALA DDD CA  
5597  C C   . ALA D 97  ? 3.670 4.054 2.420 0.084  0.152  -0.362 97  ALA DDD C   
5598  O O   . ALA D 97  ? 3.659 4.051 2.415 0.084  0.163  -0.370 97  ALA DDD O   
5599  C CB  . ALA D 97  ? 3.727 4.105 2.405 0.052  0.136  -0.348 97  ALA DDD CB  
5600  N N   . ARG D 98  ? 3.624 4.006 2.400 0.101  0.142  -0.350 98  ARG DDD N   
5601  C CA  . ARG D 98  ? 3.572 3.959 2.386 0.124  0.141  -0.344 98  ARG DDD CA  
5602  C C   . ARG D 98  ? 3.534 3.923 2.348 0.136  0.121  -0.318 98  ARG DDD C   
5603  O O   . ARG D 98  ? 3.543 3.926 2.344 0.133  0.110  -0.308 98  ARG DDD O   
5604  C CB  . ARG D 98  ? 3.562 3.946 2.412 0.133  0.147  -0.356 98  ARG DDD CB  
5605  C CG  . ARG D 98  ? 3.528 3.916 2.418 0.156  0.146  -0.349 98  ARG DDD CG  
5606  C CD  . ARG D 98  ? 3.526 3.910 2.451 0.163  0.153  -0.364 98  ARG DDD CD  
5607  N NE  . ARG D 98  ? 3.498 3.886 2.462 0.184  0.149  -0.355 98  ARG DDD NE  
5608  C CZ  . ARG D 98  ? 3.481 3.868 2.458 0.197  0.135  -0.336 98  ARG DDD CZ  
5609  N NH1 . ARG D 98  ? 3.484 3.868 2.441 0.191  0.122  -0.324 98  ARG DDD NH1 
5610  N NH2 . ARG D 98  ? 3.460 3.852 2.472 0.214  0.133  -0.330 98  ARG DDD NH2 
5611  N N   . THR D 99  ? 3.496 3.891 2.322 0.149  0.118  -0.307 99  THR DDD N   
5612  C CA  . THR D 99  ? 3.451 3.850 2.283 0.164  0.101  -0.283 99  THR DDD CA  
5613  C C   . THR D 99  ? 3.398 3.803 2.270 0.184  0.103  -0.281 99  THR DDD C   
5614  O O   . THR D 99  ? 3.408 3.816 2.294 0.187  0.117  -0.293 99  THR DDD O   
5615  C CB  . THR D 99  ? 3.455 3.857 2.257 0.157  0.091  -0.271 99  THR DDD CB  
5616  O OG1 . THR D 99  ? 3.425 3.831 2.235 0.172  0.074  -0.250 99  THR DDD OG1 
5617  C CG2 . THR D 99  ? 3.460 3.867 2.262 0.156  0.102  -0.276 99  THR DDD CG2 
5618  N N   . GLU D 100 ? 3.334 3.742 2.225 0.199  0.090  -0.266 100 GLU DDD N   
5619  C CA  . GLU D 100 ? 3.283 3.698 2.211 0.219  0.090  -0.260 100 GLU DDD CA  
5620  C C   . GLU D 100 ? 3.235 3.659 2.158 0.228  0.080  -0.243 100 GLU DDD C   
5621  O O   . GLU D 100 ? 3.211 3.642 2.163 0.244  0.079  -0.237 100 GLU DDD O   
5622  C CB  . GLU D 100 ? 3.279 3.693 2.229 0.228  0.081  -0.253 100 GLU DDD CB  
5623  C CG  . GLU D 100 ? 3.302 3.708 2.262 0.221  0.091  -0.270 100 GLU DDD CG  
5624  C CD  . GLU D 100 ? 3.294 3.699 2.282 0.231  0.084  -0.264 100 GLU DDD CD  
5625  O OE1 . GLU D 100 ? 3.271 3.684 2.274 0.244  0.073  -0.247 100 GLU DDD OE1 
5626  O OE2 . GLU D 100 ? 3.309 3.705 2.305 0.225  0.090  -0.278 100 GLU DDD OE2 
5627  N N   . ASN D 101 ? 3.213 3.636 2.103 0.218  0.072  -0.236 101 ASN DDD N   
5628  C CA  . ASN D 101 ? 3.181 3.611 2.063 0.225  0.061  -0.220 101 ASN DDD CA  
5629  C C   . ASN D 101 ? 3.174 3.607 2.059 0.226  0.071  -0.226 101 ASN DDD C   
5630  O O   . ASN D 101 ? 3.187 3.614 2.046 0.210  0.079  -0.236 101 ASN DDD O   
5631  C CB  . ASN D 101 ? 3.185 3.612 2.031 0.213  0.047  -0.210 101 ASN DDD CB  
5632  C CG  . ASN D 101 ? 3.160 3.593 2.000 0.222  0.033  -0.193 101 ASN DDD CG  
5633  O OD1 . ASN D 101 ? 3.138 3.578 1.998 0.236  0.033  -0.189 101 ASN DDD OD1 
5634  N ND2 . ASN D 101 ? 3.158 3.589 1.972 0.214  0.018  -0.184 101 ASN DDD ND2 
5635  N N   . VAL D 102 ? 3.151 3.591 2.063 0.243  0.072  -0.221 102 VAL DDD N   
5636  C CA  . VAL D 102 ? 3.143 3.588 2.061 0.246  0.080  -0.225 102 VAL DDD CA  
5637  C C   . VAL D 102 ? 3.135 3.582 2.029 0.244  0.067  -0.211 102 VAL DDD C   
5638  O O   . VAL D 102 ? 3.125 3.577 2.027 0.257  0.053  -0.195 102 VAL DDD O   
5639  C CB  . VAL D 102 ? 3.119 3.571 2.077 0.265  0.083  -0.223 102 VAL DDD CB  
5640  C CG1 . VAL D 102 ? 3.117 3.574 2.080 0.269  0.091  -0.225 102 VAL DDD CG1 
5641  C CG2 . VAL D 102 ? 3.121 3.570 2.104 0.267  0.094  -0.236 102 VAL DDD CG2 
5642  N N   . ARG D 103 ? 3.139 3.582 2.007 0.229  0.072  -0.216 103 ARG DDD N   
5643  C CA  . ARG D 103 ? 3.136 3.579 1.979 0.225  0.060  -0.204 103 ARG DDD CA  
5644  C C   . ARG D 103 ? 3.154 3.600 1.999 0.226  0.068  -0.208 103 ARG DDD C   
5645  O O   . ARG D 103 ? 3.163 3.607 2.002 0.214  0.084  -0.223 103 ARG DDD O   
5646  C CB  . ARG D 103 ? 3.142 3.576 1.946 0.205  0.055  -0.205 103 ARG DDD CB  
5647  C CG  . ARG D 103 ? 3.133 3.564 1.934 0.203  0.047  -0.201 103 ARG DDD CG  
5648  C CD  . ARG D 103 ? 3.107 3.542 1.911 0.216  0.026  -0.183 103 ARG DDD CD  
5649  N NE  . ARG D 103 ? 3.108 3.542 1.886 0.209  0.014  -0.173 103 ARG DDD NE  
5650  C CZ  . ARG D 103 ? 3.090 3.529 1.874 0.222  0.000  -0.159 103 ARG DDD CZ  
5651  N NH1 . ARG D 103 ? 3.063 3.512 1.877 0.242  -0.005 -0.152 103 ARG DDD NH1 
5652  N NH2 . ARG D 103 ? 3.106 3.541 1.864 0.214  -0.012 -0.151 103 ARG DDD NH2 
5653  N N   . SER D 104 ? 3.021 3.163 1.807 -0.038 -0.044 -0.059 104 SER DDD N   
5654  C CA  . SER D 104 ? 3.055 3.199 1.854 -0.035 -0.054 -0.059 104 SER DDD CA  
5655  C C   . SER D 104 ? 3.066 3.217 1.883 -0.035 -0.048 -0.065 104 SER DDD C   
5656  O O   . SER D 104 ? 3.073 3.223 1.913 -0.034 -0.048 -0.065 104 SER DDD O   
5657  C CB  . SER D 104 ? 3.067 3.212 1.849 -0.035 -0.064 -0.059 104 SER DDD CB  
5658  O OG  . SER D 104 ? 3.066 3.215 1.861 -0.033 -0.072 -0.062 104 SER DDD OG  
5659  N N   . LEU D 105 ? 3.087 3.243 1.894 -0.038 -0.043 -0.071 105 LEU DDD N   
5660  C CA  . LEU D 105 ? 3.101 3.263 1.920 -0.040 -0.036 -0.076 105 LEU DDD CA  
5661  C C   . LEU D 105 ? 3.131 3.289 1.957 -0.043 -0.025 -0.077 105 LEU DDD C   
5662  O O   . LEU D 105 ? 3.165 3.320 1.978 -0.046 -0.019 -0.077 105 LEU DDD O   
5663  C CB  . LEU D 105 ? 3.092 3.260 1.896 -0.043 -0.033 -0.080 105 LEU DDD CB  
5664  C CG  . LEU D 105 ? 3.077 3.252 1.891 -0.046 -0.028 -0.084 105 LEU DDD CG  
5665  C CD1 . LEU D 105 ? 3.071 3.248 1.900 -0.043 -0.035 -0.085 105 LEU DDD CD1 
5666  C CD2 . LEU D 105 ? 3.068 3.248 1.871 -0.050 -0.025 -0.085 105 LEU DDD CD2 
5667  N N   . LEU D 106 ? 3.135 3.292 1.982 -0.043 -0.021 -0.079 106 LEU DDD N   
5668  C CA  . LEU D 106 ? 3.124 3.277 1.981 -0.047 -0.008 -0.081 106 LEU DDD CA  
5669  C C   . LEU D 106 ? 3.106 3.261 1.949 -0.054 0.001  -0.086 106 LEU DDD C   
5670  O O   . LEU D 106 ? 3.095 3.246 1.931 -0.059 0.009  -0.087 106 LEU DDD O   
5671  C CB  . LEU D 106 ? 3.125 3.276 2.009 -0.044 -0.006 -0.082 106 LEU DDD CB  
5672  C CG  . LEU D 106 ? 3.125 3.271 2.022 -0.049 0.009  -0.087 106 LEU DDD CG  
5673  C CD1 . LEU D 106 ? 3.127 3.265 2.017 -0.051 0.014  -0.085 106 LEU DDD CD1 
5674  C CD2 . LEU D 106 ? 3.129 3.271 2.057 -0.046 0.012  -0.087 106 LEU DDD CD2 
5675  N N   . SER D 107 ? 3.085 3.248 1.927 -0.055 -0.001 -0.089 107 SER DDD N   
5676  C CA  . SER D 107 ? 3.081 3.247 1.912 -0.063 0.006  -0.092 107 SER DDD CA  
5677  C C   . SER D 107 ? 3.105 3.271 1.917 -0.068 0.008  -0.091 107 SER DDD C   
5678  O O   . SER D 107 ? 3.118 3.284 1.922 -0.076 0.014  -0.093 107 SER DDD O   
5679  C CB  . SER D 107 ? 3.050 3.225 1.884 -0.063 0.000  -0.092 107 SER DDD CB  
5680  O OG  . SER D 107 ? 3.024 3.203 1.849 -0.060 -0.009 -0.090 107 SER DDD OG  
5681  N N   . ASP D 108 ? 3.133 3.298 1.938 -0.063 0.002  -0.087 108 ASP DDD N   
5682  C CA  . ASP D 108 ? 3.157 3.321 1.946 -0.066 0.003  -0.085 108 ASP DDD CA  
5683  C C   . ASP D 108 ? 3.164 3.321 1.950 -0.072 0.013  -0.087 108 ASP DDD C   
5684  O O   . ASP D 108 ? 3.177 3.334 1.951 -0.077 0.015  -0.086 108 ASP DDD O   
5685  C CB  . ASP D 108 ? 3.184 3.344 1.967 -0.060 -0.003 -0.081 108 ASP DDD CB  
5686  C CG  . ASP D 108 ? 3.195 3.361 1.971 -0.057 -0.010 -0.080 108 ASP DDD CG  
5687  O OD1 . ASP D 108 ? 3.192 3.365 1.970 -0.060 -0.010 -0.082 108 ASP DDD OD1 
5688  O OD2 . ASP D 108 ? 3.223 3.385 1.992 -0.053 -0.014 -0.077 108 ASP DDD OD2 
5689  N N   . TYR D 109 ? 3.160 3.312 1.959 -0.072 0.019  -0.089 109 TYR DDD N   
5690  C CA  . TYR D 109 ? 3.163 3.306 1.960 -0.077 0.029  -0.091 109 TYR DDD CA  
5691  C C   . TYR D 109 ? 3.145 3.288 1.933 -0.087 0.037  -0.096 109 TYR DDD C   
5692  O O   . TYR D 109 ? 3.136 3.272 1.924 -0.093 0.047  -0.100 109 TYR DDD O   
5693  C CB  . TYR D 109 ? 3.177 3.313 1.994 -0.072 0.032  -0.091 109 TYR DDD CB  
5694  C CG  . TYR D 109 ? 3.184 3.318 2.005 -0.065 0.024  -0.084 109 TYR DDD CG  
5695  C CD1 . TYR D 109 ? 3.201 3.333 2.009 -0.065 0.024  -0.081 109 TYR DDD CD1 
5696  C CD2 . TYR D 109 ? 3.191 3.325 2.028 -0.058 0.017  -0.081 109 TYR DDD CD2 
5697  C CE1 . TYR D 109 ? 3.230 3.359 2.038 -0.059 0.017  -0.074 109 TYR DDD CE1 
5698  C CE2 . TYR D 109 ? 3.224 3.355 2.062 -0.052 0.009  -0.073 109 TYR DDD CE2 
5699  C CZ  . TYR D 109 ? 3.242 3.370 2.064 -0.053 0.009  -0.070 109 TYR DDD CZ  
5700  O OH  . TYR D 109 ? 3.260 3.386 2.081 -0.049 0.000  -0.062 109 TYR DDD OH  
5701  N N   . ALA D 110 ? 3.126 3.276 1.908 -0.091 0.033  -0.096 110 ALA DDD N   
5702  C CA  . ALA D 110 ? 3.125 3.277 1.894 -0.102 0.037  -0.098 110 ALA DDD CA  
5703  C C   . ALA D 110 ? 3.124 3.281 1.881 -0.104 0.030  -0.093 110 ALA DDD C   
5704  O O   . ALA D 110 ? 3.127 3.280 1.876 -0.110 0.034  -0.093 110 ALA DDD O   
5705  C CB  . ALA D 110 ? 3.115 3.272 1.886 -0.106 0.036  -0.100 110 ALA DDD CB  
5706  N N   . THR D 111 ? 3.130 3.295 1.890 -0.099 0.021  -0.089 111 THR DDD N   
5707  C CA  . THR D 111 ? 3.143 3.312 1.897 -0.099 0.016  -0.084 111 THR DDD CA  
5708  C C   . THR D 111 ? 3.158 3.322 1.906 -0.098 0.019  -0.083 111 THR DDD C   
5709  O O   . THR D 111 ? 3.157 3.321 1.898 -0.105 0.020  -0.081 111 THR DDD O   
5710  C CB  . THR D 111 ? 3.132 3.308 1.893 -0.090 0.009  -0.082 111 THR DDD CB  
5711  O OG1 . THR D 111 ? 3.134 3.317 1.900 -0.092 0.005  -0.082 111 THR DDD OG1 
5712  C CG2 . THR D 111 ? 3.116 3.295 1.873 -0.088 0.006  -0.078 111 THR DDD CG2 
5713  N N   . TRP D 112 ? 3.166 3.324 1.918 -0.091 0.020  -0.083 112 TRP DDD N   
5714  C CA  . TRP D 112 ? 3.163 3.316 1.911 -0.087 0.021  -0.080 112 TRP DDD CA  
5715  C C   . TRP D 112 ? 3.162 3.308 1.907 -0.094 0.029  -0.082 112 TRP DDD C   
5716  O O   . TRP D 112 ? 3.155 3.298 1.902 -0.099 0.035  -0.087 112 TRP DDD O   
5717  C CB  . TRP D 112 ? 3.169 3.319 1.922 -0.078 0.018  -0.078 112 TRP DDD CB  
5718  C CG  . TRP D 112 ? 3.175 3.330 1.925 -0.073 0.011  -0.076 112 TRP DDD CG  
5719  C CD1 . TRP D 112 ? 3.165 3.327 1.919 -0.071 0.006  -0.077 112 TRP DDD CD1 
5720  C CD2 . TRP D 112 ? 3.194 3.348 1.936 -0.068 0.009  -0.072 112 TRP DDD CD2 
5721  N NE1 . TRP D 112 ? 3.177 3.341 1.926 -0.067 0.001  -0.076 112 TRP DDD NE1 
5722  C CE2 . TRP D 112 ? 3.193 3.352 1.934 -0.065 0.003  -0.073 112 TRP DDD CE2 
5723  C CE3 . TRP D 112 ? 3.202 3.350 1.937 -0.068 0.011  -0.068 112 TRP DDD CE3 
5724  C CZ2 . TRP D 112 ? 3.200 3.357 1.931 -0.062 0.001  -0.071 112 TRP DDD CZ2 
5725  C CZ3 . TRP D 112 ? 3.208 3.355 1.933 -0.064 0.009  -0.065 112 TRP DDD CZ3 
5726  C CH2 . TRP D 112 ? 3.208 3.359 1.931 -0.062 0.004  -0.067 112 TRP DDD CH2 
5727  N N   . PRO D 113 ? 3.155 3.298 1.896 -0.093 0.030  -0.079 113 PRO DDD N   
5728  C CA  . PRO D 113 ? 3.167 3.303 1.905 -0.100 0.037  -0.080 113 PRO DDD CA  
5729  C C   . PRO D 113 ? 3.192 3.320 1.938 -0.095 0.042  -0.081 113 PRO DDD C   
5730  O O   . PRO D 113 ? 3.184 3.312 1.936 -0.087 0.038  -0.078 113 PRO DDD O   
5731  C CB  . PRO D 113 ? 3.153 3.292 1.885 -0.101 0.035  -0.075 113 PRO DDD CB  
5732  C CG  . PRO D 113 ? 3.150 3.290 1.883 -0.091 0.031  -0.071 113 PRO DDD CG  
5733  C CD  . PRO D 113 ? 3.148 3.292 1.885 -0.087 0.026  -0.073 113 PRO DDD CD  
5734  N N   . TYR D 114 ? 3.233 3.353 1.981 -0.101 0.050  -0.085 114 TYR DDD N   
5735  C CA  . TYR D 114 ? 3.268 3.379 2.027 -0.098 0.056  -0.085 114 TYR DDD CA  
5736  C C   . TYR D 114 ? 3.297 3.404 2.054 -0.100 0.059  -0.082 114 TYR DDD C   
5737  O O   . TYR D 114 ? 3.305 3.412 2.052 -0.108 0.061  -0.085 114 TYR DDD O   
5738  C CB  . TYR D 114 ? 3.277 3.383 2.044 -0.103 0.065  -0.094 114 TYR DDD CB  
5739  C CG  . TYR D 114 ? 3.272 3.382 2.047 -0.099 0.062  -0.096 114 TYR DDD CG  
5740  C CD1 . TYR D 114 ? 3.264 3.382 2.029 -0.102 0.057  -0.096 114 TYR DDD CD1 
5741  C CD2 . TYR D 114 ? 3.277 3.383 2.071 -0.093 0.065  -0.096 114 TYR DDD CD2 
5742  C CE1 . TYR D 114 ? 3.258 3.380 2.031 -0.099 0.055  -0.098 114 TYR DDD CE1 
5743  C CE2 . TYR D 114 ? 3.277 3.386 2.080 -0.090 0.062  -0.097 114 TYR DDD CE2 
5744  C CZ  . TYR D 114 ? 3.268 3.385 2.059 -0.093 0.058  -0.098 114 TYR DDD CZ  
5745  O OH  . TYR D 114 ? 3.268 3.388 2.070 -0.089 0.056  -0.100 114 TYR DDD OH  
5746  N N   . ASP D 115 ? 3.327 3.430 2.092 -0.093 0.058  -0.077 115 ASP DDD N   
5747  C CA  . ASP D 115 ? 3.353 3.452 2.117 -0.093 0.061  -0.072 115 ASP DDD CA  
5748  C C   . ASP D 115 ? 3.387 3.476 2.158 -0.100 0.071  -0.078 115 ASP DDD C   
5749  O O   . ASP D 115 ? 3.394 3.481 2.160 -0.105 0.074  -0.078 115 ASP DDD O   
5750  C CB  . ASP D 115 ? 3.351 3.448 2.120 -0.084 0.056  -0.063 115 ASP DDD CB  
5751  C CG  . ASP D 115 ? 3.340 3.444 2.097 -0.078 0.047  -0.057 115 ASP DDD CG  
5752  O OD1 . ASP D 115 ? 3.339 3.446 2.085 -0.080 0.046  -0.055 115 ASP DDD OD1 
5753  O OD2 . ASP D 115 ? 3.320 3.424 2.081 -0.073 0.041  -0.055 115 ASP DDD OD2 
5754  N N   . TYR D 116 ? 3.417 3.502 2.202 -0.100 0.077  -0.084 116 TYR DDD N   
5755  C CA  . TYR D 116 ? 3.441 3.515 2.236 -0.106 0.089  -0.091 116 TYR DDD CA  
5756  C C   . TYR D 116 ? 3.461 3.533 2.253 -0.115 0.096  -0.102 116 TYR DDD C   
5757  O O   . TYR D 116 ? 3.490 3.566 2.284 -0.112 0.094  -0.104 116 TYR DDD O   
5758  C CB  . TYR D 116 ? 3.443 3.511 2.263 -0.099 0.092  -0.087 116 TYR DDD CB  
5759  C CG  . TYR D 116 ? 3.442 3.513 2.264 -0.090 0.082  -0.074 116 TYR DDD CG  
5760  C CD1 . TYR D 116 ? 3.436 3.513 2.255 -0.082 0.072  -0.067 116 TYR DDD CD1 
5761  C CD2 . TYR D 116 ? 3.448 3.514 2.273 -0.090 0.084  -0.069 116 TYR DDD CD2 
5762  C CE1 . TYR D 116 ? 3.429 3.507 2.246 -0.076 0.063  -0.055 116 TYR DDD CE1 
5763  C CE2 . TYR D 116 ? 3.444 3.512 2.268 -0.083 0.077  -0.056 116 TYR DDD CE2 
5764  C CZ  . TYR D 116 ? 3.432 3.505 2.250 -0.076 0.066  -0.050 116 TYR DDD CZ  
5765  O OH  . TYR D 116 ? 3.411 3.485 2.225 -0.071 0.059  -0.038 116 TYR DDD OH  
5766  N N   . TRP D 117 ? 3.469 3.534 2.255 -0.126 0.106  -0.111 117 TRP DDD N   
5767  C CA  . TRP D 117 ? 3.472 3.532 2.249 -0.137 0.114  -0.123 117 TRP DDD CA  
5768  C C   . TRP D 117 ? 3.498 3.545 2.287 -0.144 0.130  -0.133 117 TRP DDD C   
5769  O O   . TRP D 117 ? 3.523 3.565 2.315 -0.145 0.132  -0.131 117 TRP DDD O   
5770  C CB  . TRP D 117 ? 3.455 3.520 2.207 -0.148 0.109  -0.124 117 TRP DDD CB  
5771  C CG  . TRP D 117 ? 3.424 3.502 2.168 -0.143 0.096  -0.117 117 TRP DDD CG  
5772  C CD1 . TRP D 117 ? 3.397 3.483 2.140 -0.135 0.086  -0.106 117 TRP DDD CD1 
5773  C CD2 . TRP D 117 ? 3.421 3.503 2.157 -0.146 0.094  -0.120 117 TRP DDD CD2 
5774  N NE1 . TRP D 117 ? 3.385 3.480 2.122 -0.133 0.077  -0.103 117 TRP DDD NE1 
5775  C CE2 . TRP D 117 ? 3.400 3.494 2.133 -0.140 0.082  -0.111 117 TRP DDD CE2 
5776  C CE3 . TRP D 117 ? 3.431 3.508 2.162 -0.155 0.103  -0.129 117 TRP DDD CE3 
5777  C CZ2 . TRP D 117 ? 3.397 3.498 2.125 -0.140 0.076  -0.110 117 TRP DDD CZ2 
5778  C CZ3 . TRP D 117 ? 3.423 3.508 2.147 -0.156 0.097  -0.128 117 TRP DDD CZ3 
5779  C CH2 . TRP D 117 ? 3.409 3.506 2.133 -0.148 0.084  -0.118 117 TRP DDD CH2 
5780  N N   . GLY D 118 ? 3.503 3.543 2.296 -0.149 0.141  -0.143 118 GLY DDD N   
5781  C CA  . GLY D 118 ? 3.522 3.548 2.323 -0.158 0.159  -0.155 118 GLY DDD CA  
5782  C C   . GLY D 118 ? 3.543 3.563 2.315 -0.175 0.163  -0.165 118 GLY DDD C   
5783  O O   . GLY D 118 ? 3.543 3.572 2.292 -0.180 0.152  -0.161 118 GLY DDD O   
5784  N N   . GLN D 119 ? 3.555 3.562 2.328 -0.185 0.177  -0.176 119 GLN DDD N   
5785  C CA  . GLN D 119 ? 3.562 3.562 2.306 -0.203 0.181  -0.186 119 GLN DDD CA  
5786  C C   . GLN D 119 ? 3.581 3.579 2.305 -0.214 0.186  -0.194 119 GLN DDD C   
5787  O O   . GLN D 119 ? 3.588 3.585 2.282 -0.229 0.182  -0.198 119 GLN DDD O   
5788  C CB  . GLN D 119 ? 3.556 3.541 2.308 -0.211 0.195  -0.196 119 GLN DDD CB  
5789  C CG  . GLN D 119 ? 3.552 3.524 2.325 -0.213 0.217  -0.209 119 GLN DDD CG  
5790  C CD  . GLN D 119 ? 3.552 3.510 2.337 -0.218 0.230  -0.218 119 GLN DDD CD  
5791  O OE1 . GLN D 119 ? 3.534 3.494 2.318 -0.218 0.223  -0.212 119 GLN DDD OE1 
5792  N NE2 . GLN D 119 ? 3.562 3.507 2.363 -0.223 0.251  -0.232 119 GLN DDD NE2 
5793  N N   . GLY D 120 ? 3.586 3.585 2.327 -0.207 0.193  -0.196 120 GLY DDD N   
5794  C CA  . GLY D 120 ? 3.600 3.598 2.325 -0.215 0.198  -0.203 120 GLY DDD CA  
5795  C C   . GLY D 120 ? 3.635 3.615 2.359 -0.227 0.222  -0.221 120 GLY DDD C   
5796  O O   . GLY D 120 ? 3.653 3.622 2.387 -0.230 0.232  -0.228 120 GLY DDD O   
5797  N N   . THR D 121 ? 3.651 3.627 2.364 -0.235 0.230  -0.228 121 THR DDD N   
5798  C CA  . THR D 121 ? 3.690 3.649 2.401 -0.248 0.255  -0.247 121 THR DDD CA  
5799  C C   . THR D 121 ? 3.725 3.682 2.403 -0.262 0.258  -0.252 121 THR DDD C   
5800  O O   . THR D 121 ? 3.724 3.694 2.400 -0.255 0.246  -0.242 121 THR DDD O   
5801  C CB  . THR D 121 ? 3.676 3.630 2.432 -0.236 0.271  -0.250 121 THR DDD CB  
5802  O OG1 . THR D 121 ? 3.710 3.644 2.469 -0.247 0.295  -0.268 121 THR DDD OG1 
5803  C CG2 . THR D 121 ? 3.661 3.619 2.428 -0.230 0.275  -0.250 121 THR DDD CG2 
5804  N N   . GLN D 122 ? 3.766 3.706 2.418 -0.282 0.275  -0.268 122 GLN DDD N   
5805  C CA  . GLN D 122 ? 3.795 3.732 2.408 -0.300 0.278  -0.274 122 GLN DDD CA  
5806  C C   . GLN D 122 ? 3.832 3.763 2.462 -0.298 0.298  -0.282 122 GLN DDD C   
5807  O O   . GLN D 122 ? 3.831 3.750 2.488 -0.295 0.319  -0.294 122 GLN DDD O   
5808  C CB  . GLN D 122 ? 3.811 3.731 2.386 -0.324 0.287  -0.287 122 GLN DDD CB  
5809  C CG  . GLN D 122 ? 3.820 3.736 2.349 -0.346 0.288  -0.292 122 GLN DDD CG  
5810  C CD  . GLN D 122 ? 3.794 3.727 2.301 -0.347 0.260  -0.274 122 GLN DDD CD  
5811  O OE1 . GLN D 122 ? 3.757 3.698 2.262 -0.344 0.241  -0.264 122 GLN DDD OE1 
5812  N NE2 . GLN D 122 ? 3.799 3.737 2.290 -0.351 0.257  -0.271 122 GLN DDD NE2 
5813  N N   . VAL D 123 ? 3.872 3.813 2.490 -0.298 0.290  -0.275 123 VAL DDD N   
5814  C CA  . VAL D 123 ? 3.913 3.847 2.533 -0.302 0.308  -0.284 123 VAL DDD CA  
5815  C C   . VAL D 123 ? 3.973 3.902 2.542 -0.325 0.308  -0.288 123 VAL DDD C   
5816  O O   . VAL D 123 ? 3.993 3.936 2.540 -0.326 0.285  -0.274 123 VAL DDD O   
5817  C CB  . VAL D 123 ? 3.876 3.826 2.529 -0.282 0.299  -0.271 123 VAL DDD CB  
5818  C CG1 . VAL D 123 ? 3.874 3.817 2.531 -0.286 0.318  -0.280 123 VAL DDD CG1 
5819  C CG2 . VAL D 123 ? 3.855 3.811 2.556 -0.260 0.295  -0.265 123 VAL DDD CG2 
5820  N N   . THR D 124 ? 4.021 3.930 2.571 -0.343 0.334  -0.306 124 THR DDD N   
5821  C CA  . THR D 124 ? 4.052 3.952 2.549 -0.368 0.337  -0.312 124 THR DDD CA  
5822  C C   . THR D 124 ? 4.081 3.973 2.581 -0.372 0.360  -0.321 124 THR DDD C   
5823  O O   . THR D 124 ? 4.118 3.995 2.638 -0.374 0.388  -0.338 124 THR DDD O   
5824  C CB  . THR D 124 ? 4.068 3.950 2.530 -0.390 0.347  -0.326 124 THR DDD CB  
5825  O OG1 . THR D 124 ? 4.075 3.939 2.561 -0.390 0.377  -0.345 124 THR DDD OG1 
5826  C CG2 . THR D 124 ? 4.033 3.922 2.494 -0.386 0.325  -0.317 124 THR DDD CG2 
5827  N N   . VAL D 125 ? 4.073 3.976 2.558 -0.373 0.348  -0.311 125 VAL DDD N   
5828  C CA  . VAL D 125 ? 4.075 3.972 2.563 -0.377 0.368  -0.317 125 VAL DDD CA  
5829  C C   . VAL D 125 ? 4.104 3.983 2.535 -0.408 0.382  -0.330 125 VAL DDD C   
5830  O O   . VAL D 125 ? 4.102 3.986 2.490 -0.421 0.362  -0.320 125 VAL DDD O   
5831  C CB  . VAL D 125 ? 4.051 3.969 2.553 -0.363 0.349  -0.300 125 VAL DDD CB  
5832  C CG1 . VAL D 125 ? 4.024 3.947 2.583 -0.341 0.358  -0.299 125 VAL DDD CG1 
5833  C CG2 . VAL D 125 ? 4.022 3.960 2.518 -0.355 0.314  -0.280 125 VAL DDD CG2 
5834  N N   . SER D 126 ? 4.118 3.977 2.548 -0.418 0.416  -0.349 126 SER DDD N   
5835  C CA  . SER D 126 ? 4.157 3.992 2.533 -0.449 0.436  -0.367 126 SER DDD CA  
5836  C C   . SER D 126 ? 4.148 3.975 2.512 -0.459 0.457  -0.373 126 SER DDD C   
5837  O O   . SER D 126 ? 4.146 3.990 2.523 -0.448 0.443  -0.358 126 SER DDD O   
5838  C CB  . SER D 126 ? 4.185 4.000 2.569 -0.455 0.461  -0.387 126 SER DDD CB  
5839  O OG  . SER D 126 ? 4.195 3.999 2.621 -0.446 0.492  -0.401 126 SER DDD OG  
5840  N N   . SER D 127 ? 4.128 3.930 2.465 -0.481 0.490  -0.395 127 SER DDD N   
5841  C CA  . SER D 127 ? 4.105 3.894 2.428 -0.493 0.517  -0.405 127 SER DDD CA  
5842  C C   . SER D 127 ? 4.112 3.874 2.445 -0.503 0.559  -0.432 127 SER DDD C   
5843  O O   . SER D 127 ? 4.081 3.836 2.445 -0.498 0.587  -0.442 127 SER DDD O   
5844  C CB  . SER D 127 ? 4.120 3.905 2.374 -0.520 0.506  -0.400 127 SER DDD CB  
5845  O OG  . SER D 127 ? 4.077 3.887 2.331 -0.509 0.471  -0.375 127 SER DDD OG  
5846  N N   . ASN E 5   ? 1.793 2.589 2.729 0.534  0.532  0.312  334 ASN EEE N   
5847  C CA  . ASN E 5   ? 1.815 2.455 2.586 0.539  0.509  0.281  334 ASN EEE CA  
5848  C C   . ASN E 5   ? 1.792 2.371 2.502 0.466  0.479  0.274  334 ASN EEE C   
5849  O O   . ASN E 5   ? 1.835 2.335 2.438 0.452  0.514  0.268  334 ASN EEE O   
5850  C CB  . ASN E 5   ? 1.900 2.448 2.547 0.593  0.571  0.269  334 ASN EEE CB  
5851  C CG  . ASN E 5   ? 1.950 2.552 2.625 0.612  0.651  0.288  334 ASN EEE CG  
5852  O OD1 . ASN E 5   ? 1.909 2.554 2.619 0.562  0.670  0.304  334 ASN EEE OD1 
5853  N ND2 . ASN E 5   ? 2.037 2.633 2.689 0.686  0.702  0.286  334 ASN EEE ND2 
5854  N N   . LEU E 6   ? 1.754 2.366 2.527 0.425  0.414  0.275  335 LEU EEE N   
5855  C CA  . LEU E 6   ? 1.735 2.296 2.461 0.362  0.378  0.268  335 LEU EEE CA  
5856  C C   . LEU E 6   ? 1.730 2.208 2.379 0.362  0.322  0.244  335 LEU EEE C   
5857  O O   . LEU E 6   ? 1.714 2.227 2.421 0.378  0.278  0.242  335 LEU EEE O   
5858  C CB  . LEU E 6   ? 1.696 2.356 2.552 0.316  0.353  0.290  335 LEU EEE CB  
5859  C CG  . LEU E 6   ? 1.668 2.282 2.497 0.260  0.298  0.282  335 LEU EEE CG  
5860  C CD1 . LEU E 6   ? 1.680 2.202 2.391 0.235  0.320  0.274  335 LEU EEE CD1 
5861  C CD2 . LEU E 6   ? 1.647 2.351 2.600 0.215  0.274  0.305  335 LEU EEE CD2 
5862  N N   . CYS E 7   ? 1.758 2.135 2.285 0.342  0.321  0.228  336 CYS EEE N   
5863  C CA  . CYS E 7   ? 1.773 2.065 2.211 0.343  0.280  0.206  336 CYS EEE CA  
5864  C C   . CYS E 7   ? 1.731 2.057 2.232 0.324  0.217  0.204  336 CYS EEE C   
5865  O O   . CYS E 7   ? 1.688 2.032 2.219 0.282  0.196  0.209  336 CYS EEE O   
5866  C CB  . CYS E 7   ? 1.786 1.991 2.110 0.313  0.286  0.195  336 CYS EEE CB  
5867  S SG  . CYS E 7   ? 1.882 2.010 2.092 0.333  0.347  0.190  336 CYS EEE SG  
5868  N N   . PRO E 8   ? 1.763 2.088 2.273 0.356  0.186  0.197  337 PRO EEE N   
5869  C CA  . PRO E 8   ? 1.737 2.086 2.296 0.342  0.124  0.194  337 PRO EEE CA  
5870  C C   . PRO E 8   ? 1.718 1.982 2.179 0.320  0.094  0.176  337 PRO EEE C   
5871  O O   . PRO E 8   ? 1.741 1.954 2.144 0.342  0.074  0.164  337 PRO EEE O   
5872  C CB  . PRO E 8   ? 1.777 2.150 2.370 0.392  0.109  0.195  337 PRO EEE CB  
5873  C CG  . PRO E 8   ? 1.828 2.127 2.321 0.429  0.151  0.186  337 PRO EEE CG  
5874  C CD  . PRO E 8   ? 1.826 2.115 2.290 0.409  0.205  0.191  337 PRO EEE CD  
5875  N N   . PHE E 9   ? 1.680 1.930 2.124 0.279  0.093  0.176  338 PHE EEE N   
5876  C CA  . PHE E 9   ? 1.667 1.861 2.049 0.257  0.059  0.162  338 PHE EEE CA  
5877  C C   . PHE E 9   ? 1.657 1.879 2.096 0.249  0.005  0.161  338 PHE EEE C   
5878  O O   . PHE E 9   ? 1.650 1.823 2.034 0.246  -0.028 0.147  338 PHE EEE O   
5879  C CB  . PHE E 9   ? 1.665 1.840 2.016 0.223  0.078  0.164  338 PHE EEE CB  
5880  C CG  . PHE E 9   ? 1.698 1.835 1.978 0.227  0.123  0.164  338 PHE EEE CG  
5881  C CD1 . PHE E 9   ? 1.714 1.793 1.910 0.244  0.129  0.151  338 PHE EEE CD1 
5882  C CD2 . PHE E 9   ? 1.715 1.868 2.005 0.211  0.158  0.176  338 PHE EEE CD2 
5883  C CE1 . PHE E 9   ? 1.744 1.778 1.867 0.243  0.165  0.150  338 PHE EEE CE1 
5884  C CE2 . PHE E 9   ? 1.757 1.865 1.970 0.213  0.195  0.174  338 PHE EEE CE2 
5885  C CZ  . PHE E 9   ? 1.770 1.818 1.900 0.228  0.196  0.161  338 PHE EEE CZ  
5886  N N   . GLY E 10  ? 1.667 1.964 2.211 0.245  -0.004 0.176  339 GLY EEE N   
5887  C CA  . GLY E 10  ? 1.688 2.019 2.297 0.234  -0.060 0.177  339 GLY EEE CA  
5888  C C   . GLY E 10  ? 1.736 2.024 2.295 0.262  -0.100 0.163  339 GLY EEE C   
5889  O O   . GLY E 10  ? 1.813 2.069 2.350 0.246  -0.147 0.153  339 GLY EEE O   
5890  N N   . GLU E 11  ? 1.750 2.025 2.279 0.302  -0.081 0.161  340 GLU EEE N   
5891  C CA  . GLU E 11  ? 1.775 2.005 2.251 0.332  -0.117 0.150  340 GLU EEE CA  
5892  C C   . GLU E 11  ? 1.721 1.856 2.068 0.334  -0.102 0.134  340 GLU EEE C   
5893  O O   . GLU E 11  ? 1.735 1.822 2.021 0.363  -0.109 0.128  340 GLU EEE O   
5894  C CB  . GLU E 11  ? 1.860 2.131 2.383 0.378  -0.110 0.160  340 GLU EEE CB  
5895  C CG  . GLU E 11  ? 1.924 2.174 2.405 0.404  -0.048 0.162  340 GLU EEE CG  
5896  C CD  . GLU E 11  ? 1.994 2.289 2.528 0.455  -0.035 0.173  340 GLU EEE CD  
5897  O OE1 . GLU E 11  ? 2.008 2.370 2.614 0.463  0.006  0.186  340 GLU EEE OE1 
5898  O OE2 . GLU E 11  ? 2.062 2.324 2.564 0.490  -0.064 0.169  340 GLU EEE OE2 
5899  N N   . VAL E 12  ? 1.648 1.759 1.958 0.303  -0.083 0.129  341 VAL EEE N   
5900  C CA  . VAL E 12  ? 1.643 1.680 1.846 0.297  -0.071 0.117  341 VAL EEE CA  
5901  C C   . VAL E 12  ? 1.601 1.622 1.789 0.272  -0.098 0.109  341 VAL EEE C   
5902  O O   . VAL E 12  ? 1.636 1.611 1.763 0.278  -0.122 0.098  341 VAL EEE O   
5903  C CB  . VAL E 12  ? 1.637 1.660 1.802 0.290  -0.020 0.120  341 VAL EEE CB  
5904  C CG1 . VAL E 12  ? 1.642 1.604 1.712 0.278  -0.012 0.110  341 VAL EEE CG1 
5905  C CG2 . VAL E 12  ? 1.668 1.690 1.833 0.320  0.008  0.125  341 VAL EEE CG2 
5906  N N   . PHE E 13  ? 1.527 1.579 1.761 0.246  -0.091 0.115  342 PHE EEE N   
5907  C CA  . PHE E 13  ? 1.518 1.550 1.738 0.223  -0.113 0.108  342 PHE EEE CA  
5908  C C   . PHE E 13  ? 1.570 1.600 1.816 0.223  -0.167 0.103  342 PHE EEE C   
5909  O O   . PHE E 13  ? 1.584 1.562 1.767 0.228  -0.192 0.090  342 PHE EEE O   
5910  C CB  . PHE E 13  ? 1.483 1.542 1.744 0.197  -0.092 0.119  342 PHE EEE CB  
5911  C CG  . PHE E 13  ? 1.440 1.489 1.659 0.194  -0.047 0.122  342 PHE EEE CG  
5912  C CD1 . PHE E 13  ? 1.430 1.497 1.656 0.203  -0.011 0.130  342 PHE EEE CD1 
5913  C CD2 . PHE E 13  ? 1.431 1.450 1.600 0.184  -0.043 0.117  342 PHE EEE CD2 
5914  C CE1 . PHE E 13  ? 1.431 1.479 1.608 0.197  0.024  0.131  342 PHE EEE CE1 
5915  C CE2 . PHE E 13  ? 1.414 1.428 1.547 0.178  -0.009 0.121  342 PHE EEE CE2 
5916  C CZ  . PHE E 13  ? 1.420 1.444 1.553 0.181  0.022  0.127  342 PHE EEE CZ  
5917  N N   . ASN E 14  ? 1.629 1.715 1.966 0.215  -0.183 0.115  343 ASN EEE N   
5918  C CA  . ASN E 14  ? 1.723 1.817 2.100 0.206  -0.241 0.114  343 ASN EEE CA  
5919  C C   . ASN E 14  ? 1.755 1.834 2.106 0.238  -0.269 0.108  343 ASN EEE C   
5920  O O   . ASN E 14  ? 1.794 1.872 2.166 0.233  -0.324 0.105  343 ASN EEE O   
5921  C CB  . ASN E 14  ? 1.764 1.937 2.259 0.182  -0.246 0.133  343 ASN EEE CB  
5922  C CG  . ASN E 14  ? 1.823 1.990 2.332 0.144  -0.242 0.139  343 ASN EEE CG  
5923  O OD1 . ASN E 14  ? 1.858 1.973 2.333 0.126  -0.280 0.129  343 ASN EEE OD1 
5924  N ND2 . ASN E 14  ? 1.930 2.139 2.481 0.132  -0.195 0.154  343 ASN EEE ND2 
5925  N N   . ALA E 15  ? 1.761 1.821 2.062 0.267  -0.238 0.106  344 ALA EEE N   
5926  C CA  . ALA E 15  ? 1.812 1.845 2.072 0.300  -0.261 0.102  344 ALA EEE CA  
5927  C C   . ALA E 15  ? 1.846 1.817 2.040 0.298  -0.311 0.087  344 ALA EEE C   
5928  O O   . ALA E 15  ? 1.854 1.774 1.979 0.286  -0.302 0.075  344 ALA EEE O   
5929  C CB  . ALA E 15  ? 1.827 1.820 2.012 0.321  -0.216 0.099  344 ALA EEE CB  
5930  N N   . THR E 16  ? 1.853 1.829 2.066 0.311  -0.363 0.088  345 THR EEE N   
5931  C CA  . THR E 16  ? 1.887 1.803 2.040 0.308  -0.423 0.075  345 THR EEE CA  
5932  C C   . THR E 16  ? 1.913 1.738 1.931 0.323  -0.406 0.060  345 THR EEE C   
5933  O O   . THR E 16  ? 1.899 1.674 1.858 0.310  -0.413 0.047  345 THR EEE O   
5934  C CB  . THR E 16  ? 1.923 1.866 2.121 0.323  -0.481 0.082  345 THR EEE CB  
5935  O OG1 . THR E 16  ? 1.928 1.901 2.147 0.358  -0.455 0.093  345 THR EEE OG1 
5936  C CG2 . THR E 16  ? 1.902 1.924 2.225 0.294  -0.518 0.093  345 THR EEE CG2 
5937  N N   . ARG E 17  ? 1.962 1.764 1.929 0.351  -0.383 0.063  346 ARG EEE N   
5938  C CA  . ARG E 17  ? 2.043 1.764 1.883 0.362  -0.361 0.053  346 ARG EEE CA  
5939  C C   . ARG E 17  ? 1.981 1.712 1.809 0.356  -0.295 0.058  346 ARG EEE C   
5940  O O   . ARG E 17  ? 1.962 1.743 1.857 0.358  -0.271 0.069  346 ARG EEE O   
5941  C CB  . ARG E 17  ? 2.165 1.839 1.944 0.392  -0.389 0.055  346 ARG EEE CB  
5942  C CG  . ARG E 17  ? 2.281 1.864 1.922 0.401  -0.382 0.046  346 ARG EEE CG  
5943  C CD  . ARG E 17  ? 2.396 1.923 1.970 0.429  -0.420 0.049  346 ARG EEE CD  
5944  N NE  . ARG E 17  ? 2.456 1.980 2.049 0.432  -0.490 0.044  346 ARG EEE NE  
5945  C CZ  . ARG E 17  ? 2.474 2.041 2.142 0.446  -0.537 0.054  346 ARG EEE CZ  
5946  N NH1 . ARG E 17  ? 2.445 2.060 2.175 0.466  -0.518 0.069  346 ARG EEE NH1 
5947  N NH2 . ARG E 17  ? 2.528 2.090 2.207 0.442  -0.606 0.048  346 ARG EEE NH2 
5948  N N   . PHE E 18  ? 1.965 1.652 1.711 0.350  -0.268 0.050  347 PHE EEE N   
5949  C CA  . PHE E 18  ? 1.919 1.609 1.640 0.340  -0.211 0.055  347 PHE EEE CA  
5950  C C   . PHE E 18  ? 1.965 1.592 1.583 0.352  -0.197 0.056  347 PHE EEE C   
5951  O O   . PHE E 18  ? 2.044 1.622 1.604 0.368  -0.229 0.052  347 PHE EEE O   
5952  C CB  . PHE E 18  ? 1.897 1.602 1.620 0.320  -0.188 0.050  347 PHE EEE CB  
5953  C CG  . PHE E 18  ? 1.840 1.606 1.650 0.302  -0.170 0.056  347 PHE EEE CG  
5954  C CD1 . PHE E 18  ? 1.827 1.631 1.719 0.296  -0.198 0.059  347 PHE EEE CD1 
5955  C CD2 . PHE E 18  ? 1.803 1.588 1.611 0.287  -0.126 0.062  347 PHE EEE CD2 
5956  C CE1 . PHE E 18  ? 1.779 1.634 1.744 0.278  -0.178 0.067  347 PHE EEE CE1 
5957  C CE2 . PHE E 18  ? 1.744 1.576 1.620 0.271  -0.111 0.068  347 PHE EEE CE2 
5958  C CZ  . PHE E 18  ? 1.741 1.606 1.693 0.267  -0.134 0.071  347 PHE EEE CZ  
5959  N N   . ALA E 19  ? 1.946 1.570 1.538 0.340  -0.152 0.063  348 ALA EEE N   
5960  C CA  . ALA E 19  ? 2.013 1.576 1.507 0.342  -0.132 0.068  348 ALA EEE CA  
5961  C C   . ALA E 19  ? 2.011 1.561 1.446 0.327  -0.109 0.065  348 ALA EEE C   
5962  O O   . ALA E 19  ? 1.937 1.530 1.414 0.316  -0.101 0.060  348 ALA EEE O   
5963  C CB  . ALA E 19  ? 2.019 1.582 1.517 0.333  -0.100 0.078  348 ALA EEE CB  
5964  N N   . SER E 20  ? 2.098 1.590 1.438 0.328  -0.098 0.070  349 SER EEE N   
5965  C CA  . SER E 20  ? 2.116 1.601 1.396 0.313  -0.064 0.072  349 SER EEE CA  
5966  C C   . SER E 20  ? 2.023 1.546 1.327 0.281  -0.023 0.082  349 SER EEE C   
5967  O O   . SER E 20  ? 1.993 1.498 1.298 0.274  -0.018 0.090  349 SER EEE O   
5968  C CB  . SER E 20  ? 2.257 1.666 1.426 0.322  -0.065 0.076  349 SER EEE CB  
5969  O OG  . SER E 20  ? 2.346 1.714 1.481 0.350  -0.107 0.065  349 SER EEE OG  
5970  N N   . VAL E 21  ? 1.960 1.529 1.278 0.265  0.005  0.084  350 VAL EEE N   
5971  C CA  . VAL E 21  ? 1.896 1.518 1.255 0.233  0.036  0.093  350 VAL EEE CA  
5972  C C   . VAL E 21  ? 1.926 1.506 1.233 0.208  0.053  0.107  350 VAL EEE C   
5973  O O   . VAL E 21  ? 1.949 1.535 1.287 0.194  0.055  0.109  350 VAL EEE O   
5974  C CB  . VAL E 21  ? 1.887 1.564 1.257 0.223  0.062  0.096  350 VAL EEE CB  
5975  C CG1 . VAL E 21  ? 1.975 1.625 1.266 0.222  0.084  0.103  350 VAL EEE CG1 
5976  C CG2 . VAL E 21  ? 1.838 1.575 1.260 0.190  0.084  0.106  350 VAL EEE CG2 
5977  N N   . TYR E 22  ? 1.977 1.506 1.199 0.201  0.065  0.115  351 TYR EEE N   
5978  C CA  . TYR E 22  ? 2.033 1.510 1.191 0.171  0.083  0.130  351 TYR EEE CA  
5979  C C   . TYR E 22  ? 2.041 1.451 1.179 0.187  0.061  0.128  351 TYR EEE C   
5980  O O   . TYR E 22  ? 2.066 1.432 1.162 0.161  0.074  0.138  351 TYR EEE O   
5981  C CB  . TYR E 22  ? 2.145 1.571 1.208 0.165  0.097  0.140  351 TYR EEE CB  
5982  C CG  . TYR E 22  ? 2.205 1.551 1.203 0.203  0.068  0.134  351 TYR EEE CG  
5983  C CD1 . TYR E 22  ? 2.194 1.552 1.210 0.240  0.043  0.119  351 TYR EEE CD1 
5984  C CD2 . TYR E 22  ? 2.275 1.527 1.189 0.202  0.061  0.144  351 TYR EEE CD2 
5985  C CE1 . TYR E 22  ? 2.252 1.538 1.208 0.273  0.009  0.114  351 TYR EEE CE1 
5986  C CE2 . TYR E 22  ? 2.339 1.519 1.194 0.239  0.029  0.140  351 TYR EEE CE2 
5987  C CZ  . TYR E 22  ? 2.326 1.526 1.203 0.274  0.002  0.125  351 TYR EEE CZ  
5988  O OH  . TYR E 22  ? 2.397 1.528 1.216 0.309  -0.036 0.122  351 TYR EEE OH  
5989  N N   . ALA E 23  ? 2.025 1.427 1.189 0.228  0.028  0.116  352 ALA EEE N   
5990  C CA  . ALA E 23  ? 2.077 1.431 1.238 0.257  0.003  0.114  352 ALA EEE CA  
5991  C C   . ALA E 23  ? 2.022 1.440 1.288 0.270  -0.006 0.105  352 ALA EEE C   
5992  O O   . ALA E 23  ? 2.047 1.462 1.344 0.304  -0.035 0.101  352 ALA EEE O   
5993  C CB  . ALA E 23  ? 2.136 1.441 1.252 0.292  -0.029 0.111  352 ALA EEE CB  
5994  N N   . TRP E 24  ? 1.972 1.448 1.287 0.242  0.016  0.106  353 TRP EEE N   
5995  C CA  . TRP E 24  ? 1.892 1.433 1.303 0.247  0.013  0.100  353 TRP EEE CA  
5996  C C   . TRP E 24  ? 1.949 1.467 1.377 0.270  0.007  0.100  353 TRP EEE C   
5997  O O   . TRP E 24  ? 2.035 1.486 1.396 0.271  0.016  0.105  353 TRP EEE O   
5998  C CB  . TRP E 24  ? 1.823 1.412 1.260 0.210  0.039  0.103  353 TRP EEE CB  
5999  C CG  . TRP E 24  ? 1.849 1.397 1.225 0.178  0.062  0.113  353 TRP EEE CG  
6000  C CD1 . TRP E 24  ? 1.892 1.417 1.205 0.149  0.077  0.122  353 TRP EEE CD1 
6001  C CD2 . TRP E 24  ? 1.878 1.401 1.246 0.166  0.074  0.115  353 TRP EEE CD2 
6002  N NE1 . TRP E 24  ? 1.944 1.429 1.212 0.116  0.092  0.130  353 TRP EEE NE1 
6003  C CE2 . TRP E 24  ? 1.941 1.418 1.236 0.128  0.090  0.124  353 TRP EEE CE2 
6004  C CE3 . TRP E 24  ? 1.867 1.400 1.278 0.184  0.074  0.110  353 TRP EEE CE3 
6005  C CZ2 . TRP E 24  ? 1.991 1.421 1.245 0.106  0.101  0.127  353 TRP EEE CZ2 
6006  C CZ3 . TRP E 24  ? 1.922 1.410 1.292 0.169  0.090  0.112  353 TRP EEE CZ3 
6007  C CH2 . TRP E 24  ? 1.985 1.416 1.273 0.130  0.101  0.119  353 TRP EEE CH2 
6008  N N   . ASN E 25  ? 1.927 1.500 1.442 0.288  -0.007 0.095  354 ASN EEE N   
6009  C CA  . ASN E 25  ? 1.944 1.519 1.498 0.320  -0.014 0.096  354 ASN EEE CA  
6010  C C   . ASN E 25  ? 1.876 1.484 1.473 0.308  0.014  0.098  354 ASN EEE C   
6011  O O   . ASN E 25  ? 1.788 1.458 1.449 0.292  0.016  0.097  354 ASN EEE O   
6012  C CB  . ASN E 25  ? 1.955 1.572 1.577 0.346  -0.052 0.093  354 ASN EEE CB  
6013  C CG  . ASN E 25  ? 2.059 1.640 1.665 0.386  -0.075 0.096  354 ASN EEE CG  
6014  O OD1 . ASN E 25  ? 2.145 1.692 1.728 0.404  -0.059 0.101  354 ASN EEE OD1 
6015  N ND2 . ASN E 25  ? 2.100 1.681 1.711 0.403  -0.116 0.094  354 ASN EEE ND2 
6016  N N   . ARG E 26  ? 1.921 1.478 1.473 0.316  0.034  0.101  355 ARG EEE N   
6017  C CA  . ARG E 26  ? 1.923 1.495 1.497 0.309  0.063  0.102  355 ARG EEE CA  
6018  C C   . ARG E 26  ? 1.913 1.519 1.555 0.351  0.063  0.103  355 ARG EEE C   
6019  O O   . ARG E 26  ? 1.955 1.531 1.583 0.389  0.050  0.105  355 ARG EEE O   
6020  C CB  . ARG E 26  ? 2.016 1.501 1.488 0.294  0.086  0.103  355 ARG EEE CB  
6021  C CG  . ARG E 26  ? 2.032 1.511 1.504 0.293  0.114  0.102  355 ARG EEE CG  
6022  C CD  . ARG E 26  ? 2.106 1.513 1.482 0.255  0.131  0.102  355 ARG EEE CD  
6023  N NE  . ARG E 26  ? 2.060 1.510 1.449 0.205  0.128  0.104  355 ARG EEE NE  
6024  C CZ  . ARG E 26  ? 2.114 1.535 1.449 0.162  0.138  0.106  355 ARG EEE CZ  
6025  N NH1 . ARG E 26  ? 2.209 1.544 1.461 0.158  0.153  0.104  355 ARG EEE NH1 
6026  N NH2 . ARG E 26  ? 2.076 1.554 1.440 0.125  0.132  0.111  355 ARG EEE NH2 
6027  N N   . LYS E 27  ? 1.870 1.541 1.585 0.345  0.079  0.105  356 LYS EEE N   
6028  C CA  . LYS E 27  ? 1.878 1.596 1.667 0.379  0.090  0.110  356 LYS EEE CA  
6029  C C   . LYS E 27  ? 1.891 1.589 1.651 0.373  0.133  0.110  356 LYS EEE C   
6030  O O   . LYS E 27  ? 1.855 1.569 1.614 0.335  0.143  0.110  356 LYS EEE O   
6031  C CB  . LYS E 27  ? 1.831 1.645 1.734 0.371  0.072  0.114  356 LYS EEE CB  
6032  C CG  . LYS E 27  ? 1.846 1.728 1.845 0.406  0.074  0.123  356 LYS EEE CG  
6033  C CD  . LYS E 27  ? 1.903 1.798 1.934 0.438  0.034  0.124  356 LYS EEE CD  
6034  C CE  . LYS E 27  ? 1.890 1.888 2.052 0.450  0.018  0.135  356 LYS EEE CE  
6035  N NZ  . LYS E 27  ? 1.928 1.965 2.139 0.486  0.055  0.145  356 LYS EEE NZ  
6036  N N   . ARG E 28  ? 1.962 1.619 1.691 0.411  0.155  0.111  357 ARG EEE N   
6037  C CA  . ARG E 28  ? 2.015 1.634 1.696 0.413  0.197  0.110  357 ARG EEE CA  
6038  C C   . ARG E 28  ? 1.947 1.656 1.730 0.430  0.220  0.118  357 ARG EEE C   
6039  O O   . ARG E 28  ? 2.000 1.739 1.832 0.478  0.229  0.123  357 ARG EEE O   
6040  C CB  . ARG E 28  ? 2.169 1.686 1.753 0.451  0.212  0.105  357 ARG EEE CB  
6041  C CG  . ARG E 28  ? 2.267 1.716 1.770 0.451  0.253  0.101  357 ARG EEE CG  
6042  C CD  . ARG E 28  ? 2.417 1.729 1.783 0.462  0.255  0.093  357 ARG EEE CD  
6043  N NE  . ARG E 28  ? 2.508 1.729 1.765 0.441  0.283  0.086  357 ARG EEE NE  
6044  C CZ  . ARG E 28  ? 2.602 1.792 1.829 0.477  0.322  0.083  357 ARG EEE CZ  
6045  N NH1 . ARG E 28  ? 2.592 1.850 1.904 0.536  0.342  0.088  357 ARG EEE NH1 
6046  N NH2 . ARG E 28  ? 2.704 1.796 1.814 0.453  0.340  0.075  357 ARG EEE NH2 
6047  N N   . ILE E 29  ? 1.871 1.623 1.684 0.391  0.230  0.121  358 ILE EEE N   
6048  C CA  . ILE E 29  ? 1.845 1.675 1.743 0.398  0.257  0.132  358 ILE EEE CA  
6049  C C   . ILE E 29  ? 1.909 1.681 1.733 0.416  0.307  0.130  358 ILE EEE C   
6050  O O   . ILE E 29  ? 1.922 1.616 1.644 0.386  0.313  0.122  358 ILE EEE O   
6051  C CB  . ILE E 29  ? 1.804 1.689 1.753 0.350  0.245  0.137  358 ILE EEE CB  
6052  C CG1 . ILE E 29  ? 1.772 1.689 1.766 0.333  0.196  0.135  358 ILE EEE CG1 
6053  C CG2 . ILE E 29  ? 1.796 1.759 1.832 0.353  0.272  0.151  358 ILE EEE CG2 
6054  C CD1 . ILE E 29  ? 1.754 1.747 1.855 0.357  0.174  0.142  358 ILE EEE CD1 
6055  N N   . SER E 30  ? 1.943 1.751 1.814 0.464  0.339  0.136  359 SER EEE N   
6056  C CA  . SER E 30  ? 2.041 1.793 1.841 0.494  0.392  0.134  359 SER EEE CA  
6057  C C   . SER E 30  ? 2.042 1.894 1.951 0.533  0.429  0.150  359 SER EEE C   
6058  O O   . SER E 30  ? 1.981 1.933 2.014 0.545  0.406  0.160  359 SER EEE O   
6059  C CB  . SER E 30  ? 2.138 1.777 1.827 0.532  0.395  0.122  359 SER EEE CB  
6060  O OG  . SER E 30  ? 2.142 1.696 1.736 0.489  0.362  0.111  359 SER EEE OG  
6061  N N   . ASN E 31  ? 2.124 1.950 1.986 0.549  0.485  0.151  360 ASN EEE N   
6062  C CA  . ASN E 31  ? 2.163 2.079 2.114 0.589  0.536  0.167  360 ASN EEE CA  
6063  C C   . ASN E 31  ? 2.054 2.115 2.169 0.560  0.515  0.187  360 ASN EEE C   
6064  O O   . ASN E 31  ? 2.024 2.181 2.257 0.595  0.510  0.199  360 ASN EEE O   
6065  C CB  . ASN E 31  ? 2.270 2.172 2.218 0.668  0.560  0.166  360 ASN EEE CB  
6066  C CG  . ASN E 31  ? 2.419 2.162 2.190 0.693  0.585  0.146  360 ASN EEE CG  
6067  O OD1 . ASN E 31  ? 2.461 2.100 2.125 0.657  0.551  0.131  360 ASN EEE OD1 
6068  N ND2 . ASN E 31  ? 2.515 2.237 2.253 0.754  0.645  0.147  360 ASN EEE ND2 
6069  N N   . CYS E 32  ? 2.015 2.085 2.131 0.499  0.502  0.190  361 CYS EEE N   
6070  C CA  . CYS E 32  ? 1.939 2.124 2.188 0.461  0.484  0.209  361 CYS EEE CA  
6071  C C   . CYS E 32  ? 1.921 2.077 2.121 0.405  0.490  0.212  361 CYS EEE C   
6072  O O   . CYS E 32  ? 1.956 2.010 2.032 0.388  0.486  0.197  361 CYS EEE O   
6073  C CB  . CYS E 32  ? 1.884 2.103 2.197 0.445  0.417  0.205  361 CYS EEE CB  
6074  S SG  . CYS E 32  ? 1.906 2.011 2.095 0.410  0.369  0.183  361 CYS EEE SG  
6075  N N   . VAL E 33  ? 1.868 2.110 2.163 0.375  0.498  0.232  362 VAL EEE N   
6076  C CA  . VAL E 33  ? 1.865 2.087 2.130 0.320  0.494  0.239  362 VAL EEE CA  
6077  C C   . VAL E 33  ? 1.796 2.050 2.124 0.281  0.430  0.238  362 VAL EEE C   
6078  O O   . VAL E 33  ? 1.746 2.082 2.187 0.287  0.407  0.246  362 VAL EEE O   
6079  C CB  . VAL E 33  ? 1.906 2.187 2.221 0.310  0.547  0.263  362 VAL EEE CB  
6080  C CG1 . VAL E 33  ? 1.900 2.163 2.193 0.253  0.534  0.273  362 VAL EEE CG1 
6081  C CG2 . VAL E 33  ? 2.014 2.250 2.246 0.351  0.614  0.262  362 VAL EEE CG2 
6082  N N   . ALA E 34  ? 1.804 1.995 2.059 0.246  0.402  0.229  363 ALA EEE N   
6083  C CA  . ALA E 34  ? 1.772 1.975 2.063 0.211  0.346  0.227  363 ALA EEE CA  
6084  C C   . ALA E 34  ? 1.812 2.004 2.087 0.169  0.351  0.240  363 ALA EEE C   
6085  O O   . ALA E 34  ? 1.892 2.019 2.069 0.162  0.367  0.236  363 ALA EEE O   
6086  C CB  . ALA E 34  ? 1.759 1.896 1.974 0.214  0.310  0.206  363 ALA EEE CB  
6087  N N   . ASP E 35  ? 1.801 2.049 2.163 0.142  0.334  0.256  364 ASP EEE N   
6088  C CA  . ASP E 35  ? 1.802 2.022 2.140 0.101  0.319  0.265  364 ASP EEE CA  
6089  C C   . ASP E 35  ? 1.696 1.876 2.002 0.095  0.264  0.246  364 ASP EEE C   
6090  O O   . ASP E 35  ? 1.646 1.855 2.014 0.092  0.226  0.243  364 ASP EEE O   
6091  C CB  . ASP E 35  ? 1.870 2.149 2.299 0.071  0.323  0.289  364 ASP EEE CB  
6092  C CG  . ASP E 35  ? 1.961 2.198 2.344 0.034  0.326  0.304  364 ASP EEE CG  
6093  O OD1 . ASP E 35  ? 1.985 2.154 2.281 0.032  0.307  0.292  364 ASP EEE OD1 
6094  O OD2 . ASP E 35  ? 2.052 2.326 2.487 0.008  0.348  0.328  364 ASP EEE OD2 
6095  N N   . TYR E 36  ? 1.647 1.765 1.858 0.097  0.262  0.235  365 TYR EEE N   
6096  C CA  . TYR E 36  ? 1.575 1.659 1.749 0.094  0.218  0.219  365 TYR EEE CA  
6097  C C   . TYR E 36  ? 1.537 1.619 1.734 0.068  0.189  0.227  365 TYR EEE C   
6098  O O   . TYR E 36  ? 1.474 1.547 1.674 0.069  0.150  0.216  365 TYR EEE O   
6099  C CB  . TYR E 36  ? 1.597 1.626 1.673 0.097  0.226  0.209  365 TYR EEE CB  
6100  C CG  . TYR E 36  ? 1.646 1.655 1.681 0.122  0.252  0.199  365 TYR EEE CG  
6101  C CD1 . TYR E 36  ? 1.627 1.628 1.655 0.140  0.234  0.183  365 TYR EEE CD1 
6102  C CD2 . TYR E 36  ? 1.729 1.716 1.718 0.127  0.296  0.205  365 TYR EEE CD2 
6103  C CE1 . TYR E 36  ? 1.664 1.631 1.642 0.163  0.256  0.175  365 TYR EEE CE1 
6104  C CE2 . TYR E 36  ? 1.771 1.723 1.707 0.153  0.319  0.195  365 TYR EEE CE2 
6105  C CZ  . TYR E 36  ? 1.734 1.675 1.666 0.170  0.298  0.180  365 TYR EEE CZ  
6106  O OH  . TYR E 36  ? 1.757 1.650 1.628 0.196  0.321  0.170  365 TYR EEE OH  
6107  N N   . SER E 37  ? 1.579 1.664 1.786 0.046  0.209  0.247  366 SER EEE N   
6108  C CA  . SER E 37  ? 1.602 1.676 1.829 0.019  0.184  0.259  366 SER EEE CA  
6109  C C   . SER E 37  ? 1.569 1.669 1.865 0.017  0.145  0.253  366 SER EEE C   
6110  O O   . SER E 37  ? 1.588 1.654 1.871 0.009  0.107  0.248  366 SER EEE O   
6111  C CB  . SER E 37  ? 1.643 1.723 1.881 -0.005 0.217  0.285  366 SER EEE CB  
6112  O OG  . SER E 37  ? 1.618 1.757 1.949 -0.017 0.226  0.298  366 SER EEE OG  
6113  N N   . VAL E 38  ? 1.530 1.683 1.892 0.028  0.151  0.252  367 VAL EEE N   
6114  C CA  . VAL E 38  ? 1.499 1.678 1.925 0.028  0.109  0.244  367 VAL EEE CA  
6115  C C   . VAL E 38  ? 1.454 1.582 1.827 0.040  0.068  0.222  367 VAL EEE C   
6116  O O   . VAL E 38  ? 1.461 1.573 1.853 0.028  0.028  0.219  367 VAL EEE O   
6117  C CB  . VAL E 38  ? 1.523 1.759 2.005 0.052  0.120  0.241  367 VAL EEE CB  
6118  C CG1 . VAL E 38  ? 1.507 1.755 2.031 0.057  0.069  0.229  367 VAL EEE CG1 
6119  C CG2 . VAL E 38  ? 1.562 1.863 2.117 0.043  0.160  0.265  367 VAL EEE CG2 
6120  N N   . LEU E 39  ? 1.419 1.521 1.726 0.062  0.078  0.209  368 LEU EEE N   
6121  C CA  . LEU E 39  ? 1.400 1.468 1.660 0.078  0.047  0.189  368 LEU EEE CA  
6122  C C   . LEU E 39  ? 1.423 1.450 1.638 0.069  0.033  0.190  368 LEU EEE C   
6123  O O   . LEU E 39  ? 1.422 1.424 1.634 0.072  -0.001 0.181  368 LEU EEE O   
6124  C CB  . LEU E 39  ? 1.378 1.441 1.591 0.100  0.066  0.178  368 LEU EEE CB  
6125  C CG  . LEU E 39  ? 1.374 1.460 1.615 0.120  0.066  0.171  368 LEU EEE CG  
6126  C CD1 . LEU E 39  ? 1.396 1.529 1.703 0.118  0.090  0.186  368 LEU EEE CD1 
6127  C CD2 . LEU E 39  ? 1.375 1.437 1.554 0.138  0.083  0.160  368 LEU EEE CD2 
6128  N N   . TYR E 40  ? 1.454 1.468 1.630 0.062  0.057  0.200  369 TYR EEE N   
6129  C CA  . TYR E 40  ? 1.468 1.447 1.597 0.062  0.044  0.202  369 TYR EEE CA  
6130  C C   . TYR E 40  ? 1.467 1.420 1.613 0.044  0.026  0.214  369 TYR EEE C   
6131  O O   . TYR E 40  ? 1.458 1.376 1.576 0.053  -0.001 0.208  369 TYR EEE O   
6132  C CB  . TYR E 40  ? 1.510 1.482 1.586 0.059  0.068  0.208  369 TYR EEE CB  
6133  C CG  . TYR E 40  ? 1.577 1.551 1.648 0.043  0.102  0.225  369 TYR EEE CG  
6134  C CD1 . TYR E 40  ? 1.638 1.590 1.699 0.024  0.106  0.244  369 TYR EEE CD1 
6135  C CD2 . TYR E 40  ? 1.604 1.591 1.665 0.048  0.133  0.222  369 TYR EEE CD2 
6136  C CE1 . TYR E 40  ? 1.685 1.634 1.729 0.010  0.143  0.260  369 TYR EEE CE1 
6137  C CE2 . TYR E 40  ? 1.658 1.641 1.701 0.038  0.170  0.236  369 TYR EEE CE2 
6138  C CZ  . TYR E 40  ? 1.689 1.655 1.725 0.018  0.176  0.256  369 TYR EEE CZ  
6139  O OH  . TYR E 40  ? 1.720 1.680 1.732 0.009  0.217  0.270  369 TYR EEE OH  
6140  N N   . ASN E 41  ? 1.480 1.448 1.669 0.020  0.039  0.230  370 ASN EEE N   
6141  C CA  . ASN E 41  ? 1.562 1.499 1.765 -0.005 0.022  0.244  370 ASN EEE CA  
6142  C C   . ASN E 41  ? 1.596 1.517 1.826 -0.005 -0.021 0.231  370 ASN EEE C   
6143  O O   . ASN E 41  ? 1.662 1.538 1.887 -0.024 -0.044 0.239  370 ASN EEE O   
6144  C CB  . ASN E 41  ? 1.591 1.554 1.832 -0.036 0.054  0.269  370 ASN EEE CB  
6145  C CG  . ASN E 41  ? 1.620 1.563 1.807 -0.041 0.087  0.285  370 ASN EEE CG  
6146  O OD1 . ASN E 41  ? 1.654 1.548 1.781 -0.035 0.073  0.286  370 ASN EEE OD1 
6147  N ND2 . ASN E 41  ? 1.606 1.584 1.810 -0.051 0.131  0.299  370 ASN EEE ND2 
6148  N N   . SER E 42  ? 1.605 1.548 1.848 0.016  -0.033 0.212  371 SER EEE N   
6149  C CA  . SER E 42  ? 1.656 1.577 1.908 0.021  -0.076 0.196  371 SER EEE CA  
6150  C C   . SER E 42  ? 1.682 1.550 1.866 0.050  -0.097 0.178  371 SER EEE C   
6151  O O   . SER E 42  ? 1.641 1.525 1.796 0.076  -0.081 0.168  371 SER EEE O   
6152  C CB  . SER E 42  ? 1.642 1.609 1.936 0.031  -0.080 0.186  371 SER EEE CB  
6153  O OG  . SER E 42  ? 1.655 1.587 1.928 0.044  -0.121 0.167  371 SER EEE OG  
6154  N N   . ALA E 43  ? 1.755 1.561 1.916 0.046  -0.131 0.174  372 ALA EEE N   
6155  C CA  . ALA E 43  ? 1.811 1.558 1.904 0.078  -0.149 0.159  372 ALA EEE CA  
6156  C C   . ALA E 43  ? 1.785 1.534 1.855 0.109  -0.160 0.135  372 ALA EEE C   
6157  O O   . ALA E 43  ? 1.811 1.537 1.830 0.143  -0.159 0.124  372 ALA EEE O   
6158  C CB  . ALA E 43  ? 1.899 1.567 1.967 0.064  -0.182 0.162  372 ALA EEE CB  
6159  N N   . SER E 44  ? 1.736 1.515 1.842 0.101  -0.169 0.129  373 SER EEE N   
6160  C CA  . SER E 44  ? 1.730 1.491 1.805 0.126  -0.190 0.107  373 SER EEE CA  
6161  C C   . SER E 44  ? 1.639 1.448 1.706 0.149  -0.161 0.101  373 SER EEE C   
6162  O O   . SER E 44  ? 1.615 1.448 1.701 0.150  -0.166 0.096  373 SER EEE O   
6163  C CB  . SER E 44  ? 1.764 1.521 1.877 0.103  -0.225 0.105  373 SER EEE CB  
6164  O OG  . SER E 44  ? 1.754 1.568 1.944 0.069  -0.211 0.126  373 SER EEE OG  
6165  N N   . PHE E 45  ? 1.587 1.408 1.625 0.165  -0.134 0.103  374 PHE EEE N   
6166  C CA  . PHE E 45  ? 1.536 1.390 1.552 0.185  -0.109 0.098  374 PHE EEE CA  
6167  C C   . PHE E 45  ? 1.566 1.409 1.539 0.210  -0.100 0.095  374 PHE EEE C   
6168  O O   . PHE E 45  ? 1.582 1.423 1.559 0.206  -0.096 0.106  374 PHE EEE O   
6169  C CB  . PHE E 45  ? 1.485 1.390 1.529 0.169  -0.077 0.111  374 PHE EEE CB  
6170  C CG  . PHE E 45  ? 1.479 1.408 1.568 0.153  -0.075 0.116  374 PHE EEE CG  
6171  C CD1 . PHE E 45  ? 1.504 1.433 1.594 0.164  -0.089 0.105  374 PHE EEE CD1 
6172  C CD2 . PHE E 45  ? 1.462 1.417 1.591 0.131  -0.056 0.132  374 PHE EEE CD2 
6173  C CE1 . PHE E 45  ? 1.484 1.441 1.620 0.156  -0.087 0.111  374 PHE EEE CE1 
6174  C CE2 . PHE E 45  ? 1.448 1.434 1.623 0.124  -0.049 0.138  374 PHE EEE CE2 
6175  C CZ  . PHE E 45  ? 1.456 1.447 1.639 0.137  -0.066 0.127  374 PHE EEE CZ  
6176  N N   . SER E 46  ? 1.605 1.446 1.540 0.237  -0.097 0.082  375 SER EEE N   
6177  C CA  . SER E 46  ? 1.635 1.480 1.537 0.267  -0.085 0.080  375 SER EEE CA  
6178  C C   . SER E 46  ? 1.578 1.483 1.502 0.256  -0.059 0.096  375 SER EEE C   
6179  O O   . SER E 46  ? 1.564 1.475 1.488 0.267  -0.058 0.104  375 SER EEE O   
6180  C CB  . SER E 46  ? 1.667 1.504 1.526 0.294  -0.080 0.065  375 SER EEE CB  
6181  O OG  . SER E 46  ? 1.759 1.525 1.577 0.313  -0.107 0.049  375 SER EEE OG  
6182  N N   . THR E 47  ? 1.553 1.494 1.490 0.236  -0.042 0.100  376 THR EEE N   
6183  C CA  . THR E 47  ? 1.528 1.521 1.472 0.224  -0.019 0.112  376 THR EEE CA  
6184  C C   . THR E 47  ? 1.496 1.494 1.458 0.193  -0.011 0.120  376 THR EEE C   
6185  O O   . THR E 47  ? 1.488 1.478 1.449 0.187  -0.008 0.114  376 THR EEE O   
6186  C CB  . THR E 47  ? 1.560 1.578 1.480 0.234  -0.004 0.107  376 THR EEE CB  
6187  O OG1 . THR E 47  ? 1.620 1.630 1.521 0.268  -0.008 0.099  376 THR EEE OG1 
6188  C CG2 . THR E 47  ? 1.531 1.601 1.456 0.215  0.015  0.120  376 THR EEE CG2 
6189  N N   . PHE E 48  ? 1.492 1.498 1.465 0.177  -0.007 0.134  377 PHE EEE N   
6190  C CA  . PHE E 48  ? 1.474 1.486 1.453 0.151  0.009  0.143  377 PHE EEE CA  
6191  C C   . PHE E 48  ? 1.518 1.557 1.478 0.138  0.019  0.153  377 PHE EEE C   
6192  O O   . PHE E 48  ? 1.574 1.609 1.531 0.126  0.019  0.166  377 PHE EEE O   
6193  C CB  . PHE E 48  ? 1.459 1.449 1.461 0.140  0.004  0.150  377 PHE EEE CB  
6194  C CG  . PHE E 48  ? 1.432 1.423 1.447 0.123  0.022  0.154  377 PHE EEE CG  
6195  C CD1 . PHE E 48  ? 1.422 1.420 1.414 0.110  0.044  0.160  377 PHE EEE CD1 
6196  C CD2 . PHE E 48  ? 1.432 1.418 1.483 0.123  0.016  0.152  377 PHE EEE CD2 
6197  C CE1 . PHE E 48  ? 1.406 1.400 1.404 0.102  0.064  0.163  377 PHE EEE CE1 
6198  C CE2 . PHE E 48  ? 1.407 1.404 1.478 0.114  0.035  0.157  377 PHE EEE CE2 
6199  C CZ  . PHE E 48  ? 1.398 1.398 1.441 0.106  0.062  0.162  377 PHE EEE CZ  
6200  N N   . LYS E 49  ? 1.536 1.599 1.481 0.138  0.025  0.150  378 LYS EEE N   
6201  C CA  . LYS E 49  ? 1.555 1.649 1.484 0.120  0.030  0.160  378 LYS EEE CA  
6202  C C   . LYS E 49  ? 1.545 1.615 1.446 0.093  0.044  0.162  378 LYS EEE C   
6203  O O   . LYS E 49  ? 1.505 1.556 1.392 0.092  0.053  0.153  378 LYS EEE O   
6204  C CB  . LYS E 49  ? 1.586 1.720 1.515 0.126  0.033  0.159  378 LYS EEE CB  
6205  C CG  . LYS E 49  ? 1.618 1.788 1.570 0.154  0.024  0.162  378 LYS EEE CG  
6206  C CD  . LYS E 49  ? 1.658 1.878 1.615 0.163  0.034  0.163  378 LYS EEE CD  
6207  C CE  . LYS E 49  ? 1.727 1.920 1.658 0.162  0.046  0.151  378 LYS EEE CE  
6208  N NZ  . LYS E 49  ? 1.781 1.999 1.712 0.191  0.055  0.146  378 LYS EEE NZ  
6209  N N   . CYS E 50  ? 1.562 1.625 1.447 0.074  0.044  0.172  379 CYS EEE N   
6210  C CA  . CYS E 50  ? 1.609 1.638 1.451 0.050  0.059  0.173  379 CYS EEE CA  
6211  C C   . CYS E 50  ? 1.646 1.691 1.456 0.024  0.052  0.181  379 CYS EEE C   
6212  O O   . CYS E 50  ? 1.720 1.799 1.543 0.021  0.035  0.191  379 CYS EEE O   
6213  C CB  . CYS E 50  ? 1.624 1.625 1.461 0.048  0.066  0.180  379 CYS EEE CB  
6214  S SG  . CYS E 50  ? 1.618 1.602 1.492 0.067  0.080  0.173  379 CYS EEE SG  
6215  N N   . TYR E 51  ? 1.658 1.676 1.426 0.004  0.061  0.176  380 TYR EEE N   
6216  C CA  . TYR E 51  ? 1.684 1.711 1.417 -0.031 0.051  0.183  380 TYR EEE CA  
6217  C C   . TYR E 51  ? 1.727 1.684 1.387 -0.054 0.059  0.181  380 TYR EEE C   
6218  O O   . TYR E 51  ? 1.780 1.684 1.405 -0.048 0.078  0.171  380 TYR EEE O   
6219  C CB  . TYR E 51  ? 1.694 1.740 1.429 -0.037 0.054  0.180  380 TYR EEE CB  
6220  C CG  . TYR E 51  ? 1.645 1.755 1.439 -0.013 0.050  0.181  380 TYR EEE CG  
6221  C CD1 . TYR E 51  ? 1.614 1.714 1.431 0.021  0.058  0.170  380 TYR EEE CD1 
6222  C CD2 . TYR E 51  ? 1.645 1.825 1.471 -0.022 0.038  0.193  380 TYR EEE CD2 
6223  C CE1 . TYR E 51  ? 1.590 1.736 1.445 0.047  0.056  0.169  380 TYR EEE CE1 
6224  C CE2 . TYR E 51  ? 1.618 1.854 1.491 0.006  0.040  0.194  380 TYR EEE CE2 
6225  C CZ  . TYR E 51  ? 1.594 1.807 1.476 0.042  0.050  0.181  380 TYR EEE CZ  
6226  O OH  . TYR E 51  ? 1.564 1.821 1.479 0.072  0.052  0.180  380 TYR EEE OH  
6227  N N   . GLY E 52  ? 1.713 1.666 1.344 -0.075 0.045  0.191  381 GLY EEE N   
6228  C CA  . GLY E 52  ? 1.736 1.617 1.280 -0.102 0.048  0.190  381 GLY EEE CA  
6229  C C   . GLY E 52  ? 1.714 1.535 1.227 -0.080 0.076  0.183  381 GLY EEE C   
6230  O O   . GLY E 52  ? 1.758 1.506 1.192 -0.092 0.089  0.177  381 GLY EEE O   
6231  N N   . VAL E 53  ? 1.642 1.490 1.212 -0.051 0.086  0.185  382 VAL EEE N   
6232  C CA  . VAL E 53  ? 1.679 1.486 1.231 -0.034 0.114  0.185  382 VAL EEE CA  
6233  C C   . VAL E 53  ? 1.608 1.457 1.229 -0.015 0.113  0.193  382 VAL EEE C   
6234  O O   . VAL E 53  ? 1.516 1.408 1.203 0.002  0.105  0.190  382 VAL EEE O   
6235  C CB  . VAL E 53  ? 1.703 1.475 1.244 -0.016 0.143  0.172  382 VAL EEE CB  
6236  C CG1 . VAL E 53  ? 1.613 1.430 1.230 0.008  0.141  0.166  382 VAL EEE CG1 
6237  C CG2 . VAL E 53  ? 1.783 1.516 1.298 -0.001 0.176  0.173  382 VAL EEE CG2 
6238  N N   . SER E 54  ? 1.649 1.475 1.243 -0.020 0.120  0.204  383 SER EEE N   
6239  C CA  . SER E 54  ? 1.660 1.506 1.303 -0.007 0.122  0.215  383 SER EEE CA  
6240  C C   . SER E 54  ? 1.674 1.522 1.359 0.012  0.153  0.210  383 SER EEE C   
6241  O O   . SER E 54  ? 1.790 1.604 1.437 0.013  0.184  0.209  383 SER EEE O   
6242  C CB  . SER E 54  ? 1.732 1.544 1.322 -0.020 0.123  0.230  383 SER EEE CB  
6243  O OG  . SER E 54  ? 1.723 1.557 1.314 -0.028 0.085  0.240  383 SER EEE OG  
6244  N N   . PRO E 55  ? 1.650 1.539 1.411 0.027  0.143  0.207  384 PRO EEE N   
6245  C CA  . PRO E 55  ? 1.654 1.556 1.466 0.042  0.165  0.204  384 PRO EEE CA  
6246  C C   . PRO E 55  ? 1.693 1.592 1.523 0.036  0.183  0.221  384 PRO EEE C   
6247  O O   . PRO E 55  ? 1.708 1.618 1.567 0.043  0.211  0.223  384 PRO EEE O   
6248  C CB  . PRO E 55  ? 1.598 1.534 1.472 0.054  0.138  0.197  384 PRO EEE CB  
6249  C CG  . PRO E 55  ? 1.613 1.555 1.479 0.048  0.110  0.203  384 PRO EEE CG  
6250  C CD  . PRO E 55  ? 1.636 1.559 1.436 0.032  0.111  0.205  384 PRO EEE CD  
6251  N N   . THR E 56  ? 1.707 1.596 1.520 0.024  0.166  0.233  385 THR EEE N   
6252  C CA  . THR E 56  ? 1.774 1.648 1.587 0.012  0.183  0.253  385 THR EEE CA  
6253  C C   . THR E 56  ? 1.838 1.681 1.591 0.007  0.224  0.258  385 THR EEE C   
6254  O O   . THR E 56  ? 1.896 1.738 1.661 0.001  0.254  0.274  385 THR EEE O   
6255  C CB  . THR E 56  ? 1.813 1.668 1.599 0.003  0.153  0.265  385 THR EEE CB  
6256  O OG1 . THR E 56  ? 1.840 1.674 1.557 -0.002 0.142  0.263  385 THR EEE OG1 
6257  C CG2 . THR E 56  ? 1.777 1.654 1.615 0.014  0.117  0.260  385 THR EEE CG2 
6258  N N   . LYS E 57  ? 1.845 1.660 1.532 0.009  0.227  0.247  386 LYS EEE N   
6259  C CA  . LYS E 57  ? 1.937 1.700 1.536 0.004  0.260  0.250  386 LYS EEE CA  
6260  C C   . LYS E 57  ? 1.959 1.716 1.553 0.024  0.296  0.236  386 LYS EEE C   
6261  O O   . LYS E 57  ? 2.016 1.738 1.558 0.030  0.337  0.241  386 LYS EEE O   
6262  C CB  . LYS E 57  ? 1.994 1.715 1.507 -0.013 0.231  0.248  386 LYS EEE CB  
6263  C CG  . LYS E 57  ? 2.032 1.748 1.532 -0.027 0.203  0.265  386 LYS EEE CG  
6264  C CD  . LYS E 57  ? 2.060 1.751 1.490 -0.043 0.166  0.265  386 LYS EEE CD  
6265  C CE  . LYS E 57  ? 2.149 1.768 1.464 -0.057 0.182  0.264  386 LYS EEE CE  
6266  N NZ  . LYS E 57  ? 2.229 1.803 1.492 -0.058 0.214  0.280  386 LYS EEE NZ  
6267  N N   . LEU E 58  ? 2.189 2.116 1.678 0.102  0.288  0.278  387 LEU EEE N   
6268  C CA  . LEU E 58  ? 2.194 2.184 1.740 0.109  0.318  0.247  387 LEU EEE CA  
6269  C C   . LEU E 58  ? 2.263 2.301 1.863 0.083  0.360  0.267  387 LEU EEE C   
6270  O O   . LEU E 58  ? 2.245 2.340 1.905 0.093  0.383  0.244  387 LEU EEE O   
6271  C CB  . LEU E 58  ? 2.083 2.081 1.695 0.125  0.288  0.215  387 LEU EEE CB  
6272  C CG  . LEU E 58  ? 1.989 1.972 1.663 0.113  0.262  0.224  387 LEU EEE CG  
6273  C CD1 . LEU E 58  ? 1.981 1.978 1.696 0.082  0.284  0.253  387 LEU EEE CD1 
6274  C CD2 . LEU E 58  ? 1.895 1.898 1.630 0.126  0.247  0.192  387 LEU EEE CD2 
6275  N N   . ASN E 59  ? 2.376 2.393 1.957 0.051  0.370  0.308  388 ASN EEE N   
6276  C CA  . ASN E 59  ? 2.418 2.488 2.038 0.018  0.416  0.331  388 ASN EEE CA  
6277  C C   . ASN E 59  ? 2.508 2.599 2.052 0.018  0.462  0.339  388 ASN EEE C   
6278  O O   . ASN E 59  ? 2.613 2.739 2.166 -0.015 0.503  0.368  388 ASN EEE O   
6279  C CB  . ASN E 59  ? 2.461 2.499 2.105 -0.024 0.405  0.369  388 ASN EEE CB  
6280  C CG  . ASN E 59  ? 2.577 2.524 2.124 -0.039 0.387  0.405  388 ASN EEE CG  
6281  O OD1 . ASN E 59  ? 2.684 2.623 2.159 -0.054 0.417  0.432  388 ASN EEE OD1 
6282  N ND2 . ASN E 59  ? 2.563 2.439 2.106 -0.033 0.340  0.408  388 ASN EEE ND2 
6283  N N   . ASP E 60  ? 2.503 2.571 1.971 0.051  0.455  0.315  389 ASP EEE N   
6284  C CA  . ASP E 60  ? 2.566 2.658 1.958 0.059  0.499  0.310  389 ASP EEE CA  
6285  C C   . ASP E 60  ? 2.504 2.589 1.861 0.102  0.484  0.261  389 ASP EEE C   
6286  O O   . ASP E 60  ? 2.593 2.652 1.846 0.112  0.491  0.257  389 ASP EEE O   
6287  C CB  . ASP E 60  ? 2.703 2.744 1.986 0.034  0.508  0.354  389 ASP EEE CB  
6288  C CG  . ASP E 60  ? 2.745 2.694 1.959 0.040  0.449  0.371  389 ASP EEE CG  
6289  O OD1 . ASP E 60  ? 2.739 2.666 1.920 0.073  0.413  0.341  389 ASP EEE OD1 
6290  O OD2 . ASP E 60  ? 2.780 2.680 1.972 0.011  0.439  0.415  389 ASP EEE OD2 
6291  N N   . LEU E 61  ? 2.357 2.461 1.794 0.122  0.464  0.227  390 LEU EEE N   
6292  C CA  . LEU E 61  ? 2.322 2.422 1.743 0.157  0.454  0.178  390 LEU EEE CA  
6293  C C   . LEU E 61  ? 2.248 2.390 1.777 0.172  0.458  0.153  390 LEU EEE C   
6294  O O   . LEU E 61  ? 2.229 2.376 1.835 0.158  0.434  0.166  390 LEU EEE O   
6295  C CB  . LEU E 61  ? 2.294 2.334 1.669 0.166  0.397  0.168  390 LEU EEE CB  
6296  C CG  . LEU E 61  ? 2.239 2.272 1.630 0.190  0.374  0.121  390 LEU EEE CG  
6297  C CD1 . LEU E 61  ? 2.317 2.344 1.627 0.209  0.397  0.089  390 LEU EEE CD1 
6298  C CD2 . LEU E 61  ? 2.203 2.199 1.589 0.190  0.316  0.116  390 LEU EEE CD2 
6299  N N   . CYS E 62  ? 2.252 2.414 1.779 0.201  0.481  0.115  391 CYS EEE N   
6300  C CA  . CYS E 62  ? 2.180 2.381 1.800 0.222  0.491  0.091  391 CYS EEE CA  
6301  C C   . CYS E 62  ? 2.129 2.283 1.751 0.241  0.449  0.057  391 CYS EEE C   
6302  O O   . CYS E 62  ? 2.195 2.309 1.742 0.258  0.445  0.027  391 CYS EEE O   
6303  C CB  . CYS E 62  ? 2.236 2.488 1.852 0.246  0.548  0.072  391 CYS EEE CB  
6304  S SG  . CYS E 62  ? 2.280 2.615 1.928 0.218  0.605  0.114  391 CYS EEE SG  
6305  N N   . PHE E 63  ? 2.029 2.184 1.730 0.236  0.419  0.061  392 PHE EEE N   
6306  C CA  . PHE E 63  ? 1.970 2.084 1.686 0.248  0.382  0.034  392 PHE EEE CA  
6307  C C   . PHE E 63  ? 1.939 2.078 1.719 0.275  0.397  0.015  392 PHE EEE C   
6308  O O   . PHE E 63  ? 1.919 2.118 1.769 0.276  0.420  0.032  392 PHE EEE O   
6309  C CB  . PHE E 63  ? 1.906 2.005 1.661 0.225  0.341  0.052  392 PHE EEE CB  
6310  C CG  . PHE E 63  ? 1.943 2.008 1.639 0.209  0.315  0.064  392 PHE EEE CG  
6311  C CD1 . PHE E 63  ? 1.969 1.996 1.616 0.213  0.288  0.040  392 PHE EEE CD1 
6312  C CD2 . PHE E 63  ? 1.961 2.033 1.653 0.188  0.317  0.099  392 PHE EEE CD2 
6313  C CE1 . PHE E 63  ? 1.997 2.004 1.599 0.203  0.260  0.050  392 PHE EEE CE1 
6314  C CE2 . PHE E 63  ? 2.005 2.043 1.643 0.181  0.289  0.110  392 PHE EEE CE2 
6315  C CZ  . PHE E 63  ? 2.022 2.032 1.619 0.190  0.260  0.085  392 PHE EEE CZ  
6316  N N   . THR E 64  ? 1.931 2.022 1.688 0.296  0.382  -0.019 393 THR EEE N   
6317  C CA  . THR E 64  ? 1.923 2.015 1.725 0.329  0.390  -0.040 393 THR EEE CA  
6318  C C   . THR E 64  ? 1.852 1.969 1.745 0.321  0.368  -0.019 393 THR EEE C   
6319  O O   . THR E 64  ? 1.848 2.014 1.808 0.342  0.385  -0.016 393 THR EEE O   
6320  C CB  . THR E 64  ? 1.952 1.965 1.695 0.345  0.372  -0.078 393 THR EEE CB  
6321  O OG1 . THR E 64  ? 1.929 1.901 1.633 0.313  0.335  -0.075 393 THR EEE OG1 
6322  C CG2 . THR E 64  ? 2.044 2.038 1.712 0.370  0.404  -0.109 393 THR EEE CG2 
6323  N N   . ASN E 65  ? 1.833 1.921 1.727 0.292  0.330  -0.006 394 ASN EEE N   
6324  C CA  . ASN E 65  ? 1.780 1.880 1.743 0.280  0.304  0.012  394 ASN EEE CA  
6325  C C   . ASN E 65  ? 1.701 1.794 1.659 0.244  0.280  0.034  394 ASN EEE C   
6326  O O   . ASN E 65  ? 1.689 1.745 1.592 0.232  0.266  0.026  394 ASN EEE O   
6327  C CB  . ASN E 65  ? 1.820 1.867 1.783 0.294  0.279  -0.007 394 ASN EEE CB  
6328  C CG  . ASN E 65  ? 1.893 1.943 1.876 0.337  0.297  -0.025 394 ASN EEE CG  
6329  O OD1 . ASN E 65  ? 1.894 2.001 1.947 0.352  0.306  -0.012 394 ASN EEE OD1 
6330  N ND2 . ASN E 65  ? 1.974 1.964 1.896 0.356  0.302  -0.056 394 ASN EEE ND2 
6331  N N   . VAL E 66  ? 1.620 1.750 1.639 0.229  0.274  0.058  395 VAL EEE N   
6332  C CA  . VAL E 66  ? 1.575 1.691 1.598 0.199  0.247  0.076  395 VAL EEE CA  
6333  C C   . VAL E 66  ? 1.545 1.649 1.608 0.198  0.220  0.074  395 VAL EEE C   
6334  O O   . VAL E 66  ? 1.536 1.677 1.656 0.207  0.222  0.081  395 VAL EEE O   
6335  C CB  . VAL E 66  ? 1.570 1.723 1.617 0.177  0.259  0.104  395 VAL EEE CB  
6336  C CG1 . VAL E 66  ? 1.558 1.683 1.604 0.151  0.231  0.118  395 VAL EEE CG1 
6337  C CG2 . VAL E 66  ? 1.624 1.784 1.622 0.178  0.289  0.109  395 VAL EEE CG2 
6338  N N   . TYR E 67  ? 1.539 1.598 1.572 0.189  0.195  0.065  396 TYR EEE N   
6339  C CA  . TYR E 67  ? 1.532 1.571 1.585 0.182  0.169  0.066  396 TYR EEE CA  
6340  C C   . TYR E 67  ? 1.535 1.577 1.598 0.157  0.154  0.082  396 TYR EEE C   
6341  O O   . TYR E 67  ? 1.562 1.594 1.594 0.147  0.155  0.083  396 TYR EEE O   
6342  C CB  . TYR E 67  ? 1.536 1.526 1.547 0.184  0.157  0.046  396 TYR EEE CB  
6343  C CG  . TYR E 67  ? 1.583 1.552 1.578 0.208  0.169  0.028  396 TYR EEE CG  
6344  C CD1 . TYR E 67  ? 1.597 1.586 1.630 0.234  0.178  0.031  396 TYR EEE CD1 
6345  C CD2 . TYR E 67  ? 1.629 1.557 1.571 0.208  0.169  0.007  396 TYR EEE CD2 
6346  C CE1 . TYR E 67  ? 1.638 1.601 1.654 0.264  0.188  0.012  396 TYR EEE CE1 
6347  C CE2 . TYR E 67  ? 1.691 1.587 1.610 0.230  0.178  -0.013 396 TYR EEE CE2 
6348  C CZ  . TYR E 67  ? 1.688 1.597 1.642 0.261  0.189  -0.011 396 TYR EEE CZ  
6349  O OH  . TYR E 67  ? 1.718 1.588 1.647 0.291  0.198  -0.032 396 TYR EEE OH  
6350  N N   . ALA E 68  ? 1.528 1.583 1.631 0.148  0.139  0.093  397 ALA EEE N   
6351  C CA  . ALA E 68  ? 1.509 1.558 1.618 0.124  0.122  0.105  397 ALA EEE CA  
6352  C C   . ALA E 68  ? 1.517 1.537 1.619 0.118  0.097  0.099  397 ALA EEE C   
6353  O O   . ALA E 68  ? 1.525 1.557 1.657 0.120  0.084  0.105  397 ALA EEE O   
6354  C CB  . ALA E 68  ? 1.507 1.598 1.665 0.113  0.126  0.123  397 ALA EEE CB  
6355  N N   . ASP E 69  ? 1.528 1.516 1.590 0.112  0.091  0.088  398 ASP EEE N   
6356  C CA  . ASP E 69  ? 1.551 1.510 1.593 0.102  0.073  0.082  398 ASP EEE CA  
6357  C C   . ASP E 69  ? 1.560 1.511 1.601 0.085  0.061  0.087  398 ASP EEE C   
6358  O O   . ASP E 69  ? 1.593 1.540 1.623 0.083  0.067  0.085  398 ASP EEE O   
6359  C CB  . ASP E 69  ? 1.565 1.503 1.569 0.102  0.079  0.066  398 ASP EEE CB  
6360  C CG  . ASP E 69  ? 1.557 1.494 1.554 0.116  0.091  0.058  398 ASP EEE CG  
6361  O OD1 . ASP E 69  ? 1.546 1.484 1.561 0.129  0.092  0.063  398 ASP EEE OD1 
6362  O OD2 . ASP E 69  ? 1.534 1.469 1.509 0.114  0.098  0.045  398 ASP EEE OD2 
6363  N N   . SER E 70  ? 1.556 1.501 1.606 0.075  0.041  0.093  399 SER EEE N   
6364  C CA  . SER E 70  ? 1.569 1.498 1.611 0.057  0.025  0.094  399 SER EEE CA  
6365  C C   . SER E 70  ? 1.557 1.455 1.559 0.049  0.011  0.084  399 SER EEE C   
6366  O O   . SER E 70  ? 1.577 1.470 1.572 0.053  0.004  0.087  399 SER EEE O   
6367  C CB  . SER E 70  ? 1.603 1.559 1.690 0.046  0.012  0.110  399 SER EEE CB  
6368  O OG  . SER E 70  ? 1.644 1.624 1.758 0.056  0.002  0.116  399 SER EEE OG  
6369  N N   . PHE E 71  ? 1.532 1.404 1.503 0.041  0.009  0.073  400 PHE EEE N   
6370  C CA  . PHE E 71  ? 1.558 1.400 1.482 0.032  0.001  0.061  400 PHE EEE CA  
6371  C C   . PHE E 71  ? 1.562 1.376 1.458 0.028  0.000  0.047  400 PHE EEE C   
6372  O O   . PHE E 71  ? 1.542 1.354 1.454 0.034  0.005  0.048  400 PHE EEE O   
6373  C CB  . PHE E 71  ? 1.579 1.423 1.479 0.037  0.017  0.053  400 PHE EEE CB  
6374  C CG  . PHE E 71  ? 1.587 1.449 1.495 0.049  0.039  0.042  400 PHE EEE CG  
6375  C CD1 . PHE E 71  ? 1.623 1.479 1.511 0.053  0.047  0.026  400 PHE EEE CD1 
6376  C CD2 . PHE E 71  ? 1.607 1.490 1.539 0.059  0.049  0.047  400 PHE EEE CD2 
6377  C CE1 . PHE E 71  ? 1.635 1.515 1.536 0.068  0.061  0.017  400 PHE EEE CE1 
6378  C CE2 . PHE E 71  ? 1.622 1.523 1.558 0.069  0.063  0.037  400 PHE EEE CE2 
6379  C CZ  . PHE E 71  ? 1.636 1.539 1.560 0.074  0.068  0.024  400 PHE EEE CZ  
6380  N N   . VAL E 72  ? 1.616 1.403 1.465 0.020  -0.005 0.033  401 VAL EEE N   
6381  C CA  . VAL E 72  ? 1.664 1.416 1.475 0.020  -0.006 0.014  401 VAL EEE CA  
6382  C C   . VAL E 72  ? 1.682 1.439 1.460 0.030  0.018  -0.007 401 VAL EEE C   
6383  O O   . VAL E 72  ? 1.731 1.496 1.486 0.021  0.023  -0.005 401 VAL EEE O   
6384  C CB  . VAL E 72  ? 1.722 1.439 1.500 -0.001 -0.034 0.012  401 VAL EEE CB  
6385  C CG1 . VAL E 72  ? 1.778 1.450 1.497 0.001  -0.031 -0.015 401 VAL EEE CG1 
6386  C CG2 . VAL E 72  ? 1.736 1.453 1.553 -0.015 -0.057 0.028  401 VAL EEE CG2 
6387  N N   . ILE E 73  ? 1.683 1.433 1.457 0.049  0.030  -0.024 402 ILE EEE N   
6388  C CA  . ILE E 73  ? 1.715 1.479 1.464 0.063  0.054  -0.049 402 ILE EEE CA  
6389  C C   . ILE E 73  ? 1.776 1.497 1.500 0.081  0.052  -0.070 402 ILE EEE C   
6390  O O   . ILE E 73  ? 1.797 1.478 1.527 0.079  0.032  -0.061 402 ILE EEE O   
6391  C CB  . ILE E 73  ? 1.670 1.488 1.460 0.079  0.074  -0.048 402 ILE EEE CB  
6392  C CG1 . ILE E 73  ? 1.652 1.472 1.481 0.094  0.066  -0.036 402 ILE EEE CG1 
6393  C CG2 . ILE E 73  ? 1.644 1.492 1.440 0.059  0.081  -0.036 402 ILE EEE CG2 
6394  C CD1 . ILE E 73  ? 1.631 1.497 1.489 0.116  0.080  -0.042 402 ILE EEE CD1 
6395  N N   . ARG E 74  ? 1.824 1.551 1.520 0.097  0.072  -0.097 403 ARG EEE N   
6396  C CA  . ARG E 74  ? 1.921 1.602 1.590 0.123  0.072  -0.122 403 ARG EEE CA  
6397  C C   . ARG E 74  ? 1.899 1.597 1.614 0.157  0.076  -0.120 403 ARG EEE C   
6398  O O   . ARG E 74  ? 1.881 1.647 1.638 0.164  0.090  -0.114 403 ARG EEE O   
6399  C CB  . ARG E 74  ? 2.008 1.693 1.629 0.132  0.096  -0.155 403 ARG EEE CB  
6400  C CG  . ARG E 74  ? 1.999 1.764 1.650 0.151  0.131  -0.168 403 ARG EEE CG  
6401  C CD  . ARG E 74  ? 2.067 1.841 1.664 0.147  0.158  -0.194 403 ARG EEE CD  
6402  N NE  . ARG E 74  ? 2.045 1.906 1.676 0.162  0.195  -0.209 403 ARG EEE NE  
6403  C CZ  . ARG E 74  ? 2.069 1.964 1.730 0.207  0.212  -0.235 403 ARG EEE CZ  
6404  N NH1 . ARG E 74  ? 2.099 1.934 1.753 0.243  0.195  -0.248 403 ARG EEE NH1 
6405  N NH2 . ARG E 74  ? 2.071 2.062 1.774 0.215  0.244  -0.247 403 ARG EEE NH2 
6406  N N   . GLY E 75  ? 1.944 1.578 1.646 0.173  0.060  -0.124 404 GLY EEE N   
6407  C CA  . GLY E 75  ? 1.964 1.592 1.695 0.204  0.055  -0.115 404 GLY EEE CA  
6408  C C   . GLY E 75  ? 1.950 1.651 1.717 0.241  0.076  -0.128 404 GLY EEE C   
6409  O O   . GLY E 75  ? 1.980 1.708 1.784 0.254  0.071  -0.111 404 GLY EEE O   
6410  N N   . ASP E 76  ? 1.958 1.693 1.715 0.256  0.099  -0.158 405 ASP EEE N   
6411  C CA  . ASP E 76  ? 1.940 1.760 1.739 0.290  0.120  -0.175 405 ASP EEE CA  
6412  C C   . ASP E 76  ? 1.839 1.737 1.689 0.270  0.122  -0.153 405 ASP EEE C   
6413  O O   . ASP E 76  ? 1.811 1.765 1.706 0.298  0.123  -0.154 405 ASP EEE O   
6414  C CB  . ASP E 76  ? 2.004 1.862 1.784 0.292  0.151  -0.207 405 ASP EEE CB  
6415  C CG  . ASP E 76  ? 2.134 1.942 1.878 0.336  0.157  -0.241 405 ASP EEE CG  
6416  O OD1 . ASP E 76  ? 2.212 1.951 1.948 0.365  0.135  -0.239 405 ASP EEE OD1 
6417  O OD2 . ASP E 76  ? 2.196 2.030 1.915 0.340  0.186  -0.271 405 ASP EEE OD2 
6418  N N   . GLU E 77  ? 1.808 1.707 1.650 0.225  0.121  -0.134 406 GLU EEE N   
6419  C CA  . GLU E 77  ? 1.774 1.738 1.651 0.201  0.127  -0.118 406 GLU EEE CA  
6420  C C   . GLU E 77  ? 1.737 1.686 1.635 0.198  0.106  -0.091 406 GLU EEE C   
6421  O O   . GLU E 77  ? 1.736 1.732 1.660 0.184  0.108  -0.081 406 GLU EEE O   
6422  C CB  . GLU E 77  ? 1.818 1.780 1.667 0.159  0.135  -0.113 406 GLU EEE CB  
6423  C CG  . GLU E 77  ? 1.891 1.870 1.710 0.157  0.160  -0.138 406 GLU EEE CG  
6424  C CD  . GLU E 77  ? 1.927 1.871 1.692 0.118  0.162  -0.131 406 GLU EEE CD  
6425  O OE1 . GLU E 77  ? 1.922 1.813 1.670 0.101  0.138  -0.111 406 GLU EEE OE1 
6426  O OE2 . GLU E 77  ? 1.958 1.931 1.698 0.106  0.188  -0.146 406 GLU EEE OE2 
6427  N N   . VAL E 78  ? 1.740 1.623 1.621 0.208  0.087  -0.080 407 VAL EEE N   
6428  C CA  . VAL E 78  ? 1.696 1.563 1.590 0.205  0.072  -0.052 407 VAL EEE CA  
6429  C C   . VAL E 78  ? 1.658 1.586 1.585 0.225  0.073  -0.051 407 VAL EEE C   
6430  O O   . VAL E 78  ? 1.572 1.523 1.512 0.208  0.071  -0.036 407 VAL EEE O   
6431  C CB  . VAL E 78  ? 1.762 1.552 1.632 0.217  0.055  -0.043 407 VAL EEE CB  
6432  C CG1 . VAL E 78  ? 1.778 1.561 1.656 0.233  0.044  -0.022 407 VAL EEE CG1 
6433  C CG2 . VAL E 78  ? 1.771 1.512 1.620 0.181  0.046  -0.031 407 VAL EEE CG2 
6434  N N   . ARG E 79  ? 1.695 1.648 1.635 0.262  0.074  -0.069 408 ARG EEE N   
6435  C CA  . ARG E 79  ? 1.705 1.726 1.682 0.285  0.070  -0.072 408 ARG EEE CA  
6436  C C   . ARG E 79  ? 1.624 1.710 1.623 0.251  0.080  -0.071 408 ARG EEE C   
6437  O O   . ARG E 79  ? 1.609 1.725 1.624 0.253  0.069  -0.062 408 ARG EEE O   
6438  C CB  . ARG E 79  ? 1.809 1.878 1.810 0.322  0.078  -0.101 408 ARG EEE CB  
6439  C CG  . ARG E 79  ? 1.973 1.980 1.953 0.368  0.068  -0.108 408 ARG EEE CG  
6440  C CD  . ARG E 79  ? 2.115 2.191 2.135 0.416  0.073  -0.135 408 ARG EEE CD  
6441  N NE  . ARG E 79  ? 2.178 2.357 2.238 0.401  0.100  -0.157 408 ARG EEE NE  
6442  C CZ  . ARG E 79  ? 2.186 2.471 2.303 0.400  0.101  -0.162 408 ARG EEE CZ  
6443  N NH1 . ARG E 79  ? 2.200 2.505 2.338 0.418  0.073  -0.147 408 ARG EEE NH1 
6444  N NH2 . ARG E 79  ? 2.153 2.524 2.301 0.377  0.128  -0.181 408 ARG EEE NH2 
6445  N N   . GLN E 80  ? 1.618 1.719 1.614 0.222  0.098  -0.081 409 GLN EEE N   
6446  C CA  . GLN E 80  ? 1.603 1.759 1.616 0.189  0.109  -0.083 409 GLN EEE CA  
6447  C C   . GLN E 80  ? 1.559 1.682 1.557 0.163  0.100  -0.062 409 GLN EEE C   
6448  O O   . GLN E 80  ? 1.557 1.714 1.566 0.139  0.105  -0.063 409 GLN EEE O   
6449  C CB  . GLN E 80  ? 1.651 1.817 1.650 0.165  0.131  -0.096 409 GLN EEE CB  
6450  C CG  . GLN E 80  ? 1.699 1.927 1.722 0.185  0.150  -0.123 409 GLN EEE CG  
6451  C CD  . GLN E 80  ? 1.744 2.021 1.768 0.148  0.176  -0.132 409 GLN EEE CD  
6452  O OE1 . GLN E 80  ? 1.774 2.010 1.761 0.111  0.180  -0.120 409 GLN EEE OE1 
6453  N NE2 . GLN E 80  ? 1.786 2.153 1.854 0.157  0.192  -0.152 409 GLN EEE NE2 
6454  N N   . ILE E 81  ? 1.538 1.601 1.515 0.167  0.089  -0.044 410 ILE EEE N   
6455  C CA  . ILE E 81  ? 1.496 1.535 1.465 0.150  0.084  -0.024 410 ILE EEE CA  
6456  C C   . ILE E 81  ? 1.452 1.507 1.427 0.168  0.073  -0.018 410 ILE EEE C   
6457  O O   . ILE E 81  ? 1.412 1.433 1.375 0.184  0.065  -0.003 410 ILE EEE O   
6458  C CB  . ILE E 81  ? 1.527 1.509 1.477 0.142  0.080  -0.008 410 ILE EEE CB  
6459  C CG1 . ILE E 81  ? 1.543 1.504 1.478 0.130  0.084  -0.017 410 ILE EEE CG1 
6460  C CG2 . ILE E 81  ? 1.497 1.471 1.448 0.127  0.080  0.008  410 ILE EEE CG2 
6461  C CD1 . ILE E 81  ? 1.526 1.512 1.458 0.108  0.095  -0.025 410 ILE EEE CD1 
6462  N N   . ALA E 82  ? 1.421 1.526 1.411 0.162  0.073  -0.028 411 ALA EEE N   
6463  C CA  . ALA E 82  ? 1.435 1.569 1.430 0.178  0.059  -0.027 411 ALA EEE CA  
6464  C C   . ALA E 82  ? 1.407 1.593 1.417 0.156  0.060  -0.043 411 ALA EEE C   
6465  O O   . ALA E 82  ? 1.367 1.586 1.397 0.139  0.071  -0.057 411 ALA EEE O   
6466  C CB  . ALA E 82  ? 1.476 1.625 1.482 0.214  0.048  -0.031 411 ALA EEE CB  
6467  N N   . PRO E 83  ? 1.414 1.607 1.412 0.153  0.049  -0.041 412 PRO EEE N   
6468  C CA  . PRO E 83  ? 1.421 1.661 1.432 0.130  0.044  -0.058 412 PRO EEE CA  
6469  C C   . PRO E 83  ? 1.413 1.733 1.470 0.137  0.037  -0.074 412 PRO EEE C   
6470  O O   . PRO E 83  ? 1.403 1.740 1.473 0.173  0.026  -0.072 412 PRO EEE O   
6471  C CB  . PRO E 83  ? 1.453 1.681 1.434 0.136  0.028  -0.053 412 PRO EEE CB  
6472  C CG  . PRO E 83  ? 1.466 1.665 1.430 0.170  0.022  -0.034 412 PRO EEE CG  
6473  C CD  . PRO E 83  ? 1.436 1.593 1.402 0.170  0.040  -0.024 412 PRO EEE CD  
6474  N N   . GLY E 84  ? 1.422 1.788 1.502 0.103  0.045  -0.090 413 GLY EEE N   
6475  C CA  . GLY E 84  ? 1.446 1.909 1.581 0.102  0.040  -0.108 413 GLY EEE CA  
6476  C C   . GLY E 84  ? 1.443 1.938 1.609 0.115  0.061  -0.115 413 GLY EEE C   
6477  O O   . GLY E 84  ? 1.415 2.002 1.633 0.110  0.065  -0.132 413 GLY EEE O   
6478  N N   . GLN E 85  ? 1.460 1.887 1.596 0.129  0.074  -0.104 414 GLN EEE N   
6479  C CA  . GLN E 85  ? 1.474 1.911 1.620 0.139  0.096  -0.113 414 GLN EEE CA  
6480  C C   . GLN E 85  ? 1.466 1.923 1.613 0.090  0.121  -0.119 414 GLN EEE C   
6481  O O   . GLN E 85  ? 1.436 1.854 1.555 0.053  0.119  -0.111 414 GLN EEE O   
6482  C CB  . GLN E 85  ? 1.505 1.852 1.609 0.158  0.098  -0.099 414 GLN EEE CB  
6483  C CG  . GLN E 85  ? 1.550 1.871 1.650 0.204  0.078  -0.090 414 GLN EEE CG  
6484  C CD  . GLN E 85  ? 1.607 1.966 1.736 0.247  0.078  -0.106 414 GLN EEE CD  
6485  O OE1 . GLN E 85  ? 1.652 2.036 1.793 0.247  0.100  -0.123 414 GLN EEE OE1 
6486  N NE2 . GLN E 85  ? 1.660 2.020 1.796 0.287  0.054  -0.100 414 GLN EEE NE2 
6487  N N   . THR E 86  ? 1.486 1.996 1.657 0.092  0.144  -0.135 415 THR EEE N   
6488  C CA  . THR E 86  ? 1.504 2.033 1.668 0.045  0.172  -0.139 415 THR EEE CA  
6489  C C   . THR E 86  ? 1.506 2.030 1.654 0.062  0.198  -0.148 415 THR EEE C   
6490  O O   . THR E 86  ? 1.494 2.036 1.662 0.112  0.195  -0.160 415 THR EEE O   
6491  C CB  . THR E 86  ? 1.514 2.149 1.732 0.014  0.179  -0.154 415 THR EEE CB  
6492  O OG1 . THR E 86  ? 1.511 2.237 1.791 0.058  0.175  -0.171 415 THR EEE OG1 
6493  C CG2 . THR E 86  ? 1.515 2.141 1.731 -0.020 0.157  -0.147 415 THR EEE CG2 
6494  N N   . GLY E 87  ? 1.515 2.009 1.623 0.023  0.220  -0.143 416 GLY EEE N   
6495  C CA  . GLY E 87  ? 1.540 2.014 1.613 0.030  0.245  -0.151 416 GLY EEE CA  
6496  C C   . GLY E 87  ? 1.549 1.934 1.551 -0.007 0.247  -0.131 416 GLY EEE C   
6497  O O   . GLY E 87  ? 1.517 1.880 1.508 -0.046 0.240  -0.116 416 GLY EEE O   
6498  N N   . LYS E 88  ? 1.608 1.937 1.561 0.006  0.253  -0.132 417 LYS EEE N   
6499  C CA  . LYS E 88  ? 1.695 1.942 1.577 -0.026 0.251  -0.114 417 LYS EEE CA  
6500  C C   . LYS E 88  ? 1.647 1.821 1.518 -0.022 0.217  -0.091 417 LYS EEE C   
6501  O O   . LYS E 88  ? 1.643 1.785 1.495 -0.055 0.211  -0.073 417 LYS EEE O   
6502  C CB  . LYS E 88  ? 1.793 2.006 1.624 -0.011 0.263  -0.124 417 LYS EEE CB  
6503  C CG  . LYS E 88  ? 1.885 2.173 1.724 -0.005 0.302  -0.152 417 LYS EEE CG  
6504  C CD  . LYS E 88  ? 1.941 2.296 1.791 -0.054 0.333  -0.149 417 LYS EEE CD  
6505  C CE  . LYS E 88  ? 1.933 2.412 1.867 -0.041 0.355  -0.172 417 LYS EEE CE  
6506  N NZ  . LYS E 88  ? 1.912 2.442 1.882 -0.090 0.358  -0.161 417 LYS EEE NZ  
6507  N N   . ILE E 89  ? 1.626 1.775 1.509 0.016  0.198  -0.092 418 ILE EEE N   
6508  C CA  . ILE E 89  ? 1.621 1.708 1.497 0.022  0.169  -0.071 418 ILE EEE CA  
6509  C C   . ILE E 89  ? 1.595 1.704 1.504 0.015  0.161  -0.065 418 ILE EEE C   
6510  O O   . ILE E 89  ? 1.576 1.643 1.468 -0.003 0.150  -0.048 418 ILE EEE O   
6511  C CB  . ILE E 89  ? 1.620 1.681 1.501 0.059  0.154  -0.075 418 ILE EEE CB  
6512  C CG1 . ILE E 89  ? 1.666 1.699 1.508 0.067  0.162  -0.088 418 ILE EEE CG1 
6513  C CG2 . ILE E 89  ? 1.615 1.625 1.494 0.060  0.130  -0.053 418 ILE EEE CG2 
6514  C CD1 . ILE E 89  ? 1.697 1.685 1.484 0.036  0.161  -0.078 418 ILE EEE CD1 
6515  N N   . ALA E 90  ? 1.588 1.762 1.542 0.031  0.164  -0.078 419 ALA EEE N   
6516  C CA  . ALA E 90  ? 1.575 1.777 1.558 0.026  0.153  -0.077 419 ALA EEE CA  
6517  C C   . ALA E 90  ? 1.594 1.781 1.558 -0.019 0.158  -0.070 419 ALA EEE C   
6518  O O   . ALA E 90  ? 1.592 1.732 1.541 -0.024 0.144  -0.058 419 ALA EEE O   
6519  C CB  . ALA E 90  ? 1.570 1.857 1.603 0.043  0.157  -0.095 419 ALA EEE CB  
6520  N N   . ASP E 91  ? 1.639 1.859 1.599 -0.050 0.179  -0.077 420 ASP EEE N   
6521  C CA  . ASP E 91  ? 1.688 1.908 1.638 -0.099 0.185  -0.073 420 ASP EEE CA  
6522  C C   . ASP E 91  ? 1.705 1.844 1.592 -0.127 0.189  -0.055 420 ASP EEE C   
6523  O O   . ASP E 91  ? 1.768 1.874 1.635 -0.163 0.186  -0.047 420 ASP EEE O   
6524  C CB  . ASP E 91  ? 1.754 2.071 1.743 -0.123 0.208  -0.091 420 ASP EEE CB  
6525  C CG  . ASP E 91  ? 1.765 2.163 1.818 -0.105 0.196  -0.107 420 ASP EEE CG  
6526  O OD1 . ASP E 91  ? 1.770 2.140 1.823 -0.099 0.171  -0.103 420 ASP EEE OD1 
6527  O OD2 . ASP E 91  ? 1.811 2.303 1.912 -0.095 0.210  -0.124 420 ASP EEE OD2 
6528  N N   . TYR E 92  ? 1.674 1.777 1.528 -0.113 0.192  -0.048 421 TYR EEE N   
6529  C CA  . TYR E 92  ? 1.720 1.750 1.508 -0.140 0.193  -0.029 421 TYR EEE CA  
6530  C C   . TYR E 92  ? 1.723 1.681 1.487 -0.113 0.167  -0.013 421 TYR EEE C   
6531  O O   . TYR E 92  ? 1.779 1.673 1.490 -0.131 0.160  0.006  421 TYR EEE O   
6532  C CB  . TYR E 92  ? 1.738 1.795 1.498 -0.158 0.220  -0.034 421 TYR EEE CB  
6533  C CG  . TYR E 92  ? 1.723 1.860 1.508 -0.191 0.251  -0.048 421 TYR EEE CG  
6534  C CD1 . TYR E 92  ? 1.735 1.871 1.522 -0.236 0.254  -0.041 421 TYR EEE CD1 
6535  C CD2 . TYR E 92  ? 1.713 1.929 1.524 -0.179 0.278  -0.070 421 TYR EEE CD2 
6536  C CE1 . TYR E 92  ? 1.755 1.974 1.572 -0.273 0.282  -0.053 421 TYR EEE CE1 
6537  C CE2 . TYR E 92  ? 1.714 2.021 1.560 -0.208 0.309  -0.083 421 TYR EEE CE2 
6538  C CZ  . TYR E 92  ? 1.737 2.050 1.589 -0.259 0.310  -0.074 421 TYR EEE CZ  
6539  O OH  . TYR E 92  ? 1.764 2.177 1.659 -0.294 0.340  -0.086 421 TYR EEE OH  
6540  N N   . ASN E 93  ? 1.665 1.632 1.463 -0.075 0.152  -0.017 422 ASN EEE N   
6541  C CA  . ASN E 93  ? 1.658 1.573 1.442 -0.053 0.130  -0.003 422 ASN EEE CA  
6542  C C   . ASN E 93  ? 1.636 1.542 1.453 -0.031 0.114  0.003  422 ASN EEE C   
6543  O O   . ASN E 93  ? 1.682 1.540 1.483 -0.032 0.100  0.018  422 ASN EEE O   
6544  C CB  . ASN E 93  ? 1.634 1.560 1.417 -0.034 0.131  -0.012 422 ASN EEE CB  
6545  C CG  . ASN E 93  ? 1.665 1.590 1.402 -0.054 0.148  -0.018 422 ASN EEE CG  
6546  O OD1 . ASN E 93  ? 1.690 1.567 1.379 -0.062 0.137  -0.007 422 ASN EEE OD1 
6547  N ND2 . ASN E 93  ? 1.642 1.623 1.392 -0.063 0.175  -0.035 422 ASN EEE ND2 
6548  N N   . TYR E 94  ? 1.592 1.539 1.447 -0.010 0.116  -0.008 423 TYR EEE N   
6549  C CA  . TYR E 94  ? 1.552 1.498 1.433 0.011  0.105  -0.004 423 TYR EEE CA  
6550  C C   . TYR E 94  ? 1.506 1.501 1.414 0.016  0.111  -0.018 423 TYR EEE C   
6551  O O   . TYR E 94  ? 1.445 1.474 1.373 0.035  0.112  -0.026 423 TYR EEE O   
6552  C CB  . TYR E 94  ? 1.544 1.479 1.436 0.034  0.095  0.004  423 TYR EEE CB  
6553  C CG  . TYR E 94  ? 1.539 1.473 1.453 0.052  0.089  0.012  423 TYR EEE CG  
6554  C CD1 . TYR E 94  ? 1.571 1.480 1.483 0.053  0.084  0.022  423 TYR EEE CD1 
6555  C CD2 . TYR E 94  ? 1.517 1.473 1.449 0.070  0.089  0.010  423 TYR EEE CD2 
6556  C CE1 . TYR E 94  ? 1.557 1.472 1.488 0.070  0.084  0.027  423 TYR EEE CE1 
6557  C CE2 . TYR E 94  ? 1.494 1.450 1.438 0.083  0.088  0.019  423 TYR EEE CE2 
6558  C CZ  . TYR E 94  ? 1.520 1.459 1.465 0.083  0.087  0.026  423 TYR EEE CZ  
6559  O OH  . TYR E 94  ? 1.534 1.479 1.488 0.096  0.092  0.033  423 TYR EEE OH  
6560  N N   . LYS E 95  ? 1.717 1.601 1.219 -0.007 0.092  -0.038 424 LYS EEE N   
6561  C CA  . LYS E 95  ? 1.759 1.665 1.252 -0.029 0.084  -0.045 424 LYS EEE CA  
6562  C C   . LYS E 95  ? 1.746 1.635 1.227 -0.007 0.085  -0.041 424 LYS EEE C   
6563  O O   . LYS E 95  ? 1.773 1.610 1.227 0.015  0.096  -0.036 424 LYS EEE O   
6564  C CB  . LYS E 95  ? 1.872 1.738 1.310 -0.068 0.084  -0.053 424 LYS EEE CB  
6565  C CG  . LYS E 95  ? 1.923 1.827 1.361 -0.100 0.070  -0.058 424 LYS EEE CG  
6566  C CD  . LYS E 95  ? 1.944 1.910 1.416 -0.130 0.065  -0.057 424 LYS EEE CD  
6567  C CE  . LYS E 95  ? 1.986 2.002 1.467 -0.162 0.050  -0.057 424 LYS EEE CE  
6568  N NZ  . LYS E 95  ? 1.945 2.041 1.490 -0.141 0.043  -0.050 424 LYS EEE NZ  
6569  N N   . LEU E 96  ? 1.727 1.661 1.230 -0.011 0.076  -0.041 425 LEU EEE N   
6570  C CA  . LEU E 96  ? 1.774 1.693 1.254 0.003  0.076  -0.038 425 LEU EEE CA  
6571  C C   . LEU E 96  ? 1.828 1.739 1.264 -0.031 0.065  -0.048 425 LEU EEE C   
6572  O O   . LEU E 96  ? 1.838 1.796 1.295 -0.060 0.053  -0.050 425 LEU EEE O   
6573  C CB  . LEU E 96  ? 1.729 1.708 1.270 0.028  0.071  -0.027 425 LEU EEE CB  
6574  C CG  . LEU E 96  ? 1.715 1.691 1.290 0.063  0.080  -0.014 425 LEU EEE CG  
6575  C CD1 . LEU E 96  ? 1.672 1.702 1.303 0.081  0.073  -0.003 425 LEU EEE CD1 
6576  C CD2 . LEU E 96  ? 1.753 1.671 1.285 0.083  0.094  -0.009 425 LEU EEE CD2 
6577  N N   . PRO E 97  ? 1.888 1.741 1.259 -0.030 0.070  -0.053 426 PRO EEE N   
6578  C CA  . PRO E 97  ? 1.968 1.801 1.284 -0.067 0.056  -0.063 426 PRO EEE CA  
6579  C C   . PRO E 97  ? 1.956 1.860 1.305 -0.070 0.040  -0.057 426 PRO EEE C   
6580  O O   . PRO E 97  ? 1.890 1.831 1.285 -0.037 0.044  -0.045 426 PRO EEE O   
6581  C CB  . PRO E 97  ? 2.052 1.790 1.283 -0.054 0.071  -0.070 426 PRO EEE CB  
6582  C CG  . PRO E 97  ? 2.001 1.748 1.268 -0.003 0.089  -0.056 426 PRO EEE CG  
6583  C CD  . PRO E 97  ? 1.905 1.705 1.249 0.007  0.088  -0.047 426 PRO EEE CD  
6584  N N   . ASP E 98  ? 2.041 1.960 1.365 -0.111 0.020  -0.062 427 ASP EEE N   
6585  C CA  . ASP E 98  ? 2.061 2.057 1.420 -0.120 -0.001 -0.053 427 ASP EEE CA  
6586  C C   . ASP E 98  ? 2.100 2.071 1.426 -0.092 0.003  -0.049 427 ASP EEE C   
6587  O O   . ASP E 98  ? 2.126 2.162 1.504 -0.073 -0.004 -0.035 427 ASP EEE O   
6588  C CB  . ASP E 98  ? 2.137 2.148 1.468 -0.175 -0.025 -0.058 427 ASP EEE CB  
6589  C CG  . ASP E 98  ? 2.171 2.183 1.513 -0.205 -0.024 -0.063 427 ASP EEE CG  
6590  O OD1 . ASP E 98  ? 2.139 2.197 1.548 -0.187 -0.013 -0.056 427 ASP EEE OD1 
6591  O OD2 . ASP E 98  ? 2.272 2.233 1.549 -0.249 -0.033 -0.073 427 ASP EEE OD2 
6592  N N   . ASP E 99  ? 2.132 2.012 1.374 -0.088 0.016  -0.061 428 ASP EEE N   
6593  C CA  . ASP E 99  ? 2.115 1.959 1.313 -0.059 0.027  -0.058 428 ASP EEE CA  
6594  C C   . ASP E 99  ? 2.009 1.841 1.241 -0.010 0.055  -0.047 428 ASP EEE C   
6595  O O   . ASP E 99  ? 2.065 1.827 1.239 0.013  0.076  -0.050 428 ASP EEE O   
6596  C CB  . ASP E 99  ? 2.264 2.012 1.346 -0.081 0.029  -0.076 428 ASP EEE CB  
6597  C CG  . ASP E 99  ? 2.363 2.022 1.391 -0.088 0.044  -0.091 428 ASP EEE CG  
6598  O OD1 . ASP E 99  ? 2.313 1.974 1.387 -0.060 0.063  -0.084 428 ASP EEE OD1 
6599  O OD2 . ASP E 99  ? 2.505 2.090 1.443 -0.123 0.037  -0.108 428 ASP EEE OD2 
6600  N N   . PHE E 100 ? 1.864 1.761 1.185 0.007  0.054  -0.035 429 PHE EEE N   
6601  C CA  . PHE E 100 ? 1.797 1.696 1.162 0.049  0.074  -0.021 429 PHE EEE CA  
6602  C C   . PHE E 100 ? 1.761 1.682 1.137 0.076  0.079  -0.005 429 PHE EEE C   
6603  O O   . PHE E 100 ? 1.719 1.695 1.121 0.067  0.061  0.001  429 PHE EEE O   
6604  C CB  . PHE E 100 ? 1.722 1.677 1.169 0.052  0.069  -0.015 429 PHE EEE CB  
6605  C CG  . PHE E 100 ? 1.655 1.618 1.150 0.088  0.082  0.000  429 PHE EEE CG  
6606  C CD1 . PHE E 100 ? 1.671 1.580 1.137 0.109  0.102  0.003  429 PHE EEE CD1 
6607  C CD2 . PHE E 100 ? 1.575 1.599 1.143 0.101  0.074  0.013  429 PHE EEE CD2 
6608  C CE1 . PHE E 100 ? 1.622 1.548 1.138 0.139  0.112  0.021  429 PHE EEE CE1 
6609  C CE2 . PHE E 100 ? 1.521 1.551 1.131 0.128  0.083  0.028  429 PHE EEE CE2 
6610  C CZ  . PHE E 100 ? 1.546 1.531 1.132 0.146  0.100  0.033  429 PHE EEE CZ  
6611  N N   . THR E 101 ? 1.762 1.646 1.120 0.109  0.102  0.003  430 THR EEE N   
6612  C CA  . THR E 101 ? 1.782 1.684 1.149 0.138  0.112  0.022  430 THR EEE CA  
6613  C C   . THR E 101 ? 1.742 1.663 1.171 0.172  0.128  0.042  430 THR EEE C   
6614  O O   . THR E 101 ? 1.792 1.674 1.192 0.198  0.153  0.049  430 THR EEE O   
6615  C CB  . THR E 101 ? 1.895 1.732 1.166 0.145  0.128  0.015  430 THR EEE CB  
6616  O OG1 . THR E 101 ? 1.964 1.733 1.195 0.161  0.152  0.008  430 THR EEE OG1 
6617  C CG2 . THR E 101 ? 1.970 1.786 1.176 0.106  0.107  -0.005 430 THR EEE CG2 
6618  N N   . GLY E 102 ? 1.686 1.664 1.194 0.170  0.115  0.051  431 GLY EEE N   
6619  C CA  . GLY E 102 ? 1.664 1.663 1.235 0.194  0.122  0.070  431 GLY EEE CA  
6620  C C   . GLY E 102 ? 1.617 1.675 1.261 0.189  0.103  0.078  431 GLY EEE C   
6621  O O   . GLY E 102 ? 1.622 1.708 1.270 0.175  0.088  0.074  431 GLY EEE O   
6622  N N   . CYS E 103 ? 1.591 1.663 1.288 0.200  0.103  0.090  432 CYS EEE N   
6623  C CA  . CYS E 103 ? 1.540 1.655 1.302 0.197  0.087  0.097  432 CYS EEE CA  
6624  C C   . CYS E 103 ? 1.511 1.620 1.298 0.192  0.082  0.090  432 CYS EEE C   
6625  O O   . CYS E 103 ? 1.542 1.624 1.315 0.198  0.092  0.093  432 CYS EEE O   
6626  C CB  . CYS E 103 ? 1.538 1.677 1.339 0.215  0.088  0.124  432 CYS EEE CB  
6627  S SG  . CYS E 103 ? 1.618 1.763 1.383 0.224  0.097  0.136  432 CYS EEE SG  
6628  N N   . VAL E 104 ? 1.461 1.593 1.280 0.182  0.067  0.083  433 VAL EEE N   
6629  C CA  . VAL E 104 ? 1.433 1.561 1.273 0.175  0.060  0.075  433 VAL EEE CA  
6630  C C   . VAL E 104 ? 1.404 1.548 1.294 0.185  0.051  0.091  433 VAL EEE C   
6631  O O   . VAL E 104 ? 1.404 1.570 1.316 0.188  0.044  0.096  433 VAL EEE O   
6632  C CB  . VAL E 104 ? 1.461 1.601 1.295 0.159  0.054  0.054  433 VAL EEE CB  
6633  C CG1 . VAL E 104 ? 1.464 1.604 1.320 0.155  0.047  0.046  433 VAL EEE CG1 
6634  C CG2 . VAL E 104 ? 1.496 1.613 1.279 0.143  0.061  0.039  433 VAL EEE CG2 
6635  N N   . ILE E 105 ? 1.398 1.531 1.304 0.188  0.050  0.102  434 ILE EEE N   
6636  C CA  . ILE E 105 ? 1.400 1.542 1.350 0.192  0.038  0.120  434 ILE EEE CA  
6637  C C   . ILE E 105 ? 1.388 1.515 1.343 0.181  0.026  0.109  434 ILE EEE C   
6638  O O   . ILE E 105 ? 1.402 1.516 1.342 0.178  0.029  0.108  434 ILE EEE O   
6639  C CB  . ILE E 105 ? 1.407 1.558 1.374 0.203  0.046  0.149  434 ILE EEE CB  
6640  C CG1 . ILE E 105 ? 1.429 1.587 1.373 0.215  0.063  0.155  434 ILE EEE CG1 
6641  C CG2 . ILE E 105 ? 1.384 1.549 1.398 0.202  0.032  0.170  434 ILE EEE CG2 
6642  C CD1 . ILE E 105 ? 1.457 1.617 1.399 0.231  0.079  0.178  434 ILE EEE CD1 
6643  N N   . ALA E 106 ? 1.378 1.503 1.350 0.177  0.014  0.101  435 ALA EEE N   
6644  C CA  . ALA E 106 ? 1.403 1.507 1.368 0.167  0.004  0.085  435 ALA EEE CA  
6645  C C   . ALA E 106 ? 1.420 1.511 1.410 0.165  -0.012 0.092  435 ALA EEE C   
6646  O O   . ALA E 106 ? 1.444 1.542 1.450 0.173  -0.013 0.095  435 ALA EEE O   
6647  C CB  . ALA E 106 ? 1.417 1.522 1.359 0.165  0.011  0.060  435 ALA EEE CB  
6648  N N   . TRP E 107 ? 1.440 1.511 1.431 0.153  -0.026 0.095  436 TRP EEE N   
6649  C CA  . TRP E 107 ? 1.479 1.525 1.482 0.145  -0.045 0.099  436 TRP EEE CA  
6650  C C   . TRP E 107 ? 1.493 1.505 1.464 0.133  -0.054 0.076  436 TRP EEE C   
6651  O O   . TRP E 107 ? 1.494 1.508 1.445 0.128  -0.051 0.071  436 TRP EEE O   
6652  C CB  . TRP E 107 ? 1.506 1.564 1.544 0.137  -0.058 0.131  436 TRP EEE CB  
6653  C CG  . TRP E 107 ? 1.519 1.588 1.558 0.128  -0.063 0.144  436 TRP EEE CG  
6654  C CD1 . TRP E 107 ? 1.563 1.614 1.598 0.110  -0.084 0.146  436 TRP EEE CD1 
6655  C CD2 . TRP E 107 ? 1.511 1.609 1.555 0.139  -0.047 0.159  436 TRP EEE CD2 
6656  N NE1 . TRP E 107 ? 1.566 1.640 1.608 0.110  -0.083 0.164  436 TRP EEE NE1 
6657  C CE2 . TRP E 107 ? 1.531 1.632 1.580 0.130  -0.059 0.172  436 TRP EEE CE2 
6658  C CE3 . TRP E 107 ? 1.511 1.630 1.553 0.157  -0.024 0.163  436 TRP EEE CE3 
6659  C CZ2 . TRP E 107 ? 1.536 1.660 1.589 0.141  -0.046 0.190  436 TRP EEE CZ2 
6660  C CZ3 . TRP E 107 ? 1.523 1.656 1.562 0.167  -0.011 0.177  436 TRP EEE CZ3 
6661  C CH2 . TRP E 107 ? 1.537 1.673 1.584 0.161  -0.021 0.191  436 TRP EEE CH2 
6662  N N   . ASN E 108 ? 1.519 1.495 1.481 0.131  -0.064 0.064  437 ASN EEE N   
6663  C CA  . ASN E 108 ? 1.556 1.490 1.479 0.120  -0.074 0.042  437 ASN EEE CA  
6664  C C   . ASN E 108 ? 1.541 1.466 1.464 0.097  -0.097 0.058  437 ASN EEE C   
6665  O O   . ASN E 108 ? 1.528 1.464 1.486 0.089  -0.111 0.084  437 ASN EEE O   
6666  C CB  . ASN E 108 ? 1.618 1.506 1.527 0.125  -0.079 0.027  437 ASN EEE CB  
6667  C CG  . ASN E 108 ? 1.673 1.513 1.530 0.119  -0.082 -0.001 437 ASN EEE CG  
6668  O OD1 . ASN E 108 ? 1.697 1.512 1.532 0.097  -0.102 0.001  437 ASN EEE OD1 
6669  N ND2 . ASN E 108 ? 1.701 1.530 1.536 0.138  -0.063 -0.024 437 ASN EEE ND2 
6670  N N   . SER E 109 ? 1.545 1.457 1.433 0.088  -0.100 0.045  438 SER EEE N   
6671  C CA  . SER E 109 ? 1.577 1.488 1.463 0.067  -0.123 0.061  438 SER EEE CA  
6672  C C   . SER E 109 ? 1.677 1.542 1.507 0.053  -0.135 0.037  438 SER EEE C   
6673  O O   . SER E 109 ? 1.715 1.585 1.528 0.043  -0.143 0.043  438 SER EEE O   
6674  C CB  . SER E 109 ? 1.521 1.475 1.424 0.074  -0.112 0.079  438 SER EEE CB  
6675  O OG  . SER E 109 ? 1.488 1.443 1.360 0.085  -0.089 0.058  438 SER EEE OG  
6676  N N   . ASN E 110 ? 1.745 1.561 1.543 0.055  -0.136 0.013  439 ASN EEE N   
6677  C CA  . ASN E 110 ? 1.804 1.563 1.540 0.040  -0.150 -0.011 439 ASN EEE CA  
6678  C C   . ASN E 110 ? 1.831 1.581 1.570 0.009  -0.187 0.011  439 ASN EEE C   
6679  O O   . ASN E 110 ? 1.842 1.585 1.548 -0.005 -0.199 0.009  439 ASN EEE O   
6680  C CB  . ASN E 110 ? 1.859 1.564 1.565 0.051  -0.143 -0.037 439 ASN EEE CB  
6681  C CG  . ASN E 110 ? 1.922 1.575 1.555 0.052  -0.136 -0.070 439 ASN EEE CG  
6682  O OD1 . ASN E 110 ? 1.888 1.558 1.496 0.053  -0.125 -0.077 439 ASN EEE OD1 
6683  N ND2 . ASN E 110 ? 2.002 1.588 1.596 0.055  -0.140 -0.090 439 ASN EEE ND2 
6684  N N   . ASN E 111 ? 1.847 1.604 1.630 -0.001 -0.205 0.035  440 ASN EEE N   
6685  C CA  . ASN E 111 ? 1.870 1.626 1.671 -0.035 -0.244 0.061  440 ASN EEE CA  
6686  C C   . ASN E 111 ? 1.788 1.594 1.605 -0.044 -0.254 0.085  440 ASN EEE C   
6687  O O   . ASN E 111 ? 1.806 1.607 1.621 -0.074 -0.289 0.102  440 ASN EEE O   
6688  C CB  . ASN E 111 ? 1.908 1.684 1.769 -0.040 -0.252 0.090  440 ASN EEE CB  
6689  C CG  . ASN E 111 ? 1.863 1.710 1.785 -0.015 -0.226 0.115  440 ASN EEE CG  
6690  O OD1 . ASN E 111 ? 1.865 1.722 1.785 0.013  -0.195 0.099  440 ASN EEE OD1 
6691  N ND2 . ASN E 111 ? 1.815 1.713 1.793 -0.026 -0.239 0.155  440 ASN EEE ND2 
6692  N N   . LEU E 112 ? 1.705 1.553 1.535 -0.019 -0.226 0.088  441 LEU EEE N   
6693  C CA  . LEU E 112 ? 1.680 1.578 1.534 -0.020 -0.230 0.116  441 LEU EEE CA  
6694  C C   . LEU E 112 ? 1.675 1.561 1.478 -0.013 -0.217 0.096  441 LEU EEE C   
6695  O O   . LEU E 112 ? 1.694 1.596 1.493 -0.023 -0.234 0.114  441 LEU EEE O   
6696  C CB  . LEU E 112 ? 1.636 1.592 1.552 0.003  -0.207 0.142  441 LEU EEE CB  
6697  C CG  . LEU E 112 ? 1.651 1.631 1.623 -0.004 -0.218 0.169  441 LEU EEE CG  
6698  C CD1 . LEU E 112 ? 1.611 1.634 1.626 0.024  -0.187 0.184  441 LEU EEE CD1 
6699  C CD2 . LEU E 112 ? 1.665 1.674 1.671 -0.030 -0.252 0.206  441 LEU EEE CD2 
6700  N N   . ASP E 113 ? 1.661 1.524 1.428 0.005  -0.188 0.063  442 ASP EEE N   
6701  C CA  . ASP E 113 ? 1.661 1.525 1.392 0.015  -0.168 0.050  442 ASP EEE CA  
6702  C C   . ASP E 113 ? 1.720 1.532 1.381 0.008  -0.166 0.014  442 ASP EEE C   
6703  O O   . ASP E 113 ? 1.718 1.529 1.349 0.018  -0.142 -0.001 442 ASP EEE O   
6704  C CB  . ASP E 113 ? 1.606 1.500 1.362 0.040  -0.133 0.048  442 ASP EEE CB  
6705  C CG  . ASP E 113 ? 1.549 1.489 1.363 0.050  -0.129 0.080  442 ASP EEE CG  
6706  O OD1 . ASP E 113 ? 1.563 1.522 1.389 0.047  -0.140 0.105  442 ASP EEE OD1 
6707  O OD2 . ASP E 113 ? 1.488 1.445 1.333 0.064  -0.114 0.082  442 ASP EEE OD2 
6708  N N   . SER E 114 ? 1.782 1.547 1.412 -0.009 -0.189 0.003  443 SER EEE N   
6709  C CA  . SER E 114 ? 1.840 1.547 1.396 -0.013 -0.186 -0.033 443 SER EEE CA  
6710  C C   . SER E 114 ? 1.927 1.590 1.434 -0.043 -0.224 -0.033 443 SER EEE C   
6711  O O   . SER E 114 ? 1.919 1.565 1.441 -0.063 -0.254 -0.022 443 SER EEE O   
6712  C CB  . SER E 114 ? 1.848 1.524 1.402 0.002  -0.170 -0.055 443 SER EEE CB  
6713  O OG  . SER E 114 ? 1.768 1.488 1.366 0.028  -0.138 -0.054 443 SER EEE OG  
6714  N N   . LYS E 115 ? 2.021 1.663 1.466 -0.050 -0.224 -0.045 444 LYS EEE N   
6715  C CA  . LYS E 115 ? 2.170 1.763 1.549 -0.080 -0.260 -0.050 444 LYS EEE CA  
6716  C C   . LYS E 115 ? 2.236 1.754 1.531 -0.076 -0.247 -0.092 444 LYS EEE C   
6717  O O   . LYS E 115 ? 2.197 1.718 1.484 -0.048 -0.206 -0.113 444 LYS EEE O   
6718  C CB  . LYS E 115 ? 2.240 1.859 1.601 -0.088 -0.268 -0.033 444 LYS EEE CB  
6719  C CG  . LYS E 115 ? 2.244 1.933 1.683 -0.084 -0.275 0.009  444 LYS EEE CG  
6720  C CD  . LYS E 115 ? 2.301 2.012 1.723 -0.088 -0.282 0.029  444 LYS EEE CD  
6721  C CE  . LYS E 115 ? 2.258 2.034 1.754 -0.070 -0.271 0.064  444 LYS EEE CE  
6722  N NZ  . LYS E 115 ? 2.300 2.098 1.791 -0.077 -0.290 0.094  444 LYS EEE NZ  
6723  N N   . VAL E 116 ? 2.329 1.785 1.563 -0.104 -0.282 -0.103 445 VAL EEE N   
6724  C CA  . VAL E 116 ? 2.441 1.811 1.576 -0.102 -0.272 -0.144 445 VAL EEE CA  
6725  C C   . VAL E 116 ? 2.441 1.819 1.527 -0.086 -0.240 -0.159 445 VAL EEE C   
6726  O O   . VAL E 116 ? 2.466 1.821 1.519 -0.058 -0.201 -0.187 445 VAL EEE O   
6727  C CB  . VAL E 116 ? 2.567 1.864 1.635 -0.141 -0.321 -0.151 445 VAL EEE CB  
6728  C CG1 . VAL E 116 ? 2.557 1.841 1.673 -0.158 -0.348 -0.138 445 VAL EEE CG1 
6729  C CG2 . VAL E 116 ? 2.598 1.917 1.646 -0.173 -0.358 -0.127 445 VAL EEE CG2 
6730  N N   . GLY E 117 ? 2.405 1.821 1.492 -0.100 -0.255 -0.135 446 GLY EEE N   
6731  C CA  . GLY E 117 ? 2.420 1.846 1.461 -0.090 -0.228 -0.142 446 GLY EEE CA  
6732  C C   . GLY E 117 ? 2.344 1.828 1.443 -0.059 -0.183 -0.139 446 GLY EEE C   
6733  O O   . GLY E 117 ? 2.339 1.829 1.400 -0.049 -0.154 -0.148 446 GLY EEE O   
6734  N N   . GLY E 118 ? 2.294 1.821 1.478 -0.046 -0.177 -0.125 447 GLY EEE N   
6735  C CA  . GLY E 118 ? 2.215 1.799 1.460 -0.021 -0.139 -0.119 447 GLY EEE CA  
6736  C C   . GLY E 118 ? 2.148 1.788 1.447 -0.025 -0.147 -0.084 447 GLY EEE C   
6737  O O   . GLY E 118 ? 2.187 1.827 1.451 -0.036 -0.153 -0.075 447 GLY EEE O   
6738  N N   . ASN E 119 ? 2.081 1.763 1.458 -0.016 -0.147 -0.065 448 ASN EEE N   
6739  C CA  . ASN E 119 ? 2.033 1.764 1.462 -0.015 -0.150 -0.032 448 ASN EEE CA  
6740  C C   . ASN E 119 ? 2.020 1.773 1.448 0.000  -0.114 -0.036 448 ASN EEE C   
6741  O O   . ASN E 119 ? 1.989 1.767 1.457 0.016  -0.090 -0.040 448 ASN EEE O   
6742  C CB  . ASN E 119 ? 1.965 1.729 1.469 -0.009 -0.160 -0.011 448 ASN EEE CB  
6743  C CG  . ASN E 119 ? 1.888 1.695 1.438 -0.007 -0.166 0.026  448 ASN EEE CG  
6744  O OD1 . ASN E 119 ? 1.850 1.664 1.383 -0.003 -0.157 0.033  448 ASN EEE OD1 
6745  N ND2 . ASN E 119 ? 1.842 1.678 1.452 -0.006 -0.182 0.050  448 ASN EEE ND2 
6746  N N   . TYR E 120 ? 2.051 1.794 1.432 -0.008 -0.112 -0.033 449 TYR EEE N   
6747  C CA  . TYR E 120 ? 2.015 1.770 1.382 0.000  -0.080 -0.036 449 TYR EEE CA  
6748  C C   . TYR E 120 ? 1.938 1.723 1.349 0.006  -0.078 -0.007 449 TYR EEE C   
6749  O O   . TYR E 120 ? 1.873 1.664 1.275 0.009  -0.054 -0.008 449 TYR EEE O   
6750  C CB  . TYR E 120 ? 2.077 1.802 1.368 -0.012 -0.078 -0.046 449 TYR EEE CB  
6751  C CG  . TYR E 120 ? 2.120 1.810 1.358 -0.013 -0.071 -0.077 449 TYR EEE CG  
6752  C CD1 . TYR E 120 ? 2.110 1.809 1.352 0.002  -0.037 -0.100 449 TYR EEE CD1 
6753  C CD2 . TYR E 120 ? 2.182 1.830 1.361 -0.028 -0.098 -0.083 449 TYR EEE CD2 
6754  C CE1 . TYR E 120 ? 2.150 1.816 1.342 0.007  -0.026 -0.128 449 TYR EEE CE1 
6755  C CE2 . TYR E 120 ? 2.246 1.852 1.366 -0.027 -0.089 -0.114 449 TYR EEE CE2 
6756  C CZ  . TYR E 120 ? 2.226 1.840 1.353 -0.007 -0.051 -0.136 449 TYR EEE CZ  
6757  O OH  . TYR E 120 ? 2.311 1.882 1.379 0.001  -0.038 -0.166 449 TYR EEE OH  
6758  N N   . ASN E 121 ? 1.926 1.726 1.380 0.007  -0.102 0.017  450 ASN EEE N   
6759  C CA  . ASN E 121 ? 1.910 1.733 1.399 0.017  -0.102 0.048  450 ASN EEE CA  
6760  C C   . ASN E 121 ? 1.857 1.701 1.389 0.034  -0.076 0.046  450 ASN EEE C   
6761  O O   . ASN E 121 ? 1.861 1.714 1.411 0.045  -0.069 0.067  450 ASN EEE O   
6762  C CB  . ASN E 121 ? 1.919 1.759 1.444 0.014  -0.135 0.078  450 ASN EEE CB  
6763  C CG  . ASN E 121 ? 1.987 1.811 1.470 -0.005 -0.166 0.086  450 ASN EEE CG  
6764  O OD1 . ASN E 121 ? 2.026 1.834 1.492 -0.022 -0.189 0.075  450 ASN EEE OD1 
6765  N ND2 . ASN E 121 ? 2.035 1.856 1.497 -0.003 -0.168 0.107  450 ASN EEE ND2 
6766  N N   . TYR E 122 ? 1.821 1.671 1.367 0.037  -0.063 0.024  451 TYR EEE N   
6767  C CA  . TYR E 122 ? 1.764 1.634 1.341 0.049  -0.039 0.019  451 TYR EEE CA  
6768  C C   . TYR E 122 ? 1.741 1.605 1.284 0.044  -0.014 -0.002 451 TYR EEE C   
6769  O O   . TYR E 122 ? 1.768 1.622 1.282 0.038  -0.010 -0.021 451 TYR EEE O   
6770  C CB  . TYR E 122 ? 1.768 1.655 1.386 0.056  -0.042 0.012  451 TYR EEE CB  
6771  C CG  . TYR E 122 ? 1.782 1.685 1.445 0.062  -0.060 0.038  451 TYR EEE CG  
6772  C CD1 . TYR E 122 ? 1.776 1.700 1.472 0.076  -0.049 0.055  451 TYR EEE CD1 
6773  C CD2 . TYR E 122 ? 1.841 1.739 1.512 0.051  -0.089 0.046  451 TYR EEE CD2 
6774  C CE1 . TYR E 122 ? 1.806 1.752 1.547 0.083  -0.062 0.082  451 TYR EEE CE1 
6775  C CE2 . TYR E 122 ? 1.853 1.775 1.572 0.054  -0.105 0.074  451 TYR EEE CE2 
6776  C CZ  . TYR E 122 ? 1.835 1.785 1.592 0.071  -0.090 0.093  451 TYR EEE CZ  
6777  O OH  . TYR E 122 ? 1.848 1.827 1.655 0.076  -0.103 0.123  451 TYR EEE OH  
6778  N N   . LEU E 123 ? 1.697 1.564 1.241 0.047  0.004  0.004  452 LEU EEE N   
6779  C CA  . LEU E 123 ? 1.697 1.558 1.208 0.036  0.026  -0.008 452 LEU EEE CA  
6780  C C   . LEU E 123 ? 1.646 1.528 1.180 0.038  0.043  -0.016 452 LEU EEE C   
6781  O O   . LEU E 123 ? 1.598 1.494 1.170 0.050  0.039  -0.010 452 LEU EEE O   
6782  C CB  . LEU E 123 ? 1.746 1.580 1.224 0.031  0.026  0.009  452 LEU EEE CB  
6783  C CG  . LEU E 123 ? 1.809 1.628 1.271 0.031  0.003  0.025  452 LEU EEE CG  
6784  C CD1 . LEU E 123 ? 1.846 1.639 1.284 0.032  0.004  0.047  452 LEU EEE CD1 
6785  C CD2 . LEU E 123 ? 1.867 1.677 1.291 0.018  -0.002 0.009  452 LEU EEE CD2 
6786  N N   . TYR E 124 ? 1.645 1.530 1.157 0.024  0.061  -0.025 453 TYR EEE N   
6787  C CA  . TYR E 124 ? 1.632 1.540 1.160 0.019  0.076  -0.032 453 TYR EEE CA  
6788  C C   . TYR E 124 ? 1.655 1.557 1.148 -0.003 0.092  -0.035 453 TYR EEE C   
6789  O O   . TYR E 124 ? 1.687 1.587 1.155 -0.011 0.097  -0.039 453 TYR EEE O   
6790  C CB  . TYR E 124 ? 1.639 1.586 1.201 0.027  0.079  -0.046 453 TYR EEE CB  
6791  C CG  . TYR E 124 ? 1.681 1.646 1.231 0.023  0.091  -0.060 453 TYR EEE CG  
6792  C CD1 . TYR E 124 ? 1.732 1.677 1.258 0.028  0.086  -0.066 453 TYR EEE CD1 
6793  C CD2 . TYR E 124 ? 1.697 1.700 1.259 0.014  0.108  -0.066 453 TYR EEE CD2 
6794  C CE1 . TYR E 124 ? 1.781 1.739 1.289 0.028  0.101  -0.079 453 TYR EEE CE1 
6795  C CE2 . TYR E 124 ? 1.730 1.755 1.283 0.014  0.124  -0.076 453 TYR EEE CE2 
6796  C CZ  . TYR E 124 ? 1.771 1.771 1.295 0.023  0.123  -0.084 453 TYR EEE CZ  
6797  O OH  . TYR E 124 ? 1.802 1.819 1.311 0.027  0.142  -0.095 453 TYR EEE OH  
6798  N N   . ARG E 125 ? 1.680 1.577 1.171 -0.015 0.099  -0.032 454 ARG EEE N   
6799  C CA  . ARG E 125 ? 1.746 1.637 1.206 -0.042 0.113  -0.032 454 ARG EEE CA  
6800  C C   . ARG E 125 ? 1.769 1.716 1.253 -0.052 0.124  -0.043 454 ARG EEE C   
6801  O O   . ARG E 125 ? 1.793 1.777 1.318 -0.038 0.121  -0.050 454 ARG EEE O   
6802  C CB  . ARG E 125 ? 1.764 1.622 1.207 -0.053 0.114  -0.026 454 ARG EEE CB  
6803  C CG  . ARG E 125 ? 1.812 1.649 1.217 -0.085 0.125  -0.024 454 ARG EEE CG  
6804  C CD  . ARG E 125 ? 1.847 1.632 1.222 -0.095 0.124  -0.019 454 ARG EEE CD  
6805  N NE  . ARG E 125 ? 1.863 1.593 1.216 -0.072 0.120  -0.008 454 ARG EEE NE  
6806  C CZ  . ARG E 125 ? 1.890 1.573 1.202 -0.075 0.123  0.004  454 ARG EEE CZ  
6807  N NH1 . ARG E 125 ? 1.904 1.584 1.191 -0.103 0.130  0.005  454 ARG EEE NH1 
6808  N NH2 . ARG E 125 ? 1.902 1.543 1.202 -0.050 0.118  0.018  454 ARG EEE NH2 
6809  N N   . LEU E 126 ? 1.827 1.783 1.290 -0.076 0.138  -0.042 455 LEU EEE N   
6810  C CA  . LEU E 126 ? 1.821 1.839 1.308 -0.083 0.152  -0.049 455 LEU EEE CA  
6811  C C   . LEU E 126 ? 1.838 1.878 1.324 -0.118 0.161  -0.043 455 LEU EEE C   
6812  O O   . LEU E 126 ? 1.803 1.906 1.329 -0.122 0.168  -0.044 455 LEU EEE O   
6813  C CB  . LEU E 126 ? 1.868 1.882 1.328 -0.078 0.163  -0.051 455 LEU EEE CB  
6814  C CG  . LEU E 126 ? 1.891 1.961 1.377 -0.066 0.179  -0.060 455 LEU EEE CG  
6815  C CD1 . LEU E 126 ? 1.859 1.952 1.389 -0.039 0.170  -0.069 455 LEU EEE CD1 
6816  C CD2 . LEU E 126 ? 1.937 1.987 1.381 -0.059 0.188  -0.065 455 LEU EEE CD2 
6817  N N   . PHE E 127 ? 1.886 1.875 1.328 -0.142 0.161  -0.034 456 PHE EEE N   
6818  C CA  . PHE E 127 ? 1.909 1.903 1.339 -0.182 0.166  -0.027 456 PHE EEE CA  
6819  C C   . PHE E 127 ? 1.904 1.824 1.296 -0.193 0.155  -0.023 456 PHE EEE C   
6820  O O   . PHE E 127 ? 1.874 1.742 1.247 -0.168 0.147  -0.023 456 PHE EEE O   
6821  C CB  . PHE E 127 ? 1.976 1.970 1.376 -0.205 0.181  -0.018 456 PHE EEE CB  
6822  C CG  . PHE E 127 ? 1.964 2.006 1.380 -0.187 0.196  -0.021 456 PHE EEE CG  
6823  C CD1 . PHE E 127 ? 1.931 2.053 1.397 -0.181 0.207  -0.025 456 PHE EEE CD1 
6824  C CD2 . PHE E 127 ? 1.992 1.997 1.368 -0.174 0.200  -0.020 456 PHE EEE CD2 
6825  C CE1 . PHE E 127 ? 1.924 2.083 1.399 -0.160 0.224  -0.030 456 PHE EEE CE1 
6826  C CE2 . PHE E 127 ? 1.997 2.038 1.377 -0.157 0.215  -0.027 456 PHE EEE CE2 
6827  C CZ  . PHE E 127 ? 1.968 2.083 1.396 -0.148 0.228  -0.032 456 PHE EEE CZ  
6828  N N   . ARG E 128 ? 1.907 1.823 1.286 -0.232 0.154  -0.019 457 ARG EEE N   
6829  C CA  . ARG E 128 ? 1.966 1.802 1.297 -0.247 0.146  -0.018 457 ARG EEE CA  
6830  C C   . ARG E 128 ? 1.988 1.834 1.308 -0.298 0.145  -0.014 457 ARG EEE C   
6831  O O   . ARG E 128 ? 1.903 1.831 1.271 -0.311 0.144  -0.015 457 ARG EEE O   
6832  C CB  . ARG E 128 ? 1.971 1.794 1.316 -0.218 0.135  -0.027 457 ARG EEE CB  
6833  C CG  . ARG E 128 ? 2.030 1.760 1.324 -0.204 0.132  -0.024 457 ARG EEE CG  
6834  C CD  . ARG E 128 ? 1.988 1.716 1.303 -0.167 0.125  -0.030 457 ARG EEE CD  
6835  N NE  . ARG E 128 ? 2.042 1.685 1.306 -0.158 0.126  -0.028 457 ARG EEE NE  
6836  C CZ  . ARG E 128 ? 2.105 1.701 1.328 -0.181 0.124  -0.034 457 ARG EEE CZ  
6837  N NH1 . ARG E 128 ? 2.107 1.744 1.340 -0.219 0.117  -0.041 457 ARG EEE NH1 
6838  N NH2 . ARG E 128 ? 2.169 1.679 1.340 -0.166 0.128  -0.033 457 ARG EEE NH2 
6839  N N   . LYS E 129 ? 2.091 1.856 1.350 -0.325 0.144  -0.009 458 LYS EEE N   
6840  C CA  . LYS E 129 ? 2.181 1.933 1.415 -0.382 0.140  -0.004 458 LYS EEE CA  
6841  C C   . LYS E 129 ? 2.167 1.963 1.430 -0.394 0.125  -0.013 458 LYS EEE C   
6842  O O   . LYS E 129 ? 2.203 2.064 1.493 -0.434 0.121  -0.007 458 LYS EEE O   
6843  C CB  . LYS E 129 ? 2.283 1.912 1.436 -0.398 0.138  -0.002 458 LYS EEE CB  
6844  C CG  . LYS E 129 ? 2.341 1.917 1.456 -0.393 0.150  0.011  458 LYS EEE CG  
6845  C CD  . LYS E 129 ? 2.418 2.007 1.519 -0.444 0.158  0.026  458 LYS EEE CD  
6846  C CE  . LYS E 129 ? 2.441 2.031 1.534 -0.429 0.172  0.040  458 LYS EEE CE  
6847  N NZ  . LYS E 129 ? 2.480 2.096 1.565 -0.478 0.182  0.056  458 LYS EEE NZ  
6848  N N   . SER E 130 ? 2.142 1.908 1.401 -0.360 0.118  -0.024 459 SER EEE N   
6849  C CA  . SER E 130 ? 2.119 1.916 1.396 -0.366 0.103  -0.033 459 SER EEE CA  
6850  C C   . SER E 130 ? 2.026 1.850 1.342 -0.311 0.103  -0.040 459 SER EEE C   
6851  O O   . SER E 130 ? 1.983 1.798 1.308 -0.274 0.112  -0.038 459 SER EEE O   
6852  C CB  . SER E 130 ? 2.219 1.920 1.424 -0.393 0.093  -0.040 459 SER EEE CB  
6853  O OG  . SER E 130 ? 2.256 1.877 1.423 -0.351 0.097  -0.047 459 SER EEE OG  
6854  N N   . ASN E 131 ? 1.990 1.844 1.324 -0.309 0.090  -0.046 460 ASN EEE N   
6855  C CA  . ASN E 131 ? 1.929 1.805 1.297 -0.261 0.088  -0.051 460 ASN EEE CA  
6856  C C   . ASN E 131 ? 1.959 1.739 1.272 -0.237 0.091  -0.056 460 ASN EEE C   
6857  O O   . ASN E 131 ? 2.013 1.714 1.259 -0.263 0.089  -0.060 460 ASN EEE O   
6858  C CB  . ASN E 131 ? 1.899 1.849 1.308 -0.270 0.075  -0.052 460 ASN EEE CB  
6859  C CG  . ASN E 131 ? 1.853 1.903 1.320 -0.291 0.075  -0.043 460 ASN EEE CG  
6860  O OD1 . ASN E 131 ? 1.781 1.877 1.290 -0.267 0.087  -0.039 460 ASN EEE OD1 
6861  N ND2 . ASN E 131 ? 1.906 1.990 1.374 -0.336 0.061  -0.039 460 ASN EEE ND2 
6862  N N   . LEU E 132 ? 1.912 1.695 1.249 -0.189 0.095  -0.056 461 LEU EEE N   
6863  C CA  . LEU E 132 ? 1.938 1.648 1.237 -0.158 0.100  -0.057 461 LEU EEE CA  
6864  C C   . LEU E 132 ? 1.989 1.673 1.254 -0.168 0.093  -0.065 461 LEU EEE C   
6865  O O   . LEU E 132 ? 1.962 1.714 1.264 -0.179 0.081  -0.067 461 LEU EEE O   
6866  C CB  . LEU E 132 ? 1.873 1.618 1.222 -0.111 0.103  -0.051 461 LEU EEE CB  
6867  C CG  . LEU E 132 ? 1.863 1.608 1.228 -0.093 0.109  -0.042 461 LEU EEE CG  
6868  C CD1 . LEU E 132 ? 1.800 1.582 1.215 -0.053 0.107  -0.037 461 LEU EEE CD1 
6869  C CD2 . LEU E 132 ? 1.943 1.601 1.250 -0.090 0.118  -0.036 461 LEU EEE CD2 
6870  N N   . LYS E 133 ? 2.084 1.674 1.281 -0.162 0.100  -0.069 462 LYS EEE N   
6871  C CA  . LYS E 133 ? 2.149 1.701 1.304 -0.157 0.097  -0.077 462 LYS EEE CA  
6872  C C   . LYS E 133 ? 2.080 1.677 1.286 -0.109 0.101  -0.071 462 LYS EEE C   
6873  O O   . LYS E 133 ? 2.049 1.670 1.298 -0.078 0.108  -0.061 462 LYS EEE O   
6874  C CB  . LYS E 133 ? 2.284 1.715 1.348 -0.156 0.108  -0.083 462 LYS EEE CB  
6875  C CG  . LYS E 133 ? 2.418 1.792 1.412 -0.212 0.097  -0.095 462 LYS EEE CG  
6876  C CD  . LYS E 133 ? 2.579 1.819 1.474 -0.208 0.110  -0.102 462 LYS EEE CD  
6877  C CE  . LYS E 133 ? 2.716 1.887 1.533 -0.268 0.097  -0.115 462 LYS EEE CE  
6878  N NZ  . LYS E 133 ? 2.752 1.915 1.568 -0.308 0.093  -0.109 462 LYS EEE NZ  
6879  N N   . PRO E 134 ? 2.063 1.674 1.263 -0.104 0.095  -0.076 463 PRO EEE N   
6880  C CA  . PRO E 134 ? 1.998 1.649 1.243 -0.061 0.100  -0.067 463 PRO EEE CA  
6881  C C   . PRO E 134 ? 2.006 1.607 1.240 -0.017 0.120  -0.057 463 PRO EEE C   
6882  O O   . PRO E 134 ? 2.089 1.605 1.255 -0.014 0.132  -0.061 463 PRO EEE O   
6883  C CB  . PRO E 134 ? 2.047 1.687 1.255 -0.068 0.094  -0.075 463 PRO EEE CB  
6884  C CG  . PRO E 134 ? 2.090 1.729 1.266 -0.123 0.076  -0.085 463 PRO EEE CG  
6885  C CD  . PRO E 134 ? 2.118 1.707 1.266 -0.143 0.082  -0.088 463 PRO EEE CD  
6886  N N   . PHE E 135 ? 1.932 1.586 1.232 0.015  0.122  -0.044 464 PHE EEE N   
6887  C CA  . PHE E 135 ? 1.941 1.569 1.248 0.056  0.137  -0.028 464 PHE EEE CA  
6888  C C   . PHE E 135 ? 2.000 1.570 1.272 0.052  0.144  -0.026 464 PHE EEE C   
6889  O O   . PHE E 135 ? 2.032 1.547 1.275 0.082  0.160  -0.016 464 PHE EEE O   
6890  C CB  . PHE E 135 ? 1.986 1.571 1.254 0.085  0.152  -0.025 464 PHE EEE CB  
6891  C CG  . PHE E 135 ? 1.947 1.585 1.247 0.096  0.148  -0.022 464 PHE EEE CG  
6892  C CD1 . PHE E 135 ? 1.864 1.579 1.244 0.111  0.140  -0.008 464 PHE EEE CD1 
6893  C CD2 . PHE E 135 ? 2.006 1.612 1.252 0.092  0.151  -0.032 464 PHE EEE CD2 
6894  C CE1 . PHE E 135 ? 1.813 1.573 1.222 0.121  0.136  -0.003 464 PHE EEE CE1 
6895  C CE2 . PHE E 135 ? 1.989 1.645 1.263 0.102  0.147  -0.026 464 PHE EEE CE2 
6896  C CZ  . PHE E 135 ? 1.893 1.626 1.250 0.117  0.140  -0.011 464 PHE EEE CZ  
6897  N N   . GLU E 136 ? 2.036 1.619 1.311 0.018  0.135  -0.033 465 GLU EEE N   
6898  C CA  . GLU E 136 ? 2.118 1.651 1.364 0.013  0.140  -0.028 465 GLU EEE CA  
6899  C C   . GLU E 136 ? 2.083 1.667 1.389 0.033  0.136  -0.013 465 GLU EEE C   
6900  O O   . GLU E 136 ? 2.061 1.718 1.425 0.033  0.126  -0.014 465 GLU EEE O   
6901  C CB  . GLU E 136 ? 2.170 1.684 1.382 -0.035 0.134  -0.039 465 GLU EEE CB  
6902  C CG  . GLU E 136 ? 2.229 1.682 1.402 -0.040 0.141  -0.032 465 GLU EEE CG  
6903  C CD  . GLU E 136 ? 2.314 1.723 1.435 -0.089 0.138  -0.041 465 GLU EEE CD  
6904  O OE1 . GLU E 136 ? 2.330 1.767 1.450 -0.124 0.128  -0.053 465 GLU EEE OE1 
6905  O OE2 . GLU E 136 ? 2.370 1.721 1.454 -0.094 0.145  -0.034 465 GLU EEE OE2 
6906  N N   . ARG E 137 ? 2.116 1.658 1.405 0.049  0.143  0.000  466 ARG EEE N   
6907  C CA  . ARG E 137 ? 2.071 1.650 1.406 0.069  0.138  0.017  466 ARG EEE CA  
6908  C C   . ARG E 137 ? 2.089 1.632 1.392 0.053  0.138  0.021  466 ARG EEE C   
6909  O O   . ARG E 137 ? 2.092 1.579 1.364 0.073  0.147  0.036  466 ARG EEE O   
6910  C CB  . ARG E 137 ? 2.102 1.673 1.453 0.113  0.146  0.037  466 ARG EEE CB  
6911  C CG  . ARG E 137 ? 2.066 1.684 1.470 0.132  0.135  0.056  466 ARG EEE CG  
6912  C CD  . ARG E 137 ? 2.081 1.702 1.508 0.174  0.144  0.081  466 ARG EEE CD  
6913  N NE  . ARG E 137 ? 2.041 1.704 1.516 0.187  0.130  0.103  466 ARG EEE NE  
6914  C CZ  . ARG E 137 ? 2.053 1.696 1.515 0.189  0.125  0.117  466 ARG EEE CZ  
6915  N NH1 . ARG E 137 ? 2.094 1.671 1.496 0.180  0.135  0.112  466 ARG EEE NH1 
6916  N NH2 . ARG E 137 ? 2.018 1.705 1.525 0.197  0.109  0.138  466 ARG EEE NH2 
6917  N N   . ASP E 138 ? 2.070 1.643 1.379 0.019  0.130  0.010  467 ASP EEE N   
6918  C CA  . ASP E 138 ? 2.105 1.648 1.381 -0.003 0.131  0.014  467 ASP EEE CA  
6919  C C   . ASP E 138 ? 2.047 1.628 1.356 0.011  0.123  0.026  467 ASP EEE C   
6920  O O   . ASP E 138 ? 1.980 1.625 1.336 0.011  0.114  0.020  467 ASP EEE O   
6921  C CB  . ASP E 138 ? 2.123 1.686 1.389 -0.047 0.130  -0.001 467 ASP EEE CB  
6922  C CG  . ASP E 138 ? 2.168 1.686 1.388 -0.072 0.135  0.005  467 ASP EEE CG  
6923  O OD1 . ASP E 138 ? 2.177 1.656 1.378 -0.054 0.137  0.020  467 ASP EEE OD1 
6924  O OD2 . ASP E 138 ? 2.180 1.708 1.388 -0.111 0.135  -0.004 467 ASP EEE OD2 
6925  N N   . ILE E 139 ? 2.061 1.597 1.342 0.022  0.125  0.044  468 ILE EEE N   
6926  C CA  . ILE E 139 ? 2.030 1.590 1.330 0.033  0.114  0.059  468 ILE EEE CA  
6927  C C   . ILE E 139 ? 2.097 1.618 1.350 0.013  0.116  0.066  468 ILE EEE C   
6928  O O   . ILE E 139 ? 2.112 1.643 1.369 0.022  0.106  0.081  468 ILE EEE O   
6929  C CB  . ILE E 139 ? 2.000 1.556 1.322 0.074  0.111  0.082  468 ILE EEE CB  
6930  C CG1 . ILE E 139 ? 2.080 1.562 1.356 0.091  0.123  0.099  468 ILE EEE CG1 
6931  C CG2 . ILE E 139 ? 1.958 1.550 1.322 0.092  0.111  0.077  468 ILE EEE CG2 
6932  C CD1 . ILE E 139 ? 2.083 1.571 1.388 0.134  0.122  0.127  468 ILE EEE CD1 
6933  N N   . SER E 140 ? 2.152 1.632 1.361 -0.016 0.127  0.057  469 SER EEE N   
6934  C CA  . SER E 140 ? 2.221 1.661 1.382 -0.040 0.131  0.066  469 SER EEE CA  
6935  C C   . SER E 140 ? 2.170 1.669 1.350 -0.060 0.126  0.060  469 SER EEE C   
6936  O O   . SER E 140 ? 2.099 1.658 1.317 -0.067 0.124  0.043  469 SER EEE O   
6937  C CB  . SER E 140 ? 2.305 1.687 1.417 -0.070 0.142  0.058  469 SER EEE CB  
6938  O OG  . SER E 140 ? 2.290 1.720 1.420 -0.105 0.143  0.040  469 SER EEE OG  
6939  N N   . THR E 141 ? 2.180 1.662 1.331 -0.065 0.124  0.074  470 THR EEE N   
6940  C CA  . THR E 141 ? 2.147 1.673 1.299 -0.084 0.123  0.070  470 THR EEE CA  
6941  C C   . THR E 141 ? 2.209 1.705 1.314 -0.120 0.136  0.073  470 THR EEE C   
6942  O O   . THR E 141 ? 2.240 1.729 1.316 -0.128 0.136  0.085  470 THR EEE O   
6943  C CB  . THR E 141 ? 2.152 1.686 1.305 -0.062 0.108  0.084  470 THR EEE CB  
6944  O OG1 . THR E 141 ? 2.275 1.751 1.380 -0.061 0.108  0.108  470 THR EEE OG1 
6945  C CG2 . THR E 141 ? 2.093 1.649 1.291 -0.028 0.094  0.088  470 THR EEE CG2 
6946  N N   . GLU E 142 ? 2.247 1.725 1.343 -0.144 0.145  0.065  471 GLU EEE N   
6947  C CA  . GLU E 142 ? 2.332 1.787 1.390 -0.187 0.157  0.068  471 GLU EEE CA  
6948  C C   . GLU E 142 ? 2.263 1.794 1.344 -0.206 0.164  0.061  471 GLU EEE C   
6949  O O   . GLU E 142 ? 2.194 1.791 1.323 -0.201 0.163  0.044  471 GLU EEE O   
6950  C CB  . GLU E 142 ? 2.390 1.816 1.438 -0.210 0.161  0.059  471 GLU EEE CB  
6951  C CG  . GLU E 142 ? 2.489 1.862 1.486 -0.254 0.169  0.068  471 GLU EEE CG  
6952  C CD  . GLU E 142 ? 2.505 1.865 1.495 -0.289 0.169  0.056  471 GLU EEE CD  
6953  O OE1 . GLU E 142 ? 2.470 1.823 1.474 -0.271 0.163  0.043  471 GLU EEE OE1 
6954  O OE2 . GLU E 142 ? 2.538 1.898 1.510 -0.336 0.175  0.061  471 GLU EEE OE2 
6955  N N   . ILE E 143 ? 2.275 1.797 1.320 -0.226 0.172  0.074  472 ILE EEE N   
6956  C CA  . ILE E 143 ? 2.284 1.875 1.343 -0.243 0.184  0.069  472 ILE EEE CA  
6957  C C   . ILE E 143 ? 2.255 1.889 1.342 -0.276 0.194  0.060  472 ILE EEE C   
6958  O O   . ILE E 143 ? 2.307 1.903 1.363 -0.312 0.200  0.071  472 ILE EEE O   
6959  C CB  . ILE E 143 ? 2.392 1.956 1.398 -0.257 0.193  0.088  472 ILE EEE CB  
6960  C CG1 . ILE E 143 ? 2.439 1.954 1.416 -0.226 0.178  0.101  472 ILE EEE CG1 
6961  C CG2 . ILE E 143 ? 2.380 2.015 1.397 -0.267 0.209  0.082  472 ILE EEE CG2 
6962  C CD1 . ILE E 143 ? 2.385 1.933 1.400 -0.188 0.162  0.089  472 ILE EEE CD1 
6963  N N   . TYR E 144 ? 2.188 1.896 1.329 -0.266 0.195  0.044  473 TYR EEE N   
6964  C CA  . TYR E 144 ? 2.170 1.929 1.350 -0.291 0.199  0.036  473 TYR EEE CA  
6965  C C   . TYR E 144 ? 2.176 1.983 1.357 -0.330 0.217  0.046  473 TYR EEE C   
6966  O O   . TYR E 144 ? 2.130 1.999 1.330 -0.319 0.232  0.045  473 TYR EEE O   
6967  C CB  . TYR E 144 ? 2.107 1.931 1.346 -0.263 0.194  0.019  473 TYR EEE CB  
6968  C CG  . TYR E 144 ? 2.111 1.998 1.393 -0.288 0.197  0.015  473 TYR EEE CG  
6969  C CD1 . TYR E 144 ? 2.151 2.006 1.422 -0.316 0.187  0.016  473 TYR EEE CD1 
6970  C CD2 . TYR E 144 ? 2.074 2.050 1.401 -0.286 0.211  0.012  473 TYR EEE CD2 
6971  C CE1 . TYR E 144 ? 2.132 2.048 1.440 -0.344 0.186  0.015  473 TYR EEE CE1 
6972  C CE2 . TYR E 144 ? 2.060 2.103 1.432 -0.309 0.212  0.013  473 TYR EEE CE2 
6973  C CZ  . TYR E 144 ? 2.086 2.101 1.449 -0.340 0.197  0.015  473 TYR EEE CZ  
6974  O OH  . TYR E 144 ? 2.064 2.147 1.470 -0.367 0.194  0.019  473 TYR EEE OH  
6975  N N   . GLN E 145 ? 2.210 1.993 1.372 -0.374 0.218  0.056  474 GLN EEE N   
6976  C CA  . GLN E 145 ? 2.228 2.062 1.398 -0.420 0.233  0.071  474 GLN EEE CA  
6977  C C   . GLN E 145 ? 2.178 2.111 1.417 -0.427 0.235  0.063  474 GLN EEE C   
6978  O O   . GLN E 145 ? 2.182 2.108 1.433 -0.448 0.219  0.059  474 GLN EEE O   
6979  C CB  . GLN E 145 ? 2.295 2.052 1.414 -0.467 0.228  0.085  474 GLN EEE CB  
6980  C CG  . GLN E 145 ? 2.318 2.126 1.447 -0.522 0.241  0.103  474 GLN EEE CG  
6981  C CD  . GLN E 145 ? 2.401 2.121 1.474 -0.571 0.233  0.116  474 GLN EEE CD  
6982  O OE1 . GLN E 145 ? 2.440 2.062 1.468 -0.563 0.218  0.109  474 GLN EEE OE1 
6983  N NE2 . GLN E 145 ? 2.442 2.195 1.514 -0.623 0.244  0.137  474 GLN EEE NE2 
6984  N N   . ALA E 146 ? 2.142 2.162 1.421 -0.410 0.253  0.063  475 ALA EEE N   
6985  C CA  . ALA E 146 ? 2.103 2.231 1.454 -0.412 0.259  0.061  475 ALA EEE CA  
6986  C C   . ALA E 146 ? 2.160 2.340 1.524 -0.468 0.270  0.083  475 ALA EEE C   
6987  O O   . ALA E 146 ? 2.185 2.380 1.570 -0.504 0.255  0.087  475 ALA EEE O   
6988  C CB  . ALA E 146 ? 2.049 2.236 1.430 -0.367 0.277  0.052  475 ALA EEE CB  
6989  N N   . GLY E 147 ? 2.185 2.389 1.534 -0.478 0.295  0.099  476 GLY EEE N   
6990  C CA  . GLY E 147 ? 2.218 2.490 1.589 -0.528 0.312  0.124  476 GLY EEE CA  
6991  C C   . GLY E 147 ? 2.297 2.492 1.617 -0.585 0.298  0.140  476 GLY EEE C   
6992  O O   . GLY E 147 ? 2.290 2.395 1.574 -0.588 0.273  0.128  476 GLY EEE O   
6993  N N   . SER E 148 ? 2.376 2.602 1.689 -0.629 0.317  0.166  477 SER EEE N   
6994  C CA  . SER E 148 ? 2.479 2.637 1.744 -0.692 0.308  0.186  477 SER EEE CA  
6995  C C   . SER E 148 ? 2.548 2.572 1.726 -0.678 0.303  0.182  477 SER EEE C   
6996  O O   . SER E 148 ? 2.586 2.511 1.723 -0.689 0.278  0.173  477 SER EEE O   
6997  C CB  . SER E 148 ? 2.527 2.765 1.812 -0.737 0.333  0.218  477 SER EEE CB  
6998  O OG  . SER E 148 ? 2.478 2.859 1.849 -0.727 0.349  0.224  477 SER EEE OG  
6999  N N   . THR E 149 ? 2.566 2.587 1.716 -0.653 0.325  0.189  478 THR EEE N   
7000  C CA  . THR E 149 ? 2.623 2.532 1.691 -0.649 0.324  0.197  478 THR EEE CA  
7001  C C   . THR E 149 ? 2.629 2.433 1.661 -0.618 0.298  0.177  478 THR EEE C   
7002  O O   . THR E 149 ? 2.556 2.380 1.618 -0.571 0.289  0.154  478 THR EEE O   
7003  C CB  . THR E 149 ? 2.602 2.538 1.651 -0.613 0.349  0.200  478 THR EEE CB  
7004  O OG1 . THR E 149 ? 2.584 2.636 1.681 -0.630 0.377  0.214  478 THR EEE OG1 
7005  C CG2 . THR E 149 ? 2.683 2.525 1.652 -0.622 0.352  0.219  478 THR EEE CG2 
7006  N N   . PRO E 150 ? 2.722 2.412 1.691 -0.642 0.285  0.186  479 PRO EEE N   
7007  C CA  . PRO E 150 ? 2.718 2.309 1.653 -0.609 0.264  0.171  479 PRO EEE CA  
7008  C C   . PRO E 150 ? 2.706 2.257 1.606 -0.560 0.267  0.172  479 PRO EEE C   
7009  O O   . PRO E 150 ? 2.734 2.263 1.593 -0.572 0.279  0.193  479 PRO EEE O   
7010  C CB  . PRO E 150 ? 2.825 2.310 1.702 -0.656 0.253  0.183  479 PRO EEE CB  
7011  C CG  . PRO E 150 ? 2.893 2.409 1.760 -0.715 0.270  0.211  479 PRO EEE CG  
7012  C CD  . PRO E 150 ? 2.830 2.477 1.755 -0.701 0.292  0.214  479 PRO EEE CD  
7013  N N   . CYS E 151 ? 2.657 2.204 1.576 -0.508 0.255  0.152  480 CYS EEE N   
7014  C CA  . CYS E 151 ? 2.656 2.180 1.552 -0.460 0.252  0.152  480 CYS EEE CA  
7015  C C   . CYS E 151 ? 2.729 2.139 1.573 -0.443 0.237  0.159  480 CYS EEE C   
7016  O O   . CYS E 151 ? 2.738 2.107 1.588 -0.437 0.225  0.148  480 CYS EEE O   
7017  C CB  . CYS E 151 ? 2.550 2.141 1.499 -0.415 0.248  0.129  480 CYS EEE CB  
7018  S SG  . CYS E 151 ? 2.513 2.224 1.503 -0.423 0.273  0.126  480 CYS EEE SG  
7019  N N   . ASN E 152 ? 2.790 2.155 1.585 -0.433 0.240  0.179  481 ASN EEE N   
7020  C CA  . ASN E 152 ? 2.868 2.127 1.611 -0.413 0.228  0.194  481 ASN EEE CA  
7021  C C   . ASN E 152 ? 2.792 2.065 1.547 -0.358 0.216  0.190  481 ASN EEE C   
7022  O O   . ASN E 152 ? 2.859 2.092 1.573 -0.343 0.212  0.210  481 ASN EEE O   
7023  C CB  . ASN E 152 ? 3.013 2.211 1.692 -0.446 0.238  0.224  481 ASN EEE CB  
7024  C CG  . ASN E 152 ? 3.060 2.331 1.739 -0.470 0.256  0.234  481 ASN EEE CG  
7025  O OD1 . ASN E 152 ? 3.028 2.393 1.758 -0.476 0.266  0.217  481 ASN EEE OD1 
7026  N ND2 . ASN E 152 ? 3.151 2.379 1.774 -0.482 0.263  0.261  481 ASN EEE ND2 
7027  N N   . GLY E 153 ? 2.663 1.995 1.476 -0.332 0.209  0.165  482 GLY EEE N   
7028  C CA  . GLY E 153 ? 2.602 1.962 1.436 -0.286 0.195  0.159  482 GLY EEE CA  
7029  C C   . GLY E 153 ? 2.587 2.006 1.417 -0.286 0.202  0.158  482 GLY EEE C   
7030  O O   . GLY E 153 ? 2.581 2.014 1.416 -0.253 0.188  0.156  482 GLY EEE O   
7031  N N   . VAL E 154 ? 2.591 2.042 1.410 -0.321 0.222  0.162  483 VAL EEE N   
7032  C CA  . VAL E 154 ? 2.563 2.071 1.372 -0.322 0.235  0.160  483 VAL EEE CA  
7033  C C   . VAL E 154 ? 2.472 2.065 1.341 -0.315 0.243  0.134  483 VAL EEE C   
7034  O O   . VAL E 154 ? 2.483 2.104 1.391 -0.336 0.250  0.127  483 VAL EEE O   
7035  C CB  . VAL E 154 ? 2.640 2.140 1.406 -0.363 0.257  0.182  483 VAL EEE CB  
7036  C CG1 . VAL E 154 ? 2.659 2.218 1.411 -0.362 0.276  0.180  483 VAL EEE CG1 
7037  C CG2 . VAL E 154 ? 2.725 2.133 1.430 -0.370 0.248  0.211  483 VAL EEE CG2 
7038  N N   . GLU E 155 ? 2.405 2.034 1.281 -0.286 0.241  0.119  484 GLU EEE N   
7039  C CA  . GLU E 155 ? 2.338 2.041 1.268 -0.272 0.249  0.094  484 GLU EEE CA  
7040  C C   . GLU E 155 ? 2.362 2.123 1.284 -0.288 0.280  0.095  484 GLU EEE C   
7041  O O   . GLU E 155 ? 2.433 2.171 1.301 -0.306 0.292  0.114  484 GLU EEE O   
7042  C CB  . GLU E 155 ? 2.302 2.003 1.239 -0.233 0.229  0.078  484 GLU EEE CB  
7043  C CG  . GLU E 155 ? 2.257 1.939 1.235 -0.215 0.206  0.071  484 GLU EEE CG  
7044  C CD  . GLU E 155 ? 2.223 1.915 1.219 -0.181 0.187  0.056  484 GLU EEE CD  
7045  O OE1 . GLU E 155 ? 2.196 1.936 1.215 -0.171 0.196  0.036  484 GLU EEE OE1 
7046  O OE2 . GLU E 155 ? 2.228 1.879 1.215 -0.165 0.163  0.065  484 GLU EEE OE2 
7047  N N   . GLY E 156 ? 2.331 2.164 1.304 -0.279 0.295  0.077  485 GLY EEE N   
7048  C CA  . GLY E 156 ? 2.361 2.257 1.331 -0.280 0.327  0.074  485 GLY EEE CA  
7049  C C   . GLY E 156 ? 2.323 2.302 1.362 -0.291 0.346  0.071  485 GLY EEE C   
7050  O O   . GLY E 156 ? 2.264 2.268 1.358 -0.274 0.334  0.054  485 GLY EEE O   
7051  N N   . PHE E 157 ? 2.357 2.383 1.395 -0.319 0.376  0.088  486 PHE EEE N   
7052  C CA  . PHE E 157 ? 2.342 2.462 1.446 -0.333 0.398  0.092  486 PHE EEE CA  
7053  C C   . PHE E 157 ? 2.292 2.411 1.443 -0.359 0.376  0.095  486 PHE EEE C   
7054  O O   . PHE E 157 ? 2.339 2.414 1.464 -0.398 0.368  0.114  486 PHE EEE O   
7055  C CB  . PHE E 157 ? 2.443 2.607 1.529 -0.362 0.433  0.117  486 PHE EEE CB  
7056  C CG  . PHE E 157 ? 2.468 2.744 1.624 -0.371 0.461  0.125  486 PHE EEE CG  
7057  C CD1 . PHE E 157 ? 2.474 2.792 1.683 -0.414 0.455  0.142  486 PHE EEE CD1 
7058  C CD2 . PHE E 157 ? 2.496 2.837 1.663 -0.336 0.494  0.117  486 PHE EEE CD2 
7059  C CE1 . PHE E 157 ? 2.466 2.897 1.745 -0.423 0.479  0.154  486 PHE EEE CE1 
7060  C CE2 . PHE E 157 ? 2.491 2.942 1.728 -0.340 0.522  0.128  486 PHE EEE CE2 
7061  C CZ  . PHE E 157 ? 2.469 2.971 1.766 -0.384 0.513  0.148  486 PHE EEE CZ  
7062  N N   . ASN E 158 ? 2.220 2.380 1.431 -0.338 0.365  0.078  487 ASN EEE N   
7063  C CA  . ASN E 158 ? 2.174 2.337 1.429 -0.360 0.343  0.078  487 ASN EEE CA  
7064  C C   . ASN E 158 ? 2.167 2.226 1.380 -0.360 0.313  0.074  487 ASN EEE C   
7065  O O   . ASN E 158 ? 2.148 2.184 1.370 -0.388 0.297  0.079  487 ASN EEE O   
7066  C CB  . ASN E 158 ? 2.213 2.423 1.492 -0.413 0.353  0.102  487 ASN EEE CB  
7067  C CG  . ASN E 158 ? 2.236 2.553 1.554 -0.416 0.388  0.114  487 ASN EEE CG  
7068  O OD1 . ASN E 158 ? 2.232 2.591 1.567 -0.372 0.405  0.101  487 ASN EEE OD1 
7069  N ND2 . ASN E 158 ? 2.275 2.635 1.608 -0.466 0.399  0.140  487 ASN EEE ND2 
7070  N N   . CYS E 159 ? 2.182 2.181 1.350 -0.329 0.305  0.066  488 CYS EEE N   
7071  C CA  . CYS E 159 ? 2.194 2.104 1.330 -0.318 0.277  0.063  488 CYS EEE CA  
7072  C C   . CYS E 159 ? 2.167 2.060 1.298 -0.272 0.265  0.047  488 CYS EEE C   
7073  O O   . CYS E 159 ? 2.174 2.064 1.270 -0.258 0.274  0.047  488 CYS EEE O   
7074  C CB  . CYS E 159 ? 2.267 2.103 1.340 -0.343 0.275  0.084  488 CYS EEE CB  
7075  S SG  . CYS E 159 ? 2.300 2.092 1.374 -0.385 0.264  0.094  488 CYS EEE SG  
7076  N N   . TYR E 160 ? 2.137 2.016 1.298 -0.251 0.244  0.035  489 TYR EEE N   
7077  C CA  . TYR E 160 ? 2.102 1.981 1.278 -0.210 0.230  0.018  489 TYR EEE CA  
7078  C C   . TYR E 160 ? 2.069 1.886 1.239 -0.198 0.205  0.021  489 TYR EEE C   
7079  O O   . TYR E 160 ? 2.075 1.866 1.247 -0.215 0.200  0.027  489 TYR EEE O   
7080  C CB  . TYR E 160 ? 2.070 2.018 1.307 -0.196 0.236  0.002  489 TYR EEE CB  
7081  C CG  . TYR E 160 ? 2.112 2.131 1.370 -0.212 0.264  0.005  489 TYR EEE CG  
7082  C CD1 . TYR E 160 ? 2.178 2.216 1.408 -0.205 0.286  0.005  489 TYR EEE CD1 
7083  C CD2 . TYR E 160 ? 2.105 2.174 1.408 -0.236 0.269  0.011  489 TYR EEE CD2 
7084  C CE1 . TYR E 160 ? 2.206 2.315 1.458 -0.217 0.315  0.011  489 TYR EEE CE1 
7085  C CE2 . TYR E 160 ? 2.124 2.269 1.454 -0.252 0.294  0.019  489 TYR EEE CE2 
7086  C CZ  . TYR E 160 ? 2.177 2.345 1.484 -0.241 0.319  0.020  489 TYR EEE CZ  
7087  O OH  . TYR E 160 ? 2.214 2.463 1.551 -0.253 0.348  0.030  489 TYR EEE OH  
7088  N N   . PHE E 161 ? 2.048 1.842 1.206 -0.169 0.190  0.017  490 PHE EEE N   
7089  C CA  . PHE E 161 ? 2.014 1.769 1.182 -0.147 0.166  0.019  490 PHE EEE CA  
7090  C C   . PHE E 161 ? 1.944 1.738 1.171 -0.133 0.161  0.004  490 PHE EEE C   
7091  O O   . PHE E 161 ? 1.904 1.745 1.158 -0.122 0.167  -0.011 490 PHE EEE O   
7092  C CB  . PHE E 161 ? 2.030 1.765 1.173 -0.126 0.150  0.022  490 PHE EEE CB  
7093  C CG  . PHE E 161 ? 2.009 1.709 1.161 -0.105 0.126  0.031  490 PHE EEE CG  
7094  C CD1 . PHE E 161 ? 2.053 1.702 1.177 -0.107 0.121  0.053  490 PHE EEE CD1 
7095  C CD2 . PHE E 161 ? 1.961 1.682 1.151 -0.082 0.110  0.022  490 PHE EEE CD2 
7096  C CE1 . PHE E 161 ? 2.052 1.676 1.188 -0.084 0.101  0.065  490 PHE EEE CE1 
7097  C CE2 . PHE E 161 ? 1.951 1.649 1.155 -0.063 0.090  0.035  490 PHE EEE CE2 
7098  C CZ  . PHE E 161 ? 1.993 1.647 1.172 -0.062 0.086  0.057  490 PHE EEE CZ  
7099  N N   . PRO E 162 ? 1.933 1.704 1.176 -0.131 0.152  0.007  491 PRO EEE N   
7100  C CA  . PRO E 162 ? 1.877 1.687 1.170 -0.126 0.152  -0.006 491 PRO EEE CA  
7101  C C   . PRO E 162 ? 1.828 1.658 1.158 -0.094 0.138  -0.015 491 PRO EEE C   
7102  O O   . PRO E 162 ? 1.796 1.664 1.168 -0.089 0.139  -0.025 491 PRO EEE O   
7103  C CB  . PRO E 162 ? 1.899 1.664 1.179 -0.137 0.148  0.002  491 PRO EEE CB  
7104  C CG  . PRO E 162 ? 1.944 1.645 1.183 -0.127 0.141  0.017  491 PRO EEE CG  
7105  C CD  . PRO E 162 ? 1.975 1.680 1.186 -0.132 0.145  0.023  491 PRO EEE CD  
7106  N N   . LEU E 163 ? 1.840 1.646 1.157 -0.075 0.125  -0.010 492 LEU EEE N   
7107  C CA  . LEU E 163 ? 1.818 1.637 1.169 -0.049 0.109  -0.015 492 LEU EEE CA  
7108  C C   . LEU E 163 ? 1.812 1.650 1.156 -0.043 0.109  -0.027 492 LEU EEE C   
7109  O O   . LEU E 163 ? 1.859 1.692 1.164 -0.056 0.119  -0.027 492 LEU EEE O   
7110  C CB  . LEU E 163 ? 1.861 1.641 1.203 -0.035 0.091  0.002  492 LEU EEE CB  
7111  C CG  . LEU E 163 ? 1.910 1.660 1.252 -0.032 0.093  0.014  492 LEU EEE CG  
7112  C CD1 . LEU E 163 ? 1.913 1.646 1.269 -0.008 0.076  0.030  492 LEU EEE CD1 
7113  C CD2 . LEU E 163 ? 1.900 1.674 1.273 -0.035 0.101  0.002  492 LEU EEE CD2 
7114  N N   . GLN E 164 ? 1.780 1.636 1.157 -0.025 0.098  -0.036 493 GLN EEE N   
7115  C CA  . GLN E 164 ? 1.804 1.665 1.170 -0.016 0.094  -0.050 493 GLN EEE CA  
7116  C C   . GLN E 164 ? 1.783 1.637 1.176 0.001  0.070  -0.048 493 GLN EEE C   
7117  O O   . GLN E 164 ? 1.761 1.619 1.189 0.007  0.062  -0.038 493 GLN EEE O   
7118  C CB  . GLN E 164 ? 1.792 1.693 1.175 -0.014 0.117  -0.066 493 GLN EEE CB  
7119  C CG  . GLN E 164 ? 1.820 1.716 1.167 -0.008 0.125  -0.081 493 GLN EEE CG  
7120  C CD  . GLN E 164 ? 1.811 1.752 1.171 -0.007 0.155  -0.090 493 GLN EEE CD  
7121  O OE1 . GLN E 164 ? 1.838 1.782 1.161 -0.014 0.175  -0.092 493 GLN EEE OE1 
7122  N NE2 . GLN E 164 ? 1.771 1.751 1.185 0.003  0.159  -0.093 493 GLN EEE NE2 
7123  N N   . SER E 165 ? 1.801 1.641 1.173 0.006  0.060  -0.058 494 SER EEE N   
7124  C CA  . SER E 165 ? 1.786 1.617 1.181 0.016  0.035  -0.058 494 SER EEE CA  
7125  C C   . SER E 165 ? 1.752 1.603 1.178 0.029  0.043  -0.075 494 SER EEE C   
7126  O O   . SER E 165 ? 1.723 1.596 1.148 0.032  0.068  -0.088 494 SER EEE O   
7127  C CB  . SER E 165 ? 1.839 1.637 1.188 0.009  0.014  -0.057 494 SER EEE CB  
7128  O OG  . SER E 165 ? 1.836 1.621 1.176 0.002  -0.003 -0.033 494 SER EEE OG  
7129  N N   . TYR E 166 ? 1.739 1.584 1.193 0.037  0.023  -0.073 495 TYR EEE N   
7130  C CA  . TYR E 166 ? 1.744 1.603 1.231 0.051  0.028  -0.086 495 TYR EEE CA  
7131  C C   . TYR E 166 ? 1.805 1.628 1.257 0.054  0.019  -0.103 495 TYR EEE C   
7132  O O   . TYR E 166 ? 1.827 1.654 1.279 0.069  0.037  -0.121 495 TYR EEE O   
7133  C CB  . TYR E 166 ? 1.712 1.585 1.253 0.057  0.013  -0.070 495 TYR EEE CB  
7134  C CG  . TYR E 166 ? 1.666 1.577 1.245 0.063  0.030  -0.065 495 TYR EEE CG  
7135  C CD1 . TYR E 166 ? 1.659 1.596 1.250 0.071  0.050  -0.079 495 TYR EEE CD1 
7136  C CD2 . TYR E 166 ? 1.666 1.585 1.267 0.062  0.025  -0.047 495 TYR EEE CD2 
7137  C CE1 . TYR E 166 ? 1.647 1.619 1.270 0.072  0.062  -0.074 495 TYR EEE CE1 
7138  C CE2 . TYR E 166 ? 1.651 1.597 1.277 0.065  0.039  -0.045 495 TYR EEE CE2 
7139  C CZ  . TYR E 166 ? 1.661 1.634 1.298 0.068  0.055  -0.058 495 TYR EEE CZ  
7140  O OH  . TYR E 166 ? 1.709 1.709 1.367 0.066  0.065  -0.055 495 TYR EEE OH  
7141  N N   . GLY E 167 ? 1.837 1.625 1.258 0.042  -0.007 -0.098 496 GLY EEE N   
7142  C CA  . GLY E 167 ? 1.913 1.654 1.287 0.040  -0.020 -0.115 496 GLY EEE CA  
7143  C C   . GLY E 167 ? 1.888 1.620 1.294 0.051  -0.027 -0.122 496 GLY EEE C   
7144  O O   . GLY E 167 ? 1.914 1.632 1.305 0.067  -0.008 -0.144 496 GLY EEE O   
7145  N N   . PHE E 168 ? 1.854 1.596 1.306 0.045  -0.051 -0.102 497 PHE EEE N   
7146  C CA  . PHE E 168 ? 1.870 1.601 1.354 0.052  -0.063 -0.103 497 PHE EEE CA  
7147  C C   . PHE E 168 ? 1.956 1.626 1.390 0.036  -0.091 -0.113 497 PHE EEE C   
7148  O O   . PHE E 168 ? 1.962 1.623 1.384 0.014  -0.120 -0.098 497 PHE EEE O   
7149  C CB  . PHE E 168 ? 1.815 1.585 1.366 0.050  -0.076 -0.074 497 PHE EEE CB  
7150  C CG  . PHE E 168 ? 1.747 1.567 1.337 0.063  -0.051 -0.066 497 PHE EEE CG  
7151  C CD1 . PHE E 168 ? 1.734 1.573 1.345 0.081  -0.028 -0.078 497 PHE EEE CD1 
7152  C CD2 . PHE E 168 ? 1.716 1.561 1.320 0.058  -0.052 -0.046 497 PHE EEE CD2 
7153  C CE1 . PHE E 168 ? 1.687 1.570 1.329 0.088  -0.009 -0.070 497 PHE EEE CE1 
7154  C CE2 . PHE E 168 ? 1.680 1.559 1.310 0.067  -0.031 -0.041 497 PHE EEE CE2 
7155  C CZ  . PHE E 168 ? 1.657 1.555 1.305 0.080  -0.011 -0.053 497 PHE EEE CZ  
7156  N N   . GLN E 169 ? 2.027 1.654 1.432 0.048  -0.081 -0.138 498 GLN EEE N   
7157  C CA  . GLN E 169 ? 2.122 1.676 1.473 0.034  -0.107 -0.152 498 GLN EEE CA  
7158  C C   . GLN E 169 ? 2.130 1.671 1.523 0.039  -0.117 -0.148 498 GLN EEE C   
7159  O O   . GLN E 169 ? 2.091 1.664 1.530 0.064  -0.093 -0.147 498 GLN EEE O   
7160  C CB  . GLN E 169 ? 2.199 1.703 1.469 0.045  -0.085 -0.185 498 GLN EEE CB  
7161  C CG  . GLN E 169 ? 2.203 1.735 1.444 0.045  -0.065 -0.187 498 GLN EEE CG  
7162  C CD  . GLN E 169 ? 2.328 1.798 1.471 0.034  -0.069 -0.208 498 GLN EEE CD  
7163  O OE1 . GLN E 169 ? 2.427 1.836 1.513 0.045  -0.061 -0.234 498 GLN EEE OE1 
7164  N NE2 . GLN E 169 ? 2.343 1.827 1.463 0.014  -0.082 -0.195 498 GLN EEE NE2 
7165  N N   . PRO E 170 ? 2.175 1.673 1.557 0.014  -0.155 -0.140 499 PRO EEE N   
7166  C CA  . PRO E 170 ? 2.181 1.656 1.595 0.015  -0.166 -0.136 499 PRO EEE CA  
7167  C C   . PRO E 170 ? 2.242 1.666 1.623 0.045  -0.138 -0.165 499 PRO EEE C   
7168  O O   . PRO E 170 ? 2.219 1.644 1.642 0.057  -0.135 -0.158 499 PRO EEE O   
7169  C CB  . PRO E 170 ? 2.263 1.684 1.644 -0.024 -0.212 -0.130 499 PRO EEE CB  
7170  C CG  . PRO E 170 ? 2.257 1.711 1.626 -0.045 -0.230 -0.115 499 PRO EEE CG  
7171  C CD  . PRO E 170 ? 2.232 1.707 1.575 -0.021 -0.192 -0.133 499 PRO EEE CD  
7172  N N   . THR E 171 ? 2.331 1.714 1.640 0.057  -0.119 -0.194 500 THR EEE N   
7173  C CA  . THR E 171 ? 2.409 1.739 1.676 0.090  -0.088 -0.224 500 THR EEE CA  
7174  C C   . THR E 171 ? 2.330 1.732 1.643 0.127  -0.044 -0.223 500 THR EEE C   
7175  O O   . THR E 171 ? 2.339 1.716 1.640 0.160  -0.016 -0.240 500 THR EEE O   
7176  C CB  . THR E 171 ? 2.553 1.802 1.712 0.084  -0.087 -0.255 500 THR EEE CB  
7177  O OG1 . THR E 171 ? 2.562 1.855 1.706 0.074  -0.082 -0.252 500 THR EEE OG1 
7178  C CG2 . THR E 171 ? 2.653 1.814 1.755 0.049  -0.132 -0.262 500 THR EEE CG2 
7179  N N   . ASN E 172 ? 2.270 1.754 1.632 0.121  -0.037 -0.204 501 ASN EEE N   
7180  C CA  . ASN E 172 ? 2.236 1.796 1.649 0.148  -0.001 -0.198 501 ASN EEE CA  
7181  C C   . ASN E 172 ? 2.221 1.796 1.690 0.172  0.006  -0.190 501 ASN EEE C   
7182  O O   . ASN E 172 ? 2.234 1.788 1.727 0.159  -0.021 -0.177 501 ASN EEE O   
7183  C CB  . ASN E 172 ? 2.169 1.803 1.628 0.132  -0.005 -0.175 501 ASN EEE CB  
7184  C CG  . ASN E 172 ? 2.217 1.872 1.641 0.130  0.016  -0.183 501 ASN EEE CG  
7185  O OD1 . ASN E 172 ? 2.287 1.946 1.695 0.106  -0.001 -0.174 501 ASN EEE OD1 
7186  N ND2 . ASN E 172 ? 2.220 1.892 1.635 0.155  0.051  -0.197 501 ASN EEE ND2 
7187  N N   . GLY E 173 ? 2.213 1.829 1.705 0.204  0.041  -0.195 502 GLY EEE N   
7188  C CA  . GLY E 173 ? 2.168 1.816 1.720 0.229  0.051  -0.183 502 GLY EEE CA  
7189  C C   . GLY E 173 ? 2.054 1.764 1.674 0.213  0.035  -0.154 502 GLY EEE C   
7190  O O   . GLY E 173 ? 2.004 1.753 1.630 0.192  0.030  -0.146 502 GLY EEE O   
7191  N N   . VAL E 174 ? 2.009 1.726 1.673 0.225  0.029  -0.140 503 VAL EEE N   
7192  C CA  . VAL E 174 ? 1.901 1.661 1.621 0.209  0.010  -0.112 503 VAL EEE CA  
7193  C C   . VAL E 174 ? 1.775 1.613 1.524 0.205  0.023  -0.103 503 VAL EEE C   
7194  O O   . VAL E 174 ? 1.694 1.555 1.464 0.185  0.009  -0.086 503 VAL EEE O   
7195  C CB  . VAL E 174 ? 1.908 1.671 1.670 0.228  0.009  -0.098 503 VAL EEE CB  
7196  C CG1 . VAL E 174 ? 1.837 1.636 1.646 0.211  -0.009 -0.070 503 VAL EEE CG1 
7197  C CG2 . VAL E 174 ? 2.014 1.692 1.743 0.236  0.000  -0.108 503 VAL EEE CG2 
7198  N N   . GLY E 175 ? 1.752 1.625 1.500 0.222  0.050  -0.113 504 GLY EEE N   
7199  C CA  . GLY E 175 ? 1.709 1.650 1.478 0.214  0.063  -0.106 504 GLY EEE CA  
7200  C C   . GLY E 175 ? 1.711 1.643 1.446 0.188  0.057  -0.110 504 GLY EEE C   
7201  O O   . GLY E 175 ? 1.637 1.606 1.391 0.173  0.054  -0.097 504 GLY EEE O   
7202  N N   . TYR E 176 ? 1.800 1.682 1.482 0.184  0.057  -0.127 505 TYR EEE N   
7203  C CA  . TYR E 176 ? 1.839 1.709 1.482 0.161  0.051  -0.130 505 TYR EEE CA  
7204  C C   . TYR E 176 ? 1.828 1.656 1.459 0.141  0.018  -0.121 505 TYR EEE C   
7205  O O   . TYR E 176 ? 1.834 1.637 1.425 0.123  0.008  -0.124 505 TYR EEE O   
7206  C CB  . TYR E 176 ? 1.965 1.810 1.553 0.168  0.071  -0.151 505 TYR EEE CB  
7207  C CG  . TYR E 176 ? 2.001 1.899 1.607 0.187  0.104  -0.155 505 TYR EEE CG  
7208  C CD1 . TYR E 176 ? 2.043 1.948 1.668 0.217  0.121  -0.161 505 TYR EEE CD1 
7209  C CD2 . TYR E 176 ? 1.978 1.921 1.584 0.173  0.118  -0.151 505 TYR EEE CD2 
7210  C CE1 . TYR E 176 ? 2.039 2.002 1.687 0.235  0.151  -0.161 505 TYR EEE CE1 
7211  C CE2 . TYR E 176 ? 1.968 1.966 1.595 0.186  0.148  -0.151 505 TYR EEE CE2 
7212  C CZ  . TYR E 176 ? 2.011 2.025 1.663 0.218  0.164  -0.155 505 TYR EEE CZ  
7213  O OH  . TYR E 176 ? 2.042 2.122 1.722 0.231  0.192  -0.151 505 TYR EEE OH  
7214  N N   . GLN E 177 ? 1.791 1.615 1.459 0.143  0.002  -0.108 506 GLN EEE N   
7215  C CA  . GLN E 177 ? 1.756 1.566 1.437 0.122  -0.028 -0.089 506 GLN EEE CA  
7216  C C   . GLN E 177 ? 1.679 1.542 1.398 0.117  -0.026 -0.067 506 GLN EEE C   
7217  O O   . GLN E 177 ? 1.667 1.571 1.412 0.129  -0.008 -0.065 506 GLN EEE O   
7218  C CB  . GLN E 177 ? 1.755 1.539 1.459 0.126  -0.043 -0.082 506 GLN EEE CB  
7219  C CG  . GLN E 177 ? 1.839 1.551 1.493 0.127  -0.051 -0.103 506 GLN EEE CG  
7220  C CD  . GLN E 177 ? 1.856 1.532 1.528 0.125  -0.070 -0.093 506 GLN EEE CD  
7221  O OE1 . GLN E 177 ? 1.811 1.515 1.531 0.117  -0.083 -0.068 506 GLN EEE OE1 
7222  N NE2 . GLN E 177 ? 1.924 1.532 1.553 0.134  -0.069 -0.114 506 GLN EEE NE2 
7223  N N   . PRO E 178 ? 1.653 1.516 1.375 0.099  -0.046 -0.050 507 PRO EEE N   
7224  C CA  . PRO E 178 ? 1.607 1.511 1.358 0.098  -0.041 -0.030 507 PRO EEE CA  
7225  C C   . PRO E 178 ? 1.594 1.523 1.396 0.105  -0.045 -0.009 507 PRO EEE C   
7226  O O   . PRO E 178 ? 1.608 1.524 1.427 0.099  -0.065 0.004  507 PRO EEE O   
7227  C CB  . PRO E 178 ? 1.623 1.514 1.356 0.081  -0.060 -0.018 507 PRO EEE CB  
7228  C CG  . PRO E 178 ? 1.679 1.530 1.397 0.069  -0.086 -0.021 507 PRO EEE CG  
7229  C CD  . PRO E 178 ? 1.712 1.535 1.409 0.081  -0.073 -0.047 507 PRO EEE CD  
7230  N N   . TYR E 179 ? 1.574 1.539 1.398 0.116  -0.028 -0.005 508 TYR EEE N   
7231  C CA  . TYR E 179 ? 1.554 1.545 1.418 0.124  -0.028 0.017  508 TYR EEE CA  
7232  C C   . TYR E 179 ? 1.521 1.530 1.389 0.122  -0.024 0.034  508 TYR EEE C   
7233  O O   . TYR E 179 ? 1.486 1.494 1.327 0.119  -0.012 0.025  508 TYR EEE O   
7234  C CB  . TYR E 179 ? 1.551 1.565 1.430 0.138  -0.013 0.011  508 TYR EEE CB  
7235  C CG  . TYR E 179 ? 1.589 1.589 1.478 0.147  -0.017 0.004  508 TYR EEE CG  
7236  C CD1 . TYR E 179 ? 1.644 1.612 1.504 0.147  -0.017 -0.017 508 TYR EEE CD1 
7237  C CD2 . TYR E 179 ? 1.600 1.614 1.522 0.157  -0.018 0.018  508 TYR EEE CD2 
7238  C CE1 . TYR E 179 ? 1.693 1.639 1.557 0.160  -0.017 -0.024 508 TYR EEE CE1 
7239  C CE2 . TYR E 179 ? 1.647 1.642 1.576 0.168  -0.021 0.013  508 TYR EEE CE2 
7240  C CZ  . TYR E 179 ? 1.681 1.639 1.581 0.170  -0.020 -0.009 508 TYR EEE CZ  
7241  O OH  . TYR E 179 ? 1.692 1.623 1.594 0.185  -0.020 -0.014 508 TYR EEE OH  
7242  N N   . ARG E 180 ? 1.530 1.550 1.428 0.123  -0.033 0.059  509 ARG EEE N   
7243  C CA  . ARG E 180 ? 1.542 1.580 1.449 0.129  -0.026 0.080  509 ARG EEE CA  
7244  C C   . ARG E 180 ? 1.530 1.589 1.447 0.143  -0.008 0.083  509 ARG EEE C   
7245  O O   . ARG E 180 ? 1.572 1.642 1.515 0.148  -0.011 0.091  509 ARG EEE O   
7246  C CB  . ARG E 180 ? 1.561 1.609 1.499 0.125  -0.043 0.109  509 ARG EEE CB  
7247  C CG  . ARG E 180 ? 1.585 1.615 1.507 0.109  -0.063 0.108  509 ARG EEE CG  
7248  C CD  . ARG E 180 ? 1.583 1.631 1.542 0.102  -0.083 0.141  509 ARG EEE CD  
7249  N NE  . ARG E 180 ? 1.609 1.644 1.547 0.088  -0.102 0.143  509 ARG EEE NE  
7250  C CZ  . ARG E 180 ? 1.639 1.698 1.604 0.082  -0.119 0.174  509 ARG EEE CZ  
7251  N NH1 . ARG E 180 ? 1.617 1.715 1.633 0.090  -0.118 0.207  509 ARG EEE NH1 
7252  N NH2 . ARG E 180 ? 1.698 1.744 1.638 0.068  -0.137 0.175  509 ARG EEE NH2 
7253  N N   . VAL E 181 ? 1.496 1.552 1.387 0.147  0.008  0.079  510 VAL EEE N   
7254  C CA  . VAL E 181 ? 1.449 1.517 1.334 0.156  0.025  0.076  510 VAL EEE CA  
7255  C C   . VAL E 181 ? 1.489 1.554 1.367 0.168  0.037  0.095  510 VAL EEE C   
7256  O O   . VAL E 181 ? 1.551 1.597 1.405 0.167  0.041  0.094  510 VAL EEE O   
7257  C CB  . VAL E 181 ? 1.428 1.488 1.279 0.146  0.033  0.051  510 VAL EEE CB  
7258  C CG1 . VAL E 181 ? 1.417 1.487 1.255 0.149  0.045  0.048  510 VAL EEE CG1 
7259  C CG2 . VAL E 181 ? 1.431 1.496 1.289 0.140  0.025  0.035  510 VAL EEE CG2 
7260  N N   . VAL E 182 ? 1.476 1.559 1.373 0.181  0.044  0.112  511 VAL EEE N   
7261  C CA  . VAL E 182 ? 1.458 1.536 1.339 0.198  0.063  0.126  511 VAL EEE CA  
7262  C C   . VAL E 182 ? 1.455 1.525 1.302 0.198  0.075  0.110  511 VAL EEE C   
7263  O O   . VAL E 182 ? 1.447 1.536 1.308 0.193  0.068  0.105  511 VAL EEE O   
7264  C CB  . VAL E 182 ? 1.445 1.549 1.367 0.213  0.065  0.158  511 VAL EEE CB  
7265  C CG1 . VAL E 182 ? 1.484 1.582 1.386 0.235  0.089  0.172  511 VAL EEE CG1 
7266  C CG2 . VAL E 182 ? 1.438 1.556 1.398 0.207  0.048  0.176  511 VAL EEE CG2 
7267  N N   . VAL E 183 ? 1.468 1.508 1.268 0.203  0.091  0.104  512 VAL EEE N   
7268  C CA  . VAL E 183 ? 1.509 1.536 1.267 0.198  0.100  0.089  512 VAL EEE CA  
7269  C C   . VAL E 183 ? 1.548 1.553 1.276 0.220  0.121  0.102  512 VAL EEE C   
7270  O O   . VAL E 183 ? 1.586 1.552 1.278 0.228  0.134  0.101  512 VAL EEE O   
7271  C CB  . VAL E 183 ? 1.560 1.560 1.276 0.176  0.098  0.063  512 VAL EEE CB  
7272  C CG1 . VAL E 183 ? 1.617 1.597 1.282 0.168  0.105  0.050  512 VAL EEE CG1 
7273  C CG2 . VAL E 183 ? 1.546 1.573 1.290 0.159  0.082  0.051  512 VAL EEE CG2 
7274  N N   . LEU E 184 ? 1.540 1.567 1.280 0.231  0.125  0.114  513 LEU EEE N   
7275  C CA  . LEU E 184 ? 1.581 1.592 1.290 0.255  0.149  0.128  513 LEU EEE CA  
7276  C C   . LEU E 184 ? 1.632 1.605 1.270 0.244  0.155  0.105  513 LEU EEE C   
7277  O O   . LEU E 184 ? 1.622 1.616 1.259 0.235  0.146  0.101  513 LEU EEE O   
7278  C CB  . LEU E 184 ? 1.553 1.608 1.310 0.268  0.149  0.154  513 LEU EEE CB  
7279  C CG  . LEU E 184 ? 1.509 1.602 1.337 0.272  0.140  0.179  513 LEU EEE CG  
7280  C CD1 . LEU E 184 ? 1.501 1.634 1.371 0.283  0.142  0.208  513 LEU EEE CD1 
7281  C CD2 . LEU E 184 ? 1.524 1.605 1.354 0.289  0.152  0.193  513 LEU EEE CD2 
7282  N N   . SER E 185 ? 1.700 1.617 1.279 0.243  0.166  0.090  514 SER EEE N   
7283  C CA  . SER E 185 ? 1.764 1.628 1.260 0.234  0.174  0.070  514 SER EEE CA  
7284  C C   . SER E 185 ? 1.800 1.637 1.258 0.267  0.202  0.083  514 SER EEE C   
7285  O O   . SER E 185 ? 1.786 1.623 1.266 0.297  0.220  0.104  514 SER EEE O   
7286  C CB  . SER E 185 ? 1.819 1.627 1.266 0.217  0.174  0.049  514 SER EEE CB  
7287  O OG  . SER E 185 ? 1.808 1.620 1.291 0.224  0.174  0.058  514 SER EEE OG  
7288  N N   . PHE E 186 ? 1.836 1.654 1.239 0.262  0.205  0.074  515 PHE EEE N   
7289  C CA  . PHE E 186 ? 1.893 1.675 1.240 0.292  0.234  0.082  515 PHE EEE CA  
7290  C C   . PHE E 186 ? 1.969 1.665 1.208 0.279  0.241  0.053  515 PHE EEE C   
7291  O O   . PHE E 186 ? 2.006 1.698 1.217 0.242  0.218  0.033  515 PHE EEE O   
7292  C CB  . PHE E 186 ? 1.890 1.718 1.253 0.294  0.230  0.094  515 PHE EEE CB  
7293  C CG  . PHE E 186 ? 1.834 1.741 1.297 0.304  0.222  0.123  515 PHE EEE CG  
7294  C CD1 . PHE E 186 ? 1.856 1.783 1.356 0.338  0.245  0.153  515 PHE EEE CD1 
7295  C CD2 . PHE E 186 ? 1.774 1.731 1.293 0.279  0.193  0.121  515 PHE EEE CD2 
7296  C CE1 . PHE E 186 ? 1.790 1.784 1.379 0.341  0.235  0.181  515 PHE EEE CE1 
7297  C CE2 . PHE E 186 ? 1.721 1.736 1.323 0.286  0.185  0.146  515 PHE EEE CE2 
7298  C CZ  . PHE E 186 ? 1.718 1.750 1.354 0.314  0.205  0.176  515 PHE EEE CZ  
7299  N N   . GLU E 187 ? 2.128 1.979 1.968 0.205  0.174  0.059  516 GLU EEE N   
7300  C CA  . GLU E 187 ? 2.078 1.979 2.009 0.175  0.140  0.072  516 GLU EEE CA  
7301  C C   . GLU E 187 ? 2.083 1.946 2.008 0.151  0.130  0.013  516 GLU EEE C   
7302  O O   . GLU E 187 ? 2.099 1.929 1.992 0.148  0.147  -0.028 516 GLU EEE O   
7303  C CB  . GLU E 187 ? 2.059 1.989 2.065 0.163  0.109  0.092  516 GLU EEE CB  
7304  C CG  . GLU E 187 ? 2.066 1.952 2.071 0.152  0.106  0.041  516 GLU EEE CG  
7305  C CD  . GLU E 187 ? 2.057 1.963 2.141 0.135  0.067  0.053  516 GLU EEE CD  
7306  O OE1 . GLU E 187 ? 2.063 2.025 2.193 0.139  0.053  0.117  516 GLU EEE OE1 
7307  O OE2 . GLU E 187 ? 2.062 1.936 2.162 0.120  0.051  0.005  516 GLU EEE OE2 
7308  N N   . LEU E 188 ? 2.087 1.958 2.037 0.137  0.099  0.019  517 LEU EEE N   
7309  C CA  . LEU E 188 ? 2.114 1.943 2.039 0.132  0.085  -0.032 517 LEU EEE CA  
7310  C C   . LEU E 188 ? 2.150 1.950 2.111 0.116  0.015  -0.029 517 LEU EEE C   
7311  O O   . LEU E 188 ? 2.166 1.972 2.146 0.099  -0.024 0.013  517 LEU EEE O   
7312  C CB  . LEU E 188 ? 2.138 1.965 2.012 0.139  0.107  -0.029 517 LEU EEE CB  
7313  C CG  . LEU E 188 ? 2.192 1.988 2.016 0.149  0.122  -0.081 517 LEU EEE CG  
7314  C CD1 . LEU E 188 ? 2.201 2.003 1.975 0.155  0.158  -0.074 517 LEU EEE CD1 
7315  C CD2 . LEU E 188 ? 2.262 2.010 2.073 0.155  0.069  -0.106 517 LEU EEE CD2 
7316  N N   . LEU E 189 ? 2.192 1.959 2.162 0.120  -0.007 -0.066 518 LEU EEE N   
7317  C CA  . LEU E 189 ? 2.282 1.991 2.268 0.110  -0.088 -0.069 518 LEU EEE CA  
7318  C C   . LEU E 189 ? 2.406 2.028 2.307 0.135  -0.122 -0.116 518 LEU EEE C   
7319  O O   . LEU E 189 ? 2.439 2.068 2.299 0.142  -0.095 -0.118 518 LEU EEE O   
7320  C CB  . LEU E 189 ? 2.272 1.975 2.286 0.117  -0.093 -0.092 518 LEU EEE CB  
7321  C CG  . LEU E 189 ? 2.180 1.954 2.256 0.103  -0.057 -0.054 518 LEU EEE CG  
7322  C CD1 . LEU E 189 ? 2.169 1.928 2.274 0.106  -0.074 -0.077 518 LEU EEE CD1 
7323  C CD2 . LEU E 189 ? 2.151 1.977 2.284 0.078  -0.081 0.026  518 LEU EEE CD2 
7324  N N   . HIS E 190 ? 2.501 2.032 2.362 0.155  -0.183 -0.153 519 HIS EEE N   
7325  C CA  . HIS E 190 ? 2.639 2.068 2.380 0.211  -0.208 -0.212 519 HIS EEE CA  
7326  C C   . HIS E 190 ? 2.664 2.102 2.373 0.271  -0.163 -0.260 519 HIS EEE C   
7327  O O   . HIS E 190 ? 2.807 2.149 2.409 0.336  -0.197 -0.306 519 HIS EEE O   
7328  C CB  . HIS E 190 ? 2.781 2.069 2.471 0.198  -0.334 -0.207 519 HIS EEE CB  
7329  C CG  . HIS E 190 ? 2.852 2.088 2.485 0.188  -0.371 -0.197 519 HIS EEE CG  
7330  N ND1 . HIS E 190 ? 3.015 2.109 2.498 0.247  -0.420 -0.252 519 HIS EEE ND1 
7331  C CD2 . HIS E 190 ? 2.790 2.089 2.486 0.135  -0.371 -0.136 519 HIS EEE CD2 
7332  C CE1 . HIS E 190 ? 3.053 2.119 2.512 0.221  -0.452 -0.228 519 HIS EEE CE1 
7333  N NE2 . HIS E 190 ? 2.910 2.109 2.506 0.150  -0.421 -0.154 519 HIS EEE NE2 
7334  N N   . ALA E 191 ? 2.565 2.111 2.354 0.255  -0.094 -0.244 520 ALA EEE N   
7335  C CA  . ALA E 191 ? 2.579 2.172 2.371 0.299  -0.044 -0.267 520 ALA EEE CA  
7336  C C   . ALA E 191 ? 2.536 2.221 2.327 0.313  0.039  -0.259 520 ALA EEE C   
7337  O O   . ALA E 191 ? 2.472 2.192 2.286 0.272  0.063  -0.234 520 ALA EEE O   
7338  C CB  . ALA E 191 ? 2.506 2.143 2.390 0.260  -0.043 -0.245 520 ALA EEE CB  
7339  N N   . PRO E 192 ? 2.580 2.314 2.347 0.372  0.082  -0.270 521 PRO EEE N   
7340  C CA  . PRO E 192 ? 2.531 2.373 2.320 0.373  0.154  -0.242 521 PRO EEE CA  
7341  C C   . PRO E 192 ? 2.415 2.316 2.293 0.297  0.175  -0.202 521 PRO EEE C   
7342  O O   . PRO E 192 ? 2.375 2.297 2.311 0.275  0.169  -0.191 521 PRO EEE O   
7343  C CB  . PRO E 192 ? 2.578 2.488 2.360 0.447  0.188  -0.238 521 PRO EEE CB  
7344  C CG  . PRO E 192 ? 2.707 2.499 2.394 0.516  0.134  -0.288 521 PRO EEE CG  
7345  C CD  . PRO E 192 ? 2.682 2.375 2.394 0.447  0.062  -0.300 521 PRO EEE CD  
7346  N N   . ALA E 193 ? 2.376 2.288 2.246 0.264  0.195  -0.184 522 ALA EEE N   
7347  C CA  . ALA E 193 ? 2.306 2.230 2.213 0.204  0.203  -0.152 522 ALA EEE CA  
7348  C C   . ALA E 193 ? 2.281 2.276 2.242 0.185  0.224  -0.117 522 ALA EEE C   
7349  O O   . ALA E 193 ? 2.305 2.373 2.282 0.221  0.248  -0.106 522 ALA EEE O   
7350  C CB  . ALA E 193 ? 2.307 2.218 2.172 0.190  0.217  -0.144 522 ALA EEE CB  
7351  N N   . THR E 194 ? 2.256 2.228 2.237 0.136  0.210  -0.095 523 THR EEE N   
7352  C CA  . THR E 194 ? 2.257 2.272 2.290 0.104  0.206  -0.055 523 THR EEE CA  
7353  C C   . THR E 194 ? 2.277 2.222 2.277 0.053  0.179  -0.030 523 THR EEE C   
7354  O O   . THR E 194 ? 2.299 2.240 2.330 0.020  0.153  -0.002 523 THR EEE O   
7355  C CB  . THR E 194 ? 2.238 2.267 2.322 0.112  0.191  -0.063 523 THR EEE CB  
7356  O OG1 . THR E 194 ? 2.229 2.177 2.293 0.095  0.163  -0.081 523 THR EEE OG1 
7357  C CG2 . THR E 194 ? 2.251 2.309 2.337 0.173  0.203  -0.093 523 THR EEE CG2 
7358  N N   . VAL E 195 ? 2.295 2.178 2.225 0.051  0.180  -0.038 524 VAL EEE N   
7359  C CA  . VAL E 195 ? 2.371 2.159 2.233 0.020  0.148  -0.017 524 VAL EEE CA  
7360  C C   . VAL E 195 ? 2.443 2.206 2.243 0.019  0.159  -0.011 524 VAL EEE C   
7361  O O   . VAL E 195 ? 2.486 2.192 2.218 0.046  0.166  -0.031 524 VAL EEE O   
7362  C CB  . VAL E 195 ? 2.379 2.079 2.185 0.037  0.130  -0.035 524 VAL EEE CB  
7363  C CG1 . VAL E 195 ? 2.476 2.055 2.188 0.018  0.085  -0.016 524 VAL EEE CG1 
7364  C CG2 . VAL E 195 ? 2.331 2.065 2.203 0.044  0.125  -0.046 524 VAL EEE CG2 
7365  N N   . CYS E 196 ? 2.477 2.291 2.306 -0.011 0.158  0.027  525 CYS EEE N   
7366  C CA  . CYS E 196 ? 2.520 2.324 2.304 -0.019 0.165  0.042  525 CYS EEE CA  
7367  C C   . CYS E 196 ? 2.613 2.321 2.344 -0.072 0.106  0.084  525 CYS EEE C   
7368  O O   . CYS E 196 ? 2.639 2.296 2.374 -0.101 0.059  0.103  525 CYS EEE O   
7369  C CB  . CYS E 196 ? 2.494 2.435 2.348 -0.008 0.206  0.064  525 CYS EEE CB  
7370  S SG  . CYS E 196 ? 2.454 2.484 2.363 0.055  0.247  0.024  525 CYS EEE SG  
7371  N N   . GLY E 197 ? 2.687 2.356 2.360 -0.083 0.099  0.099  526 GLY EEE N   
7372  C CA  . GLY E 197 ? 2.840 2.407 2.455 -0.139 0.029  0.148  526 GLY EEE CA  
7373  C C   . GLY E 197 ? 2.881 2.566 2.580 -0.185 0.031  0.216  526 GLY EEE C   
7374  O O   . GLY E 197 ? 2.821 2.673 2.622 -0.163 0.091  0.228  526 GLY EEE O   
7375  N N   . PRO E 198 ? 3.029 2.627 2.682 -0.244 -0.039 0.271  527 PRO EEE N   
7376  C CA  . PRO E 198 ? 3.050 2.774 2.794 -0.295 -0.044 0.357  527 PRO EEE CA  
7377  C C   . PRO E 198 ? 3.021 2.849 2.776 -0.252 0.034  0.342  527 PRO EEE C   
7378  O O   . PRO E 198 ? 2.958 2.961 2.809 -0.214 0.104  0.349  527 PRO EEE O   
7379  C CB  . PRO E 198 ? 3.197 2.749 2.858 -0.372 -0.161 0.412  527 PRO EEE CB  
7380  C CG  . PRO E 198 ? 3.283 2.600 2.757 -0.326 -0.192 0.327  527 PRO EEE CG  
7381  C CD  . PRO E 198 ? 3.177 2.543 2.677 -0.262 -0.128 0.260  527 PRO EEE CD  
7382  N N   . LYS E 199 ? 3.089 2.803 2.736 -0.250 0.017  0.323  528 LYS EEE N   
7383  C CA  . LYS E 199 ? 3.027 2.820 2.673 -0.223 0.074  0.320  528 LYS EEE CA  
7384  C C   . LYS E 199 ? 2.907 2.864 2.626 -0.155 0.168  0.286  528 LYS EEE C   
7385  O O   . LYS E 199 ? 2.859 2.870 2.563 -0.113 0.221  0.264  528 LYS EEE O   
7386  C CB  . LYS E 199 ? 3.055 2.683 2.551 -0.192 0.066  0.258  528 LYS EEE CB  
7387  C CG  . LYS E 199 ? 3.170 2.634 2.565 -0.244 -0.023 0.296  528 LYS EEE CG  
7388  C CD  . LYS E 199 ? 3.157 2.701 2.596 -0.287 -0.026 0.364  528 LYS EEE CD  
7389  C CE  . LYS E 199 ? 3.297 2.643 2.598 -0.321 -0.111 0.379  528 LYS EEE CE  
7390  N NZ  . LYS E 199 ? 3.288 2.725 2.636 -0.355 -0.104 0.440  528 LYS EEE NZ  
7391  N N   . GLN F 1   ? 2.168 2.846 2.490 -0.325 0.283  0.284  1   GLN FFF N   
7392  C CA  . GLN F 1   ? 2.168 2.691 2.438 -0.309 0.256  0.281  1   GLN FFF CA  
7393  C C   . GLN F 1   ? 2.066 2.575 2.315 -0.235 0.233  0.252  1   GLN FFF C   
7394  O O   . GLN F 1   ? 2.041 2.646 2.328 -0.206 0.227  0.227  1   GLN FFF O   
7395  C CB  . GLN F 1   ? 2.227 2.698 2.523 -0.360 0.234  0.270  1   GLN FFF CB  
7396  C CG  . GLN F 1   ? 2.277 2.590 2.518 -0.350 0.212  0.271  1   GLN FFF CG  
7397  C CD  . GLN F 1   ? 2.319 2.596 2.588 -0.387 0.186  0.248  1   GLN FFF CD  
7398  O OE1 . GLN F 1   ? 2.298 2.567 2.574 -0.354 0.158  0.217  1   GLN FFF OE1 
7399  N NE2 . GLN F 1   ? 2.409 2.664 2.692 -0.458 0.196  0.263  1   GLN FFF NE2 
7400  N N   . VAL F 2   ? 2.000 2.396 2.190 -0.205 0.221  0.255  2   VAL FFF N   
7401  C CA  . VAL F 2   ? 1.894 2.257 2.057 -0.145 0.199  0.229  2   VAL FFF CA  
7402  C C   . VAL F 2   ? 1.848 2.183 2.036 -0.152 0.168  0.203  2   VAL FFF C   
7403  O O   . VAL F 2   ? 1.853 2.119 2.039 -0.189 0.158  0.209  2   VAL FFF O   
7404  C CB  . VAL F 2   ? 1.886 2.152 1.982 -0.119 0.198  0.240  2   VAL FFF CB  
7405  C CG1 . VAL F 2   ? 1.832 2.062 1.903 -0.071 0.175  0.213  2   VAL FFF CG1 
7406  C CG2 . VAL F 2   ? 1.921 2.219 1.988 -0.109 0.226  0.264  2   VAL FFF CG2 
7407  N N   . GLN F 3   ? 1.810 2.192 2.013 -0.113 0.154  0.176  3   GLN FFF N   
7408  C CA  . GLN F 3   ? 1.802 2.163 2.020 -0.109 0.123  0.150  3   GLN FFF CA  
7409  C C   . GLN F 3   ? 1.784 2.111 1.962 -0.051 0.110  0.132  3   GLN FFF C   
7410  O O   . GLN F 3   ? 1.781 2.158 1.952 -0.012 0.120  0.128  3   GLN FFF O   
7411  C CB  . GLN F 3   ? 1.803 2.271 2.086 -0.129 0.118  0.135  3   GLN FFF CB  
7412  C CG  . GLN F 3   ? 1.848 2.306 2.164 -0.197 0.115  0.139  3   GLN FFF CG  
7413  C CD  . GLN F 3   ? 1.863 2.454 2.249 -0.229 0.120  0.131  3   GLN FFF CD  
7414  O OE1 . GLN F 3   ? 1.835 2.505 2.252 -0.202 0.104  0.106  3   GLN FFF OE1 
7415  N NE2 . GLN F 3   ? 1.908 2.529 2.317 -0.287 0.144  0.152  3   GLN FFF NE2 
7416  N N   . LEU F 4   ? 1.794 2.037 1.945 -0.047 0.090  0.122  4   LEU FFF N   
7417  C CA  . LEU F 4   ? 1.804 2.008 1.918 -0.004 0.075  0.105  4   LEU FFF CA  
7418  C C   . LEU F 4   ? 1.818 2.051 1.958 0.000  0.052  0.083  4   LEU FFF C   
7419  O O   . LEU F 4   ? 1.834 2.070 2.005 -0.036 0.041  0.079  4   LEU FFF O   
7420  C CB  . LEU F 4   ? 1.826 1.934 1.896 -0.006 0.069  0.108  4   LEU FFF CB  
7421  C CG  . LEU F 4   ? 1.850 1.930 1.896 -0.015 0.087  0.131  4   LEU FFF CG  
7422  C CD1 . LEU F 4   ? 1.859 1.861 1.860 -0.004 0.079  0.129  4   LEU FFF CD1 
7423  C CD2 . LEU F 4   ? 1.849 1.977 1.884 0.008  0.108  0.138  4   LEU FFF CD2 
7424  N N   . VAL F 5   ? 1.827 2.077 1.950 0.044  0.045  0.070  5   VAL FFF N   
7425  C CA  . VAL F 5   ? 1.842 2.122 1.981 0.058  0.022  0.051  5   VAL FFF CA  
7426  C C   . VAL F 5   ? 1.839 2.051 1.919 0.098  0.011  0.043  5   VAL FFF C   
7427  O O   . VAL F 5   ? 1.847 2.063 1.899 0.138  0.018  0.042  5   VAL FFF O   
7428  C CB  . VAL F 5   ? 1.862 2.256 2.044 0.075  0.023  0.045  5   VAL FFF CB  
7429  C CG1 . VAL F 5   ? 1.882 2.312 2.076 0.095  -0.003 0.026  5   VAL FFF CG1 
7430  C CG2 . VAL F 5   ? 1.860 2.329 2.101 0.027  0.037  0.054  5   VAL FFF CG2 
7431  N N   . GLU F 6   ? 1.822 1.972 1.882 0.085  -0.003 0.036  6   GLU FFF N   
7432  C CA  . GLU F 6   ? 1.833 1.922 1.838 0.113  -0.013 0.029  6   GLU FFF CA  
7433  C C   . GLU F 6   ? 1.862 1.993 1.868 0.145  -0.029 0.018  6   GLU FFF C   
7434  O O   . GLU F 6   ? 1.853 2.065 1.911 0.137  -0.038 0.012  6   GLU FFF O   
7435  C CB  . GLU F 6   ? 1.818 1.849 1.809 0.090  -0.024 0.023  6   GLU FFF CB  
7436  C CG  . GLU F 6   ? 1.809 1.795 1.790 0.068  -0.011 0.033  6   GLU FFF CG  
7437  C CD  . GLU F 6   ? 1.814 1.816 1.836 0.033  -0.009 0.039  6   GLU FFF CD  
7438  O OE1 . GLU F 6   ? 1.804 1.865 1.869 0.021  -0.009 0.039  6   GLU FFF OE1 
7439  O OE2 . GLU F 6   ? 1.813 1.767 1.821 0.019  -0.006 0.044  6   GLU FFF OE2 
7440  N N   . SER F 7   ? 1.912 1.991 1.861 0.179  -0.033 0.017  7   SER FFF N   
7441  C CA  . SER F 7   ? 1.937 2.031 1.867 0.215  -0.051 0.010  7   SER FFF CA  
7442  C C   . SER F 7   ? 1.964 1.962 1.814 0.237  -0.049 0.015  7   SER FFF C   
7443  O O   . SER F 7   ? 1.954 1.891 1.774 0.224  -0.033 0.021  7   SER FFF O   
7444  C CB  . SER F 7   ? 1.960 2.133 1.913 0.252  -0.051 0.009  7   SER FFF CB  
7445  O OG  . SER F 7   ? 1.996 2.153 1.931 0.270  -0.030 0.017  7   SER FFF OG  
7446  N N   . GLY F 8   ? 2.002 1.989 1.818 0.267  -0.065 0.012  8   GLY FFF N   
7447  C CA  . GLY F 8   ? 2.063 1.954 1.797 0.284  -0.063 0.019  8   GLY FFF CA  
7448  C C   . GLY F 8   ? 2.053 1.910 1.770 0.253  -0.069 0.016  8   GLY FFF C   
7449  O O   . GLY F 8   ? 2.106 1.886 1.756 0.255  -0.064 0.023  8   GLY FFF O   
7450  N N   . GLY F 9   ? 1.996 1.907 1.769 0.223  -0.079 0.005  9   GLY FFF N   
7451  C CA  . GLY F 9   ? 1.973 1.868 1.736 0.202  -0.089 -0.003 9   GLY FFF CA  
7452  C C   . GLY F 9   ? 1.978 1.880 1.707 0.231  -0.108 -0.005 9   GLY FFF C   
7453  O O   . GLY F 9   ? 1.970 1.918 1.708 0.265  -0.119 -0.005 9   GLY FFF O   
7454  N N   . GLY F 10  ? 1.968 1.832 1.656 0.221  -0.111 -0.007 10  GLY FFF N   
7455  C CA  . GLY F 10  ? 1.991 1.862 1.641 0.245  -0.129 -0.009 10  GLY FFF CA  
7456  C C   . GLY F 10  ? 1.998 1.808 1.584 0.234  -0.121 -0.004 10  GLY FFF C   
7457  O O   . GLY F 10  ? 1.932 1.724 1.527 0.200  -0.109 -0.009 10  GLY FFF O   
7458  N N   . LEU F 11  ? 2.057 1.838 1.577 0.264  -0.128 0.008  11  LEU FFF N   
7459  C CA  . LEU F 11  ? 2.115 1.850 1.566 0.257  -0.123 0.015  11  LEU FFF CA  
7460  C C   . LEU F 11  ? 2.202 1.841 1.579 0.256  -0.100 0.039  11  LEU FFF C   
7461  O O   . LEU F 11  ? 2.261 1.869 1.618 0.286  -0.098 0.051  11  LEU FFF O   
7462  C CB  . LEU F 11  ? 2.167 1.934 1.589 0.294  -0.147 0.014  11  LEU FFF CB  
7463  C CG  . LEU F 11  ? 2.196 1.969 1.583 0.284  -0.153 0.007  11  LEU FFF CG  
7464  C CD1 . LEU F 11  ? 2.117 1.953 1.575 0.253  -0.162 -0.024 11  LEU FFF CD1 
7465  C CD2 . LEU F 11  ? 2.272 2.062 1.610 0.329  -0.176 0.013  11  LEU FFF CD2 
7466  N N   . MET F 12  ? 2.253 1.850 1.591 0.222  -0.081 0.044  12  MET FFF N   
7467  C CA  . MET F 12  ? 2.362 1.862 1.621 0.211  -0.058 0.066  12  MET FFF CA  
7468  C C   . MET F 12  ? 2.386 1.865 1.598 0.175  -0.043 0.071  12  MET FFF C   
7469  O O   . MET F 12  ? 2.308 1.833 1.565 0.141  -0.036 0.054  12  MET FFF O   
7470  C CB  . MET F 12  ? 2.372 1.847 1.657 0.188  -0.041 0.064  12  MET FFF CB  
7471  C CG  . MET F 12  ? 2.455 1.891 1.724 0.226  -0.044 0.074  12  MET FFF CG  
7472  S SD  . MET F 12  ? 2.650 1.993 1.808 0.272  -0.048 0.100  12  MET FFF SD  
7473  C CE  . MET F 12  ? 2.745 1.970 1.813 0.223  -0.018 0.116  12  MET FFF CE  
7474  N N   . GLN F 13  ? 2.488 1.898 1.608 0.185  -0.037 0.094  13  GLN FFF N   
7475  C CA  . GLN F 13  ? 2.529 1.914 1.592 0.147  -0.018 0.103  13  GLN FFF CA  
7476  C C   . GLN F 13  ? 2.458 1.815 1.528 0.096  0.009  0.101  13  GLN FFF C   
7477  O O   . GLN F 13  ? 2.476 1.759 1.519 0.096  0.017  0.111  13  GLN FFF O   
7478  C CB  . GLN F 13  ? 2.689 1.999 1.646 0.169  -0.016 0.132  13  GLN FFF CB  
7479  C CG  . GLN F 13  ? 2.816 2.002 1.693 0.178  -0.004 0.159  13  GLN FFF CG  
7480  C CD  . GLN F 13  ? 2.996 2.098 1.758 0.175  0.008  0.190  13  GLN FFF CD  
7481  O OE1 . GLN F 13  ? 3.041 2.179 1.778 0.199  -0.005 0.196  13  GLN FFF OE1 
7482  N NE2 . GLN F 13  ? 3.131 2.124 1.819 0.138  0.034  0.210  13  GLN FFF NE2 
7483  N N   . ALA F 14  ? 2.359 1.780 1.469 0.058  0.019  0.084  14  ALA FFF N   
7484  C CA  . ALA F 14  ? 2.328 1.756 1.459 0.008  0.040  0.076  14  ALA FFF CA  
7485  C C   . ALA F 14  ? 2.462 1.786 1.509 -0.022 0.063  0.098  14  ALA FFF C   
7486  O O   . ALA F 14  ? 2.547 1.817 1.513 -0.028 0.073  0.120  14  ALA FFF O   
7487  C CB  . ALA F 14  ? 2.272 1.781 1.429 -0.019 0.048  0.059  14  ALA FFF CB  
7488  N N   . GLY F 15  ? 2.508 1.800 1.568 -0.042 0.072  0.093  15  GLY FFF N   
7489  C CA  . GLY F 15  ? 2.655 1.835 1.636 -0.071 0.092  0.110  15  GLY FFF CA  
7490  C C   . GLY F 15  ? 2.744 1.839 1.696 -0.025 0.080  0.120  15  GLY FFF C   
7491  O O   . GLY F 15  ? 2.817 1.823 1.721 -0.046 0.094  0.124  15  GLY FFF O   
7492  N N   . GLY F 16  ? 2.749 1.874 1.728 0.035  0.057  0.121  16  GLY FFF N   
7493  C CA  . GLY F 16  ? 2.775 1.858 1.751 0.087  0.043  0.124  16  GLY FFF CA  
7494  C C   . GLY F 16  ? 2.699 1.827 1.749 0.080  0.043  0.103  16  GLY FFF C   
7495  O O   . GLY F 16  ? 2.691 1.839 1.762 0.029  0.058  0.091  16  GLY FFF O   
7496  N N   . SER F 17  ? 2.655 1.807 1.743 0.129  0.028  0.098  17  SER FFF N   
7497  C CA  . SER F 17  ? 2.543 1.750 1.706 0.127  0.027  0.080  17  SER FFF CA  
7498  C C   . SER F 17  ? 2.462 1.744 1.688 0.176  0.007  0.074  17  SER FFF C   
7499  O O   . SER F 17  ? 2.517 1.787 1.715 0.220  -0.007 0.084  17  SER FFF O   
7500  C CB  . SER F 17  ? 2.602 1.723 1.718 0.120  0.041  0.079  17  SER FFF CB  
7501  O OG  . SER F 17  ? 2.511 1.690 1.694 0.113  0.042  0.062  17  SER FFF OG  
7502  N N   . LEU F 18  ? 2.358 1.717 1.666 0.166  0.005  0.059  18  LEU FFF N   
7503  C CA  . LEU F 18  ? 2.315 1.752 1.691 0.201  -0.010 0.053  18  LEU FFF CA  
7504  C C   . LEU F 18  ? 2.302 1.762 1.720 0.194  -0.001 0.045  18  LEU FFF C   
7505  O O   . LEU F 18  ? 2.302 1.761 1.731 0.155  0.011  0.038  18  LEU FFF O   
7506  C CB  . LEU F 18  ? 2.239 1.760 1.676 0.189  -0.024 0.044  18  LEU FFF CB  
7507  C CG  . LEU F 18  ? 2.208 1.804 1.700 0.221  -0.044 0.039  18  LEU FFF CG  
7508  C CD1 . LEU F 18  ? 2.281 1.854 1.735 0.274  -0.051 0.048  18  LEU FFF CD1 
7509  C CD2 . LEU F 18  ? 2.163 1.809 1.679 0.214  -0.060 0.031  18  LEU FFF CD2 
7510  N N   . ARG F 19  ? 2.299 1.784 1.737 0.233  -0.006 0.044  19  ARG FFF N   
7511  C CA  . ARG F 19  ? 2.244 1.760 1.721 0.234  0.003  0.038  19  ARG FFF CA  
7512  C C   . ARG F 19  ? 2.145 1.767 1.710 0.234  -0.006 0.034  19  ARG FFF C   
7513  O O   . ARG F 19  ? 2.142 1.809 1.728 0.258  -0.021 0.034  19  ARG FFF O   
7514  C CB  . ARG F 19  ? 2.335 1.804 1.765 0.280  0.007  0.040  19  ARG FFF CB  
7515  C CG  . ARG F 19  ? 2.310 1.806 1.767 0.286  0.019  0.033  19  ARG FFF CG  
7516  C CD  . ARG F 19  ? 2.419 1.860 1.819 0.339  0.021  0.032  19  ARG FFF CD  
7517  N NE  . ARG F 19  ? 2.445 1.904 1.857 0.349  0.034  0.023  19  ARG FFF NE  
7518  C CZ  . ARG F 19  ? 2.565 1.970 1.924 0.392  0.040  0.018  19  ARG FFF CZ  
7519  N NH1 . ARG F 19  ? 2.699 2.017 1.983 0.431  0.035  0.022  19  ARG FFF NH1 
7520  N NH2 . ARG F 19  ? 2.555 1.989 1.929 0.398  0.052  0.008  19  ARG FFF NH2 
7521  N N   . LEU F 20  ? 2.082 1.741 1.693 0.206  0.002  0.030  20  LEU FFF N   
7522  C CA  . LEU F 20  ? 2.015 1.761 1.704 0.198  -0.003 0.028  20  LEU FFF CA  
7523  C C   . LEU F 20  ? 1.996 1.770 1.705 0.209  0.010  0.029  20  LEU FFF C   
7524  O O   . LEU F 20  ? 2.005 1.734 1.678 0.205  0.023  0.029  20  LEU FFF O   
7525  C CB  . LEU F 20  ? 1.965 1.721 1.681 0.158  -0.004 0.024  20  LEU FFF CB  
7526  C CG  . LEU F 20  ? 1.953 1.720 1.678 0.150  -0.020 0.019  20  LEU FFF CG  
7527  C CD1 . LEU F 20  ? 1.975 1.704 1.670 0.125  -0.016 0.016  20  LEU FFF CD1 
7528  C CD2 . LEU F 20  ? 1.902 1.732 1.692 0.138  -0.030 0.014  20  LEU FFF CD2 
7529  N N   . SER F 21  ? 1.952 1.804 1.715 0.220  0.006  0.030  21  SER FFF N   
7530  C CA  . SER F 21  ? 1.943 1.841 1.728 0.237  0.019  0.032  21  SER FFF CA  
7531  C C   . SER F 21  ? 1.846 1.821 1.703 0.207  0.022  0.037  21  SER FFF C   
7532  O O   . SER F 21  ? 1.814 1.847 1.716 0.202  0.009  0.034  21  SER FFF O   
7533  C CB  . SER F 21  ? 2.030 1.955 1.805 0.288  0.014  0.029  21  SER FFF CB  
7534  O OG  . SER F 21  ? 2.130 1.975 1.837 0.313  0.006  0.028  21  SER FFF OG  
7535  N N   . CYS F 22  ? 1.810 1.781 1.672 0.186  0.037  0.043  22  CYS FFF N   
7536  C CA  . CYS F 22  ? 1.775 1.803 1.693 0.155  0.043  0.052  22  CYS FFF CA  
7537  C C   . CYS F 22  ? 1.766 1.849 1.696 0.171  0.062  0.058  22  CYS FFF C   
7538  O O   . CYS F 22  ? 1.741 1.794 1.637 0.178  0.076  0.060  22  CYS FFF O   
7539  C CB  . CYS F 22  ? 1.771 1.755 1.680 0.123  0.046  0.058  22  CYS FFF CB  
7540  S SG  . CYS F 22  ? 1.761 1.788 1.716 0.090  0.058  0.075  22  CYS FFF SG  
7541  N N   . ALA F 23  ? 1.777 1.945 1.757 0.175  0.061  0.058  23  ALA FFF N   
7542  C CA  . ALA F 23  ? 1.809 2.057 1.814 0.189  0.080  0.063  23  ALA FFF CA  
7543  C C   . ALA F 23  ? 1.790 2.072 1.833 0.143  0.095  0.080  23  ALA FFF C   
7544  O O   . ALA F 23  ? 1.782 2.075 1.863 0.104  0.085  0.084  23  ALA FFF O   
7545  C CB  . ALA F 23  ? 1.836 2.169 1.876 0.216  0.071  0.053  23  ALA FFF CB  
7546  N N   . VAL F 24  ? 1.774 2.069 1.802 0.148  0.117  0.090  24  VAL FFF N   
7547  C CA  . VAL F 24  ? 1.743 2.061 1.790 0.109  0.135  0.111  24  VAL FFF CA  
7548  C C   . VAL F 24  ? 1.739 2.168 1.824 0.114  0.156  0.117  24  VAL FFF C   
7549  O O   . VAL F 24  ? 1.758 2.211 1.819 0.159  0.165  0.107  24  VAL FFF O   
7550  C CB  . VAL F 24  ? 1.753 2.002 1.746 0.112  0.144  0.119  24  VAL FFF CB  
7551  C CG1 . VAL F 24  ? 1.756 2.009 1.759 0.073  0.158  0.145  24  VAL FFF CG1 
7552  C CG2 . VAL F 24  ? 1.760 1.917 1.712 0.116  0.125  0.108  24  VAL FFF CG2 
7553  N N   . SER F 25  ? 1.749 2.239 1.887 0.069  0.164  0.131  25  SER FFF N   
7554  C CA  . SER F 25  ? 1.800 2.407 1.978 0.061  0.189  0.140  25  SER FFF CA  
7555  C C   . SER F 25  ? 1.857 2.454 2.040 0.006  0.209  0.170  25  SER FFF C   
7556  O O   . SER F 25  ? 1.865 2.426 2.069 -0.042 0.199  0.178  25  SER FFF O   
7557  C CB  . SER F 25  ? 1.792 2.506 2.033 0.058  0.181  0.127  25  SER FFF CB  
7558  O OG  . SER F 25  ? 1.794 2.499 2.074 0.002  0.168  0.130  25  SER FFF OG  
7559  N N   . GLY F 26  ? 1.931 2.554 2.090 0.014  0.236  0.186  26  GLY FFF N   
7560  C CA  . GLY F 26  ? 2.010 2.617 2.158 -0.031 0.258  0.219  26  GLY FFF CA  
7561  C C   . GLY F 26  ? 2.077 2.675 2.169 0.001  0.278  0.229  26  GLY FFF C   
7562  O O   . GLY F 26  ? 2.083 2.725 2.162 0.051  0.282  0.209  26  GLY FFF O   
7563  N N   . ARG F 27  ? 2.153 2.693 2.209 -0.025 0.289  0.257  27  ARG FFF N   
7564  C CA  . ARG F 27  ? 2.211 2.736 2.207 0.004  0.305  0.267  27  ARG FFF CA  
7565  C C   . ARG F 27  ? 2.216 2.667 2.165 0.050  0.282  0.239  27  ARG FFF C   
7566  O O   . ARG F 27  ? 2.234 2.597 2.148 0.043  0.267  0.246  27  ARG FFF O   
7567  C CB  . ARG F 27  ? 2.263 2.731 2.226 -0.033 0.316  0.305  27  ARG FFF CB  
7568  C CG  . ARG F 27  ? 2.320 2.850 2.314 -0.085 0.344  0.338  27  ARG FFF CG  
7569  C CD  . ARG F 27  ? 2.404 2.869 2.343 -0.106 0.359  0.379  27  ARG FFF CD  
7570  N NE  . ARG F 27  ? 2.476 2.979 2.436 -0.165 0.387  0.415  27  ARG FFF NE  
7571  C CZ  . ARG F 27  ? 2.553 3.033 2.465 -0.185 0.411  0.457  27  ARG FFF CZ  
7572  N NH1 . ARG F 27  ? 2.565 2.993 2.408 -0.147 0.409  0.466  27  ARG FFF NH1 
7573  N NH2 . ARG F 27  ? 2.615 3.128 2.549 -0.246 0.438  0.490  27  ARG FFF NH2 
7574  N N   . THR F 28  ? 2.227 2.712 2.174 0.095  0.278  0.209  28  THR FFF N   
7575  C CA  . THR F 28  ? 2.242 2.656 2.142 0.136  0.259  0.180  28  THR FFF CA  
7576  C C   . THR F 28  ? 2.332 2.702 2.168 0.148  0.265  0.184  28  THR FFF C   
7577  O O   . THR F 28  ? 2.371 2.662 2.170 0.156  0.245  0.170  28  THR FFF O   
7578  C CB  . THR F 28  ? 2.213 2.669 2.110 0.185  0.260  0.151  28  THR FFF CB  
7579  O OG1 . THR F 28  ? 2.173 2.668 2.125 0.182  0.249  0.143  28  THR FFF OG1 
7580  C CG2 . THR F 28  ? 2.217 2.588 2.054 0.221  0.245  0.124  28  THR FFF CG2 
7581  N N   . PHE F 29  ? 2.382 2.810 2.204 0.149  0.291  0.201  29  PHE FFF N   
7582  C CA  . PHE F 29  ? 2.405 2.816 2.163 0.168  0.300  0.202  29  PHE FFF CA  
7583  C C   . PHE F 29  ? 2.325 2.655 2.053 0.147  0.284  0.216  29  PHE FFF C   
7584  O O   . PHE F 29  ? 2.327 2.619 2.003 0.168  0.275  0.200  29  PHE FFF O   
7585  C CB  . PHE F 29  ? 2.524 3.021 2.280 0.164  0.334  0.226  29  PHE FFF CB  
7586  C CG  . PHE F 29  ? 2.625 3.124 2.392 0.117  0.347  0.271  29  PHE FFF CG  
7587  C CD1 . PHE F 29  ? 2.688 3.135 2.401 0.111  0.346  0.293  29  PHE FFF CD1 
7588  C CD2 . PHE F 29  ? 2.641 3.193 2.467 0.078  0.360  0.292  29  PHE FFF CD2 
7589  C CE1 . PHE F 29  ? 2.715 3.149 2.428 0.072  0.359  0.337  29  PHE FFF CE1 
7590  C CE2 . PHE F 29  ? 2.676 3.214 2.504 0.031  0.374  0.335  29  PHE FFF CE2 
7591  C CZ  . PHE F 29  ? 2.712 3.184 2.479 0.030  0.373  0.359  29  PHE FFF CZ  
7592  N N   . SER F 30  ? 2.242 2.550 2.002 0.110  0.279  0.242  30  SER FFF N   
7593  C CA  . SER F 30  ? 2.233 2.474 1.965 0.093  0.267  0.263  30  SER FFF CA  
7594  C C   . SER F 30  ? 2.144 2.316 1.878 0.096  0.235  0.240  30  SER FFF C   
7595  O O   . SER F 30  ? 2.187 2.308 1.900 0.088  0.223  0.252  30  SER FFF O   
7596  C CB  . SER F 30  ? 2.294 2.535 2.049 0.052  0.280  0.303  30  SER FFF CB  
7597  O OG  . SER F 30  ? 2.287 2.576 2.104 0.029  0.287  0.302  30  SER FFF OG  
7598  N N   . THR F 31  ? 2.027 2.198 1.781 0.109  0.224  0.208  31  THR FFF N   
7599  C CA  . THR F 31  ? 1.948 2.059 1.703 0.109  0.197  0.186  31  THR FFF CA  
7600  C C   . THR F 31  ? 1.932 2.008 1.635 0.125  0.186  0.171  31  THR FFF C   
7601  O O   . THR F 31  ? 1.943 2.030 1.614 0.146  0.192  0.150  31  THR FFF O   
7602  C CB  . THR F 31  ? 1.908 2.025 1.686 0.122  0.190  0.160  31  THR FFF CB  
7603  O OG1 . THR F 31  ? 1.879 2.049 1.709 0.109  0.199  0.172  31  THR FFF OG1 
7604  C CG2 . THR F 31  ? 1.886 1.946 1.666 0.117  0.165  0.143  31  THR FFF CG2 
7605  N N   . ALA F 32  ? 1.911 1.947 1.606 0.115  0.170  0.177  32  ALA FFF N   
7606  C CA  . ALA F 32  ? 1.898 1.913 1.553 0.125  0.156  0.159  32  ALA FFF CA  
7607  C C   . ALA F 32  ? 1.855 1.839 1.515 0.123  0.140  0.127  32  ALA FFF C   
7608  O O   . ALA F 32  ? 1.849 1.827 1.477 0.133  0.139  0.101  32  ALA FFF O   
7609  C CB  . ALA F 32  ? 1.906 1.903 1.551 0.121  0.146  0.180  32  ALA FFF CB  
7610  N N   . ALA F 33  ? 1.818 1.779 1.512 0.110  0.128  0.129  33  ALA FFF N   
7611  C CA  . ALA F 33  ? 1.769 1.700 1.467 0.104  0.112  0.105  33  ALA FFF CA  
7612  C C   . ALA F 33  ? 1.738 1.660 1.479 0.095  0.107  0.110  33  ALA FFF C   
7613  O O   . ALA F 33  ? 1.733 1.665 1.501 0.085  0.111  0.132  33  ALA FFF O   
7614  C CB  . ALA F 33  ? 1.753 1.675 1.437 0.100  0.097  0.100  33  ALA FFF CB  
7615  N N   . MET F 34  ? 1.723 1.625 1.465 0.095  0.099  0.090  34  MET FFF N   
7616  C CA  . MET F 34  ? 1.711 1.604 1.487 0.087  0.090  0.089  34  MET FFF CA  
7617  C C   . MET F 34  ? 1.711 1.574 1.477 0.079  0.074  0.075  34  MET FFF C   
7618  O O   . MET F 34  ? 1.737 1.586 1.469 0.080  0.073  0.059  34  MET FFF O   
7619  C CB  . MET F 34  ? 1.736 1.632 1.514 0.101  0.093  0.079  34  MET FFF CB  
7620  C CG  . MET F 34  ? 1.767 1.708 1.559 0.113  0.109  0.088  34  MET FFF CG  
7621  S SD  . MET F 34  ? 1.792 1.779 1.642 0.092  0.113  0.112  34  MET FFF SD  
7622  C CE  . MET F 34  ? 1.780 1.764 1.663 0.089  0.095  0.100  34  MET FFF CE  
7623  N N   . GLY F 35  ? 1.708 1.564 1.501 0.070  0.064  0.078  35  GLY FFF N   
7624  C CA  . GLY F 35  ? 1.722 1.559 1.509 0.065  0.050  0.064  35  GLY FFF CA  
7625  C C   . GLY F 35  ? 1.733 1.561 1.541 0.061  0.041  0.058  35  GLY FFF C   
7626  O O   . GLY F 35  ? 1.773 1.612 1.612 0.058  0.041  0.067  35  GLY FFF O   
7627  N N   . TRP F 36  ? 1.732 1.546 1.524 0.058  0.034  0.042  36  TRP FFF N   
7628  C CA  . TRP F 36  ? 1.725 1.531 1.529 0.056  0.023  0.035  36  TRP FFF CA  
7629  C C   . TRP F 36  ? 1.728 1.533 1.538 0.052  0.013  0.028  36  TRP FFF C   
7630  O O   . TRP F 36  ? 1.776 1.587 1.567 0.051  0.014  0.022  36  TRP FFF O   
7631  C CB  . TRP F 36  ? 1.751 1.537 1.525 0.059  0.023  0.025  36  TRP FFF CB  
7632  C CG  . TRP F 36  ? 1.768 1.553 1.538 0.073  0.029  0.030  36  TRP FFF CG  
7633  C CD1 . TRP F 36  ? 1.802 1.572 1.542 0.082  0.040  0.030  36  TRP FFF CD1 
7634  C CD2 . TRP F 36  ? 1.770 1.573 1.566 0.084  0.023  0.033  36  TRP FFF CD2 
7635  N NE1 . TRP F 36  ? 1.815 1.593 1.560 0.102  0.042  0.033  36  TRP FFF NE1 
7636  C CE2 . TRP F 36  ? 1.795 1.599 1.577 0.103  0.031  0.036  36  TRP FFF CE2 
7637  C CE3 . TRP F 36  ? 1.780 1.602 1.608 0.079  0.010  0.031  36  TRP FFF CE3 
7638  C CZ2 . TRP F 36  ? 1.818 1.652 1.621 0.121  0.027  0.037  36  TRP FFF CZ2 
7639  C CZ3 . TRP F 36  ? 1.791 1.643 1.642 0.091  0.005  0.032  36  TRP FFF CZ3 
7640  C CH2 . TRP F 36  ? 1.808 1.670 1.648 0.114  0.013  0.035  36  TRP FFF CH2 
7641  N N   . PHE F 37  ? 1.716 1.517 1.551 0.051  0.003  0.028  37  PHE FFF N   
7642  C CA  . PHE F 37  ? 1.717 1.511 1.555 0.053  -0.009 0.017  37  PHE FFF CA  
7643  C C   . PHE F 37  ? 1.735 1.527 1.579 0.051  -0.019 0.004  37  PHE FFF C   
7644  O O   . PHE F 37  ? 1.753 1.549 1.612 0.047  -0.021 0.007  37  PHE FFF O   
7645  C CB  . PHE F 37  ? 1.724 1.501 1.578 0.054  -0.013 0.027  37  PHE FFF CB  
7646  C CG  . PHE F 37  ? 1.741 1.519 1.582 0.062  -0.005 0.041  37  PHE FFF CG  
7647  C CD1 . PHE F 37  ? 1.733 1.522 1.573 0.058  0.008  0.057  37  PHE FFF CD1 
7648  C CD2 . PHE F 37  ? 1.779 1.554 1.607 0.077  -0.011 0.037  37  PHE FFF CD2 
7649  C CE1 . PHE F 37  ? 1.740 1.534 1.564 0.066  0.015  0.070  37  PHE FFF CE1 
7650  C CE2 . PHE F 37  ? 1.795 1.575 1.607 0.089  -0.006 0.051  37  PHE FFF CE2 
7651  C CZ  . PHE F 37  ? 1.765 1.554 1.575 0.082  0.007  0.067  37  PHE FFF CZ  
7652  N N   . ARG F 38  ? 1.724 1.517 1.555 0.055  -0.026 -0.012 38  ARG FFF N   
7653  C CA  . ARG F 38  ? 1.697 1.489 1.527 0.055  -0.038 -0.026 38  ARG FFF CA  
7654  C C   . ARG F 38  ? 1.678 1.463 1.514 0.063  -0.049 -0.041 38  ARG FFF C   
7655  O O   . ARG F 38  ? 1.651 1.441 1.479 0.072  -0.046 -0.043 38  ARG FFF O   
7656  C CB  . ARG F 38  ? 1.713 1.514 1.512 0.054  -0.032 -0.032 38  ARG FFF CB  
7657  C CG  . ARG F 38  ? 1.716 1.534 1.495 0.052  -0.027 -0.042 38  ARG FFF CG  
7658  C CD  . ARG F 38  ? 1.720 1.538 1.462 0.041  -0.017 -0.042 38  ARG FFF CD  
7659  N NE  . ARG F 38  ? 1.713 1.562 1.441 0.032  -0.010 -0.052 38  ARG FFF NE  
7660  C CZ  . ARG F 38  ? 1.750 1.601 1.443 0.013  0.002  -0.053 38  ARG FFF CZ  
7661  N NH1 . ARG F 38  ? 1.774 1.585 1.438 0.006  0.007  -0.042 38  ARG FFF NH1 
7662  N NH2 . ARG F 38  ? 1.766 1.660 1.454 0.001  0.010  -0.064 38  ARG FFF NH2 
7663  N N   . GLN F 39  ? 1.698 1.473 1.546 0.061  -0.062 -0.052 39  GLN FFF N   
7664  C CA  . GLN F 39  ? 1.753 1.514 1.596 0.072  -0.075 -0.073 39  GLN FFF CA  
7665  C C   . GLN F 39  ? 1.761 1.542 1.589 0.074  -0.082 -0.091 39  GLN FFF C   
7666  O O   . GLN F 39  ? 1.755 1.540 1.593 0.066  -0.090 -0.092 39  GLN FFF O   
7667  C CB  . GLN F 39  ? 1.809 1.534 1.674 0.063  -0.086 -0.075 39  GLN FFF CB  
7668  C CG  . GLN F 39  ? 1.870 1.568 1.726 0.073  -0.101 -0.100 39  GLN FFF CG  
7669  C CD  . GLN F 39  ? 1.960 1.600 1.821 0.071  -0.105 -0.096 39  GLN FFF CD  
7670  O OE1 . GLN F 39  ? 1.999 1.620 1.881 0.046  -0.104 -0.082 39  GLN FFF OE1 
7671  N NE2 . GLN F 39  ? 2.042 1.653 1.881 0.097  -0.110 -0.108 39  GLN FFF NE2 
7672  N N   . ALA F 40  ? 1.797 1.598 1.602 0.086  -0.079 -0.103 40  ALA FFF N   
7673  C CA  . ALA F 40  ? 1.828 1.649 1.610 0.090  -0.083 -0.120 40  ALA FFF CA  
7674  C C   . ALA F 40  ? 1.859 1.664 1.646 0.100  -0.102 -0.144 40  ALA FFF C   
7675  O O   . ALA F 40  ? 1.945 1.717 1.747 0.104  -0.109 -0.149 40  ALA FFF O   
7676  C CB  . ALA F 40  ? 1.840 1.696 1.597 0.094  -0.070 -0.124 40  ALA FFF CB  
7677  N N   . PRO F 41  ? 1.834 1.654 1.603 0.104  -0.111 -0.161 41  PRO FFF N   
7678  C CA  . PRO F 41  ? 1.868 1.673 1.634 0.115  -0.128 -0.191 41  PRO FFF CA  
7679  C C   . PRO F 41  ? 1.871 1.677 1.624 0.138  -0.125 -0.207 41  PRO FFF C   
7680  O O   . PRO F 41  ? 1.826 1.674 1.563 0.145  -0.110 -0.204 41  PRO FFF O   
7681  C CB  . PRO F 41  ? 1.896 1.731 1.637 0.117  -0.135 -0.202 41  PRO FFF CB  
7682  C CG  . PRO F 41  ? 1.878 1.741 1.595 0.112  -0.115 -0.179 41  PRO FFF CG  
7683  C CD  . PRO F 41  ? 1.830 1.677 1.572 0.099  -0.104 -0.153 41  PRO FFF CD  
7684  N N   . GLY F 42  ? 1.923 1.683 1.683 0.150  -0.137 -0.222 42  GLY FFF N   
7685  C CA  . GLY F 42  ? 1.977 1.731 1.720 0.183  -0.138 -0.242 42  GLY FFF CA  
7686  C C   . GLY F 42  ? 1.990 1.735 1.741 0.193  -0.128 -0.223 42  GLY FFF C   
7687  O O   . GLY F 42  ? 2.007 1.718 1.747 0.223  -0.135 -0.236 42  GLY FFF O   
7688  N N   . LYS F 43  ? 1.980 1.748 1.746 0.172  -0.114 -0.193 43  LYS FFF N   
7689  C CA  . LYS F 43  ? 1.992 1.780 1.763 0.181  -0.101 -0.175 43  LYS FFF CA  
7690  C C   . LYS F 43  ? 2.005 1.742 1.793 0.168  -0.102 -0.150 43  LYS FFF C   
7691  O O   . LYS F 43  ? 1.973 1.684 1.776 0.141  -0.104 -0.139 43  LYS FFF O   
7692  C CB  . LYS F 43  ? 1.984 1.834 1.755 0.161  -0.084 -0.161 43  LYS FFF CB  
7693  C CG  . LYS F 43  ? 2.019 1.939 1.774 0.173  -0.075 -0.177 43  LYS FFF CG  
7694  C CD  . LYS F 43  ? 2.024 1.989 1.773 0.144  -0.057 -0.161 43  LYS FFF CD  
7695  C CE  . LYS F 43  ? 2.050 2.095 1.791 0.149  -0.045 -0.174 43  LYS FFF CE  
7696  N NZ  . LYS F 43  ? 2.053 2.129 1.807 0.157  -0.040 -0.168 43  LYS FFF NZ  
7697  N N   . GLU F 44  ? 2.064 1.795 1.848 0.188  -0.098 -0.139 44  GLU FFF N   
7698  C CA  . GLU F 44  ? 2.119 1.803 1.911 0.179  -0.096 -0.112 44  GLU FFF CA  
7699  C C   . GLU F 44  ? 2.045 1.767 1.852 0.151  -0.081 -0.089 44  GLU FFF C   
7700  O O   . GLU F 44  ? 2.017 1.798 1.820 0.148  -0.073 -0.094 44  GLU FFF O   
7701  C CB  . GLU F 44  ? 2.210 1.879 1.985 0.217  -0.098 -0.108 44  GLU FFF CB  
7702  C CG  . GLU F 44  ? 2.316 1.954 2.068 0.256  -0.112 -0.135 44  GLU FFF CG  
7703  C CD  . GLU F 44  ? 2.418 1.970 2.162 0.248  -0.125 -0.149 44  GLU FFF CD  
7704  O OE1 . GLU F 44  ? 2.494 1.970 2.236 0.233  -0.127 -0.130 44  GLU FFF OE1 
7705  O OE2 . GLU F 44  ? 2.444 2.006 2.182 0.256  -0.133 -0.179 44  GLU FFF OE2 
7706  N N   . ARG F 45  ? 2.035 1.724 1.856 0.129  -0.078 -0.067 45  ARG FFF N   
7707  C CA  . ARG F 45  ? 1.996 1.716 1.828 0.105  -0.065 -0.049 45  ARG FFF CA  
7708  C C   . ARG F 45  ? 1.946 1.696 1.768 0.116  -0.054 -0.037 45  ARG FFF C   
7709  O O   . ARG F 45  ? 2.010 1.738 1.825 0.132  -0.056 -0.026 45  ARG FFF O   
7710  C CB  . ARG F 45  ? 2.027 1.718 1.881 0.081  -0.064 -0.033 45  ARG FFF CB  
7711  C CG  . ARG F 45  ? 2.030 1.710 1.887 0.075  -0.052 -0.005 45  ARG FFF CG  
7712  C CD  . ARG F 45  ? 2.093 1.721 1.936 0.087  -0.056 0.005  45  ARG FFF CD  
7713  N NE  . ARG F 45  ? 2.106 1.753 1.929 0.111  -0.050 0.015  45  ARG FFF NE  
7714  C CZ  . ARG F 45  ? 2.095 1.737 1.911 0.110  -0.040 0.040  45  ARG FFF CZ  
7715  N NH1 . ARG F 45  ? 2.110 1.729 1.939 0.086  -0.032 0.061  45  ARG FFF NH1 
7716  N NH2 . ARG F 45  ? 2.076 1.745 1.873 0.134  -0.038 0.044  45  ARG FFF NH2 
7717  N N   . GLU F 46  ? 1.879 1.675 1.695 0.107  -0.045 -0.040 46  GLU FFF N   
7718  C CA  . GLU F 46  ? 1.862 1.700 1.667 0.111  -0.037 -0.037 46  GLU FFF CA  
7719  C C   . GLU F 46  ? 1.799 1.638 1.603 0.091  -0.025 -0.021 46  GLU FFF C   
7720  O O   . GLU F 46  ? 1.766 1.586 1.577 0.077  -0.023 -0.015 46  GLU FFF O   
7721  C CB  . GLU F 46  ? 1.894 1.783 1.689 0.111  -0.035 -0.058 46  GLU FFF CB  
7722  C CG  . GLU F 46  ? 1.905 1.796 1.692 0.085  -0.028 -0.060 46  GLU FFF CG  
7723  C CD  . GLU F 46  ? 1.924 1.845 1.700 0.083  -0.028 -0.079 46  GLU FFF CD  
7724  O OE1 . GLU F 46  ? 1.898 1.841 1.656 0.061  -0.016 -0.081 46  GLU FFF OE1 
7725  O OE2 . GLU F 46  ? 1.950 1.867 1.730 0.103  -0.038 -0.093 46  GLU FFF OE2 
7726  N N   . PHE F 47  ? 1.752 1.619 1.547 0.094  -0.019 -0.016 47  PHE FFF N   
7727  C CA  . PHE F 47  ? 1.716 1.587 1.502 0.078  -0.007 -0.006 47  PHE FFF CA  
7728  C C   . PHE F 47  ? 1.668 1.545 1.442 0.057  -0.001 -0.017 47  PHE FFF C   
7729  O O   . PHE F 47  ? 1.671 1.572 1.438 0.053  -0.002 -0.032 47  PHE FFF O   
7730  C CB  . PHE F 47  ? 1.730 1.636 1.505 0.087  -0.006 -0.005 47  PHE FFF CB  
7731  C CG  . PHE F 47  ? 1.722 1.634 1.481 0.071  0.005  0.000  47  PHE FFF CG  
7732  C CD1 . PHE F 47  ? 1.711 1.592 1.472 0.069  0.012  0.017  47  PHE FFF CD1 
7733  C CD2 . PHE F 47  ? 1.737 1.688 1.480 0.057  0.009  -0.016 47  PHE FFF CD2 
7734  C CE1 . PHE F 47  ? 1.727 1.612 1.470 0.060  0.022  0.018  47  PHE FFF CE1 
7735  C CE2 . PHE F 47  ? 1.748 1.695 1.471 0.043  0.018  -0.016 47  PHE FFF CE2 
7736  C CZ  . PHE F 47  ? 1.748 1.660 1.470 0.047  0.024  0.000  47  PHE FFF CZ  
7737  N N   . VAL F 48  ? 1.649 1.503 1.414 0.046  0.007  -0.008 48  VAL FFF N   
7738  C CA  . VAL F 48  ? 1.661 1.501 1.401 0.028  0.015  -0.015 48  VAL FFF CA  
7739  C C   . VAL F 48  ? 1.691 1.529 1.406 0.017  0.025  -0.015 48  VAL FFF C   
7740  O O   . VAL F 48  ? 1.751 1.606 1.446 -0.002 0.029  -0.028 48  VAL FFF O   
7741  C CB  . VAL F 48  ? 1.653 1.460 1.396 0.032  0.013  -0.007 48  VAL FFF CB  
7742  C CG1 . VAL F 48  ? 1.672 1.451 1.379 0.021  0.020  -0.010 48  VAL FFF CG1 
7743  C CG2 . VAL F 48  ? 1.645 1.454 1.409 0.040  0.001  -0.012 48  VAL FFF CG2 
7744  N N   . ALA F 49  ? 1.667 1.489 1.385 0.026  0.029  -0.003 49  ALA FFF N   
7745  C CA  . ALA F 49  ? 1.668 1.483 1.360 0.021  0.038  -0.005 49  ALA FFF CA  
7746  C C   . ALA F 49  ? 1.650 1.470 1.357 0.038  0.042  0.011  49  ALA FFF C   
7747  O O   . ALA F 49  ? 1.621 1.438 1.356 0.048  0.039  0.023  49  ALA FFF O   
7748  C CB  . ALA F 49  ? 1.697 1.465 1.355 0.013  0.045  -0.010 49  ALA FFF CB  
7749  N N   . ALA F 50  ? 1.650 1.482 1.337 0.038  0.047  0.009  50  ALA FFF N   
7750  C CA  . ALA F 50  ? 1.631 1.470 1.322 0.053  0.055  0.023  50  ALA FFF CA  
7751  C C   . ALA F 50  ? 1.652 1.475 1.304 0.051  0.064  0.011  50  ALA FFF C   
7752  O O   . ALA F 50  ? 1.655 1.469 1.278 0.033  0.063  -0.008 50  ALA FFF O   
7753  C CB  . ALA F 50  ? 1.622 1.492 1.323 0.062  0.051  0.034  50  ALA FFF CB  
7754  N N   . ILE F 51  ? 1.668 1.491 1.318 0.067  0.074  0.020  51  ILE FFF N   
7755  C CA  . ILE F 51  ? 1.740 1.546 1.350 0.073  0.083  0.008  51  ILE FFF CA  
7756  C C   . ILE F 51  ? 1.767 1.609 1.380 0.090  0.092  0.021  51  ILE FFF C   
7757  O O   . ILE F 51  ? 1.761 1.623 1.408 0.100  0.097  0.042  51  ILE FFF O   
7758  C CB  . ILE F 51  ? 1.790 1.552 1.385 0.084  0.088  0.002  51  ILE FFF CB  
7759  C CG1 . ILE F 51  ? 1.882 1.610 1.425 0.093  0.096  -0.016 51  ILE FFF CG1 
7760  C CG2 . ILE F 51  ? 1.763 1.550 1.398 0.104  0.091  0.021  51  ILE FFF CG2 
7761  C CD1 . ILE F 51  ? 1.944 1.609 1.454 0.105  0.098  -0.025 51  ILE FFF CD1 
7762  N N   . ARG F 52  ? 1.828 1.679 1.405 0.090  0.095  0.009  52  ARG FFF N   
7763  C CA  . ARG F 52  ? 1.870 1.755 1.439 0.108  0.106  0.021  52  ARG FFF CA  
7764  C C   . ARG F 52  ? 1.930 1.802 1.489 0.128  0.120  0.018  52  ARG FFF C   
7765  O O   . ARG F 52  ? 1.971 1.799 1.496 0.130  0.120  -0.005 52  ARG FFF O   
7766  C CB  . ARG F 52  ? 1.876 1.779 1.405 0.104  0.103  0.004  52  ARG FFF CB  
7767  C CG  . ARG F 52  ? 1.854 1.802 1.377 0.122  0.112  0.024  52  ARG FFF CG  
7768  C CD  . ARG F 52  ? 1.860 1.829 1.338 0.122  0.108  0.004  52  ARG FFF CD  
7769  N NE  . ARG F 52  ? 1.820 1.811 1.301 0.108  0.091  -0.005 52  ARG FFF NE  
7770  C CZ  . ARG F 52  ? 1.776 1.798 1.276 0.115  0.083  0.018  52  ARG FFF CZ  
7771  N NH1 . ARG F 52  ? 1.762 1.787 1.279 0.131  0.092  0.054  52  ARG FFF NH1 
7772  N NH2 . ARG F 52  ? 1.767 1.818 1.268 0.107  0.066  0.005  52  ARG FFF NH2 
7773  N N   . TRP F 53  ? 1.955 1.866 1.541 0.142  0.132  0.041  53  TRP FFF N   
7774  C CA  . TRP F 53  ? 1.999 1.922 1.583 0.166  0.147  0.040  53  TRP FFF CA  
7775  C C   . TRP F 53  ? 2.099 2.007 1.626 0.183  0.153  0.015  53  TRP FFF C   
7776  O O   . TRP F 53  ? 2.189 2.062 1.692 0.202  0.156  -0.004 53  TRP FFF O   
7777  C CB  . TRP F 53  ? 1.963 1.947 1.586 0.170  0.161  0.070  53  TRP FFF CB  
7778  C CG  . TRP F 53  ? 1.939 1.951 1.592 0.186  0.170  0.073  53  TRP FFF CG  
7779  C CD1 . TRP F 53  ? 1.969 2.036 1.626 0.206  0.190  0.079  53  TRP FFF CD1 
7780  C CD2 . TRP F 53  ? 1.900 1.899 1.585 0.185  0.160  0.071  53  TRP FFF CD2 
7781  N NE1 . TRP F 53  ? 1.942 2.037 1.636 0.219  0.192  0.079  53  TRP FFF NE1 
7782  C CE2 . TRP F 53  ? 1.911 1.964 1.621 0.206  0.173  0.074  53  TRP FFF CE2 
7783  C CE3 . TRP F 53  ? 1.880 1.834 1.574 0.169  0.142  0.065  53  TRP FFF CE3 
7784  C CZ2 . TRP F 53  ? 1.903 1.966 1.646 0.214  0.165  0.071  53  TRP FFF CZ2 
7785  C CZ3 . TRP F 53  ? 1.869 1.827 1.592 0.176  0.136  0.063  53  TRP FFF CZ3 
7786  C CH2 . TRP F 53  ? 1.888 1.900 1.636 0.199  0.146  0.066  53  TRP FFF CH2 
7787  N N   . SER F 54  ? 2.107 2.037 1.608 0.178  0.154  0.014  54  SER FFF N   
7788  C CA  . SER F 54  ? 2.161 2.086 1.605 0.194  0.161  -0.011 54  SER FFF CA  
7789  C C   . SER F 54  ? 2.186 2.063 1.589 0.173  0.146  -0.043 54  SER FFF C   
7790  O O   . SER F 54  ? 2.249 2.150 1.624 0.166  0.142  -0.052 54  SER FFF O   
7791  C CB  . SER F 54  ? 2.177 2.163 1.614 0.203  0.172  0.007  54  SER FFF CB  
7792  O OG  . SER F 54  ? 2.240 2.224 1.619 0.215  0.175  -0.020 54  SER FFF OG  
7793  N N   . GLY F 55  ? 2.169 1.983 1.565 0.161  0.138  -0.059 55  GLY FFF N   
7794  C CA  . GLY F 55  ? 2.190 1.950 1.540 0.135  0.128  -0.091 55  GLY FFF CA  
7795  C C   . GLY F 55  ? 2.173 1.868 1.525 0.116  0.121  -0.096 55  GLY FFF C   
7796  O O   . GLY F 55  ? 2.230 1.861 1.533 0.096  0.117  -0.124 55  GLY FFF O   
7797  N N   . GLY F 56  ? 2.112 1.823 1.515 0.118  0.118  -0.071 56  GLY FFF N   
7798  C CA  . GLY F 56  ? 2.107 1.764 1.512 0.104  0.112  -0.072 56  GLY FFF CA  
7799  C C   . GLY F 56  ? 2.094 1.742 1.493 0.061  0.102  -0.083 56  GLY FFF C   
7800  O O   . GLY F 56  ? 2.106 1.703 1.494 0.044  0.099  -0.086 56  GLY FFF O   
7801  N N   . SER F 57  ? 2.075 1.777 1.479 0.045  0.097  -0.090 57  SER FFF N   
7802  C CA  . SER F 57  ? 2.057 1.784 1.470 0.007  0.087  -0.099 57  SER FFF CA  
7803  C C   . SER F 57  ? 1.976 1.737 1.446 0.011  0.081  -0.074 57  SER FFF C   
7804  O O   . SER F 57  ? 1.929 1.734 1.433 0.034  0.081  -0.052 57  SER FFF O   
7805  C CB  . SER F 57  ? 2.062 1.851 1.468 0.000  0.081  -0.112 57  SER FFF CB  
7806  O OG  . SER F 57  ? 2.052 1.864 1.450 0.032  0.087  -0.103 57  SER FFF OG  
7807  N N   . ALA F 58  ? 1.965 1.699 1.437 -0.012 0.078  -0.077 58  ALA FFF N   
7808  C CA  . ALA F 58  ? 1.921 1.676 1.439 -0.008 0.072  -0.059 58  ALA FFF CA  
7809  C C   . ALA F 58  ? 1.879 1.693 1.417 -0.029 0.063  -0.066 58  ALA FFF C   
7810  O O   . ALA F 58  ? 1.894 1.722 1.406 -0.057 0.062  -0.089 58  ALA FFF O   
7811  C CB  . ALA F 58  ? 1.964 1.657 1.468 -0.013 0.075  -0.057 58  ALA FFF CB  
7812  N N   . TYR F 59  ? 1.813 1.662 1.393 -0.016 0.057  -0.050 59  TYR FFF N   
7813  C CA  . TYR F 59  ? 1.797 1.701 1.399 -0.028 0.048  -0.057 59  TYR FFF CA  
7814  C C   . TYR F 59  ? 1.822 1.709 1.442 -0.031 0.046  -0.052 59  TYR FFF C   
7815  O O   . TYR F 59  ? 1.797 1.695 1.448 -0.009 0.040  -0.037 59  TYR FFF O   
7816  C CB  . TYR F 59  ? 1.737 1.697 1.364 -0.001 0.039  -0.046 59  TYR FFF CB  
7817  C CG  . TYR F 59  ? 1.695 1.722 1.338 -0.005 0.029  -0.058 59  TYR FFF CG  
7818  C CD1 . TYR F 59  ? 1.694 1.754 1.325 -0.040 0.029  -0.083 59  TYR FFF CD1 
7819  C CD2 . TYR F 59  ? 1.649 1.705 1.318 0.025  0.019  -0.044 59  TYR FFF CD2 
7820  C CE1 . TYR F 59  ? 1.669 1.808 1.319 -0.041 0.020  -0.096 59  TYR FFF CE1 
7821  C CE2 . TYR F 59  ? 1.622 1.745 1.305 0.031  0.009  -0.057 59  TYR FFF CE2 
7822  C CZ  . TYR F 59  ? 1.645 1.818 1.321 -0.001 0.010  -0.083 59  TYR FFF CZ  
7823  O OH  . TYR F 59  ? 1.682 1.937 1.376 0.007  0.000  -0.097 59  TYR FFF OH  
7824  N N   . TYR F 60  ? 1.894 1.751 1.488 -0.061 0.052  -0.064 60  TYR FFF N   
7825  C CA  . TYR F 60  ? 1.893 1.737 1.492 -0.070 0.052  -0.062 60  TYR FFF CA  
7826  C C   . TYR F 60  ? 1.832 1.752 1.464 -0.068 0.044  -0.068 60  TYR FFF C   
7827  O O   . TYR F 60  ? 1.805 1.786 1.440 -0.080 0.042  -0.083 60  TYR FFF O   
7828  C CB  . TYR F 60  ? 2.009 1.799 1.561 -0.106 0.062  -0.072 60  TYR FFF CB  
7829  C CG  . TYR F 60  ? 2.087 1.795 1.613 -0.089 0.066  -0.060 60  TYR FFF CG  
7830  C CD1 . TYR F 60  ? 2.110 1.786 1.620 -0.070 0.069  -0.058 60  TYR FFF CD1 
7831  C CD2 . TYR F 60  ? 2.173 1.846 1.693 -0.084 0.066  -0.050 60  TYR FFF CD2 
7832  C CE1 . TYR F 60  ? 2.193 1.806 1.683 -0.046 0.072  -0.048 60  TYR FFF CE1 
7833  C CE2 . TYR F 60  ? 2.251 1.860 1.749 -0.060 0.068  -0.038 60  TYR FFF CE2 
7834  C CZ  . TYR F 60  ? 2.277 1.858 1.762 -0.040 0.070  -0.038 60  TYR FFF CZ  
7835  O OH  . TYR F 60  ? 2.374 1.905 1.841 -0.011 0.071  -0.028 60  TYR FFF OH  
7836  N N   . ALA F 61  ? 1.782 1.703 1.440 -0.049 0.039  -0.058 61  ALA FFF N   
7837  C CA  . ALA F 61  ? 1.760 1.742 1.445 -0.039 0.031  -0.066 61  ALA FFF CA  
7838  C C   . ALA F 61  ? 1.807 1.814 1.477 -0.073 0.038  -0.081 61  ALA FFF C   
7839  O O   . ALA F 61  ? 1.857 1.813 1.494 -0.100 0.048  -0.080 61  ALA FFF O   
7840  C CB  . ALA F 61  ? 1.717 1.677 1.425 -0.010 0.023  -0.054 61  ALA FFF CB  
7841  N N   . ASP F 62  ? 1.830 1.915 1.521 -0.068 0.034  -0.094 62  ASP FFF N   
7842  C CA  . ASP F 62  ? 1.874 2.019 1.556 -0.107 0.043  -0.113 62  ASP FFF CA  
7843  C C   . ASP F 62  ? 1.853 1.962 1.514 -0.127 0.053  -0.109 62  ASP FFF C   
7844  O O   . ASP F 62  ? 1.889 2.003 1.524 -0.174 0.066  -0.117 62  ASP FFF O   
7845  C CB  . ASP F 62  ? 1.920 2.172 1.634 -0.086 0.034  -0.129 62  ASP FFF CB  
7846  C CG  . ASP F 62  ? 1.968 2.239 1.699 -0.047 0.021  -0.124 62  ASP FFF CG  
7847  O OD1 . ASP F 62  ? 2.007 2.218 1.743 -0.013 0.013  -0.106 62  ASP FFF OD1 
7848  O OD2 . ASP F 62  ? 1.994 2.336 1.729 -0.055 0.017  -0.138 62  ASP FFF OD2 
7849  N N   . SER F 63  ? 1.811 1.883 1.480 -0.097 0.046  -0.098 63  SER FFF N   
7850  C CA  . SER F 63  ? 1.830 1.877 1.480 -0.107 0.053  -0.095 63  SER FFF CA  
7851  C C   . SER F 63  ? 1.867 1.816 1.476 -0.121 0.059  -0.078 63  SER FFF C   
7852  O O   . SER F 63  ? 1.911 1.833 1.492 -0.134 0.066  -0.073 63  SER FFF O   
7853  C CB  . SER F 63  ? 1.797 1.855 1.472 -0.067 0.041  -0.095 63  SER FFF CB  
7854  O OG  . SER F 63  ? 1.758 1.783 1.455 -0.034 0.027  -0.086 63  SER FFF OG  
7855  N N   . VAL F 64  ? 1.858 1.759 1.461 -0.116 0.057  -0.071 64  VAL FFF N   
7856  C CA  . VAL F 64  ? 1.902 1.711 1.466 -0.119 0.062  -0.057 64  VAL FFF CA  
7857  C C   . VAL F 64  ? 1.928 1.703 1.454 -0.153 0.073  -0.062 64  VAL FFF C   
7858  O O   . VAL F 64  ? 1.960 1.650 1.437 -0.161 0.080  -0.054 64  VAL FFF O   
7859  C CB  . VAL F 64  ? 1.886 1.664 1.472 -0.078 0.051  -0.044 64  VAL FFF CB  
7860  C CG1 . VAL F 64  ? 1.855 1.657 1.474 -0.051 0.039  -0.042 64  VAL FFF CG1 
7861  C CG2 . VAL F 64  ? 1.877 1.677 1.487 -0.067 0.048  -0.046 64  VAL FFF CG2 
7862  N N   . LYS F 65  ? 1.895 1.731 1.437 -0.170 0.074  -0.078 65  LYS FFF N   
7863  C CA  . LYS F 65  ? 1.944 1.758 1.451 -0.209 0.083  -0.090 65  LYS FFF CA  
7864  C C   . LYS F 65  ? 2.019 1.769 1.470 -0.252 0.097  -0.087 65  LYS FFF C   
7865  O O   . LYS F 65  ? 2.025 1.821 1.479 -0.276 0.104  -0.091 65  LYS FFF O   
7866  C CB  . LYS F 65  ? 1.938 1.855 1.475 -0.226 0.080  -0.110 65  LYS FFF CB  
7867  C CG  . LYS F 65  ? 1.973 1.889 1.501 -0.232 0.077  -0.122 65  LYS FFF CG  
7868  C CD  . LYS F 65  ? 1.960 1.984 1.533 -0.214 0.065  -0.134 65  LYS FFF CD  
7869  C CE  . LYS F 65  ? 1.985 2.002 1.553 -0.197 0.059  -0.136 65  LYS FFF CE  
7870  N NZ  . LYS F 65  ? 1.923 2.008 1.532 -0.151 0.045  -0.130 65  LYS FFF NZ  
7871  N N   . GLY F 66  ? 2.096 1.738 1.493 -0.255 0.103  -0.080 66  GLY FFF N   
7872  C CA  . GLY F 66  ? 2.187 1.741 1.514 -0.297 0.118  -0.076 66  GLY FFF CA  
7873  C C   . GLY F 66  ? 2.203 1.674 1.496 -0.265 0.117  -0.052 66  GLY FFF C   
7874  O O   . GLY F 66  ? 2.305 1.688 1.530 -0.293 0.130  -0.043 66  GLY FFF O   
7875  N N   . ARG F 67  ? 2.128 1.625 1.464 -0.210 0.103  -0.042 67  ARG FFF N   
7876  C CA  . ARG F 67  ? 2.169 1.611 1.483 -0.175 0.099  -0.021 67  ARG FFF CA  
7877  C C   . ARG F 67  ? 2.159 1.576 1.490 -0.123 0.087  -0.015 67  ARG FFF C   
7878  O O   . ARG F 67  ? 2.238 1.566 1.516 -0.104 0.089  -0.005 67  ARG FFF O   
7879  C CB  . ARG F 67  ? 2.122 1.636 1.473 -0.167 0.093  -0.018 67  ARG FFF CB  
7880  C CG  . ARG F 67  ? 2.136 1.694 1.476 -0.217 0.107  -0.026 67  ARG FFF CG  
7881  C CD  . ARG F 67  ? 2.085 1.703 1.446 -0.208 0.104  -0.024 67  ARG FFF CD  
7882  N NE  . ARG F 67  ? 1.979 1.669 1.408 -0.166 0.087  -0.032 67  ARG FFF NE  
7883  C CZ  . ARG F 67  ? 1.937 1.619 1.382 -0.125 0.073  -0.024 67  ARG FFF CZ  
7884  N NH1 . ARG F 67  ? 1.995 1.611 1.393 -0.114 0.073  -0.008 67  ARG FFF NH1 
7885  N NH2 . ARG F 67  ? 1.847 1.586 1.350 -0.096 0.059  -0.033 67  ARG FFF NH2 
7886  N N   . PHE F 68  ? 2.159 1.730 1.450 -0.119 0.114  -0.062 68  PHE FFF N   
7887  C CA  . PHE F 68  ? 2.158 1.714 1.482 -0.060 0.103  -0.060 68  PHE FFF CA  
7888  C C   . PHE F 68  ? 2.242 1.744 1.525 -0.062 0.102  -0.061 68  PHE FFF C   
7889  O O   . PHE F 68  ? 2.324 1.810 1.563 -0.110 0.108  -0.064 68  PHE FFF O   
7890  C CB  . PHE F 68  ? 2.052 1.714 1.480 -0.033 0.101  -0.061 68  PHE FFF CB  
7891  C CG  . PHE F 68  ? 2.036 1.728 1.491 -0.020 0.099  -0.061 68  PHE FFF CG  
7892  C CD1 . PHE F 68  ? 2.113 1.760 1.509 -0.041 0.102  -0.060 68  PHE FFF CD1 
7893  C CD2 . PHE F 68  ? 1.944 1.704 1.475 0.010  0.092  -0.062 68  PHE FFF CD2 
7894  C CE1 . PHE F 68  ? 2.092 1.766 1.509 -0.028 0.100  -0.060 68  PHE FFF CE1 
7895  C CE2 . PHE F 68  ? 1.915 1.694 1.462 0.022  0.088  -0.064 68  PHE FFF CE2 
7896  C CZ  . PHE F 68  ? 1.997 1.737 1.490 0.005  0.092  -0.063 68  PHE FFF CZ  
7897  N N   . THR F 69  ? 2.258 1.733 1.551 -0.012 0.095  -0.059 69  THR FFF N   
7898  C CA  . THR F 69  ? 2.288 1.735 1.561 0.000  0.095  -0.062 69  THR FFF CA  
7899  C C   . THR F 69  ? 2.190 1.689 1.535 0.053  0.092  -0.061 69  THR FFF C   
7900  O O   . THR F 69  ? 2.165 1.634 1.500 0.095  0.085  -0.059 69  THR FFF O   
7901  C CB  . THR F 69  ? 2.439 1.753 1.594 -0.001 0.092  -0.063 69  THR FFF CB  
7902  O OG1 . THR F 69  ? 2.506 1.763 1.585 -0.058 0.094  -0.063 69  THR FFF OG1 
7903  C CG2 . THR F 69  ? 2.482 1.769 1.610 0.003  0.093  -0.068 69  THR FFF CG2 
7904  N N   . ILE F 70  ? 2.103 1.679 1.513 0.049  0.096  -0.061 70  ILE FFF N   
7905  C CA  . ILE F 70  ? 2.013 1.638 1.482 0.087  0.096  -0.059 70  ILE FFF CA  
7906  C C   . ILE F 70  ? 2.065 1.637 1.481 0.100  0.100  -0.063 70  ILE FFF C   
7907  O O   . ILE F 70  ? 2.093 1.627 1.459 0.069  0.103  -0.067 70  ILE FFF O   
7908  C CB  . ILE F 70  ? 1.906 1.620 1.451 0.077  0.097  -0.057 70  ILE FFF CB  
7909  C CG1 . ILE F 70  ? 1.847 1.605 1.448 0.109  0.097  -0.052 70  ILE FFF CG1 
7910  C CG2 . ILE F 70  ? 1.927 1.651 1.458 0.047  0.101  -0.060 70  ILE FFF CG2 
7911  C CD1 . ILE F 70  ? 1.788 1.612 1.448 0.102  0.095  -0.048 70  ILE FFF CD1 
7912  N N   . SER F 71  ? 2.073 1.646 1.500 0.146  0.100  -0.062 71  SER FFF N   
7913  C CA  . SER F 71  ? 2.166 1.694 1.544 0.174  0.104  -0.068 71  SER FFF CA  
7914  C C   . SER F 71  ? 2.149 1.749 1.591 0.216  0.108  -0.066 71  SER FFF C   
7915  O O   . SER F 71  ? 2.099 1.752 1.598 0.225  0.103  -0.061 71  SER FFF O   
7916  C CB  . SER F 71  ? 2.295 1.712 1.573 0.190  0.097  -0.073 71  SER FFF CB  
7917  O OG  . SER F 71  ? 2.307 1.725 1.596 0.221  0.089  -0.071 71  SER FFF OG  
7918  N N   . ARG F 72  ? 2.204 1.808 1.634 0.239  0.117  -0.070 72  ARG FFF N   
7919  C CA  . ARG F 72  ? 2.181 1.868 1.673 0.273  0.124  -0.068 72  ARG FFF CA  
7920  C C   . ARG F 72  ? 2.247 1.898 1.682 0.321  0.130  -0.078 72  ARG FFF C   
7921  O O   . ARG F 72  ? 2.319 1.881 1.671 0.319  0.130  -0.085 72  ARG FFF O   
7922  C CB  . ARG F 72  ? 2.148 1.905 1.699 0.245  0.133  -0.060 72  ARG FFF CB  
7923  C CG  . ARG F 72  ? 2.215 1.935 1.721 0.225  0.140  -0.063 72  ARG FFF CG  
7924  C CD  . ARG F 72  ? 2.284 2.023 1.780 0.255  0.154  -0.067 72  ARG FFF CD  
7925  N NE  . ARG F 72  ? 2.339 2.036 1.784 0.238  0.158  -0.071 72  ARG FFF NE  
7926  C CZ  . ARG F 72  ? 2.432 2.037 1.789 0.241  0.155  -0.081 72  ARG FFF CZ  
7927  N NH1 . ARG F 72  ? 2.524 2.059 1.826 0.261  0.147  -0.088 72  ARG FFF NH1 
7928  N NH2 . ARG F 72  ? 2.452 2.028 1.769 0.222  0.158  -0.085 72  ARG FFF NH2 
7929  N N   . ASP F 73  ? 2.247 1.966 1.724 0.364  0.133  -0.080 73  ASP FFF N   
7930  C CA  . ASP F 73  ? 2.321 2.038 1.761 0.423  0.140  -0.092 73  ASP FFF CA  
7931  C C   . ASP F 73  ? 2.243 2.078 1.758 0.424  0.158  -0.088 73  ASP FFF C   
7932  O O   . ASP F 73  ? 2.174 2.108 1.767 0.427  0.159  -0.083 73  ASP FFF O   
7933  C CB  . ASP F 73  ? 2.393 2.100 1.815 0.476  0.127  -0.099 73  ASP FFF CB  
7934  C CG  . ASP F 73  ? 2.480 2.189 1.861 0.548  0.132  -0.114 73  ASP FFF CG  
7935  O OD1 . ASP F 73  ? 2.499 2.214 1.862 0.554  0.148  -0.119 73  ASP FFF OD1 
7936  O OD2 . ASP F 73  ? 2.552 2.257 1.915 0.601  0.119  -0.122 73  ASP FFF OD2 
7937  N N   . LYS F 74  ? 2.247 2.069 1.734 0.417  0.173  -0.090 74  LYS FFF N   
7938  C CA  . LYS F 74  ? 2.205 2.124 1.750 0.404  0.192  -0.084 74  LYS FFF CA  
7939  C C   . LYS F 74  ? 2.197 2.216 1.783 0.452  0.204  -0.090 74  LYS FFF C   
7940  O O   . LYS F 74  ? 2.149 2.276 1.811 0.430  0.215  -0.081 74  LYS FFF O   
7941  C CB  . LYS F 74  ? 2.267 2.135 1.755 0.394  0.203  -0.087 74  LYS FFF CB  
7942  C CG  . LYS F 74  ? 2.272 2.083 1.744 0.338  0.195  -0.079 74  LYS FFF CG  
7943  C CD  . LYS F 74  ? 2.349 2.123 1.770 0.327  0.204  -0.082 74  LYS FFF CD  
7944  C CE  . LYS F 74  ? 2.331 2.187 1.802 0.309  0.220  -0.072 74  LYS FFF CE  
7945  N NZ  . LYS F 74  ? 2.386 2.199 1.801 0.299  0.226  -0.075 74  LYS FFF NZ  
7946  N N   . ALA F 75  ? 2.261 2.246 1.793 0.515  0.201  -0.106 75  ALA FFF N   
7947  C CA  . ALA F 75  ? 2.277 2.363 1.839 0.574  0.210  -0.117 75  ALA FFF CA  
7948  C C   . ALA F 75  ? 2.220 2.401 1.865 0.572  0.198  -0.112 75  ALA FFF C   
7949  O O   . ALA F 75  ? 2.188 2.503 1.898 0.592  0.210  -0.115 75  ALA FFF O   
7950  C CB  . ALA F 75  ? 2.387 2.388 1.852 0.648  0.204  -0.137 75  ALA FFF CB  
7951  N N   . LYS F 76  ? 2.223 2.341 1.865 0.546  0.176  -0.105 76  LYS FFF N   
7952  C CA  . LYS F 76  ? 2.185 2.372 1.894 0.541  0.160  -0.101 76  LYS FFF CA  
7953  C C   . LYS F 76  ? 2.073 2.307 1.854 0.467  0.161  -0.083 76  LYS FFF C   
7954  O O   . LYS F 76  ? 2.024 2.319 1.862 0.454  0.149  -0.078 76  LYS FFF O   
7955  C CB  . LYS F 76  ? 2.259 2.339 1.907 0.563  0.135  -0.105 76  LYS FFF CB  
7956  C CG  . LYS F 76  ? 2.356 2.412 1.948 0.647  0.125  -0.123 76  LYS FFF CG  
7957  C CD  . LYS F 76  ? 2.401 2.359 1.937 0.664  0.097  -0.124 76  LYS FFF CD  
7958  C CE  . LYS F 76  ? 2.484 2.448 1.983 0.752  0.082  -0.140 76  LYS FFF CE  
7959  N NZ  . LYS F 76  ? 2.581 2.530 2.021 0.814  0.094  -0.156 76  LYS FFF NZ  
7960  N N   . ASN F 77  ? 2.032 2.234 1.803 0.422  0.174  -0.074 77  ASN FFF N   
7961  C CA  . ASN F 77  ? 1.959 2.186 1.781 0.358  0.173  -0.057 77  ASN FFF CA  
7962  C C   . ASN F 77  ? 1.930 2.116 1.759 0.339  0.150  -0.053 77  ASN FFF C   
7963  O O   . ASN F 77  ? 1.867 2.103 1.752 0.306  0.143  -0.044 77  ASN FFF O   
7964  C CB  . ASN F 77  ? 1.930 2.282 1.824 0.338  0.185  -0.050 77  ASN FFF CB  
7965  C CG  . ASN F 77  ? 1.986 2.378 1.870 0.344  0.211  -0.051 77  ASN FFF CG  
7966  O OD1 . ASN F 77  ? 2.042 2.363 1.876 0.336  0.219  -0.050 77  ASN FFF OD1 
7967  N ND2 . ASN F 77  ? 2.022 2.535 1.953 0.357  0.226  -0.054 77  ASN FFF ND2 
7968  N N   . THR F 78  ? 1.977 2.068 1.746 0.359  0.138  -0.060 78  THR FFF N   
7969  C CA  . THR F 78  ? 1.979 2.021 1.740 0.347  0.118  -0.058 78  THR FFF CA  
7970  C C   . THR F 78  ? 1.976 1.927 1.687 0.315  0.117  -0.056 78  THR FFF C   
7971  O O   . THR F 78  ? 2.025 1.919 1.679 0.322  0.125  -0.061 78  THR FFF O   
7972  C CB  . THR F 78  ? 2.066 2.078 1.789 0.399  0.105  -0.069 78  THR FFF CB  
7973  O OG1 . THR F 78  ? 2.065 2.175 1.830 0.438  0.109  -0.075 78  THR FFF OG1 
7974  C CG2 . THR F 78  ? 2.078 2.065 1.806 0.388  0.085  -0.066 78  THR FFF CG2 
7975  N N   . VAL F 79  ? 1.907 1.849 1.639 0.281  0.107  -0.049 79  VAL FFF N   
7976  C CA  . VAL F 79  ? 1.896 1.763 1.584 0.253  0.103  -0.049 79  VAL FFF CA  
7977  C C   . VAL F 79  ? 1.890 1.719 1.558 0.258  0.088  -0.051 79  VAL FFF C   
7978  O O   . VAL F 79  ? 1.842 1.718 1.554 0.267  0.079  -0.049 79  VAL FFF O   
7979  C CB  . VAL F 79  ? 1.851 1.746 1.575 0.213  0.105  -0.041 79  VAL FFF CB  
7980  C CG1 . VAL F 79  ? 1.825 1.773 1.608 0.201  0.096  -0.034 79  VAL FFF CG1 
7981  C CG2 . VAL F 79  ? 1.862 1.704 1.547 0.186  0.103  -0.043 79  VAL FFF CG2 
7982  N N   . TYR F 80  ? 1.943 1.689 1.541 0.250  0.086  -0.054 80  TYR FFF N   
7983  C CA  . TYR F 80  ? 1.983 1.672 1.540 0.253  0.074  -0.056 80  TYR FFF CA  
7984  C C   . TYR F 80  ? 1.972 1.639 1.517 0.206  0.075  -0.053 80  TYR FFF C   
7985  O O   . TYR F 80  ? 2.008 1.666 1.538 0.179  0.084  -0.054 80  TYR FFF O   
7986  C CB  . TYR F 80  ? 2.074 1.672 1.540 0.283  0.071  -0.063 80  TYR FFF CB  
7987  C CG  . TYR F 80  ? 2.104 1.727 1.574 0.339  0.070  -0.069 80  TYR FFF CG  
7988  C CD1 . TYR F 80  ? 2.105 1.776 1.610 0.375  0.058  -0.070 80  TYR FFF CD1 
7989  C CD2 . TYR F 80  ? 2.163 1.767 1.600 0.357  0.081  -0.074 80  TYR FFF CD2 
7990  C CE1 . TYR F 80  ? 2.139 1.853 1.654 0.430  0.058  -0.077 80  TYR FFF CE1 
7991  C CE2 . TYR F 80  ? 2.200 1.838 1.640 0.414  0.082  -0.082 80  TYR FFF CE2 
7992  C CZ  . TYR F 80  ? 2.185 1.884 1.667 0.451  0.071  -0.084 80  TYR FFF CZ  
7993  O OH  . TYR F 80  ? 2.182 1.933 1.674 0.509  0.072  -0.093 80  TYR FFF OH  
7994  N N   . LEU F 81  ? 1.926 1.594 1.479 0.198  0.067  -0.051 81  LEU FFF N   
7995  C CA  . LEU F 81  ? 1.909 1.552 1.436 0.159  0.069  -0.051 81  LEU FFF CA  
7996  C C   . LEU F 81  ? 2.006 1.566 1.455 0.163  0.062  -0.052 81  LEU FFF C   
7997  O O   . LEU F 81  ? 1.998 1.560 1.456 0.186  0.051  -0.051 81  LEU FFF O   
7998  C CB  . LEU F 81  ? 1.807 1.518 1.401 0.148  0.065  -0.049 81  LEU FFF CB  
7999  C CG  . LEU F 81  ? 1.814 1.529 1.396 0.112  0.070  -0.051 81  LEU FFF CG  
8000  C CD1 . LEU F 81  ? 1.816 1.547 1.396 0.086  0.080  -0.053 81  LEU FFF CD1 
8001  C CD2 . LEU F 81  ? 1.760 1.528 1.394 0.112  0.064  -0.051 81  LEU FFF CD2 
8002  N N   . GLN F 82  ? 2.109 1.593 1.479 0.140  0.067  -0.054 82  GLN FFF N   
8003  C CA  . GLN F 82  ? 2.210 1.597 1.485 0.129  0.063  -0.053 82  GLN FFF CA  
8004  C C   . GLN F 82  ? 2.156 1.570 1.440 0.082  0.070  -0.051 82  GLN FFF C   
8005  O O   . GLN F 82  ? 2.096 1.553 1.402 0.043  0.081  -0.053 82  GLN FFF O   
8006  C CB  . GLN F 82  ? 2.362 1.645 1.536 0.119  0.065  -0.055 82  GLN FFF CB  
8007  C CG  . GLN F 82  ? 2.505 1.663 1.563 0.120  0.056  -0.053 82  GLN FFF CG  
8008  C CD  . GLN F 82  ? 2.529 1.675 1.589 0.184  0.040  -0.054 82  GLN FFF CD  
8009  O OE1 . GLN F 82  ? 2.537 1.700 1.618 0.235  0.035  -0.058 82  GLN FFF OE1 
8010  N NE2 . GLN F 82  ? 2.561 1.688 1.603 0.181  0.032  -0.050 82  GLN FFF NE2 
8011  N N   . MET F 83  ? 2.164 1.564 1.435 0.087  0.063  -0.049 83  MET FFF N   
8012  C CA  . MET F 83  ? 2.154 1.592 1.437 0.049  0.071  -0.048 83  MET FFF CA  
8013  C C   . MET F 83  ? 2.263 1.603 1.439 0.022  0.072  -0.045 83  MET FFF C   
8014  O O   . MET F 83  ? 2.317 1.620 1.465 0.043  0.062  -0.042 83  MET FFF O   
8015  C CB  . MET F 83  ? 2.089 1.594 1.445 0.076  0.062  -0.049 83  MET FFF CB  
8016  C CG  . MET F 83  ? 2.012 1.599 1.460 0.097  0.060  -0.050 83  MET FFF CG  
8017  S SD  . MET F 83  ? 1.991 1.631 1.505 0.128  0.045  -0.050 83  MET FFF SD  
8018  C CE  . MET F 83  ? 1.989 1.667 1.513 0.100  0.053  -0.054 83  MET FFF CE  
8019  N N   . ASN F 84  ? 2.329 1.624 1.441 -0.027 0.083  -0.045 84  ASN FFF N   
8020  C CA  . ASN F 84  ? 2.459 1.654 1.455 -0.070 0.088  -0.040 84  ASN FFF CA  
8021  C C   . ASN F 84  ? 2.403 1.673 1.428 -0.112 0.102  -0.041 84  ASN FFF C   
8022  O O   . ASN F 84  ? 2.254 1.645 1.378 -0.111 0.109  -0.047 84  ASN FFF O   
8023  C CB  . ASN F 84  ? 2.595 1.712 1.507 -0.114 0.093  -0.041 84  ASN FFF CB  
8024  C CG  . ASN F 84  ? 2.649 1.710 1.542 -0.070 0.082  -0.043 84  ASN FFF CG  
8025  O OD1 . ASN F 84  ? 2.719 1.724 1.588 -0.011 0.067  -0.042 84  ASN FFF OD1 
8026  N ND2 . ASN F 84  ? 2.629 1.709 1.531 -0.096 0.089  -0.048 84  ASN FFF ND2 
8027  N N   . SER F 85  ? 2.514 1.710 1.448 -0.143 0.106  -0.036 85  SER FFF N   
8028  C CA  . SER F 85  ? 2.529 1.784 1.464 -0.193 0.124  -0.036 85  SER FFF CA  
8029  C C   . SER F 85  ? 2.418 1.793 1.461 -0.158 0.124  -0.042 85  SER FFF C   
8030  O O   . SER F 85  ? 2.388 1.869 1.482 -0.188 0.140  -0.049 85  SER FFF O   
8031  C CB  . SER F 85  ? 2.532 1.844 1.468 -0.262 0.143  -0.040 85  SER FFF CB  
8032  O OG  . SER F 85  ? 2.666 1.861 1.495 -0.301 0.141  -0.035 85  SER FFF OG  
8033  N N   . LEU F 86  ? 2.375 1.736 1.449 -0.096 0.105  -0.041 86  LEU FFF N   
8034  C CA  . LEU F 86  ? 2.271 1.734 1.446 -0.061 0.101  -0.048 86  LEU FFF CA  
8035  C C   . LEU F 86  ? 2.279 1.796 1.449 -0.093 0.118  -0.052 86  LEU FFF C   
8036  O O   . LEU F 86  ? 2.350 1.800 1.434 -0.118 0.123  -0.046 86  LEU FFF O   
8037  C CB  . LEU F 86  ? 2.248 1.678 1.436 -0.004 0.078  -0.046 86  LEU FFF CB  
8038  C CG  . LEU F 86  ? 2.245 1.624 1.428 0.034  0.061  -0.043 86  LEU FFF CG  
8039  C CD1 . LEU F 86  ? 2.365 1.614 1.432 0.036  0.053  -0.036 86  LEU FFF CD1 
8040  C CD2 . LEU F 86  ? 2.159 1.584 1.417 0.086  0.043  -0.045 86  LEU FFF CD2 
8041  N N   . LYS F 87  ? 2.213 1.847 1.468 -0.090 0.126  -0.062 87  LYS FFF N   
8042  C CA  . LYS F 87  ? 2.231 1.943 1.502 -0.102 0.140  -0.070 87  LYS FFF CA  
8043  C C   . LYS F 87  ? 2.193 1.913 1.502 -0.048 0.124  -0.073 87  LYS FFF C   
8044  O O   . LYS F 87  ? 2.131 1.820 1.469 -0.010 0.103  -0.070 87  LYS FFF O   
8045  C CB  . LYS F 87  ? 2.203 2.036 1.541 -0.118 0.154  -0.081 87  LYS FFF CB  
8046  C CG  . LYS F 87  ? 2.269 2.124 1.569 -0.184 0.175  -0.080 87  LYS FFF CG  
8047  C CD  . LYS F 87  ? 2.240 2.242 1.607 -0.196 0.189  -0.095 87  LYS FFF CD  
8048  C CE  . LYS F 87  ? 2.267 2.312 1.640 -0.243 0.197  -0.097 87  LYS FFF CE  
8049  N NZ  . LYS F 87  ? 2.207 2.381 1.671 -0.217 0.195  -0.110 87  LYS FFF NZ  
8050  N N   . TYR F 88  ? 2.216 1.979 1.522 -0.047 0.133  -0.081 88  TYR FFF N   
8051  C CA  . TYR F 88  ? 2.176 1.948 1.511 0.000  0.117  -0.087 88  TYR FFF CA  
8052  C C   . TYR F 88  ? 2.073 1.916 1.493 0.033  0.108  -0.096 88  TYR FFF C   
8053  O O   . TYR F 88  ? 2.029 1.855 1.474 0.071  0.087  -0.097 88  TYR FFF O   
8054  C CB  . TYR F 88  ? 2.228 2.027 1.527 -0.009 0.132  -0.094 88  TYR FFF CB  
8055  C CG  . TYR F 88  ? 2.319 2.023 1.529 -0.022 0.130  -0.085 88  TYR FFF CG  
8056  C CD1 . TYR F 88  ? 2.339 1.956 1.527 0.009  0.103  -0.077 88  TYR FFF CD1 
8057  C CD2 . TYR F 88  ? 2.386 2.093 1.530 -0.065 0.155  -0.085 88  TYR FFF CD2 
8058  C CE1 . TYR F 88  ? 2.436 1.962 1.536 0.003  0.098  -0.069 88  TYR FFF CE1 
8059  C CE2 . TYR F 88  ? 2.468 2.079 1.520 -0.077 0.152  -0.075 88  TYR FFF CE2 
8060  C CZ  . TYR F 88  ? 2.499 2.014 1.526 -0.040 0.122  -0.067 88  TYR FFF CZ  
8061  O OH  . TYR F 88  ? 2.587 2.003 1.515 -0.047 0.117  -0.058 88  TYR FFF OH  
8062  N N   . GLU F 89  ? 2.039 1.956 1.497 0.017  0.121  -0.101 89  GLU FFF N   
8063  C CA  . GLU F 89  ? 1.959 1.940 1.488 0.047  0.113  -0.109 89  GLU FFF CA  
8064  C C   . GLU F 89  ? 1.849 1.783 1.405 0.063  0.094  -0.099 89  GLU FFF C   
8065  O O   . GLU F 89  ? 1.731 1.694 1.333 0.090  0.083  -0.103 89  GLU FFF O   
8066  C CB  . GLU F 89  ? 2.003 2.076 1.558 0.022  0.131  -0.116 89  GLU FFF CB  
8067  C CG  . GLU F 89  ? 2.090 2.258 1.660 0.033  0.144  -0.133 89  GLU FFF CG  
8068  C CD  . GLU F 89  ? 2.210 2.370 1.729 0.020  0.158  -0.136 89  GLU FFF CD  
8069  O OE1 . GLU F 89  ? 2.231 2.447 1.759 0.050  0.161  -0.150 89  GLU FFF OE1 
8070  O OE2 . GLU F 89  ? 2.335 2.427 1.797 -0.018 0.164  -0.124 89  GLU FFF OE2 
8071  N N   . ASP F 90  ? 1.884 1.747 1.403 0.048  0.091  -0.088 90  ASP FFF N   
8072  C CA  . ASP F 90  ? 1.894 1.719 1.434 0.063  0.077  -0.080 90  ASP FFF CA  
8073  C C   . ASP F 90  ? 1.892 1.687 1.447 0.098  0.055  -0.078 90  ASP FFF C   
8074  O O   . ASP F 90  ? 1.867 1.652 1.451 0.112  0.043  -0.072 90  ASP FFF O   
8075  C CB  . ASP F 90  ? 1.967 1.725 1.454 0.042  0.081  -0.071 90  ASP FFF CB  
8076  C CG  . ASP F 90  ? 2.002 1.780 1.469 0.000  0.099  -0.072 90  ASP FFF CG  
8077  O OD1 . ASP F 90  ? 1.961 1.821 1.471 -0.008 0.108  -0.080 90  ASP FFF OD1 
8078  O OD2 . ASP F 90  ? 2.095 1.804 1.499 -0.023 0.103  -0.065 90  ASP FFF OD2 
8079  N N   . THR F 91  ? 1.923 1.708 1.458 0.108  0.049  -0.082 91  THR FFF N   
8080  C CA  . THR F 91  ? 1.934 1.695 1.482 0.136  0.026  -0.082 91  THR FFF CA  
8081  C C   . THR F 91  ? 1.884 1.683 1.487 0.152  0.016  -0.086 91  THR FFF C   
8082  O O   . THR F 91  ? 1.920 1.752 1.529 0.159  0.021  -0.095 91  THR FFF O   
8083  C CB  . THR F 91  ? 2.004 1.747 1.513 0.143  0.022  -0.088 91  THR FFF CB  
8084  O OG1 . THR F 91  ? 2.123 1.813 1.570 0.130  0.026  -0.082 91  THR FFF OG1 
8085  C CG2 . THR F 91  ? 2.006 1.730 1.530 0.168  -0.005 -0.090 91  THR FFF CG2 
8086  N N   . ALA F 92  ? 1.844 1.637 1.479 0.159  0.003  -0.079 92  ALA FFF N   
8087  C CA  . ALA F 92  ? 1.797 1.613 1.475 0.167  -0.006 -0.079 92  ALA FFF CA  
8088  C C   . ALA F 92  ? 1.768 1.577 1.473 0.169  -0.021 -0.071 92  ALA FFF C   
8089  O O   . ALA F 92  ? 1.796 1.587 1.489 0.172  -0.025 -0.067 92  ALA FFF O   
8090  C CB  . ALA F 92  ? 1.770 1.623 1.465 0.159  0.010  -0.080 92  ALA FFF CB  
8091  N N   . VAL F 93  ? 1.726 1.548 1.461 0.169  -0.029 -0.069 93  VAL FFF N   
8092  C CA  . VAL F 93  ? 1.720 1.555 1.488 0.163  -0.036 -0.060 93  VAL FFF CA  
8093  C C   . VAL F 93  ? 1.709 1.565 1.494 0.157  -0.019 -0.055 93  VAL FFF C   
8094  O O   . VAL F 93  ? 1.724 1.587 1.512 0.156  -0.016 -0.057 93  VAL FFF O   
8095  C CB  . VAL F 93  ? 1.740 1.569 1.521 0.158  -0.055 -0.059 93  VAL FFF CB  
8096  C CG1 . VAL F 93  ? 1.758 1.615 1.575 0.145  -0.058 -0.050 93  VAL FFF CG1 
8097  C CG2 . VAL F 93  ? 1.773 1.576 1.532 0.162  -0.074 -0.065 93  VAL FFF CG2 
8098  N N   . TYR F 94  ? 1.706 1.570 1.496 0.158  -0.011 -0.051 94  TYR FFF N   
8099  C CA  . TYR F 94  ? 1.678 1.556 1.476 0.152  0.005  -0.047 94  TYR FFF CA  
8100  C C   . TYR F 94  ? 1.655 1.560 1.489 0.149  0.001  -0.040 94  TYR FFF C   
8101  O O   . TYR F 94  ? 1.641 1.562 1.491 0.154  -0.006 -0.038 94  TYR FFF O   
8102  C CB  . TYR F 94  ? 1.706 1.563 1.473 0.156  0.015  -0.048 94  TYR FFF CB  
8103  C CG  . TYR F 94  ? 1.724 1.560 1.453 0.146  0.023  -0.053 94  TYR FFF CG  
8104  C CD1 . TYR F 94  ? 1.754 1.572 1.461 0.149  0.016  -0.057 94  TYR FFF CD1 
8105  C CD2 . TYR F 94  ? 1.726 1.565 1.440 0.131  0.039  -0.054 94  TYR FFF CD2 
8106  C CE1 . TYR F 94  ? 1.782 1.591 1.453 0.136  0.027  -0.062 94  TYR FFF CE1 
8107  C CE2 . TYR F 94  ? 1.762 1.596 1.444 0.114  0.048  -0.060 94  TYR FFF CE2 
8108  C CZ  . TYR F 94  ? 1.784 1.605 1.445 0.116  0.044  -0.063 94  TYR FFF CZ  
8109  O OH  . TYR F 94  ? 1.792 1.616 1.420 0.096  0.056  -0.068 94  TYR FFF OH  
8110  N N   . TYR F 95  ? 1.648 1.561 1.490 0.140  0.006  -0.037 95  TYR FFF N   
8111  C CA  . TYR F 95  ? 1.653 1.586 1.519 0.130  0.006  -0.029 95  TYR FFF CA  
8112  C C   . TYR F 95  ? 1.630 1.575 1.495 0.130  0.024  -0.026 95  TYR FFF C   
8113  O O   . TYR F 95  ? 1.602 1.538 1.451 0.129  0.030  -0.029 95  TYR FFF O   
8114  C CB  . TYR F 95  ? 1.688 1.603 1.547 0.121  -0.004 -0.027 95  TYR FFF CB  
8115  C CG  . TYR F 95  ? 1.721 1.611 1.570 0.121  -0.023 -0.030 95  TYR FFF CG  
8116  C CD1 . TYR F 95  ? 1.729 1.621 1.589 0.103  -0.036 -0.025 95  TYR FFF CD1 
8117  C CD2 . TYR F 95  ? 1.750 1.617 1.574 0.135  -0.028 -0.040 95  TYR FFF CD2 
8118  C CE1 . TYR F 95  ? 1.753 1.614 1.595 0.099  -0.055 -0.029 95  TYR FFF CE1 
8119  C CE2 . TYR F 95  ? 1.773 1.609 1.579 0.137  -0.045 -0.045 95  TYR FFF CE2 
8120  C CZ  . TYR F 95  ? 1.774 1.602 1.587 0.118  -0.061 -0.039 95  TYR FFF CZ  
8121  O OH  . TYR F 95  ? 1.789 1.579 1.576 0.118  -0.081 -0.044 95  TYR FFF OH  
8122  N N   . CYS F 96  ? 1.633 1.602 1.514 0.132  0.031  -0.022 96  CYS FFF N   
8123  C CA  . CYS F 96  ? 1.645 1.625 1.523 0.131  0.046  -0.019 96  CYS FFF CA  
8124  C C   . CYS F 96  ? 1.628 1.620 1.519 0.114  0.046  -0.010 96  CYS FFF C   
8125  O O   . CYS F 96  ? 1.595 1.598 1.501 0.101  0.036  -0.005 96  CYS FFF O   
8126  C CB  . CYS F 96  ? 1.662 1.663 1.544 0.148  0.055  -0.021 96  CYS FFF CB  
8127  S SG  . CYS F 96  ? 1.661 1.726 1.587 0.142  0.055  -0.014 96  CYS FFF SG  
8128  N N   . ALA F 97  ? 1.653 1.638 1.529 0.111  0.056  -0.008 97  ALA FFF N   
8129  C CA  . ALA F 97  ? 1.694 1.674 1.565 0.096  0.056  0.001  97  ALA FFF CA  
8130  C C   . ALA F 97  ? 1.697 1.691 1.561 0.096  0.073  0.004  97  ALA FFF C   
8131  O O   . ALA F 97  ? 1.704 1.694 1.555 0.109  0.080  -0.004 97  ALA FFF O   
8132  C CB  . ALA F 97  ? 1.726 1.675 1.575 0.099  0.044  -0.002 97  ALA FFF CB  
8133  N N   . ARG F 98  ? 1.700 1.705 1.564 0.080  0.078  0.014  98  ARG FFF N   
8134  C CA  . ARG F 98  ? 1.715 1.734 1.569 0.080  0.095  0.018  98  ARG FFF CA  
8135  C C   . ARG F 98  ? 1.742 1.731 1.566 0.065  0.092  0.027  98  ARG FFF C   
8136  O O   . ARG F 98  ? 1.817 1.787 1.636 0.048  0.080  0.036  98  ARG FFF O   
8137  C CB  . ARG F 98  ? 1.733 1.806 1.613 0.074  0.109  0.022  98  ARG FFF CB  
8138  C CG  . ARG F 98  ? 1.763 1.856 1.630 0.075  0.129  0.025  98  ARG FFF CG  
8139  C CD  . ARG F 98  ? 1.771 1.935 1.669 0.078  0.145  0.025  98  ARG FFF CD  
8140  N NE  . ARG F 98  ? 1.790 1.979 1.673 0.078  0.167  0.028  98  ARG FFF NE  
8141  C CZ  . ARG F 98  ? 1.826 2.025 1.700 0.047  0.176  0.042  98  ARG FFF CZ  
8142  N NH1 . ARG F 98  ? 1.865 2.041 1.736 0.012  0.163  0.053  98  ARG FFF NH1 
8143  N NH2 . ARG F 98  ? 1.834 2.058 1.691 0.050  0.197  0.043  98  ARG FFF NH2 
8144  N N   . THR F 99  ? 1.712 1.690 1.511 0.072  0.098  0.026  99  THR FFF N   
8145  C CA  . THR F 99  ? 1.711 1.659 1.475 0.063  0.095  0.035  99  THR FFF CA  
8146  C C   . THR F 99  ? 1.692 1.656 1.441 0.060  0.115  0.039  99  THR FFF C   
8147  O O   . THR F 99  ? 1.636 1.617 1.390 0.074  0.126  0.028  99  THR FFF O   
8148  C CB  . THR F 99  ? 1.709 1.629 1.452 0.078  0.078  0.028  99  THR FFF CB  
8149  O OG1 . THR F 99  ? 1.737 1.624 1.441 0.073  0.071  0.038  99  THR FFF OG1 
8150  C CG2 . THR F 99  ? 1.683 1.618 1.426 0.090  0.082  0.015  99  THR FFF CG2 
8151  N N   . GLU F 100 ? 1.748 1.700 1.472 0.041  0.119  0.052  100 GLU FFF N   
8152  C CA  . GLU F 100 ? 1.800 1.763 1.501 0.037  0.139  0.057  100 GLU FFF CA  
8153  C C   . GLU F 100 ? 1.810 1.732 1.467 0.047  0.129  0.055  100 GLU FFF C   
8154  O O   . GLU F 100 ? 1.815 1.739 1.445 0.047  0.143  0.057  100 GLU FFF O   
8155  C CB  . GLU F 100 ? 1.874 1.851 1.568 0.006  0.152  0.073  100 GLU FFF CB  
8156  C CG  . GLU F 100 ? 1.881 1.920 1.625 -0.005 0.162  0.073  100 GLU FFF CG  
8157  C CD  . GLU F 100 ? 1.951 2.029 1.694 -0.043 0.181  0.087  100 GLU FFF CD  
8158  O OE1 . GLU F 100 ? 2.011 2.061 1.708 -0.061 0.189  0.099  100 GLU FFF OE1 
8159  O OE2 . GLU F 100 ? 1.964 2.106 1.752 -0.055 0.187  0.087  100 GLU FFF OE2 
8160  N N   . ASN F 101 ? 1.818 1.710 1.467 0.058  0.105  0.051  101 ASN FFF N   
8161  C CA  . ASN F 101 ? 1.832 1.696 1.443 0.071  0.090  0.048  101 ASN FFF CA  
8162  C C   . ASN F 101 ? 1.794 1.682 1.412 0.083  0.093  0.032  101 ASN FFF C   
8163  O O   . ASN F 101 ? 1.749 1.654 1.395 0.090  0.087  0.020  101 ASN FFF O   
8164  C CB  . ASN F 101 ? 1.843 1.678 1.444 0.083  0.063  0.048  101 ASN FFF CB  
8165  C CG  . ASN F 101 ? 1.867 1.681 1.429 0.102  0.044  0.045  101 ASN FFF CG  
8166  O OD1 . ASN F 101 ? 1.872 1.695 1.416 0.103  0.049  0.042  101 ASN FFF OD1 
8167  N ND2 . ASN F 101 ? 1.895 1.680 1.438 0.120  0.019  0.044  101 ASN FFF ND2 
8168  N N   . VAL F 102 ? 1.844 1.727 1.431 0.082  0.103  0.032  102 VAL FFF N   
8169  C CA  . VAL F 102 ? 1.878 1.771 1.455 0.087  0.103  0.017  102 VAL FFF CA  
8170  C C   . VAL F 102 ? 1.900 1.792 1.463 0.094  0.078  0.010  102 VAL FFF C   
8171  O O   . VAL F 102 ? 1.981 1.853 1.509 0.098  0.069  0.018  102 VAL FFF O   
8172  C CB  . VAL F 102 ? 1.955 1.837 1.495 0.085  0.121  0.018  102 VAL FFF CB  
8173  C CG1 . VAL F 102 ? 1.978 1.854 1.494 0.087  0.118  0.002  102 VAL FFF CG1 
8174  C CG2 . VAL F 102 ? 1.976 1.875 1.533 0.084  0.147  0.023  102 VAL FFF CG2 
8175  N N   . ARG F 103 ? 1.862 1.779 1.447 0.096  0.069  -0.004 103 ARG FFF N   
8176  C CA  . ARG F 103 ? 1.858 1.800 1.441 0.103  0.045  -0.013 103 ARG FFF CA  
8177  C C   . ARG F 103 ? 1.840 1.802 1.413 0.088  0.046  -0.028 103 ARG FFF C   
8178  O O   . ARG F 103 ? 1.824 1.787 1.410 0.075  0.057  -0.035 103 ARG FFF O   
8179  C CB  . ARG F 103 ? 1.832 1.797 1.451 0.113  0.034  -0.017 103 ARG FFF CB  
8180  C CG  . ARG F 103 ? 1.860 1.792 1.478 0.124  0.031  -0.003 103 ARG FFF CG  
8181  C CD  . ARG F 103 ? 1.919 1.825 1.498 0.142  0.012  0.004  103 ARG FFF CD  
8182  N NE  . ARG F 103 ? 1.920 1.867 1.504 0.163  -0.011 -0.011 103 ARG FFF NE  
8183  C CZ  . ARG F 103 ? 1.971 1.924 1.524 0.181  -0.030 -0.013 103 ARG FFF CZ  
8184  N NH1 . ARG F 103 ? 2.020 1.927 1.526 0.179  -0.030 -0.001 103 ARG FFF NH1 
8185  N NH2 . ARG F 103 ? 1.989 2.000 1.558 0.202  -0.050 -0.029 103 ARG FFF NH2 
8186  N N   . SER F 104 ? 1.868 1.837 1.411 0.087  0.033  -0.033 104 SER FFF N   
8187  C CA  . SER F 104 ? 1.893 1.874 1.415 0.065  0.031  -0.047 104 SER FFF CA  
8188  C C   . SER F 104 ? 1.844 1.872 1.398 0.049  0.025  -0.061 104 SER FFF C   
8189  O O   . SER F 104 ? 1.825 1.833 1.367 0.026  0.037  -0.067 104 SER FFF O   
8190  C CB  . SER F 104 ? 1.951 1.944 1.440 0.069  0.012  -0.050 104 SER FFF CB  
8191  O OG  . SER F 104 ? 1.983 2.005 1.461 0.044  0.003  -0.067 104 SER FFF OG  
8192  N N   . LEU F 105 ? 1.823 1.908 1.408 0.063  0.007  -0.065 105 LEU FFF N   
8193  C CA  . LEU F 105 ? 1.808 1.951 1.429 0.051  0.004  -0.077 105 LEU FFF CA  
8194  C C   . LEU F 105 ? 1.777 1.887 1.418 0.050  0.022  -0.071 105 LEU FFF C   
8195  O O   . LEU F 105 ? 1.815 1.903 1.468 0.076  0.023  -0.060 105 LEU FFF O   
8196  C CB  . LEU F 105 ? 1.828 2.037 1.476 0.081  -0.018 -0.083 105 LEU FFF CB  
8197  C CG  . LEU F 105 ? 1.858 2.146 1.547 0.072  -0.021 -0.097 105 LEU FFF CG  
8198  C CD1 . LEU F 105 ? 1.879 2.223 1.562 0.029  -0.023 -0.112 105 LEU FFF CD1 
8199  C CD2 . LEU F 105 ? 1.885 2.229 1.598 0.116  -0.040 -0.102 105 LEU FFF CD2 
8200  N N   . LEU F 106 ? 1.742 1.841 1.376 0.021  0.034  -0.077 106 LEU FFF N   
8201  C CA  . LEU F 106 ? 1.684 1.749 1.330 0.022  0.049  -0.072 106 LEU FFF CA  
8202  C C   . LEU F 106 ? 1.610 1.721 1.298 0.036  0.043  -0.074 106 LEU FFF C   
8203  O O   . LEU F 106 ? 1.531 1.618 1.236 0.056  0.048  -0.065 106 LEU FFF O   
8204  C CB  . LEU F 106 ? 1.720 1.751 1.331 -0.012 0.059  -0.079 106 LEU FFF CB  
8205  C CG  . LEU F 106 ? 1.714 1.708 1.328 -0.010 0.072  -0.075 106 LEU FFF CG  
8206  C CD1 . LEU F 106 ? 1.688 1.650 1.316 0.023  0.079  -0.063 106 LEU FFF CD1 
8207  C CD2 . LEU F 106 ? 1.773 1.706 1.331 -0.039 0.080  -0.081 106 LEU FFF CD2 
8208  N N   . SER F 107 ? 1.607 1.790 1.311 0.026  0.033  -0.086 107 SER FFF N   
8209  C CA  . SER F 107 ? 1.592 1.832 1.332 0.039  0.029  -0.093 107 SER FFF CA  
8210  C C   . SER F 107 ? 1.591 1.816 1.347 0.084  0.020  -0.085 107 SER FFF C   
8211  O O   . SER F 107 ? 1.619 1.858 1.395 0.098  0.020  -0.087 107 SER FFF O   
8212  C CB  . SER F 107 ? 1.586 1.923 1.342 0.025  0.019  -0.109 107 SER FFF CB  
8213  O OG  . SER F 107 ? 1.577 1.951 1.337 0.054  -0.001 -0.112 107 SER FFF OG  
8214  N N   . ASP F 108 ? 1.614 1.804 1.352 0.102  0.012  -0.076 108 ASP FFF N   
8215  C CA  . ASP F 108 ? 1.655 1.808 1.389 0.137  0.003  -0.065 108 ASP FFF CA  
8216  C C   . ASP F 108 ? 1.628 1.734 1.371 0.137  0.014  -0.056 108 ASP FFF C   
8217  O O   . ASP F 108 ? 1.669 1.751 1.409 0.161  0.004  -0.051 108 ASP FFF O   
8218  C CB  . ASP F 108 ? 1.727 1.832 1.428 0.142  -0.001 -0.053 108 ASP FFF CB  
8219  C CG  . ASP F 108 ? 1.798 1.933 1.482 0.165  -0.023 -0.059 108 ASP FFF CG  
8220  O OD1 . ASP F 108 ? 1.825 2.025 1.527 0.183  -0.037 -0.073 108 ASP FFF OD1 
8221  O OD2 . ASP F 108 ? 1.880 1.977 1.530 0.166  -0.025 -0.049 108 ASP FFF OD2 
8222  N N   . TYR F 109 ? 1.589 1.676 1.335 0.113  0.031  -0.054 109 TYR FFF N   
8223  C CA  . TYR F 109 ? 1.585 1.631 1.340 0.114  0.040  -0.045 109 TYR FFF CA  
8224  C C   . TYR F 109 ? 1.582 1.646 1.357 0.120  0.037  -0.052 109 TYR FFF C   
8225  O O   . TYR F 109 ? 1.585 1.621 1.367 0.119  0.043  -0.047 109 TYR FFF O   
8226  C CB  . TYR F 109 ? 1.588 1.605 1.331 0.095  0.057  -0.041 109 TYR FFF CB  
8227  C CG  . TYR F 109 ? 1.605 1.596 1.330 0.095  0.062  -0.032 109 TYR FFF CG  
8228  C CD1 . TYR F 109 ? 1.606 1.578 1.331 0.105  0.060  -0.020 109 TYR FFF CD1 
8229  C CD2 . TYR F 109 ? 1.629 1.609 1.327 0.083  0.071  -0.035 109 TYR FFF CD2 
8230  C CE1 . TYR F 109 ? 1.632 1.585 1.336 0.102  0.068  -0.010 109 TYR FFF CE1 
8231  C CE2 . TYR F 109 ? 1.652 1.612 1.330 0.085  0.078  -0.028 109 TYR FFF CE2 
8232  C CZ  . TYR F 109 ? 1.653 1.603 1.336 0.094  0.078  -0.015 109 TYR FFF CZ  
8233  O OH  . TYR F 109 ? 1.692 1.625 1.350 0.093  0.087  -0.007 109 TYR FFF OH  
8234  N N   . ALA F 110 ? 1.596 1.710 1.380 0.131  0.027  -0.064 110 ALA FFF N   
8235  C CA  . ALA F 110 ? 1.616 1.747 1.412 0.150  0.021  -0.070 110 ALA FFF CA  
8236  C C   . ALA F 110 ? 1.695 1.809 1.480 0.186  0.002  -0.069 110 ALA FFF C   
8237  O O   . ALA F 110 ? 1.704 1.765 1.479 0.196  -0.002 -0.061 110 ALA FFF O   
8238  C CB  . ALA F 110 ? 1.597 1.801 1.406 0.140  0.025  -0.086 110 ALA FFF CB  
8239  N N   . THR F 111 ? 1.794 1.944 1.571 0.205  -0.011 -0.075 111 THR FFF N   
8240  C CA  . THR F 111 ? 1.903 2.028 1.652 0.247  -0.033 -0.075 111 THR FFF CA  
8241  C C   . THR F 111 ? 1.963 1.993 1.682 0.243  -0.036 -0.056 111 THR FFF C   
8242  O O   . THR F 111 ? 2.055 2.038 1.751 0.266  -0.049 -0.054 111 THR FFF O   
8243  C CB  . THR F 111 ? 1.958 2.122 1.697 0.259  -0.045 -0.079 111 THR FFF CB  
8244  O OG1 . THR F 111 ? 1.973 2.238 1.741 0.266  -0.047 -0.099 111 THR FFF OG1 
8245  C CG2 . THR F 111 ? 2.016 2.127 1.709 0.300  -0.069 -0.074 111 THR FFF CG2 
8246  N N   . TRP F 112 ? 1.951 1.956 1.668 0.213  -0.023 -0.043 112 TRP FFF N   
8247  C CA  . TRP F 112 ? 1.972 1.904 1.656 0.205  -0.024 -0.025 112 TRP FFF CA  
8248  C C   . TRP F 112 ? 1.955 1.849 1.647 0.188  -0.017 -0.016 112 TRP FFF C   
8249  O O   . TRP F 112 ? 1.948 1.870 1.673 0.178  -0.007 -0.023 112 TRP FFF O   
8250  C CB  . TRP F 112 ? 1.976 1.911 1.655 0.182  -0.011 -0.017 112 TRP FFF CB  
8251  C CG  . TRP F 112 ? 2.048 1.989 1.697 0.201  -0.026 -0.020 112 TRP FFF CG  
8252  C CD1 . TRP F 112 ? 2.051 2.056 1.712 0.218  -0.037 -0.036 112 TRP FFF CD1 
8253  C CD2 . TRP F 112 ? 2.142 2.028 1.741 0.205  -0.035 -0.006 112 TRP FFF CD2 
8254  N NE1 . TRP F 112 ? 2.095 2.091 1.721 0.236  -0.053 -0.034 112 TRP FFF NE1 
8255  C CE2 . TRP F 112 ? 2.160 2.076 1.743 0.230  -0.052 -0.015 112 TRP FFF CE2 
8256  C CE3 . TRP F 112 ? 2.197 2.014 1.763 0.188  -0.029 0.013  112 TRP FFF CE3 
8257  C CZ2 . TRP F 112 ? 2.227 2.096 1.755 0.242  -0.065 -0.005 112 TRP FFF CZ2 
8258  C CZ3 . TRP F 112 ? 2.265 2.035 1.775 0.194  -0.039 0.024  112 TRP FFF CZ3 
8259  C CH2 . TRP F 112 ? 2.276 2.066 1.764 0.223  -0.058 0.015  112 TRP FFF CH2 
8260  N N   . PRO F 113 ? 1.958 1.787 1.617 0.180  -0.023 -0.001 113 PRO FFF N   
8261  C CA  . PRO F 113 ? 1.931 1.727 1.594 0.161  -0.021 0.006  113 PRO FFF CA  
8262  C C   . PRO F 113 ? 1.863 1.677 1.552 0.127  0.001  0.016  113 PRO FFF C   
8263  O O   . PRO F 113 ? 1.856 1.687 1.543 0.120  0.013  0.020  113 PRO FFF O   
8264  C CB  . PRO F 113 ? 2.014 1.729 1.614 0.168  -0.041 0.016  113 PRO FFF CB  
8265  C CG  . PRO F 113 ? 2.046 1.754 1.619 0.166  -0.038 0.025  113 PRO FFF CG  
8266  C CD  . PRO F 113 ? 2.003 1.786 1.613 0.182  -0.031 0.010  113 PRO FFF CD  
8267  N N   . TYR F 114 ? 1.823 1.637 1.533 0.110  0.006  0.019  114 TYR FFF N   
8268  C CA  . TYR F 114 ? 1.784 1.630 1.525 0.084  0.025  0.026  114 TYR FFF CA  
8269  C C   . TYR F 114 ? 1.843 1.659 1.568 0.055  0.022  0.041  114 TYR FFF C   
8270  O O   . TYR F 114 ? 1.911 1.685 1.617 0.053  0.004  0.041  114 TYR FFF O   
8271  C CB  . TYR F 114 ? 1.689 1.576 1.470 0.090  0.033  0.015  114 TYR FFF CB  
8272  C CG  . TYR F 114 ? 1.605 1.520 1.393 0.105  0.040  0.004  114 TYR FFF CG  
8273  C CD1 . TYR F 114 ? 1.594 1.510 1.372 0.122  0.030  -0.006 114 TYR FFF CD1 
8274  C CD2 . TYR F 114 ? 1.551 1.491 1.352 0.100  0.057  0.003  114 TYR FFF CD2 
8275  C CE1 . TYR F 114 ? 1.569 1.516 1.353 0.126  0.037  -0.016 114 TYR FFF CE1 
8276  C CE2 . TYR F 114 ? 1.537 1.488 1.332 0.106  0.063  -0.007 114 TYR FFF CE2 
8277  C CZ  . TYR F 114 ? 1.545 1.503 1.333 0.114  0.053  -0.016 114 TYR FFF CZ  
8278  O OH  . TYR F 114 ? 1.553 1.529 1.335 0.111  0.058  -0.026 114 TYR FFF OH  
8279  N N   . ASP F 115 ? 1.858 1.694 1.587 0.030  0.038  0.052  115 ASP FFF N   
8280  C CA  . ASP F 115 ? 1.914 1.728 1.623 -0.008 0.038  0.067  115 ASP FFF CA  
8281  C C   . ASP F 115 ? 1.874 1.730 1.625 -0.027 0.040  0.066  115 ASP FFF C   
8282  O O   . ASP F 115 ? 1.924 1.746 1.654 -0.057 0.027  0.073  115 ASP FFF O   
8283  C CB  . ASP F 115 ? 1.959 1.789 1.653 -0.027 0.058  0.079  115 ASP FFF CB  
8284  C CG  . ASP F 115 ? 2.011 1.781 1.645 -0.015 0.050  0.085  115 ASP FFF CG  
8285  O OD1 . ASP F 115 ? 2.067 1.760 1.645 -0.023 0.031  0.093  115 ASP FFF OD1 
8286  O OD2 . ASP F 115 ? 1.985 1.781 1.625 0.003  0.061  0.080  115 ASP FFF OD2 
8287  N N   . TYR F 116 ? 1.805 1.728 1.609 -0.010 0.052  0.055  116 TYR FFF N   
8288  C CA  . TYR F 116 ? 1.805 1.781 1.653 -0.021 0.053  0.052  116 TYR FFF CA  
8289  C C   . TYR F 116 ? 1.773 1.749 1.639 0.009  0.042  0.037  116 TYR FFF C   
8290  O O   . TYR F 116 ? 1.753 1.726 1.617 0.038  0.048  0.029  116 TYR FFF O   
8291  C CB  . TYR F 116 ? 1.801 1.857 1.685 -0.024 0.077  0.053  116 TYR FFF CB  
8292  C CG  . TYR F 116 ? 1.859 1.922 1.722 -0.049 0.093  0.066  116 TYR FFF CG  
8293  C CD1 . TYR F 116 ? 1.870 1.909 1.705 -0.032 0.103  0.066  116 TYR FFF CD1 
8294  C CD2 . TYR F 116 ? 1.916 2.012 1.784 -0.094 0.099  0.078  116 TYR FFF CD2 
8295  C CE1 . TYR F 116 ? 1.923 1.964 1.732 -0.054 0.119  0.078  116 TYR FFF CE1 
8296  C CE2 . TYR F 116 ? 1.956 2.058 1.798 -0.121 0.116  0.091  116 TYR FFF CE2 
8297  C CZ  . TYR F 116 ? 1.967 2.038 1.778 -0.099 0.127  0.091  116 TYR FFF CZ  
8298  O OH  . TYR F 116 ? 2.015 2.087 1.794 -0.125 0.144  0.105  116 TYR FFF OH  
8299  N N   . TRP F 117 ? 1.776 1.756 1.657 0.000  0.028  0.035  117 TRP FFF N   
8300  C CA  . TRP F 117 ? 1.741 1.716 1.633 0.026  0.017  0.022  117 TRP FFF CA  
8301  C C   . TRP F 117 ? 1.726 1.756 1.656 0.020  0.015  0.019  117 TRP FFF C   
8302  O O   . TRP F 117 ? 1.737 1.795 1.679 -0.013 0.011  0.026  117 TRP FFF O   
8303  C CB  . TRP F 117 ? 1.775 1.682 1.630 0.027  -0.004 0.019  117 TRP FFF CB  
8304  C CG  . TRP F 117 ? 1.786 1.650 1.605 0.047  -0.005 0.017  117 TRP FFF CG  
8305  C CD1 . TRP F 117 ? 1.825 1.653 1.610 0.038  -0.006 0.026  117 TRP FFF CD1 
8306  C CD2 . TRP F 117 ? 1.770 1.631 1.586 0.078  -0.005 0.005  117 TRP FFF CD2 
8307  N NE1 . TRP F 117 ? 1.834 1.640 1.597 0.067  -0.010 0.019  117 TRP FFF NE1 
8308  C CE2 . TRP F 117 ? 1.790 1.623 1.575 0.090  -0.008 0.006  117 TRP FFF CE2 
8309  C CE3 . TRP F 117 ? 1.751 1.633 1.583 0.096  -0.003 -0.006 117 TRP FFF CE3 
8310  C CZ2 . TRP F 117 ? 1.784 1.624 1.562 0.117  -0.008 -0.005 117 TRP FFF CZ2 
8311  C CZ3 . TRP F 117 ? 1.745 1.626 1.565 0.117  -0.001 -0.016 117 TRP FFF CZ3 
8312  C CH2 . TRP F 117 ? 1.763 1.631 1.562 0.127  -0.003 -0.016 117 TRP FFF CH2 
8313  N N   . GLY F 118 ? 1.710 1.756 1.654 0.050  0.015  0.008  118 GLY FFF N   
8314  C CA  . GLY F 118 ? 1.730 1.821 1.704 0.055  0.007  0.003  118 GLY FFF CA  
8315  C C   . GLY F 118 ? 1.775 1.829 1.736 0.048  -0.017 -0.001 118 GLY FFF C   
8316  O O   . GLY F 118 ? 1.807 1.798 1.732 0.051  -0.023 -0.002 118 GLY FFF O   
8317  N N   . GLN F 119 ? 1.803 1.896 1.788 0.044  -0.030 -0.004 119 GLN FFF N   
8318  C CA  . GLN F 119 ? 1.835 1.892 1.803 0.035  -0.054 -0.009 119 GLN FFF CA  
8319  C C   . GLN F 119 ? 1.778 1.788 1.719 0.070  -0.057 -0.018 119 GLN FFF C   
8320  O O   . GLN F 119 ? 1.776 1.737 1.689 0.067  -0.073 -0.023 119 GLN FFF O   
8321  C CB  . GLN F 119 ? 1.895 2.017 1.898 0.018  -0.069 -0.010 119 GLN FFF CB  
8322  C CG  . GLN F 119 ? 1.928 2.107 1.959 0.054  -0.068 -0.018 119 GLN FFF CG  
8323  C CD  . GLN F 119 ? 1.997 2.236 2.058 0.040  -0.090 -0.022 119 GLN FFF CD  
8324  O OE1 . GLN F 119 ? 2.056 2.326 2.133 -0.005 -0.098 -0.017 119 GLN FFF OE1 
8325  N NE2 . GLN F 119 ? 2.025 2.277 2.088 0.076  -0.102 -0.031 119 GLN FFF NE2 
8326  N N   . GLY F 120 ? 1.727 1.745 1.668 0.097  -0.040 -0.021 120 GLY FFF N   
8327  C CA  . GLY F 120 ? 1.700 1.677 1.611 0.122  -0.038 -0.029 120 GLY FFF CA  
8328  C C   . GLY F 120 ? 1.682 1.668 1.591 0.142  -0.048 -0.035 120 GLY FFF C   
8329  O O   . GLY F 120 ? 1.674 1.704 1.611 0.138  -0.060 -0.034 120 GLY FFF O   
8330  N N   . THR F 121 ? 1.656 1.603 1.531 0.160  -0.044 -0.040 121 THR FFF N   
8331  C CA  . THR F 121 ? 1.660 1.596 1.516 0.182  -0.055 -0.045 121 THR FFF CA  
8332  C C   . THR F 121 ? 1.653 1.534 1.461 0.186  -0.054 -0.050 121 THR FFF C   
8333  O O   . THR F 121 ? 1.639 1.500 1.430 0.179  -0.037 -0.050 121 THR FFF O   
8334  C CB  . THR F 121 ? 1.678 1.633 1.534 0.205  -0.047 -0.045 121 THR FFF CB  
8335  O OG1 . THR F 121 ? 1.735 1.708 1.593 0.226  -0.067 -0.049 121 THR FFF OG1 
8336  C CG2 . THR F 121 ? 1.713 1.613 1.520 0.216  -0.032 -0.046 121 THR FFF CG2 
8337  N N   . GLN F 122 ? 1.668 1.528 1.453 0.196  -0.070 -0.054 122 GLN FFF N   
8338  C CA  . GLN F 122 ? 1.719 1.530 1.456 0.197  -0.068 -0.058 122 GLN FFF CA  
8339  C C   . GLN F 122 ? 1.740 1.514 1.430 0.208  -0.057 -0.057 122 GLN FFF C   
8340  O O   . GLN F 122 ? 1.748 1.519 1.431 0.229  -0.065 -0.056 122 GLN FFF O   
8341  C CB  . GLN F 122 ? 1.769 1.570 1.495 0.201  -0.092 -0.063 122 GLN FFF CB  
8342  C CG  . GLN F 122 ? 1.830 1.584 1.505 0.202  -0.090 -0.069 122 GLN FFF CG  
8343  C CD  . GLN F 122 ? 1.832 1.585 1.506 0.191  -0.080 -0.073 122 GLN FFF CD  
8344  O OE1 . GLN F 122 ? 1.831 1.594 1.529 0.184  -0.089 -0.074 122 GLN FFF OE1 
8345  N NE2 . GLN F 122 ? 1.843 1.581 1.483 0.190  -0.061 -0.076 122 GLN FFF NE2 
8346  N N   . VAL F 123 ? 1.764 1.513 1.422 0.195  -0.039 -0.059 123 VAL FFF N   
8347  C CA  . VAL F 123 ? 1.837 1.533 1.429 0.194  -0.028 -0.058 123 VAL FFF CA  
8348  C C   . VAL F 123 ? 1.854 1.529 1.410 0.184  -0.026 -0.062 123 VAL FFF C   
8349  O O   . VAL F 123 ? 1.835 1.541 1.411 0.171  -0.017 -0.067 123 VAL FFF O   
8350  C CB  . VAL F 123 ? 1.864 1.557 1.447 0.176  -0.006 -0.056 123 VAL FFF CB  
8351  C CG1 . VAL F 123 ? 1.951 1.580 1.455 0.164  0.004  -0.054 123 VAL FFF CG1 
8352  C CG2 . VAL F 123 ? 1.852 1.566 1.467 0.188  -0.006 -0.052 123 VAL FFF CG2 
8353  N N   . THR F 124 ? 1.891 1.517 1.392 0.192  -0.035 -0.062 124 THR FFF N   
8354  C CA  . THR F 124 ? 1.934 1.535 1.389 0.184  -0.032 -0.066 124 THR FFF CA  
8355  C C   . THR F 124 ? 2.014 1.553 1.388 0.169  -0.019 -0.061 124 THR FFF C   
8356  O O   . THR F 124 ? 2.116 1.600 1.446 0.187  -0.032 -0.056 124 THR FFF O   
8357  C CB  . THR F 124 ? 1.944 1.538 1.400 0.205  -0.059 -0.069 124 THR FFF CB  
8358  O OG1 . THR F 124 ? 2.011 1.570 1.440 0.226  -0.077 -0.065 124 THR FFF OG1 
8359  C CG2 . THR F 124 ? 1.893 1.536 1.416 0.210  -0.074 -0.073 124 THR FFF CG2 
8360  N N   . VAL F 125 ? 2.011 1.559 1.362 0.138  0.006  -0.063 125 VAL FFF N   
8361  C CA  . VAL F 125 ? 2.083 1.571 1.349 0.110  0.022  -0.058 125 VAL FFF CA  
8362  C C   . VAL F 125 ? 2.104 1.558 1.310 0.107  0.021  -0.059 125 VAL FFF C   
8363  O O   . VAL F 125 ? 2.043 1.549 1.276 0.105  0.028  -0.067 125 VAL FFF O   
8364  C CB  . VAL F 125 ? 2.106 1.634 1.377 0.069  0.050  -0.059 125 VAL FFF CB  
8365  C CG1 . VAL F 125 ? 2.152 1.635 1.392 0.053  0.056  -0.052 125 VAL FFF CG1 
8366  C CG2 . VAL F 125 ? 2.040 1.663 1.396 0.073  0.056  -0.068 125 VAL FFF CG2 
8367  N N   . SER F 126 ? 2.190 1.553 1.309 0.109  0.012  -0.051 126 SER FFF N   
8368  C CA  . SER F 126 ? 2.267 1.578 1.319 0.116  0.003  -0.050 126 SER FFF CA  
8369  C C   . SER F 126 ? 2.356 1.592 1.298 0.076  0.022  -0.043 126 SER FFF C   
8370  O O   . SER F 126 ? 2.366 1.631 1.305 0.032  0.050  -0.042 126 SER FFF O   
8371  C CB  . SER F 126 ? 2.314 1.581 1.358 0.162  -0.032 -0.048 126 SER FFF CB  
8372  O OG  . SER F 126 ? 2.408 1.586 1.377 0.168  -0.039 -0.039 126 SER FFF OG  
8373  N N   . SER F 127 ? 2.422 1.567 1.272 0.088  0.008  -0.037 127 SER FFF N   
8374  C CA  . SER F 127 ? 2.507 1.552 1.228 0.050  0.021  -0.026 127 SER FFF CA  
8375  C C   . SER F 127 ? 2.584 1.506 1.212 0.087  -0.010 -0.018 127 SER FFF C   
8376  O O   . SER F 127 ? 2.620 1.429 1.142 0.076  -0.012 -0.007 127 SER FFF O   
8377  C CB  . SER F 127 ? 2.515 1.593 1.212 0.018  0.044  -0.030 127 SER FFF CB  
8378  O OG  . SER F 127 ? 2.424 1.611 1.190 -0.016 0.075  -0.038 127 SER FFF OG  
8379  N N   . THR G 1   ? 1.442 1.992 1.706 -0.002 0.082  0.250  0   THR HHH N   
8380  C CA  . THR G 1   ? 1.470 1.960 1.684 0.023  0.106  0.203  0   THR HHH CA  
8381  C C   . THR G 1   ? 1.445 1.884 1.655 0.019  0.075  0.192  0   THR HHH C   
8382  O O   . THR G 1   ? 1.409 1.850 1.645 -0.005 0.033  0.217  0   THR HHH O   
8383  C CB  . THR G 1   ? 1.495 1.937 1.649 0.020  0.116  0.162  0   THR HHH CB  
8384  O OG1 . THR G 1   ? 1.528 1.915 1.643 0.040  0.132  0.123  0   THR HHH OG1 
8385  C CG2 . THR G 1   ? 1.471 1.880 1.613 -0.011 0.075  0.159  0   THR HHH CG2 
8386  N N   . GLN G 2   ? 1.453 1.845 1.628 0.040  0.094  0.158  1   GLN HHH N   
8387  C CA  . GLN G 2   ? 1.467 1.813 1.633 0.042  0.072  0.147  1   GLN HHH CA  
8388  C C   . GLN G 2   ? 1.473 1.763 1.602 0.021  0.039  0.128  1   GLN HHH C   
8389  O O   . GLN G 2   ? 1.501 1.775 1.639 0.007  -0.001 0.142  1   GLN HHH O   
8390  C CB  . GLN G 2   ? 1.491 1.805 1.630 0.071  0.104  0.118  1   GLN HHH CB  
8391  C CG  . GLN G 2   ? 1.501 1.769 1.627 0.074  0.086  0.109  1   GLN HHH CG  
8392  C CD  . GLN G 2   ? 1.517 1.817 1.690 0.082  0.076  0.140  1   GLN HHH CD  
8393  O OE1 . GLN G 2   ? 1.523 1.865 1.727 0.102  0.102  0.156  1   GLN HHH OE1 
8394  N NE2 . GLN G 2   ? 1.515 1.790 1.688 0.068  0.037  0.149  1   GLN HHH NE2 
8395  N N   . MET G 3   ? 1.471 1.733 1.559 0.021  0.053  0.098  2   MET HHH N   
8396  C CA  . MET G 3   ? 1.474 1.682 1.522 0.010  0.031  0.074  2   MET HHH CA  
8397  C C   . MET G 3   ? 1.429 1.640 1.459 -0.002 0.037  0.065  2   MET HHH C   
8398  O O   . MET G 3   ? 1.468 1.695 1.490 0.007  0.069  0.056  2   MET HHH O   
8399  C CB  . MET G 3   ? 1.499 1.663 1.512 0.027  0.046  0.045  2   MET HHH CB  
8400  C CG  . MET G 3   ? 1.513 1.628 1.489 0.023  0.026  0.026  2   MET HHH CG  
8401  S SD  . MET G 3   ? 1.588 1.680 1.563 0.011  -0.025 0.042  2   MET HHH SD  
8402  C CE  . MET G 3   ? 1.603 1.715 1.613 0.018  -0.031 0.066  2   MET HHH CE  
8403  N N   . GLN G 4   ? 1.376 1.567 1.396 -0.019 0.005  0.066  3   GLN HHH N   
8404  C CA  . GLN G 4   ? 1.353 1.541 1.355 -0.032 0.004  0.058  3   GLN HHH CA  
8405  C C   . GLN G 4   ? 1.364 1.499 1.330 -0.032 -0.017 0.036  3   GLN HHH C   
8406  O O   . GLN G 4   ? 1.421 1.527 1.382 -0.031 -0.045 0.040  3   GLN HHH O   
8407  C CB  . GLN G 4   ? 1.337 1.562 1.371 -0.054 -0.018 0.090  3   GLN HHH CB  
8408  C CG  . GLN G 4   ? 1.317 1.546 1.337 -0.068 -0.019 0.087  3   GLN HHH CG  
8409  C CD  . GLN G 4   ? 1.309 1.569 1.363 -0.092 -0.049 0.123  3   GLN HHH CD  
8410  O OE1 . GLN G 4   ? 1.304 1.591 1.396 -0.099 -0.065 0.153  3   GLN HHH OE1 
8411  N NE2 . GLN G 4   ? 1.306 1.563 1.349 -0.107 -0.059 0.124  3   GLN HHH NE2 
8412  N N   . LEU G 5   ? 1.345 1.466 1.285 -0.031 -0.003 0.016  4   LEU HHH N   
8413  C CA  . LEU G 5   ? 1.358 1.436 1.266 -0.026 -0.018 -0.002 4   LEU HHH CA  
8414  C C   . LEU G 5   ? 1.385 1.460 1.288 -0.041 -0.038 0.002  4   LEU HHH C   
8415  O O   . LEU G 5   ? 1.413 1.513 1.321 -0.051 -0.023 0.002  4   LEU HHH O   
8416  C CB  . LEU G 5   ? 1.355 1.422 1.244 -0.013 0.011  -0.024 4   LEU HHH CB  
8417  C CG  . LEU G 5   ? 1.381 1.445 1.273 0.001  0.030  -0.027 4   LEU HHH CG  
8418  C CD1 . LEU G 5   ? 1.383 1.433 1.256 0.010  0.052  -0.045 4   LEU HHH CD1 
8419  C CD2 . LEU G 5   ? 1.412 1.455 1.302 0.009  0.007  -0.021 4   LEU HHH CD2 
8420  N N   . VAL G 6   ? 1.416 1.456 1.306 -0.041 -0.072 0.004  5   VAL HHH N   
8421  C CA  . VAL G 6   ? 1.446 1.471 1.327 -0.051 -0.097 0.006  5   VAL HHH CA  
8422  C C   . VAL G 6   ? 1.467 1.459 1.314 -0.032 -0.092 -0.017 5   VAL HHH C   
8423  O O   . VAL G 6   ? 1.486 1.456 1.314 -0.012 -0.086 -0.028 5   VAL HHH O   
8424  C CB  . VAL G 6   ? 1.492 1.494 1.378 -0.063 -0.143 0.024  5   VAL HHH CB  
8425  C CG1 . VAL G 6   ? 1.483 1.516 1.405 -0.075 -0.147 0.048  5   VAL HHH CG1 
8426  C CG2 . VAL G 6   ? 1.567 1.506 1.413 -0.045 -0.170 0.009  5   VAL HHH CG2 
8427  N N   . GLN G 7   ? 1.492 1.486 1.334 -0.037 -0.093 -0.020 6   GLN HHH N   
8428  C CA  . GLN G 7   ? 1.527 1.501 1.344 -0.018 -0.085 -0.036 6   GLN HHH CA  
8429  C C   . GLN G 7   ? 1.559 1.504 1.362 -0.016 -0.117 -0.034 6   GLN HHH C   
8430  O O   . GLN G 7   ? 1.517 1.469 1.335 -0.038 -0.137 -0.019 6   GLN HHH O   
8431  C CB  . GLN G 7   ? 1.504 1.512 1.331 -0.024 -0.054 -0.041 6   GLN HHH CB  
8432  C CG  . GLN G 7   ? 1.483 1.507 1.316 -0.022 -0.025 -0.046 6   GLN HHH CG  
8433  C CD  . GLN G 7   ? 1.460 1.496 1.291 -0.019 -0.001 -0.055 6   GLN HHH CD  
8434  O OE1 . GLN G 7   ? 1.421 1.473 1.258 -0.029 0.019  -0.057 6   GLN HHH OE1 
8435  N NE2 . GLN G 7   ? 1.468 1.492 1.287 -0.005 -0.003 -0.058 6   GLN HHH NE2 
8436  N N   . SER G 8   ? 1.621 1.535 1.394 0.011  -0.120 -0.047 7   SER HHH N   
8437  C CA  . SER G 8   ? 1.665 1.544 1.418 0.022  -0.146 -0.048 7   SER HHH CA  
8438  C C   . SER G 8   ? 1.644 1.556 1.422 0.001  -0.144 -0.039 7   SER HHH C   
8439  O O   . SER G 8   ? 1.612 1.567 1.411 -0.013 -0.115 -0.037 7   SER HHH O   
8440  C CB  . SER G 8   ? 1.685 1.542 1.405 0.060  -0.136 -0.063 7   SER HHH CB  
8441  O OG  . SER G 8   ? 1.647 1.548 1.385 0.064  -0.100 -0.063 7   SER HHH OG  
8442  N N   . GLY G 9   ? 1.681 1.564 1.450 -0.001 -0.175 -0.033 8   GLY HHH N   
8443  C CA  . GLY G 9   ? 1.684 1.592 1.473 -0.020 -0.179 -0.022 8   GLY HHH CA  
8444  C C   . GLY G 9   ? 1.667 1.601 1.460 -0.007 -0.153 -0.028 8   GLY HHH C   
8445  O O   . GLY G 9   ? 1.662 1.602 1.447 0.015  -0.128 -0.039 8   GLY HHH O   
8446  N N   . THR G 10  ? 1.653 1.604 1.460 -0.022 -0.159 -0.018 9   THR HHH N   
8447  C CA  . THR G 10  ? 1.625 1.608 1.443 -0.017 -0.140 -0.017 9   THR HHH CA  
8448  C C   . THR G 10  ? 1.638 1.592 1.438 0.021  -0.148 -0.022 9   THR HHH C   
8449  O O   . THR G 10  ? 1.619 1.528 1.400 0.032  -0.179 -0.023 9   THR HHH O   
8450  C CB  . THR G 10  ? 1.656 1.664 1.493 -0.048 -0.150 -0.003 9   THR HHH CB  
8451  O OG1 . THR G 10  ? 1.683 1.711 1.529 -0.076 -0.144 0.003  9   THR HHH OG1 
8452  C CG2 . THR G 10  ? 1.661 1.706 1.512 -0.051 -0.131 0.001  9   THR HHH CG2 
8453  N N   . GLU G 11  ? 1.660 1.642 1.466 0.040  -0.121 -0.024 10  GLU HHH N   
8454  C CA  . GLU G 11  ? 1.738 1.707 1.529 0.083  -0.118 -0.027 10  GLU HHH CA  
8455  C C   . GLU G 11  ? 1.727 1.738 1.547 0.082  -0.110 -0.012 10  GLU HHH C   
8456  O O   . GLU G 11  ? 1.688 1.748 1.535 0.065  -0.086 -0.005 10  GLU HHH O   
8457  C CB  . GLU G 11  ? 1.762 1.736 1.540 0.109  -0.091 -0.035 10  GLU HHH CB  
8458  C CG  . GLU G 11  ? 1.797 1.732 1.548 0.109  -0.100 -0.048 10  GLU HHH CG  
8459  C CD  . GLU G 11  ? 1.874 1.743 1.579 0.141  -0.128 -0.060 10  GLU HHH CD  
8460  O OE1 . GLU G 11  ? 1.902 1.747 1.594 0.162  -0.145 -0.059 10  GLU HHH OE1 
8461  O OE2 . GLU G 11  ? 1.907 1.744 1.586 0.146  -0.134 -0.069 10  GLU HHH OE2 
8462  N N   . VAL G 12  ? 1.748 1.740 1.564 0.098  -0.131 -0.007 11  VAL HHH N   
8463  C CA  . VAL G 12  ? 1.726 1.755 1.568 0.111  -0.125 0.009  11  VAL HHH CA  
8464  C C   . VAL G 12  ? 1.758 1.776 1.580 0.168  -0.112 0.005  11  VAL HHH C   
8465  O O   . VAL G 12  ? 1.835 1.795 1.619 0.200  -0.133 -0.006 11  VAL HHH O   
8466  C CB  . VAL G 12  ? 1.730 1.745 1.579 0.096  -0.156 0.019  11  VAL HHH CB  
8467  C CG1 . VAL G 12  ? 1.705 1.769 1.589 0.101  -0.149 0.039  11  VAL HHH CG1 
8468  C CG2 . VAL G 12  ? 1.700 1.713 1.556 0.046  -0.172 0.022  11  VAL HHH CG2 
8469  N N   . LYS G 13  ? 1.722 1.793 1.566 0.181  -0.080 0.016  12  LYS HHH N   
8470  C CA  . LYS G 13  ? 1.762 1.836 1.588 0.238  -0.059 0.017  12  LYS HHH CA  
8471  C C   . LYS G 13  ? 1.745 1.888 1.617 0.251  -0.042 0.044  12  LYS HHH C   
8472  O O   . LYS G 13  ? 1.718 1.907 1.635 0.209  -0.042 0.062  12  LYS HHH O   
8473  C CB  . LYS G 13  ? 1.765 1.843 1.575 0.245  -0.035 0.008  12  LYS HHH CB  
8474  C CG  . LYS G 13  ? 1.801 1.815 1.568 0.237  -0.053 -0.017 12  LYS HHH CG  
8475  C CD  . LYS G 13  ? 1.891 1.832 1.600 0.281  -0.075 -0.034 12  LYS HHH CD  
8476  C CE  . LYS G 13  ? 1.963 1.897 1.634 0.333  -0.051 -0.040 12  LYS HHH CE  
8477  N NZ  . LYS G 13  ? 2.063 1.933 1.676 0.389  -0.068 -0.055 12  LYS HHH NZ  
8478  N N   . LYS G 14  ? 1.757 1.903 1.615 0.310  -0.028 0.049  13  LYS HHH N   
8479  C CA  . LYS G 14  ? 1.727 1.945 1.631 0.334  -0.008 0.081  13  LYS HHH CA  
8480  C C   . LYS G 14  ? 1.678 1.956 1.603 0.343  0.030  0.097  13  LYS HHH C   
8481  O O   . LYS G 14  ? 1.656 1.908 1.542 0.362  0.043  0.081  13  LYS HHH O   
8482  C CB  . LYS G 14  ? 1.807 1.995 1.682 0.398  -0.013 0.078  13  LYS HHH CB  
8483  C CG  . LYS G 14  ? 1.839 1.971 1.701 0.389  -0.053 0.069  13  LYS HHH CG  
8484  C CD  . LYS G 14  ? 1.818 2.007 1.741 0.363  -0.061 0.098  13  LYS HHH CD  
8485  C CE  . LYS G 14  ? 1.866 2.089 1.807 0.421  -0.048 0.120  13  LYS HHH CE  
8486  N NZ  . LYS G 14  ? 1.935 2.084 1.835 0.457  -0.078 0.105  13  LYS HHH NZ  
8487  N N   . PRO G 15  ? 1.637 1.999 1.627 0.324  0.045  0.132  14  PRO HHH N   
8488  C CA  . PRO G 15  ? 1.626 2.051 1.644 0.330  0.078  0.156  14  PRO HHH CA  
8489  C C   . PRO G 15  ? 1.688 2.112 1.668 0.402  0.106  0.155  14  PRO HHH C   
8490  O O   . PRO G 15  ? 1.752 2.182 1.726 0.453  0.110  0.163  14  PRO HHH O   
8491  C CB  . PRO G 15  ? 1.597 2.108 1.689 0.311  0.082  0.199  14  PRO HHH CB  
8492  C CG  . PRO G 15  ? 1.577 2.061 1.679 0.268  0.046  0.192  14  PRO HHH CG  
8493  C CD  . PRO G 15  ? 1.614 2.012 1.654 0.292  0.027  0.154  14  PRO HHH CD  
8494  N N   . GLY G 16  ? 1.685 2.101 1.639 0.407  0.124  0.146  15  GLY HHH N   
8495  C CA  . GLY G 16  ? 1.751 2.167 1.663 0.474  0.153  0.146  15  GLY HHH CA  
8496  C C   . GLY G 16  ? 1.806 2.125 1.634 0.494  0.139  0.101  15  GLY HHH C   
8497  O O   . GLY G 16  ? 1.896 2.211 1.688 0.522  0.160  0.097  15  GLY HHH O   
8498  N N   . GLU G 17  ? 1.789 2.033 1.587 0.477  0.102  0.072  16  GLU HHH N   
8499  C CA  . GLU G 17  ? 1.831 1.977 1.552 0.488  0.079  0.033  16  GLU HHH CA  
8500  C C   . GLU G 17  ? 1.750 1.894 1.467 0.453  0.086  0.025  16  GLU HHH C   
8501  O O   . GLU G 17  ? 1.690 1.894 1.464 0.409  0.099  0.046  16  GLU HHH O   
8502  C CB  . GLU G 17  ? 1.878 1.959 1.587 0.461  0.035  0.013  16  GLU HHH CB  
8503  C CG  . GLU G 17  ? 1.980 2.028 1.664 0.510  0.021  0.009  16  GLU HHH CG  
8504  C CD  . GLU G 17  ? 2.012 2.007 1.695 0.480  -0.023 -0.001 16  GLU HHH CD  
8505  O OE1 . GLU G 17  ? 1.973 1.972 1.686 0.416  -0.039 -0.002 16  GLU HHH OE1 
8506  O OE2 . GLU G 17  ? 2.104 2.053 1.757 0.521  -0.040 -0.008 16  GLU HHH OE2 
8507  N N   . SER G 18  ? 1.758 1.832 1.408 0.473  0.076  -0.002 17  SER HHH N   
8508  C CA  . SER G 18  ? 1.737 1.797 1.375 0.447  0.079  -0.012 17  SER HHH CA  
8509  C C   . SER G 18  ? 1.722 1.716 1.344 0.404  0.040  -0.036 17  SER HHH C   
8510  O O   . SER G 18  ? 1.767 1.709 1.365 0.412  0.010  -0.050 17  SER HHH O   
8511  C CB  . SER G 18  ? 1.818 1.851 1.391 0.501  0.095  -0.021 17  SER HHH CB  
8512  O OG  . SER G 18  ? 1.935 1.908 1.447 0.555  0.079  -0.039 17  SER HHH OG  
8513  N N   . LEU G 19  ? 1.684 1.682 1.321 0.363  0.040  -0.039 18  LEU HHH N   
8514  C CA  . LEU G 19  ? 1.680 1.641 1.323 0.315  0.010  -0.053 18  LEU HHH CA  
8515  C C   . LEU G 19  ? 1.667 1.617 1.302 0.294  0.013  -0.060 18  LEU HHH C   
8516  O O   . LEU G 19  ? 1.619 1.618 1.284 0.283  0.041  -0.046 18  LEU HHH O   
8517  C CB  . LEU G 19  ? 1.654 1.666 1.360 0.270  0.011  -0.037 18  LEU HHH CB  
8518  C CG  . LEU G 19  ? 1.658 1.650 1.378 0.219  -0.011 -0.045 18  LEU HHH CG  
8519  C CD1 . LEU G 19  ? 1.715 1.649 1.407 0.221  -0.049 -0.057 18  LEU HHH CD1 
8520  C CD2 . LEU G 19  ? 1.611 1.656 1.384 0.177  -0.003 -0.030 18  LEU HHH CD2 
8521  N N   . LYS G 20  ? 1.716 1.604 1.316 0.286  -0.017 -0.078 19  LYS HHH N   
8522  C CA  . LYS G 20  ? 1.724 1.600 1.319 0.266  -0.018 -0.083 19  LYS HHH CA  
8523  C C   . LYS G 20  ? 1.694 1.555 1.312 0.220  -0.045 -0.086 19  LYS HHH C   
8524  O O   . LYS G 20  ? 1.750 1.555 1.339 0.221  -0.080 -0.096 19  LYS HHH O   
8525  C CB  . LYS G 20  ? 1.820 1.637 1.348 0.303  -0.030 -0.098 19  LYS HHH CB  
8526  C CG  . LYS G 20  ? 1.832 1.635 1.354 0.284  -0.036 -0.102 19  LYS HHH CG  
8527  C CD  . LYS G 20  ? 1.910 1.667 1.367 0.322  -0.040 -0.112 19  LYS HHH CD  
8528  C CE  . LYS G 20  ? 2.005 1.677 1.403 0.336  -0.086 -0.130 19  LYS HHH CE  
8529  N NZ  . LYS G 20  ? 2.073 1.694 1.405 0.364  -0.098 -0.141 19  LYS HHH NZ  
8530  N N   . ILE G 21  ? 1.625 1.531 1.290 0.183  -0.029 -0.077 20  ILE HHH N   
8531  C CA  . ILE G 21  ? 1.605 1.510 1.296 0.142  -0.046 -0.076 20  ILE HHH CA  
8532  C C   . ILE G 21  ? 1.591 1.480 1.274 0.134  -0.049 -0.080 20  ILE HHH C   
8533  O O   . ILE G 21  ? 1.540 1.441 1.218 0.146  -0.027 -0.080 20  ILE HHH O   
8534  C CB  . ILE G 21  ? 1.564 1.519 1.300 0.110  -0.030 -0.066 20  ILE HHH CB  
8535  C CG1 . ILE G 21  ? 1.542 1.534 1.299 0.103  0.002  -0.061 20  ILE HHH CG1 
8536  C CG2 . ILE G 21  ? 1.570 1.538 1.314 0.117  -0.033 -0.060 20  ILE HHH CG2 
8537  C CD1 . ILE G 21  ? 1.508 1.533 1.299 0.067  0.011  -0.055 20  ILE HHH CD1 
8538  N N   . SER G 22  ? 1.616 1.482 1.301 0.113  -0.077 -0.080 21  SER HHH N   
8539  C CA  . SER G 22  ? 1.624 1.472 1.304 0.105  -0.088 -0.080 21  SER HHH CA  
8540  C C   . SER G 22  ? 1.525 1.417 1.250 0.073  -0.071 -0.071 21  SER HHH C   
8541  O O   . SER G 22  ? 1.446 1.370 1.197 0.055  -0.058 -0.067 21  SER HHH O   
8542  C CB  . SER G 22  ? 1.712 1.509 1.369 0.102  -0.133 -0.080 21  SER HHH CB  
8543  O OG  . SER G 22  ? 1.707 1.523 1.402 0.066  -0.148 -0.066 21  SER HHH OG  
8544  N N   . CYS G 23  ? 1.485 1.374 1.213 0.069  -0.071 -0.068 22  CYS HHH N   
8545  C CA  . CYS G 23  ? 1.443 1.366 1.208 0.045  -0.059 -0.059 22  CYS HHH CA  
8546  C C   . CYS G 23  ? 1.440 1.345 1.202 0.045  -0.077 -0.054 22  CYS HHH C   
8547  O O   . CYS G 23  ? 1.439 1.331 1.184 0.063  -0.068 -0.059 22  CYS HHH O   
8548  C CB  . CYS G 23  ? 1.434 1.388 1.214 0.046  -0.021 -0.063 22  CYS HHH CB  
8549  S SG  . CYS G 23  ? 1.440 1.419 1.249 0.030  -0.004 -0.056 22  CYS HHH SG  
8550  N N   . LYS G 24  ? 1.455 1.361 1.236 0.026  -0.103 -0.040 23  LYS HHH N   
8551  C CA  . LYS G 24  ? 1.495 1.386 1.279 0.021  -0.128 -0.029 23  LYS HHH CA  
8552  C C   . LYS G 24  ? 1.456 1.396 1.286 0.006  -0.109 -0.013 23  LYS HHH C   
8553  O O   . LYS G 24  ? 1.437 1.414 1.294 -0.009 -0.093 -0.006 23  LYS HHH O   
8554  C CB  . LYS G 24  ? 1.567 1.425 1.343 0.009  -0.176 -0.019 23  LYS HHH CB  
8555  C CG  . LYS G 24  ? 1.655 1.483 1.423 0.006  -0.212 -0.008 23  LYS HHH CG  
8556  C CD  . LYS G 24  ? 1.740 1.519 1.490 -0.006 -0.267 0.000  23  LYS HHH CD  
8557  C CE  . LYS G 24  ? 1.801 1.534 1.526 -0.004 -0.306 0.005  23  LYS HHH CE  
8558  N NZ  . LYS G 24  ? 1.868 1.554 1.583 -0.024 -0.366 0.019  23  LYS HHH NZ  
8559  N N   . GLY G 25  ? 1.468 1.406 1.303 0.012  -0.111 -0.007 24  GLY HHH N   
8560  C CA  . GLY G 25  ? 1.460 1.442 1.339 0.004  -0.093 0.010  24  GLY HHH CA  
8561  C C   . GLY G 25  ? 1.498 1.495 1.409 -0.015 -0.126 0.038  24  GLY HHH C   
8562  O O   . GLY G 25  ? 1.532 1.506 1.437 -0.013 -0.152 0.046  24  GLY HHH O   
8563  N N   . SER G 26  ? 1.504 1.541 1.449 -0.034 -0.125 0.056  25  SER HHH N   
8564  C CA  . SER G 26  ? 1.520 1.591 1.511 -0.055 -0.150 0.092  25  SER HHH CA  
8565  C C   . SER G 26  ? 1.494 1.610 1.523 -0.048 -0.127 0.108  25  SER HHH C   
8566  O O   . SER G 26  ? 1.424 1.579 1.468 -0.039 -0.084 0.105  25  SER HHH O   
8567  C CB  . SER G 26  ? 1.529 1.637 1.545 -0.075 -0.149 0.108  25  SER HHH CB  
8568  O OG  . SER G 26  ? 1.524 1.695 1.595 -0.087 -0.145 0.145  25  SER HHH OG  
8569  N N   . GLY G 27  ? 1.536 1.642 1.577 -0.050 -0.155 0.125  26  GLY HHH N   
8570  C CA  . GLY G 27  ? 1.541 1.697 1.630 -0.047 -0.141 0.151  26  GLY HHH CA  
8571  C C   . GLY G 27  ? 1.546 1.672 1.617 -0.030 -0.144 0.142  26  GLY HHH C   
8572  O O   . GLY G 27  ? 1.584 1.648 1.605 -0.024 -0.166 0.120  26  GLY HHH O   
8573  N N   . TYR G 28  ? 1.513 1.684 1.626 -0.019 -0.121 0.159  27  TYR HHH N   
8574  C CA  . TYR G 28  ? 1.556 1.710 1.667 -0.007 -0.129 0.162  27  TYR HHH CA  
8575  C C   . TYR G 28  ? 1.535 1.683 1.627 0.020  -0.083 0.136  27  TYR HHH C   
8576  O O   . TYR G 28  ? 1.544 1.716 1.641 0.029  -0.044 0.125  27  TYR HHH O   
8577  C CB  . TYR G 28  ? 1.586 1.798 1.764 -0.016 -0.143 0.208  27  TYR HHH CB  
8578  C CG  . TYR G 28  ? 1.645 1.848 1.836 -0.047 -0.202 0.236  27  TYR HHH CG  
8579  C CD1 . TYR G 28  ? 1.697 1.842 1.856 -0.054 -0.250 0.235  27  TYR HHH CD1 
8580  C CD2 . TYR G 28  ? 1.658 1.903 1.887 -0.069 -0.213 0.263  27  TYR HHH CD2 
8581  C CE1 . TYR G 28  ? 1.744 1.867 1.907 -0.083 -0.311 0.259  27  TYR HHH CE1 
8582  C CE2 . TYR G 28  ? 1.697 1.927 1.938 -0.101 -0.273 0.291  27  TYR HHH CE2 
8583  C CZ  . TYR G 28  ? 1.735 1.901 1.942 -0.108 -0.323 0.288  27  TYR HHH CZ  
8584  O OH  . TYR G 28  ? 1.785 1.925 1.998 -0.141 -0.388 0.315  27  TYR HHH OH  
8585  N N   . GLY G 29  ? 1.524 1.637 1.593 0.032  -0.092 0.129  28  GLY HHH N   
8586  C CA  . GLY G 29  ? 1.498 1.598 1.549 0.055  -0.056 0.108  28  GLY HHH CA  
8587  C C   . GLY G 29  ? 1.485 1.546 1.485 0.061  -0.039 0.074  28  GLY HHH C   
8588  O O   . GLY G 29  ? 1.446 1.503 1.437 0.076  -0.005 0.058  28  GLY HHH O   
8589  N N   . PHE G 30  ? 1.504 1.538 1.473 0.050  -0.063 0.065  29  PHE HHH N   
8590  C CA  . PHE G 30  ? 1.523 1.525 1.446 0.056  -0.050 0.036  29  PHE HHH CA  
8591  C C   . PHE G 30  ? 1.529 1.502 1.421 0.075  -0.038 0.024  29  PHE HHH C   
8592  O O   . PHE G 30  ? 1.539 1.501 1.407 0.082  -0.015 0.005  29  PHE HHH O   
8593  C CB  . PHE G 30  ? 1.560 1.531 1.453 0.046  -0.085 0.032  29  PHE HHH CB  
8594  C CG  . PHE G 30  ? 1.582 1.527 1.434 0.055  -0.072 0.006  29  PHE HHH CG  
8595  C CD1 . PHE G 30  ? 1.585 1.549 1.446 0.047  -0.054 -0.001 29  PHE HHH CD1 
8596  C CD2 . PHE G 30  ? 1.605 1.510 1.408 0.073  -0.077 -0.007 29  PHE HHH CD2 
8597  C CE1 . PHE G 30  ? 1.594 1.540 1.423 0.055  -0.043 -0.020 29  PHE HHH CE1 
8598  C CE2 . PHE G 30  ? 1.622 1.512 1.393 0.083  -0.063 -0.025 29  PHE HHH CE2 
8599  C CZ  . PHE G 30  ? 1.612 1.524 1.399 0.074  -0.047 -0.031 29  PHE HHH CZ  
8600  N N   . ILE G 31  ? 1.546 1.511 1.441 0.080  -0.054 0.037  30  ILE HHH N   
8601  C CA  . ILE G 31  ? 1.550 1.485 1.410 0.097  -0.050 0.029  30  ILE HHH CA  
8602  C C   . ILE G 31  ? 1.512 1.459 1.382 0.106  -0.009 0.021  30  ILE HHH C   
8603  O O   . ILE G 31  ? 1.508 1.434 1.345 0.117  0.002  0.011  30  ILE HHH O   
8604  C CB  . ILE G 31  ? 1.568 1.495 1.433 0.098  -0.078 0.049  30  ILE HHH CB  
8605  C CG1 . ILE G 31  ? 1.599 1.491 1.419 0.115  -0.077 0.042  30  ILE HHH CG1 
8606  C CG2 . ILE G 31  ? 1.544 1.515 1.470 0.096  -0.065 0.070  30  ILE HHH CG2 
8607  C CD1 . ILE G 31  ? 1.643 1.494 1.399 0.123  -0.089 0.024  30  ILE HHH CD1 
8608  N N   . THR G 32  ? 1.487 1.466 1.398 0.104  0.013  0.026  31  THR HHH N   
8609  C CA  . THR G 32  ? 1.507 1.488 1.425 0.113  0.047  0.019  31  THR HHH CA  
8610  C C   . THR G 32  ? 1.541 1.518 1.442 0.108  0.066  0.000  31  THR HHH C   
8611  O O   . THR G 32  ? 1.584 1.551 1.481 0.113  0.088  -0.008 31  THR HHH O   
8612  C CB  . THR G 32  ? 1.491 1.503 1.452 0.118  0.064  0.029  31  THR HHH CB  
8613  O OG1 . THR G 32  ? 1.458 1.493 1.430 0.110  0.073  0.025  31  THR HHH OG1 
8614  C CG2 . THR G 32  ? 1.513 1.544 1.505 0.121  0.044  0.054  31  THR HHH CG2 
8615  N N   . TYR G 33  ? 1.539 1.521 1.432 0.096  0.054  -0.005 32  TYR HHH N   
8616  C CA  . TYR G 33  ? 1.508 1.493 1.393 0.088  0.068  -0.020 32  TYR HHH CA  
8617  C C   . TYR G 33  ? 1.467 1.432 1.320 0.091  0.070  -0.030 32  TYR HHH C   
8618  O O   . TYR G 33  ? 1.476 1.424 1.305 0.098  0.053  -0.028 32  TYR HHH O   
8619  C CB  . TYR G 33  ? 1.532 1.534 1.425 0.075  0.052  -0.017 32  TYR HHH CB  
8620  C CG  . TYR G 33  ? 1.553 1.589 1.480 0.070  0.063  -0.008 32  TYR HHH CG  
8621  C CD1 . TYR G 33  ? 1.572 1.631 1.531 0.072  0.054  0.013  32  TYR HHH CD1 
8622  C CD2 . TYR G 33  ? 1.560 1.608 1.486 0.066  0.084  -0.018 32  TYR HHH CD2 
8623  C CE1 . TYR G 33  ? 1.578 1.677 1.569 0.073  0.069  0.025  32  TYR HHH CE1 
8624  C CE2 . TYR G 33  ? 1.578 1.657 1.528 0.067  0.099  -0.010 32  TYR HHH CE2 
8625  C CZ  . TYR G 33  ? 1.589 1.697 1.573 0.072  0.093  0.013  32  TYR HHH CZ  
8626  O OH  . TYR G 33  ? 1.621 1.768 1.630 0.078  0.111  0.024  32  TYR HHH OH  
8627  N N   . TRP G 34  ? 1.436 1.401 1.286 0.087  0.091  -0.039 33  TRP HHH N   
8628  C CA  . TRP G 34  ? 1.444 1.401 1.274 0.087  0.096  -0.044 33  TRP HHH CA  
8629  C C   . TRP G 34  ? 1.405 1.373 1.235 0.074  0.097  -0.053 33  TRP HHH C   
8630  O O   . TRP G 34  ? 1.431 1.405 1.273 0.064  0.108  -0.058 33  TRP HHH O   
8631  C CB  . TRP G 34  ? 1.465 1.414 1.297 0.087  0.114  -0.043 33  TRP HHH CB  
8632  C CG  . TRP G 34  ? 1.483 1.420 1.314 0.099  0.115  -0.033 33  TRP HHH CG  
8633  C CD1 . TRP G 34  ? 1.514 1.449 1.359 0.106  0.110  -0.027 33  TRP HHH CD1 
8634  C CD2 . TRP G 34  ? 1.500 1.429 1.321 0.104  0.122  -0.024 33  TRP HHH CD2 
8635  N NE1 . TRP G 34  ? 1.539 1.462 1.379 0.116  0.112  -0.017 33  TRP HHH NE1 
8636  C CE2 . TRP G 34  ? 1.531 1.451 1.356 0.115  0.120  -0.015 33  TRP HHH CE2 
8637  C CE3 . TRP G 34  ? 1.522 1.458 1.335 0.101  0.130  -0.018 33  TRP HHH CE3 
8638  C CZ2 . TRP G 34  ? 1.574 1.486 1.391 0.121  0.125  -0.002 33  TRP HHH CZ2 
8639  C CZ3 . TRP G 34  ? 1.565 1.499 1.373 0.108  0.136  -0.003 33  TRP HHH CZ3 
8640  C CH2 . TRP G 34  ? 1.590 1.510 1.398 0.117  0.134  0.005  33  TRP HHH CH2 
8641  N N   . ILE G 35  ? 1.363 1.331 1.177 0.076  0.084  -0.054 34  ILE HHH N   
8642  C CA  . ILE G 35  ? 1.342 1.320 1.157 0.064  0.081  -0.059 34  ILE HHH CA  
8643  C C   . ILE G 35  ? 1.336 1.320 1.148 0.062  0.095  -0.060 34  ILE HHH C   
8644  O O   . ILE G 35  ? 1.288 1.270 1.084 0.077  0.095  -0.055 34  ILE HHH O   
8645  C CB  . ILE G 35  ? 1.381 1.352 1.183 0.068  0.058  -0.060 34  ILE HHH CB  
8646  C CG1 . ILE G 35  ? 1.404 1.377 1.220 0.061  0.041  -0.054 34  ILE HHH CG1 
8647  C CG2 . ILE G 35  ? 1.399 1.380 1.200 0.059  0.056  -0.064 34  ILE HHH CG2 
8648  C CD1 . ILE G 35  ? 1.450 1.408 1.260 0.072  0.030  -0.047 34  ILE HHH CD1 
8649  N N   . GLY G 36  ? 1.367 1.358 1.190 0.046  0.104  -0.064 35  GLY HHH N   
8650  C CA  . GLY G 36  ? 1.369 1.370 1.194 0.036  0.111  -0.061 35  GLY HHH CA  
8651  C C   . GLY G 36  ? 1.362 1.376 1.187 0.029  0.101  -0.063 35  GLY HHH C   
8652  O O   . GLY G 36  ? 1.359 1.372 1.182 0.027  0.090  -0.068 35  GLY HHH O   
8653  N N   . TRP G 37  ? 1.369 1.397 1.199 0.024  0.104  -0.056 36  TRP HHH N   
8654  C CA  . TRP G 37  ? 1.375 1.418 1.208 0.015  0.096  -0.055 36  TRP HHH CA  
8655  C C   . TRP G 37  ? 1.394 1.444 1.238 -0.008 0.099  -0.052 36  TRP HHH C   
8656  O O   . TRP G 37  ? 1.412 1.465 1.265 -0.012 0.107  -0.042 36  TRP HHH O   
8657  C CB  . TRP G 37  ? 1.374 1.429 1.203 0.036  0.094  -0.047 36  TRP HHH CB  
8658  C CG  . TRP G 37  ? 1.370 1.407 1.178 0.058  0.083  -0.053 36  TRP HHH CG  
8659  C CD1 . TRP G 37  ? 1.396 1.419 1.187 0.078  0.085  -0.052 36  TRP HHH CD1 
8660  C CD2 . TRP G 37  ? 1.378 1.403 1.177 0.058  0.064  -0.059 36  TRP HHH CD2 
8661  N NE1 . TRP G 37  ? 1.421 1.419 1.189 0.092  0.066  -0.060 36  TRP HHH NE1 
8662  C CE2 . TRP G 37  ? 1.414 1.413 1.188 0.079  0.052  -0.063 36  TRP HHH CE2 
8663  C CE3 . TRP G 37  ? 1.392 1.423 1.199 0.042  0.053  -0.061 36  TRP HHH CE3 
8664  C CZ2 . TRP G 37  ? 1.458 1.435 1.218 0.083  0.027  -0.068 36  TRP HHH CZ2 
8665  C CZ3 . TRP G 37  ? 1.421 1.435 1.217 0.046  0.031  -0.064 36  TRP HHH CZ3 
8666  C CH2 . TRP G 37  ? 1.457 1.442 1.230 0.065  0.017  -0.067 36  TRP HHH CH2 
8667  N N   . VAL G 38  ? 1.397 1.451 1.241 -0.024 0.091  -0.057 37  VAL HHH N   
8668  C CA  . VAL G 38  ? 1.394 1.447 1.240 -0.049 0.089  -0.056 37  VAL HHH CA  
8669  C C   . VAL G 38  ? 1.400 1.476 1.254 -0.057 0.077  -0.049 37  VAL HHH C   
8670  O O   . VAL G 38  ? 1.407 1.486 1.256 -0.051 0.070  -0.054 37  VAL HHH O   
8671  C CB  . VAL G 38  ? 1.394 1.424 1.222 -0.060 0.090  -0.071 37  VAL HHH CB  
8672  C CG1 . VAL G 38  ? 1.436 1.455 1.255 -0.085 0.083  -0.073 37  VAL HHH CG1 
8673  C CG2 . VAL G 38  ? 1.402 1.410 1.225 -0.048 0.101  -0.077 37  VAL HHH CG2 
8674  N N   . ARG G 39  ? 1.422 1.513 1.291 -0.071 0.074  -0.035 38  ARG HHH N   
8675  C CA  . ARG G 39  ? 1.440 1.556 1.322 -0.082 0.062  -0.025 38  ARG HHH CA  
8676  C C   . ARG G 39  ? 1.456 1.557 1.326 -0.113 0.051  -0.031 38  ARG HHH C   
8677  O O   . ARG G 39  ? 1.483 1.569 1.350 -0.129 0.049  -0.029 38  ARG HHH O   
8678  C CB  . ARG G 39  ? 1.470 1.619 1.380 -0.076 0.064  0.000  38  ARG HHH CB  
8679  C CG  . ARG G 39  ? 1.501 1.680 1.429 -0.083 0.052  0.013  38  ARG HHH CG  
8680  C CD  . ARG G 39  ? 1.524 1.747 1.485 -0.070 0.058  0.042  38  ARG HHH CD  
8681  N NE  . ARG G 39  ? 1.566 1.804 1.551 -0.094 0.057  0.063  38  ARG HHH NE  
8682  C CZ  . ARG G 39  ? 1.660 1.946 1.683 -0.090 0.061  0.095  38  ARG HHH CZ  
8683  N NH1 . ARG G 39  ? 1.694 2.017 1.731 -0.058 0.071  0.108  38  ARG HHH NH1 
8684  N NH2 . ARG G 39  ? 1.713 2.011 1.760 -0.118 0.054  0.117  38  ARG HHH NH2 
8685  N N   . GLN G 40  ? 1.454 1.556 1.312 -0.120 0.041  -0.038 39  GLN HHH N   
8686  C CA  . GLN G 40  ? 1.482 1.576 1.326 -0.148 0.028  -0.040 39  GLN HHH CA  
8687  C C   . GLN G 40  ? 1.473 1.599 1.340 -0.154 0.014  -0.022 39  GLN HHH C   
8688  O O   . GLN G 40  ? 1.428 1.566 1.297 -0.142 0.012  -0.022 39  GLN HHH O   
8689  C CB  . GLN G 40  ? 1.496 1.570 1.307 -0.149 0.030  -0.058 39  GLN HHH CB  
8690  C CG  . GLN G 40  ? 1.531 1.593 1.317 -0.174 0.017  -0.063 39  GLN HHH CG  
8691  C CD  . GLN G 40  ? 1.571 1.607 1.316 -0.172 0.026  -0.082 39  GLN HHH CD  
8692  O OE1 . GLN G 40  ? 1.585 1.634 1.326 -0.163 0.032  -0.084 39  GLN HHH OE1 
8693  N NE2 . GLN G 40  ? 1.602 1.601 1.317 -0.180 0.026  -0.094 39  GLN HHH NE2 
8694  N N   . MET G 41  ? 1.498 1.639 1.385 -0.172 0.004  -0.004 40  MET HHH N   
8695  C CA  . MET G 41  ? 1.537 1.715 1.451 -0.178 -0.009 0.017  40  MET HHH CA  
8696  C C   . MET G 41  ? 1.608 1.775 1.499 -0.201 -0.027 0.010  40  MET HHH C   
8697  O O   . MET G 41  ? 1.712 1.844 1.565 -0.216 -0.029 -0.008 40  MET HHH O   
8698  C CB  . MET G 41  ? 1.525 1.729 1.474 -0.191 -0.015 0.044  40  MET HHH CB  
8699  C CG  . MET G 41  ? 1.486 1.729 1.471 -0.162 0.000  0.064  40  MET HHH CG  
8700  S SD  . MET G 41  ? 1.501 1.778 1.529 -0.179 -0.003 0.099  40  MET HHH SD  
8701  C CE  . MET G 41  ? 1.508 1.854 1.583 -0.148 0.008  0.132  40  MET HHH CE  
8702  N N   . PRO G 42  ? 1.596 1.791 1.505 -0.204 -0.040 0.025  41  PRO HHH N   
8703  C CA  . PRO G 42  ? 1.607 1.795 1.495 -0.227 -0.058 0.022  41  PRO HHH CA  
8704  C C   . PRO G 42  ? 1.655 1.813 1.511 -0.259 -0.071 0.015  41  PRO HHH C   
8705  O O   . PRO G 42  ? 1.612 1.781 1.488 -0.279 -0.087 0.033  41  PRO HHH O   
8706  C CB  . PRO G 42  ? 1.610 1.838 1.536 -0.227 -0.072 0.048  41  PRO HHH CB  
8707  C CG  . PRO G 42  ? 1.581 1.831 1.537 -0.191 -0.056 0.056  41  PRO HHH CG  
8708  C CD  . PRO G 42  ? 1.585 1.820 1.536 -0.182 -0.038 0.047  41  PRO HHH CD  
8709  N N   . GLY G 43  ? 1.713 1.835 1.521 -0.261 -0.065 -0.010 42  GLY HHH N   
8710  C CA  . GLY G 43  ? 1.797 1.878 1.557 -0.286 -0.078 -0.023 42  GLY HHH CA  
8711  C C   . GLY G 43  ? 1.813 1.867 1.572 -0.294 -0.080 -0.024 42  GLY HHH C   
8712  O O   . GLY G 43  ? 1.897 1.925 1.637 -0.323 -0.104 -0.021 42  GLY HHH O   
8713  N N   . LYS G 44  ? 1.750 1.805 1.528 -0.271 -0.059 -0.027 43  LYS HHH N   
8714  C CA  . LYS G 44  ? 1.760 1.794 1.545 -0.277 -0.059 -0.024 43  LYS HHH CA  
8715  C C   . LYS G 44  ? 1.753 1.751 1.508 -0.255 -0.037 -0.049 43  LYS HHH C   
8716  O O   . LYS G 44  ? 1.701 1.701 1.439 -0.235 -0.021 -0.064 43  LYS HHH O   
8717  C CB  . LYS G 44  ? 1.740 1.822 1.587 -0.268 -0.054 0.004  43  LYS HHH CB  
8718  C CG  . LYS G 44  ? 1.729 1.861 1.617 -0.277 -0.068 0.033  43  LYS HHH CG  
8719  C CD  . LYS G 44  ? 1.763 1.895 1.662 -0.315 -0.098 0.054  43  LYS HHH CD  
8720  C CE  . LYS G 44  ? 1.739 1.938 1.702 -0.315 -0.104 0.093  43  LYS HHH CE  
8721  N NZ  . LYS G 44  ? 1.800 2.004 1.772 -0.355 -0.139 0.114  43  LYS HHH NZ  
8722  N N   . GLY G 45  ? 1.776 1.748 1.533 -0.258 -0.037 -0.049 44  GLY HHH N   
8723  C CA  . GLY G 45  ? 1.764 1.701 1.497 -0.237 -0.018 -0.069 44  GLY HHH CA  
8724  C C   . GLY G 45  ? 1.662 1.634 1.432 -0.208 0.005  -0.062 44  GLY HHH C   
8725  O O   . GLY G 45  ? 1.605 1.625 1.413 -0.202 0.007  -0.044 44  GLY HHH O   
8726  N N   . LEU G 46  ? 1.636 1.582 1.391 -0.189 0.022  -0.077 45  LEU HHH N   
8727  C CA  . LEU G 46  ? 1.608 1.577 1.387 -0.161 0.042  -0.075 45  LEU HHH CA  
8728  C C   . LEU G 46  ? 1.616 1.591 1.425 -0.161 0.043  -0.056 45  LEU HHH C   
8729  O O   . LEU G 46  ? 1.696 1.633 1.491 -0.172 0.038  -0.059 45  LEU HHH O   
8730  C CB  . LEU G 46  ? 1.619 1.559 1.368 -0.142 0.058  -0.097 45  LEU HHH CB  
8731  C CG  . LEU G 46  ? 1.635 1.574 1.354 -0.140 0.061  -0.111 45  LEU HHH CG  
8732  C CD1 . LEU G 46  ? 1.660 1.576 1.354 -0.118 0.079  -0.129 45  LEU HHH CD1 
8733  C CD2 . LEU G 46  ? 1.576 1.561 1.320 -0.134 0.061  -0.101 45  LEU HHH CD2 
8734  N N   . GLU G 47  ? 1.579 1.599 1.424 -0.148 0.050  -0.037 46  GLU HHH N   
8735  C CA  . GLU G 47  ? 1.575 1.612 1.449 -0.143 0.056  -0.016 46  GLU HHH CA  
8736  C C   . GLU G 47  ? 1.528 1.567 1.399 -0.111 0.075  -0.024 46  GLU HHH C   
8737  O O   . GLU G 47  ? 1.495 1.554 1.367 -0.093 0.080  -0.028 46  GLU HHH O   
8738  C CB  . GLU G 47  ? 1.606 1.694 1.518 -0.147 0.052  0.013  46  GLU HHH CB  
8739  C CG  . GLU G 47  ? 1.671 1.764 1.587 -0.177 0.030  0.022  46  GLU HHH CG  
8740  C CD  . GLU G 47  ? 1.662 1.814 1.618 -0.174 0.028  0.049  46  GLU HHH CD  
8741  O OE1 . GLU G 47  ? 1.667 1.855 1.659 -0.172 0.032  0.079  46  GLU HHH OE1 
8742  O OE2 . GLU G 47  ? 1.671 1.834 1.622 -0.173 0.022  0.043  46  GLU HHH OE2 
8743  N N   . TRP G 48  ? 1.532 1.548 1.400 -0.106 0.082  -0.024 47  TRP HHH N   
8744  C CA  . TRP G 48  ? 1.515 1.534 1.383 -0.077 0.098  -0.026 47  TRP HHH CA  
8745  C C   . TRP G 48  ? 1.454 1.515 1.347 -0.064 0.105  -0.001 47  TRP HHH C   
8746  O O   . TRP G 48  ? 1.428 1.502 1.342 -0.077 0.102  0.021  47  TRP HHH O   
8747  C CB  . TRP G 48  ? 1.594 1.575 1.450 -0.076 0.102  -0.034 47  TRP HHH CB  
8748  C CG  . TRP G 48  ? 1.623 1.605 1.477 -0.049 0.115  -0.036 47  TRP HHH CG  
8749  C CD1 . TRP G 48  ? 1.640 1.614 1.481 -0.033 0.120  -0.053 47  TRP HHH CD1 
8750  C CD2 . TRP G 48  ? 1.639 1.633 1.506 -0.037 0.122  -0.018 47  TRP HHH CD2 
8751  N NE1 . TRP G 48  ? 1.634 1.610 1.478 -0.012 0.127  -0.047 47  TRP HHH NE1 
8752  C CE2 . TRP G 48  ? 1.635 1.621 1.491 -0.014 0.130  -0.027 47  TRP HHH CE2 
8753  C CE3 . TRP G 48  ? 1.679 1.691 1.567 -0.045 0.123  0.009  47  TRP HHH CE3 
8754  C CZ2 . TRP G 48  ? 1.655 1.648 1.513 0.003  0.137  -0.015 47  TRP HHH CZ2 
8755  C CZ3 . TRP G 48  ? 1.696 1.719 1.588 -0.027 0.133  0.023  47  TRP HHH CZ3 
8756  C CH2 . TRP G 48  ? 1.685 1.696 1.560 -0.003 0.140  0.010  47  TRP HHH CH2 
8757  N N   . MET G 49  ? 1.429 1.508 1.318 -0.038 0.111  -0.004 48  MET HHH N   
8758  C CA  . MET G 49  ? 1.445 1.561 1.347 -0.017 0.120  0.017  48  MET HHH CA  
8759  C C   . MET G 49  ? 1.449 1.561 1.345 0.003  0.132  0.023  48  MET HHH C   
8760  O O   . MET G 49  ? 1.437 1.575 1.350 0.005  0.141  0.048  48  MET HHH O   
8761  C CB  . MET G 49  ? 1.442 1.568 1.334 0.003  0.117  0.007  48  MET HHH CB  
8762  C CG  . MET G 49  ? 1.427 1.559 1.324 -0.015 0.104  0.003  48  MET HHH CG  
8763  S SD  . MET G 49  ? 1.403 1.543 1.289 0.010  0.098  -0.004 48  MET HHH SD  
8764  C CE  . MET G 49  ? 1.399 1.584 1.304 0.034  0.109  0.024  48  MET HHH CE  
8765  N N   . GLY G 50  ? 1.456 1.538 1.329 0.016  0.132  0.003  49  GLY HHH N   
8766  C CA  . GLY G 50  ? 1.464 1.538 1.324 0.038  0.141  0.006  49  GLY HHH CA  
8767  C C   . GLY G 50  ? 1.464 1.507 1.305 0.047  0.135  -0.015 49  GLY HHH C   
8768  O O   . GLY G 50  ? 1.444 1.480 1.280 0.041  0.126  -0.030 49  GLY HHH O   
8769  N N   . ILE G 51  ? 1.482 1.510 1.313 0.059  0.139  -0.013 50  ILE HHH N   
8770  C CA  . ILE G 51  ? 1.496 1.501 1.314 0.068  0.133  -0.027 50  ILE HHH CA  
8771  C C   . ILE G 51  ? 1.500 1.503 1.296 0.094  0.132  -0.021 50  ILE HHH C   
8772  O O   . ILE G 51  ? 1.480 1.497 1.275 0.103  0.143  -0.005 50  ILE HHH O   
8773  C CB  . ILE G 51  ? 1.534 1.518 1.361 0.057  0.136  -0.031 50  ILE HHH CB  
8774  C CG1 . ILE G 51  ? 1.597 1.567 1.420 0.064  0.129  -0.043 50  ILE HHH CG1 
8775  C CG2 . ILE G 51  ? 1.530 1.510 1.361 0.060  0.144  -0.015 50  ILE HHH CG2 
8776  C CD1 . ILE G 51  ? 1.649 1.606 1.481 0.053  0.133  -0.053 50  ILE HHH CD1 
8777  N N   . ILE G 52  ? 1.509 1.495 1.288 0.105  0.119  -0.032 51  ILE HHH N   
8778  C CA  . ILE G 52  ? 1.527 1.498 1.277 0.129  0.112  -0.029 51  ILE HHH CA  
8779  C C   . ILE G 52  ? 1.532 1.482 1.284 0.125  0.099  -0.034 51  ILE HHH C   
8780  O O   . ILE G 52  ? 1.540 1.490 1.310 0.111  0.091  -0.042 51  ILE HHH O   
8781  C CB  . ILE G 52  ? 1.539 1.503 1.257 0.148  0.100  -0.035 51  ILE HHH CB  
8782  C CG1 . ILE G 52  ? 1.576 1.520 1.252 0.176  0.095  -0.033 51  ILE HHH CG1 
8783  C CG2 . ILE G 52  ? 1.545 1.494 1.265 0.137  0.079  -0.048 51  ILE HHH CG2 
8784  C CD1 . ILE G 52  ? 1.633 1.566 1.269 0.202  0.088  -0.038 51  ILE HHH CD1 
8785  N N   . TYR G 53  ? 1.539 1.477 1.276 0.138  0.098  -0.027 52  TYR HHH N   
8786  C CA  . TYR G 53  ? 1.527 1.448 1.264 0.139  0.081  -0.027 52  TYR HHH CA  
8787  C C   . TYR G 53  ? 1.525 1.423 1.221 0.156  0.058  -0.031 52  TYR HHH C   
8788  O O   . TYR G 53  ? 1.548 1.434 1.210 0.176  0.058  -0.027 52  TYR HHH O   
8789  C CB  . TYR G 53  ? 1.532 1.451 1.279 0.142  0.091  -0.016 52  TYR HHH CB  
8790  C CG  . TYR G 53  ? 1.546 1.451 1.295 0.144  0.073  -0.012 52  TYR HHH CG  
8791  C CD1 . TYR G 53  ? 1.545 1.455 1.320 0.133  0.062  -0.016 52  TYR HHH CD1 
8792  C CD2 . TYR G 53  ? 1.569 1.460 1.295 0.158  0.066  -0.003 52  TYR HHH CD2 
8793  C CE1 . TYR G 53  ? 1.532 1.437 1.317 0.134  0.044  -0.007 52  TYR HHH CE1 
8794  C CE2 . TYR G 53  ? 1.586 1.466 1.317 0.159  0.045  0.003  52  TYR HHH CE2 
8795  C CZ  . TYR G 53  ? 1.551 1.440 1.315 0.146  0.034  0.002  52  TYR HHH CZ  
8796  O OH  . TYR G 53  ? 1.546 1.432 1.323 0.145  0.013  0.013  52  TYR HHH OH  
8797  N N   . PRO G 54  ? 1.501 1.389 1.197 0.149  0.035  -0.039 53  PRO HHH N   
8798  C CA  . PRO G 54  ? 1.560 1.413 1.211 0.163  0.006  -0.045 53  PRO HHH CA  
8799  C C   . PRO G 54  ? 1.647 1.475 1.266 0.178  -0.007 -0.039 53  PRO HHH C   
8800  O O   . PRO G 54  ? 1.708 1.505 1.272 0.199  -0.021 -0.045 53  PRO HHH O   
8801  C CB  . PRO G 54  ? 1.539 1.390 1.213 0.143  -0.019 -0.045 53  PRO HHH CB  
8802  C CG  . PRO G 54  ? 1.491 1.378 1.211 0.124  0.003  -0.045 53  PRO HHH CG  
8803  C CD  . PRO G 54  ? 1.465 1.370 1.200 0.127  0.034  -0.041 53  PRO HHH CD  
8804  N N   . GLY G 55  ? 1.662 1.502 1.312 0.168  -0.003 -0.028 54  GLY HHH N   
8805  C CA  . GLY G 55  ? 1.722 1.542 1.350 0.178  -0.018 -0.019 54  GLY HHH CA  
8806  C C   . GLY G 55  ? 1.795 1.599 1.368 0.204  -0.009 -0.020 54  GLY HHH C   
8807  O O   . GLY G 55  ? 1.892 1.658 1.410 0.220  -0.035 -0.026 54  GLY HHH O   
8808  N N   . ASP G 56  ? 1.808 1.638 1.393 0.209  0.024  -0.012 55  ASP HHH N   
8809  C CA  . ASP G 56  ? 1.877 1.706 1.415 0.235  0.039  -0.006 55  ASP HHH CA  
8810  C C   . ASP G 56  ? 1.843 1.697 1.384 0.242  0.063  -0.009 55  ASP HHH C   
8811  O O   . ASP G 56  ? 1.921 1.794 1.445 0.259  0.086  0.003  55  ASP HHH O   
8812  C CB  . ASP G 56  ? 1.916 1.759 1.468 0.235  0.055  0.013  55  ASP HHH CB  
8813  C CG  . ASP G 56  ? 1.907 1.781 1.520 0.213  0.079  0.022  55  ASP HHH CG  
8814  O OD1 . ASP G 56  ? 1.907 1.796 1.550 0.199  0.087  0.014  55  ASP HHH OD1 
8815  O OD2 . ASP G 56  ? 1.956 1.835 1.585 0.210  0.086  0.037  55  ASP HHH OD2 
8816  N N   . SER G 57  ? 1.762 1.619 1.323 0.229  0.057  -0.021 56  SER HHH N   
8817  C CA  . SER G 57  ? 1.733 1.614 1.301 0.233  0.075  -0.023 56  SER HHH CA  
8818  C C   . SER G 57  ? 1.691 1.614 1.289 0.229  0.108  -0.004 56  SER HHH C   
8819  O O   . SER G 57  ? 1.682 1.628 1.268 0.246  0.126  0.004  56  SER HHH O   
8820  C CB  . SER G 57  ? 1.786 1.644 1.293 0.266  0.066  -0.033 56  SER HHH CB  
8821  O OG  . SER G 57  ? 1.813 1.624 1.293 0.265  0.030  -0.049 56  SER HHH OG  
8822  N N   . GLU G 58  ? 1.675 1.607 1.313 0.207  0.114  0.004  57  GLU HHH N   
8823  C CA  . GLU G 58  ? 1.667 1.628 1.340 0.194  0.138  0.023  57  GLU HHH CA  
8824  C C   . GLU G 58  ? 1.637 1.620 1.344 0.175  0.144  0.019  57  GLU HHH C   
8825  O O   . GLU G 58  ? 1.665 1.637 1.396 0.154  0.136  0.006  57  GLU HHH O   
8826  C CB  . GLU G 58  ? 1.664 1.615 1.363 0.178  0.136  0.029  57  GLU HHH CB  
8827  C CG  . GLU G 58  ? 1.635 1.603 1.372 0.159  0.152  0.045  57  GLU HHH CG  
8828  C CD  . GLU G 58  ? 1.651 1.601 1.407 0.149  0.150  0.051  57  GLU HHH CD  
8829  O OE1 . GLU G 58  ? 1.637 1.566 1.389 0.153  0.136  0.041  57  GLU HHH OE1 
8830  O OE2 . GLU G 58  ? 1.661 1.617 1.439 0.136  0.159  0.068  57  GLU HHH OE2 
8831  N N   . THR G 59  ? 1.636 1.649 1.345 0.182  0.159  0.031  58  THR HHH N   
8832  C CA  . THR G 59  ? 1.619 1.653 1.353 0.167  0.162  0.029  58  THR HHH CA  
8833  C C   . THR G 59  ? 1.586 1.650 1.360 0.146  0.176  0.051  58  THR HHH C   
8834  O O   . THR G 59  ? 1.632 1.718 1.405 0.155  0.190  0.076  58  THR HHH O   
8835  C CB  . THR G 59  ? 1.678 1.724 1.384 0.195  0.165  0.027  58  THR HHH CB  
8836  O OG1 . THR G 59  ? 1.709 1.719 1.367 0.219  0.149  0.011  58  THR HHH OG1 
8837  C CG2 . THR G 59  ? 1.683 1.740 1.409 0.183  0.160  0.018  58  THR HHH CG2 
8838  N N   . ARG G 60  ? 1.521 1.583 1.325 0.117  0.171  0.045  59  ARG HHH N   
8839  C CA  . ARG G 60  ? 1.519 1.602 1.359 0.091  0.177  0.066  59  ARG HHH CA  
8840  C C   . ARG G 60  ? 1.498 1.600 1.355 0.078  0.173  0.062  59  ARG HHH C   
8841  O O   . ARG G 60  ? 1.517 1.600 1.362 0.077  0.163  0.038  59  ARG HHH O   
8842  C CB  . ARG G 60  ? 1.513 1.563 1.366 0.067  0.170  0.060  59  ARG HHH CB  
8843  C CG  . ARG G 60  ? 1.549 1.577 1.388 0.081  0.171  0.061  59  ARG HHH CG  
8844  C CD  . ARG G 60  ? 1.568 1.563 1.421 0.062  0.166  0.060  59  ARG HHH CD  
8845  N NE  . ARG G 60  ? 1.599 1.573 1.438 0.078  0.165  0.057  59  ARG HHH NE  
8846  C CZ  . ARG G 60  ? 1.651 1.592 1.497 0.071  0.160  0.052  59  ARG HHH CZ  
8847  N NH1 . ARG G 60  ? 1.672 1.590 1.531 0.051  0.156  0.045  59  ARG HHH NH1 
8848  N NH2 . ARG G 60  ? 1.698 1.626 1.534 0.087  0.159  0.053  59  ARG HHH NH2 
8849  N N   . TYR G 61  ? 1.502 1.643 1.386 0.068  0.180  0.089  60  TYR HHH N   
8850  C CA  . TYR G 61  ? 1.496 1.661 1.401 0.054  0.175  0.092  60  TYR HHH CA  
8851  C C   . TYR G 61  ? 1.469 1.632 1.406 0.014  0.165  0.107  60  TYR HHH C   
8852  O O   . TYR G 61  ? 1.448 1.609 1.398 0.003  0.166  0.126  60  TYR HHH O   
8853  C CB  . TYR G 61  ? 1.546 1.763 1.456 0.079  0.189  0.116  60  TYR HHH CB  
8854  C CG  . TYR G 61  ? 1.592 1.801 1.461 0.120  0.194  0.098  60  TYR HHH CG  
8855  C CD1 . TYR G 61  ? 1.597 1.781 1.448 0.125  0.181  0.070  60  TYR HHH CD1 
8856  C CD2 . TYR G 61  ? 1.658 1.880 1.503 0.154  0.209  0.110  60  TYR HHH CD2 
8857  C CE1 . TYR G 61  ? 1.639 1.805 1.448 0.160  0.179  0.055  60  TYR HHH CE1 
8858  C CE2 . TYR G 61  ? 1.697 1.899 1.494 0.192  0.209  0.092  60  TYR HHH CE2 
8859  C CZ  . TYR G 61  ? 1.688 1.859 1.468 0.194  0.192  0.064  60  TYR HHH CZ  
8860  O OH  . TYR G 61  ? 1.761 1.903 1.490 0.230  0.186  0.046  60  TYR HHH OH  
8861  N N   . SER G 62  ? 1.474 1.635 1.421 -0.007 0.153  0.097  61  SER HHH N   
8862  C CA  . SER G 62  ? 1.529 1.696 1.506 -0.044 0.139  0.116  61  SER HHH CA  
8863  C C   . SER G 62  ? 1.544 1.776 1.557 -0.042 0.148  0.159  61  SER HHH C   
8864  O O   . SER G 62  ? 1.599 1.871 1.612 -0.012 0.162  0.165  61  SER HHH O   
8865  C CB  . SER G 62  ? 1.560 1.712 1.532 -0.063 0.124  0.096  61  SER HHH CB  
8866  O OG  . SER G 62  ? 1.598 1.762 1.598 -0.098 0.108  0.119  61  SER HHH OG  
8867  N N   . PRO G 63  ? 1.536 1.781 1.582 -0.071 0.140  0.193  62  PRO HHH N   
8868  C CA  . PRO G 63  ? 1.526 1.844 1.617 -0.072 0.148  0.242  62  PRO HHH CA  
8869  C C   . PRO G 63  ? 1.501 1.860 1.610 -0.069 0.146  0.246  62  PRO HHH C   
8870  O O   . PRO G 63  ? 1.483 1.909 1.619 -0.048 0.163  0.278  62  PRO HHH O   
8871  C CB  . PRO G 63  ? 1.554 1.861 1.677 -0.119 0.126  0.270  62  PRO HHH CB  
8872  C CG  . PRO G 63  ? 1.572 1.801 1.659 -0.125 0.117  0.239  62  PRO HHH CG  
8873  C CD  . PRO G 63  ? 1.550 1.741 1.593 -0.102 0.122  0.187  62  PRO HHH CD  
8874  N N   . SER G 64  ? 1.508 1.827 1.600 -0.087 0.127  0.215  63  SER HHH N   
8875  C CA  . SER G 64  ? 1.518 1.864 1.623 -0.090 0.120  0.214  63  SER HHH CA  
8876  C C   . SER G 64  ? 1.503 1.860 1.583 -0.045 0.138  0.193  63  SER HHH C   
8877  O O   . SER G 64  ? 1.543 1.911 1.626 -0.045 0.130  0.187  63  SER HHH O   
8878  C CB  . SER G 64  ? 1.548 1.841 1.636 -0.125 0.093  0.187  63  SER HHH CB  
8879  O OG  . SER G 64  ? 1.598 1.856 1.692 -0.162 0.074  0.196  63  SER HHH OG  
8880  N N   . PHE G 65  ? 1.477 1.824 1.528 -0.010 0.156  0.183  64  PHE HHH N   
8881  C CA  . PHE G 65  ? 1.448 1.793 1.466 0.034  0.168  0.161  64  PHE HHH CA  
8882  C C   . PHE G 65  ? 1.468 1.837 1.471 0.076  0.192  0.176  64  PHE HHH C   
8883  O O   . PHE G 65  ? 1.477 1.862 1.461 0.115  0.203  0.172  64  PHE HHH O   
8884  C CB  . PHE G 65  ? 1.412 1.692 1.390 0.030  0.155  0.116  64  PHE HHH CB  
8885  C CG  . PHE G 65  ? 1.392 1.656 1.377 -0.001 0.135  0.103  64  PHE HHH CG  
8886  C CD1 . PHE G 65  ? 1.380 1.666 1.371 0.007  0.130  0.104  64  PHE HHH CD1 
8887  C CD2 . PHE G 65  ? 1.400 1.627 1.382 -0.036 0.121  0.091  64  PHE HHH CD2 
8888  C CE1 . PHE G 65  ? 1.370 1.644 1.366 -0.022 0.111  0.093  64  PHE HHH CE1 
8889  C CE2 . PHE G 65  ? 1.397 1.609 1.378 -0.062 0.103  0.078  64  PHE HHH CE2 
8890  C CZ  . PHE G 65  ? 1.376 1.613 1.365 -0.057 0.098  0.081  64  PHE HHH CZ  
8891  N N   . GLN G 66  ? 1.474 1.844 1.483 0.069  0.200  0.193  65  GLN HHH N   
8892  C CA  . GLN G 66  ? 1.508 1.896 1.495 0.108  0.223  0.206  65  GLN HHH CA  
8893  C C   . GLN G 66  ? 1.512 1.932 1.480 0.156  0.239  0.208  65  GLN HHH C   
8894  O O   . GLN G 66  ? 1.521 1.901 1.436 0.189  0.239  0.177  65  GLN HHH O   
8895  C CB  . GLN G 66  ? 1.549 1.983 1.576 0.091  0.232  0.253  65  GLN HHH CB  
8896  C CG  . GLN G 66  ? 1.607 2.066 1.613 0.130  0.257  0.272  65  GLN HHH CG  
8897  C CD  . GLN G 66  ? 1.642 2.039 1.596 0.143  0.255  0.241  65  GLN HHH CD  
8898  O OE1 . GLN G 66  ? 1.662 2.012 1.617 0.112  0.239  0.224  65  GLN HHH OE1 
8899  N NE2 . GLN G 66  ? 1.662 2.061 1.570 0.191  0.271  0.234  65  GLN HHH NE2 
8900  N N   . GLY G 67  ? 1.514 2.002 1.524 0.161  0.249  0.244  66  GLY HHH N   
8901  C CA  . GLY G 67  ? 1.569 2.101 1.566 0.214  0.272  0.258  66  GLY HHH CA  
8902  C C   . GLY G 67  ? 1.583 2.110 1.579 0.223  0.261  0.241  66  GLY HHH C   
8903  O O   . GLY G 67  ? 1.598 2.177 1.606 0.259  0.278  0.263  66  GLY HHH O   
8904  N N   . GLN G 68  ? 1.598 2.067 1.582 0.194  0.235  0.204  67  GLN HHH N   
8905  C CA  . GLN G 68  ? 1.648 2.100 1.623 0.201  0.220  0.183  67  GLN HHH CA  
8906  C C   . GLN G 68  ? 1.690 2.074 1.598 0.233  0.213  0.141  67  GLN HHH C   
8907  O O   . GLN G 68  ? 1.751 2.134 1.627 0.281  0.221  0.136  67  GLN HHH O   
8908  C CB  . GLN G 68  ? 1.622 2.058 1.628 0.146  0.195  0.175  67  GLN HHH CB  
8909  C CG  . GLN G 68  ? 1.606 2.099 1.674 0.110  0.194  0.217  67  GLN HHH CG  
8910  C CD  . GLN G 68  ? 1.595 2.153 1.704 0.123  0.200  0.249  67  GLN HHH CD  
8911  O OE1 . GLN G 68  ? 1.574 2.122 1.685 0.116  0.184  0.236  67  GLN HHH OE1 
8912  N NE2 . GLN G 68  ? 1.584 2.213 1.727 0.143  0.223  0.293  67  GLN HHH NE2 
8913  N N   . VAL G 69  ? 1.653 1.983 1.539 0.209  0.199  0.114  68  VAL HHH N   
8914  C CA  . VAL G 69  ? 1.622 1.883 1.458 0.218  0.180  0.074  68  VAL HHH CA  
8915  C C   . VAL G 69  ? 1.628 1.854 1.424 0.232  0.184  0.062  68  VAL HHH C   
8916  O O   . VAL G 69  ? 1.619 1.862 1.433 0.217  0.195  0.078  68  VAL HHH O   
8917  C CB  . VAL G 69  ? 1.547 1.782 1.401 0.173  0.158  0.057  68  VAL HHH CB  
8918  C CG1 . VAL G 69  ? 1.530 1.802 1.422 0.157  0.153  0.071  68  VAL HHH CG1 
8919  C CG2 . VAL G 69  ? 1.508 1.734 1.379 0.136  0.157  0.057  68  VAL HHH CG2 
8920  N N   . THR G 70  ? 1.636 1.811 1.379 0.260  0.171  0.036  69  THR HHH N   
8921  C CA  . THR G 70  ? 1.651 1.782 1.348 0.274  0.166  0.021  69  THR HHH CA  
8922  C C   . THR G 70  ? 1.635 1.716 1.327 0.244  0.139  -0.005 69  THR HHH C   
8923  O O   . THR G 70  ? 1.629 1.684 1.312 0.243  0.119  -0.021 69  THR HHH O   
8924  C CB  . THR G 70  ? 1.712 1.821 1.348 0.329  0.170  0.014  69  THR HHH CB  
8925  O OG1 . THR G 70  ? 1.732 1.897 1.376 0.357  0.201  0.043  69  THR HHH OG1 
8926  C CG2 . THR G 70  ? 1.747 1.800 1.328 0.342  0.157  -0.004 69  THR HHH CG2 
8927  N N   . ILE G 71  ? 1.607 1.677 1.308 0.222  0.138  -0.006 70  ILE HHH N   
8928  C CA  . ILE G 71  ? 1.594 1.622 1.289 0.200  0.116  -0.026 70  ILE HHH CA  
8929  C C   . ILE G 71  ? 1.643 1.632 1.289 0.226  0.107  -0.035 70  ILE HHH C   
8930  O O   . ILE G 71  ? 1.628 1.627 1.268 0.235  0.122  -0.024 70  ILE HHH O   
8931  C CB  . ILE G 71  ? 1.559 1.600 1.294 0.164  0.122  -0.021 70  ILE HHH CB  
8932  C CG1 . ILE G 71  ? 1.538 1.609 1.313 0.137  0.126  -0.014 70  ILE HHH CG1 
8933  C CG2 . ILE G 71  ? 1.569 1.576 1.298 0.150  0.105  -0.036 70  ILE HHH CG2 
8934  C CD1 . ILE G 71  ? 1.520 1.599 1.325 0.106  0.133  -0.008 70  ILE HHH CD1 
8935  N N   . SER G 72  ? 1.703 1.648 1.314 0.237  0.080  -0.053 71  SER HHH N   
8936  C CA  . SER G 72  ? 1.765 1.662 1.324 0.258  0.061  -0.063 71  SER HHH CA  
8937  C C   . SER G 72  ? 1.714 1.585 1.287 0.228  0.035  -0.071 71  SER HHH C   
8938  O O   . SER G 72  ? 1.652 1.542 1.270 0.197  0.034  -0.070 71  SER HHH O   
8939  C CB  . SER G 72  ? 1.865 1.724 1.366 0.295  0.046  -0.075 71  SER HHH CB  
8940  O OG  . SER G 72  ? 1.858 1.726 1.377 0.291  0.041  -0.078 71  SER HHH OG  
8941  N N   . ALA G 73  ? 1.744 1.575 1.281 0.237  0.014  -0.076 72  ALA HHH N   
8942  C CA  . ALA G 73  ? 1.746 1.557 1.299 0.211  -0.013 -0.078 72  ALA HHH CA  
8943  C C   . ALA G 73  ? 1.824 1.577 1.319 0.228  -0.048 -0.086 72  ALA HHH C   
8944  O O   . ALA G 73  ? 1.874 1.614 1.335 0.249  -0.043 -0.084 72  ALA HHH O   
8945  C CB  . ALA G 73  ? 1.713 1.554 1.308 0.191  0.005  -0.067 72  ALA HHH CB  
8946  N N   . ASP G 74  ? 1.840 1.557 1.324 0.219  -0.084 -0.093 73  ASP HHH N   
8947  C CA  . ASP G 74  ? 1.917 1.571 1.352 0.225  -0.130 -0.099 73  ASP HHH CA  
8948  C C   . ASP G 74  ? 1.855 1.522 1.338 0.190  -0.147 -0.085 73  ASP HHH C   
8949  O O   . ASP G 74  ? 1.830 1.497 1.343 0.164  -0.171 -0.079 73  ASP HHH O   
8950  C CB  . ASP G 74  ? 2.005 1.609 1.404 0.233  -0.163 -0.111 73  ASP HHH CB  
8951  C CG  . ASP G 74  ? 2.116 1.638 1.441 0.250  -0.211 -0.122 73  ASP HHH CG  
8952  O OD1 . ASP G 74  ? 2.140 1.646 1.441 0.254  -0.219 -0.119 73  ASP HHH OD1 
8953  O OD2 . ASP G 74  ? 2.169 1.640 1.456 0.260  -0.242 -0.133 73  ASP HHH OD2 
8954  N N   . LYS G 75  ? 1.844 1.526 1.334 0.191  -0.135 -0.076 74  LYS HHH N   
8955  C CA  . LYS G 75  ? 1.818 1.525 1.361 0.162  -0.142 -0.060 74  LYS HHH CA  
8956  C C   . LYS G 75  ? 1.823 1.492 1.359 0.146  -0.195 -0.053 74  LYS HHH C   
8957  O O   . LYS G 75  ? 1.772 1.472 1.364 0.118  -0.203 -0.035 74  LYS HHH O   
8958  C CB  . LYS G 75  ? 1.855 1.575 1.396 0.173  -0.122 -0.053 74  LYS HHH CB  
8959  C CG  . LYS G 75  ? 1.967 1.633 1.439 0.195  -0.149 -0.057 74  LYS HHH CG  
8960  C CD  . LYS G 75  ? 2.007 1.691 1.488 0.199  -0.132 -0.045 74  LYS HHH CD  
8961  C CE  . LYS G 75  ? 2.128 1.761 1.552 0.211  -0.169 -0.043 74  LYS HHH CE  
8962  N NZ  . LYS G 75  ? 2.144 1.800 1.591 0.208  -0.156 -0.027 74  LYS HHH NZ  
8963  N N   . SER G 76  ? 1.884 1.487 1.352 0.163  -0.231 -0.065 75  SER HHH N   
8964  C CA  . SER G 76  ? 1.940 1.490 1.387 0.147  -0.292 -0.060 75  SER HHH CA  
8965  C C   . SER G 76  ? 1.900 1.459 1.388 0.118  -0.314 -0.051 75  SER HHH C   
8966  O O   . SER G 76  ? 1.936 1.459 1.421 0.097  -0.367 -0.039 75  SER HHH O   
8967  C CB  . SER G 76  ? 2.062 1.528 1.411 0.178  -0.325 -0.080 75  SER HHH CB  
8968  O OG  . SER G 76  ? 2.085 1.515 1.405 0.187  -0.338 -0.094 75  SER HHH OG  
8969  N N   . ILE G 77  ? 1.831 1.435 1.356 0.115  -0.278 -0.054 76  ILE HHH N   
8970  C CA  . ILE G 77  ? 1.800 1.428 1.374 0.084  -0.291 -0.041 76  ILE HHH CA  
8971  C C   . ILE G 77  ? 1.679 1.387 1.320 0.072  -0.240 -0.033 76  ILE HHH C   
8972  O O   . ILE G 77  ? 1.616 1.348 1.287 0.056  -0.236 -0.029 76  ILE HHH O   
8973  C CB  . ILE G 77  ? 1.877 1.456 1.408 0.095  -0.313 -0.057 76  ILE HHH CB  
8974  C CG1 . ILE G 77  ? 1.911 1.487 1.402 0.132  -0.274 -0.080 76  ILE HHH CG1 
8975  C CG2 . ILE G 77  ? 1.974 1.469 1.448 0.096  -0.376 -0.059 76  ILE HHH CG2 
8976  C CD1 . ILE G 77  ? 1.941 1.495 1.414 0.140  -0.282 -0.090 76  ILE HHH CD1 
8977  N N   . ASN G 78  ? 1.652 1.394 1.312 0.079  -0.206 -0.031 77  ASN HHH N   
8978  C CA  . ASN G 78  ? 1.610 1.417 1.324 0.070  -0.161 -0.025 77  ASN HHH CA  
8979  C C   . ASN G 78  ? 1.594 1.412 1.305 0.073  -0.139 -0.038 77  ASN HHH C   
8980  O O   . ASN G 78  ? 1.591 1.451 1.344 0.056  -0.122 -0.031 77  ASN HHH O   
8981  C CB  . ASN G 78  ? 1.601 1.451 1.376 0.042  -0.168 -0.001 77  ASN HHH CB  
8982  C CG  . ASN G 78  ? 1.643 1.499 1.437 0.039  -0.179 0.016  77  ASN HHH CG  
8983  O OD1 . ASN G 78  ? 1.704 1.536 1.466 0.057  -0.177 0.009  77  ASN HHH OD1 
8984  N ND2 . ASN G 78  ? 1.625 1.520 1.473 0.018  -0.191 0.043  77  ASN HHH ND2 
8985  N N   . THR G 79  ? 1.601 1.385 1.262 0.097  -0.139 -0.055 78  THR HHH N   
8986  C CA  . THR G 79  ? 1.569 1.362 1.227 0.102  -0.122 -0.065 78  THR HHH CA  
8987  C C   . THR G 79  ? 1.544 1.354 1.189 0.125  -0.083 -0.073 78  THR HHH C   
8988  O O   . THR G 79  ? 1.576 1.356 1.174 0.152  -0.086 -0.080 78  THR HHH O   
8989  C CB  . THR G 79  ? 1.641 1.382 1.256 0.112  -0.158 -0.073 78  THR HHH CB  
8990  O OG1 . THR G 79  ? 1.652 1.380 1.286 0.086  -0.198 -0.060 78  THR HHH OG1 
8991  C CG2 . THR G 79  ? 1.654 1.410 1.273 0.117  -0.143 -0.080 78  THR HHH CG2 
8992  N N   . ALA G 80  ? 1.511 1.366 1.194 0.113  -0.051 -0.070 79  ALA HHH N   
8993  C CA  . ALA G 80  ? 1.529 1.406 1.209 0.127  -0.018 -0.073 79  ALA HHH CA  
8994  C C   . ALA G 80  ? 1.558 1.436 1.231 0.132  -0.020 -0.078 79  ALA HHH C   
8995  O O   . ALA G 80  ? 1.522 1.400 1.211 0.114  -0.036 -0.077 79  ALA HHH O   
8996  C CB  . ALA G 80  ? 1.488 1.402 1.208 0.110  0.010  -0.068 79  ALA HHH CB  
8997  N N   . TYR G 81  ? 1.599 1.480 1.249 0.158  -0.004 -0.079 80  TYR HHH N   
8998  C CA  . TYR G 81  ? 1.607 1.494 1.252 0.171  -0.001 -0.081 80  TYR HHH CA  
8999  C C   . TYR G 81  ? 1.602 1.538 1.275 0.170  0.033  -0.070 80  TYR HHH C   
9000  O O   . TYR G 81  ? 1.581 1.535 1.263 0.169  0.053  -0.063 80  TYR HHH O   
9001  C CB  . TYR G 81  ? 1.671 1.518 1.259 0.211  -0.014 -0.089 80  TYR HHH CB  
9002  C CG  . TYR G 81  ? 1.736 1.523 1.286 0.214  -0.054 -0.099 80  TYR HHH CG  
9003  C CD1 . TYR G 81  ? 1.759 1.526 1.318 0.194  -0.084 -0.101 80  TYR HHH CD1 
9004  C CD2 . TYR G 81  ? 1.796 1.543 1.299 0.235  -0.066 -0.105 80  TYR HHH CD2 
9005  C CE1 . TYR G 81  ? 1.818 1.527 1.345 0.193  -0.127 -0.107 80  TYR HHH CE1 
9006  C CE2 . TYR G 81  ? 1.843 1.530 1.309 0.235  -0.110 -0.113 80  TYR HHH CE2 
9007  C CZ  . TYR G 81  ? 1.849 1.516 1.328 0.213  -0.142 -0.113 80  TYR HHH CZ  
9008  O OH  . TYR G 81  ? 1.895 1.499 1.340 0.209  -0.190 -0.117 80  TYR HHH OH  
9009  N N   . LEU G 82  ? 1.644 1.600 1.331 0.169  0.036  -0.067 81  LEU HHH N   
9010  C CA  . LEU G 82  ? 1.630 1.633 1.343 0.171  0.062  -0.053 81  LEU HHH CA  
9011  C C   . LEU G 82  ? 1.648 1.651 1.345 0.199  0.058  -0.051 81  LEU HHH C   
9012  O O   . LEU G 82  ? 1.658 1.637 1.348 0.194  0.035  -0.060 81  LEU HHH O   
9013  C CB  . LEU G 82  ? 1.587 1.617 1.343 0.131  0.065  -0.048 81  LEU HHH CB  
9014  C CG  . LEU G 82  ? 1.557 1.632 1.344 0.124  0.082  -0.032 81  LEU HHH CG  
9015  C CD1 . LEU G 82  ? 1.549 1.648 1.348 0.128  0.104  -0.017 81  LEU HHH CD1 
9016  C CD2 . LEU G 82  ? 1.532 1.618 1.348 0.086  0.076  -0.032 81  LEU HHH CD2 
9017  N N   . GLN G 83  ? 1.628 1.659 1.320 0.229  0.080  -0.039 82  GLN HHH N   
9018  C CA  . GLN G 83  ? 1.651 1.683 1.325 0.265  0.080  -0.037 82  GLN HHH CA  
9019  C C   . GLN G 83  ? 1.625 1.724 1.337 0.272  0.108  -0.010 82  GLN HHH C   
9020  O O   . GLN G 83  ? 1.622 1.759 1.365 0.253  0.127  0.006  82  GLN HHH O   
9021  C CB  . GLN G 83  ? 1.731 1.717 1.339 0.313  0.074  -0.050 82  GLN HHH CB  
9022  C CG  . GLN G 83  ? 1.758 1.741 1.344 0.324  0.089  -0.047 82  GLN HHH CG  
9023  C CD  . GLN G 83  ? 1.859 1.791 1.370 0.373  0.080  -0.062 82  GLN HHH CD  
9024  O OE1 . GLN G 83  ? 1.894 1.821 1.376 0.415  0.085  -0.063 82  GLN HHH OE1 
9025  N NE2 . GLN G 83  ? 1.911 1.800 1.387 0.371  0.066  -0.073 82  GLN HHH NE2 
9026  N N   . TRP G 84  ? 1.622 1.735 1.335 0.297  0.108  -0.004 83  TRP HHH N   
9027  C CA  . TRP G 84  ? 1.595 1.778 1.351 0.306  0.132  0.026  83  TRP HHH CA  
9028  C C   . TRP G 84  ? 1.654 1.841 1.375 0.369  0.146  0.031  83  TRP HHH C   
9029  O O   . TRP G 84  ? 1.681 1.821 1.362 0.397  0.128  0.012  83  TRP HHH O   
9030  C CB  . TRP G 84  ? 1.557 1.760 1.357 0.273  0.117  0.032  83  TRP HHH CB  
9031  C CG  . TRP G 84  ? 1.504 1.725 1.345 0.217  0.114  0.038  83  TRP HHH CG  
9032  C CD1 . TRP G 84  ? 1.498 1.773 1.386 0.193  0.129  0.064  83  TRP HHH CD1 
9033  C CD2 . TRP G 84  ? 1.466 1.647 1.302 0.178  0.092  0.017  83  TRP HHH CD2 
9034  N NE1 . TRP G 84  ? 1.473 1.735 1.377 0.144  0.117  0.057  83  TRP HHH NE1 
9035  C CE2 . TRP G 84  ? 1.448 1.657 1.321 0.137  0.097  0.028  83  TRP HHH CE2 
9036  C CE3 . TRP G 84  ? 1.475 1.602 1.280 0.176  0.069  -0.007 83  TRP HHH CE3 
9037  C CZ2 . TRP G 84  ? 1.437 1.620 1.311 0.099  0.084  0.013  83  TRP HHH CZ2 
9038  C CZ3 . TRP G 84  ? 1.464 1.575 1.277 0.135  0.056  -0.017 83  TRP HHH CZ3 
9039  C CH2 . TRP G 84  ? 1.447 1.586 1.293 0.100  0.066  -0.008 83  TRP HHH CH2 
9040  N N   . SER G 85  ? 1.679 1.922 1.413 0.392  0.179  0.058  84  SER HHH N   
9041  C CA  . SER G 85  ? 1.722 1.993 1.431 0.456  0.204  0.072  84  SER HHH CA  
9042  C C   . SER G 85  ? 1.714 2.007 1.446 0.474  0.200  0.082  84  SER HHH C   
9043  O O   . SER G 85  ? 1.785 2.052 1.468 0.531  0.203  0.072  84  SER HHH O   
9044  C CB  . SER G 85  ? 1.715 2.062 1.458 0.460  0.239  0.110  84  SER HHH CB  
9045  O OG  . SER G 85  ? 1.653 1.995 1.414 0.413  0.235  0.110  84  SER HHH OG  
9046  N N   . SER G 86  ? 1.648 1.983 1.447 0.426  0.192  0.099  85  SER HHH N   
9047  C CA  . SER G 86  ? 1.616 1.983 1.452 0.431  0.187  0.114  85  SER HHH CA  
9048  C C   . SER G 86  ? 1.550 1.945 1.450 0.362  0.170  0.126  85  SER HHH C   
9049  O O   . SER G 86  ? 1.482 1.924 1.425 0.329  0.182  0.149  85  SER HHH O   
9050  C CB  . SER G 86  ? 1.634 2.077 1.493 0.480  0.221  0.151  85  SER HHH CB  
9051  O OG  . SER G 86  ? 1.636 2.117 1.539 0.483  0.215  0.170  85  SER HHH OG  
9052  N N   . LEU G 87  ? 1.569 1.931 1.471 0.342  0.142  0.110  86  LEU HHH N   
9053  C CA  . LEU G 87  ? 1.540 1.903 1.479 0.276  0.120  0.110  86  LEU HHH CA  
9054  C C   . LEU G 87  ? 1.545 1.983 1.552 0.256  0.124  0.148  86  LEU HHH C   
9055  O O   . LEU G 87  ? 1.574 2.033 1.593 0.286  0.123  0.160  86  LEU HHH O   
9056  C CB  . LEU G 87  ? 1.546 1.844 1.455 0.265  0.088  0.080  86  LEU HHH CB  
9057  C CG  . LEU G 87  ? 1.558 1.785 1.417 0.255  0.075  0.047  86  LEU HHH CG  
9058  C CD1 . LEU G 87  ? 1.567 1.735 1.397 0.254  0.042  0.025  86  LEU HHH CD1 
9059  C CD2 . LEU G 87  ? 1.519 1.752 1.399 0.203  0.075  0.045  86  LEU HHH CD2 
9060  N N   . LYS G 88  ? 1.535 2.004 1.582 0.206  0.123  0.164  87  LYS HHH N   
9061  C CA  . LYS G 88  ? 1.524 2.051 1.633 0.170  0.114  0.197  87  LYS HHH CA  
9062  C C   . LYS G 88  ? 1.489 1.977 1.592 0.133  0.083  0.177  87  LYS HHH C   
9063  O O   . LYS G 88  ? 1.476 1.900 1.535 0.122  0.070  0.142  87  LYS HHH O   
9064  C CB  . LYS G 88  ? 1.542 2.100 1.686 0.127  0.119  0.218  87  LYS HHH CB  
9065  C CG  . LYS G 88  ? 1.582 2.184 1.739 0.154  0.149  0.244  87  LYS HHH CG  
9066  C CD  . LYS G 88  ? 1.606 2.194 1.764 0.115  0.148  0.243  87  LYS HHH CD  
9067  C CE  . LYS G 88  ? 1.632 2.293 1.847 0.102  0.161  0.293  87  LYS HHH CE  
9068  N NZ  . LYS G 88  ? 1.664 2.362 1.872 0.154  0.195  0.311  87  LYS HHH NZ  
9069  N N   . ALA G 89  ? 1.452 1.981 1.599 0.112  0.070  0.203  88  ALA HHH N   
9070  C CA  . ALA G 89  ? 1.414 1.919 1.562 0.065  0.039  0.192  88  ALA HHH CA  
9071  C C   . ALA G 89  ? 1.381 1.855 1.514 0.018  0.033  0.176  88  ALA HHH C   
9072  O O   . ALA G 89  ? 1.389 1.809 1.484 0.002  0.020  0.145  88  ALA HHH O   
9073  C CB  . ALA G 89  ? 1.410 1.973 1.612 0.048  0.027  0.229  88  ALA HHH CB  
9074  N N   . SER G 90  ? 1.386 1.893 1.547 0.001  0.043  0.198  89  SER HHH N   
9075  C CA  . SER G 90  ? 1.416 1.892 1.563 -0.040 0.037  0.185  89  SER HHH CA  
9076  C C   . SER G 90  ? 1.451 1.861 1.542 -0.030 0.041  0.143  89  SER HHH C   
9077  O O   . SER G 90  ? 1.507 1.876 1.574 -0.064 0.027  0.122  89  SER HHH O   
9078  C CB  . SER G 90  ? 1.427 1.941 1.606 -0.044 0.052  0.214  89  SER HHH CB  
9079  O OG  . SER G 90  ? 1.422 1.915 1.573 -0.016 0.074  0.199  89  SER HHH OG  
9080  N N   . ASP G 91  ? 1.477 1.877 1.546 0.015  0.058  0.133  90  ASP HHH N   
9081  C CA  . ASP G 91  ? 1.503 1.845 1.524 0.026  0.061  0.098  90  ASP HHH CA  
9082  C C   . ASP G 91  ? 1.502 1.804 1.498 0.012  0.040  0.074  90  ASP HHH C   
9083  O O   . ASP G 91  ? 1.533 1.791 1.494 0.017  0.039  0.049  90  ASP HHH O   
9084  C CB  . ASP G 91  ? 1.524 1.864 1.524 0.078  0.080  0.095  90  ASP HHH CB  
9085  C CG  . ASP G 91  ? 1.523 1.900 1.541 0.090  0.103  0.118  90  ASP HHH CG  
9086  O OD1 . ASP G 91  ? 1.504 1.884 1.537 0.057  0.104  0.124  90  ASP HHH OD1 
9087  O OD2 . ASP G 91  ? 1.545 1.946 1.559 0.135  0.121  0.129  90  ASP HHH OD2 
9088  N N   . THR G 92  ? 1.480 1.799 1.494 -0.005 0.024  0.084  91  THR HHH N   
9089  C CA  . THR G 92  ? 1.463 1.750 1.458 -0.030 0.003  0.068  91  THR HHH CA  
9090  C C   . THR G 92  ? 1.413 1.678 1.392 -0.066 0.001  0.054  91  THR HHH C   
9091  O O   . THR G 92  ? 1.363 1.645 1.359 -0.093 0.000  0.066  91  THR HHH O   
9092  C CB  . THR G 92  ? 1.498 1.812 1.518 -0.047 -0.015 0.086  91  THR HHH CB  
9093  O OG1 . THR G 92  ? 1.564 1.896 1.597 -0.009 -0.014 0.098  91  THR HHH OG1 
9094  C CG2 . THR G 92  ? 1.506 1.791 1.503 -0.074 -0.035 0.071  91  THR HHH CG2 
9095  N N   . ALA G 93  ? 1.415 1.641 1.362 -0.067 -0.001 0.030  92  ALA HHH N   
9096  C CA  . ALA G 93  ? 1.449 1.650 1.375 -0.089 0.003  0.014  92  ALA HHH CA  
9097  C C   . ALA G 93  ? 1.466 1.636 1.366 -0.080 0.002  -0.005 92  ALA HHH C   
9098  O O   . ALA G 93  ? 1.467 1.631 1.364 -0.058 -0.005 -0.005 92  ALA HHH O   
9099  C CB  . ALA G 93  ? 1.462 1.664 1.393 -0.086 0.019  0.016  92  ALA HHH CB  
9100  N N   . ILE G 94  ? 1.480 1.631 1.362 -0.095 0.006  -0.019 93  ILE HHH N   
9101  C CA  . ILE G 94  ? 1.465 1.593 1.328 -0.087 0.008  -0.032 93  ILE HHH CA  
9102  C C   . ILE G 94  ? 1.405 1.522 1.265 -0.074 0.025  -0.039 93  ILE HHH C   
9103  O O   . ILE G 94  ? 1.386 1.504 1.247 -0.085 0.034  -0.039 93  ILE HHH O   
9104  C CB  . ILE G 94  ? 1.507 1.630 1.354 -0.109 0.004  -0.038 93  ILE HHH CB  
9105  C CG1 . ILE G 94  ? 1.547 1.657 1.385 -0.100 0.008  -0.046 93  ILE HHH CG1 
9106  C CG2 . ILE G 94  ? 1.507 1.628 1.342 -0.130 0.009  -0.043 93  ILE HHH CG2 
9107  C CD1 . ILE G 94  ? 1.596 1.713 1.427 -0.115 0.000  -0.042 93  ILE HHH CD1 
9108  N N   . TYR G 95  ? 1.350 1.454 1.203 -0.052 0.026  -0.044 94  TYR HHH N   
9109  C CA  . TYR G 95  ? 1.309 1.401 1.158 -0.035 0.040  -0.048 94  TYR HHH CA  
9110  C C   . TYR G 95  ? 1.302 1.378 1.141 -0.035 0.040  -0.058 94  TYR HHH C   
9111  O O   . TYR G 95  ? 1.300 1.367 1.135 -0.029 0.026  -0.057 94  TYR HHH O   
9112  C CB  . TYR G 95  ? 1.278 1.371 1.127 -0.006 0.040  -0.043 94  TYR HHH CB  
9113  C CG  . TYR G 95  ? 1.254 1.375 1.120 -0.002 0.045  -0.028 94  TYR HHH CG  
9114  C CD1 . TYR G 95  ? 1.237 1.374 1.115 -0.003 0.060  -0.019 94  TYR HHH CD1 
9115  C CD2 . TYR G 95  ? 1.243 1.378 1.117 0.001  0.033  -0.020 94  TYR HHH CD2 
9116  C CE1 . TYR G 95  ? 1.234 1.406 1.137 -0.002 0.064  0.001  94  TYR HHH CE1 
9117  C CE2 . TYR G 95  ? 1.223 1.391 1.119 0.006  0.039  -0.002 94  TYR HHH CE2 
9118  C CZ  . TYR G 95  ? 1.223 1.413 1.136 0.003  0.055  0.010  94  TYR HHH CZ  
9119  O OH  . TYR G 95  ? 1.229 1.460 1.171 0.006  0.060  0.034  94  TYR HHH OH  
9120  N N   . TYR G 96  ? 1.320 1.391 1.156 -0.043 0.053  -0.064 95  TYR HHH N   
9121  C CA  . TYR G 96  ? 1.357 1.419 1.189 -0.041 0.057  -0.069 95  TYR HHH CA  
9122  C C   . TYR G 96  ? 1.360 1.409 1.191 -0.022 0.064  -0.070 95  TYR HHH C   
9123  O O   . TYR G 96  ? 1.366 1.413 1.197 -0.019 0.075  -0.069 95  TYR HHH O   
9124  C CB  . TYR G 96  ? 1.402 1.461 1.225 -0.055 0.069  -0.076 95  TYR HHH CB  
9125  C CG  . TYR G 96  ? 1.447 1.516 1.261 -0.074 0.064  -0.076 95  TYR HHH CG  
9126  C CD1 . TYR G 96  ? 1.478 1.560 1.293 -0.079 0.057  -0.071 95  TYR HHH CD1 
9127  C CD2 . TYR G 96  ? 1.473 1.538 1.279 -0.089 0.063  -0.078 95  TYR HHH CD2 
9128  C CE1 . TYR G 96  ? 1.506 1.598 1.310 -0.096 0.053  -0.070 95  TYR HHH CE1 
9129  C CE2 . TYR G 96  ? 1.503 1.573 1.296 -0.107 0.056  -0.078 95  TYR HHH CE2 
9130  C CZ  . TYR G 96  ? 1.526 1.611 1.317 -0.109 0.052  -0.075 95  TYR HHH CZ  
9131  O OH  . TYR G 96  ? 1.612 1.704 1.387 -0.126 0.046  -0.073 95  TYR HHH OH  
9132  N N   . CYS G 97  ? 1.383 1.425 1.213 -0.011 0.055  -0.069 96  CYS HHH N   
9133  C CA  . CYS G 97  ? 1.423 1.452 1.250 0.004  0.061  -0.069 96  CYS HHH CA  
9134  C C   . CYS G 97  ? 1.429 1.462 1.264 -0.002 0.072  -0.071 96  CYS HHH C   
9135  O O   . CYS G 97  ? 1.424 1.471 1.265 -0.012 0.068  -0.068 96  CYS HHH O   
9136  C CB  . CYS G 97  ? 1.450 1.465 1.269 0.019  0.041  -0.066 96  CYS HHH CB  
9137  S SG  . CYS G 97  ? 1.491 1.507 1.321 0.009  0.022  -0.059 96  CYS HHH SG  
9138  N N   . ALA G 98  ? 1.447 1.471 1.282 0.006  0.086  -0.074 97  ALA HHH N   
9139  C CA  . ALA G 98  ? 1.477 1.500 1.315 0.006  0.100  -0.077 97  ALA HHH CA  
9140  C C   . ALA G 98  ? 1.503 1.515 1.346 0.021  0.105  -0.074 97  ALA HHH C   
9141  O O   . ALA G 98  ? 1.525 1.523 1.362 0.027  0.110  -0.074 97  ALA HHH O   
9142  C CB  . ALA G 98  ? 1.506 1.520 1.333 -0.004 0.112  -0.086 97  ALA HHH CB  
9143  N N   . GLY G 99  ? 1.518 1.540 1.374 0.027  0.103  -0.067 98  GLY HHH N   
9144  C CA  . GLY G 99  ? 1.553 1.568 1.417 0.041  0.105  -0.061 98  GLY HHH CA  
9145  C C   . GLY G 99  ? 1.582 1.592 1.450 0.048  0.126  -0.066 98  GLY HHH C   
9146  O O   . GLY G 99  ? 1.616 1.638 1.484 0.046  0.136  -0.069 98  GLY HHH O   
9147  N N   . GLY G 100 ? 1.604 1.595 1.469 0.059  0.131  -0.065 99  GLY HHH N   
9148  C CA  . GLY G 100 ? 1.621 1.605 1.495 0.072  0.145  -0.064 99  GLY HHH CA  
9149  C C   . GLY G 100 ? 1.596 1.586 1.487 0.083  0.135  -0.050 99  GLY HHH C   
9150  O O   . GLY G 100 ? 1.610 1.596 1.493 0.081  0.119  -0.045 99  GLY HHH O   
9151  N N   . SER G 101 ? 1.573 1.573 1.483 0.097  0.143  -0.042 100 SER HHH N   
9152  C CA  . SER G 101 ? 1.574 1.577 1.501 0.107  0.134  -0.026 100 SER HHH CA  
9153  C C   . SER G 101 ? 1.568 1.539 1.484 0.117  0.142  -0.030 100 SER HHH C   
9154  O O   . SER G 101 ? 1.654 1.616 1.576 0.130  0.157  -0.031 100 SER HHH O   
9155  C CB  . SER G 101 ? 1.608 1.644 1.568 0.118  0.137  -0.010 100 SER HHH CB  
9156  O OG  . SER G 101 ? 1.688 1.725 1.647 0.130  0.163  -0.019 100 SER HHH OG  
9157  N N   . GLY G 102 ? 1.560 1.513 1.457 0.111  0.133  -0.032 101 GLY HHH N   
9158  C CA  . GLY G 102 ? 1.572 1.498 1.459 0.115  0.140  -0.032 101 GLY HHH CA  
9159  C C   . GLY G 102 ? 1.558 1.468 1.427 0.101  0.147  -0.042 101 GLY HHH C   
9160  O O   . GLY G 102 ? 1.517 1.434 1.381 0.092  0.149  -0.052 101 GLY HHH O   
9161  N N   . ILE G 103 ? 1.598 1.490 1.459 0.100  0.148  -0.035 102 ILE HHH N   
9162  C CA  . ILE G 103 ? 1.628 1.509 1.480 0.085  0.151  -0.037 102 ILE HHH CA  
9163  C C   . ILE G 103 ? 1.624 1.469 1.474 0.083  0.157  -0.044 102 ILE HHH C   
9164  O O   . ILE G 103 ? 1.639 1.471 1.496 0.098  0.161  -0.044 102 ILE HHH O   
9165  C CB  . ILE G 103 ? 1.678 1.565 1.525 0.085  0.148  -0.020 102 ILE HHH CB  
9166  C CG1 . ILE G 103 ? 1.727 1.620 1.572 0.068  0.150  -0.015 102 ILE HHH CG1 
9167  C CG2 . ILE G 103 ? 1.700 1.568 1.551 0.094  0.149  -0.007 102 ILE HHH CG2 
9168  C CD1 . ILE G 103 ? 1.737 1.648 1.578 0.059  0.148  -0.026 102 ILE HHH CD1 
9169  N N   . SER G 104 ? 1.603 1.431 1.444 0.065  0.156  -0.048 103 SER HHH N   
9170  C CA  . SER G 104 ? 1.628 1.411 1.456 0.061  0.156  -0.060 103 SER HHH CA  
9171  C C   . SER G 104 ? 1.619 1.401 1.441 0.078  0.165  -0.077 103 SER HHH C   
9172  O O   . SER G 104 ? 1.631 1.382 1.447 0.094  0.171  -0.083 103 SER HHH O   
9173  C CB  . SER G 104 ? 1.660 1.408 1.491 0.064  0.153  -0.049 103 SER HHH CB  
9174  O OG  . SER G 104 ? 1.692 1.423 1.521 0.041  0.143  -0.039 103 SER HHH OG  
9175  N N   . THR G 105 ? 1.600 1.417 1.424 0.076  0.167  -0.082 104 THR HHH N   
9176  C CA  . THR G 105 ? 1.627 1.458 1.448 0.089  0.176  -0.093 104 THR HHH CA  
9177  C C   . THR G 105 ? 1.639 1.479 1.445 0.073  0.174  -0.104 104 THR HHH C   
9178  O O   . THR G 105 ? 1.606 1.464 1.415 0.055  0.165  -0.099 104 THR HHH O   
9179  C CB  . THR G 105 ? 1.623 1.496 1.470 0.101  0.177  -0.080 104 THR HHH CB  
9180  O OG1 . THR G 105 ? 1.616 1.494 1.471 0.123  0.189  -0.081 104 THR HHH OG1 
9181  C CG2 . THR G 105 ? 1.622 1.532 1.475 0.090  0.169  -0.077 104 THR HHH CG2 
9182  N N   . PRO G 106 ? 1.690 1.520 1.476 0.081  0.184  -0.118 105 PRO HHH N   
9183  C CA  . PRO G 106 ? 1.687 1.524 1.455 0.067  0.182  -0.128 105 PRO HHH CA  
9184  C C   . PRO G 106 ? 1.635 1.527 1.427 0.064  0.180  -0.116 105 PRO HHH C   
9185  O O   . PRO G 106 ? 1.592 1.509 1.407 0.079  0.185  -0.106 105 PRO HHH O   
9186  C CB  . PRO G 106 ? 1.755 1.569 1.492 0.085  0.196  -0.145 105 PRO HHH CB  
9187  C CG  . PRO G 106 ? 1.765 1.588 1.522 0.114  0.210  -0.137 105 PRO HHH CG  
9188  C CD  . PRO G 106 ? 1.751 1.566 1.532 0.109  0.199  -0.124 105 PRO HHH CD  
9189  N N   . MET G 107 ? 1.650 1.556 1.440 0.043  0.170  -0.116 106 MET HHH N   
9190  C CA  . MET G 107 ? 1.670 1.619 1.478 0.038  0.163  -0.106 106 MET HHH CA  
9191  C C   . MET G 107 ? 1.640 1.612 1.446 0.046  0.173  -0.107 106 MET HHH C   
9192  O O   . MET G 107 ? 1.643 1.609 1.425 0.038  0.176  -0.117 106 MET HHH O   
9193  C CB  . MET G 107 ? 1.738 1.691 1.541 0.017  0.150  -0.106 106 MET HHH CB  
9194  C CG  . MET G 107 ? 1.815 1.760 1.626 0.013  0.143  -0.099 106 MET HHH CG  
9195  S SD  . MET G 107 ? 1.877 1.817 1.680 -0.010 0.133  -0.098 106 MET HHH SD  
9196  C CE  . MET G 107 ? 1.867 1.826 1.689 -0.003 0.129  -0.081 106 MET HHH CE  
9197  N N   . ASP G 108 ? 1.625 1.624 1.456 0.061  0.178  -0.094 107 ASP HHH N   
9198  C CA  . ASP G 108 ? 1.640 1.670 1.477 0.074  0.193  -0.088 107 ASP HHH CA  
9199  C C   . ASP G 108 ? 1.526 1.601 1.385 0.060  0.181  -0.071 107 ASP HHH C   
9200  O O   . ASP G 108 ? 1.524 1.635 1.393 0.068  0.192  -0.059 107 ASP HHH O   
9201  C CB  . ASP G 108 ? 1.735 1.771 1.590 0.100  0.207  -0.079 107 ASP HHH CB  
9202  C CG  . ASP G 108 ? 1.766 1.814 1.655 0.102  0.194  -0.062 107 ASP HHH CG  
9203  O OD1 . ASP G 108 ? 1.797 1.811 1.680 0.102  0.188  -0.068 107 ASP HHH OD1 
9204  O OD2 . ASP G 108 ? 1.778 1.869 1.701 0.104  0.189  -0.041 107 ASP HHH OD2 
9205  N N   . VAL G 109 ? 1.419 1.492 1.284 0.042  0.159  -0.068 108 VAL HHH N   
9206  C CA  . VAL G 109 ? 1.366 1.470 1.249 0.027  0.141  -0.052 108 VAL HHH CA  
9207  C C   . VAL G 109 ? 1.331 1.417 1.199 0.011  0.124  -0.060 108 VAL HHH C   
9208  O O   . VAL G 109 ? 1.345 1.405 1.206 0.013  0.119  -0.067 108 VAL HHH O   
9209  C CB  . VAL G 109 ? 1.356 1.478 1.272 0.031  0.126  -0.031 108 VAL HHH CB  
9210  C CG1 . VAL G 109 ? 1.380 1.474 1.294 0.043  0.124  -0.036 108 VAL HHH CG1 
9211  C CG2 . VAL G 109 ? 1.342 1.472 1.267 0.014  0.097  -0.019 108 VAL HHH CG2 
9212  N N   . TRP G 110 ? 1.312 1.415 1.177 -0.004 0.117  -0.056 109 TRP HHH N   
9213  C CA  . TRP G 110 ? 1.292 1.382 1.143 -0.019 0.103  -0.063 109 TRP HHH CA  
9214  C C   . TRP G 110 ? 1.274 1.383 1.140 -0.030 0.080  -0.048 109 TRP HHH C   
9215  O O   . TRP G 110 ? 1.281 1.419 1.160 -0.035 0.080  -0.033 109 TRP HHH O   
9216  C CB  . TRP G 110 ? 1.306 1.390 1.132 -0.027 0.114  -0.075 109 TRP HHH CB  
9217  C CG  . TRP G 110 ? 1.315 1.368 1.121 -0.021 0.127  -0.091 109 TRP HHH CG  
9218  C CD1 . TRP G 110 ? 1.353 1.394 1.150 -0.006 0.145  -0.098 109 TRP HHH CD1 
9219  C CD2 . TRP G 110 ? 1.280 1.310 1.075 -0.031 0.121  -0.099 109 TRP HHH CD2 
9220  N NE1 . TRP G 110 ? 1.355 1.359 1.133 -0.007 0.148  -0.111 109 TRP HHH NE1 
9221  C CE2 . TRP G 110 ? 1.313 1.312 1.091 -0.024 0.133  -0.110 109 TRP HHH CE2 
9222  C CE3 . TRP G 110 ? 1.257 1.290 1.056 -0.043 0.107  -0.095 109 TRP HHH CE3 
9223  C CZ2 . TRP G 110 ? 1.320 1.294 1.089 -0.034 0.128  -0.115 109 TRP HHH CZ2 
9224  C CZ3 . TRP G 110 ? 1.283 1.297 1.075 -0.051 0.105  -0.099 109 TRP HHH CZ3 
9225  C CH2 . TRP G 110 ? 1.311 1.297 1.090 -0.049 0.114  -0.108 109 TRP HHH CH2 
9226  N N   . GLY G 111 ? 1.294 1.386 1.157 -0.033 0.061  -0.049 110 GLY HHH N   
9227  C CA  . GLY G 111 ? 1.331 1.427 1.198 -0.044 0.036  -0.039 110 GLY HHH CA  
9228  C C   . GLY G 111 ? 1.345 1.452 1.203 -0.058 0.038  -0.041 110 GLY HHH C   
9229  O O   . GLY G 111 ? 1.355 1.456 1.199 -0.059 0.055  -0.054 110 GLY HHH O   
9230  N N   . GLN G 112 ? 1.367 1.488 1.234 -0.072 0.020  -0.027 111 GLN HHH N   
9231  C CA  . GLN G 112 ? 1.396 1.531 1.253 -0.088 0.022  -0.026 111 GLN HHH CA  
9232  C C   . GLN G 112 ? 1.412 1.528 1.257 -0.088 0.017  -0.038 111 GLN HHH C   
9233  O O   . GLN G 112 ? 1.437 1.561 1.271 -0.100 0.020  -0.039 111 GLN HHH O   
9234  C CB  . GLN G 112 ? 1.396 1.552 1.268 -0.103 0.002  -0.004 111 GLN HHH CB  
9235  C CG  . GLN G 112 ? 1.385 1.520 1.264 -0.105 -0.032 0.003  111 GLN HHH CG  
9236  C CD  . GLN G 112 ? 1.378 1.531 1.273 -0.124 -0.053 0.028  111 GLN HHH CD  
9237  O OE1 . GLN G 112 ? 1.350 1.530 1.266 -0.131 -0.053 0.047  111 GLN HHH OE1 
9238  N NE2 . GLN G 112 ? 1.376 1.521 1.267 -0.134 -0.073 0.032  111 GLN HHH NE2 
9239  N N   . GLY G 113 ? 1.409 1.504 1.254 -0.073 0.011  -0.043 112 GLY HHH N   
9240  C CA  . GLY G 113 ? 1.439 1.524 1.278 -0.068 0.010  -0.049 112 GLY HHH CA  
9241  C C   . GLY G 113 ? 1.478 1.554 1.318 -0.064 -0.014 -0.043 112 GLY HHH C   
9242  O O   . GLY G 113 ? 1.509 1.590 1.355 -0.076 -0.032 -0.032 112 GLY HHH O   
9243  N N   . THR G 114 ? 1.514 1.578 1.350 -0.046 -0.015 -0.047 113 THR HHH N   
9244  C CA  . THR G 114 ? 1.550 1.603 1.383 -0.034 -0.034 -0.043 113 THR HHH CA  
9245  C C   . THR G 114 ? 1.553 1.628 1.395 -0.041 -0.028 -0.039 113 THR HHH C   
9246  O O   . THR G 114 ? 1.519 1.606 1.365 -0.037 -0.009 -0.040 113 THR HHH O   
9247  C CB  . THR G 114 ? 1.587 1.614 1.404 -0.004 -0.036 -0.049 113 THR HHH CB  
9248  O OG1 . THR G 114 ? 1.595 1.602 1.405 -0.001 -0.043 -0.051 113 THR HHH OG1 
9249  C CG2 . THR G 114 ? 1.618 1.625 1.423 0.016  -0.055 -0.047 113 THR HHH CG2 
9250  N N   . THR G 115 ? 1.570 1.650 1.416 -0.052 -0.044 -0.030 114 THR HHH N   
9251  C CA  . THR G 115 ? 1.559 1.661 1.417 -0.058 -0.044 -0.022 114 THR HHH CA  
9252  C C   . THR G 115 ? 1.567 1.662 1.426 -0.028 -0.050 -0.019 114 THR HHH C   
9253  O O   . THR G 115 ? 1.599 1.667 1.448 -0.015 -0.071 -0.019 114 THR HHH O   
9254  C CB  . THR G 115 ? 1.564 1.677 1.426 -0.084 -0.060 -0.013 114 THR HHH CB  
9255  O OG1 . THR G 115 ? 1.589 1.689 1.445 -0.092 -0.071 -0.013 114 THR HHH OG1 
9256  C CG2 . THR G 115 ? 1.571 1.705 1.434 -0.109 -0.049 -0.013 114 THR HHH CG2 
9257  N N   . VAL G 116 ? 1.535 1.652 1.406 -0.016 -0.034 -0.014 115 VAL HHH N   
9258  C CA  . VAL G 116 ? 1.541 1.663 1.415 0.018  -0.033 -0.007 115 VAL HHH CA  
9259  C C   . VAL G 116 ? 1.549 1.710 1.453 0.005  -0.034 0.011  115 VAL HHH C   
9260  O O   . VAL G 116 ? 1.567 1.754 1.487 -0.019 -0.024 0.018  115 VAL HHH O   
9261  C CB  . VAL G 116 ? 1.527 1.653 1.396 0.044  -0.011 -0.009 115 VAL HHH CB  
9262  C CG1 . VAL G 116 ? 1.547 1.686 1.418 0.083  -0.004 0.001  115 VAL HHH CG1 
9263  C CG2 . VAL G 116 ? 1.525 1.612 1.365 0.054  -0.013 -0.025 115 VAL HHH CG2 
9264  N N   . THR G 117 ? 1.560 1.720 1.468 0.020  -0.049 0.019  116 THR HHH N   
9265  C CA  . THR G 117 ? 1.565 1.764 1.504 0.014  -0.052 0.040  116 THR HHH CA  
9266  C C   . THR G 117 ? 1.589 1.799 1.534 0.061  -0.046 0.050  116 THR HHH C   
9267  O O   . THR G 117 ? 1.642 1.817 1.565 0.089  -0.060 0.043  116 THR HHH O   
9268  C CB  . THR G 117 ? 1.563 1.758 1.505 -0.015 -0.077 0.045  116 THR HHH CB  
9269  O OG1 . THR G 117 ? 1.590 1.743 1.509 0.000  -0.096 0.036  116 THR HHH OG1 
9270  C CG2 . THR G 117 ? 1.553 1.751 1.490 -0.059 -0.077 0.040  116 THR HHH CG2 
9271  N N   . VAL G 118 ? 1.542 1.800 1.515 0.070  -0.025 0.068  117 VAL HHH N   
9272  C CA  . VAL G 118 ? 1.520 1.806 1.506 0.118  -0.010 0.085  117 VAL HHH CA  
9273  C C   . VAL G 118 ? 1.505 1.836 1.533 0.111  -0.019 0.112  117 VAL HHH C   
9274  O O   . VAL G 118 ? 1.507 1.892 1.576 0.089  -0.011 0.136  117 VAL HHH O   
9275  C CB  . VAL G 118 ? 1.522 1.842 1.520 0.130  0.019  0.095  117 VAL HHH CB  
9276  C CG1 . VAL G 118 ? 1.550 1.906 1.559 0.184  0.039  0.115  117 VAL HHH CG1 
9277  C CG2 . VAL G 118 ? 1.542 1.819 1.502 0.130  0.026  0.070  117 VAL HHH CG2 
9278  N N   . ALA G 119 ? 1.511 1.820 1.531 0.128  -0.038 0.110  118 ALA HHH N   
9279  C CA  . ALA G 119 ? 1.518 1.867 1.576 0.128  -0.049 0.137  118 ALA HHH CA  
9280  C C   . ALA G 119 ? 1.555 1.859 1.589 0.161  -0.069 0.128  118 ALA HHH C   
9281  O O   . ALA G 119 ? 1.544 1.785 1.537 0.153  -0.088 0.103  118 ALA HHH O   
9282  C CB  . ALA G 119 ? 1.493 1.861 1.576 0.069  -0.067 0.146  118 ALA HHH CB  
9283  N N   . SER G 120 ? 1.599 1.936 1.659 0.197  -0.067 0.150  119 SER HHH N   
9284  C CA  . SER G 120 ? 1.655 1.958 1.705 0.220  -0.092 0.150  119 SER HHH CA  
9285  C C   . SER G 120 ? 1.628 1.924 1.690 0.163  -0.122 0.154  119 SER HHH C   
9286  O O   . SER G 120 ? 1.566 1.906 1.659 0.116  -0.120 0.167  119 SER HHH O   
9287  C CB  . SER G 120 ? 1.686 2.040 1.772 0.267  -0.079 0.179  119 SER HHH CB  
9288  O OG  . SER G 120 ? 1.666 2.107 1.811 0.246  -0.060 0.212  119 SER HHH OG  
9289  N N   . THR G 121 ? 1.671 1.910 1.706 0.166  -0.152 0.142  120 THR HHH N   
9290  C CA  . THR G 121 ? 1.674 1.897 1.710 0.114  -0.182 0.144  120 THR HHH CA  
9291  C C   . THR G 121 ? 1.689 1.944 1.763 0.111  -0.200 0.172  120 THR HHH C   
9292  O O   . THR G 121 ? 1.722 1.997 1.815 0.158  -0.192 0.187  120 THR HHH O   
9293  C CB  . THR G 121 ? 1.712 1.857 1.701 0.113  -0.206 0.121  120 THR HHH CB  
9294  O OG1 . THR G 121 ? 1.766 1.870 1.744 0.150  -0.229 0.123  120 THR HHH OG1 
9295  C CG2 . THR G 121 ? 1.730 1.839 1.682 0.129  -0.191 0.095  120 THR HHH CG2 
9296  N N   . LYS G 122 ? 1.668 1.929 1.750 0.059  -0.221 0.181  121 LYS HHH N   
9297  C CA  . LYS G 122 ? 1.674 1.956 1.785 0.046  -0.247 0.207  121 LYS HHH CA  
9298  C C   . LYS G 122 ? 1.653 1.915 1.747 -0.010 -0.270 0.204  121 LYS HHH C   
9299  O O   . LYS G 122 ? 1.602 1.881 1.689 -0.049 -0.259 0.197  121 LYS HHH O   
9300  C CB  . LYS G 122 ? 1.674 2.034 1.839 0.041  -0.234 0.237  121 LYS HHH CB  
9301  C CG  . LYS G 122 ? 1.709 2.097 1.911 0.043  -0.257 0.268  121 LYS HHH CG  
9302  C CD  . LYS G 122 ? 1.697 2.101 1.907 -0.018 -0.282 0.282  121 LYS HHH CD  
9303  C CE  . LYS G 122 ? 1.704 2.162 1.966 -0.021 -0.298 0.321  121 LYS HHH CE  
9304  N NZ  . LYS G 122 ? 1.753 2.185 2.020 0.019  -0.317 0.330  121 LYS HHH NZ  
9305  N N   . GLY G 123 ? 1.699 1.923 1.781 -0.011 -0.301 0.208  122 GLY HHH N   
9306  C CA  . GLY G 123 ? 1.703 1.904 1.765 -0.058 -0.324 0.208  122 GLY HHH CA  
9307  C C   . GLY G 123 ? 1.676 1.925 1.760 -0.104 -0.334 0.231  122 GLY HHH C   
9308  O O   . GLY G 123 ? 1.658 1.944 1.776 -0.097 -0.340 0.254  122 GLY HHH O   
9309  N N   . PRO G 124 ? 1.643 1.891 1.703 -0.150 -0.337 0.226  123 PRO HHH N   
9310  C CA  . PRO G 124 ? 1.628 1.914 1.693 -0.194 -0.345 0.243  123 PRO HHH CA  
9311  C C   . PRO G 124 ? 1.644 1.929 1.718 -0.209 -0.379 0.269  123 PRO HHH C   
9312  O O   . PRO G 124 ? 1.640 1.888 1.700 -0.208 -0.397 0.270  123 PRO HHH O   
9313  C CB  . PRO G 124 ? 1.620 1.896 1.647 -0.227 -0.334 0.226  123 PRO HHH CB  
9314  C CG  . PRO G 124 ? 1.620 1.849 1.629 -0.211 -0.339 0.214  123 PRO HHH CG  
9315  C CD  . PRO G 124 ? 1.633 1.843 1.658 -0.160 -0.334 0.207  123 PRO HHH CD  
9316  N N   . SER G 125 ? 1.655 1.981 1.754 -0.226 -0.390 0.292  124 SER HHH N   
9317  C CA  . SER G 125 ? 1.673 2.008 1.775 -0.255 -0.423 0.319  124 SER HHH CA  
9318  C C   . SER G 125 ? 1.669 2.003 1.728 -0.303 -0.423 0.313  124 SER HHH C   
9319  O O   . SER G 125 ? 1.630 1.977 1.670 -0.318 -0.401 0.297  124 SER HHH O   
9320  C CB  . SER G 125 ? 1.684 2.064 1.827 -0.258 -0.435 0.346  124 SER HHH CB  
9321  O OG  . SER G 125 ? 1.711 2.087 1.890 -0.216 -0.447 0.362  124 SER HHH OG  
9322  N N   . VAL G 126 ? 1.712 2.032 1.755 -0.324 -0.446 0.327  125 VAL HHH N   
9323  C CA  . VAL G 126 ? 1.746 2.071 1.746 -0.365 -0.445 0.327  125 VAL HHH CA  
9324  C C   . VAL G 126 ? 1.777 2.121 1.776 -0.395 -0.475 0.357  125 VAL HHH C   
9325  O O   . VAL G 126 ? 1.790 2.121 1.804 -0.392 -0.502 0.379  125 VAL HHH O   
9326  C CB  . VAL G 126 ? 1.778 2.073 1.755 -0.364 -0.440 0.318  125 VAL HHH CB  
9327  C CG1 . VAL G 126 ? 1.806 2.116 1.741 -0.401 -0.434 0.321  125 VAL HHH CG1 
9328  C CG2 . VAL G 126 ? 1.759 2.033 1.737 -0.334 -0.413 0.289  125 VAL HHH CG2 
9329  N N   . PHE G 127 ? 1.784 2.153 1.761 -0.424 -0.474 0.359  126 PHE HHH N   
9330  C CA  . PHE G 127 ? 1.819 2.208 1.783 -0.459 -0.502 0.386  126 PHE HHH CA  
9331  C C   . PHE G 127 ? 1.818 2.204 1.718 -0.490 -0.493 0.378  126 PHE HHH C   
9332  O O   . PHE G 127 ? 1.811 2.189 1.679 -0.488 -0.464 0.350  126 PHE HHH O   
9333  C CB  . PHE G 127 ? 1.850 2.265 1.839 -0.465 -0.513 0.396  126 PHE HHH CB  
9334  C CG  . PHE G 127 ? 1.850 2.277 1.903 -0.427 -0.512 0.403  126 PHE HHH CG  
9335  C CD1 . PHE G 127 ? 1.866 2.287 1.958 -0.402 -0.531 0.423  126 PHE HHH CD1 
9336  C CD2 . PHE G 127 ? 1.852 2.295 1.926 -0.414 -0.493 0.391  126 PHE HHH CD2 
9337  C CE1 . PHE G 127 ? 1.856 2.287 2.001 -0.361 -0.527 0.429  126 PHE HHH CE1 
9338  C CE2 . PHE G 127 ? 1.834 2.295 1.966 -0.376 -0.488 0.400  126 PHE HHH CE2 
9339  C CZ  . PHE G 127 ? 1.836 2.292 2.002 -0.347 -0.504 0.418  126 PHE HHH CZ  
9340  N N   . PRO G 128 ? 1.821 2.215 1.697 -0.517 -0.515 0.403  127 PRO HHH N   
9341  C CA  . PRO G 128 ? 1.842 2.240 1.652 -0.544 -0.504 0.399  127 PRO HHH CA  
9342  C C   . PRO G 128 ? 1.862 2.267 1.627 -0.570 -0.511 0.394  127 PRO HHH C   
9343  O O   . PRO G 128 ? 1.858 2.272 1.652 -0.574 -0.532 0.405  127 PRO HHH O   
9344  C CB  . PRO G 128 ? 1.880 2.285 1.692 -0.559 -0.528 0.434  127 PRO HHH CB  
9345  C CG  . PRO G 128 ? 1.881 2.290 1.746 -0.555 -0.563 0.459  127 PRO HHH CG  
9346  C CD  . PRO G 128 ? 1.834 2.233 1.745 -0.520 -0.550 0.438  127 PRO HHH CD  
9347  N N   . LEU G 129 ? 1.886 2.287 1.580 -0.585 -0.494 0.381  128 LEU HHH N   
9348  C CA  . LEU G 129 ? 1.948 2.343 1.577 -0.611 -0.503 0.374  128 LEU HHH CA  
9349  C C   . LEU G 129 ? 2.015 2.419 1.579 -0.632 -0.506 0.389  128 LEU HHH C   
9350  O O   . LEU G 129 ? 2.052 2.450 1.559 -0.626 -0.475 0.371  128 LEU HHH O   
9351  C CB  . LEU G 129 ? 1.938 2.309 1.531 -0.601 -0.474 0.334  128 LEU HHH CB  
9352  C CG  . LEU G 129 ? 1.876 2.243 1.530 -0.581 -0.468 0.320  128 LEU HHH CG  
9353  C CD1 . LEU G 129 ? 1.872 2.214 1.490 -0.569 -0.437 0.282  128 LEU HHH CD1 
9354  C CD2 . LEU G 129 ? 1.877 2.254 1.563 -0.598 -0.503 0.338  128 LEU HHH CD2 
9355  N N   . ALA G 130 ? 2.056 2.476 1.628 -0.652 -0.540 0.425  129 ALA HHH N   
9356  C CA  . ALA G 130 ? 2.148 2.582 1.664 -0.673 -0.545 0.448  129 ALA HHH CA  
9357  C C   . ALA G 130 ? 2.260 2.679 1.678 -0.690 -0.543 0.431  129 ALA HHH C   
9358  O O   . ALA G 130 ? 2.286 2.686 1.689 -0.702 -0.562 0.419  129 ALA HHH O   
9359  C CB  . ALA G 130 ? 2.168 2.620 1.724 -0.690 -0.585 0.491  129 ALA HHH CB  
9360  N N   . PRO G 131 ? 2.140 2.674 1.840 -0.283 -0.180 0.438  130 PRO HHH N   
9361  C CA  . PRO G 131 ? 2.158 2.734 1.815 -0.272 -0.163 0.425  130 PRO HHH CA  
9362  C C   . PRO G 131 ? 2.209 2.799 1.808 -0.253 -0.171 0.438  130 PRO HHH C   
9363  O O   . PRO G 131 ? 2.205 2.771 1.796 -0.249 -0.188 0.463  130 PRO HHH O   
9364  C CB  . PRO G 131 ? 2.180 2.780 1.848 -0.284 -0.132 0.451  130 PRO HHH CB  
9365  C CG  . PRO G 131 ? 2.202 2.776 1.898 -0.303 -0.137 0.497  130 PRO HHH CG  
9366  C CD  . PRO G 131 ? 2.170 2.694 1.892 -0.304 -0.168 0.480  130 PRO HHH CD  
9367  N N   . SER G 132 ? 2.248 2.871 1.802 -0.240 -0.158 0.422  131 SER HHH N   
9368  C CA  . SER G 132 ? 2.318 2.960 1.806 -0.219 -0.164 0.431  131 SER HHH CA  
9369  C C   . SER G 132 ? 2.353 3.030 1.799 -0.210 -0.133 0.448  131 SER HHH C   
9370  O O   . SER G 132 ? 2.345 3.035 1.811 -0.217 -0.109 0.437  131 SER HHH O   
9371  C CB  A SER G 132 ? 2.309 2.957 1.777 -0.207 -0.189 0.383  131 SER HHH CB  
9372  C CB  B SER G 132 ? 2.312 2.961 1.779 -0.206 -0.189 0.384  131 SER HHH CB  
9373  O OG  A SER G 132 ? 2.267 2.923 1.741 -0.211 -0.179 0.342  131 SER HHH OG  
9374  O OG  B SER G 132 ? 2.317 2.954 1.788 -0.199 -0.219 0.390  131 SER HHH OG  
9375  N N   . SER G 133 ? 2.374 3.066 1.760 -0.191 -0.132 0.474  132 SER HHH N   
9376  C CA  . SER G 133 ? 2.407 3.135 1.740 -0.175 -0.101 0.497  132 SER HHH CA  
9377  C C   . SER G 133 ? 2.475 3.217 1.726 -0.144 -0.115 0.488  132 SER HHH C   
9378  O O   . SER G 133 ? 2.451 3.184 1.692 -0.138 -0.146 0.442  132 SER HHH O   
9379  C CB  . SER G 133 ? 2.416 3.150 1.769 -0.190 -0.076 0.560  132 SER HHH CB  
9380  O OG  . SER G 133 ? 2.464 3.243 1.771 -0.173 -0.042 0.585  132 SER HHH OG  
9381  N N   . GLY G 138 ? 2.619 3.534 1.724 -0.082 0.048  0.617  137 GLY HHH N   
9382  C CA  . GLY G 138 ? 2.551 3.443 1.732 -0.109 0.036  0.578  137 GLY HHH CA  
9383  C C   . GLY G 138 ? 2.552 3.485 1.759 -0.106 0.072  0.574  137 GLY HHH C   
9384  O O   . GLY G 138 ? 2.571 3.554 1.775 -0.102 0.110  0.623  137 GLY HHH O   
9385  N N   . GLY G 139 ? 2.526 3.438 1.758 -0.109 0.062  0.520  138 GLY HHH N   
9386  C CA  . GLY G 139 ? 2.506 3.450 1.758 -0.101 0.091  0.506  138 GLY HHH CA  
9387  C C   . GLY G 139 ? 2.421 3.353 1.769 -0.136 0.087  0.504  138 GLY HHH C   
9388  O O   . GLY G 139 ? 2.396 3.358 1.803 -0.160 0.104  0.552  138 GLY HHH O   
9389  N N   . THR G 140 ? 2.386 3.276 1.751 -0.140 0.065  0.450  139 THR HHH N   
9390  C CA  . THR G 140 ? 2.334 3.202 1.782 -0.171 0.054  0.442  139 THR HHH CA  
9391  C C   . THR G 140 ? 2.333 3.147 1.799 -0.191 0.015  0.429  139 THR HHH C   
9392  O O   . THR G 140 ? 2.383 3.174 1.796 -0.178 -0.006 0.404  139 THR HHH O   
9393  C CB  . THR G 140 ? 2.299 3.160 1.755 -0.159 0.061  0.397  139 THR HHH CB  
9394  O OG1 . THR G 140 ? 2.207 3.043 1.737 -0.187 0.047  0.391  139 THR HHH OG1 
9395  C CG2 . THR G 140 ? 2.322 3.141 1.714 -0.137 0.044  0.342  139 THR HHH CG2 
9396  N N   . ALA G 141 ? 2.271 3.067 1.808 -0.221 0.004  0.444  140 ALA HHH N   
9397  C CA  . ALA G 141 ? 2.212 2.959 1.776 -0.238 -0.031 0.433  140 ALA HHH CA  
9398  C C   . ALA G 141 ? 2.117 2.845 1.752 -0.259 -0.037 0.423  140 ALA HHH C   
9399  O O   . ALA G 141 ? 2.069 2.825 1.745 -0.272 -0.019 0.451  140 ALA HHH O   
9400  C CB  . ALA G 141 ? 2.253 2.993 1.811 -0.247 -0.041 0.477  140 ALA HHH CB  
9401  N N   . ALA G 142 ? 2.067 2.756 1.717 -0.263 -0.061 0.386  141 ALA HHH N   
9402  C CA  . ALA G 142 ? 1.990 2.657 1.697 -0.276 -0.068 0.369  141 ALA HHH CA  
9403  C C   . ALA G 142 ? 1.947 2.573 1.681 -0.289 -0.098 0.372  141 ALA HHH C   
9404  O O   . ALA G 142 ? 1.963 2.576 1.669 -0.282 -0.115 0.368  141 ALA HHH O   
9405  C CB  . ALA G 142 ? 1.978 2.634 1.670 -0.263 -0.065 0.322  141 ALA HHH CB  
9406  N N   . LEU G 143 ? 1.905 2.512 1.691 -0.303 -0.104 0.375  142 LEU HHH N   
9407  C CA  . LEU G 143 ? 1.919 2.483 1.733 -0.312 -0.132 0.378  142 LEU HHH CA  
9408  C C   . LEU G 143 ? 1.877 2.422 1.732 -0.316 -0.137 0.353  142 LEU HHH C   
9409  O O   . LEU G 143 ? 1.867 2.436 1.733 -0.314 -0.118 0.343  142 LEU HHH O   
9410  C CB  . LEU G 143 ? 1.978 2.533 1.805 -0.328 -0.137 0.425  142 LEU HHH CB  
9411  C CG  . LEU G 143 ? 1.998 2.577 1.863 -0.349 -0.120 0.452  142 LEU HHH CG  
9412  C CD1 . LEU G 143 ? 1.965 2.512 1.882 -0.364 -0.138 0.443  142 LEU HHH CD1 
9413  C CD2 . LEU G 143 ? 2.061 2.652 1.920 -0.363 -0.112 0.504  142 LEU HHH CD2 
9414  N N   . GLY G 144 ? 1.854 2.358 1.727 -0.316 -0.161 0.345  143 GLY HHH N   
9415  C CA  . GLY G 144 ? 1.795 2.278 1.698 -0.314 -0.167 0.319  143 GLY HHH CA  
9416  C C   . GLY G 144 ? 1.791 2.229 1.708 -0.310 -0.194 0.315  143 GLY HHH C   
9417  O O   . GLY G 144 ? 1.786 2.206 1.690 -0.308 -0.210 0.333  143 GLY HHH O   
9418  N N   . CYS G 145 ? 1.786 2.206 1.724 -0.304 -0.199 0.292  144 CYS HHH N   
9419  C CA  . CYS G 145 ? 1.788 2.166 1.735 -0.292 -0.222 0.280  144 CYS HHH CA  
9420  C C   . CYS G 145 ? 1.752 2.136 1.692 -0.274 -0.217 0.247  144 CYS HHH C   
9421  O O   . CYS G 145 ? 1.734 2.141 1.671 -0.273 -0.196 0.231  144 CYS HHH O   
9422  C CB  . CYS G 145 ? 1.790 2.143 1.766 -0.299 -0.233 0.280  144 CYS HHH CB  
9423  S SG  . CYS G 145 ? 1.885 2.201 1.873 -0.320 -0.256 0.316  144 CYS HHH SG  
9424  N N   . LEU G 146 ? 1.743 2.107 1.679 -0.258 -0.233 0.240  145 LEU HHH N   
9425  C CA  . LEU G 146 ? 1.700 2.069 1.639 -0.241 -0.228 0.213  145 LEU HHH CA  
9426  C C   . LEU G 146 ? 1.738 2.071 1.688 -0.225 -0.242 0.205  145 LEU HHH C   
9427  O O   . LEU G 146 ? 1.799 2.102 1.746 -0.216 -0.264 0.215  145 LEU HHH O   
9428  C CB  . LEU G 146 ? 1.668 2.059 1.597 -0.233 -0.234 0.210  145 LEU HHH CB  
9429  C CG  . LEU G 146 ? 1.636 2.042 1.573 -0.221 -0.227 0.187  145 LEU HHH CG  
9430  C CD1 . LEU G 146 ? 1.619 2.042 1.553 -0.234 -0.203 0.171  145 LEU HHH CD1 
9431  C CD2 . LEU G 146 ? 1.655 2.089 1.592 -0.212 -0.238 0.186  145 LEU HHH CD2 
9432  N N   . VAL G 147 ? 1.728 2.059 1.685 -0.218 -0.231 0.186  146 VAL HHH N   
9433  C CA  . VAL G 147 ? 1.735 2.032 1.695 -0.198 -0.242 0.174  146 VAL HHH CA  
9434  C C   . VAL G 147 ? 1.745 2.055 1.702 -0.176 -0.232 0.157  146 VAL HHH C   
9435  O O   . VAL G 147 ? 1.703 2.031 1.661 -0.178 -0.210 0.145  146 VAL HHH O   
9436  C CB  . VAL G 147 ? 1.728 2.019 1.697 -0.203 -0.236 0.168  146 VAL HHH CB  
9437  C CG1 . VAL G 147 ? 1.766 2.021 1.732 -0.180 -0.251 0.154  146 VAL HHH CG1 
9438  C CG2 . VAL G 147 ? 1.739 2.033 1.719 -0.229 -0.242 0.188  146 VAL HHH CG2 
9439  N N   . LYS G 148 ? 1.810 2.112 1.764 -0.156 -0.247 0.158  147 LYS HHH N   
9440  C CA  . LYS G 148 ? 1.827 2.158 1.784 -0.138 -0.237 0.148  147 LYS HHH CA  
9441  C C   . LYS G 148 ? 1.837 2.144 1.789 -0.103 -0.243 0.138  147 LYS HHH C   
9442  O O   . LYS G 148 ? 1.876 2.138 1.816 -0.090 -0.267 0.140  147 LYS HHH O   
9443  C CB  . LYS G 148 ? 1.858 2.215 1.818 -0.138 -0.247 0.159  147 LYS HHH CB  
9444  C CG  . LYS G 148 ? 1.884 2.291 1.858 -0.132 -0.235 0.150  147 LYS HHH CG  
9445  C CD  . LYS G 148 ? 1.955 2.391 1.932 -0.122 -0.251 0.159  147 LYS HHH CD  
9446  C CE  . LYS G 148 ? 1.982 2.476 1.983 -0.114 -0.240 0.151  147 LYS HHH CE  
9447  N NZ  . LYS G 148 ? 1.986 2.518 2.000 -0.147 -0.224 0.144  147 LYS HHH NZ  
9448  N N   . ASP G 149 ? 1.826 2.159 1.782 -0.090 -0.224 0.128  148 ASP HHH N   
9449  C CA  . ASP G 149 ? 1.856 2.182 1.805 -0.050 -0.224 0.120  148 ASP HHH CA  
9450  C C   . ASP G 149 ? 1.866 2.137 1.794 -0.032 -0.239 0.111  148 ASP HHH C   
9451  O O   . ASP G 149 ? 1.882 2.115 1.795 -0.008 -0.264 0.110  148 ASP HHH O   
9452  C CB  . ASP G 149 ? 1.901 2.243 1.853 -0.028 -0.240 0.126  148 ASP HHH CB  
9453  C CG  . ASP G 149 ? 1.908 2.317 1.885 -0.040 -0.226 0.131  148 ASP HHH CG  
9454  O OD1 . ASP G 149 ? 1.906 2.349 1.899 -0.057 -0.201 0.127  148 ASP HHH OD1 
9455  O OD2 . ASP G 149 ? 1.931 2.357 1.912 -0.032 -0.243 0.139  148 ASP HHH OD2 
9456  N N   . TYR G 150 ? 1.846 2.109 1.770 -0.042 -0.225 0.104  149 TYR HHH N   
9457  C CA  . TYR G 150 ? 1.842 2.062 1.748 -0.024 -0.237 0.093  149 TYR HHH CA  
9458  C C   . TYR G 150 ? 1.818 2.049 1.714 -0.009 -0.209 0.084  149 TYR HHH C   
9459  O O   . TYR G 150 ? 1.780 2.047 1.688 -0.026 -0.181 0.089  149 TYR HHH O   
9460  C CB  . TYR G 150 ? 1.836 2.036 1.749 -0.055 -0.251 0.097  149 TYR HHH CB  
9461  C CG  . TYR G 150 ? 1.810 2.039 1.735 -0.082 -0.227 0.100  149 TYR HHH CG  
9462  C CD1 . TYR G 150 ? 1.813 2.037 1.729 -0.073 -0.216 0.090  149 TYR HHH CD1 
9463  C CD2 . TYR G 150 ? 1.790 2.048 1.729 -0.112 -0.218 0.112  149 TYR HHH CD2 
9464  C CE1 . TYR G 150 ? 1.796 2.042 1.718 -0.092 -0.194 0.092  149 TYR HHH CE1 
9465  C CE2 . TYR G 150 ? 1.761 2.041 1.704 -0.132 -0.196 0.112  149 TYR HHH CE2 
9466  C CZ  . TYR G 150 ? 1.761 2.033 1.695 -0.121 -0.184 0.103  149 TYR HHH CZ  
9467  O OH  . TYR G 150 ? 1.731 2.018 1.664 -0.135 -0.164 0.102  149 TYR HHH OH  
9468  N N   . PHE G 151 ? 1.847 2.045 1.718 0.021  -0.219 0.072  150 PHE HHH N   
9469  C CA  . PHE G 151 ? 1.856 2.057 1.708 0.046  -0.195 0.064  150 PHE HHH CA  
9470  C C   . PHE G 151 ? 1.888 2.045 1.710 0.075  -0.220 0.049  150 PHE HHH C   
9471  O O   . PHE G 151 ? 1.931 2.054 1.743 0.090  -0.252 0.041  150 PHE HHH O   
9472  C CB  . PHE G 151 ? 1.871 2.101 1.720 0.072  -0.174 0.069  150 PHE HHH CB  
9473  C CG  . PHE G 151 ? 1.866 2.113 1.703 0.087  -0.138 0.071  150 PHE HHH CG  
9474  C CD1 . PHE G 151 ? 1.838 2.101 1.688 0.056  -0.112 0.078  150 PHE HHH CD1 
9475  C CD2 . PHE G 151 ? 1.910 2.155 1.721 0.134  -0.129 0.067  150 PHE HHH CD2 
9476  C CE1 . PHE G 151 ? 1.852 2.122 1.688 0.068  -0.078 0.083  150 PHE HHH CE1 
9477  C CE2 . PHE G 151 ? 1.924 2.182 1.721 0.146  -0.094 0.074  150 PHE HHH CE2 
9478  C CZ  . PHE G 151 ? 1.891 2.160 1.703 0.112  -0.068 0.082  150 PHE HHH CZ  
9479  N N   . PRO G 152 ? 1.885 2.036 1.692 0.084  -0.208 0.042  151 PRO HHH N   
9480  C CA  . PRO G 152 ? 1.851 2.029 1.668 0.063  -0.176 0.050  151 PRO HHH CA  
9481  C C   . PRO G 152 ? 1.821 2.004 1.663 0.024  -0.187 0.054  151 PRO HHH C   
9482  O O   . PRO G 152 ? 1.822 1.991 1.676 0.012  -0.217 0.053  151 PRO HHH O   
9483  C CB  . PRO G 152 ? 1.896 2.058 1.679 0.097  -0.166 0.041  151 PRO HHH CB  
9484  C CG  . PRO G 152 ? 1.934 2.060 1.699 0.119  -0.207 0.024  151 PRO HHH CG  
9485  C CD  . PRO G 152 ? 1.944 2.058 1.717 0.119  -0.230 0.024  151 PRO HHH CD  
9486  N N   . GLU G 153 ? 1.810 2.010 1.656 0.006  -0.161 0.059  152 GLU HHH N   
9487  C CA  . GLU G 153 ? 1.809 2.020 1.675 -0.024 -0.168 0.063  152 GLU HHH CA  
9488  C C   . GLU G 153 ? 1.837 2.036 1.693 -0.006 -0.183 0.052  152 GLU HHH C   
9489  O O   . GLU G 153 ? 1.858 2.038 1.686 0.028  -0.184 0.042  152 GLU HHH O   
9490  C CB  . GLU G 153 ? 1.784 2.018 1.658 -0.050 -0.138 0.071  152 GLU HHH CB  
9491  C CG  . GLU G 153 ? 1.804 2.032 1.655 -0.037 -0.107 0.070  152 GLU HHH CG  
9492  C CD  . GLU G 153 ? 1.793 2.034 1.649 -0.064 -0.087 0.074  152 GLU HHH CD  
9493  O OE1 . GLU G 153 ? 1.766 2.023 1.639 -0.086 -0.099 0.078  152 GLU HHH OE1 
9494  O OE2 . GLU G 153 ? 1.802 2.032 1.640 -0.063 -0.060 0.075  152 GLU HHH OE2 
9495  N N   . PRO G 154 ? 1.826 2.039 1.703 -0.028 -0.197 0.054  153 PRO HHH N   
9496  C CA  . PRO G 154 ? 1.792 2.030 1.697 -0.066 -0.193 0.068  153 PRO HHH CA  
9497  C C   . PRO G 154 ? 1.791 2.026 1.722 -0.088 -0.225 0.075  153 PRO HHH C   
9498  O O   . PRO G 154 ? 1.810 2.018 1.739 -0.077 -0.255 0.067  153 PRO HHH O   
9499  C CB  . PRO G 154 ? 1.801 2.063 1.711 -0.068 -0.183 0.068  153 PRO HHH CB  
9500  C CG  . PRO G 154 ? 1.821 2.071 1.724 -0.044 -0.206 0.055  153 PRO HHH CG  
9501  C CD  . PRO G 154 ? 1.841 2.054 1.718 -0.016 -0.216 0.045  153 PRO HHH CD  
9502  N N   . VAL G 155 ? 1.760 2.018 1.711 -0.119 -0.218 0.091  154 VAL HHH N   
9503  C CA  . VAL G 155 ? 1.754 2.012 1.730 -0.147 -0.242 0.105  154 VAL HHH CA  
9504  C C   . VAL G 155 ? 1.721 2.020 1.721 -0.172 -0.233 0.118  154 VAL HHH C   
9505  O O   . VAL G 155 ? 1.688 2.012 1.678 -0.169 -0.204 0.117  154 VAL HHH O   
9506  C CB  . VAL G 155 ? 1.764 2.016 1.737 -0.156 -0.242 0.116  154 VAL HHH CB  
9507  C CG1 . VAL G 155 ? 1.780 2.029 1.774 -0.185 -0.262 0.135  154 VAL HHH CG1 
9508  C CG2 . VAL G 155 ? 1.804 2.024 1.757 -0.128 -0.251 0.104  154 VAL HHH CG2 
9509  N N   . THR G 156 ? 1.734 2.038 1.763 -0.195 -0.256 0.130  155 THR HHH N   
9510  C CA  . THR G 156 ? 1.707 2.059 1.767 -0.221 -0.249 0.148  155 THR HHH CA  
9511  C C   . THR G 156 ? 1.694 2.046 1.772 -0.253 -0.258 0.174  155 THR HHH C   
9512  O O   . THR G 156 ? 1.706 2.014 1.784 -0.258 -0.285 0.175  155 THR HHH O   
9513  C CB  . THR G 156 ? 1.721 2.090 1.809 -0.223 -0.268 0.143  155 THR HHH CB  
9514  O OG1 . THR G 156 ? 1.774 2.103 1.875 -0.235 -0.307 0.142  155 THR HHH OG1 
9515  C CG2 . THR G 156 ? 1.717 2.085 1.784 -0.187 -0.261 0.119  155 THR HHH CG2 
9516  N N   . VAL G 157 ? 1.664 2.060 1.751 -0.270 -0.236 0.193  156 VAL HHH N   
9517  C CA  . VAL G 157 ? 1.678 2.079 1.775 -0.298 -0.238 0.222  156 VAL HHH CA  
9518  C C   . VAL G 157 ? 1.695 2.152 1.828 -0.323 -0.230 0.245  156 VAL HHH C   
9519  O O   . VAL G 157 ? 1.696 2.198 1.833 -0.312 -0.209 0.239  156 VAL HHH O   
9520  C CB  . VAL G 157 ? 1.652 2.058 1.716 -0.292 -0.215 0.225  156 VAL HHH CB  
9521  C CG1 . VAL G 157 ? 1.682 2.081 1.747 -0.313 -0.223 0.252  156 VAL HHH CG1 
9522  C CG2 . VAL G 157 ? 1.628 2.001 1.662 -0.266 -0.215 0.200  156 VAL HHH CG2 
9523  N N   . SER G 158 ? 1.735 2.189 1.893 -0.354 -0.244 0.274  157 SER HHH N   
9524  C CA  . SER G 158 ? 1.757 2.271 1.954 -0.383 -0.232 0.305  157 SER HHH CA  
9525  C C   . SER G 158 ? 1.770 2.274 1.964 -0.408 -0.231 0.340  157 SER HHH C   
9526  O O   . SER G 158 ? 1.787 2.230 1.955 -0.404 -0.248 0.337  157 SER HHH O   
9527  C CB  . SER G 158 ? 1.784 2.315 2.032 -0.401 -0.256 0.305  157 SER HHH CB  
9528  O OG  . SER G 158 ? 1.851 2.324 2.114 -0.425 -0.292 0.313  157 SER HHH OG  
9529  N N   . TRP G 159 ? 1.759 2.323 1.975 -0.428 -0.210 0.372  158 TRP HHH N   
9530  C CA  . TRP G 159 ? 1.794 2.357 1.997 -0.446 -0.200 0.409  158 TRP HHH CA  
9531  C C   . TRP G 159 ? 1.835 2.423 2.090 -0.489 -0.206 0.450  158 TRP HHH C   
9532  O O   . TRP G 159 ? 1.802 2.460 2.101 -0.499 -0.193 0.458  158 TRP HHH O   
9533  C CB  . TRP G 159 ? 1.780 2.390 1.945 -0.425 -0.163 0.412  158 TRP HHH CB  
9534  C CG  . TRP G 159 ? 1.746 2.319 1.859 -0.394 -0.161 0.380  158 TRP HHH CG  
9535  C CD1 . TRP G 159 ? 1.699 2.274 1.793 -0.366 -0.152 0.344  158 TRP HHH CD1 
9536  C CD2 . TRP G 159 ? 1.764 2.293 1.838 -0.388 -0.169 0.383  158 TRP HHH CD2 
9537  N NE1 . TRP G 159 ? 1.692 2.231 1.744 -0.348 -0.154 0.325  158 TRP HHH NE1 
9538  C CE2 . TRP G 159 ? 1.729 2.245 1.770 -0.360 -0.165 0.347  158 TRP HHH CE2 
9539  C CE3 . TRP G 159 ? 1.823 2.325 1.888 -0.403 -0.180 0.414  158 TRP HHH CE3 
9540  C CZ2 . TRP G 159 ? 1.753 2.238 1.758 -0.348 -0.173 0.340  158 TRP HHH CZ2 
9541  C CZ3 . TRP G 159 ? 1.844 2.311 1.866 -0.386 -0.188 0.406  158 TRP HHH CZ3 
9542  C CH2 . TRP G 159 ? 1.806 2.269 1.802 -0.359 -0.184 0.369  158 TRP HHH CH2 
9543  N N   . ASN G 160 ? 1.907 2.439 2.158 -0.512 -0.225 0.475  159 ASN HHH N   
9544  C CA  . ASN G 160 ? 1.976 2.509 2.276 -0.560 -0.236 0.517  159 ASN HHH CA  
9545  C C   . ASN G 160 ? 1.964 2.499 2.320 -0.580 -0.265 0.501  159 ASN HHH C   
9546  O O   . ASN G 160 ? 1.991 2.583 2.406 -0.616 -0.261 0.530  159 ASN HHH O   
9547  C CB  . ASN G 160 ? 2.007 2.621 2.322 -0.577 -0.198 0.563  159 ASN HHH CB  
9548  C CG  . ASN G 160 ? 2.054 2.644 2.317 -0.570 -0.183 0.590  159 ASN HHH CG  
9549  O OD1 . ASN G 160 ? 2.043 2.598 2.250 -0.535 -0.183 0.565  159 ASN HHH OD1 
9550  N ND2 . ASN G 160 ? 2.109 2.718 2.391 -0.604 -0.171 0.643  159 ASN HHH ND2 
9551  N N   . SER G 161 ? 1.927 2.406 2.264 -0.556 -0.292 0.457  160 SER HHH N   
9552  C CA  . SER G 161 ? 1.923 2.393 2.300 -0.565 -0.325 0.432  160 SER HHH CA  
9553  C C   . SER G 161 ? 1.850 2.398 2.242 -0.539 -0.306 0.407  160 SER HHH C   
9554  O O   . SER G 161 ? 1.848 2.384 2.253 -0.529 -0.331 0.375  160 SER HHH O   
9555  C CB  . SER G 161 ? 1.980 2.455 2.420 -0.620 -0.347 0.465  160 SER HHH CB  
9556  O OG  . SER G 161 ? 1.996 2.425 2.459 -0.630 -0.392 0.437  160 SER HHH OG  
9557  N N   . GLY G 162 ? 1.802 2.423 2.184 -0.524 -0.263 0.419  161 GLY HHH N   
9558  C CA  . GLY G 162 ? 1.745 2.439 2.135 -0.497 -0.241 0.399  161 GLY HHH CA  
9559  C C   . GLY G 162 ? 1.736 2.533 2.166 -0.513 -0.208 0.434  161 GLY HHH C   
9560  O O   . GLY G 162 ? 1.686 2.548 2.123 -0.487 -0.189 0.421  161 GLY HHH O   
9561  N N   . ALA G 163 ? 1.793 2.603 2.246 -0.550 -0.202 0.479  162 ALA HHH N   
9562  C CA  . ALA G 163 ? 1.819 2.729 2.307 -0.566 -0.166 0.521  162 ALA HHH CA  
9563  C C   . ALA G 163 ? 1.840 2.756 2.264 -0.539 -0.128 0.533  162 ALA HHH C   
9564  O O   . ALA G 163 ? 1.911 2.849 2.339 -0.562 -0.110 0.577  162 ALA HHH O   
9565  C CB  . ALA G 163 ? 1.858 2.778 2.408 -0.625 -0.181 0.566  162 ALA HHH CB  
9566  N N   . LEU G 164 ? 1.807 2.701 2.172 -0.493 -0.118 0.494  163 LEU HHH N   
9567  C CA  . LEU G 164 ? 1.802 2.703 2.103 -0.463 -0.085 0.495  163 LEU HHH CA  
9568  C C   . LEU G 164 ? 1.761 2.638 2.014 -0.418 -0.080 0.445  163 LEU HHH C   
9569  O O   . LEU G 164 ? 1.734 2.536 1.945 -0.406 -0.096 0.421  163 LEU HHH O   
9570  C CB  . LEU G 164 ? 1.839 2.673 2.102 -0.475 -0.094 0.512  163 LEU HHH CB  
9571  C CG  . LEU G 164 ? 1.861 2.720 2.071 -0.459 -0.061 0.531  163 LEU HHH CG  
9572  C CD1 . LEU G 164 ? 1.902 2.819 2.144 -0.489 -0.042 0.589  163 LEU HHH CD1 
9573  C CD2 . LEU G 164 ? 1.854 2.636 2.006 -0.447 -0.076 0.519  163 LEU HHH CD2 
9574  N N   . THR G 165 ? 1.758 2.695 2.020 -0.393 -0.061 0.432  164 THR HHH N   
9575  C CA  . THR G 165 ? 1.740 2.660 1.953 -0.348 -0.050 0.390  164 THR HHH CA  
9576  C C   . THR G 165 ? 1.744 2.706 1.912 -0.322 -0.011 0.396  164 THR HHH C   
9577  O O   . THR G 165 ? 1.725 2.667 1.845 -0.285 0.000  0.364  164 THR HHH O   
9578  C CB  . THR G 165 ? 1.741 2.690 1.987 -0.333 -0.056 0.369  164 THR HHH CB  
9579  O OG1 . THR G 165 ? 1.750 2.798 2.041 -0.336 -0.036 0.395  164 THR HHH OG1 
9580  C CG2 . THR G 165 ? 1.744 2.650 2.027 -0.354 -0.096 0.358  164 THR HHH CG2 
9581  N N   . SER G 166 ? 1.769 2.784 1.949 -0.338 0.007  0.436  165 SER HHH N   
9582  C CA  . SER G 166 ? 1.791 2.852 1.925 -0.312 0.044  0.447  165 SER HHH CA  
9583  C C   . SER G 166 ? 1.818 2.808 1.873 -0.291 0.043  0.420  165 SER HHH C   
9584  O O   . SER G 166 ? 1.853 2.818 1.886 -0.307 0.038  0.439  165 SER HHH O   
9585  C CB  . SER G 166 ? 1.810 2.936 1.976 -0.338 0.061  0.500  165 SER HHH CB  
9586  O OG  . SER G 166 ? 1.758 2.945 2.008 -0.366 0.055  0.524  165 SER HHH OG  
9587  N N   . GLY G 167 ? 1.802 2.757 1.817 -0.259 0.044  0.378  166 GLY HHH N   
9588  C CA  . GLY G 167 ? 1.806 2.704 1.748 -0.237 0.046  0.348  166 GLY HHH CA  
9589  C C   . GLY G 167 ? 1.776 2.597 1.712 -0.254 0.015  0.331  166 GLY HHH C   
9590  O O   . GLY G 167 ? 1.762 2.556 1.661 -0.258 0.011  0.333  166 GLY HHH O   
9591  N N   . VAL G 168 ? 1.740 2.530 1.708 -0.259 -0.004 0.313  167 VAL HHH N   
9592  C CA  . VAL G 168 ? 1.720 2.443 1.691 -0.273 -0.033 0.298  167 VAL HHH CA  
9593  C C   . VAL G 168 ? 1.742 2.421 1.689 -0.251 -0.035 0.258  167 VAL HHH C   
9594  O O   . VAL G 168 ? 1.784 2.475 1.750 -0.239 -0.032 0.248  167 VAL HHH O   
9595  C CB  . VAL G 168 ? 1.674 2.396 1.704 -0.300 -0.057 0.316  167 VAL HHH CB  
9596  C CG1 . VAL G 168 ? 1.646 2.303 1.672 -0.310 -0.085 0.306  167 VAL HHH CG1 
9597  C CG2 . VAL G 168 ? 1.708 2.481 1.773 -0.325 -0.051 0.360  167 VAL HHH CG2 
9598  N N   . HIS G 169 ? 1.765 2.398 1.675 -0.248 -0.041 0.238  168 HIS HHH N   
9599  C CA  . HIS G 169 ? 1.776 2.361 1.663 -0.232 -0.043 0.204  168 HIS HHH CA  
9600  C C   . HIS G 169 ? 1.779 2.324 1.686 -0.245 -0.067 0.199  168 HIS HHH C   
9601  O O   . HIS G 169 ? 1.770 2.305 1.673 -0.258 -0.080 0.208  168 HIS HHH O   
9602  C CB  . HIS G 169 ? 1.811 2.377 1.644 -0.222 -0.031 0.185  168 HIS HHH CB  
9603  C CG  . HIS G 169 ? 1.874 2.474 1.675 -0.205 -0.008 0.189  168 HIS HHH CG  
9604  N ND1 . HIS G 169 ? 1.912 2.500 1.681 -0.179 0.010  0.167  168 HIS HHH ND1 
9605  C CD2 . HIS G 169 ? 1.915 2.558 1.707 -0.207 0.001  0.212  168 HIS HHH CD2 
9606  C CE1 . HIS G 169 ? 1.974 2.597 1.714 -0.163 0.028  0.175  168 HIS HHH CE1 
9607  N NE2 . HIS G 169 ? 1.960 2.621 1.715 -0.181 0.025  0.204  168 HIS HHH NE2 
9608  N N   . THR G 170 ? 1.791 2.315 1.714 -0.235 -0.073 0.184  169 THR HHH N   
9609  C CA  . THR G 170 ? 1.773 2.258 1.709 -0.239 -0.094 0.176  169 THR HHH CA  
9610  C C   . THR G 170 ? 1.746 2.197 1.658 -0.221 -0.085 0.150  169 THR HHH C   
9611  O O   . THR G 170 ? 1.766 2.216 1.677 -0.204 -0.075 0.140  169 THR HHH O   
9612  C CB  . THR G 170 ? 1.788 2.277 1.764 -0.244 -0.113 0.186  169 THR HHH CB  
9613  O OG1 . THR G 170 ? 1.805 2.311 1.801 -0.266 -0.124 0.213  169 THR HHH OG1 
9614  C CG2 . THR G 170 ? 1.794 2.242 1.775 -0.236 -0.131 0.172  169 THR HHH CG2 
9615  N N   . PHE G 171 ? 1.709 2.138 1.606 -0.226 -0.088 0.140  170 PHE HHH N   
9616  C CA  . PHE G 171 ? 1.703 2.103 1.574 -0.218 -0.074 0.119  170 PHE HHH CA  
9617  C C   . PHE G 171 ? 1.676 2.050 1.557 -0.205 -0.077 0.110  170 PHE HHH C   
9618  O O   . PHE G 171 ? 1.654 2.028 1.558 -0.203 -0.094 0.117  170 PHE HHH O   
9619  C CB  . PHE G 171 ? 1.715 2.111 1.574 -0.232 -0.079 0.114  170 PHE HHH CB  
9620  C CG  . PHE G 171 ? 1.736 2.155 1.575 -0.240 -0.076 0.120  170 PHE HHH CG  
9621  C CD1 . PHE G 171 ? 1.762 2.173 1.564 -0.234 -0.059 0.106  170 PHE HHH CD1 
9622  C CD2 . PHE G 171 ? 1.737 2.180 1.586 -0.250 -0.090 0.140  170 PHE HHH CD2 
9623  C CE1 . PHE G 171 ? 1.792 2.223 1.569 -0.237 -0.056 0.110  170 PHE HHH CE1 
9624  C CE2 . PHE G 171 ? 1.763 2.228 1.588 -0.254 -0.085 0.147  170 PHE HHH CE2 
9625  C CZ  . PHE G 171 ? 1.790 2.251 1.578 -0.246 -0.069 0.131  170 PHE HHH CZ  
9626  N N   . PRO G 172 ? 1.691 2.038 1.550 -0.194 -0.061 0.095  171 PRO HHH N   
9627  C CA  . PRO G 172 ? 1.693 2.015 1.555 -0.181 -0.060 0.089  171 PRO HHH CA  
9628  C C   . PRO G 172 ? 1.675 1.999 1.555 -0.190 -0.074 0.092  171 PRO HHH C   
9629  O O   . PRO G 172 ? 1.684 2.022 1.567 -0.207 -0.079 0.094  171 PRO HHH O   
9630  C CB  . PRO G 172 ? 1.728 2.018 1.559 -0.177 -0.037 0.076  171 PRO HHH CB  
9631  C CG  . PRO G 172 ? 1.746 2.040 1.554 -0.177 -0.026 0.073  171 PRO HHH CG  
9632  C CD  . PRO G 172 ? 1.734 2.067 1.559 -0.192 -0.041 0.084  171 PRO HHH CD  
9633  N N   . ALA G 173 ? 1.665 1.979 1.555 -0.174 -0.082 0.092  172 ALA HHH N   
9634  C CA  . ALA G 173 ? 1.649 1.965 1.553 -0.173 -0.092 0.094  172 ALA HHH CA  
9635  C C   . ALA G 173 ? 1.646 1.959 1.544 -0.179 -0.073 0.088  172 ALA HHH C   
9636  O O   . ALA G 173 ? 1.650 1.942 1.529 -0.176 -0.052 0.082  172 ALA HHH O   
9637  C CB  . ALA G 173 ? 1.658 1.960 1.566 -0.148 -0.103 0.093  172 ALA HHH CB  
9638  N N   . VAL G 174 ? 1.645 1.979 1.560 -0.189 -0.080 0.091  173 VAL HHH N   
9639  C CA  . VAL G 174 ? 1.678 2.019 1.599 -0.199 -0.065 0.087  173 VAL HHH CA  
9640  C C   . VAL G 174 ? 1.649 2.008 1.589 -0.182 -0.071 0.093  173 VAL HHH C   
9641  O O   . VAL G 174 ? 1.646 2.020 1.598 -0.175 -0.093 0.098  173 VAL HHH O   
9642  C CB  . VAL G 174 ? 1.736 2.095 1.661 -0.228 -0.068 0.083  173 VAL HHH CB  
9643  C CG1 . VAL G 174 ? 1.778 2.112 1.674 -0.239 -0.056 0.074  173 VAL HHH CG1 
9644  C CG2 . VAL G 174 ? 1.743 2.132 1.680 -0.233 -0.092 0.089  173 VAL HHH CG2 
9645  N N   . LEU G 175 ? 1.653 2.009 1.594 -0.172 -0.051 0.094  174 LEU HHH N   
9646  C CA  . LEU G 175 ? 1.668 2.046 1.624 -0.150 -0.052 0.100  174 LEU HHH CA  
9647  C C   . LEU G 175 ? 1.659 2.086 1.648 -0.169 -0.054 0.103  174 LEU HHH C   
9648  O O   . LEU G 175 ? 1.667 2.105 1.668 -0.192 -0.035 0.104  174 LEU HHH O   
9649  C CB  . LEU G 175 ? 1.698 2.055 1.638 -0.130 -0.026 0.102  174 LEU HHH CB  
9650  C CG  . LEU G 175 ? 1.722 2.108 1.677 -0.110 -0.013 0.110  174 LEU HHH CG  
9651  C CD1 . LEU G 175 ? 1.715 2.107 1.666 -0.074 -0.035 0.109  174 LEU HHH CD1 
9652  C CD2 . LEU G 175 ? 1.770 2.131 1.703 -0.097 0.018  0.116  174 LEU HHH CD2 
9653  N N   . GLN G 176 ? 1.653 2.105 1.656 -0.162 -0.078 0.106  175 GLN HHH N   
9654  C CA  . GLN G 176 ? 1.659 2.168 1.696 -0.173 -0.084 0.110  175 GLN HHH CA  
9655  C C   . GLN G 176 ? 1.667 2.210 1.726 -0.162 -0.063 0.116  175 GLN HHH C   
9656  O O   . GLN G 176 ? 1.678 2.196 1.719 -0.136 -0.048 0.119  175 GLN HHH O   
9657  C CB  . GLN G 176 ? 1.661 2.183 1.701 -0.154 -0.113 0.114  175 GLN HHH CB  
9658  C CG  . GLN G 176 ? 1.660 2.170 1.688 -0.172 -0.133 0.113  175 GLN HHH CG  
9659  C CD  . GLN G 176 ? 1.668 2.164 1.687 -0.148 -0.159 0.120  175 GLN HHH CD  
9660  O OE1 . GLN G 176 ? 1.677 2.131 1.675 -0.146 -0.168 0.121  175 GLN HHH OE1 
9661  N NE2 . GLN G 176 ? 1.681 2.210 1.715 -0.128 -0.170 0.125  175 GLN HHH NE2 
9662  N N   . SER G 177 ? 1.666 2.267 1.762 -0.180 -0.062 0.120  176 SER HHH N   
9663  C CA  . SER G 177 ? 1.661 2.318 1.791 -0.168 -0.044 0.130  176 SER HHH CA  
9664  C C   . SER G 177 ? 1.662 2.318 1.778 -0.115 -0.049 0.135  176 SER HHH C   
9665  O O   . SER G 177 ? 1.688 2.353 1.804 -0.091 -0.025 0.143  176 SER HHH O   
9666  C CB  . SER G 177 ? 1.648 2.378 1.825 -0.193 -0.054 0.132  176 SER HHH CB  
9667  O OG  . SER G 177 ? 1.635 2.373 1.807 -0.187 -0.087 0.127  176 SER HHH OG  
9668  N N   . SER G 178 ? 1.659 2.298 1.759 -0.096 -0.078 0.131  177 SER HHH N   
9669  C CA  . SER G 178 ? 1.675 2.295 1.752 -0.046 -0.093 0.131  177 SER HHH CA  
9670  C C   . SER G 178 ? 1.663 2.236 1.707 -0.018 -0.077 0.128  177 SER HHH C   
9671  O O   . SER G 178 ? 1.691 2.259 1.718 0.028  -0.081 0.128  177 SER HHH O   
9672  C CB  . SER G 178 ? 1.698 2.279 1.755 -0.045 -0.126 0.127  177 SER HHH CB  
9673  O OG  . SER G 178 ? 1.741 2.309 1.782 0.000  -0.146 0.127  177 SER HHH OG  
9674  N N   . GLY G 179 ? 1.626 2.164 1.656 -0.040 -0.060 0.125  178 GLY HHH N   
9675  C CA  . GLY G 179 ? 1.637 2.130 1.631 -0.013 -0.046 0.123  178 GLY HHH CA  
9676  C C   . GLY G 179 ? 1.631 2.063 1.592 -0.002 -0.072 0.112  178 GLY HHH C   
9677  O O   . GLY G 179 ? 1.645 2.039 1.573 0.025  -0.069 0.106  178 GLY HHH O   
9678  N N   . LEU G 180 ? 1.624 2.050 1.592 -0.023 -0.098 0.109  179 LEU HHH N   
9679  C CA  . LEU G 180 ? 1.636 2.013 1.583 -0.023 -0.125 0.102  179 LEU HHH CA  
9680  C C   . LEU G 180 ? 1.618 1.993 1.574 -0.066 -0.125 0.103  179 LEU HHH C   
9681  O O   . LEU G 180 ? 1.614 2.025 1.592 -0.092 -0.120 0.108  179 LEU HHH O   
9682  C CB  . LEU G 180 ? 1.651 2.020 1.597 -0.005 -0.156 0.103  179 LEU HHH CB  
9683  C CG  . LEU G 180 ? 1.686 2.069 1.626 0.039  -0.157 0.103  179 LEU HHH CG  
9684  C CD1 . LEU G 180 ? 1.713 2.073 1.643 0.058  -0.191 0.103  179 LEU HHH CD1 
9685  C CD2 . LEU G 180 ? 1.726 2.082 1.636 0.076  -0.147 0.095  179 LEU HHH CD2 
9686  N N   . TYR G 181 ? 1.604 1.942 1.543 -0.072 -0.132 0.099  180 TYR HHH N   
9687  C CA  . TYR G 181 ? 1.586 1.923 1.528 -0.105 -0.128 0.100  180 TYR HHH CA  
9688  C C   . TYR G 181 ? 1.599 1.944 1.550 -0.123 -0.151 0.107  180 TYR HHH C   
9689  O O   . TYR G 181 ? 1.625 1.959 1.577 -0.108 -0.174 0.111  180 TYR HHH O   
9690  C CB  . TYR G 181 ? 1.572 1.876 1.495 -0.098 -0.128 0.094  180 TYR HHH CB  
9691  C CG  . TYR G 181 ? 1.566 1.858 1.472 -0.080 -0.105 0.089  180 TYR HHH CG  
9692  C CD1 . TYR G 181 ? 1.565 1.861 1.467 -0.096 -0.077 0.090  180 TYR HHH CD1 
9693  C CD2 . TYR G 181 ? 1.580 1.850 1.467 -0.046 -0.110 0.083  180 TYR HHH CD2 
9694  C CE1 . TYR G 181 ? 1.581 1.859 1.463 -0.080 -0.054 0.088  180 TYR HHH CE1 
9695  C CE2 . TYR G 181 ? 1.603 1.860 1.469 -0.026 -0.087 0.081  180 TYR HHH CE2 
9696  C CZ  . TYR G 181 ? 1.602 1.863 1.466 -0.043 -0.058 0.085  180 TYR HHH CZ  
9697  O OH  . TYR G 181 ? 1.650 1.892 1.488 -0.023 -0.035 0.086  180 TYR HHH OH  
9698  N N   . SER G 182 ? 1.600 1.959 1.554 -0.152 -0.144 0.109  181 SER HHH N   
9699  C CA  . SER G 182 ? 1.588 1.954 1.545 -0.171 -0.160 0.118  181 SER HHH CA  
9700  C C   . SER G 182 ? 1.563 1.926 1.510 -0.191 -0.148 0.118  181 SER HHH C   
9701  O O   . SER G 182 ? 1.553 1.914 1.492 -0.193 -0.127 0.108  181 SER HHH O   
9702  C CB  . SER G 182 ? 1.590 1.990 1.558 -0.180 -0.166 0.122  181 SER HHH CB  
9703  O OG  . SER G 182 ? 1.585 1.991 1.546 -0.199 -0.176 0.131  181 SER HHH OG  
9704  N N   . LEU G 183 ? 1.546 1.910 1.493 -0.202 -0.161 0.129  182 LEU HHH N   
9705  C CA  . LEU G 183 ? 1.546 1.912 1.486 -0.213 -0.150 0.131  182 LEU HHH CA  
9706  C C   . LEU G 183 ? 1.569 1.947 1.510 -0.229 -0.162 0.148  182 LEU HHH C   
9707  O O   . LEU G 183 ? 1.570 1.936 1.521 -0.227 -0.182 0.161  182 LEU HHH O   
9708  C CB  . LEU G 183 ? 1.557 1.902 1.500 -0.199 -0.153 0.127  182 LEU HHH CB  
9709  C CG  . LEU G 183 ? 1.573 1.928 1.518 -0.206 -0.147 0.132  182 LEU HHH CG  
9710  C CD1 . LEU G 183 ? 1.587 1.928 1.530 -0.188 -0.142 0.121  182 LEU HHH CD1 
9711  C CD2 . LEU G 183 ? 1.589 1.950 1.551 -0.220 -0.167 0.151  182 LEU HHH CD2 
9712  N N   . SER G 184 ? 1.608 2.006 1.535 -0.241 -0.149 0.150  183 SER HHH N   
9713  C CA  . SER G 184 ? 1.637 2.053 1.559 -0.255 -0.155 0.169  183 SER HHH CA  
9714  C C   . SER G 184 ? 1.629 2.057 1.555 -0.259 -0.145 0.179  183 SER HHH C   
9715  O O   . SER G 184 ? 1.619 2.045 1.541 -0.251 -0.129 0.166  183 SER HHH O   
9716  C CB  . SER G 184 ? 1.667 2.103 1.567 -0.261 -0.149 0.164  183 SER HHH CB  
9717  O OG  . SER G 184 ? 1.705 2.140 1.609 -0.258 -0.155 0.151  183 SER HHH OG  
9718  N N   . SER G 185 ? 1.644 2.083 1.579 -0.271 -0.153 0.204  184 SER HHH N   
9719  C CA  . SER G 185 ? 1.650 2.114 1.595 -0.279 -0.142 0.220  184 SER HHH CA  
9720  C C   . SER G 185 ? 1.679 2.168 1.612 -0.291 -0.139 0.246  184 SER HHH C   
9721  O O   . SER G 185 ? 1.727 2.200 1.662 -0.298 -0.156 0.262  184 SER HHH O   
9722  C CB  . SER G 185 ? 1.635 2.088 1.613 -0.284 -0.157 0.228  184 SER HHH CB  
9723  O OG  . SER G 185 ? 1.633 2.121 1.630 -0.297 -0.149 0.250  184 SER HHH OG  
9724  N N   . VAL G 186 ? 1.666 2.189 1.583 -0.290 -0.117 0.251  185 VAL HHH N   
9725  C CA  . VAL G 186 ? 1.685 2.234 1.578 -0.295 -0.109 0.273  185 VAL HHH CA  
9726  C C   . VAL G 186 ? 1.713 2.308 1.615 -0.297 -0.087 0.292  185 VAL HHH C   
9727  O O   . VAL G 186 ? 1.738 2.344 1.653 -0.288 -0.076 0.279  185 VAL HHH O   
9728  C CB  . VAL G 186 ? 1.687 2.233 1.536 -0.283 -0.104 0.251  185 VAL HHH CB  
9729  C CG1 . VAL G 186 ? 1.685 2.203 1.533 -0.284 -0.126 0.239  185 VAL HHH CG1 
9730  C CG2 . VAL G 186 ? 1.673 2.217 1.504 -0.270 -0.086 0.221  185 VAL HHH CG2 
9731  N N   . VAL G 187 ? 1.742 2.365 1.635 -0.305 -0.080 0.324  186 VAL HHH N   
9732  C CA  . VAL G 187 ? 1.755 2.434 1.657 -0.306 -0.055 0.349  186 VAL HHH CA  
9733  C C   . VAL G 187 ? 1.801 2.505 1.654 -0.297 -0.039 0.364  186 VAL HHH C   
9734  O O   . VAL G 187 ? 1.822 2.506 1.658 -0.305 -0.053 0.379  186 VAL HHH O   
9735  C CB  . VAL G 187 ? 1.761 2.455 1.719 -0.333 -0.062 0.384  186 VAL HHH CB  
9736  C CG1 . VAL G 187 ? 1.785 2.441 1.746 -0.352 -0.085 0.408  186 VAL HHH CG1 
9737  C CG2 . VAL G 187 ? 1.786 2.551 1.760 -0.336 -0.035 0.415  186 VAL HHH CG2 
9738  N N   . THR G 188 ? 1.816 2.560 1.642 -0.278 -0.012 0.360  187 THR HHH N   
9739  C CA  . THR G 188 ? 1.866 2.640 1.640 -0.263 0.005  0.375  187 THR HHH CA  
9740  C C   . THR G 188 ? 1.905 2.731 1.707 -0.279 0.022  0.427  187 THR HHH C   
9741  O O   . THR G 188 ? 1.864 2.732 1.713 -0.285 0.035  0.440  187 THR HHH O   
9742  C CB  . THR G 188 ? 1.874 2.662 1.598 -0.231 0.027  0.345  187 THR HHH CB  
9743  O OG1 . THR G 188 ? 1.854 2.598 1.581 -0.225 0.016  0.304  187 THR HHH OG1 
9744  C CG2 . THR G 188 ? 1.914 2.697 1.566 -0.213 0.029  0.337  187 THR HHH CG2 
9745  N N   . VAL G 189 ? 1.981 2.807 1.758 -0.285 0.020  0.457  188 VAL HHH N   
9746  C CA  . VAL G 189 ? 2.029 2.895 1.833 -0.305 0.033  0.514  188 VAL HHH CA  
9747  C C   . VAL G 189 ? 2.133 3.025 1.870 -0.285 0.052  0.535  188 VAL HHH C   
9748  O O   . VAL G 189 ? 2.156 3.015 1.835 -0.267 0.039  0.511  188 VAL HHH O   
9749  C CB  . VAL G 189 ? 2.005 2.822 1.848 -0.338 0.004  0.536  188 VAL HHH CB  
9750  C CG1 . VAL G 189 ? 2.049 2.891 1.910 -0.362 0.016  0.596  188 VAL HHH CG1 
9751  C CG2 . VAL G 189 ? 1.944 2.738 1.848 -0.355 -0.014 0.516  188 VAL HHH CG2 
9752  N N   . PRO G 190 ? 2.207 3.164 1.950 -0.286 0.084  0.580  189 PRO HHH N   
9753  C CA  . PRO G 190 ? 2.308 3.291 1.987 -0.267 0.104  0.608  189 PRO HHH CA  
9754  C C   . PRO G 190 ? 2.372 3.303 2.024 -0.278 0.079  0.627  189 PRO HHH C   
9755  O O   . PRO G 190 ? 2.366 3.265 2.068 -0.311 0.061  0.650  189 PRO HHH O   
9756  C CB  . PRO G 190 ? 2.306 3.368 2.022 -0.278 0.140  0.663  189 PRO HHH CB  
9757  C CG  . PRO G 190 ? 2.223 3.316 2.008 -0.288 0.145  0.646  189 PRO HHH CG  
9758  C CD  . PRO G 190 ? 2.165 3.181 1.977 -0.304 0.104  0.605  189 PRO HHH CD  
9759  N N   . SER G 191 ? 2.439 3.361 2.012 -0.248 0.077  0.616  190 SER HHH N   
9760  C CA  . SER G 191 ? 2.495 3.369 2.031 -0.250 0.051  0.628  190 SER HHH CA  
9761  C C   . SER G 191 ? 2.506 3.370 2.088 -0.284 0.051  0.688  190 SER HHH C   
9762  O O   . SER G 191 ? 2.484 3.291 2.098 -0.305 0.020  0.684  190 SER HHH O   
9763  C CB  . SER G 191 ? 2.588 3.480 2.033 -0.214 0.060  0.630  190 SER HHH CB  
9764  O OG  . SER G 191 ? 2.585 3.452 1.986 -0.190 0.038  0.569  190 SER HHH OG  
9765  N N   . SER G 192 ? 2.525 3.442 2.109 -0.290 0.086  0.742  191 SER HHH N   
9766  C CA  . SER G 192 ? 2.548 3.455 2.157 -0.321 0.091  0.809  191 SER HHH CA  
9767  C C   . SER G 192 ? 2.467 3.366 2.173 -0.368 0.084  0.825  191 SER HHH C   
9768  O O   . SER G 192 ? 2.499 3.399 2.236 -0.400 0.094  0.883  191 SER HHH O   
9769  C CB  . SER G 192 ? 2.634 3.607 2.205 -0.308 0.133  0.861  191 SER HHH CB  
9770  O OG  . SER G 192 ? 2.627 3.677 2.220 -0.299 0.166  0.854  191 SER HHH OG  
9771  N N   . SER G 193 ? 2.360 3.248 2.109 -0.372 0.068  0.775  192 SER HHH N   
9772  C CA  . SER G 193 ? 2.309 3.181 2.146 -0.413 0.053  0.779  192 SER HHH CA  
9773  C C   . SER G 193 ? 2.306 3.089 2.153 -0.435 0.015  0.788  192 SER HHH C   
9774  O O   . SER G 193 ? 2.310 3.073 2.215 -0.476 0.006  0.820  192 SER HHH O   
9775  C CB  . SER G 193 ? 2.238 3.119 2.103 -0.402 0.044  0.722  192 SER HHH CB  
9776  O OG  . SER G 193 ? 2.230 3.181 2.071 -0.373 0.077  0.707  192 SER HHH OG  
9777  N N   . LEU G 194 ? 2.294 3.024 2.086 -0.409 -0.009 0.758  193 LEU HHH N   
9778  C CA  . LEU G 194 ? 2.296 2.939 2.090 -0.417 -0.049 0.750  193 LEU HHH CA  
9779  C C   . LEU G 194 ? 2.364 2.971 2.156 -0.441 -0.051 0.813  193 LEU HHH C   
9780  O O   . LEU G 194 ? 2.335 2.872 2.156 -0.463 -0.079 0.819  193 LEU HHH O   
9781  C CB  . LEU G 194 ? 2.300 2.919 2.031 -0.378 -0.067 0.710  193 LEU HHH CB  
9782  C CG  . LEU G 194 ? 2.252 2.909 1.969 -0.352 -0.061 0.654  193 LEU HHH CG  
9783  C CD1 . LEU G 194 ? 2.260 2.895 1.921 -0.321 -0.082 0.620  193 LEU HHH CD1 
9784  C CD2 . LEU G 194 ? 2.190 2.839 1.966 -0.365 -0.070 0.617  193 LEU HHH CD2 
9785  N N   . GLY G 195 ? 2.447 3.095 2.200 -0.435 -0.020 0.859  194 GLY HHH N   
9786  C CA  . GLY G 195 ? 2.548 3.163 2.285 -0.453 -0.016 0.926  194 GLY HHH CA  
9787  C C   . GLY G 195 ? 2.570 3.152 2.381 -0.507 -0.023 0.962  194 GLY HHH C   
9788  O O   . GLY G 195 ? 2.660 3.177 2.458 -0.524 -0.034 1.006  194 GLY HHH O   
9789  N N   . THR G 196 ? 2.499 3.122 2.383 -0.532 -0.019 0.944  195 THR HHH N   
9790  C CA  . THR G 196 ? 2.501 3.093 2.463 -0.585 -0.034 0.965  195 THR HHH CA  
9791  C C   . THR G 196 ? 2.436 3.022 2.447 -0.587 -0.059 0.905  195 THR HHH C   
9792  O O   . THR G 196 ? 2.444 2.943 2.459 -0.591 -0.098 0.881  195 THR HHH O   
9793  C CB  . THR G 196 ? 2.515 3.185 2.529 -0.623 0.004  1.024  195 THR HHH CB  
9794  O OG1 . THR G 196 ? 2.447 3.222 2.464 -0.599 0.037  1.003  195 THR HHH OG1 
9795  C CG2 . THR G 196 ? 2.613 3.272 2.587 -0.632 0.026  1.095  195 THR HHH CG2 
9796  N N   . GLN G 197 ? 2.390 3.063 2.432 -0.580 -0.036 0.882  196 GLN HHH N   
9797  C CA  . GLN G 197 ? 2.320 3.003 2.417 -0.586 -0.053 0.833  196 GLN HHH CA  
9798  C C   . GLN G 197 ? 2.282 2.875 2.354 -0.565 -0.094 0.782  196 GLN HHH C   
9799  O O   . GLN G 197 ? 2.256 2.839 2.268 -0.525 -0.094 0.752  196 GLN HHH O   
9800  C CB  . GLN G 197 ? 2.259 3.035 2.356 -0.557 -0.023 0.805  196 GLN HHH CB  
9801  C CG  . GLN G 197 ? 2.178 2.961 2.320 -0.555 -0.040 0.754  196 GLN HHH CG  
9802  C CD  . GLN G 197 ? 2.175 2.968 2.402 -0.601 -0.055 0.771  196 GLN HHH CD  
9803  O OE1 . GLN G 197 ? 2.216 3.043 2.483 -0.639 -0.041 0.824  196 GLN HHH OE1 
9804  N NE2 . GLN G 197 ? 2.111 2.876 2.366 -0.599 -0.083 0.725  196 GLN HHH NE2 
9805  N N   . THR G 198 ? 2.278 2.811 2.394 -0.593 -0.128 0.774  197 THR HHH N   
9806  C CA  . THR G 198 ? 2.256 2.709 2.357 -0.574 -0.167 0.725  197 THR HHH CA  
9807  C C   . THR G 198 ? 2.182 2.679 2.285 -0.543 -0.161 0.669  197 THR HHH C   
9808  O O   . THR G 198 ? 2.171 2.745 2.310 -0.551 -0.139 0.669  197 THR HHH O   
9809  C CB  . THR G 198 ? 2.290 2.677 2.440 -0.611 -0.203 0.728  197 THR HHH CB  
9810  O OG1 . THR G 198 ? 2.398 2.743 2.547 -0.643 -0.205 0.785  197 THR HHH OG1 
9811  C CG2 . THR G 198 ? 2.274 2.577 2.401 -0.586 -0.241 0.681  197 THR HHH CG2 
9812  N N   . TYR G 199 ? 2.153 2.604 2.218 -0.510 -0.180 0.626  198 TYR HHH N   
9813  C CA  . TYR G 199 ? 2.076 2.548 2.143 -0.484 -0.181 0.572  198 TYR HHH CA  
9814  C C   . TYR G 199 ? 2.071 2.466 2.136 -0.473 -0.218 0.538  198 TYR HHH C   
9815  O O   . TYR G 199 ? 2.098 2.458 2.119 -0.446 -0.227 0.522  198 TYR HHH O   
9816  C CB  . TYR G 199 ? 2.046 2.561 2.064 -0.450 -0.156 0.555  198 TYR HHH CB  
9817  C CG  . TYR G 199 ? 2.051 2.646 2.070 -0.454 -0.118 0.579  198 TYR HHH CG  
9818  C CD1 . TYR G 199 ? 2.009 2.663 2.062 -0.454 -0.101 0.566  198 TYR HHH CD1 
9819  C CD2 . TYR G 199 ? 2.101 2.715 2.083 -0.452 -0.100 0.617  198 TYR HHH CD2 
9820  C CE1 . TYR G 199 ? 2.023 2.755 2.076 -0.452 -0.065 0.589  198 TYR HHH CE1 
9821  C CE2 . TYR G 199 ? 2.119 2.809 2.097 -0.450 -0.064 0.641  198 TYR HHH CE2 
9822  C CZ  . TYR G 199 ? 2.081 2.832 2.095 -0.449 -0.045 0.626  198 TYR HHH CZ  
9823  O OH  . TYR G 199 ? 2.100 2.930 2.109 -0.442 -0.008 0.649  198 TYR HHH OH  
9824  N N   . ILE G 200 ? 2.056 2.428 2.164 -0.492 -0.238 0.529  199 ILE HHH N   
9825  C CA  . ILE G 200 ? 2.037 2.344 2.144 -0.477 -0.272 0.491  199 ILE HHH CA  
9826  C C   . ILE G 200 ? 1.951 2.300 2.067 -0.455 -0.261 0.449  199 ILE HHH C   
9827  O O   . ILE G 200 ? 1.908 2.326 2.050 -0.464 -0.238 0.454  199 ILE HHH O   
9828  C CB  . ILE G 200 ? 2.096 2.348 2.240 -0.510 -0.304 0.503  199 ILE HHH CB  
9829  C CG1 . ILE G 200 ? 2.170 2.354 2.294 -0.526 -0.319 0.542  199 ILE HHH CG1 
9830  C CG2 . ILE G 200 ? 2.092 2.295 2.238 -0.491 -0.334 0.458  199 ILE HHH CG2 
9831  C CD1 . ILE G 200 ? 2.231 2.358 2.393 -0.567 -0.349 0.561  199 ILE HHH CD1 
9832  N N   . CYS G 201 ? 1.939 2.251 2.031 -0.425 -0.275 0.411  200 CYS HHH N   
9833  C CA  . CYS G 201 ? 1.924 2.260 2.022 -0.403 -0.269 0.371  200 CYS HHH CA  
9834  C C   . CYS G 201 ? 1.953 2.230 2.060 -0.397 -0.302 0.347  200 CYS HHH C   
9835  O O   . CYS G 201 ? 1.968 2.182 2.052 -0.386 -0.325 0.345  200 CYS HHH O   
9836  C CB  . CYS G 201 ? 1.908 2.263 1.968 -0.373 -0.249 0.349  200 CYS HHH CB  
9837  S SG  . CYS G 201 ? 1.908 2.210 1.941 -0.338 -0.268 0.312  200 CYS HHH SG  
9838  N N   . ASN G 202 ? 1.966 2.265 2.104 -0.401 -0.306 0.330  201 ASN HHH N   
9839  C CA  . ASN G 202 ? 1.987 2.236 2.134 -0.394 -0.339 0.305  201 ASN HHH CA  
9840  C C   . ASN G 202 ? 1.918 2.176 2.043 -0.355 -0.330 0.267  201 ASN HHH C   
9841  O O   . ASN G 202 ? 1.858 2.173 1.992 -0.349 -0.306 0.259  201 ASN HHH O   
9842  C CB  . ASN G 202 ? 2.014 2.284 2.213 -0.428 -0.355 0.315  201 ASN HHH CB  
9843  C CG  . ASN G 202 ? 2.042 2.329 2.271 -0.471 -0.351 0.361  201 ASN HHH CG  
9844  O OD1 . ASN G 202 ? 2.000 2.352 2.236 -0.480 -0.318 0.384  201 ASN HHH OD1 
9845  N ND2 . ASN G 202 ? 2.105 2.332 2.350 -0.499 -0.385 0.374  201 ASN HHH ND2 
9846  N N   . VAL G 203 ? 1.909 2.111 2.003 -0.327 -0.347 0.244  202 VAL HHH N   
9847  C CA  . VAL G 203 ? 1.868 2.074 1.936 -0.288 -0.335 0.213  202 VAL HHH CA  
9848  C C   . VAL G 203 ? 1.901 2.060 1.962 -0.268 -0.364 0.187  202 VAL HHH C   
9849  O O   . VAL G 203 ? 1.947 2.045 1.994 -0.263 -0.392 0.186  202 VAL HHH O   
9850  C CB  . VAL G 203 ? 1.848 2.045 1.883 -0.268 -0.323 0.212  202 VAL HHH CB  
9851  C CG1 . VAL G 203 ? 1.809 2.017 1.825 -0.235 -0.306 0.184  202 VAL HHH CG1 
9852  C CG2 . VAL G 203 ? 1.833 2.070 1.869 -0.287 -0.300 0.236  202 VAL HHH CG2 
9853  N N   . ASN G 204 ? 1.886 2.068 1.950 -0.253 -0.357 0.166  203 ASN HHH N   
9854  C CA  . ASN G 204 ? 1.915 2.060 1.969 -0.230 -0.384 0.138  203 ASN HHH CA  
9855  C C   . ASN G 204 ? 1.898 2.047 1.918 -0.187 -0.364 0.116  203 ASN HHH C   
9856  O O   . ASN G 204 ? 1.870 2.065 1.890 -0.184 -0.331 0.117  203 ASN HHH O   
9857  C CB  . ASN G 204 ? 1.902 2.074 1.992 -0.249 -0.399 0.136  203 ASN HHH CB  
9858  C CG  . ASN G 204 ? 1.921 2.106 2.054 -0.297 -0.411 0.165  203 ASN HHH CG  
9859  O OD1 . ASN G 204 ? 1.949 2.091 2.078 -0.314 -0.425 0.182  203 ASN HHH OD1 
9860  N ND2 . ASN G 204 ? 1.917 2.162 2.092 -0.319 -0.405 0.174  203 ASN HHH ND2 
9861  N N   . HIS G 205 ? 1.923 2.022 1.912 -0.156 -0.382 0.097  204 HIS HHH N   
9862  C CA  . HIS G 205 ? 1.890 1.986 1.844 -0.112 -0.366 0.076  204 HIS HHH CA  
9863  C C   . HIS G 205 ? 1.930 1.989 1.867 -0.088 -0.397 0.051  204 HIS HHH C   
9864  O O   . HIS G 205 ? 1.984 1.986 1.906 -0.080 -0.431 0.044  204 HIS HHH O   
9865  C CB  . HIS G 205 ? 1.890 1.970 1.820 -0.091 -0.356 0.078  204 HIS HHH CB  
9866  C CG  . HIS G 205 ? 1.868 1.959 1.771 -0.053 -0.332 0.064  204 HIS HHH CG  
9867  N ND1 . HIS G 205 ? 1.900 1.964 1.774 -0.016 -0.338 0.054  204 HIS HHH ND1 
9868  C CD2 . HIS G 205 ? 1.829 1.956 1.729 -0.047 -0.300 0.061  204 HIS HHH CD2 
9869  C CE1 . HIS G 205 ? 1.890 1.978 1.748 0.009  -0.309 0.048  204 HIS HHH CE1 
9870  N NE2 . HIS G 205 ? 1.847 1.969 1.720 -0.010 -0.286 0.052  204 HIS HHH NE2 
9871  N N   . LYS G 206 ? 1.921 2.005 1.856 -0.074 -0.389 0.039  205 LYS HHH N   
9872  C CA  . LYS G 206 ? 1.972 2.028 1.893 -0.053 -0.422 0.015  205 LYS HHH CA  
9873  C C   . LYS G 206 ? 2.008 2.014 1.877 -0.005 -0.430 -0.005 205 LYS HHH C   
9874  O O   . LYS G 206 ? 2.068 2.019 1.920 0.005  -0.470 -0.019 205 LYS HHH O   
9875  C CB  . LYS G 206 ? 1.961 2.062 1.889 -0.046 -0.407 0.009  205 LYS HHH CB  
9876  C CG  . LYS G 206 ? 1.923 2.085 1.894 -0.082 -0.385 0.031  205 LYS HHH CG  
9877  C CD  . LYS G 206 ? 1.917 2.118 1.915 -0.088 -0.397 0.025  205 LYS HHH CD  
9878  C CE  . LYS G 206 ? 1.934 2.127 1.971 -0.122 -0.442 0.025  205 LYS HHH CE  
9879  N NZ  . LYS G 206 ? 1.914 2.163 1.989 -0.132 -0.453 0.023  205 LYS HHH NZ  
9880  N N   . PRO G 207 ? 1.984 2.006 1.825 0.027  -0.393 -0.004 206 PRO HHH N   
9881  C CA  . PRO G 207 ? 2.020 2.006 1.812 0.077  -0.396 -0.020 206 PRO HHH CA  
9882  C C   . PRO G 207 ? 2.060 1.992 1.837 0.086  -0.428 -0.025 206 PRO HHH C   
9883  O O   . PRO G 207 ? 2.116 2.003 1.851 0.126  -0.451 -0.047 206 PRO HHH O   
9884  C CB  . PRO G 207 ? 1.986 2.012 1.774 0.088  -0.346 -0.006 206 PRO HHH CB  
9885  C CG  . PRO G 207 ? 1.939 2.011 1.755 0.058  -0.321 0.006  206 PRO HHH CG  
9886  C CD  . PRO G 207 ? 1.930 2.005 1.786 0.014  -0.347 0.013  206 PRO HHH CD  
9887  N N   . SER G 208 ? 2.040 1.974 1.845 0.052  -0.428 -0.006 207 SER HHH N   
9888  C CA  . SER G 208 ? 2.079 1.958 1.868 0.060  -0.455 -0.006 207 SER HHH CA  
9889  C C   . SER G 208 ? 2.097 1.932 1.907 0.022  -0.498 -0.004 207 SER HHH C   
9890  O O   . SER G 208 ? 2.125 1.908 1.924 0.022  -0.521 0.000  207 SER HHH O   
9891  C CB  . SER G 208 ? 2.052 1.962 1.852 0.054  -0.427 0.016  207 SER HHH CB  
9892  O OG  . SER G 208 ? 2.004 1.949 1.847 0.003  -0.416 0.039  207 SER HHH OG  
9893  N N   . ASN G 209 ? 2.070 1.925 1.911 -0.009 -0.508 -0.005 208 ASN HHH N   
9894  C CA  . ASN G 209 ? 2.116 1.939 1.987 -0.053 -0.548 -0.002 208 ASN HHH CA  
9895  C C   . ASN G 209 ? 2.151 1.947 2.035 -0.082 -0.553 0.024  208 ASN HHH C   
9896  O O   . ASN G 209 ? 2.242 1.962 2.110 -0.084 -0.594 0.018  208 ASN HHH O   
9897  C CB  . ASN G 209 ? 2.188 1.943 2.028 -0.030 -0.598 -0.034 208 ASN HHH CB  
9898  C CG  . ASN G 209 ? 2.197 1.954 2.077 -0.072 -0.633 -0.038 208 ASN HHH CG  
9899  O OD1 . ASN G 209 ? 2.250 1.941 2.113 -0.069 -0.682 -0.061 208 ASN HHH OD1 
9900  N ND2 . ASN G 209 ? 2.121 1.954 2.054 -0.110 -0.610 -0.019 208 ASN HHH ND2 
9901  N N   . THR G 210 ? 2.104 1.955 2.010 -0.100 -0.515 0.051  209 THR HHH N   
9902  C CA  . THR G 210 ? 2.118 1.957 2.037 -0.129 -0.513 0.080  209 THR HHH CA  
9903  C C   . THR G 210 ? 2.068 1.974 2.034 -0.176 -0.487 0.108  209 THR HHH C   
9904  O O   . THR G 210 ? 1.984 1.955 1.956 -0.170 -0.449 0.111  209 THR HHH O   
9905  C CB  . THR G 210 ? 2.100 1.940 1.990 -0.095 -0.493 0.084  209 THR HHH CB  
9906  O OG1 . THR G 210 ? 2.020 1.920 1.906 -0.072 -0.456 0.076  209 THR HHH OG1 
9907  C CG2 . THR G 210 ? 2.178 1.939 2.022 -0.054 -0.524 0.067  209 THR HHH CG2 
9908  N N   . LYS G 211 ? 2.125 2.014 2.121 -0.220 -0.508 0.129  210 LYS HHH N   
9909  C CA  . LYS G 211 ? 2.109 2.053 2.145 -0.265 -0.485 0.164  210 LYS HHH CA  
9910  C C   . LYS G 211 ? 2.119 2.043 2.135 -0.264 -0.476 0.187  210 LYS HHH C   
9911  O O   . LYS G 211 ? 2.160 2.020 2.139 -0.234 -0.495 0.176  210 LYS HHH O   
9912  C CB  . LYS G 211 ? 2.161 2.098 2.240 -0.312 -0.511 0.177  210 LYS HHH CB  
9913  C CG  . LYS G 211 ? 2.142 2.133 2.263 -0.359 -0.489 0.217  210 LYS HHH CG  
9914  C CD  . LYS G 211 ? 2.144 2.175 2.321 -0.401 -0.500 0.227  210 LYS HHH CD  
9915  C CE  . LYS G 211 ? 2.228 2.189 2.420 -0.426 -0.551 0.221  210 LYS HHH CE  
9916  N NZ  . LYS G 211 ? 2.298 2.217 2.504 -0.468 -0.562 0.259  210 LYS HHH NZ  
9917  N N   . VAL G 212 ? 2.093 2.071 2.128 -0.288 -0.447 0.215  211 VAL HHH N   
9918  C CA  . VAL G 212 ? 2.129 2.092 2.148 -0.294 -0.441 0.243  211 VAL HHH CA  
9919  C C   . VAL G 212 ? 2.141 2.152 2.193 -0.338 -0.423 0.279  211 VAL HHH C   
9920  O O   . VAL G 212 ? 2.082 2.167 2.150 -0.343 -0.392 0.280  211 VAL HHH O   
9921  C CB  . VAL G 212 ? 2.083 2.076 2.074 -0.259 -0.416 0.234  211 VAL HHH CB  
9922  C CG1 . VAL G 212 ? 2.117 2.091 2.089 -0.259 -0.418 0.260  211 VAL HHH CG1 
9923  C CG2 . VAL G 212 ? 2.082 2.049 2.046 -0.213 -0.425 0.200  211 VAL HHH CG2 
9924  N N   . ASP G 213 ? 2.234 2.200 2.292 -0.367 -0.441 0.309  212 ASP HHH N   
9925  C CA  . ASP G 213 ? 2.258 2.263 2.341 -0.408 -0.423 0.352  212 ASP HHH CA  
9926  C C   . ASP G 213 ? 2.276 2.275 2.323 -0.394 -0.409 0.373  212 ASP HHH C   
9927  O O   . ASP G 213 ? 2.391 2.323 2.420 -0.400 -0.430 0.395  212 ASP HHH O   
9928  C CB  . ASP G 213 ? 2.341 2.300 2.456 -0.452 -0.451 0.374  212 ASP HHH CB  
9929  C CG  . ASP G 213 ? 2.336 2.316 2.494 -0.471 -0.466 0.355  212 ASP HHH CG  
9930  O OD1 . ASP G 213 ? 2.270 2.303 2.432 -0.447 -0.451 0.326  212 ASP HHH OD1 
9931  O OD2 . ASP G 213 ? 2.400 2.343 2.588 -0.509 -0.494 0.370  212 ASP HHH OD2 
9932  N N   . LYS G 214 ? 2.198 2.263 2.233 -0.376 -0.378 0.368  213 LYS HHH N   
9933  C CA  . LYS G 214 ? 2.190 2.260 2.189 -0.357 -0.366 0.381  213 LYS HHH CA  
9934  C C   . LYS G 214 ? 2.152 2.273 2.156 -0.383 -0.341 0.418  213 LYS HHH C   
9935  O O   . LYS G 214 ? 2.068 2.260 2.083 -0.386 -0.312 0.413  213 LYS HHH O   
9936  C CB  . LYS G 214 ? 2.152 2.259 2.132 -0.321 -0.352 0.348  213 LYS HHH CB  
9937  C CG  . LYS G 214 ? 2.186 2.299 2.132 -0.299 -0.347 0.355  213 LYS HHH CG  
9938  C CD  . LYS G 214 ? 2.289 2.330 2.211 -0.287 -0.376 0.371  213 LYS HHH CD  
9939  C CE  . LYS G 214 ? 2.339 2.395 2.229 -0.262 -0.373 0.379  213 LYS HHH CE  
9940  N NZ  . LYS G 214 ? 2.444 2.426 2.306 -0.250 -0.399 0.400  213 LYS HHH NZ  
9941  N N   . LYS G 215 ? 2.174 2.254 2.164 -0.397 -0.350 0.456  214 LYS HHH N   
9942  C CA  . LYS G 215 ? 2.160 2.280 2.145 -0.418 -0.326 0.498  214 LYS HHH CA  
9943  C C   . LYS G 215 ? 2.103 2.270 2.051 -0.387 -0.307 0.489  214 LYS HHH C   
9944  O O   . LYS G 215 ? 2.086 2.224 2.005 -0.356 -0.322 0.470  214 LYS HHH O   
9945  C CB  . LYS G 215 ? 2.245 2.294 2.218 -0.437 -0.345 0.540  214 LYS HHH CB  
9946  C CG  . LYS G 215 ? 2.282 2.359 2.234 -0.448 -0.322 0.587  214 LYS HHH CG  
9947  C CD  . LYS G 215 ? 2.302 2.407 2.292 -0.495 -0.306 0.629  214 LYS HHH CD  
9948  C CE  . LYS G 215 ? 2.359 2.464 2.318 -0.504 -0.289 0.683  214 LYS HHH CE  
9949  N NZ  . LYS G 215 ? 2.396 2.524 2.397 -0.553 -0.274 0.731  214 LYS HHH NZ  
9950  N N   . VAL G 216 ? 2.067 2.305 2.015 -0.396 -0.276 0.500  215 VAL HHH N   
9951  C CA  . VAL G 216 ? 2.045 2.329 1.955 -0.373 -0.258 0.494  215 VAL HHH CA  
9952  C C   . VAL G 216 ? 2.104 2.401 1.992 -0.385 -0.244 0.542  215 VAL HHH C   
9953  O O   . VAL G 216 ? 2.135 2.441 2.050 -0.416 -0.233 0.574  215 VAL HHH O   
9954  C CB  . VAL G 216 ? 1.977 2.326 1.896 -0.367 -0.233 0.464  215 VAL HHH CB  
9955  C CG1 . VAL G 216 ? 1.971 2.355 1.849 -0.343 -0.222 0.450  215 VAL HHH CG1 
9956  C CG2 . VAL G 216 ? 1.936 2.271 1.881 -0.359 -0.243 0.424  215 VAL HHH CG2 
9957  N N   . GLU G 217 ? 2.138 2.440 1.978 -0.362 -0.244 0.548  216 GLU HHH N   
9958  C CA  . GLU G 217 ? 2.224 2.545 2.031 -0.366 -0.228 0.593  216 GLU HHH CA  
9959  C C   . GLU G 217 ? 2.235 2.579 1.990 -0.332 -0.230 0.579  216 GLU HHH C   
9960  O O   . GLU G 217 ? 2.231 2.567 1.982 -0.310 -0.248 0.543  216 GLU HHH O   
9961  C CB  . GLU G 217 ? 2.331 2.585 2.138 -0.384 -0.243 0.638  216 GLU HHH CB  
9962  C CG  . GLU G 217 ? 2.389 2.564 2.183 -0.365 -0.279 0.626  216 GLU HHH CG  
9963  C CD  . GLU G 217 ? 2.522 2.620 2.307 -0.382 -0.294 0.673  216 GLU HHH CD  
9964  O OE1 . GLU G 217 ? 2.553 2.624 2.379 -0.419 -0.297 0.688  216 GLU HHH OE1 
9965  O OE2 . GLU G 217 ? 2.618 2.684 2.355 -0.361 -0.303 0.697  216 GLU HHH OE2 
9966  N N   . PRO G 218 ? 2.273 2.652 1.987 -0.327 -0.212 0.608  217 PRO HHH N   
9967  C CA  . PRO G 218 ? 2.296 2.697 1.958 -0.295 -0.218 0.594  217 PRO HHH CA  
9968  C C   . PRO G 218 ? 2.351 2.700 1.988 -0.273 -0.249 0.603  217 PRO HHH C   
9969  O O   . PRO G 218 ? 2.388 2.678 2.034 -0.283 -0.260 0.633  217 PRO HHH O   
9970  C CB  . PRO G 218 ? 2.334 2.776 1.956 -0.295 -0.191 0.631  217 PRO HHH CB  
9971  C CG  . PRO G 218 ? 2.362 2.781 2.013 -0.328 -0.178 0.681  217 PRO HHH CG  
9972  C CD  . PRO G 218 ? 2.305 2.706 2.020 -0.350 -0.185 0.655  217 PRO HHH CD  
9973  N N   . LYS G 219 ? 2.355 2.729 1.963 -0.243 -0.263 0.575  218 LYS HHH N   
9974  C CA  . LYS G 219 ? 2.394 2.736 1.987 -0.215 -0.295 0.568  218 LYS HHH CA  
9975  C C   . LYS G 219 ? 2.457 2.789 1.992 -0.194 -0.302 0.608  218 LYS HHH C   
9976  O O   . LYS G 219 ? 2.500 2.849 2.007 -0.203 -0.280 0.641  218 LYS HHH O   
9977  C CB  . LYS G 219 ? 2.367 2.756 1.971 -0.198 -0.305 0.515  218 LYS HHH CB  
9978  C CG  . LYS G 219 ? 2.386 2.755 2.003 -0.173 -0.334 0.495  218 LYS HHH CG  
9979  C CD  . LYS G 219 ? 2.355 2.784 1.973 -0.155 -0.344 0.454  218 LYS HHH CD  
9980  C CE  . LYS G 219 ? 2.275 2.743 1.924 -0.175 -0.327 0.415  218 LYS HHH CE  
9981  N NZ  . LYS G 219 ? 2.221 2.659 1.917 -0.187 -0.323 0.400  218 LYS HHH NZ  
9982  N N   . SER G 220 ? 2.457 2.762 1.972 -0.163 -0.331 0.607  219 SER HHH N   
9983  C CA  . SER G 220 ? 2.514 2.826 1.968 -0.130 -0.344 0.630  219 SER HHH CA  
9984  C C   . SER G 220 ? 2.489 2.834 1.944 -0.096 -0.372 0.592  219 SER HHH C   
9985  O O   . SER G 220 ? 2.483 2.889 1.912 -0.079 -0.378 0.573  219 SER HHH O   
9986  C CB  . SER G 220 ? 2.593 2.827 2.019 -0.127 -0.350 0.684  219 SER HHH CB  
9987  O OG  . SER G 220 ? 2.648 2.891 2.008 -0.098 -0.355 0.715  219 SER HHH OG  
9988  N N   . ASP H 1   ? 1.873 2.125 1.890 -0.109 0.328  0.271  1   ASP LLL N   
9989  C CA  . ASP H 1   ? 1.825 2.134 1.894 -0.120 0.326  0.258  1   ASP LLL CA  
9990  C C   . ASP H 1   ? 1.796 2.061 1.895 -0.151 0.292  0.229  1   ASP LLL C   
9991  O O   . ASP H 1   ? 1.789 2.083 1.949 -0.186 0.286  0.241  1   ASP LLL O   
9992  C CB  . ASP H 1   ? 1.859 2.241 1.981 -0.140 0.354  0.305  1   ASP LLL CB  
9993  C CG  . ASP H 1   ? 1.823 2.286 1.994 -0.137 0.359  0.299  1   ASP LLL CG  
9994  O OD1 . ASP H 1   ? 1.748 2.203 1.908 -0.119 0.340  0.256  1   ASP LLL OD1 
9995  O OD2 . ASP H 1   ? 1.829 2.367 2.053 -0.152 0.383  0.339  1   ASP LLL OD2 
9996  N N   . ILE H 2   ? 1.781 1.989 1.839 -0.136 0.270  0.193  2   ILE LLL N   
9997  C CA  . ILE H 2   ? 1.760 1.913 1.828 -0.158 0.239  0.164  2   ILE LLL CA  
9998  C C   . ILE H 2   ? 1.729 1.920 1.827 -0.163 0.224  0.138  2   ILE LLL C   
9999  O O   . ILE H 2   ? 1.736 1.979 1.831 -0.138 0.234  0.132  2   ILE LLL O   
10000 C CB  . ILE H 2   ? 1.731 1.823 1.746 -0.134 0.225  0.139  2   ILE LLL CB  
10001 C CG1 . ILE H 2   ? 1.791 1.845 1.774 -0.124 0.237  0.166  2   ILE LLL CG1 
10002 C CG2 . ILE H 2   ? 1.709 1.752 1.729 -0.150 0.198  0.109  2   ILE LLL CG2 
10003 C CD1 . ILE H 2   ? 1.799 1.811 1.735 -0.096 0.226  0.146  2   ILE LLL CD1 
10004 N N   . GLN H 3   ? 1.735 1.897 1.856 -0.192 0.199  0.121  3   GLN LLL N   
10005 C CA  . GLN H 3   ? 1.714 1.913 1.865 -0.201 0.181  0.100  3   GLN LLL CA  
10006 C C   . GLN H 3   ? 1.706 1.846 1.845 -0.218 0.151  0.069  3   GLN LLL C   
10007 O O   . GLN H 3   ? 1.751 1.833 1.888 -0.241 0.143  0.074  3   GLN LLL O   
10008 C CB  . GLN H 3   ? 1.778 2.042 1.994 -0.230 0.188  0.129  3   GLN LLL CB  
10009 C CG  . GLN H 3   ? 1.798 2.121 2.048 -0.229 0.174  0.114  3   GLN LLL CG  
10010 C CD  . GLN H 3   ? 1.861 2.277 2.174 -0.238 0.192  0.148  3   GLN LLL CD  
10011 O OE1 . GLN H 3   ? 1.947 2.387 2.278 -0.246 0.216  0.184  3   GLN LLL OE1 
10012 N NE2 . GLN H 3   ? 1.868 2.342 2.215 -0.235 0.180  0.140  3   GLN LLL NE2 
10013 N N   . LEU H 4   ? 1.651 1.802 1.779 -0.204 0.136  0.040  4   LEU LLL N   
10014 C CA  . LEU H 4   ? 1.627 1.727 1.728 -0.209 0.110  0.008  4   LEU LLL CA  
10015 C C   . LEU H 4   ? 1.622 1.755 1.753 -0.230 0.087  -0.005 4   LEU LLL C   
10016 O O   . LEU H 4   ? 1.568 1.767 1.727 -0.221 0.092  0.004  4   LEU LLL O   
10017 C CB  . LEU H 4   ? 1.573 1.661 1.628 -0.173 0.113  -0.012 4   LEU LLL CB  
10018 C CG  . LEU H 4   ? 1.585 1.639 1.605 -0.152 0.128  -0.005 4   LEU LLL CG  
10019 C CD1 . LEU H 4   ? 1.555 1.606 1.538 -0.123 0.126  -0.024 4   LEU LLL CD1 
10020 C CD2 . LEU H 4   ? 1.637 1.626 1.646 -0.164 0.123  -0.004 4   LEU LLL CD2 
10021 N N   . THR H 5   ? 1.672 1.758 1.793 -0.252 0.063  -0.025 5   THR LLL N   
10022 C CA  . THR H 5   ? 1.682 1.788 1.817 -0.271 0.034  -0.043 5   THR LLL CA  
10023 C C   . THR H 5   ? 1.679 1.724 1.758 -0.260 0.017  -0.079 5   THR LLL C   
10024 O O   . THR H 5   ? 1.713 1.688 1.767 -0.268 0.012  -0.089 5   THR LLL O   
10025 C CB  . THR H 5   ? 1.749 1.870 1.936 -0.318 0.018  -0.030 5   THR LLL CB  
10026 O OG1 . THR H 5   ? 1.821 1.906 2.019 -0.334 0.032  -0.007 5   THR LLL OG1 
10027 C CG2 . THR H 5   ? 1.711 1.929 1.958 -0.325 0.020  -0.007 5   THR LLL CG2 
10028 N N   . GLN H 6   ? 1.642 1.714 1.701 -0.238 0.012  -0.094 6   GLN LLL N   
10029 C CA  . GLN H 6   ? 1.685 1.719 1.692 -0.225 -0.002 -0.124 6   GLN LLL CA  
10030 C C   . GLN H 6   ? 1.753 1.786 1.763 -0.253 -0.035 -0.143 6   GLN LLL C   
10031 O O   . GLN H 6   ? 1.794 1.873 1.853 -0.279 -0.046 -0.128 6   GLN LLL O   
10032 C CB  . GLN H 6   ? 1.647 1.715 1.634 -0.195 0.006  -0.126 6   GLN LLL CB  
10033 C CG  . GLN H 6   ? 1.635 1.698 1.610 -0.169 0.032  -0.114 6   GLN LLL CG  
10034 C CD  . GLN H 6   ? 1.592 1.686 1.554 -0.146 0.037  -0.113 6   GLN LLL CD  
10035 O OE1 . GLN H 6   ? 1.565 1.689 1.545 -0.137 0.048  -0.098 6   GLN LLL OE1 
10036 N NE2 . GLN H 6   ? 1.571 1.654 1.499 -0.136 0.030  -0.129 6   GLN LLL NE2 
10037 N N   . SER H 7   ? 1.807 1.794 1.764 -0.245 -0.050 -0.173 7   SER LLL N   
10038 C CA  . SER H 7   ? 1.845 1.830 1.786 -0.265 -0.084 -0.197 7   SER LLL CA  
10039 C C   . SER H 7   ? 1.881 1.824 1.750 -0.239 -0.087 -0.228 7   SER LLL C   
10040 O O   . SER H 7   ? 1.897 1.788 1.732 -0.218 -0.070 -0.237 7   SER LLL O   
10041 C CB  . SER H 7   ? 1.900 1.849 1.864 -0.308 -0.107 -0.202 7   SER LLL CB  
10042 O OG  . SER H 7   ? 1.950 1.816 1.888 -0.306 -0.097 -0.209 7   SER LLL OG  
10043 N N   . PRO H 8   ? 1.896 1.866 1.738 -0.235 -0.107 -0.243 8   PRO LLL N   
10044 C CA  . PRO H 8   ? 1.869 1.904 1.748 -0.256 -0.130 -0.232 8   PRO LLL CA  
10045 C C   . PRO H 8   ? 1.776 1.877 1.685 -0.234 -0.109 -0.202 8   PRO LLL C   
10046 O O   . PRO H 8   ? 1.727 1.817 1.623 -0.208 -0.081 -0.194 8   PRO LLL O   
10047 C CB  . PRO H 8   ? 1.947 1.970 1.768 -0.253 -0.158 -0.263 8   PRO LLL CB  
10048 C CG  . PRO H 8   ? 1.961 1.952 1.720 -0.214 -0.134 -0.275 8   PRO LLL CG  
10049 C CD  . PRO H 8   ? 1.947 1.892 1.717 -0.206 -0.107 -0.269 8   PRO LLL CD  
10050 N N   . ASP H 9   ? 1.767 1.932 1.714 -0.244 -0.125 -0.187 9   ASP LLL N   
10051 C CA  . ASP H 9   ? 1.718 1.940 1.693 -0.222 -0.109 -0.159 9   ASP LLL CA  
10052 C C   . ASP H 9   ? 1.713 1.939 1.638 -0.196 -0.110 -0.164 9   ASP LLL C   
10053 O O   . ASP H 9   ? 1.649 1.883 1.571 -0.172 -0.088 -0.148 9   ASP LLL O   
10054 C CB  . ASP H 9   ? 1.730 2.021 1.768 -0.238 -0.125 -0.140 9   ASP LLL CB  
10055 C CG  . ASP H 9   ? 1.754 2.058 1.852 -0.262 -0.117 -0.124 9   ASP LLL CG  
10056 O OD1 . ASP H 9   ? 1.733 2.042 1.851 -0.245 -0.086 -0.106 9   ASP LLL OD1 
10057 O OD2 . ASP H 9   ? 1.818 2.127 1.942 -0.298 -0.142 -0.130 9   ASP LLL OD2 
10058 N N   . SER H 10  ? 1.793 2.012 1.676 -0.202 -0.136 -0.185 10  SER LLL N   
10059 C CA  . SER H 10  ? 1.812 2.034 1.637 -0.179 -0.137 -0.190 10  SER LLL CA  
10060 C C   . SER H 10  ? 1.850 2.017 1.609 -0.174 -0.138 -0.222 10  SER LLL C   
10061 O O   . SER H 10  ? 1.914 2.042 1.669 -0.194 -0.153 -0.246 10  SER LLL O   
10062 C CB  . SER H 10  ? 1.862 2.134 1.688 -0.183 -0.167 -0.183 10  SER LLL CB  
10063 O OG  . SER H 10  ? 1.928 2.197 1.689 -0.164 -0.170 -0.189 10  SER LLL OG  
10064 N N   . LEU H 11  ? 1.820 1.986 1.530 -0.148 -0.122 -0.222 11  LEU LLL N   
10065 C CA  . LEU H 11  ? 1.868 1.992 1.510 -0.134 -0.119 -0.252 11  LEU LLL CA  
10066 C C   . LEU H 11  ? 1.842 1.995 1.432 -0.109 -0.112 -0.244 11  LEU LLL C   
10067 O O   . LEU H 11  ? 1.777 1.953 1.379 -0.095 -0.087 -0.217 11  LEU LLL O   
10068 C CB  . LEU H 11  ? 1.878 1.960 1.525 -0.122 -0.090 -0.255 11  LEU LLL CB  
10069 C CG  . LEU H 11  ? 1.977 2.006 1.561 -0.105 -0.086 -0.289 11  LEU LLL CG  
10070 C CD1 . LEU H 11  ? 2.065 2.047 1.627 -0.127 -0.120 -0.324 11  LEU LLL CD1 
10071 C CD2 . LEU H 11  ? 1.950 1.947 1.547 -0.090 -0.057 -0.286 11  LEU LLL CD2 
10072 N N   . ALA H 12  ? 1.902 2.056 1.437 -0.108 -0.136 -0.265 12  ALA LLL N   
10073 C CA  . ALA H 12  ? 1.941 2.123 1.415 -0.084 -0.131 -0.260 12  ALA LLL CA  
10074 C C   . ALA H 12  ? 2.000 2.143 1.401 -0.061 -0.119 -0.294 12  ALA LLL C   
10075 O O   . ALA H 12  ? 2.078 2.174 1.446 -0.069 -0.142 -0.333 12  ALA LLL O   
10076 C CB  . ALA H 12  ? 1.993 2.209 1.450 -0.094 -0.167 -0.259 12  ALA LLL CB  
10077 N N   . VAL H 13  ? 1.971 2.134 1.349 -0.033 -0.085 -0.278 13  VAL LLL N   
10078 C CA  . VAL H 13  ? 2.029 2.164 1.344 -0.001 -0.064 -0.305 13  VAL LLL CA  
10079 C C   . VAL H 13  ? 2.049 2.239 1.316 0.026  -0.043 -0.284 13  VAL LLL C   
10080 O O   . VAL H 13  ? 2.003 2.241 1.308 0.021  -0.028 -0.240 13  VAL LLL O   
10081 C CB  . VAL H 13  ? 1.987 2.096 1.343 0.005  -0.036 -0.302 13  VAL LLL CB  
10082 C CG1 . VAL H 13  ? 2.038 2.141 1.343 0.046  -0.006 -0.316 13  VAL LLL CG1 
10083 C CG2 . VAL H 13  ? 1.997 2.046 1.385 -0.018 -0.057 -0.325 13  VAL LLL CG2 
10084 N N   . SER H 14  ? 2.114 2.292 1.296 0.054  -0.041 -0.315 14  SER LLL N   
10085 C CA  . SER H 14  ? 2.118 2.350 1.244 0.087  -0.014 -0.297 14  SER LLL CA  
10086 C C   . SER H 14  ? 2.043 2.304 1.205 0.105  0.031  -0.271 14  SER LLL C   
10087 O O   . SER H 14  ? 2.035 2.255 1.208 0.117  0.043  -0.293 14  SER LLL O   
10088 C CB  . SER H 14  ? 2.242 2.447 1.263 0.117  -0.022 -0.343 14  SER LLL CB  
10089 O OG  . SER H 14  ? 2.295 2.502 1.275 0.101  -0.061 -0.354 14  SER LLL OG  
10090 N N   . LEU H 15  ? 1.988 2.317 1.169 0.105  0.053  -0.221 15  LEU LLL N   
10091 C CA  . LEU H 15  ? 1.949 2.324 1.169 0.118  0.094  -0.189 15  LEU LLL CA  
10092 C C   . LEU H 15  ? 1.992 2.355 1.171 0.159  0.118  -0.221 15  LEU LLL C   
10093 O O   . LEU H 15  ? 2.078 2.455 1.177 0.192  0.127  -0.238 15  LEU LLL O   
10094 C CB  . LEU H 15  ? 1.977 2.426 1.186 0.119  0.112  -0.140 15  LEU LLL CB  
10095 C CG  . LEU H 15  ? 1.939 2.405 1.212 0.082  0.102  -0.093 15  LEU LLL CG  
10096 C CD1 . LEU H 15  ? 1.990 2.497 1.222 0.080  0.097  -0.059 15  LEU LLL CD1 
10097 C CD2 . LEU H 15  ? 1.877 2.374 1.219 0.071  0.128  -0.057 15  LEU LLL CD2 
10098 N N   . GLY H 16  ? 1.957 2.295 1.183 0.162  0.129  -0.228 16  GLY LLL N   
10099 C CA  . GLY H 16  ? 2.020 2.355 1.220 0.207  0.157  -0.248 16  GLY LLL CA  
10100 C C   . GLY H 16  ? 2.105 2.345 1.262 0.222  0.138  -0.306 16  GLY LLL C   
10101 O O   . GLY H 16  ? 2.149 2.375 1.273 0.266  0.160  -0.329 16  GLY LLL O   
10102 N N   . GLU H 17  ? 2.137 2.316 1.296 0.187  0.099  -0.327 17  GLU LLL N   
10103 C CA  . GLU H 17  ? 2.216 2.297 1.357 0.186  0.075  -0.375 17  GLU LLL CA  
10104 C C   . GLU H 17  ? 2.133 2.193 1.359 0.159  0.075  -0.357 17  GLU LLL C   
10105 O O   . GLU H 17  ? 2.020 2.136 1.311 0.137  0.083  -0.314 17  GLU LLL O   
10106 C CB  . GLU H 17  ? 2.290 2.326 1.392 0.158  0.031  -0.405 17  GLU LLL CB  
10107 C CG  . GLU H 17  ? 2.412 2.478 1.429 0.178  0.027  -0.417 17  GLU LLL CG  
10108 C CD  . GLU H 17  ? 2.581 2.607 1.498 0.229  0.038  -0.464 17  GLU LLL CD  
10109 O OE1 . GLU H 17  ? 2.619 2.636 1.536 0.266  0.070  -0.469 17  GLU LLL OE1 
10110 O OE2 . GLU H 17  ? 2.695 2.702 1.530 0.235  0.013  -0.497 17  GLU LLL OE2 
10111 N N   . ARG H 18  ? 2.171 2.149 1.393 0.163  0.065  -0.389 18  ARG LLL N   
10112 C CA  . ARG H 18  ? 2.101 2.046 1.394 0.139  0.061  -0.375 18  ARG LLL CA  
10113 C C   . ARG H 18  ? 2.047 1.995 1.387 0.086  0.031  -0.362 18  ARG LLL C   
10114 O O   . ARG H 18  ? 2.074 2.028 1.384 0.071  0.008  -0.373 18  ARG LLL O   
10115 C CB  . ARG H 18  ? 2.191 2.038 1.453 0.157  0.055  -0.414 18  ARG LLL CB  
10116 C CG  . ARG H 18  ? 2.147 1.960 1.471 0.142  0.057  -0.397 18  ARG LLL CG  
10117 C CD  . ARG H 18  ? 2.243 1.953 1.531 0.164  0.053  -0.431 18  ARG LLL CD  
10118 N NE  . ARG H 18  ? 2.338 2.042 1.562 0.225  0.077  -0.453 18  ARG LLL NE  
10119 C CZ  . ARG H 18  ? 2.328 2.070 1.566 0.269  0.110  -0.435 18  ARG LLL CZ  
10120 N NH1 . ARG H 18  ? 2.227 2.011 1.538 0.257  0.123  -0.395 18  ARG LLL NH1 
10121 N NH2 . ARG H 18  ? 2.420 2.163 1.596 0.327  0.132  -0.456 18  ARG LLL NH2 
10122 N N   . ALA H 19  ? 1.992 1.940 1.403 0.063  0.033  -0.338 19  ALA LLL N   
10123 C CA  . ALA H 19  ? 1.959 1.909 1.421 0.017  0.009  -0.324 19  ALA LLL CA  
10124 C C   . ALA H 19  ? 1.962 1.877 1.475 0.005  0.014  -0.314 19  ALA LLL C   
10125 O O   . ALA H 19  ? 1.921 1.866 1.466 0.018  0.038  -0.289 19  ALA LLL O   
10126 C CB  . ALA H 19  ? 1.881 1.906 1.377 0.006  0.014  -0.288 19  ALA LLL CB  
10127 N N   . THR H 20  ? 2.042 1.897 1.562 -0.019 -0.009 -0.332 20  THR LLL N   
10128 C CA  . THR H 20  ? 2.026 1.841 1.589 -0.033 -0.006 -0.322 20  THR LLL CA  
10129 C C   . THR H 20  ? 1.945 1.792 1.570 -0.074 -0.019 -0.298 20  THR LLL C   
10130 O O   . THR H 20  ? 1.972 1.841 1.597 -0.096 -0.042 -0.302 20  THR LLL O   
10131 C CB  . THR H 20  ? 2.142 1.861 1.666 -0.030 -0.019 -0.355 20  THR LLL CB  
10132 O OG1 . THR H 20  ? 2.243 1.935 1.721 -0.043 -0.048 -0.388 20  THR LLL OG1 
10133 C CG2 . THR H 20  ? 2.190 1.874 1.671 0.018  0.004  -0.368 20  THR LLL CG2 
10134 N N   . ILE H 21  ? 1.872 1.728 1.545 -0.080 -0.004 -0.271 21  ILE LLL N   
10135 C CA  . ILE H 21  ? 1.832 1.716 1.564 -0.112 -0.011 -0.248 21  ILE LLL CA  
10136 C C   . ILE H 21  ? 1.871 1.710 1.627 -0.122 -0.004 -0.238 21  ILE LLL C   
10137 O O   . ILE H 21  ? 1.875 1.707 1.630 -0.098 0.018  -0.227 21  ILE LLL O   
10138 C CB  . ILE H 21  ? 1.738 1.691 1.499 -0.106 0.003  -0.220 21  ILE LLL CB  
10139 C CG1 . ILE H 21  ? 1.736 1.727 1.468 -0.093 0.000  -0.224 21  ILE LLL CG1 
10140 C CG2 . ILE H 21  ? 1.698 1.681 1.512 -0.132 -0.004 -0.200 21  ILE LLL CG2 
10141 C CD1 . ILE H 21  ? 1.686 1.729 1.441 -0.086 0.015  -0.196 21  ILE LLL CD1 
10142 N N   . ASN H 22  ? 1.879 1.696 1.662 -0.157 -0.023 -0.238 22  ASN LLL N   
10143 C CA  . ASN H 22  ? 1.864 1.640 1.675 -0.174 -0.018 -0.223 22  ASN LLL CA  
10144 C C   . ASN H 22  ? 1.788 1.625 1.655 -0.185 -0.004 -0.187 22  ASN LLL C   
10145 O O   . ASN H 22  ? 1.760 1.658 1.653 -0.195 -0.010 -0.179 22  ASN LLL O   
10146 C CB  . ASN H 22  ? 1.926 1.648 1.738 -0.211 -0.046 -0.239 22  ASN LLL CB  
10147 C CG  . ASN H 22  ? 2.025 1.659 1.773 -0.196 -0.058 -0.276 22  ASN LLL CG  
10148 O OD1 . ASN H 22  ? 2.029 1.643 1.739 -0.154 -0.039 -0.284 22  ASN LLL OD1 
10149 N ND2 . ASN H 22  ? 2.122 1.704 1.857 -0.228 -0.090 -0.299 22  ASN LLL ND2 
10150 N N   . CYS H 23  ? 1.768 1.587 1.648 -0.179 0.015  -0.166 23  CYS LLL N   
10151 C CA  . CYS H 23  ? 1.708 1.575 1.631 -0.184 0.033  -0.132 23  CYS LLL CA  
10152 C C   . CYS H 23  ? 1.744 1.564 1.681 -0.198 0.040  -0.113 23  CYS LLL C   
10153 O O   . CYS H 23  ? 1.766 1.539 1.673 -0.175 0.050  -0.114 23  CYS LLL O   
10154 C CB  . CYS H 23  ? 1.660 1.562 1.571 -0.150 0.052  -0.124 23  CYS LLL CB  
10155 S SG  . CYS H 23  ? 1.636 1.577 1.578 -0.146 0.075  -0.090 23  CYS LLL SG  
10156 N N   . LYS H 24  ? 1.754 1.589 1.735 -0.234 0.034  -0.095 24  LYS LLL N   
10157 C CA  . LYS H 24  ? 1.807 1.598 1.804 -0.255 0.040  -0.070 24  LYS LLL CA  
10158 C C   . LYS H 24  ? 1.772 1.625 1.805 -0.252 0.066  -0.032 24  LYS LLL C   
10159 O O   . LYS H 24  ? 1.719 1.648 1.782 -0.254 0.069  -0.025 24  LYS LLL O   
10160 C CB  . LYS H 24  ? 1.868 1.630 1.891 -0.304 0.014  -0.075 24  LYS LLL CB  
10161 C CG  . LYS H 24  ? 1.948 1.650 1.986 -0.330 0.017  -0.049 24  LYS LLL CG  
10162 C CD  . LYS H 24  ? 2.029 1.706 2.100 -0.387 -0.012 -0.050 24  LYS LLL CD  
10163 C CE  . LYS H 24  ? 2.158 1.710 2.185 -0.398 -0.034 -0.076 24  LYS LLL CE  
10164 N NZ  . LYS H 24  ? 2.205 1.684 2.212 -0.383 -0.014 -0.053 24  LYS LLL NZ  
10165 N N   . SER H 25  ? 1.816 1.634 1.840 -0.244 0.083  -0.008 25  SER LLL N   
10166 C CA  . SER H 25  ? 1.806 1.674 1.850 -0.237 0.110  0.030  25  SER LLL CA  
10167 C C   . SER H 25  ? 1.872 1.718 1.949 -0.273 0.115  0.065  25  SER LLL C   
10168 O O   . SER H 25  ? 1.963 1.724 2.022 -0.284 0.105  0.064  25  SER LLL O   
10169 C CB  . SER H 25  ? 1.804 1.657 1.806 -0.195 0.126  0.033  25  SER LLL CB  
10170 O OG  . SER H 25  ? 1.893 1.671 1.875 -0.194 0.128  0.045  25  SER LLL OG  
10171 N N   . SER H 26  ? 1.852 1.772 1.972 -0.287 0.132  0.097  26  SER LLL N   
10172 C CA  . SER H 26  ? 1.904 1.827 2.068 -0.327 0.140  0.139  26  SER LLL CA  
10173 C C   . SER H 26  ? 1.919 1.792 2.053 -0.312 0.160  0.170  26  SER LLL C   
10174 O O   . SER H 26  ? 1.996 1.834 2.154 -0.348 0.161  0.203  26  SER LLL O   
10175 C CB  . SER H 26  ? 1.891 1.921 2.109 -0.338 0.156  0.166  26  SER LLL CB  
10176 O OG  . SER H 26  ? 1.856 1.944 2.053 -0.293 0.171  0.154  26  SER LLL OG  
10177 N N   . GLN H 27  ? 1.860 1.730 1.946 -0.264 0.173  0.162  27  GLN LLL N   
10178 C CA  . GLN H 27  ? 1.905 1.734 1.955 -0.242 0.191  0.190  27  GLN LLL CA  
10179 C C   . GLN H 27  ? 1.887 1.653 1.884 -0.205 0.178  0.158  27  GLN LLL C   
10180 O O   . GLN H 27  ? 1.812 1.602 1.798 -0.188 0.167  0.120  27  GLN LLL O   
10181 C CB  . GLN H 27  ? 1.887 1.795 1.932 -0.217 0.220  0.217  27  GLN LLL CB  
10182 C CG  . GLN H 27  ? 1.950 1.838 1.976 -0.209 0.241  0.263  27  GLN LLL CG  
10183 C CD  . GLN H 27  ? 1.929 1.903 1.958 -0.195 0.271  0.294  27  GLN LLL CD  
10184 O OE1 . GLN H 27  ? 1.855 1.895 1.883 -0.176 0.277  0.275  27  GLN LLL OE1 
10185 N NE2 . GLN H 27  ? 1.996 1.965 2.023 -0.202 0.292  0.345  27  GLN LLL NE2 
10186 N N   . SER H 28  ? 1.953 1.646 1.922 -0.193 0.180  0.174  28  SER LLL N   
10187 C CA  . SER H 28  ? 1.971 1.614 1.891 -0.151 0.173  0.151  28  SER LLL CA  
10188 C C   . SER H 28  ? 1.915 1.627 1.813 -0.112 0.185  0.149  28  SER LLL C   
10189 O O   . SER H 28  ? 1.951 1.717 1.855 -0.111 0.203  0.178  28  SER LLL O   
10190 C CB  . SER H 28  ? 2.061 1.615 1.959 -0.144 0.174  0.176  28  SER LLL CB  
10191 O OG  . SER H 28  ? 2.059 1.583 1.915 -0.096 0.170  0.157  28  SER LLL OG  
10192 N N   . VAL H 29  ? 1.864 1.576 1.738 -0.082 0.174  0.116  29  VAL LLL N   
10193 C CA  . VAL H 29  ? 1.798 1.574 1.654 -0.050 0.179  0.108  29  VAL LLL CA  
10194 C C   . VAL H 29  ? 1.832 1.581 1.654 -0.011 0.176  0.110  29  VAL LLL C   
10195 O O   . VAL H 29  ? 1.768 1.564 1.576 0.013  0.173  0.098  29  VAL LLL O   
10196 C CB  . VAL H 29  ? 1.723 1.542 1.589 -0.054 0.168  0.071  29  VAL LLL CB  
10197 C CG1 . VAL H 29  ? 1.697 1.543 1.599 -0.089 0.168  0.071  29  VAL LLL CG1 
10198 C CG2 . VAL H 29  ? 1.734 1.516 1.588 -0.042 0.153  0.040  29  VAL LLL CG2 
10199 N N   . LEU H 30  ? 1.941 1.616 1.752 -0.006 0.176  0.126  30  LEU LLL N   
10200 C CA  . LEU H 30  ? 2.014 1.658 1.796 0.036  0.174  0.131  30  LEU LLL CA  
10201 C C   . LEU H 30  ? 1.994 1.678 1.757 0.058  0.184  0.165  30  LEU LLL C   
10202 O O   . LEU H 30  ? 2.030 1.711 1.795 0.042  0.196  0.200  30  LEU LLL O   
10203 C CB  . LEU H 30  ? 2.156 1.696 1.929 0.034  0.170  0.139  30  LEU LLL CB  
10204 C CG  . LEU H 30  ? 2.258 1.749 2.001 0.082  0.167  0.138  30  LEU LLL CG  
10205 C CD1 . LEU H 30  ? 2.330 1.809 2.056 0.104  0.176  0.185  30  LEU LLL CD1 
10206 C CD2 . LEU H 30  ? 2.212 1.766 1.950 0.115  0.162  0.109  30  LEU LLL CD2 
10207 N N   . TYR H 31  ? 1.950 1.677 1.697 0.093  0.178  0.157  31  TYR LLL N   
10208 C CA  . TYR H 31  ? 1.963 1.725 1.686 0.121  0.180  0.186  31  TYR LLL CA  
10209 C C   . TYR H 31  ? 2.021 1.721 1.726 0.153  0.180  0.211  31  TYR LLL C   
10210 O O   . TYR H 31  ? 2.028 1.731 1.728 0.186  0.171  0.197  31  TYR LLL O   
10211 C CB  . TYR H 31  ? 1.909 1.749 1.628 0.137  0.169  0.165  31  TYR LLL CB  
10212 C CG  . TYR H 31  ? 1.866 1.766 1.576 0.125  0.171  0.167  31  TYR LLL CG  
10213 C CD1 . TYR H 31  ? 1.803 1.721 1.530 0.094  0.176  0.150  31  TYR LLL CD1 
10214 C CD2 . TYR H 31  ? 1.887 1.826 1.568 0.146  0.167  0.185  31  TYR LLL CD2 
10215 C CE1 . TYR H 31  ? 1.771 1.736 1.484 0.089  0.179  0.149  31  TYR LLL CE1 
10216 C CE2 . TYR H 31  ? 1.859 1.846 1.522 0.139  0.167  0.182  31  TYR LLL CE2 
10217 C CZ  . TYR H 31  ? 1.804 1.801 1.481 0.111  0.175  0.163  31  TYR LLL CZ  
10218 O OH  . TYR H 31  ? 1.813 1.849 1.466 0.110  0.177  0.159  31  TYR LLL OH  
10219 N N   . SER H 32  ? 2.066 1.710 1.762 0.143  0.190  0.248  32  SER LLL N   
10220 C CA  . SER H 32  ? 2.163 1.730 1.839 0.172  0.191  0.277  32  SER LLL CA  
10221 C C   . SER H 32  ? 2.157 1.765 1.815 0.224  0.182  0.280  32  SER LLL C   
10222 O O   . SER H 32  ? 2.199 1.762 1.852 0.257  0.176  0.273  32  SER LLL O   
10223 C CB  . SER H 32  ? 2.248 1.779 1.914 0.156  0.204  0.328  32  SER LLL CB  
10224 O OG  . SER H 32  ? 2.370 1.812 2.016 0.181  0.203  0.356  32  SER LLL OG  
10225 N N   . SER H 33  ? 2.123 1.818 1.771 0.231  0.179  0.288  33  SER LLL N   
10226 C CA  . SER H 33  ? 2.135 1.892 1.770 0.273  0.166  0.293  33  SER LLL CA  
10227 C C   . SER H 33  ? 2.105 1.866 1.758 0.299  0.156  0.262  33  SER LLL C   
10228 O O   . SER H 33  ? 2.155 1.883 1.800 0.341  0.154  0.278  33  SER LLL O   
10229 C CB  . SER H 33  ? 2.103 1.952 1.731 0.261  0.159  0.283  33  SER LLL CB  
10230 O OG  . SER H 33  ? 2.201 2.054 1.800 0.253  0.169  0.317  33  SER LLL OG  
10231 N N   . ILE H 34  ? 2.039 1.842 1.716 0.278  0.152  0.222  34  ILE LLL N   
10232 C CA  . ILE H 34  ? 2.025 1.846 1.721 0.298  0.146  0.192  34  ILE LLL CA  
10233 C C   . ILE H 34  ? 2.019 1.781 1.725 0.270  0.153  0.161  34  ILE LLL C   
10234 O O   . ILE H 34  ? 1.955 1.753 1.676 0.235  0.151  0.138  34  ILE LLL O   
10235 C CB  . ILE H 34  ? 1.962 1.890 1.675 0.297  0.133  0.176  34  ILE LLL CB  
10236 C CG1 . ILE H 34  ? 1.909 1.876 1.620 0.255  0.130  0.167  34  ILE LLL CG1 
10237 C CG2 . ILE H 34  ? 1.999 1.980 1.706 0.339  0.121  0.202  34  ILE LLL CG2 
10238 C CD1 . ILE H 34  ? 1.844 1.898 1.572 0.246  0.115  0.146  34  ILE LLL CD1 
10239 N N   . ASN H 35  ? 2.104 1.775 1.800 0.286  0.158  0.161  35  ASN LLL N   
10240 C CA  . ASN H 35  ? 2.139 1.738 1.837 0.257  0.160  0.133  35  ASN LLL CA  
10241 C C   . ASN H 35  ? 2.056 1.718 1.773 0.241  0.156  0.094  35  ASN LLL C   
10242 O O   . ASN H 35  ? 2.058 1.710 1.772 0.263  0.155  0.067  35  ASN LLL O   
10243 C CB  . ASN H 35  ? 2.270 1.765 1.947 0.288  0.161  0.129  35  ASN LLL CB  
10244 C CG  . ASN H 35  ? 2.344 1.865 2.014 0.351  0.161  0.127  35  ASN LLL CG  
10245 O OD1 . ASN H 35  ? 2.320 1.936 2.007 0.363  0.159  0.113  35  ASN LLL OD1 
10246 N ND2 . ASN H 35  ? 2.479 1.917 2.124 0.391  0.163  0.145  35  ASN LLL ND2 
10247 N N   . LYS H 36  ? 1.989 1.710 1.721 0.204  0.154  0.092  36  LYS LLL N   
10248 C CA  . LYS H 36  ? 1.924 1.699 1.675 0.179  0.150  0.060  36  LYS LLL CA  
10249 C C   . LYS H 36  ? 1.857 1.623 1.618 0.132  0.152  0.060  36  LYS LLL C   
10250 O O   . LYS H 36  ? 1.845 1.621 1.604 0.122  0.157  0.086  36  LYS LLL O   
10251 C CB  . LYS H 36  ? 1.903 1.774 1.664 0.188  0.144  0.061  36  LYS LLL CB  
10252 C CG  . LYS H 36  ? 1.983 1.888 1.744 0.233  0.142  0.067  36  LYS LLL CG  
10253 C CD  . LYS H 36  ? 2.046 1.940 1.810 0.254  0.146  0.042  36  LYS LLL CD  
10254 C CE  . LYS H 36  ? 2.021 1.994 1.806 0.239  0.142  0.022  36  LYS LLL CE  
10255 N NZ  . LYS H 36  ? 2.052 2.006 1.832 0.249  0.148  -0.005 36  LYS LLL NZ  
10256 N N   . ASN H 37  ? 1.825 1.580 1.597 0.107  0.149  0.032  37  ASN LLL N   
10257 C CA  . ASN H 37  ? 1.806 1.568 1.595 0.064  0.149  0.030  37  ASN LLL CA  
10258 C C   . ASN H 37  ? 1.718 1.560 1.518 0.057  0.147  0.021  37  ASN LLL C   
10259 O O   . ASN H 37  ? 1.659 1.535 1.459 0.070  0.141  0.002  37  ASN LLL O   
10260 C CB  . ASN H 37  ? 1.850 1.561 1.643 0.042  0.142  0.005  37  ASN LLL CB  
10261 C CG  . ASN H 37  ? 1.956 1.578 1.742 0.033  0.142  0.018  37  ASN LLL CG  
10262 O OD1 . ASN H 37  ? 2.067 1.623 1.833 0.048  0.136  0.000  37  ASN LLL OD1 
10263 N ND2 . ASN H 37  ? 1.957 1.573 1.757 0.009  0.149  0.048  37  ASN LLL ND2 
10264 N N   . TYR H 38  ? 1.699 1.568 1.504 0.040  0.152  0.036  38  TYR LLL N   
10265 C CA  . TYR H 38  ? 1.651 1.585 1.459 0.036  0.149  0.029  38  TYR LLL CA  
10266 C C   . TYR H 38  ? 1.636 1.582 1.465 0.009  0.146  0.010  38  TYR LLL C   
10267 O O   . TYR H 38  ? 1.652 1.615 1.489 -0.007 0.152  0.017  38  TYR LLL O   
10268 C CB  . TYR H 38  ? 1.651 1.605 1.444 0.042  0.156  0.054  38  TYR LLL CB  
10269 C CG  . TYR H 38  ? 1.652 1.626 1.424 0.071  0.150  0.065  38  TYR LLL CG  
10270 C CD1 . TYR H 38  ? 1.697 1.644 1.465 0.094  0.148  0.071  38  TYR LLL CD1 
10271 C CD2 . TYR H 38  ? 1.636 1.655 1.390 0.077  0.144  0.067  38  TYR LLL CD2 
10272 C CE1 . TYR H 38  ? 1.704 1.678 1.458 0.123  0.141  0.083  38  TYR LLL CE1 
10273 C CE2 . TYR H 38  ? 1.661 1.704 1.399 0.101  0.134  0.076  38  TYR LLL CE2 
10274 C CZ  . TYR H 38  ? 1.690 1.717 1.432 0.124  0.132  0.086  38  TYR LLL CZ  
10275 O OH  . TYR H 38  ? 1.732 1.791 1.463 0.150  0.121  0.098  38  TYR LLL OH  
10276 N N   . LEU H 39  ? 1.636 1.574 1.469 0.008  0.138  -0.013 39  LEU LLL N   
10277 C CA  . LEU H 39  ? 1.622 1.567 1.470 -0.014 0.132  -0.032 39  LEU LLL CA  
10278 C C   . LEU H 39  ? 1.554 1.532 1.398 -0.005 0.124  -0.050 39  LEU LLL C   
10279 O O   . LEU H 39  ? 1.535 1.515 1.369 0.016  0.124  -0.052 39  LEU LLL O   
10280 C CB  . LEU H 39  ? 1.706 1.596 1.557 -0.026 0.129  -0.039 39  LEU LLL CB  
10281 C CG  . LEU H 39  ? 1.715 1.606 1.579 -0.050 0.118  -0.059 39  LEU LLL CG  
10282 C CD1 . LEU H 39  ? 1.727 1.625 1.575 -0.037 0.111  -0.083 39  LEU LLL CD1 
10283 C CD2 . LEU H 39  ? 1.676 1.615 1.564 -0.068 0.119  -0.053 39  LEU LLL CD2 
10284 N N   . ALA H 40  ? 1.503 1.511 1.358 -0.020 0.119  -0.059 40  ALA LLL N   
10285 C CA  . ALA H 40  ? 1.499 1.540 1.352 -0.018 0.112  -0.070 40  ALA LLL CA  
10286 C C   . ALA H 40  ? 1.512 1.555 1.373 -0.034 0.106  -0.083 40  ALA LLL C   
10287 O O   . ALA H 40  ? 1.525 1.551 1.396 -0.048 0.105  -0.084 40  ALA LLL O   
10288 C CB  . ALA H 40  ? 1.475 1.547 1.327 -0.018 0.109  -0.063 40  ALA LLL CB  
10289 N N   . TRP H 41  ? 1.504 1.572 1.360 -0.032 0.101  -0.090 41  TRP LLL N   
10290 C CA  . TRP H 41  ? 1.483 1.558 1.339 -0.042 0.094  -0.101 41  TRP LLL CA  
10291 C C   . TRP H 41  ? 1.452 1.560 1.312 -0.048 0.089  -0.095 41  TRP LLL C   
10292 O O   . TRP H 41  ? 1.428 1.558 1.286 -0.041 0.090  -0.089 41  TRP LLL O   
10293 C CB  . TRP H 41  ? 1.497 1.562 1.336 -0.031 0.095  -0.114 41  TRP LLL CB  
10294 C CG  . TRP H 41  ? 1.513 1.530 1.343 -0.031 0.094  -0.125 41  TRP LLL CG  
10295 C CD1 . TRP H 41  ? 1.552 1.534 1.370 -0.014 0.100  -0.126 41  TRP LLL CD1 
10296 C CD2 . TRP H 41  ? 1.509 1.504 1.342 -0.051 0.083  -0.135 41  TRP LLL CD2 
10297 N NE1 . TRP H 41  ? 1.581 1.511 1.391 -0.024 0.093  -0.138 41  TRP LLL NE1 
10298 C CE2 . TRP H 41  ? 1.572 1.513 1.393 -0.049 0.082  -0.144 41  TRP LLL CE2 
10299 C CE3 . TRP H 41  ? 1.490 1.505 1.334 -0.069 0.072  -0.137 41  TRP LLL CE3 
10300 C CZ2 . TRP H 41  ? 1.627 1.537 1.451 -0.071 0.068  -0.155 41  TRP LLL CZ2 
10301 C CZ3 . TRP H 41  ? 1.530 1.524 1.379 -0.088 0.060  -0.147 41  TRP LLL CZ3 
10302 C CH2 . TRP H 41  ? 1.600 1.542 1.439 -0.092 0.057  -0.156 41  TRP LLL CH2 
10303 N N   . TYR H 42  ? 1.432 1.543 1.299 -0.060 0.082  -0.095 42  TYR LLL N   
10304 C CA  . TYR H 42  ? 1.417 1.544 1.285 -0.066 0.076  -0.089 42  TYR LLL CA  
10305 C C   . TYR H 42  ? 1.417 1.552 1.282 -0.072 0.069  -0.092 42  TYR LLL C   
10306 O O   . TYR H 42  ? 1.397 1.525 1.265 -0.075 0.065  -0.099 42  TYR LLL O   
10307 C CB  . TYR H 42  ? 1.433 1.551 1.307 -0.067 0.075  -0.086 42  TYR LLL CB  
10308 C CG  . TYR H 42  ? 1.444 1.556 1.313 -0.060 0.080  -0.083 42  TYR LLL CG  
10309 C CD1 . TYR H 42  ? 1.437 1.540 1.309 -0.054 0.089  -0.081 42  TYR LLL CD1 
10310 C CD2 . TYR H 42  ? 1.463 1.579 1.323 -0.060 0.074  -0.080 42  TYR LLL CD2 
10311 C CE1 . TYR H 42  ? 1.427 1.528 1.289 -0.046 0.094  -0.075 42  TYR LLL CE1 
10312 C CE2 . TYR H 42  ? 1.460 1.574 1.310 -0.053 0.075  -0.079 42  TYR LLL CE2 
10313 C CZ  . TYR H 42  ? 1.451 1.557 1.299 -0.044 0.086  -0.076 42  TYR LLL CZ  
10314 O OH  . TYR H 42  ? 1.491 1.597 1.324 -0.034 0.088  -0.071 42  TYR LLL OH  
10315 N N   . GLN H 43  ? 1.431 1.583 1.290 -0.075 0.066  -0.083 43  GLN LLL N   
10316 C CA  . GLN H 43  ? 1.442 1.604 1.293 -0.081 0.059  -0.078 43  GLN LLL CA  
10317 C C   . GLN H 43  ? 1.425 1.577 1.284 -0.087 0.051  -0.068 43  GLN LLL C   
10318 O O   . GLN H 43  ? 1.443 1.587 1.304 -0.091 0.050  -0.063 43  GLN LLL O   
10319 C CB  . GLN H 43  ? 1.457 1.646 1.296 -0.079 0.064  -0.071 43  GLN LLL CB  
10320 C CG  . GLN H 43  ? 1.461 1.663 1.299 -0.091 0.058  -0.052 43  GLN LLL CG  
10321 C CD  . GLN H 43  ? 1.466 1.705 1.295 -0.090 0.067  -0.039 43  GLN LLL CD  
10322 O OE1 . GLN H 43  ? 1.442 1.699 1.282 -0.103 0.067  -0.019 43  GLN LLL OE1 
10323 N NE2 . GLN H 43  ? 1.475 1.727 1.283 -0.076 0.074  -0.051 43  GLN LLL NE2 
10324 N N   . GLN H 44  ? 1.409 1.557 1.268 -0.088 0.043  -0.065 44  GLN LLL N   
10325 C CA  . GLN H 44  ? 1.430 1.561 1.289 -0.089 0.035  -0.053 44  GLN LLL CA  
10326 C C   . GLN H 44  ? 1.470 1.611 1.319 -0.091 0.027  -0.040 44  GLN LLL C   
10327 O O   . GLN H 44  ? 1.470 1.622 1.322 -0.085 0.021  -0.044 44  GLN LLL O   
10328 C CB  . GLN H 44  ? 1.421 1.537 1.292 -0.078 0.034  -0.059 44  GLN LLL CB  
10329 C CG  . GLN H 44  ? 1.448 1.543 1.317 -0.071 0.026  -0.050 44  GLN LLL CG  
10330 C CD  . GLN H 44  ? 1.431 1.514 1.309 -0.055 0.030  -0.057 44  GLN LLL CD  
10331 O OE1 . GLN H 44  ? 1.383 1.490 1.278 -0.049 0.036  -0.062 44  GLN LLL OE1 
10332 N NE2 . GLN H 44  ? 1.437 1.483 1.301 -0.048 0.027  -0.057 44  GLN LLL NE2 
10333 N N   . LYS H 45  ? 1.524 1.668 1.364 -0.101 0.026  -0.023 45  LYS LLL N   
10334 C CA  . LYS H 45  ? 1.578 1.725 1.405 -0.104 0.018  -0.003 45  LYS LLL CA  
10335 C C   . LYS H 45  ? 1.608 1.717 1.441 -0.098 0.008  0.004  45  LYS LLL C   
10336 O O   . LYS H 45  ? 1.632 1.710 1.469 -0.102 0.007  0.001  45  LYS LLL O   
10337 C CB  . LYS H 45  ? 1.616 1.783 1.436 -0.118 0.024  0.017  45  LYS LLL CB  
10338 C CG  . LYS H 45  ? 1.629 1.840 1.432 -0.113 0.034  0.015  45  LYS LLL CG  
10339 C CD  . LYS H 45  ? 1.655 1.900 1.457 -0.125 0.045  0.038  45  LYS LLL CD  
10340 C CE  . LYS H 45  ? 1.647 1.911 1.467 -0.127 0.056  0.030  45  LYS LLL CE  
10341 N NZ  . LYS H 45  ? 1.661 1.970 1.489 -0.141 0.066  0.057  45  LYS LLL NZ  
10342 N N   . PRO H 46  ? 1.643 1.753 1.474 -0.086 -0.001 0.010  46  PRO LLL N   
10343 C CA  . PRO H 46  ? 1.654 1.727 1.488 -0.073 -0.010 0.018  46  PRO LLL CA  
10344 C C   . PRO H 46  ? 1.677 1.700 1.500 -0.083 -0.016 0.034  46  PRO LLL C   
10345 O O   . PRO H 46  ? 1.691 1.719 1.504 -0.101 -0.016 0.054  46  PRO LLL O   
10346 C CB  . PRO H 46  ? 1.689 1.783 1.517 -0.062 -0.021 0.033  46  PRO LLL CB  
10347 C CG  . PRO H 46  ? 1.691 1.833 1.521 -0.066 -0.018 0.018  46  PRO LLL CG  
10348 C CD  . PRO H 46  ? 1.669 1.816 1.493 -0.081 -0.005 0.008  46  PRO LLL CD  
10349 N N   . GLY H 47  ? 1.699 1.674 1.521 -0.072 -0.019 0.026  47  GLY LLL N   
10350 C CA  . GLY H 47  ? 1.735 1.646 1.542 -0.082 -0.029 0.035  47  GLY LLL CA  
10351 C C   . GLY H 47  ? 1.707 1.607 1.514 -0.101 -0.027 0.020  47  GLY LLL C   
10352 O O   . GLY H 47  ? 1.741 1.580 1.533 -0.106 -0.038 0.017  47  GLY LLL O   
10353 N N   . GLN H 48  ? 1.671 1.625 1.490 -0.110 -0.016 0.011  48  GLN LLL N   
10354 C CA  . GLN H 48  ? 1.661 1.622 1.484 -0.126 -0.014 -0.001 48  GLN LLL CA  
10355 C C   . GLN H 48  ? 1.606 1.569 1.429 -0.105 -0.006 -0.027 48  GLN LLL C   
10356 O O   . GLN H 48  ? 1.599 1.574 1.428 -0.083 0.001  -0.034 48  GLN LLL O   
10357 C CB  . GLN H 48  ? 1.649 1.670 1.485 -0.141 -0.004 0.008  48  GLN LLL CB  
10358 C CG  . GLN H 48  ? 1.694 1.728 1.529 -0.159 -0.007 0.039  48  GLN LLL CG  
10359 C CD  . GLN H 48  ? 1.695 1.795 1.538 -0.166 0.007  0.046  48  GLN LLL CD  
10360 O OE1 . GLN H 48  ? 1.697 1.827 1.546 -0.156 0.017  0.028  48  GLN LLL OE1 
10361 N NE2 . GLN H 48  ? 1.727 1.849 1.567 -0.179 0.009  0.075  48  GLN LLL NE2 
10362 N N   . PRO H 49  ? 1.575 1.532 1.394 -0.112 -0.007 -0.040 49  PRO LLL N   
10363 C CA  . PRO H 49  ? 1.528 1.501 1.348 -0.096 0.004  -0.059 49  PRO LLL CA  
10364 C C   . PRO H 49  ? 1.463 1.491 1.301 -0.099 0.017  -0.056 49  PRO LLL C   
10365 O O   . PRO H 49  ? 1.476 1.529 1.321 -0.111 0.017  -0.043 49  PRO LLL O   
10366 C CB  . PRO H 49  ? 1.565 1.513 1.369 -0.106 -0.006 -0.069 49  PRO LLL CB  
10367 C CG  . PRO H 49  ? 1.583 1.537 1.395 -0.137 -0.018 -0.052 49  PRO LLL CG  
10368 C CD  . PRO H 49  ? 1.608 1.547 1.423 -0.139 -0.021 -0.035 49  PRO LLL CD  
10369 N N   . PRO H 50  ? 1.389 1.432 1.231 -0.085 0.028  -0.068 50  PRO LLL N   
10370 C CA  . PRO H 50  ? 1.339 1.419 1.192 -0.087 0.039  -0.069 50  PRO LLL CA  
10371 C C   . PRO H 50  ? 1.326 1.423 1.180 -0.098 0.037  -0.065 50  PRO LLL C   
10372 O O   . PRO H 50  ? 1.295 1.380 1.141 -0.103 0.029  -0.068 50  PRO LLL O   
10373 C CB  . PRO H 50  ? 1.307 1.388 1.163 -0.072 0.049  -0.078 50  PRO LLL CB  
10374 C CG  . PRO H 50  ? 1.340 1.400 1.193 -0.060 0.048  -0.081 50  PRO LLL CG  
10375 C CD  . PRO H 50  ? 1.387 1.414 1.223 -0.065 0.034  -0.079 50  PRO LLL CD  
10376 N N   . LYS H 51  ? 1.363 1.493 1.225 -0.100 0.044  -0.060 51  LYS LLL N   
10377 C CA  . LYS H 51  ? 1.409 1.572 1.278 -0.104 0.047  -0.054 51  LYS LLL CA  
10378 C C   . LYS H 51  ? 1.380 1.551 1.249 -0.087 0.058  -0.063 51  LYS LLL C   
10379 O O   . LYS H 51  ? 1.333 1.495 1.200 -0.079 0.065  -0.070 51  LYS LLL O   
10380 C CB  . LYS H 51  ? 1.455 1.649 1.329 -0.112 0.049  -0.040 51  LYS LLL CB  
10381 C CG  . LYS H 51  ? 1.482 1.723 1.370 -0.116 0.053  -0.028 51  LYS LLL CG  
10382 C CD  . LYS H 51  ? 1.537 1.813 1.431 -0.128 0.057  -0.008 51  LYS LLL CD  
10383 C CE  . LYS H 51  ? 1.576 1.915 1.487 -0.124 0.067  0.005  51  LYS LLL CE  
10384 N NZ  . LYS H 51  ? 1.606 1.971 1.542 -0.147 0.055  0.021  51  LYS LLL NZ  
10385 N N   . LEU H 52  ? 1.405 1.589 1.278 -0.083 0.058  -0.061 52  LEU LLL N   
10386 C CA  . LEU H 52  ? 1.416 1.606 1.288 -0.064 0.069  -0.065 52  LEU LLL CA  
10387 C C   . LEU H 52  ? 1.378 1.600 1.255 -0.056 0.078  -0.061 52  LEU LLL C   
10388 O O   . LEU H 52  ? 1.343 1.605 1.233 -0.063 0.075  -0.048 52  LEU LLL O   
10389 C CB  . LEU H 52  ? 1.453 1.650 1.324 -0.061 0.064  -0.061 52  LEU LLL CB  
10390 C CG  . LEU H 52  ? 1.477 1.673 1.345 -0.039 0.074  -0.061 52  LEU LLL CG  
10391 C CD1 . LEU H 52  ? 1.482 1.639 1.340 -0.034 0.082  -0.067 52  LEU LLL CD1 
10392 C CD2 . LEU H 52  ? 1.495 1.711 1.361 -0.035 0.065  -0.053 52  LEU LLL CD2 
10393 N N   . LEU H 53  ? 1.362 1.568 1.230 -0.042 0.087  -0.071 53  LEU LLL N   
10394 C CA  . LEU H 53  ? 1.408 1.635 1.270 -0.025 0.098  -0.073 53  LEU LLL CA  
10395 C C   . LEU H 53  ? 1.427 1.648 1.287 -0.001 0.106  -0.075 53  LEU LLL C   
10396 O O   . LEU H 53  ? 1.431 1.692 1.297 0.016  0.113  -0.067 53  LEU LLL O   
10397 C CB  . LEU H 53  ? 1.442 1.643 1.286 -0.025 0.099  -0.087 53  LEU LLL CB  
10398 C CG  . LEU H 53  ? 1.429 1.638 1.271 -0.043 0.091  -0.083 53  LEU LLL CG  
10399 C CD1 . LEU H 53  ? 1.441 1.626 1.264 -0.042 0.088  -0.098 53  LEU LLL CD1 
10400 C CD2 . LEU H 53  ? 1.426 1.683 1.272 -0.046 0.095  -0.066 53  LEU LLL CD2 
10401 N N   . ILE H 54  ? 1.438 1.614 1.291 0.002  0.105  -0.082 54  ILE LLL N   
10402 C CA  . ILE H 54  ? 1.482 1.635 1.327 0.027  0.113  -0.082 54  ILE LLL CA  
10403 C C   . ILE H 54  ? 1.486 1.614 1.333 0.022  0.110  -0.074 54  ILE LLL C   
10404 O O   . ILE H 54  ? 1.466 1.573 1.314 0.004  0.107  -0.077 54  ILE LLL O   
10405 C CB  . ILE H 54  ? 1.519 1.631 1.344 0.038  0.118  -0.099 54  ILE LLL CB  
10406 C CG1 . ILE H 54  ? 1.546 1.691 1.360 0.056  0.125  -0.105 54  ILE LLL CG1 
10407 C CG2 . ILE H 54  ? 1.582 1.645 1.397 0.057  0.122  -0.100 54  ILE LLL CG2 
10408 C CD1 . ILE H 54  ? 1.628 1.728 1.411 0.073  0.129  -0.128 54  ILE LLL CD1 
10409 N N   . TYR H 55  ? 1.494 1.630 1.342 0.042  0.113  -0.063 55  TYR LLL N   
10410 C CA  . TYR H 55  ? 1.504 1.618 1.347 0.045  0.112  -0.051 55  TYR LLL CA  
10411 C C   . TYR H 55  ? 1.556 1.637 1.388 0.072  0.120  -0.046 55  TYR LLL C   
10412 O O   . TYR H 55  ? 1.587 1.666 1.415 0.091  0.125  -0.054 55  TYR LLL O   
10413 C CB  . TYR H 55  ? 1.504 1.660 1.351 0.041  0.103  -0.040 55  TYR LLL CB  
10414 C CG  . TYR H 55  ? 1.507 1.714 1.366 0.058  0.099  -0.030 55  TYR LLL CG  
10415 C CD1 . TYR H 55  ? 1.495 1.750 1.371 0.048  0.094  -0.032 55  TYR LLL CD1 
10416 C CD2 . TYR H 55  ? 1.553 1.765 1.407 0.083  0.099  -0.016 55  TYR LLL CD2 
10417 C CE1 . TYR H 55  ? 1.511 1.827 1.407 0.062  0.090  -0.019 55  TYR LLL CE1 
10418 C CE2 . TYR H 55  ? 1.568 1.839 1.439 0.101  0.094  -0.005 55  TYR LLL CE2 
10419 C CZ  . TYR H 55  ? 1.540 1.867 1.435 0.089  0.090  -0.006 55  TYR LLL CZ  
10420 O OH  . TYR H 55  ? 1.542 1.940 1.462 0.104  0.086  0.009  55  TYR LLL OH  
10421 N N   . TRP H 56  ? 1.607 1.660 1.432 0.076  0.122  -0.031 56  TRP LLL N   
10422 C CA  . TRP H 56  ? 1.644 1.642 1.455 0.097  0.130  -0.023 56  TRP LLL CA  
10423 C C   . TRP H 56  ? 1.607 1.562 1.411 0.101  0.133  -0.044 56  TRP LLL C   
10424 O O   . TRP H 56  ? 1.611 1.548 1.404 0.133  0.137  -0.046 56  TRP LLL O   
10425 C CB  . TRP H 56  ? 1.694 1.713 1.501 0.131  0.130  -0.005 56  TRP LLL CB  
10426 C CG  . TRP H 56  ? 1.690 1.754 1.497 0.129  0.122  0.013  56  TRP LLL CG  
10427 C CD1 . TRP H 56  ? 1.688 1.758 1.491 0.104  0.119  0.015  56  TRP LLL CD1 
10428 C CD2 . TRP H 56  ? 1.690 1.801 1.500 0.154  0.115  0.029  56  TRP LLL CD2 
10429 N NE1 . TRP H 56  ? 1.686 1.797 1.482 0.112  0.109  0.028  56  TRP LLL NE1 
10430 C CE2 . TRP H 56  ? 1.706 1.845 1.508 0.140  0.105  0.038  56  TRP LLL CE2 
10431 C CE3 . TRP H 56  ? 1.692 1.829 1.510 0.190  0.116  0.037  56  TRP LLL CE3 
10432 C CZ2 . TRP H 56  ? 1.717 1.907 1.517 0.155  0.092  0.053  56  TRP LLL CZ2 
10433 C CZ3 . TRP H 56  ? 1.710 1.905 1.534 0.206  0.104  0.056  56  TRP LLL CZ3 
10434 C CH2 . TRP H 56  ? 1.708 1.929 1.523 0.187  0.091  0.063  56  TRP LLL CH2 
10435 N N   . ALA H 57  ? 1.524 1.468 1.332 0.072  0.129  -0.059 57  ALA LLL N   
10436 C CA  . ALA H 57  ? 1.531 1.422 1.327 0.065  0.127  -0.080 57  ALA LLL CA  
10437 C C   . ALA H 57  ? 1.511 1.417 1.293 0.086  0.128  -0.101 57  ALA LLL C   
10438 O O   . ALA H 57  ? 1.471 1.353 1.242 0.073  0.123  -0.122 57  ALA LLL O   
10439 C CB  . ALA H 57  ? 1.609 1.425 1.392 0.074  0.129  -0.074 57  ALA LLL CB  
10440 N N   . SER H 58  ? 1.505 1.456 1.289 0.116  0.135  -0.093 58  SER LLL N   
10441 C CA  . SER H 58  ? 1.554 1.519 1.322 0.149  0.142  -0.107 58  SER LLL CA  
10442 C C   . SER H 58  ? 1.528 1.585 1.318 0.163  0.148  -0.093 58  SER LLL C   
10443 O O   . SER H 58  ? 1.535 1.623 1.317 0.182  0.156  -0.103 58  SER LLL O   
10444 C CB  . SER H 58  ? 1.638 1.540 1.383 0.185  0.148  -0.110 58  SER LLL CB  
10445 O OG  . SER H 58  ? 1.652 1.568 1.410 0.202  0.150  -0.083 58  SER LLL OG  
10446 N N   . THR H 59  ? 1.527 1.629 1.342 0.154  0.143  -0.071 59  THR LLL N   
10447 C CA  . THR H 59  ? 1.529 1.721 1.370 0.160  0.142  -0.055 59  THR LLL CA  
10448 C C   . THR H 59  ? 1.481 1.711 1.334 0.124  0.136  -0.058 59  THR LLL C   
10449 O O   . THR H 59  ? 1.456 1.659 1.308 0.093  0.127  -0.061 59  THR LLL O   
10450 C CB  . THR H 59  ? 1.557 1.775 1.413 0.161  0.134  -0.033 59  THR LLL CB  
10451 O OG1 . THR H 59  ? 1.631 1.788 1.470 0.181  0.136  -0.028 59  THR LLL OG1 
10452 C CG2 . THR H 59  ? 1.563 1.868 1.446 0.182  0.134  -0.016 59  THR LLL CG2 
10453 N N   . ARG H 60  ? 1.510 1.803 1.376 0.130  0.142  -0.054 60  ARG LLL N   
10454 C CA  . ARG H 60  ? 1.510 1.838 1.387 0.096  0.137  -0.052 60  ARG LLL CA  
10455 C C   . ARG H 60  ? 1.486 1.865 1.393 0.072  0.123  -0.032 60  ARG LLL C   
10456 O O   . ARG H 60  ? 1.496 1.921 1.423 0.088  0.122  -0.017 60  ARG LLL O   
10457 C CB  . ARG H 60  ? 1.556 1.930 1.430 0.112  0.152  -0.052 60  ARG LLL CB  
10458 C CG  . ARG H 60  ? 1.630 1.955 1.466 0.145  0.164  -0.075 60  ARG LLL CG  
10459 C CD  . ARG H 60  ? 1.651 2.002 1.469 0.147  0.174  -0.083 60  ARG LLL CD  
10460 N NE  . ARG H 60  ? 1.664 2.109 1.507 0.158  0.187  -0.060 60  ARG LLL NE  
10461 C CZ  . ARG H 60  ? 1.707 2.197 1.555 0.201  0.205  -0.055 60  ARG LLL CZ  
10462 N NH1 . ARG H 60  ? 1.758 2.193 1.580 0.241  0.210  -0.072 60  ARG LLL NH1 
10463 N NH2 . ARG H 60  ? 1.689 2.279 1.567 0.206  0.217  -0.029 60  ARG LLL NH2 
10464 N N   . GLU H 61  ? 1.480 1.849 1.390 0.036  0.111  -0.033 61  GLU LLL N   
10465 C CA  . GLU H 61  ? 1.489 1.894 1.422 0.007  0.094  -0.019 61  GLU LLL CA  
10466 C C   . GLU H 61  ? 1.453 1.931 1.413 -0.003 0.097  -0.001 61  GLU LLL C   
10467 O O   . GLU H 61  ? 1.419 1.908 1.371 0.007  0.112  -0.003 61  GLU LLL O   
10468 C CB  . GLU H 61  ? 1.526 1.879 1.444 -0.022 0.082  -0.028 61  GLU LLL CB  
10469 C CG  . GLU H 61  ? 1.566 1.935 1.497 -0.051 0.061  -0.020 61  GLU LLL CG  
10470 C CD  . GLU H 61  ? 1.609 1.990 1.542 -0.048 0.048  -0.016 61  GLU LLL CD  
10471 O OE1 . GLU H 61  ? 1.644 2.082 1.599 -0.036 0.047  -0.003 61  GLU LLL OE1 
10472 O OE2 . GLU H 61  ? 1.641 1.978 1.552 -0.055 0.038  -0.026 61  GLU LLL OE2 
10473 N N   . SER H 62  ? 1.448 1.977 1.437 -0.023 0.082  0.016  62  SER LLL N   
10474 C CA  . SER H 62  ? 1.452 2.055 1.476 -0.045 0.080  0.039  62  SER LLL CA  
10475 C C   . SER H 62  ? 1.447 2.017 1.457 -0.071 0.081  0.038  62  SER LLL C   
10476 O O   . SER H 62  ? 1.415 1.916 1.402 -0.087 0.069  0.023  62  SER LLL O   
10477 C CB  . SER H 62  ? 1.487 2.129 1.541 -0.074 0.055  0.054  62  SER LLL CB  
10478 O OG  . SER H 62  ? 1.511 2.084 1.540 -0.094 0.033  0.038  62  SER LLL OG  
10479 N N   . GLY H 63  ? 1.471 2.092 1.492 -0.070 0.097  0.053  63  GLY LLL N   
10480 C CA  . GLY H 63  ? 1.484 2.090 1.495 -0.094 0.099  0.061  63  GLY LLL CA  
10481 C C   . GLY H 63  ? 1.473 2.030 1.442 -0.070 0.113  0.040  63  GLY LLL C   
10482 O O   . GLY H 63  ? 1.459 1.983 1.412 -0.088 0.109  0.040  63  GLY LLL O   
10483 N N   . VAL H 64  ? 1.462 2.014 1.414 -0.030 0.128  0.022  64  VAL LLL N   
10484 C CA  . VAL H 64  ? 1.473 1.969 1.382 -0.007 0.137  -0.004 64  VAL LLL CA  
10485 C C   . VAL H 64  ? 1.462 2.000 1.357 0.030  0.161  -0.006 64  VAL LLL C   
10486 O O   . VAL H 64  ? 1.451 2.020 1.357 0.059  0.171  -0.004 64  VAL LLL O   
10487 C CB  . VAL H 64  ? 1.499 1.928 1.394 0.004  0.130  -0.027 64  VAL LLL CB  
10488 C CG1 . VAL H 64  ? 1.532 1.905 1.389 0.020  0.134  -0.052 64  VAL LLL CG1 
10489 C CG2 . VAL H 64  ? 1.493 1.889 1.399 -0.026 0.110  -0.025 64  VAL LLL CG2 
10490 N N   . PRO H 65  ? 1.464 2.001 1.328 0.035  0.170  -0.010 65  PRO LLL N   
10491 C CA  . PRO H 65  ? 1.518 2.092 1.357 0.075  0.194  -0.015 65  PRO LLL CA  
10492 C C   . PRO H 65  ? 1.562 2.087 1.372 0.117  0.201  -0.046 65  PRO LLL C   
10493 O O   . PRO H 65  ? 1.519 1.972 1.322 0.110  0.186  -0.064 65  PRO LLL O   
10494 C CB  . PRO H 65  ? 1.550 2.109 1.351 0.066  0.195  -0.020 65  PRO LLL CB  
10495 C CG  . PRO H 65  ? 1.508 2.057 1.333 0.019  0.176  0.001  65  PRO LLL CG  
10496 C CD  . PRO H 65  ? 1.466 1.970 1.315 0.005  0.158  -0.009 65  PRO LLL CD  
10497 N N   . ASP H 66  ? 1.628 2.193 1.419 0.161  0.224  -0.049 66  ASP LLL N   
10498 C CA  . ASP H 66  ? 1.669 2.189 1.426 0.211  0.235  -0.078 66  ASP LLL CA  
10499 C C   . ASP H 66  ? 1.669 2.086 1.371 0.209  0.222  -0.116 66  ASP LLL C   
10500 O O   . ASP H 66  ? 1.672 2.017 1.357 0.226  0.216  -0.139 66  ASP LLL O   
10501 C CB  . ASP H 66  ? 1.746 2.329 1.484 0.262  0.265  -0.076 66  ASP LLL CB  
10502 C CG  . ASP H 66  ? 1.746 2.447 1.518 0.252  0.282  -0.037 66  ASP LLL CG  
10503 O OD1 . ASP H 66  ? 1.754 2.466 1.507 0.229  0.282  -0.031 66  ASP LLL OD1 
10504 O OD2 . ASP H 66  ? 1.766 2.550 1.586 0.267  0.294  -0.011 66  ASP LLL OD2 
10505 N N   . ARG H 67  ? 1.657 2.074 1.334 0.189  0.217  -0.120 67  ARG LLL N   
10506 C CA  . ARG H 67  ? 1.717 2.055 1.338 0.188  0.204  -0.155 67  ARG LLL CA  
10507 C C   . ARG H 67  ? 1.679 1.939 1.314 0.158  0.179  -0.168 67  ARG LLL C   
10508 O O   . ARG H 67  ? 1.700 1.887 1.297 0.161  0.166  -0.199 67  ARG LLL O   
10509 C CB  . ARG H 67  ? 1.743 2.113 1.341 0.170  0.202  -0.148 67  ARG LLL CB  
10510 C CG  . ARG H 67  ? 1.685 2.088 1.328 0.124  0.190  -0.115 67  ARG LLL CG  
10511 C CD  . ARG H 67  ? 1.724 2.138 1.334 0.110  0.185  -0.111 67  ARG LLL CD  
10512 N NE  . ARG H 67  ? 1.675 2.113 1.323 0.069  0.174  -0.078 67  ARG LLL NE  
10513 C CZ  . ARG H 67  ? 1.665 2.172 1.343 0.057  0.186  -0.040 67  ARG LLL CZ  
10514 N NH1 . ARG H 67  ? 1.690 2.265 1.370 0.082  0.212  -0.026 67  ARG LLL NH1 
10515 N NH2 . ARG H 67  ? 1.623 2.131 1.329 0.020  0.172  -0.015 67  ARG LLL NH2 
10516 N N   . PHE H 68  ? 1.655 1.932 1.342 0.130  0.171  -0.144 68  PHE LLL N   
10517 C CA  . PHE H 68  ? 1.668 1.885 1.373 0.106  0.153  -0.149 68  PHE LLL CA  
10518 C C   . PHE H 68  ? 1.728 1.910 1.435 0.133  0.159  -0.156 68  PHE LLL C   
10519 O O   . PHE H 68  ? 1.755 1.986 1.483 0.155  0.172  -0.139 68  PHE LLL O   
10520 C CB  . PHE H 68  ? 1.585 1.833 1.335 0.071  0.144  -0.123 68  PHE LLL CB  
10521 C CG  . PHE H 68  ? 1.564 1.819 1.312 0.041  0.133  -0.118 68  PHE LLL CG  
10522 C CD1 . PHE H 68  ? 1.542 1.750 1.288 0.020  0.116  -0.129 68  PHE LLL CD1 
10523 C CD2 . PHE H 68  ? 1.591 1.905 1.343 0.036  0.139  -0.097 68  PHE LLL CD2 
10524 C CE1 . PHE H 68  ? 1.541 1.759 1.286 -0.001 0.105  -0.122 68  PHE LLL CE1 
10525 C CE2 . PHE H 68  ? 1.584 1.899 1.331 0.012  0.129  -0.089 68  PHE LLL CE2 
10526 C CZ  . PHE H 68  ? 1.556 1.823 1.299 -0.004 0.111  -0.103 68  PHE LLL CZ  
10527 N N   . SER H 69  ? 1.767 1.868 1.455 0.130  0.148  -0.177 69  SER LLL N   
10528 C CA  . SER H 69  ? 1.800 1.850 1.485 0.154  0.151  -0.183 69  SER LLL CA  
10529 C C   . SER H 69  ? 1.793 1.764 1.475 0.126  0.133  -0.194 69  SER LLL C   
10530 O O   . SER H 69  ? 1.819 1.755 1.477 0.108  0.121  -0.214 69  SER LLL O   
10531 C CB  . SER H 69  ? 1.904 1.932 1.546 0.202  0.164  -0.203 69  SER LLL CB  
10532 O OG  . SER H 69  ? 1.987 1.973 1.581 0.200  0.157  -0.233 69  SER LLL OG  
10533 N N   . GLY H 70  ? 1.772 1.724 1.479 0.121  0.133  -0.177 70  GLY LLL N   
10534 C CA  . GLY H 70  ? 1.819 1.706 1.531 0.094  0.120  -0.179 70  GLY LLL CA  
10535 C C   . GLY H 70  ? 1.922 1.736 1.614 0.119  0.123  -0.185 70  GLY LLL C   
10536 O O   . GLY H 70  ? 1.945 1.774 1.633 0.158  0.136  -0.177 70  GLY LLL O   
10537 N N   . SER H 71  ? 2.008 1.745 1.689 0.097  0.110  -0.197 71  SER LLL N   
10538 C CA  . SER H 71  ? 2.088 1.738 1.754 0.110  0.109  -0.196 71  SER LLL CA  
10539 C C   . SER H 71  ? 2.069 1.692 1.764 0.065  0.099  -0.179 71  SER LLL C   
10540 O O   . SER H 71  ? 1.996 1.669 1.718 0.031  0.093  -0.173 71  SER LLL O   
10541 C CB  . SER H 71  ? 2.208 1.777 1.823 0.129  0.102  -0.232 71  SER LLL CB  
10542 O OG  . SER H 71  ? 2.244 1.797 1.849 0.092  0.083  -0.255 71  SER LLL OG  
10543 N N   . GLY H 72  ? 2.112 1.659 1.801 0.066  0.098  -0.169 72  GLY LLL N   
10544 C CA  . GLY H 72  ? 2.093 1.612 1.810 0.023  0.091  -0.149 72  GLY LLL CA  
10545 C C   . GLY H 72  ? 2.115 1.565 1.827 0.033  0.097  -0.125 72  GLY LLL C   
10546 O O   . GLY H 72  ? 2.072 1.535 1.776 0.074  0.110  -0.110 72  GLY LLL O   
10547 N N   . SER H 73  ? 2.155 1.539 1.876 -0.005 0.085  -0.119 73  SER LLL N   
10548 C CA  . SER H 73  ? 2.247 1.542 1.960 -0.005 0.086  -0.095 73  SER LLL CA  
10549 C C   . SER H 73  ? 2.232 1.547 1.989 -0.056 0.087  -0.059 73  SER LLL C   
10550 O O   . SER H 73  ? 2.289 1.558 2.059 -0.101 0.071  -0.065 73  SER LLL O   
10551 C CB  . SER H 73  ? 2.371 1.549 2.044 -0.003 0.069  -0.127 73  SER LLL CB  
10552 O OG  . SER H 73  ? 2.487 1.565 2.152 -0.008 0.068  -0.104 73  SER LLL OG  
10553 N N   . GLY H 74  ? 2.186 1.573 1.965 -0.049 0.105  -0.025 74  GLY LLL N   
10554 C CA  . GLY H 74  ? 2.185 1.592 1.999 -0.083 0.113  0.017  74  GLY LLL CA  
10555 C C   . GLY H 74  ? 2.117 1.603 1.972 -0.123 0.111  0.017  74  GLY LLL C   
10556 O O   . GLY H 74  ? 2.058 1.627 1.928 -0.115 0.126  0.033  74  GLY LLL O   
10557 N N   . THR H 75  ? 2.146 1.605 2.017 -0.163 0.093  -0.001 75  THR LLL N   
10558 C CA  . THR H 75  ? 2.098 1.627 2.015 -0.204 0.088  0.003  75  THR LLL CA  
10559 C C   . THR H 75  ? 2.053 1.605 1.962 -0.205 0.069  -0.040 75  THR LLL C   
10560 O O   . THR H 75  ? 1.971 1.592 1.916 -0.230 0.064  -0.039 75  THR LLL O   
10561 C CB  . THR H 75  ? 2.190 1.681 2.142 -0.257 0.079  0.027  75  THR LLL CB  
10562 O OG1 . THR H 75  ? 2.300 1.697 2.230 -0.275 0.052  -0.004 75  THR LLL OG1 
10563 C CG2 . THR H 75  ? 2.240 1.701 2.196 -0.258 0.098  0.075  75  THR LLL CG2 
10564 N N   . ASP H 76  ? 2.096 1.596 1.959 -0.176 0.060  -0.075 76  ASP LLL N   
10565 C CA  . ASP H 76  ? 2.104 1.611 1.946 -0.174 0.041  -0.117 76  ASP LLL CA  
10566 C C   . ASP H 76  ? 2.089 1.625 1.897 -0.123 0.053  -0.134 76  ASP LLL C   
10567 O O   . ASP H 76  ? 2.164 1.648 1.939 -0.088 0.061  -0.136 76  ASP LLL O   
10568 C CB  . ASP H 76  ? 2.196 1.600 2.007 -0.190 0.016  -0.147 76  ASP LLL CB  
10569 C CG  . ASP H 76  ? 2.238 1.618 2.088 -0.250 -0.003 -0.134 76  ASP LLL CG  
10570 O OD1 . ASP H 76  ? 2.197 1.656 2.090 -0.281 -0.010 -0.128 76  ASP LLL OD1 
10571 O OD2 . ASP H 76  ? 2.324 1.611 2.166 -0.266 -0.011 -0.127 76  ASP LLL OD2 
10572 N N   . PHE H 77  ? 2.035 1.648 1.850 -0.119 0.054  -0.143 77  PHE LLL N   
10573 C CA  . PHE H 77  ? 2.014 1.671 1.807 -0.079 0.065  -0.154 77  PHE LLL CA  
10574 C C   . PHE H 77  ? 1.982 1.670 1.761 -0.082 0.052  -0.181 77  PHE LLL C   
10575 O O   . PHE H 77  ? 1.958 1.670 1.759 -0.115 0.038  -0.183 77  PHE LLL O   
10576 C CB  . PHE H 77  ? 1.977 1.708 1.796 -0.071 0.082  -0.126 77  PHE LLL CB  
10577 C CG  . PHE H 77  ? 2.038 1.748 1.868 -0.069 0.094  -0.095 77  PHE LLL CG  
10578 C CD1 . PHE H 77  ? 2.094 1.776 1.901 -0.034 0.104  -0.089 77  PHE LLL CD1 
10579 C CD2 . PHE H 77  ? 2.063 1.783 1.926 -0.100 0.096  -0.071 77  PHE LLL CD2 
10580 C CE1 . PHE H 77  ? 2.135 1.796 1.947 -0.030 0.114  -0.058 77  PHE LLL CE1 
10581 C CE2 . PHE H 77  ? 2.108 1.809 1.976 -0.097 0.109  -0.040 77  PHE LLL CE2 
10582 C CZ  . PHE H 77  ? 2.146 1.814 1.987 -0.063 0.117  -0.034 77  PHE LLL CZ  
10583 N N   . THR H 78  ? 1.965 1.658 1.708 -0.047 0.058  -0.199 78  THR LLL N   
10584 C CA  . THR H 78  ? 1.938 1.657 1.656 -0.043 0.048  -0.224 78  THR LLL CA  
10585 C C   . THR H 78  ? 1.886 1.671 1.600 -0.012 0.066  -0.217 78  THR LLL C   
10586 O O   . THR H 78  ? 1.912 1.696 1.619 0.018  0.082  -0.208 78  THR LLL O   
10587 C CB  . THR H 78  ? 2.021 1.667 1.686 -0.030 0.036  -0.260 78  THR LLL CB  
10588 O OG1 . THR H 78  ? 2.093 1.663 1.764 -0.057 0.022  -0.263 78  THR LLL OG1 
10589 C CG2 . THR H 78  ? 2.036 1.705 1.676 -0.037 0.021  -0.285 78  THR LLL CG2 
10590 N N   . LEU H 79  ? 1.841 1.681 1.559 -0.022 0.060  -0.218 79  LEU LLL N   
10591 C CA  . LEU H 79  ? 1.802 1.705 1.513 -0.001 0.073  -0.212 79  LEU LLL CA  
10592 C C   . LEU H 79  ? 1.860 1.759 1.525 0.012  0.067  -0.238 79  LEU LLL C   
10593 O O   . LEU H 79  ? 1.893 1.785 1.549 -0.011 0.048  -0.250 79  LEU LLL O   
10594 C CB  . LEU H 79  ? 1.724 1.685 1.470 -0.022 0.071  -0.191 79  LEU LLL CB  
10595 C CG  . LEU H 79  ? 1.697 1.717 1.440 -0.010 0.080  -0.180 79  LEU LLL CG  
10596 C CD1 . LEU H 79  ? 1.708 1.743 1.444 0.020  0.098  -0.174 79  LEU LLL CD1 
10597 C CD2 . LEU H 79  ? 1.635 1.694 1.412 -0.030 0.078  -0.158 79  LEU LLL CD2 
10598 N N   . THR H 80  ? 1.862 1.769 1.496 0.049  0.083  -0.245 80  THR LLL N   
10599 C CA  . THR H 80  ? 1.889 1.796 1.471 0.070  0.083  -0.270 80  THR LLL CA  
10600 C C   . THR H 80  ? 1.838 1.829 1.423 0.085  0.101  -0.250 80  THR LLL C   
10601 O O   . THR H 80  ? 1.775 1.802 1.382 0.105  0.120  -0.230 80  THR LLL O   
10602 C CB  . THR H 80  ? 1.986 1.826 1.522 0.106  0.088  -0.297 80  THR LLL CB  
10603 O OG1 . THR H 80  ? 2.032 1.800 1.584 0.086  0.076  -0.300 80  THR LLL OG1 
10604 C CG2 . THR H 80  ? 2.074 1.885 1.543 0.121  0.080  -0.333 80  THR LLL CG2 
10605 N N   . ILE H 81  ? 1.863 1.885 1.429 0.075  0.093  -0.253 81  ILE LLL N   
10606 C CA  . ILE H 81  ? 1.849 1.948 1.412 0.085  0.108  -0.231 81  ILE LLL CA  
10607 C C   . ILE H 81  ? 1.920 2.020 1.418 0.118  0.116  -0.255 81  ILE LLL C   
10608 O O   . ILE H 81  ? 1.947 2.056 1.414 0.107  0.104  -0.262 81  ILE LLL O   
10609 C CB  . ILE H 81  ? 1.803 1.935 1.391 0.050  0.094  -0.211 81  ILE LLL CB  
10610 C CG1 . ILE H 81  ? 1.755 1.869 1.395 0.020  0.082  -0.198 81  ILE LLL CG1 
10611 C CG2 . ILE H 81  ? 1.772 1.978 1.369 0.053  0.111  -0.180 81  ILE LLL CG2 
10612 C CD1 . ILE H 81  ? 1.719 1.859 1.381 -0.008 0.069  -0.180 81  ILE LLL CD1 
10613 N N   . SER H 82  ? 1.976 2.067 1.449 0.159  0.136  -0.268 82  SER LLL N   
10614 C CA  . SER H 82  ? 2.072 2.174 1.477 0.200  0.150  -0.289 82  SER LLL CA  
10615 C C   . SER H 82  ? 2.034 2.231 1.446 0.195  0.164  -0.256 82  SER LLL C   
10616 O O   . SER H 82  ? 2.004 2.256 1.477 0.175  0.171  -0.218 82  SER LLL O   
10617 C CB  . SER H 82  ? 2.140 2.228 1.526 0.252  0.173  -0.301 82  SER LLL CB  
10618 O OG  . SER H 82  ? 2.109 2.287 1.539 0.268  0.201  -0.264 82  SER LLL OG  
10619 N N   . SER H 83  ? 2.060 2.271 1.410 0.210  0.165  -0.270 83  SER LLL N   
10620 C CA  . SER H 83  ? 2.015 2.316 1.362 0.210  0.182  -0.237 83  SER LLL CA  
10621 C C   . SER H 83  ? 1.896 2.224 1.300 0.160  0.166  -0.200 83  SER LLL C   
10622 O O   . SER H 83  ? 1.815 2.206 1.269 0.150  0.182  -0.159 83  SER LLL O   
10623 C CB  . SER H 83  ? 2.029 2.406 1.392 0.244  0.220  -0.211 83  SER LLL CB  
10624 O OG  . SER H 83  ? 2.138 2.491 1.445 0.299  0.237  -0.246 83  SER LLL OG  
10625 N N   . LEU H 84  ? 1.894 2.175 1.291 0.130  0.135  -0.213 84  LEU LLL N   
10626 C CA  . LEU H 84  ? 1.850 2.149 1.298 0.088  0.119  -0.181 84  LEU LLL CA  
10627 C C   . LEU H 84  ? 1.852 2.225 1.299 0.086  0.135  -0.141 84  LEU LLL C   
10628 O O   . LEU H 84  ? 1.957 2.359 1.347 0.112  0.148  -0.145 84  LEU LLL O   
10629 C CB  . LEU H 84  ? 1.866 2.119 1.298 0.065  0.085  -0.203 84  LEU LLL CB  
10630 C CG  . LEU H 84  ? 1.794 2.057 1.277 0.030  0.068  -0.174 84  LEU LLL CG  
10631 C CD1 . LEU H 84  ? 1.732 1.977 1.280 0.014  0.070  -0.164 84  LEU LLL CD1 
10632 C CD2 . LEU H 84  ? 1.813 2.047 1.278 0.013  0.035  -0.193 84  LEU LLL CD2 
10633 N N   . GLN H 85  ? 1.792 2.190 1.296 0.057  0.133  -0.104 85  GLN LLL N   
10634 C CA  . GLN H 85  ? 1.809 2.271 1.321 0.048  0.147  -0.058 85  GLN LLL CA  
10635 C C   . GLN H 85  ? 1.804 2.249 1.338 0.014  0.124  -0.036 85  GLN LLL C   
10636 O O   . GLN H 85  ? 1.743 2.138 1.296 0.000  0.101  -0.054 85  GLN LLL O   
10637 C CB  . GLN H 85  ? 1.773 2.282 1.336 0.045  0.170  -0.030 85  GLN LLL CB  
10638 C CG  . GLN H 85  ? 1.806 2.353 1.347 0.085  0.198  -0.041 85  GLN LLL CG  
10639 C CD  . GLN H 85  ? 1.854 2.477 1.366 0.099  0.222  -0.012 85  GLN LLL CD  
10640 O OE1 . GLN H 85  ? 1.892 2.511 1.348 0.105  0.217  -0.016 85  GLN LLL OE1 
10641 N NE2 . GLN H 85  ? 1.837 2.534 1.389 0.102  0.248  0.022  85  GLN LLL NE2 
10642 N N   . ALA H 86  ? 1.851 2.339 1.380 0.005  0.131  0.004  86  ALA LLL N   
10643 C CA  . ALA H 86  ? 1.835 2.311 1.385 -0.023 0.113  0.036  86  ALA LLL CA  
10644 C C   . ALA H 86  ? 1.767 2.198 1.375 -0.045 0.098  0.031  86  ALA LLL C   
10645 O O   . ALA H 86  ? 1.696 2.086 1.305 -0.049 0.076  0.012  86  ALA LLL O   
10646 C CB  . ALA H 86  ? 1.847 2.376 1.405 -0.034 0.131  0.087  86  ALA LLL CB  
10647 N N   . GLU H 87  ? 1.759 2.205 1.410 -0.056 0.110  0.047  87  GLU LLL N   
10648 C CA  . GLU H 87  ? 1.745 2.154 1.445 -0.080 0.097  0.053  87  GLU LLL CA  
10649 C C   . GLU H 87  ? 1.695 2.064 1.407 -0.072 0.089  0.014  87  GLU LLL C   
10650 O O   . GLU H 87  ? 1.644 1.985 1.391 -0.086 0.081  0.015  87  GLU LLL O   
10651 C CB  . GLU H 87  ? 1.767 2.210 1.505 -0.098 0.109  0.083  87  GLU LLL CB  
10652 C CG  . GLU H 87  ? 1.776 2.270 1.520 -0.080 0.132  0.077  87  GLU LLL CG  
10653 C CD  . GLU H 87  ? 1.775 2.300 1.569 -0.101 0.137  0.100  87  GLU LLL CD  
10654 O OE1 . GLU H 87  ? 1.796 2.288 1.618 -0.129 0.119  0.112  87  GLU LLL OE1 
10655 O OE2 . GLU H 87  ? 1.757 2.342 1.561 -0.086 0.157  0.106  87  GLU LLL OE2 
10656 N N   . ASP H 88  ? 1.695 2.056 1.376 -0.051 0.090  -0.018 88  ASP LLL N   
10657 C CA  . ASP H 88  ? 1.676 1.995 1.367 -0.045 0.083  -0.052 88  ASP LLL CA  
10658 C C   . ASP H 88  ? 1.649 1.934 1.342 -0.055 0.060  -0.062 88  ASP LLL C   
10659 O O   . ASP H 88  ? 1.593 1.846 1.304 -0.057 0.053  -0.082 88  ASP LLL O   
10660 C CB  . ASP H 88  ? 1.732 2.049 1.388 -0.020 0.092  -0.081 88  ASP LLL CB  
10661 C CG  . ASP H 88  ? 1.758 2.110 1.420 -0.002 0.116  -0.075 88  ASP LLL CG  
10662 O OD1 . ASP H 88  ? 1.722 2.083 1.425 -0.012 0.120  -0.060 88  ASP LLL OD1 
10663 O OD2 . ASP H 88  ? 1.858 2.230 1.481 0.024  0.130  -0.085 88  ASP LLL OD2 
10664 N N   . VAL H 89  ? 1.665 1.959 1.341 -0.060 0.049  -0.047 89  VAL LLL N   
10665 C CA  . VAL H 89  ? 1.653 1.927 1.338 -0.067 0.026  -0.051 89  VAL LLL CA  
10666 C C   . VAL H 89  ? 1.634 1.886 1.365 -0.078 0.023  -0.042 89  VAL LLL C   
10667 O O   . VAL H 89  ? 1.670 1.923 1.414 -0.085 0.029  -0.017 89  VAL LLL O   
10668 C CB  . VAL H 89  ? 1.684 1.978 1.344 -0.067 0.015  -0.028 89  VAL LLL CB  
10669 C CG1 . VAL H 89  ? 1.673 1.954 1.350 -0.071 -0.008 -0.027 89  VAL LLL CG1 
10670 C CG2 . VAL H 89  ? 1.749 2.066 1.354 -0.053 0.016  -0.039 89  VAL LLL CG2 
10671 N N   . ALA H 90  ? 1.601 1.833 1.353 -0.080 0.015  -0.061 90  ALA LLL N   
10672 C CA  . ALA H 90  ? 1.546 1.758 1.336 -0.085 0.014  -0.056 90  ALA LLL CA  
10673 C C   . ALA H 90  ? 1.510 1.711 1.319 -0.086 0.008  -0.076 90  ALA LLL C   
10674 O O   . ALA H 90  ? 1.505 1.709 1.299 -0.087 0.001  -0.095 90  ALA LLL O   
10675 C CB  . ALA H 90  ? 1.542 1.747 1.343 -0.087 0.029  -0.051 90  ALA LLL CB  
10676 N N   . VAL H 91  ? 1.491 1.681 1.330 -0.086 0.010  -0.073 91  VAL LLL N   
10677 C CA  . VAL H 91  ? 1.454 1.639 1.319 -0.090 0.010  -0.086 91  VAL LLL CA  
10678 C C   . VAL H 91  ? 1.421 1.588 1.285 -0.089 0.026  -0.094 91  VAL LLL C   
10679 O O   . VAL H 91  ? 1.413 1.574 1.271 -0.086 0.035  -0.086 91  VAL LLL O   
10680 C CB  . VAL H 91  ? 1.454 1.642 1.349 -0.084 0.010  -0.075 91  VAL LLL CB  
10681 C CG1 . VAL H 91  ? 1.453 1.655 1.378 -0.090 0.008  -0.081 91  VAL LLL CG1 
10682 C CG2 . VAL H 91  ? 1.464 1.662 1.357 -0.076 -0.002 -0.059 91  VAL LLL CG2 
10683 N N   . TYR H 92  ? 1.396 1.553 1.264 -0.094 0.026  -0.108 92  TYR LLL N   
10684 C CA  . TYR H 92  ? 1.399 1.535 1.263 -0.091 0.039  -0.115 92  TYR LLL CA  
10685 C C   . TYR H 92  ? 1.399 1.526 1.291 -0.097 0.042  -0.113 92  TYR LLL C   
10686 O O   . TYR H 92  ? 1.414 1.544 1.321 -0.110 0.032  -0.118 92  TYR LLL O   
10687 C CB  . TYR H 92  ? 1.440 1.561 1.275 -0.087 0.038  -0.132 92  TYR LLL CB  
10688 C CG  . TYR H 92  ? 1.436 1.575 1.244 -0.076 0.043  -0.129 92  TYR LLL CG  
10689 C CD1 . TYR H 92  ? 1.460 1.617 1.250 -0.078 0.033  -0.127 92  TYR LLL CD1 
10690 C CD2 . TYR H 92  ? 1.445 1.589 1.248 -0.065 0.058  -0.124 92  TYR LLL CD2 
10691 C CE1 . TYR H 92  ? 1.492 1.671 1.258 -0.069 0.041  -0.119 92  TYR LLL CE1 
10692 C CE2 . TYR H 92  ? 1.467 1.639 1.252 -0.057 0.065  -0.116 92  TYR LLL CE2 
10693 C CZ  . TYR H 92  ? 1.483 1.672 1.249 -0.059 0.057  -0.113 92  TYR LLL CZ  
10694 O OH  . TYR H 92  ? 1.480 1.701 1.229 -0.052 0.067  -0.100 92  TYR LLL OH  
10695 N N   . TYR H 93  ? 1.381 1.502 1.280 -0.091 0.055  -0.105 93  TYR LLL N   
10696 C CA  . TYR H 93  ? 1.357 1.474 1.278 -0.094 0.063  -0.099 93  TYR LLL CA  
10697 C C   . TYR H 93  ? 1.354 1.446 1.262 -0.088 0.074  -0.101 93  TYR LLL C   
10698 O O   . TYR H 93  ? 1.314 1.404 1.204 -0.077 0.077  -0.101 93  TYR LLL O   
10699 C CB  . TYR H 93  ? 1.330 1.462 1.261 -0.085 0.070  -0.088 93  TYR LLL CB  
10700 C CG  . TYR H 93  ? 1.318 1.469 1.258 -0.082 0.061  -0.084 93  TYR LLL CG  
10701 C CD1 . TYR H 93  ? 1.331 1.476 1.252 -0.077 0.055  -0.083 93  TYR LLL CD1 
10702 C CD2 . TYR H 93  ? 1.327 1.503 1.296 -0.084 0.059  -0.078 93  TYR LLL CD2 
10703 C CE1 . TYR H 93  ? 1.352 1.508 1.278 -0.072 0.046  -0.077 93  TYR LLL CE1 
10704 C CE2 . TYR H 93  ? 1.349 1.544 1.326 -0.076 0.050  -0.072 93  TYR LLL CE2 
10705 C CZ  . TYR H 93  ? 1.366 1.545 1.318 -0.068 0.044  -0.072 93  TYR LLL CZ  
10706 O OH  . TYR H 93  ? 1.379 1.568 1.335 -0.058 0.034  -0.064 93  TYR LLL OH  
10707 N N   . CYS H 94  ? 1.402 1.477 1.322 -0.097 0.077  -0.098 94  CYS LLL N   
10708 C CA  . CYS H 94  ? 1.457 1.506 1.368 -0.089 0.088  -0.092 94  CYS LLL CA  
10709 C C   . CYS H 94  ? 1.458 1.523 1.384 -0.088 0.101  -0.074 94  CYS LLL C   
10710 O O   . CYS H 94  ? 1.457 1.545 1.408 -0.097 0.101  -0.067 94  CYS LLL O   
10711 C CB  . CYS H 94  ? 1.527 1.537 1.437 -0.100 0.085  -0.098 94  CYS LLL CB  
10712 S SG  . CYS H 94  ? 1.579 1.595 1.527 -0.130 0.079  -0.088 94  CYS LLL SG  
10713 N N   . GLN H 95  ? 1.466 1.525 1.377 -0.073 0.110  -0.066 95  GLN LLL N   
10714 C CA  . GLN H 95  ? 1.459 1.531 1.370 -0.066 0.123  -0.051 95  GLN LLL CA  
10715 C C   . GLN H 95  ? 1.489 1.537 1.389 -0.059 0.132  -0.038 95  GLN LLL C   
10716 O O   . GLN H 95  ? 1.524 1.556 1.407 -0.048 0.127  -0.043 95  GLN LLL O   
10717 C CB  . GLN H 95  ? 1.441 1.528 1.333 -0.052 0.120  -0.056 95  GLN LLL CB  
10718 C CG  . GLN H 95  ? 1.473 1.570 1.353 -0.040 0.132  -0.045 95  GLN LLL CG  
10719 C CD  . GLN H 95  ? 1.513 1.606 1.363 -0.027 0.127  -0.049 95  GLN LLL CD  
10720 O OE1 . GLN H 95  ? 1.544 1.641 1.378 -0.021 0.121  -0.057 95  GLN LLL OE1 
10721 N NE2 . GLN H 95  ? 1.539 1.623 1.379 -0.022 0.127  -0.042 95  GLN LLL NE2 
10722 N N   . GLN H 96  ? 1.490 1.540 1.400 -0.064 0.144  -0.018 96  GLN LLL N   
10723 C CA  . GLN H 96  ? 1.508 1.536 1.402 -0.055 0.154  0.001  96  GLN LLL CA  
10724 C C   . GLN H 96  ? 1.486 1.538 1.355 -0.035 0.161  0.007  96  GLN LLL C   
10725 O O   . GLN H 96  ? 1.472 1.552 1.342 -0.032 0.165  0.003  96  GLN LLL O   
10726 C CB  . GLN H 96  ? 1.547 1.565 1.465 -0.074 0.165  0.023  96  GLN LLL CB  
10727 C CG  . GLN H 96  ? 1.560 1.622 1.492 -0.076 0.181  0.041  96  GLN LLL CG  
10728 C CD  . GLN H 96  ? 1.583 1.657 1.485 -0.054 0.196  0.059  96  GLN LLL CD  
10729 O OE1 . GLN H 96  ? 1.615 1.661 1.492 -0.043 0.196  0.068  96  GLN LLL OE1 
10730 N NE2 . GLN H 96  ? 1.578 1.694 1.478 -0.043 0.209  0.064  96  GLN LLL NE2 
10731 N N   . TYR H 97  ? 1.498 1.538 1.342 -0.019 0.161  0.014  97  TYR LLL N   
10732 C CA  . TYR H 97  ? 1.535 1.594 1.348 0.000  0.164  0.022  97  TYR LLL CA  
10733 C C   . TYR H 97  ? 1.606 1.647 1.402 0.012  0.172  0.047  97  TYR LLL C   
10734 O O   . TYR H 97  ? 1.651 1.701 1.419 0.030  0.165  0.050  97  TYR LLL O   
10735 C CB  . TYR H 97  ? 1.507 1.580 1.306 0.008  0.146  0.000  97  TYR LLL CB  
10736 C CG  . TYR H 97  ? 1.502 1.566 1.304 0.012  0.135  -0.004 97  TYR LLL CG  
10737 C CD1 . TYR H 97  ? 1.471 1.526 1.293 0.003  0.130  -0.018 97  TYR LLL CD1 
10738 C CD2 . TYR H 97  ? 1.540 1.612 1.323 0.030  0.130  0.005  97  TYR LLL CD2 
10739 C CE1 . TYR H 97  ? 1.462 1.515 1.284 0.013  0.124  -0.022 97  TYR LLL CE1 
10740 C CE2 . TYR H 97  ? 1.547 1.621 1.337 0.040  0.122  0.003  97  TYR LLL CE2 
10741 C CZ  . TYR H 97  ? 1.488 1.553 1.297 0.032  0.121  -0.011 97  TYR LLL CZ  
10742 O OH  . TYR H 97  ? 1.466 1.540 1.280 0.048  0.117  -0.013 97  TYR LLL OH  
10743 N N   . TYR H 98  ? 1.639 1.656 1.453 0.000  0.183  0.068  98  TYR LLL N   
10744 C CA  . TYR H 98  ? 1.681 1.677 1.479 0.009  0.195  0.101  98  TYR LLL CA  
10745 C C   . TYR H 98  ? 1.703 1.735 1.476 0.020  0.209  0.118  98  TYR LLL C   
10746 O O   . TYR H 98  ? 1.776 1.808 1.516 0.039  0.212  0.138  98  TYR LLL O   
10747 C CB  . TYR H 98  ? 1.700 1.655 1.524 -0.014 0.202  0.120  98  TYR LLL CB  
10748 C CG  . TYR H 98  ? 1.757 1.682 1.565 -0.006 0.214  0.158  98  TYR LLL CG  
10749 C CD1 . TYR H 98  ? 1.796 1.677 1.585 0.013  0.206  0.164  98  TYR LLL CD1 
10750 C CD2 . TYR H 98  ? 1.792 1.737 1.602 -0.015 0.234  0.193  98  TYR LLL CD2 
10751 C CE1 . TYR H 98  ? 1.871 1.720 1.642 0.023  0.215  0.202  98  TYR LLL CE1 
10752 C CE2 . TYR H 98  ? 1.858 1.776 1.651 -0.009 0.246  0.233  98  TYR LLL CE2 
10753 C CZ  . TYR H 98  ? 1.899 1.765 1.672 0.010  0.235  0.238  98  TYR LLL CZ  
10754 O OH  . TYR H 98  ? 1.959 1.791 1.711 0.018  0.246  0.281  98  TYR LLL OH  
10755 N N   . SER H 99  ? 1.675 1.740 1.461 0.011  0.218  0.112  99  SER LLL N   
10756 C CA  . SER H 99  ? 1.718 1.820 1.478 0.026  0.236  0.126  99  SER LLL CA  
10757 C C   . SER H 99  ? 1.676 1.810 1.451 0.023  0.240  0.105  99  SER LLL C   
10758 O O   . SER H 99  ? 1.645 1.776 1.461 0.003  0.233  0.093  99  SER LLL O   
10759 C CB  . SER H 99  ? 1.804 1.908 1.571 0.019  0.260  0.169  99  SER LLL CB  
10760 O OG  . SER H 99  ? 1.807 1.924 1.626 -0.009 0.271  0.178  99  SER LLL OG  
10761 N N   . THR H 100 ? 1.707 1.869 1.445 0.046  0.249  0.101  100 THR LLL N   
10762 C CA  . THR H 100 ? 1.713 1.907 1.460 0.053  0.259  0.087  100 THR LLL CA  
10763 C C   . THR H 100 ? 1.733 1.961 1.524 0.040  0.285  0.119  100 THR LLL C   
10764 O O   . THR H 100 ? 1.825 2.059 1.617 0.035  0.302  0.154  100 THR LLL O   
10765 C CB  . THR H 100 ? 1.756 1.959 1.441 0.086  0.261  0.072  100 THR LLL CB  
10766 O OG1 . THR H 100 ? 1.835 2.058 1.489 0.101  0.284  0.103  100 THR LLL OG1 
10767 C CG2 . THR H 100 ? 1.747 1.918 1.394 0.091  0.231  0.043  100 THR LLL CG2 
10768 N N   . PRO H 101 ? 1.694 1.950 1.528 0.032  0.288  0.111  101 PRO LLL N   
10769 C CA  . PRO H 101 ? 1.659 1.904 1.490 0.039  0.268  0.074  101 PRO LLL CA  
10770 C C   . PRO H 101 ? 1.644 1.854 1.502 0.012  0.242  0.059  101 PRO LLL C   
10771 O O   . PRO H 101 ? 1.636 1.847 1.537 -0.014 0.242  0.074  101 PRO LLL O   
10772 C CB  . PRO H 101 ? 1.651 1.948 1.523 0.043  0.284  0.080  101 PRO LLL CB  
10773 C CG  . PRO H 101 ? 1.666 1.993 1.590 0.015  0.301  0.119  101 PRO LLL CG  
10774 C CD  . PRO H 101 ? 1.701 2.002 1.591 0.014  0.309  0.141  101 PRO LLL CD  
10775 N N   . TYR H 102 ? 1.659 1.837 1.488 0.019  0.220  0.032  102 TYR LLL N   
10776 C CA  . TYR H 102 ? 1.631 1.785 1.482 -0.001 0.197  0.015  102 TYR LLL CA  
10777 C C   . TYR H 102 ? 1.593 1.769 1.490 -0.015 0.198  0.014  102 TYR LLL C   
10778 O O   . TYR H 102 ? 1.611 1.818 1.512 0.000  0.209  0.014  102 TYR LLL O   
10779 C CB  . TYR H 102 ? 1.654 1.789 1.474 0.009  0.177  -0.012 102 TYR LLL CB  
10780 C CG  . TYR H 102 ? 1.710 1.830 1.490 0.019  0.169  -0.014 102 TYR LLL CG  
10781 C CD1 . TYR H 102 ? 1.744 1.866 1.504 0.029  0.180  0.006  102 TYR LLL CD1 
10782 C CD2 . TYR H 102 ? 1.763 1.870 1.526 0.019  0.147  -0.035 102 TYR LLL CD2 
10783 C CE1 . TYR H 102 ? 1.780 1.894 1.503 0.040  0.168  0.004  102 TYR LLL CE1 
10784 C CE2 . TYR H 102 ? 1.801 1.905 1.534 0.026  0.135  -0.037 102 TYR LLL CE2 
10785 C CZ  . TYR H 102 ? 1.802 1.910 1.514 0.038  0.145  -0.019 102 TYR LLL CZ  
10786 O OH  . TYR H 102 ? 1.813 1.923 1.496 0.045  0.129  -0.021 102 TYR LLL OH  
10787 N N   . THR H 103 ? 1.554 1.718 1.483 -0.039 0.187  0.013  103 THR LLL N   
10788 C CA  . THR H 103 ? 1.531 1.720 1.504 -0.056 0.182  0.012  103 THR LLL CA  
10789 C C   . THR H 103 ? 1.495 1.657 1.470 -0.069 0.158  -0.008 103 THR LLL C   
10790 O O   . THR H 103 ? 1.505 1.631 1.465 -0.075 0.152  -0.012 103 THR LLL O   
10791 C CB  . THR H 103 ? 1.570 1.781 1.584 -0.077 0.193  0.038  103 THR LLL CB  
10792 O OG1 . THR H 103 ? 1.579 1.747 1.585 -0.093 0.191  0.046  103 THR LLL OG1 
10793 C CG2 . THR H 103 ? 1.614 1.870 1.632 -0.062 0.220  0.062  103 THR LLL CG2 
10794 N N   . PHE H 104 ? 1.449 1.630 1.441 -0.071 0.148  -0.019 104 PHE LLL N   
10795 C CA  . PHE H 104 ? 1.417 1.581 1.408 -0.083 0.127  -0.037 104 PHE LLL CA  
10796 C C   . PHE H 104 ? 1.417 1.596 1.446 -0.108 0.118  -0.033 104 PHE LLL C   
10797 O O   . PHE H 104 ? 1.459 1.675 1.524 -0.115 0.127  -0.015 104 PHE LLL O   
10798 C CB  . PHE H 104 ? 1.401 1.573 1.381 -0.069 0.118  -0.048 104 PHE LLL CB  
10799 C CG  . PHE H 104 ? 1.400 1.551 1.342 -0.051 0.119  -0.056 104 PHE LLL CG  
10800 C CD1 . PHE H 104 ? 1.405 1.533 1.326 -0.054 0.108  -0.066 104 PHE LLL CD1 
10801 C CD2 . PHE H 104 ? 1.431 1.589 1.360 -0.031 0.129  -0.054 104 PHE LLL CD2 
10802 C CE1 . PHE H 104 ? 1.420 1.535 1.314 -0.044 0.105  -0.072 104 PHE LLL CE1 
10803 C CE2 . PHE H 104 ? 1.442 1.575 1.334 -0.019 0.125  -0.064 104 PHE LLL CE2 
10804 C CZ  . PHE H 104 ? 1.429 1.543 1.307 -0.028 0.111  -0.072 104 PHE LLL CZ  
10805 N N   . GLY H 105 ? 1.373 1.530 1.395 -0.120 0.099  -0.049 105 GLY LLL N   
10806 C CA  . GLY H 105 ? 1.372 1.541 1.420 -0.144 0.081  -0.053 105 GLY LLL CA  
10807 C C   . GLY H 105 ? 1.342 1.551 1.403 -0.136 0.071  -0.055 105 GLY LLL C   
10808 O O   . GLY H 105 ? 1.314 1.525 1.356 -0.113 0.078  -0.056 105 GLY LLL O   
10809 N N   . GLN H 106 ? 1.356 1.591 1.445 -0.155 0.053  -0.056 106 GLN LLL N   
10810 C CA  . GLN H 106 ? 1.363 1.644 1.471 -0.147 0.042  -0.053 106 GLN LLL CA  
10811 C C   . GLN H 106 ? 1.328 1.589 1.397 -0.135 0.029  -0.068 106 GLN LLL C   
10812 O O   . GLN H 106 ? 1.301 1.591 1.378 -0.123 0.020  -0.064 106 GLN LLL O   
10813 C CB  . GLN H 106 ? 1.437 1.762 1.594 -0.174 0.025  -0.045 106 GLN LLL CB  
10814 C CG  . GLN H 106 ? 1.513 1.809 1.653 -0.201 -0.003 -0.065 106 GLN LLL CG  
10815 C CD  . GLN H 106 ? 1.569 1.811 1.697 -0.223 -0.002 -0.073 106 GLN LLL CD  
10816 O OE1 . GLN H 106 ? 1.603 1.839 1.749 -0.227 0.017  -0.057 106 GLN LLL OE1 
10817 N NE2 . GLN H 106 ? 1.600 1.797 1.693 -0.234 -0.022 -0.098 106 GLN LLL NE2 
10818 N N   . GLY H 107 ? 1.325 1.539 1.354 -0.137 0.028  -0.084 107 GLY LLL N   
10819 C CA  . GLY H 107 ? 1.349 1.548 1.340 -0.126 0.019  -0.094 107 GLY LLL CA  
10820 C C   . GLY H 107 ? 1.415 1.609 1.391 -0.141 -0.002 -0.110 107 GLY LLL C   
10821 O O   . GLY H 107 ? 1.434 1.645 1.437 -0.161 -0.017 -0.111 107 GLY LLL O   
10822 N N   . THR H 108 ? 1.464 1.639 1.398 -0.133 -0.005 -0.121 108 THR LLL N   
10823 C CA  . THR H 108 ? 1.499 1.667 1.401 -0.139 -0.024 -0.139 108 THR LLL CA  
10824 C C   . THR H 108 ? 1.523 1.707 1.396 -0.124 -0.026 -0.133 108 THR LLL C   
10825 O O   . THR H 108 ? 1.535 1.708 1.388 -0.111 -0.010 -0.129 108 THR LLL O   
10826 C CB  . THR H 108 ? 1.514 1.635 1.385 -0.140 -0.020 -0.159 108 THR LLL CB  
10827 O OG1 . THR H 108 ? 1.497 1.598 1.397 -0.156 -0.018 -0.159 108 THR LLL OG1 
10828 C CG2 . THR H 108 ? 1.577 1.685 1.407 -0.144 -0.040 -0.183 108 THR LLL CG2 
10829 N N   . LYS H 109 ? 1.533 1.747 1.407 -0.127 -0.046 -0.129 109 LYS LLL N   
10830 C CA  . LYS H 109 ? 1.529 1.757 1.369 -0.114 -0.049 -0.120 109 LYS LLL CA  
10831 C C   . LYS H 109 ? 1.567 1.776 1.354 -0.112 -0.053 -0.142 109 LYS LLL C   
10832 O O   . LYS H 109 ? 1.576 1.772 1.354 -0.124 -0.069 -0.164 109 LYS LLL O   
10833 C CB  . LYS H 109 ? 1.521 1.786 1.377 -0.113 -0.070 -0.105 109 LYS LLL CB  
10834 C CG  . LYS H 109 ? 1.526 1.802 1.352 -0.098 -0.071 -0.087 109 LYS LLL CG  
10835 C CD  . LYS H 109 ? 1.504 1.767 1.340 -0.086 -0.052 -0.065 109 LYS LLL CD  
10836 C CE  . LYS H 109 ? 1.514 1.774 1.312 -0.079 -0.048 -0.048 109 LYS LLL CE  
10837 N NZ  . LYS H 109 ? 1.469 1.705 1.275 -0.076 -0.031 -0.032 109 LYS LLL NZ  
10838 N N   . VAL H 110 ? 1.572 1.779 1.328 -0.097 -0.036 -0.135 110 VAL LLL N   
10839 C CA  . VAL H 110 ? 1.641 1.842 1.342 -0.087 -0.033 -0.152 110 VAL LLL CA  
10840 C C   . VAL H 110 ? 1.678 1.910 1.351 -0.078 -0.034 -0.131 110 VAL LLL C   
10841 O O   . VAL H 110 ? 1.630 1.873 1.318 -0.074 -0.019 -0.105 110 VAL LLL O   
10842 C CB  . VAL H 110 ? 1.633 1.812 1.325 -0.076 -0.009 -0.159 110 VAL LLL CB  
10843 C CG1 . VAL H 110 ? 1.685 1.869 1.322 -0.057 0.000  -0.170 110 VAL LLL CG1 
10844 C CG2 . VAL H 110 ? 1.636 1.777 1.347 -0.083 -0.010 -0.179 110 VAL LLL CG2 
10845 N N   . GLU H 111 ? 1.749 1.992 1.380 -0.076 -0.053 -0.143 111 GLU LLL N   
10846 C CA  . GLU H 111 ? 1.779 2.054 1.376 -0.066 -0.057 -0.121 111 GLU LLL CA  
10847 C C   . GLU H 111 ? 1.816 2.093 1.343 -0.051 -0.054 -0.142 111 GLU LLL C   
10848 O O   . GLU H 111 ? 1.830 2.077 1.337 -0.050 -0.059 -0.179 111 GLU LLL O   
10849 C CB  . GLU H 111 ? 1.818 2.114 1.434 -0.075 -0.085 -0.111 111 GLU LLL CB  
10850 C CG  . GLU H 111 ? 1.796 2.092 1.474 -0.080 -0.083 -0.088 111 GLU LLL CG  
10851 C CD  . GLU H 111 ? 1.836 2.159 1.530 -0.077 -0.103 -0.062 111 GLU LLL CD  
10852 O OE1 . GLU H 111 ? 1.833 2.178 1.533 -0.083 -0.130 -0.073 111 GLU LLL OE1 
10853 O OE2 . GLU H 111 ? 1.857 2.179 1.559 -0.068 -0.093 -0.032 111 GLU LLL OE2 
10854 N N   . ILE H 112 ? 1.827 2.135 1.318 -0.039 -0.044 -0.119 112 ILE LLL N   
10855 C CA  . ILE H 112 ? 1.895 2.217 1.314 -0.018 -0.033 -0.131 112 ILE LLL CA  
10856 C C   . ILE H 112 ? 1.953 2.280 1.318 -0.016 -0.064 -0.150 112 ILE LLL C   
10857 O O   . ILE H 112 ? 1.951 2.309 1.312 -0.018 -0.078 -0.121 112 ILE LLL O   
10858 C CB  . ILE H 112 ? 1.918 2.281 1.327 -0.009 -0.007 -0.088 112 ILE LLL CB  
10859 C CG1 . ILE H 112 ? 1.878 2.241 1.337 -0.012 0.022  -0.072 112 ILE LLL CG1 
10860 C CG2 . ILE H 112 ? 2.002 2.392 1.332 0.016  0.004  -0.095 112 ILE LLL CG2 
10861 C CD1 . ILE H 112 ? 1.903 2.261 1.344 0.006  0.044  -0.098 112 ILE LLL CD1 
10862 N N   . LYS H 113 ? 2.020 2.316 1.342 -0.010 -0.077 -0.196 113 LYS LLL N   
10863 C CA  . LYS H 113 ? 2.122 2.421 1.379 -0.008 -0.109 -0.221 113 LYS LLL CA  
10864 C C   . LYS H 113 ? 2.180 2.515 1.362 0.021  -0.091 -0.207 113 LYS LLL C   
10865 O O   . LYS H 113 ? 2.197 2.533 1.351 0.044  -0.058 -0.212 113 LYS LLL O   
10866 C CB  . LYS H 113 ? 2.197 2.439 1.422 -0.011 -0.128 -0.277 113 LYS LLL CB  
10867 C CG  . LYS H 113 ? 2.296 2.533 1.469 -0.019 -0.173 -0.307 113 LYS LLL CG  
10868 C CD  . LYS H 113 ? 2.367 2.535 1.525 -0.033 -0.196 -0.360 113 LYS LLL CD  
10869 C CE  . LYS H 113 ? 2.451 2.570 1.540 -0.002 -0.173 -0.397 113 LYS LLL CE  
10870 N NZ  . LYS H 113 ? 2.463 2.508 1.580 -0.015 -0.176 -0.428 113 LYS LLL NZ  
10871 N N   . ARG H 114 ? 2.210 2.582 1.363 0.020  -0.112 -0.185 114 ARG LLL N   
10872 C CA  . ARG H 114 ? 2.253 2.670 1.338 0.045  -0.095 -0.159 114 ARG LLL CA  
10873 C C   . ARG H 114 ? 2.294 2.721 1.302 0.051  -0.132 -0.181 114 ARG LLL C   
10874 O O   . ARG H 114 ? 2.273 2.679 1.296 0.031  -0.174 -0.209 114 ARG LLL O   
10875 C CB  . ARG H 114 ? 2.227 2.683 1.360 0.038  -0.079 -0.095 114 ARG LLL CB  
10876 C CG  . ARG H 114 ? 2.207 2.666 1.386 0.018  -0.113 -0.074 114 ARG LLL CG  
10877 C CD  . ARG H 114 ? 2.216 2.712 1.389 0.023  -0.106 -0.015 114 ARG LLL CD  
10878 N NE  . ARG H 114 ? 2.306 2.836 1.389 0.042  -0.115 -0.011 114 ARG LLL NE  
10879 C CZ  . ARG H 114 ? 2.349 2.915 1.402 0.052  -0.104 0.041  114 ARG LLL CZ  
10880 N NH1 . ARG H 114 ? 2.302 2.868 1.411 0.041  -0.085 0.092  114 ARG LLL NH1 
10881 N NH2 . ARG H 114 ? 2.450 3.047 1.413 0.072  -0.113 0.041  114 ARG LLL NH2 
10882 N N   . THR H 115 ? 1.904 2.896 1.352 0.226  -0.005 -0.267 115 THR LLL N   
10883 C CA  . THR H 115 ? 1.934 2.972 1.337 0.242  -0.001 -0.281 115 THR LLL CA  
10884 C C   . THR H 115 ? 1.874 2.849 1.276 0.187  -0.006 -0.249 115 THR LLL C   
10885 O O   . THR H 115 ? 1.775 2.744 1.221 0.139  0.008  -0.198 115 THR LLL O   
10886 C CB  . THR H 115 ? 1.954 3.157 1.364 0.266  0.036  -0.255 115 THR LLL CB  
10887 O OG1 . THR H 115 ? 1.901 3.147 1.362 0.211  0.061  -0.182 115 THR LLL OG1 
10888 C CG2 . THR H 115 ? 1.977 3.254 1.412 0.312  0.047  -0.271 115 THR LLL CG2 
10889 N N   . VAL H 116 ? 1.911 2.838 1.271 0.196  -0.029 -0.283 116 VAL LLL N   
10890 C CA  . VAL H 116 ? 1.884 2.762 1.245 0.150  -0.035 -0.257 116 VAL LLL CA  
10891 C C   . VAL H 116 ? 1.841 2.823 1.219 0.123  -0.001 -0.196 116 VAL LLL C   
10892 O O   . VAL H 116 ? 1.902 3.002 1.275 0.153  0.023  -0.186 116 VAL LLL O   
10893 C CB  . VAL H 116 ? 1.944 2.786 1.261 0.174  -0.069 -0.307 116 VAL LLL CB  
10894 C CG1 . VAL H 116 ? 1.914 2.690 1.247 0.124  -0.081 -0.283 116 VAL LLL CG1 
10895 C CG2 . VAL H 116 ? 2.003 2.762 1.306 0.212  -0.107 -0.372 116 VAL LLL CG2 
10896 N N   . ALA H 117 ? 1.785 2.730 1.189 0.072  0.001  -0.154 117 ALA LLL N   
10897 C CA  . ALA H 117 ? 1.766 2.795 1.198 0.042  0.028  -0.091 117 ALA LLL CA  
10898 C C   . ALA H 117 ? 1.769 2.737 1.210 -0.003 0.017  -0.066 117 ALA LLL C   
10899 O O   . ALA H 117 ? 1.772 2.645 1.238 -0.031 0.007  -0.064 117 ALA LLL O   
10900 C CB  . ALA H 117 ? 1.714 2.774 1.206 0.023  0.046  -0.052 117 ALA LLL CB  
10901 N N   . ALA H 118 ? 1.806 2.833 1.225 -0.004 0.022  -0.046 118 ALA LLL N   
10902 C CA  . ALA H 118 ? 1.781 2.764 1.208 -0.040 0.009  -0.025 118 ALA LLL CA  
10903 C C   . ALA H 118 ? 1.711 2.703 1.197 -0.086 0.025  0.039  118 ALA LLL C   
10904 O O   . ALA H 118 ? 1.676 2.738 1.194 -0.089 0.046  0.075  118 ALA LLL O   
10905 C CB  . ALA H 118 ? 1.846 2.891 1.221 -0.017 0.003  -0.030 118 ALA LLL CB  
10906 N N   . PRO H 119 ? 1.691 2.613 1.199 -0.122 0.013  0.054  119 PRO LLL N   
10907 C CA  . PRO H 119 ? 1.657 2.568 1.222 -0.161 0.019  0.104  119 PRO LLL CA  
10908 C C   . PRO H 119 ? 1.653 2.626 1.234 -0.181 0.024  0.156  119 PRO LLL C   
10909 O O   . PRO H 119 ? 1.657 2.633 1.204 -0.176 0.014  0.149  119 PRO LLL O   
10910 C CB  . PRO H 119 ? 1.649 2.450 1.223 -0.178 0.004  0.086  119 PRO LLL CB  
10911 C CG  . PRO H 119 ? 1.691 2.471 1.228 -0.163 -0.012 0.049  119 PRO LLL CG  
10912 C CD  . PRO H 119 ? 1.723 2.572 1.213 -0.124 -0.011 0.021  119 PRO LLL CD  
10913 N N   . SER H 120 ? 1.658 2.672 1.294 -0.203 0.034  0.208  120 SER LLL N   
10914 C CA  . SER H 120 ? 1.679 2.743 1.348 -0.229 0.037  0.271  120 SER LLL CA  
10915 C C   . SER H 120 ? 1.645 2.623 1.343 -0.259 0.016  0.278  120 SER LLL C   
10916 O O   . SER H 120 ? 1.640 2.574 1.391 -0.279 0.007  0.291  120 SER LLL O   
10917 C CB  . SER H 120 ? 1.685 2.822 1.421 -0.242 0.051  0.325  120 SER LLL CB  
10918 O OG  . SER H 120 ? 1.719 2.948 1.434 -0.210 0.075  0.321  120 SER LLL OG  
10919 N N   . VAL H 121 ? 1.633 2.590 1.299 -0.259 0.005  0.268  121 VAL LLL N   
10920 C CA  . VAL H 121 ? 1.590 2.471 1.283 -0.282 -0.014 0.271  121 VAL LLL CA  
10921 C C   . VAL H 121 ? 1.596 2.505 1.337 -0.308 -0.020 0.332  121 VAL LLL C   
10922 O O   . VAL H 121 ? 1.627 2.617 1.359 -0.307 -0.012 0.372  121 VAL LLL O   
10923 C CB  . VAL H 121 ? 1.596 2.444 1.251 -0.272 -0.027 0.236  121 VAL LLL CB  
10924 C CG1 . VAL H 121 ? 1.571 2.357 1.264 -0.294 -0.041 0.245  121 VAL LLL CG1 
10925 C CG2 . VAL H 121 ? 1.611 2.421 1.231 -0.249 -0.027 0.178  121 VAL LLL CG2 
10926 N N   . PHE H 122 ? 1.598 2.442 1.387 -0.328 -0.035 0.339  122 PHE LLL N   
10927 C CA  . PHE H 122 ? 1.636 2.477 1.482 -0.354 -0.052 0.390  122 PHE LLL CA  
10928 C C   . PHE H 122 ? 1.626 2.384 1.484 -0.357 -0.069 0.366  122 PHE LLL C   
10929 O O   . PHE H 122 ? 1.628 2.329 1.473 -0.345 -0.065 0.324  122 PHE LLL O   
10930 C CB  . PHE H 122 ? 1.655 2.509 1.567 -0.369 -0.057 0.421  122 PHE LLL CB  
10931 C CG  . PHE H 122 ? 1.704 2.659 1.634 -0.374 -0.040 0.474  122 PHE LLL CG  
10932 C CD1 . PHE H 122 ? 1.774 2.781 1.729 -0.390 -0.042 0.538  122 PHE LLL CD1 
10933 C CD2 . PHE H 122 ? 1.698 2.703 1.624 -0.361 -0.020 0.464  122 PHE LLL CD2 
10934 C CE1 . PHE H 122 ? 1.822 2.932 1.795 -0.393 -0.020 0.597  122 PHE LLL CE1 
10935 C CE2 . PHE H 122 ? 1.766 2.877 1.715 -0.362 0.001  0.519  122 PHE LLL CE2 
10936 C CZ  . PHE H 122 ? 1.822 2.988 1.794 -0.378 0.003  0.587  122 PHE LLL CZ  
10937 N N   . ILE H 123 ? 1.646 2.400 1.525 -0.370 -0.085 0.394  123 ILE LLL N   
10938 C CA  . ILE H 123 ? 1.657 2.340 1.560 -0.371 -0.101 0.377  123 ILE LLL CA  
10939 C C   . ILE H 123 ? 1.660 2.324 1.629 -0.388 -0.126 0.416  123 ILE LLL C   
10940 O O   . ILE H 123 ? 1.663 2.377 1.661 -0.405 -0.133 0.468  123 ILE LLL O   
10941 C CB  . ILE H 123 ? 1.679 2.366 1.558 -0.366 -0.104 0.366  123 ILE LLL CB  
10942 C CG1 . ILE H 123 ? 1.684 2.306 1.582 -0.360 -0.108 0.337  123 ILE LLL CG1 
10943 C CG2 . ILE H 123 ? 1.712 2.444 1.603 -0.378 -0.120 0.415  123 ILE LLL CG2 
10944 C CD1 . ILE H 123 ? 1.688 2.314 1.576 -0.356 -0.111 0.319  123 ILE LLL CD1 
10945 N N   . PHE H 124 ? 1.668 2.264 1.661 -0.380 -0.141 0.392  124 PHE LLL N   
10946 C CA  . PHE H 124 ? 1.693 2.250 1.749 -0.388 -0.174 0.413  124 PHE LLL CA  
10947 C C   . PHE H 124 ? 1.700 2.209 1.768 -0.375 -0.188 0.396  124 PHE LLL C   
10948 O O   . PHE H 124 ? 1.700 2.173 1.739 -0.352 -0.174 0.354  124 PHE LLL O   
10949 C CB  . PHE H 124 ? 1.710 2.229 1.784 -0.379 -0.185 0.390  124 PHE LLL CB  
10950 C CG  . PHE H 124 ? 1.731 2.302 1.816 -0.393 -0.176 0.412  124 PHE LLL CG  
10951 C CD1 . PHE H 124 ? 1.764 2.384 1.909 -0.420 -0.190 0.473  124 PHE LLL CD1 
10952 C CD2 . PHE H 124 ? 1.739 2.317 1.781 -0.377 -0.154 0.378  124 PHE LLL CD2 
10953 C CE1 . PHE H 124 ? 1.788 2.470 1.954 -0.432 -0.177 0.499  124 PHE LLL CE1 
10954 C CE2 . PHE H 124 ? 1.748 2.382 1.807 -0.387 -0.145 0.398  124 PHE LLL CE2 
10955 C CZ  . PHE H 124 ? 1.769 2.459 1.892 -0.414 -0.155 0.459  124 PHE LLL CZ  
10956 N N   . PRO H 125 ? 1.710 2.219 1.823 -0.388 -0.215 0.433  125 PRO LLL N   
10957 C CA  . PRO H 125 ? 1.708 2.172 1.840 -0.372 -0.231 0.416  125 PRO LLL CA  
10958 C C   . PRO H 125 ? 1.715 2.112 1.870 -0.350 -0.253 0.385  125 PRO LLL C   
10959 O O   . PRO H 125 ? 1.716 2.101 1.874 -0.351 -0.259 0.377  125 PRO LLL O   
10960 C CB  . PRO H 125 ? 1.729 2.212 1.905 -0.393 -0.260 0.470  125 PRO LLL CB  
10961 C CG  . PRO H 125 ? 1.747 2.262 1.952 -0.419 -0.268 0.518  125 PRO LLL CG  
10962 C CD  . PRO H 125 ? 1.723 2.275 1.875 -0.416 -0.231 0.496  125 PRO LLL CD  
10963 N N   . PRO H 126 ? 1.725 2.080 1.894 -0.325 -0.266 0.362  126 PRO LLL N   
10964 C CA  . PRO H 126 ? 1.754 2.044 1.946 -0.297 -0.299 0.333  126 PRO LLL CA  
10965 C C   . PRO H 126 ? 1.742 2.010 2.010 -0.319 -0.353 0.370  126 PRO LLL C   
10966 O O   . PRO H 126 ? 1.685 1.987 1.985 -0.349 -0.361 0.420  126 PRO LLL O   
10967 C CB  . PRO H 126 ? 1.793 2.061 1.976 -0.260 -0.290 0.302  126 PRO LLL CB  
10968 C CG  . PRO H 126 ? 1.768 2.085 1.960 -0.282 -0.274 0.331  126 PRO LLL CG  
10969 C CD  . PRO H 126 ? 1.729 2.098 1.894 -0.317 -0.252 0.358  126 PRO LLL CD  
10970 N N   . SER H 127 ? 1.768 1.979 2.065 -0.302 -0.393 0.345  127 SER LLL N   
10971 C CA  . SER H 127 ? 1.799 1.970 2.186 -0.317 -0.458 0.371  127 SER LLL CA  
10972 C C   . SER H 127 ? 1.822 1.950 2.237 -0.293 -0.489 0.361  127 SER LLL C   
10973 O O   . SER H 127 ? 1.801 1.922 2.164 -0.253 -0.463 0.317  127 SER LLL O   
10974 C CB  . SER H 127 ? 1.832 1.951 2.238 -0.300 -0.496 0.335  127 SER LLL CB  
10975 O OG  . SER H 127 ? 1.844 1.920 2.184 -0.243 -0.488 0.265  127 SER LLL OG  
10976 N N   . ASP H 128 ? 1.873 1.976 2.373 -0.315 -0.542 0.403  128 ASP LLL N   
10977 C CA  . ASP H 128 ? 1.955 2.002 2.496 -0.287 -0.587 0.388  128 ASP LLL CA  
10978 C C   . ASP H 128 ? 2.016 1.989 2.542 -0.230 -0.620 0.310  128 ASP LLL C   
10979 O O   . ASP H 128 ? 2.040 1.993 2.532 -0.179 -0.614 0.265  128 ASP LLL O   
10980 C CB  . ASP H 128 ? 2.005 2.034 2.648 -0.326 -0.643 0.454  128 ASP LLL CB  
10981 C CG  . ASP H 128 ? 1.995 2.063 2.645 -0.343 -0.631 0.506  128 ASP LLL CG  
10982 O OD1 . ASP H 128 ? 1.957 2.076 2.537 -0.334 -0.577 0.493  128 ASP LLL OD1 
10983 O OD2 . ASP H 128 ? 2.027 2.072 2.760 -0.367 -0.679 0.560  128 ASP LLL OD2 
10984 N N   . GLU H 129 ? 2.051 1.990 2.601 -0.233 -0.654 0.296  129 GLU LLL N   
10985 C CA  . GLU H 129 ? 2.127 1.996 2.653 -0.174 -0.692 0.217  129 GLU LLL CA  
10986 C C   . GLU H 129 ? 2.111 2.000 2.525 -0.118 -0.631 0.163  129 GLU LLL C   
10987 O O   . GLU H 129 ? 2.176 2.023 2.572 -0.059 -0.651 0.114  129 GLU LLL O   
10988 C CB  . GLU H 129 ? 2.155 2.014 2.702 -0.194 -0.714 0.215  129 GLU LLL CB  
10989 C CG  . GLU H 129 ? 2.273 2.048 2.814 -0.137 -0.777 0.137  129 GLU LLL CG  
10990 C CD  . GLU H 129 ? 2.316 2.080 2.897 -0.159 -0.811 0.136  129 GLU LLL CD  
10991 O OE1 . GLU H 129 ? 2.301 2.109 2.960 -0.226 -0.808 0.207  129 GLU LLL OE1 
10992 O OE2 . GLU H 129 ? 2.387 2.104 2.920 -0.106 -0.839 0.065  129 GLU LLL OE2 
10993 N N   . GLN H 130 ? 2.033 1.987 2.380 -0.135 -0.560 0.175  130 GLN LLL N   
10994 C CA  . GLN H 130 ? 2.013 1.991 2.263 -0.089 -0.497 0.135  130 GLN LLL CA  
10995 C C   . GLN H 130 ? 2.041 2.037 2.286 -0.064 -0.473 0.134  130 GLN LLL C   
10996 O O   . GLN H 130 ? 2.106 2.093 2.299 -0.002 -0.452 0.088  130 GLN LLL O   
10997 C CB  . GLN H 130 ? 1.904 1.947 2.104 -0.123 -0.432 0.160  130 GLN LLL CB  
10998 C CG  . GLN H 130 ? 1.862 1.930 1.978 -0.082 -0.368 0.131  130 GLN LLL CG  
10999 C CD  . GLN H 130 ? 1.774 1.889 1.843 -0.110 -0.314 0.147  130 GLN LLL CD  
11000 O OE1 . GLN H 130 ? 1.705 1.848 1.800 -0.160 -0.317 0.182  130 GLN LLL OE1 
11001 N NE2 . GLN H 130 ? 1.740 1.868 1.743 -0.075 -0.265 0.125  130 GLN LLL NE2 
11002 N N   . LEU H 131 ? 2.026 2.054 2.324 -0.108 -0.472 0.185  131 LEU LLL N   
11003 C CA  . LEU H 131 ? 2.032 2.091 2.335 -0.092 -0.447 0.190  131 LEU LLL CA  
11004 C C   . LEU H 131 ? 2.106 2.111 2.424 -0.027 -0.486 0.143  131 LEU LLL C   
11005 O O   . LEU H 131 ? 2.116 2.146 2.400 0.019  -0.447 0.117  131 LEU LLL O   
11006 C CB  . LEU H 131 ? 2.016 2.106 2.377 -0.147 -0.460 0.251  131 LEU LLL CB  
11007 C CG  . LEU H 131 ? 1.959 2.118 2.291 -0.196 -0.410 0.291  131 LEU LLL CG  
11008 C CD1 . LEU H 131 ? 1.960 2.144 2.342 -0.245 -0.434 0.353  131 LEU LLL CD1 
11009 C CD2 . LEU H 131 ? 1.928 2.134 2.218 -0.178 -0.351 0.275  131 LEU LLL CD2 
11010 N N   . LYS H 132 ? 2.163 2.099 2.533 -0.022 -0.562 0.133  132 LYS LLL N   
11011 C CA  . LYS H 132 ? 2.268 2.140 2.658 0.044  -0.615 0.081  132 LYS LLL CA  
11012 C C   . LYS H 132 ? 2.330 2.191 2.631 0.121  -0.590 0.012  132 LYS LLL C   
11013 O O   . LYS H 132 ? 2.392 2.237 2.681 0.190  -0.599 -0.031 132 LYS LLL O   
11014 C CB  . LYS H 132 ? 2.336 2.128 2.805 0.028  -0.708 0.084  132 LYS LLL CB  
11015 C CG  . LYS H 132 ? 2.326 2.122 2.889 -0.036 -0.741 0.156  132 LYS LLL CG  
11016 C CD  . LYS H 132 ? 2.399 2.116 3.057 -0.055 -0.833 0.166  132 LYS LLL CD  
11017 C CE  . LYS H 132 ? 2.386 2.102 3.052 -0.096 -0.840 0.182  132 LYS LLL CE  
11018 N NZ  . LYS H 132 ? 2.467 2.096 3.232 -0.101 -0.938 0.176  132 LYS LLL NZ  
11019 N N   . SER H 133 ? 2.331 2.203 2.571 0.115  -0.561 0.003  133 SER LLL N   
11020 C CA  . SER H 133 ? 2.396 2.258 2.541 0.188  -0.537 -0.056 133 SER LLL CA  
11021 C C   . SER H 133 ? 2.360 2.287 2.453 0.230  -0.458 -0.058 133 SER LLL C   
11022 O O   . SER H 133 ? 2.452 2.366 2.488 0.314  -0.453 -0.110 133 SER LLL O   
11023 C CB  . SER H 133 ? 2.395 2.260 2.493 0.164  -0.521 -0.055 133 SER LLL CB  
11024 O OG  . SER H 133 ? 2.337 2.276 2.391 0.134  -0.437 -0.019 133 SER LLL OG  
11025 N N   . GLY H 134 ? 2.223 2.219 2.337 0.175  -0.401 -0.004 134 GLY LLL N   
11026 C CA  . GLY H 134 ? 2.160 2.226 2.251 0.200  -0.326 0.006  134 GLY LLL CA  
11027 C C   . GLY H 134 ? 2.053 2.179 2.132 0.142  -0.263 0.051  134 GLY LLL C   
11028 O O   . GLY H 134 ? 2.009 2.191 2.128 0.119  -0.227 0.083  134 GLY LLL O   
11029 N N   . THR H 135 ? 2.035 2.150 2.066 0.122  -0.254 0.050  135 THR LLL N   
11030 C CA  . THR H 135 ? 1.953 2.116 1.971 0.068  -0.203 0.088  135 THR LLL CA  
11031 C C   . THR H 135 ? 1.863 2.028 1.934 -0.006 -0.236 0.124  135 THR LLL C   
11032 O O   . THR H 135 ? 1.856 1.982 1.972 -0.016 -0.296 0.124  135 THR LLL O   
11033 C CB  . THR H 135 ? 1.995 2.147 1.933 0.089  -0.177 0.069  135 THR LLL CB  
11034 O OG1 . THR H 135 ? 2.063 2.153 1.984 0.105  -0.236 0.036  135 THR LLL OG1 
11035 C CG2 . THR H 135 ? 2.037 2.213 1.917 0.154  -0.121 0.054  135 THR LLL CG2 
11036 N N   . ALA H 136 ? 1.775 1.985 1.840 -0.053 -0.198 0.156  136 ALA LLL N   
11037 C CA  . ALA H 136 ? 1.703 1.931 1.797 -0.117 -0.215 0.192  136 ALA LLL CA  
11038 C C   . ALA H 136 ? 1.658 1.913 1.706 -0.139 -0.174 0.198  136 ALA LLL C   
11039 O O   . ALA H 136 ? 1.650 1.938 1.684 -0.136 -0.128 0.201  136 ALA LLL O   
11040 C CB  . ALA H 136 ? 1.666 1.930 1.814 -0.144 -0.217 0.223  136 ALA LLL CB  
11041 N N   . SER H 137 ? 1.653 1.895 1.686 -0.159 -0.192 0.199  137 SER LLL N   
11042 C CA  . SER H 137 ? 1.635 1.898 1.623 -0.174 -0.159 0.199  137 SER LLL CA  
11043 C C   . SER H 137 ? 1.592 1.895 1.603 -0.226 -0.165 0.234  137 SER LLL C   
11044 O O   . SER H 137 ? 1.593 1.893 1.642 -0.248 -0.202 0.255  137 SER LLL O   
11045 C CB  . SER H 137 ? 1.673 1.896 1.622 -0.148 -0.172 0.171  137 SER LLL CB  
11046 O OG  . SER H 137 ? 1.699 1.897 1.603 -0.092 -0.154 0.139  137 SER LLL OG  
11047 N N   . VAL H 138 ? 1.558 1.899 1.548 -0.242 -0.130 0.242  138 VAL LLL N   
11048 C CA  . VAL H 138 ? 1.541 1.927 1.532 -0.281 -0.129 0.267  138 VAL LLL CA  
11049 C C   . VAL H 138 ? 1.537 1.928 1.483 -0.280 -0.108 0.252  138 VAL LLL C   
11050 O O   . VAL H 138 ? 1.513 1.897 1.428 -0.265 -0.078 0.233  138 VAL LLL O   
11051 C CB  . VAL H 138 ? 1.539 1.960 1.541 -0.294 -0.116 0.277  138 VAL LLL CB  
11052 C CG1 . VAL H 138 ? 1.540 2.008 1.533 -0.323 -0.122 0.299  138 VAL LLL CG1 
11053 C CG2 . VAL H 138 ? 1.566 1.980 1.614 -0.287 -0.134 0.286  138 VAL LLL CG2 
11054 N N   . VAL H 139 ? 1.569 1.974 1.519 -0.296 -0.124 0.264  139 VAL LLL N   
11055 C CA  . VAL H 139 ? 1.576 1.990 1.490 -0.293 -0.109 0.250  139 VAL LLL CA  
11056 C C   . VAL H 139 ? 1.554 2.027 1.457 -0.315 -0.096 0.268  139 VAL LLL C   
11057 O O   . VAL H 139 ? 1.510 2.021 1.440 -0.337 -0.110 0.301  139 VAL LLL O   
11058 C CB  . VAL H 139 ? 1.607 2.002 1.541 -0.290 -0.136 0.249  139 VAL LLL CB  
11059 C CG1 . VAL H 139 ? 1.605 1.997 1.499 -0.276 -0.121 0.225  139 VAL LLL CG1 
11060 C CG2 . VAL H 139 ? 1.643 1.980 1.597 -0.266 -0.165 0.232  139 VAL LLL CG2 
11061 N N   . CYS H 140 ? 1.576 2.054 1.436 -0.306 -0.073 0.245  140 CYS LLL N   
11062 C CA  . CYS H 140 ? 1.588 2.118 1.425 -0.315 -0.062 0.248  140 CYS LLL CA  
11063 C C   . CYS H 140 ? 1.598 2.131 1.412 -0.304 -0.054 0.232  140 CYS LLL C   
11064 O O   . CYS H 140 ? 1.661 2.145 1.457 -0.285 -0.047 0.207  140 CYS LLL O   
11065 C CB  . CYS H 140 ? 1.616 2.144 1.432 -0.311 -0.049 0.229  140 CYS LLL CB  
11066 S SG  . CYS H 140 ? 1.684 2.274 1.466 -0.314 -0.048 0.226  140 CYS LLL SG  
11067 N N   . LEU H 141 ? 1.569 2.160 1.383 -0.313 -0.053 0.248  141 LEU LLL N   
11068 C CA  . LEU H 141 ? 1.552 2.160 1.363 -0.304 -0.049 0.240  141 LEU LLL CA  
11069 C C   . LEU H 141 ? 1.550 2.213 1.323 -0.295 -0.032 0.230  141 LEU LLL C   
11070 O O   . LEU H 141 ? 1.584 2.312 1.358 -0.304 -0.029 0.256  141 LEU LLL O   
11071 C CB  . LEU H 141 ? 1.553 2.189 1.424 -0.323 -0.068 0.278  141 LEU LLL CB  
11072 C CG  . LEU H 141 ? 1.563 2.249 1.454 -0.322 -0.066 0.286  141 LEU LLL CG  
11073 C CD1 . LEU H 141 ? 1.572 2.209 1.439 -0.298 -0.067 0.244  141 LEU LLL CD1 
11074 C CD2 . LEU H 141 ? 1.568 2.283 1.541 -0.346 -0.088 0.333  141 LEU LLL CD2 
11075 N N   . LEU H 142 ? 1.563 2.202 1.301 -0.275 -0.022 0.194  142 LEU LLL N   
11076 C CA  . LEU H 142 ? 1.601 2.284 1.303 -0.257 -0.011 0.174  142 LEU LLL CA  
11077 C C   . LEU H 142 ? 1.627 2.340 1.346 -0.249 -0.009 0.176  142 LEU LLL C   
11078 O O   . LEU H 142 ? 1.681 2.340 1.391 -0.235 -0.012 0.151  142 LEU LLL O   
11079 C CB  . LEU H 142 ? 1.609 2.236 1.273 -0.240 -0.007 0.133  142 LEU LLL CB  
11080 C CG  . LEU H 142 ? 1.616 2.225 1.274 -0.246 -0.012 0.126  142 LEU LLL CG  
11081 C CD1 . LEU H 142 ? 1.605 2.180 1.297 -0.265 -0.016 0.149  142 LEU LLL CD1 
11082 C CD2 . LEU H 142 ? 1.633 2.192 1.270 -0.231 -0.012 0.090  142 LEU LLL CD2 
11083 N N   . ASN H 143 ? 1.614 2.412 1.359 -0.255 -0.003 0.207  143 ASN LLL N   
11084 C CA  . ASN H 143 ? 1.596 2.432 1.381 -0.252 -0.003 0.218  143 ASN LLL CA  
11085 C C   . ASN H 143 ? 1.592 2.480 1.342 -0.222 0.014  0.192  143 ASN LLL C   
11086 O O   . ASN H 143 ? 1.592 2.533 1.304 -0.209 0.027  0.190  143 ASN LLL O   
11087 C CB  . ASN H 143 ? 1.597 2.501 1.454 -0.279 -0.006 0.278  143 ASN LLL CB  
11088 C CG  . ASN H 143 ? 1.605 2.513 1.532 -0.287 -0.023 0.290  143 ASN LLL CG  
11089 O OD1 . ASN H 143 ? 1.586 2.415 1.516 -0.282 -0.045 0.261  143 ASN LLL OD1 
11090 N ND2 . ASN H 143 ? 1.643 2.648 1.630 -0.296 -0.012 0.333  143 ASN LLL ND2 
11091 N N   . ASN H 144 ? 1.590 2.462 1.351 -0.207 0.009  0.170  144 ASN LLL N   
11092 C CA  . ASN H 144 ? 1.605 2.534 1.352 -0.177 0.022  0.149  144 ASN LLL CA  
11093 C C   . ASN H 144 ? 1.609 2.534 1.283 -0.148 0.031  0.110  144 ASN LLL C   
11094 O O   . ASN H 144 ? 1.635 2.634 1.290 -0.141 0.045  0.123  144 ASN LLL O   
11095 C CB  . ASN H 144 ? 1.623 2.674 1.429 -0.183 0.037  0.196  144 ASN LLL CB  
11096 C CG  . ASN H 144 ? 1.617 2.671 1.515 -0.214 0.020  0.236  144 ASN LLL CG  
11097 O OD1 . ASN H 144 ? 1.650 2.769 1.608 -0.240 0.024  0.293  144 ASN LLL OD1 
11098 N ND2 . ASN H 144 ? 1.608 2.591 1.520 -0.209 -0.005 0.208  144 ASN LLL ND2 
11099 N N   . PHE H 145 ? 1.602 2.444 1.237 -0.131 0.021  0.065  145 PHE LLL N   
11100 C CA  . PHE H 145 ? 1.642 2.464 1.220 -0.103 0.019  0.021  145 PHE LLL CA  
11101 C C   . PHE H 145 ? 1.652 2.404 1.210 -0.078 0.009  -0.019 145 PHE LLL C   
11102 O O   . PHE H 145 ? 1.665 2.366 1.241 -0.085 0.003  -0.013 145 PHE LLL O   
11103 C CB  . PHE H 145 ? 1.657 2.431 1.218 -0.121 0.012  0.021  145 PHE LLL CB  
11104 C CG  . PHE H 145 ? 1.655 2.333 1.229 -0.141 0.004  0.026  145 PHE LLL CG  
11105 C CD1 . PHE H 145 ? 1.621 2.291 1.230 -0.169 0.005  0.062  145 PHE LLL CD1 
11106 C CD2 . PHE H 145 ? 1.687 2.284 1.240 -0.130 -0.003 -0.004 145 PHE LLL CD2 
11107 C CE1 . PHE H 145 ? 1.603 2.192 1.216 -0.179 0.000  0.064  145 PHE LLL CE1 
11108 C CE2 . PHE H 145 ? 1.668 2.189 1.231 -0.143 -0.003 0.007  145 PHE LLL CE2 
11109 C CZ  . PHE H 145 ? 1.630 2.150 1.217 -0.165 0.000  0.039  145 PHE LLL CZ  
11110 N N   . TYR H 146 ? 1.684 2.432 1.204 -0.047 0.003  -0.061 146 TYR LLL N   
11111 C CA  . TYR H 146 ? 1.727 2.399 1.225 -0.021 -0.012 -0.101 146 TYR LLL CA  
11112 C C   . TYR H 146 ? 1.792 2.435 1.258 -0.004 -0.028 -0.140 146 TYR LLL C   
11113 O O   . TYR H 146 ? 1.864 2.577 1.308 0.015  -0.028 -0.154 146 TYR LLL O   
11114 C CB  . TYR H 146 ? 1.746 2.463 1.248 0.012  -0.009 -0.118 146 TYR LLL CB  
11115 C CG  . TYR H 146 ? 1.797 2.429 1.282 0.036  -0.027 -0.152 146 TYR LLL CG  
11116 C CD1 . TYR H 146 ? 1.795 2.358 1.289 0.026  -0.030 -0.136 146 TYR LLL CD1 
11117 C CD2 . TYR H 146 ? 1.850 2.463 1.306 0.072  -0.043 -0.199 146 TYR LLL CD2 
11118 C CE1 . TYR H 146 ? 1.837 2.318 1.311 0.049  -0.045 -0.159 146 TYR LLL CE1 
11119 C CE2 . TYR H 146 ? 1.899 2.425 1.345 0.093  -0.061 -0.223 146 TYR LLL CE2 
11120 C CZ  . TYR H 146 ? 1.893 2.355 1.348 0.079  -0.060 -0.199 146 TYR LLL CZ  
11121 O OH  . TYR H 146 ? 1.940 2.318 1.382 0.101  -0.077 -0.215 146 TYR LLL OH  
11122 N N   . PRO H 147 ? 1.839 2.381 1.302 -0.006 -0.046 -0.158 147 PRO LLL N   
11123 C CA  . PRO H 147 ? 1.856 2.319 1.333 -0.016 -0.044 -0.141 147 PRO LLL CA  
11124 C C   . PRO H 147 ? 1.851 2.282 1.348 -0.054 -0.031 -0.099 147 PRO LLL C   
11125 O O   . PRO H 147 ? 1.828 2.305 1.336 -0.076 -0.024 -0.080 147 PRO LLL O   
11126 C CB  . PRO H 147 ? 1.913 2.294 1.384 0.001  -0.067 -0.174 147 PRO LLL CB  
11127 C CG  . PRO H 147 ? 1.930 2.322 1.402 -0.005 -0.084 -0.193 147 PRO LLL CG  
11128 C CD  . PRO H 147 ? 1.900 2.403 1.353 0.005  -0.072 -0.194 147 PRO LLL CD  
11129 N N   . ARG H 148 ? 1.884 2.241 1.382 -0.057 -0.028 -0.085 148 ARG LLL N   
11130 C CA  . ARG H 148 ? 1.888 2.211 1.397 -0.081 -0.014 -0.048 148 ARG LLL CA  
11131 C C   . ARG H 148 ? 1.901 2.206 1.433 -0.106 -0.013 -0.038 148 ARG LLL C   
11132 O O   . ARG H 148 ? 1.841 2.170 1.388 -0.128 -0.005 -0.014 148 ARG LLL O   
11133 C CB  . ARG H 148 ? 1.946 2.196 1.438 -0.065 -0.009 -0.039 148 ARG LLL CB  
11134 C CG  . ARG H 148 ? 1.958 2.190 1.443 -0.071 0.004  -0.009 148 ARG LLL CG  
11135 C CD  . ARG H 148 ? 2.033 2.216 1.483 -0.041 0.003  -0.008 148 ARG LLL CD  
11136 N NE  . ARG H 148 ? 2.045 2.235 1.482 -0.033 0.001  0.001  148 ARG LLL NE  
11137 C CZ  . ARG H 148 ? 2.085 2.252 1.512 -0.036 0.012  0.022  148 ARG LLL CZ  
11138 N NH1 . ARG H 148 ? 2.109 2.253 1.546 -0.049 0.032  0.044  148 ARG LLL NH1 
11139 N NH2 . ARG H 148 ? 2.093 2.263 1.508 -0.022 0.000  0.020  148 ARG LLL NH2 
11140 N N   . GLU H 149 ? 1.989 2.251 1.530 -0.101 -0.027 -0.056 149 GLU LLL N   
11141 C CA  . GLU H 149 ? 2.023 2.254 1.603 -0.124 -0.032 -0.045 149 GLU LLL CA  
11142 C C   . GLU H 149 ? 1.959 2.252 1.545 -0.139 -0.041 -0.052 149 GLU LLL C   
11143 O O   . GLU H 149 ? 1.979 2.295 1.557 -0.125 -0.065 -0.088 149 GLU LLL O   
11144 C CB  . GLU H 149 ? 2.145 2.316 1.746 -0.115 -0.056 -0.067 149 GLU LLL CB  
11145 C CG  . GLU H 149 ? 2.247 2.360 1.832 -0.094 -0.051 -0.062 149 GLU LLL CG  
11146 C CD  . GLU H 149 ? 2.326 2.456 1.873 -0.059 -0.068 -0.103 149 GLU LLL CD  
11147 O OE1 . GLU H 149 ? 2.424 2.546 1.978 -0.044 -0.098 -0.144 149 GLU LLL OE1 
11148 O OE2 . GLU H 149 ? 2.328 2.483 1.844 -0.045 -0.053 -0.097 149 GLU LLL OE2 
11149 N N   . ALA H 150 ? 1.879 2.198 1.477 -0.160 -0.025 -0.020 150 ALA LLL N   
11150 C CA  . ALA H 150 ? 1.835 2.208 1.445 -0.177 -0.031 -0.014 150 ALA LLL CA  
11151 C C   . ALA H 150 ? 1.794 2.137 1.447 -0.202 -0.025 0.014  150 ALA LLL C   
11152 O O   . ALA H 150 ? 1.774 2.095 1.433 -0.206 -0.003 0.042  150 ALA LLL O   
11153 C CB  . ALA H 150 ? 1.806 2.241 1.397 -0.178 -0.020 0.002  150 ALA LLL CB  
11154 N N   . LYS H 151 ? 1.799 2.144 1.482 -0.214 -0.046 0.004  151 LYS LLL N   
11155 C CA  . LYS H 151 ? 1.785 2.115 1.523 -0.238 -0.043 0.030  151 LYS LLL CA  
11156 C C   . LYS H 151 ? 1.708 2.093 1.442 -0.250 -0.041 0.047  151 LYS LLL C   
11157 O O   . LYS H 151 ? 1.710 2.141 1.420 -0.245 -0.061 0.031  151 LYS LLL O   
11158 C CB  . LYS H 151 ? 1.858 2.164 1.644 -0.246 -0.075 0.008  151 LYS LLL CB  
11159 C CG  . LYS H 151 ? 1.871 2.174 1.728 -0.271 -0.077 0.034  151 LYS LLL CG  
11160 C CD  . LYS H 151 ? 1.936 2.202 1.862 -0.282 -0.110 0.018  151 LYS LLL CD  
11161 C CE  . LYS H 151 ? 1.937 2.207 1.949 -0.308 -0.108 0.050  151 LYS LLL CE  
11162 N NZ  . LYS H 151 ? 1.989 2.220 2.092 -0.322 -0.142 0.041  151 LYS LLL NZ  
11163 N N   . VAL H 152 ? 1.643 2.021 1.396 -0.260 -0.019 0.080  152 VAL LLL N   
11164 C CA  . VAL H 152 ? 1.591 2.006 1.357 -0.273 -0.021 0.102  152 VAL LLL CA  
11165 C C   . VAL H 152 ? 1.616 2.014 1.443 -0.287 -0.019 0.118  152 VAL LLL C   
11166 O O   . VAL H 152 ? 1.638 1.999 1.487 -0.284 0.004  0.132  152 VAL LLL O   
11167 C CB  . VAL H 152 ? 1.544 1.964 1.290 -0.268 -0.004 0.121  152 VAL LLL CB  
11168 C CG1 . VAL H 152 ? 1.503 1.948 1.272 -0.281 -0.010 0.145  152 VAL LLL CG1 
11169 C CG2 . VAL H 152 ? 1.554 1.999 1.257 -0.256 -0.006 0.109  152 VAL LLL CG2 
11170 N N   . GLN H 153 ? 1.630 2.057 1.484 -0.300 -0.040 0.120  153 GLN LLL N   
11171 C CA  . GLN H 153 ? 1.633 2.056 1.555 -0.314 -0.040 0.139  153 GLN LLL CA  
11172 C C   . GLN H 153 ? 1.582 2.042 1.509 -0.321 -0.051 0.155  153 GLN LLL C   
11173 O O   . GLN H 153 ? 1.592 2.087 1.484 -0.321 -0.073 0.147  153 GLN LLL O   
11174 C CB  . GLN H 153 ? 1.687 2.099 1.664 -0.324 -0.066 0.122  153 GLN LLL CB  
11175 C CG  . GLN H 153 ? 1.707 2.120 1.770 -0.339 -0.061 0.147  153 GLN LLL CG  
11176 C CD  . GLN H 153 ? 1.754 2.137 1.894 -0.350 -0.062 0.151  153 GLN LLL CD  
11177 O OE1 . GLN H 153 ? 1.826 2.184 1.965 -0.349 -0.087 0.124  153 GLN LLL OE1 
11178 N NE2 . GLN H 153 ? 1.734 2.121 1.947 -0.357 -0.035 0.187  153 GLN LLL NE2 
11179 N N   . TRP H 154 ? 1.537 1.993 1.508 -0.324 -0.036 0.179  154 TRP LLL N   
11180 C CA  . TRP H 154 ? 1.514 1.996 1.505 -0.329 -0.049 0.196  154 TRP LLL CA  
11181 C C   . TRP H 154 ? 1.531 2.031 1.583 -0.342 -0.074 0.195  154 TRP LLL C   
11182 O O   . TRP H 154 ? 1.539 2.025 1.649 -0.347 -0.067 0.194  154 TRP LLL O   
11183 C CB  . TRP H 154 ? 1.493 1.959 1.496 -0.317 -0.024 0.215  154 TRP LLL CB  
11184 C CG  . TRP H 154 ? 1.487 1.936 1.434 -0.303 -0.012 0.213  154 TRP LLL CG  
11185 C CD1 . TRP H 154 ? 1.521 1.942 1.436 -0.288 0.011  0.205  154 TRP LLL CD1 
11186 C CD2 . TRP H 154 ? 1.463 1.923 1.387 -0.304 -0.029 0.221  154 TRP LLL CD2 
11187 N NE1 . TRP H 154 ? 1.520 1.933 1.394 -0.278 0.008  0.202  154 TRP LLL NE1 
11188 C CE2 . TRP H 154 ? 1.482 1.919 1.366 -0.290 -0.017 0.213  154 TRP LLL CE2 
11189 C CE3 . TRP H 154 ? 1.474 1.960 1.412 -0.317 -0.054 0.237  154 TRP LLL CE3 
11190 C CZ2 . TRP H 154 ? 1.493 1.933 1.364 -0.290 -0.032 0.220  154 TRP LLL CZ2 
11191 C CZ3 . TRP H 154 ? 1.488 1.976 1.411 -0.318 -0.066 0.250  154 TRP LLL CZ3 
11192 C CH2 . TRP H 154 ? 1.493 1.959 1.389 -0.306 -0.056 0.241  154 TRP LLL CH2 
11193 N N   . LYS H 155 ? 1.538 2.069 1.582 -0.347 -0.104 0.198  155 LYS LLL N   
11194 C CA  . LYS H 155 ? 1.552 2.102 1.655 -0.356 -0.133 0.202  155 LYS LLL CA  
11195 C C   . LYS H 155 ? 1.522 2.084 1.639 -0.354 -0.132 0.229  155 LYS LLL C   
11196 O O   . LYS H 155 ? 1.518 2.084 1.584 -0.351 -0.131 0.241  155 LYS LLL O   
11197 C CB  . LYS H 155 ? 1.612 2.186 1.686 -0.356 -0.176 0.180  155 LYS LLL CB  
11198 C CG  . LYS H 155 ? 1.665 2.226 1.704 -0.350 -0.184 0.146  155 LYS LLL CG  
11199 C CD  . LYS H 155 ? 1.738 2.321 1.754 -0.342 -0.233 0.114  155 LYS LLL CD  
11200 C CE  . LYS H 155 ? 1.788 2.351 1.768 -0.329 -0.243 0.074  155 LYS LLL CE  
11201 N NZ  . LYS H 155 ? 1.867 2.439 1.839 -0.316 -0.301 0.033  155 LYS LLL NZ  
11202 N N   . VAL H 156 ? 1.519 2.086 1.710 -0.355 -0.133 0.240  156 VAL LLL N   
11203 C CA  . VAL H 156 ? 1.516 2.095 1.733 -0.351 -0.143 0.261  156 VAL LLL CA  
11204 C C   . VAL H 156 ? 1.548 2.152 1.825 -0.359 -0.180 0.260  156 VAL LLL C   
11205 O O   . VAL H 156 ? 1.540 2.150 1.896 -0.362 -0.172 0.257  156 VAL LLL O   
11206 C CB  . VAL H 156 ? 1.486 2.047 1.732 -0.334 -0.108 0.272  156 VAL LLL CB  
11207 C CG1 . VAL H 156 ? 1.485 2.055 1.772 -0.325 -0.123 0.288  156 VAL LLL CG1 
11208 C CG2 . VAL H 156 ? 1.472 2.004 1.651 -0.323 -0.084 0.269  156 VAL LLL CG2 
11209 N N   . ASP H 157 ? 1.587 2.211 1.831 -0.361 -0.218 0.264  157 ASP LLL N   
11210 C CA  . ASP H 157 ? 1.634 2.284 1.919 -0.365 -0.263 0.257  157 ASP LLL CA  
11211 C C   . ASP H 157 ? 1.655 2.303 1.949 -0.371 -0.278 0.223  157 ASP LLL C   
11212 O O   . ASP H 157 ? 1.636 2.289 2.021 -0.378 -0.295 0.214  157 ASP LLL O   
11213 C CB  . ASP H 157 ? 1.631 2.290 2.012 -0.363 -0.266 0.271  157 ASP LLL CB  
11214 C CG  . ASP H 157 ? 1.623 2.274 1.998 -0.352 -0.254 0.298  157 ASP LLL CG  
11215 O OD1 . ASP H 157 ? 1.633 2.277 1.938 -0.352 -0.260 0.312  157 ASP LLL OD1 
11216 O OD2 . ASP H 157 ? 1.594 2.248 2.041 -0.343 -0.242 0.306  157 ASP LLL OD2 
11217 N N   . ASN H 158 ? 1.688 2.330 1.901 -0.367 -0.276 0.206  158 ASN LLL N   
11218 C CA  . ASN H 158 ? 1.722 2.354 1.929 -0.366 -0.295 0.167  158 ASN LLL CA  
11219 C C   . ASN H 158 ? 1.688 2.299 2.005 -0.380 -0.285 0.163  158 ASN LLL C   
11220 O O   . ASN H 158 ? 1.713 2.325 2.094 -0.386 -0.328 0.141  158 ASN LLL O   
11221 C CB  . ASN H 158 ? 1.796 2.452 1.968 -0.354 -0.355 0.142  158 ASN LLL CB  
11222 C CG  . ASN H 158 ? 1.833 2.513 1.883 -0.335 -0.355 0.144  158 ASN LLL CG  
11223 O OD1 . ASN H 158 ? 1.802 2.477 1.800 -0.333 -0.318 0.149  158 ASN LLL OD1 
11224 N ND2 . ASN H 158 ? 1.876 2.590 1.884 -0.320 -0.397 0.142  158 ASN LLL ND2 
11225 N N   . ALA H 159 ? 1.626 2.221 1.963 -0.383 -0.232 0.187  159 ALA LLL N   
11226 C CA  . ALA H 159 ? 1.593 2.174 2.023 -0.392 -0.203 0.197  159 ALA LLL CA  
11227 C C   . ALA H 159 ? 1.562 2.117 1.940 -0.384 -0.150 0.208  159 ALA LLL C   
11228 O O   . ALA H 159 ? 1.543 2.099 1.877 -0.372 -0.122 0.225  159 ALA LLL O   
11229 C CB  . ALA H 159 ? 1.570 2.177 2.092 -0.394 -0.193 0.225  159 ALA LLL CB  
11230 N N   . LEU H 160 ? 1.569 2.096 1.953 -0.389 -0.142 0.196  160 LEU LLL N   
11231 C CA  . LEU H 160 ? 1.562 2.061 1.886 -0.378 -0.099 0.202  160 LEU LLL CA  
11232 C C   . LEU H 160 ? 1.535 2.038 1.887 -0.367 -0.047 0.238  160 LEU LLL C   
11233 O O   . LEU H 160 ? 1.558 2.074 2.007 -0.374 -0.032 0.261  160 LEU LLL O   
11234 C CB  . LEU H 160 ? 1.599 2.065 1.948 -0.385 -0.104 0.188  160 LEU LLL CB  
11235 C CG  . LEU H 160 ? 1.637 2.094 1.955 -0.387 -0.159 0.143  160 LEU LLL CG  
11236 C CD1 . LEU H 160 ? 1.677 2.093 2.039 -0.394 -0.169 0.130  160 LEU LLL CD1 
11237 C CD2 . LEU H 160 ? 1.635 2.101 1.832 -0.369 -0.161 0.124  160 LEU LLL CD2 
11238 N N   . GLN H 161 ? 1.513 2.007 1.787 -0.349 -0.023 0.242  161 GLN LLL N   
11239 C CA  . GLN H 161 ? 1.525 2.014 1.796 -0.326 0.027  0.266  161 GLN LLL CA  
11240 C C   . GLN H 161 ? 1.555 2.010 1.784 -0.319 0.054  0.265  161 GLN LLL C   
11241 O O   . GLN H 161 ? 1.533 1.969 1.711 -0.326 0.032  0.241  161 GLN LLL O   
11242 C CB  . GLN H 161 ? 1.518 2.008 1.734 -0.308 0.025  0.264  161 GLN LLL CB  
11243 C CG  . GLN H 161 ? 1.505 2.025 1.769 -0.314 -0.003 0.269  161 GLN LLL CG  
11244 C CD  . GLN H 161 ? 1.504 2.046 1.843 -0.299 0.023  0.291  161 GLN LLL CD  
11245 O OE1 . GLN H 161 ? 1.549 2.094 1.916 -0.288 0.064  0.307  161 GLN LLL OE1 
11246 N NE2 . GLN H 161 ? 1.466 2.029 1.838 -0.295 0.002  0.294  161 GLN LLL NE2 
11247 N N   . SER H 162 ? 1.589 2.041 1.837 -0.300 0.100  0.292  162 SER LLL N   
11248 C CA  . SER H 162 ? 1.612 2.034 1.836 -0.292 0.129  0.303  162 SER LLL CA  
11249 C C   . SER H 162 ? 1.637 2.065 1.849 -0.257 0.184  0.336  162 SER LLL C   
11250 O O   . SER H 162 ? 1.647 2.107 1.943 -0.256 0.211  0.371  162 SER LLL O   
11251 C CB  . SER H 162 ? 1.617 2.033 1.925 -0.320 0.116  0.312  162 SER LLL CB  
11252 O OG  . SER H 162 ? 1.643 2.027 1.939 -0.313 0.144  0.330  162 SER LLL OG  
11253 N N   . GLY H 163 ? 1.649 2.052 1.763 -0.225 0.197  0.324  163 GLY LLL N   
11254 C CA  . GLY H 163 ? 1.680 2.085 1.757 -0.180 0.245  0.347  163 GLY LLL CA  
11255 C C   . GLY H 163 ? 1.684 2.088 1.697 -0.144 0.238  0.324  163 GLY LLL C   
11256 O O   . GLY H 163 ? 1.739 2.137 1.696 -0.097 0.269  0.331  163 GLY LLL O   
11257 N N   . ASN H 164 ? 1.652 2.060 1.673 -0.163 0.195  0.299  164 ASN LLL N   
11258 C CA  . ASN H 164 ? 1.649 2.051 1.630 -0.136 0.175  0.277  164 ASN LLL CA  
11259 C C   . ASN H 164 ? 1.616 1.987 1.540 -0.150 0.135  0.248  164 ASN LLL C   
11260 O O   . ASN H 164 ? 1.606 1.968 1.515 -0.140 0.105  0.231  164 ASN LLL O   
11261 C CB  . ASN H 164 ? 1.639 2.073 1.690 -0.146 0.159  0.282  164 ASN LLL CB  
11262 C CG  . ASN H 164 ? 1.616 2.070 1.733 -0.196 0.134  0.287  164 ASN LLL CG  
11263 O OD1 . ASN H 164 ? 1.615 2.054 1.707 -0.223 0.111  0.274  164 ASN LLL OD1 
11264 N ND2 . ASN H 164 ? 1.607 2.098 1.807 -0.204 0.136  0.303  164 ASN LLL ND2 
11265 N N   . SER H 165 ? 1.593 1.951 1.497 -0.171 0.132  0.244  165 SER LLL N   
11266 C CA  . SER H 165 ? 1.582 1.920 1.434 -0.180 0.103  0.221  165 SER LLL CA  
11267 C C   . SER H 165 ? 1.601 1.907 1.388 -0.148 0.122  0.214  165 SER LLL C   
11268 O O   . SER H 165 ? 1.614 1.915 1.396 -0.126 0.159  0.233  165 SER LLL O   
11269 C CB  . SER H 165 ? 1.550 1.902 1.422 -0.219 0.085  0.217  165 SER LLL CB  
11270 O OG  . SER H 165 ? 1.572 1.909 1.439 -0.220 0.104  0.220  165 SER LLL OG  
11271 N N   . GLN H 166 ? 1.598 1.886 1.339 -0.145 0.097  0.193  166 GLN LLL N   
11272 C CA  . GLN H 166 ? 1.639 1.894 1.315 -0.114 0.104  0.181  166 GLN LLL CA  
11273 C C   . GLN H 166 ? 1.665 1.921 1.326 -0.133 0.074  0.162  166 GLN LLL C   
11274 O O   . GLN H 166 ? 1.651 1.917 1.326 -0.145 0.043  0.154  166 GLN LLL O   
11275 C CB  . GLN H 166 ? 1.649 1.883 1.285 -0.067 0.101  0.169  166 GLN LLL CB  
11276 C CG  . GLN H 166 ? 1.676 1.903 1.280 -0.024 0.146  0.186  166 GLN LLL CG  
11277 C CD  . GLN H 166 ? 1.706 1.916 1.262 0.032  0.138  0.167  166 GLN LLL CD  
11278 O OE1 . GLN H 166 ? 1.691 1.902 1.271 0.033  0.108  0.151  166 GLN LLL OE1 
11279 N NE2 . GLN H 166 ? 1.771 1.961 1.255 0.083  0.160  0.167  166 GLN LLL NE2 
11280 N N   . GLU H 167 ? 1.727 1.974 1.367 -0.136 0.084  0.159  167 GLU LLL N   
11281 C CA  . GLU H 167 ? 1.736 1.990 1.362 -0.149 0.061  0.142  167 GLU LLL CA  
11282 C C   . GLU H 167 ? 1.749 1.976 1.326 -0.116 0.050  0.125  167 GLU LLL C   
11283 O O   . GLU H 167 ? 1.780 1.973 1.315 -0.081 0.068  0.127  167 GLU LLL O   
11284 C CB  . GLU H 167 ? 1.787 2.045 1.419 -0.164 0.070  0.141  167 GLU LLL CB  
11285 C CG  . GLU H 167 ? 1.821 2.107 1.503 -0.196 0.067  0.148  167 GLU LLL CG  
11286 C CD  . GLU H 167 ? 1.879 2.163 1.569 -0.207 0.063  0.138  167 GLU LLL CD  
11287 O OE1 . GLU H 167 ? 1.935 2.202 1.591 -0.193 0.061  0.123  167 GLU LLL OE1 
11288 O OE2 . GLU H 167 ? 1.901 2.200 1.634 -0.228 0.056  0.140  167 GLU LLL OE2 
11289 N N   . SER H 168 ? 1.717 1.960 1.301 -0.127 0.021  0.111  168 SER LLL N   
11290 C CA  . SER H 168 ? 1.739 1.962 1.290 -0.101 0.000  0.091  168 SER LLL CA  
11291 C C   . SER H 168 ? 1.710 1.969 1.280 -0.121 -0.013 0.085  168 SER LLL C   
11292 O O   . SER H 168 ? 1.682 1.986 1.298 -0.151 -0.025 0.095  168 SER LLL O   
11293 C CB  . SER H 168 ? 1.749 1.957 1.308 -0.086 -0.030 0.082  168 SER LLL CB  
11294 O OG  . SER H 168 ? 1.791 1.969 1.313 -0.053 -0.052 0.058  168 SER LLL OG  
11295 N N   . VAL H 169 ? 1.714 1.958 1.249 -0.102 -0.009 0.071  169 VAL LLL N   
11296 C CA  . VAL H 169 ? 1.663 1.943 1.209 -0.112 -0.014 0.062  169 VAL LLL CA  
11297 C C   . VAL H 169 ? 1.694 1.969 1.233 -0.091 -0.040 0.044  169 VAL LLL C   
11298 O O   . VAL H 169 ? 1.765 1.991 1.256 -0.056 -0.042 0.033  169 VAL LLL O   
11299 C CB  . VAL H 169 ? 1.654 1.914 1.174 -0.105 0.008  0.058  169 VAL LLL CB  
11300 C CG1 . VAL H 169 ? 1.639 1.934 1.164 -0.106 0.000  0.041  169 VAL LLL CG1 
11301 C CG2 . VAL H 169 ? 1.641 1.900 1.180 -0.126 0.026  0.074  169 VAL LLL CG2 
11302 N N   . THR H 170 ? 1.666 1.996 1.253 -0.109 -0.058 0.046  170 THR LLL N   
11303 C CA  . THR H 170 ? 1.710 2.051 1.313 -0.094 -0.085 0.031  170 THR LLL CA  
11304 C C   . THR H 170 ? 1.750 2.087 1.316 -0.072 -0.075 0.013  170 THR LLL C   
11305 O O   . THR H 170 ? 1.741 2.100 1.301 -0.081 -0.052 0.015  170 THR LLL O   
11306 C CB  . THR H 170 ? 1.698 2.111 1.380 -0.124 -0.102 0.048  170 THR LLL CB  
11307 O OG1 . THR H 170 ? 1.697 2.174 1.388 -0.134 -0.080 0.054  170 THR LLL OG1 
11308 C CG2 . THR H 170 ? 1.695 2.117 1.419 -0.152 -0.109 0.073  170 THR LLL CG2 
11309 N N   . GLU H 171 ? 1.817 2.124 1.362 -0.040 -0.097 -0.007 171 GLU LLL N   
11310 C CA  . GLU H 171 ? 1.848 2.154 1.368 -0.016 -0.095 -0.025 171 GLU LLL CA  
11311 C C   . GLU H 171 ? 1.788 2.180 1.367 -0.033 -0.095 -0.024 171 GLU LLL C   
11312 O O   . GLU H 171 ? 1.770 2.218 1.409 -0.063 -0.100 -0.005 171 GLU LLL O   
11313 C CB  . GLU H 171 ? 1.936 2.195 1.424 0.023  -0.125 -0.045 171 GLU LLL CB  
11314 C CG  . GLU H 171 ? 2.020 2.200 1.430 0.053  -0.116 -0.043 171 GLU LLL CG  
11315 C CD  . GLU H 171 ? 2.073 2.225 1.443 0.054  -0.077 -0.029 171 GLU LLL CD  
11316 O OE1 . GLU H 171 ? 2.148 2.284 1.495 0.073  -0.076 -0.037 171 GLU LLL OE1 
11317 O OE2 . GLU H 171 ? 2.072 2.218 1.443 0.035  -0.052 -0.009 171 GLU LLL OE2 
11318 N N   . GLN H 172 ? 1.779 2.184 1.343 -0.013 -0.090 -0.041 172 GLN LLL N   
11319 C CA  . GLN H 172 ? 1.743 2.239 1.355 -0.020 -0.084 -0.043 172 GLN LLL CA  
11320 C C   . GLN H 172 ? 1.700 2.258 1.391 -0.034 -0.106 -0.028 172 GLN LLL C   
11321 O O   . GLN H 172 ? 1.714 2.230 1.411 -0.023 -0.137 -0.036 172 GLN LLL O   
11322 C CB  . GLN H 172 ? 1.778 2.269 1.362 0.015  -0.084 -0.071 172 GLN LLL CB  
11323 C CG  . GLN H 172 ? 1.787 2.281 1.341 0.017  -0.062 -0.081 172 GLN LLL CG  
11324 C CD  . GLN H 172 ? 1.831 2.323 1.366 0.054  -0.068 -0.113 172 GLN LLL CD  
11325 O OE1 . GLN H 172 ? 1.840 2.347 1.391 0.077  -0.084 -0.125 172 GLN LLL OE1 
11326 N NE2 . GLN H 172 ? 1.885 2.359 1.392 0.062  -0.059 -0.130 172 GLN LLL NE2 
11327 N N   . ASP H 173 ? 1.655 2.310 1.405 -0.056 -0.092 -0.006 173 ASP LLL N   
11328 C CA  . ASP H 173 ? 1.650 2.372 1.496 -0.081 -0.109 0.024  173 ASP LLL CA  
11329 C C   . ASP H 173 ? 1.648 2.410 1.546 -0.060 -0.131 0.011  173 ASP LLL C   
11330 O O   . ASP H 173 ? 1.641 2.429 1.513 -0.031 -0.117 -0.011 173 ASP LLL O   
11331 C CB  . ASP H 173 ? 1.659 2.481 1.552 -0.109 -0.081 0.064  173 ASP LLL CB  
11332 C CG  . ASP H 173 ? 1.665 2.566 1.674 -0.137 -0.096 0.106  173 ASP LLL CG  
11333 O OD1 . ASP H 173 ? 1.681 2.533 1.734 -0.150 -0.135 0.108  173 ASP LLL OD1 
11334 O OD2 . ASP H 173 ? 1.670 2.683 1.728 -0.143 -0.070 0.136  173 ASP LLL OD2 
11335 N N   . SER H 174 ? 1.641 2.408 1.618 -0.075 -0.169 0.023  174 SER LLL N   
11336 C CA  . SER H 174 ? 1.638 2.449 1.697 -0.064 -0.201 0.017  174 SER LLL CA  
11337 C C   . SER H 174 ? 1.617 2.559 1.740 -0.065 -0.169 0.039  174 SER LLL C   
11338 O O   . SER H 174 ? 1.587 2.565 1.749 -0.040 -0.185 0.022  174 SER LLL O   
11339 C CB  . SER H 174 ? 1.628 2.429 1.781 -0.091 -0.249 0.036  174 SER LLL CB  
11340 O OG  . SER H 174 ? 1.620 2.337 1.724 -0.103 -0.258 0.036  174 SER LLL OG  
11341 N N   . LYS H 175 ? 1.619 2.633 1.749 -0.086 -0.127 0.075  175 LYS LLL N   
11342 C CA  . LYS H 175 ? 1.611 2.770 1.806 -0.087 -0.091 0.109  175 LYS LLL CA  
11343 C C   . LYS H 175 ? 1.645 2.822 1.739 -0.056 -0.048 0.085  175 LYS LLL C   
11344 O O   . LYS H 175 ? 1.643 2.870 1.732 -0.018 -0.038 0.060  175 LYS LLL O   
11345 C CB  . LYS H 175 ? 1.575 2.808 1.863 -0.134 -0.081 0.177  175 LYS LLL CB  
11346 C CG  . LYS H 175 ? 1.562 2.762 1.956 -0.169 -0.132 0.199  175 LYS LLL CG  
11347 C CD  . LYS H 175 ? 1.560 2.868 2.108 -0.184 -0.146 0.238  175 LYS LLL CD  
11348 C CE  . LYS H 175 ? 1.564 2.842 2.234 -0.225 -0.201 0.267  175 LYS LLL CE  
11349 N NZ  . LYS H 175 ? 1.570 2.951 2.406 -0.240 -0.220 0.304  175 LYS LLL NZ  
11350 N N   . ASP H 176 ? 1.686 2.824 1.708 -0.067 -0.029 0.088  176 ASP LLL N   
11351 C CA  . ASP H 176 ? 1.755 2.934 1.703 -0.043 0.008  0.074  176 ASP LLL CA  
11352 C C   . ASP H 176 ? 1.802 2.863 1.642 -0.019 0.000  0.020  176 ASP LLL C   
11353 O O   . ASP H 176 ? 1.792 2.868 1.571 0.000  0.019  0.002  176 ASP LLL O   
11354 C CB  . ASP H 176 ? 1.775 3.013 1.733 -0.072 0.033  0.124  176 ASP LLL CB  
11355 C CG  . ASP H 176 ? 1.789 2.926 1.706 -0.102 0.020  0.127  176 ASP LLL CG  
11356 O OD1 . ASP H 176 ? 1.816 2.840 1.688 -0.097 -0.003 0.090  176 ASP LLL OD1 
11357 O OD2 . ASP H 176 ? 1.814 2.993 1.745 -0.128 0.034  0.169  176 ASP LLL OD2 
11358 N N   . SER H 177 ? 1.848 2.798 1.666 -0.018 -0.030 -0.003 177 SER LLL N   
11359 C CA  . SER H 177 ? 1.893 2.732 1.623 0.005  -0.037 -0.045 177 SER LLL CA  
11360 C C   . SER H 177 ? 1.873 2.672 1.551 -0.013 -0.023 -0.040 177 SER LLL C   
11361 O O   . SER H 177 ? 1.898 2.645 1.518 0.008  -0.021 -0.072 177 SER LLL O   
11362 C CB  . SER H 177 ? 1.959 2.814 1.661 0.050  -0.035 -0.084 177 SER LLL CB  
11363 O OG  . SER H 177 ? 1.995 2.906 1.755 0.067  -0.047 -0.086 177 SER LLL OG  
11364 N N   . THR H 178 ? 1.807 2.626 1.515 -0.050 -0.017 -0.003 178 THR LLL N   
11365 C CA  . THR H 178 ? 1.753 2.534 1.424 -0.070 -0.008 0.005  178 THR LLL CA  
11366 C C   . THR H 178 ? 1.715 2.405 1.382 -0.089 -0.023 0.014  178 THR LLL C   
11367 O O   . THR H 178 ? 1.689 2.364 1.390 -0.093 -0.042 0.022  178 THR LLL O   
11368 C CB  . THR H 178 ? 1.712 2.584 1.413 -0.092 0.009  0.043  178 THR LLL CB  
11369 O OG1 . THR H 178 ? 1.667 2.560 1.437 -0.123 -0.001 0.084  178 THR LLL OG1 
11370 C CG2 . THR H 178 ? 1.722 2.703 1.424 -0.066 0.029  0.041  178 THR LLL CG2 
11371 N N   . TYR H 179 ? 1.693 2.329 1.322 -0.099 -0.017 0.012  179 TYR LLL N   
11372 C CA  . TYR H 179 ? 1.660 2.227 1.285 -0.117 -0.023 0.026  179 TYR LLL CA  
11373 C C   . TYR H 179 ? 1.618 2.230 1.278 -0.149 -0.018 0.060  179 TYR LLL C   
11374 O O   . TYR H 179 ? 1.630 2.320 1.303 -0.155 -0.008 0.072  179 TYR LLL O   
11375 C CB  . TYR H 179 ? 1.680 2.169 1.257 -0.107 -0.016 0.009  179 TYR LLL CB  
11376 C CG  . TYR H 179 ? 1.734 2.180 1.276 -0.075 -0.019 -0.019 179 TYR LLL CG  
11377 C CD1 . TYR H 179 ? 1.778 2.174 1.303 -0.055 -0.030 -0.024 179 TYR LLL CD1 
11378 C CD2 . TYR H 179 ? 1.761 2.212 1.285 -0.061 -0.017 -0.043 179 TYR LLL CD2 
11379 C CE1 . TYR H 179 ? 1.815 2.167 1.307 -0.025 -0.034 -0.045 179 TYR LLL CE1 
11380 C CE2 . TYR H 179 ? 1.814 2.218 1.312 -0.032 -0.024 -0.067 179 TYR LLL CE2 
11381 C CZ  . TYR H 179 ? 1.831 2.186 1.313 -0.015 -0.031 -0.065 179 TYR LLL CZ  
11382 O OH  . TYR H 179 ? 1.829 2.135 1.285 0.016  -0.040 -0.085 179 TYR LLL OH  
11383 N N   . SER H 180 ? 1.583 2.149 1.255 -0.165 -0.028 0.075  180 SER LLL N   
11384 C CA  . SER H 180 ? 1.543 2.127 1.242 -0.193 -0.027 0.105  180 SER LLL CA  
11385 C C   . SER H 180 ? 1.563 2.068 1.237 -0.192 -0.027 0.099  180 SER LLL C   
11386 O O   . SER H 180 ? 1.633 2.079 1.275 -0.169 -0.029 0.079  180 SER LLL O   
11387 C CB  . SER H 180 ? 1.511 2.137 1.276 -0.213 -0.044 0.136  180 SER LLL CB  
11388 O OG  . SER H 180 ? 1.497 2.203 1.293 -0.211 -0.039 0.145  180 SER LLL OG  
11389 N N   . LEU H 181 ? 1.536 2.044 1.224 -0.212 -0.025 0.118  181 LEU LLL N   
11390 C CA  . LEU H 181 ? 1.542 1.989 1.212 -0.209 -0.018 0.115  181 LEU LLL CA  
11391 C C   . LEU H 181 ? 1.530 1.981 1.237 -0.228 -0.029 0.140  181 LEU LLL C   
11392 O O   . LEU H 181 ? 1.529 2.034 1.265 -0.250 -0.034 0.162  181 LEU LLL O   
11393 C CB  . LEU H 181 ? 1.550 1.994 1.198 -0.209 -0.003 0.105  181 LEU LLL CB  
11394 C CG  . LEU H 181 ? 1.583 1.968 1.220 -0.202 0.010  0.103  181 LEU LLL CG  
11395 C CD1 . LEU H 181 ? 1.598 1.970 1.222 -0.198 0.018  0.088  181 LEU LLL CD1 
11396 C CD2 . LEU H 181 ? 1.582 1.969 1.248 -0.219 0.009  0.123  181 LEU LLL CD2 
11397 N N   . SER H 182 ? 1.550 1.948 1.253 -0.216 -0.034 0.136  182 SER LLL N   
11398 C CA  . SER H 182 ? 1.562 1.952 1.297 -0.227 -0.045 0.153  182 SER LLL CA  
11399 C C   . SER H 182 ? 1.573 1.929 1.288 -0.215 -0.024 0.149  182 SER LLL C   
11400 O O   . SER H 182 ? 1.601 1.911 1.285 -0.185 -0.016 0.136  182 SER LLL O   
11401 C CB  . SER H 182 ? 1.602 1.965 1.359 -0.217 -0.075 0.150  182 SER LLL CB  
11402 O OG  . SER H 182 ? 1.656 1.964 1.387 -0.187 -0.074 0.135  182 SER LLL OG  
11403 N N   . SER H 183 ? 1.565 1.944 1.298 -0.234 -0.015 0.161  183 SER LLL N   
11404 C CA  . SER H 183 ? 1.593 1.952 1.335 -0.229 0.002  0.166  183 SER LLL CA  
11405 C C   . SER H 183 ? 1.592 1.952 1.369 -0.233 -0.015 0.179  183 SER LLL C   
11406 O O   . SER H 183 ? 1.577 1.970 1.384 -0.257 -0.033 0.195  183 SER LLL O   
11407 C CB  . SER H 183 ? 1.601 1.981 1.355 -0.246 0.011  0.168  183 SER LLL CB  
11408 O OG  . SER H 183 ? 1.607 1.968 1.382 -0.240 0.029  0.175  183 SER LLL OG  
11409 N N   . THR H 184 ? 1.643 1.967 1.412 -0.205 -0.010 0.173  184 THR LLL N   
11410 C CA  . THR H 184 ? 1.677 1.993 1.477 -0.198 -0.028 0.179  184 THR LLL CA  
11411 C C   . THR H 184 ? 1.665 1.988 1.484 -0.192 -0.002 0.188  184 THR LLL C   
11412 O O   . THR H 184 ? 1.689 2.001 1.485 -0.173 0.030  0.186  184 THR LLL O   
11413 C CB  . THR H 184 ? 1.757 2.031 1.532 -0.162 -0.047 0.158  184 THR LLL CB  
11414 O OG1 . THR H 184 ? 1.776 2.045 1.534 -0.165 -0.063 0.147  184 THR LLL OG1 
11415 C CG2 . THR H 184 ? 1.769 2.031 1.586 -0.160 -0.082 0.160  184 THR LLL CG2 
11416 N N   . LEU H 185 ? 1.651 1.995 1.518 -0.211 -0.017 0.202  185 LEU LLL N   
11417 C CA  . LEU H 185 ? 1.647 2.004 1.550 -0.206 0.000  0.212  185 LEU LLL CA  
11418 C C   . LEU H 185 ? 1.659 1.998 1.578 -0.178 -0.016 0.208  185 LEU LLL C   
11419 O O   . LEU H 185 ? 1.655 1.992 1.599 -0.192 -0.053 0.213  185 LEU LLL O   
11420 C CB  . LEU H 185 ? 1.622 2.017 1.566 -0.243 -0.014 0.228  185 LEU LLL CB  
11421 C CG  . LEU H 185 ? 1.602 2.017 1.601 -0.244 -0.004 0.239  185 LEU LLL CG  
11422 C CD1 . LEU H 185 ? 1.600 2.020 1.609 -0.244 0.030  0.241  185 LEU LLL CD1 
11423 C CD2 . LEU H 185 ? 1.580 2.025 1.613 -0.274 -0.035 0.251  185 LEU LLL CD2 
11424 N N   . THR H 186 ? 1.692 2.019 1.596 -0.136 0.011  0.200  186 THR LLL N   
11425 C CA  . THR H 186 ? 1.767 2.075 1.675 -0.096 -0.004 0.186  186 THR LLL CA  
11426 C C   . THR H 186 ? 1.756 2.098 1.717 -0.088 0.019  0.202  186 THR LLL C   
11427 O O   . THR H 186 ? 1.752 2.124 1.728 -0.095 0.059  0.219  186 THR LLL O   
11428 C CB  . THR H 186 ? 1.869 2.143 1.710 -0.041 0.008  0.161  186 THR LLL CB  
11429 O OG1 . THR H 186 ? 1.889 2.135 1.695 -0.052 -0.020 0.146  186 THR LLL OG1 
11430 C CG2 . THR H 186 ? 1.937 2.190 1.774 0.012  -0.011 0.138  186 THR LLL CG2 
11431 N N   . LEU H 187 ? 1.758 2.096 1.755 -0.075 -0.011 0.196  187 LEU LLL N   
11432 C CA  . LEU H 187 ? 1.747 2.119 1.799 -0.057 0.006  0.206  187 LEU LLL CA  
11433 C C   . LEU H 187 ? 1.801 2.147 1.870 -0.027 -0.036 0.188  187 LEU LLL C   
11434 O O   . LEU H 187 ? 1.824 2.127 1.879 -0.036 -0.084 0.175  187 LEU LLL O   
11435 C CB  . LEU H 187 ? 1.660 2.072 1.776 -0.108 0.004  0.233  187 LEU LLL CB  
11436 C CG  . LEU H 187 ? 1.624 2.028 1.761 -0.148 -0.047 0.240  187 LEU LLL CG  
11437 C CD1 . LEU H 187 ? 1.588 2.032 1.792 -0.173 -0.055 0.260  187 LEU LLL CD1 
11438 C CD2 . LEU H 187 ? 1.610 2.006 1.706 -0.184 -0.056 0.243  187 LEU LLL CD2 
11439 N N   . SER H 188 ? 1.833 2.204 1.939 0.009  -0.021 0.188  188 SER LLL N   
11440 C CA  . SER H 188 ? 1.885 2.233 2.014 0.046  -0.061 0.167  188 SER LLL CA  
11441 C C   . SER H 188 ? 1.874 2.211 2.059 -0.004 -0.114 0.183  188 SER LLL C   
11442 O O   . SER H 188 ? 1.820 2.194 2.039 -0.053 -0.106 0.213  188 SER LLL O   
11443 C CB  . SER H 188 ? 1.907 2.301 2.071 0.093  -0.024 0.168  188 SER LLL CB  
11444 O OG  . SER H 188 ? 1.865 2.315 2.104 0.052  -0.005 0.202  188 SER LLL OG  
11445 N N   . LYS H 189 ? 1.957 2.244 2.150 0.011  -0.171 0.166  189 LYS LLL N   
11446 C CA  . LYS H 189 ? 1.968 2.241 2.219 -0.027 -0.225 0.188  189 LYS LLL CA  
11447 C C   . LYS H 189 ? 1.948 2.274 2.260 -0.035 -0.210 0.209  189 LYS LLL C   
11448 O O   . LYS H 189 ? 1.920 2.267 2.262 -0.085 -0.225 0.241  189 LYS LLL O   
11449 C CB  . LYS H 189 ? 2.034 2.243 2.300 0.007  -0.286 0.161  189 LYS LLL CB  
11450 C CG  . LYS H 189 ? 2.034 2.222 2.367 -0.025 -0.345 0.189  189 LYS LLL CG  
11451 C CD  . LYS H 189 ? 2.053 2.255 2.440 0.007  -0.356 0.185  189 LYS LLL CD  
11452 C CE  . LYS H 189 ? 2.076 2.245 2.527 -0.018 -0.421 0.212  189 LYS LLL CE  
11453 N NZ  . LYS H 189 ? 2.152 2.241 2.620 0.014  -0.485 0.184  189 LYS LLL NZ  
11454 N N   . ALA H 190 ? 1.979 2.330 2.305 0.018  -0.181 0.191  190 ALA LLL N   
11455 C CA  . ALA H 190 ? 1.975 2.387 2.369 0.018  -0.159 0.209  190 ALA LLL CA  
11456 C C   . ALA H 190 ? 1.908 2.364 2.320 -0.042 -0.137 0.242  190 ALA LLL C   
11457 O O   . ALA H 190 ? 1.862 2.333 2.320 -0.078 -0.168 0.264  190 ALA LLL O   
11458 C CB  . ALA H 190 ? 2.016 2.463 2.408 0.082  -0.108 0.192  190 ALA LLL CB  
11459 N N   . ASP H 191 ? 1.901 2.374 2.274 -0.049 -0.089 0.243  191 ASP LLL N   
11460 C CA  . ASP H 191 ? 1.850 2.363 2.244 -0.096 -0.065 0.267  191 ASP LLL CA  
11461 C C   . ASP H 191 ? 1.781 2.271 2.145 -0.148 -0.104 0.277  191 ASP LLL C   
11462 O O   . ASP H 191 ? 1.751 2.272 2.142 -0.185 -0.108 0.292  191 ASP LLL O   
11463 C CB  . ASP H 191 ? 1.888 2.417 2.251 -0.083 -0.006 0.267  191 ASP LLL CB  
11464 C CG  . ASP H 191 ? 1.930 2.503 2.331 -0.035 0.043  0.272  191 ASP LLL CG  
11465 O OD1 . ASP H 191 ? 1.927 2.544 2.411 -0.031 0.040  0.283  191 ASP LLL OD1 
11466 O OD2 . ASP H 191 ? 1.970 2.539 2.319 0.002  0.084  0.266  191 ASP LLL OD2 
11467 N N   . TYR H 192 ? 1.749 2.191 2.065 -0.147 -0.133 0.269  192 TYR LLL N   
11468 C CA  . TYR H 192 ? 1.707 2.137 1.998 -0.192 -0.164 0.285  192 TYR LLL CA  
11469 C C   . TYR H 192 ? 1.727 2.170 2.065 -0.213 -0.207 0.309  192 TYR LLL C   
11470 O O   . TYR H 192 ? 1.722 2.187 2.049 -0.249 -0.219 0.330  192 TYR LLL O   
11471 C CB  . TYR H 192 ? 1.695 2.076 1.944 -0.185 -0.185 0.276  192 TYR LLL CB  
11472 C CG  . TYR H 192 ? 1.663 2.044 1.901 -0.228 -0.214 0.302  192 TYR LLL CG  
11473 C CD1 . TYR H 192 ? 1.620 2.025 1.818 -0.256 -0.193 0.309  192 TYR LLL CD1 
11474 C CD2 . TYR H 192 ? 1.682 2.042 1.953 -0.239 -0.262 0.324  192 TYR LLL CD2 
11475 C CE1 . TYR H 192 ? 1.606 2.024 1.792 -0.289 -0.213 0.336  192 TYR LLL CE1 
11476 C CE2 . TYR H 192 ? 1.670 2.040 1.935 -0.277 -0.282 0.360  192 TYR LLL CE2 
11477 C CZ  . TYR H 192 ? 1.632 2.037 1.852 -0.300 -0.255 0.365  192 TYR LLL CZ  
11478 O OH  . TYR H 192 ? 1.622 2.050 1.834 -0.331 -0.268 0.403  192 TYR LLL OH  
11479 N N   . GLU H 193 ? 1.777 2.208 2.160 -0.185 -0.230 0.306  193 GLU LLL N   
11480 C CA  . GLU H 193 ? 1.808 2.244 2.239 -0.198 -0.275 0.331  193 GLU LLL CA  
11481 C C   . GLU H 193 ? 1.772 2.264 2.246 -0.209 -0.264 0.338  193 GLU LLL C   
11482 O O   . GLU H 193 ? 1.774 2.278 2.276 -0.225 -0.302 0.360  193 GLU LLL O   
11483 C CB  . GLU H 193 ? 1.888 2.285 2.356 -0.160 -0.308 0.320  193 GLU LLL CB  
11484 C CG  . GLU H 193 ? 1.944 2.279 2.389 -0.160 -0.342 0.319  193 GLU LLL CG  
11485 C CD  . GLU H 193 ? 2.015 2.303 2.510 -0.137 -0.399 0.319  193 GLU LLL CD  
11486 O OE1 . GLU H 193 ? 2.066 2.361 2.600 -0.099 -0.401 0.302  193 GLU LLL OE1 
11487 O OE2 . GLU H 193 ? 2.039 2.283 2.541 -0.157 -0.441 0.339  193 GLU LLL OE2 
11488 N N   . LYS H 194 ? 1.756 2.280 2.240 -0.201 -0.219 0.323  194 LYS LLL N   
11489 C CA  . LYS H 194 ? 1.755 2.332 2.299 -0.213 -0.211 0.329  194 LYS LLL CA  
11490 C C   . LYS H 194 ? 1.737 2.328 2.251 -0.255 -0.227 0.339  194 LYS LLL C   
11491 O O   . LYS H 194 ? 1.783 2.400 2.333 -0.268 -0.261 0.349  194 LYS LLL O   
11492 C CB  . LYS H 194 ? 1.762 2.368 2.338 -0.191 -0.156 0.318  194 LYS LLL CB  
11493 C CG  . LYS H 194 ? 1.791 2.417 2.429 -0.146 -0.141 0.313  194 LYS LLL CG  
11494 C CD  . LYS H 194 ? 1.804 2.455 2.447 -0.113 -0.077 0.307  194 LYS LLL CD  
11495 C CE  . LYS H 194 ? 1.767 2.455 2.441 -0.143 -0.042 0.322  194 LYS LLL CE  
11496 N NZ  . LYS H 194 ? 1.763 2.480 2.446 -0.109 0.024  0.329  194 LYS LLL NZ  
11497 N N   . HIS H 195 ? 1.694 2.272 2.143 -0.270 -0.206 0.333  195 HIS LLL N   
11498 C CA  . HIS H 195 ? 1.672 2.265 2.082 -0.301 -0.217 0.335  195 HIS LLL CA  
11499 C C   . HIS H 195 ? 1.683 2.262 2.036 -0.314 -0.248 0.355  195 HIS LLL C   
11500 O O   . HIS H 195 ? 1.710 2.258 2.056 -0.303 -0.254 0.364  195 HIS LLL O   
11501 C CB  . HIS H 195 ? 1.649 2.237 2.029 -0.305 -0.177 0.318  195 HIS LLL CB  
11502 C CG  . HIS H 195 ? 1.641 2.240 2.077 -0.289 -0.138 0.311  195 HIS LLL CG  
11503 N ND1 . HIS H 195 ? 1.635 2.270 2.160 -0.290 -0.142 0.315  195 HIS LLL ND1 
11504 C CD2 . HIS H 195 ? 1.648 2.233 2.067 -0.269 -0.093 0.305  195 HIS LLL CD2 
11505 C CE1 . HIS H 195 ? 1.642 2.290 2.209 -0.274 -0.097 0.317  195 HIS LLL CE1 
11506 N NE2 . HIS H 195 ? 1.645 2.262 2.142 -0.258 -0.065 0.311  195 HIS LLL NE2 
11507 N N   . LYS H 196 ? 1.673 2.277 1.992 -0.333 -0.270 0.363  196 LYS LLL N   
11508 C CA  . LYS H 196 ? 1.697 2.303 1.965 -0.343 -0.295 0.394  196 LYS LLL CA  
11509 C C   . LYS H 196 ? 1.690 2.309 1.884 -0.355 -0.278 0.391  196 LYS LLL C   
11510 O O   . LYS H 196 ? 1.737 2.352 1.900 -0.361 -0.277 0.417  196 LYS LLL O   
11511 C CB  . LYS H 196 ? 1.738 2.372 2.016 -0.346 -0.338 0.415  196 LYS LLL CB  
11512 C CG  . LYS H 196 ? 1.806 2.444 2.048 -0.353 -0.360 0.462  196 LYS LLL CG  
11513 C CD  . LYS H 196 ? 1.892 2.567 2.108 -0.353 -0.397 0.487  196 LYS LLL CD  
11514 C CE  . LYS H 196 ? 1.950 2.634 2.132 -0.361 -0.411 0.546  196 LYS LLL CE  
11515 N NZ  . LYS H 196 ? 2.020 2.745 2.165 -0.354 -0.446 0.575  196 LYS LLL NZ  
11516 N N   . VAL H 197 ? 1.657 2.293 1.834 -0.356 -0.267 0.361  197 VAL LLL N   
11517 C CA  . VAL H 197 ? 1.654 2.307 1.758 -0.361 -0.256 0.353  197 VAL LLL CA  
11518 C C   . VAL H 197 ? 1.613 2.240 1.708 -0.359 -0.217 0.327  197 VAL LLL C   
11519 O O   . VAL H 197 ? 1.600 2.219 1.723 -0.357 -0.207 0.300  197 VAL LLL O   
11520 C CB  . VAL H 197 ? 1.687 2.371 1.769 -0.358 -0.281 0.333  197 VAL LLL CB  
11521 C CG1 . VAL H 197 ? 1.702 2.404 1.707 -0.354 -0.270 0.317  197 VAL LLL CG1 
11522 C CG2 . VAL H 197 ? 1.730 2.442 1.809 -0.354 -0.322 0.359  197 VAL LLL CG2 
11523 N N   . TYR H 198 ? 1.604 2.219 1.664 -0.360 -0.200 0.339  198 TYR LLL N   
11524 C CA  . TYR H 198 ? 1.600 2.190 1.640 -0.356 -0.167 0.317  198 TYR LLL CA  
11525 C C   . TYR H 198 ? 1.626 2.241 1.605 -0.358 -0.160 0.310  198 TYR LLL C   
11526 O O   . TYR H 198 ? 1.711 2.356 1.662 -0.363 -0.169 0.338  198 TYR LLL O   
11527 C CB  . TYR H 198 ? 1.589 2.146 1.642 -0.350 -0.160 0.330  198 TYR LLL CB  
11528 C CG  . TYR H 198 ? 1.580 2.111 1.687 -0.337 -0.161 0.326  198 TYR LLL CG  
11529 C CD1 . TYR H 198 ? 1.596 2.129 1.742 -0.338 -0.191 0.349  198 TYR LLL CD1 
11530 C CD2 . TYR H 198 ? 1.545 2.054 1.665 -0.319 -0.132 0.303  198 TYR LLL CD2 
11531 C CE1 . TYR H 198 ? 1.584 2.097 1.779 -0.319 -0.193 0.342  198 TYR LLL CE1 
11532 C CE2 . TYR H 198 ? 1.532 2.029 1.698 -0.300 -0.129 0.300  198 TYR LLL CE2 
11533 C CZ  . TYR H 198 ? 1.549 2.048 1.754 -0.298 -0.160 0.317  198 TYR LLL CZ  
11534 O OH  . TYR H 198 ? 1.554 2.044 1.805 -0.273 -0.157 0.311  198 TYR LLL OH  
11535 N N   . ALA H 199 ? 1.619 2.225 1.581 -0.353 -0.145 0.277  199 ALA LLL N   
11536 C CA  . ALA H 199 ? 1.638 2.269 1.543 -0.348 -0.143 0.260  199 ALA LLL CA  
11537 C C   . ALA H 199 ? 1.621 2.221 1.511 -0.341 -0.116 0.234  199 ALA LLL C   
11538 O O   . ALA H 199 ? 1.621 2.183 1.547 -0.340 -0.100 0.228  199 ALA LLL O   
11539 C CB  . ALA H 199 ? 1.682 2.335 1.581 -0.344 -0.171 0.239  199 ALA LLL CB  
11540 N N   . CYS H 200 ? 1.636 2.257 1.475 -0.333 -0.111 0.221  200 CYS LLL N   
11541 C CA  . CYS H 200 ? 1.643 2.240 1.460 -0.324 -0.089 0.200  200 CYS LLL CA  
11542 C C   . CYS H 200 ? 1.651 2.267 1.425 -0.311 -0.099 0.167  200 CYS LLL C   
11543 O O   . CYS H 200 ? 1.664 2.327 1.392 -0.301 -0.099 0.171  200 CYS LLL O   
11544 C CB  . CYS H 200 ? 1.665 2.271 1.468 -0.325 -0.075 0.221  200 CYS LLL CB  
11545 S SG  . CYS H 200 ? 1.754 2.323 1.536 -0.311 -0.051 0.197  200 CYS LLL SG  
11546 N N   . GLU H 201 ? 1.671 2.254 1.465 -0.309 -0.108 0.137  201 GLU LLL N   
11547 C CA  . GLU H 201 ? 1.741 2.326 1.505 -0.292 -0.127 0.095  201 GLU LLL CA  
11548 C C   . GLU H 201 ? 1.743 2.301 1.484 -0.281 -0.107 0.078  201 GLU LLL C   
11549 O O   . GLU H 201 ? 1.754 2.266 1.530 -0.288 -0.087 0.085  201 GLU LLL O   
11550 C CB  . GLU H 201 ? 1.787 2.342 1.606 -0.300 -0.155 0.075  201 GLU LLL CB  
11551 C CG  . GLU H 201 ? 1.859 2.418 1.652 -0.280 -0.196 0.027  201 GLU LLL CG  
11552 C CD  . GLU H 201 ? 1.888 2.409 1.756 -0.291 -0.231 0.005  201 GLU LLL CD  
11553 O OE1 . GLU H 201 ? 1.885 2.361 1.818 -0.307 -0.214 0.016  201 GLU LLL OE1 
11554 O OE2 . GLU H 201 ? 1.913 2.451 1.776 -0.280 -0.277 -0.022 201 GLU LLL OE2 
11555 N N   . VAL H 202 ? 1.762 2.353 1.446 -0.259 -0.110 0.057  202 VAL LLL N   
11556 C CA  . VAL H 202 ? 1.758 2.334 1.415 -0.244 -0.091 0.042  202 VAL LLL CA  
11557 C C   . VAL H 202 ? 1.823 2.394 1.449 -0.217 -0.116 -0.009 202 VAL LLL C   
11558 O O   . VAL H 202 ? 1.857 2.486 1.433 -0.194 -0.128 -0.024 202 VAL LLL O   
11559 C CB  . VAL H 202 ? 1.718 2.349 1.345 -0.239 -0.069 0.068  202 VAL LLL CB  
11560 C CG1 . VAL H 202 ? 1.714 2.335 1.319 -0.221 -0.055 0.050  202 VAL LLL CG1 
11561 C CG2 . VAL H 202 ? 1.666 2.293 1.329 -0.263 -0.056 0.112  202 VAL LLL CG2 
11562 N N   . THR H 203 ? 1.856 2.364 1.510 -0.216 -0.122 -0.032 203 THR LLL N   
11563 C CA  . THR H 203 ? 1.925 2.411 1.558 -0.188 -0.149 -0.084 203 THR LLL CA  
11564 C C   . THR H 203 ? 1.935 2.408 1.541 -0.171 -0.127 -0.089 203 THR LLL C   
11565 O O   . THR H 203 ? 1.967 2.378 1.606 -0.182 -0.116 -0.080 203 THR LLL O   
11566 C CB  . THR H 203 ? 1.946 2.362 1.643 -0.201 -0.180 -0.102 203 THR LLL CB  
11567 O OG1 . THR H 203 ? 1.979 2.417 1.692 -0.206 -0.214 -0.112 203 THR LLL OG1 
11568 C CG2 . THR H 203 ? 1.997 2.368 1.690 -0.176 -0.210 -0.151 203 THR LLL CG2 
11569 N N   . HIS H 204 ? 1.942 2.477 1.491 -0.144 -0.119 -0.101 204 HIS LLL N   
11570 C CA  . HIS H 204 ? 1.937 2.470 1.461 -0.122 -0.103 -0.114 204 HIS LLL CA  
11571 C C   . HIS H 204 ? 1.999 2.543 1.483 -0.078 -0.131 -0.171 204 HIS LLL C   
11572 O O   . HIS H 204 ? 2.054 2.648 1.503 -0.058 -0.151 -0.193 204 HIS LLL O   
11573 C CB  . HIS H 204 ? 1.897 2.498 1.405 -0.124 -0.070 -0.078 204 HIS LLL CB  
11574 C CG  . HIS H 204 ? 1.894 2.490 1.391 -0.104 -0.057 -0.088 204 HIS LLL CG  
11575 N ND1 . HIS H 204 ? 1.905 2.580 1.374 -0.078 -0.045 -0.093 204 HIS LLL ND1 
11576 C CD2 . HIS H 204 ? 1.891 2.416 1.402 -0.103 -0.055 -0.095 204 HIS LLL CD2 
11577 C CE1 . HIS H 204 ? 1.904 2.554 1.375 -0.063 -0.039 -0.105 204 HIS LLL CE1 
11578 N NE2 . HIS H 204 ? 1.901 2.457 1.393 -0.078 -0.046 -0.106 204 HIS LLL NE2 
11579 N N   . GLN H 205 ? 2.000 2.499 1.483 -0.060 -0.134 -0.196 205 GLN LLL N   
11580 C CA  . GLN H 205 ? 2.045 2.542 1.494 -0.012 -0.164 -0.256 205 GLN LLL CA  
11581 C C   . GLN H 205 ? 2.049 2.655 1.436 0.026  -0.155 -0.270 205 GLN LLL C   
11582 O O   . GLN H 205 ? 2.111 2.730 1.458 0.069  -0.187 -0.325 205 GLN LLL O   
11583 C CB  . GLN H 205 ? 2.043 2.491 1.500 0.000  -0.157 -0.264 205 GLN LLL CB  
11584 C CG  . GLN H 205 ? 2.108 2.534 1.540 0.049  -0.193 -0.329 205 GLN LLL CG  
11585 C CD  . GLN H 205 ? 2.113 2.451 1.576 0.049  -0.200 -0.332 205 GLN LLL CD  
11586 O OE1 . GLN H 205 ? 2.043 2.347 1.531 0.019  -0.171 -0.285 205 GLN LLL OE1 
11587 N NE2 . GLN H 205 ? 2.181 2.476 1.636 0.088  -0.240 -0.389 205 GLN LLL NE2 
11588 N N   . GLY H 206 ? 1.999 2.680 1.381 0.013  -0.113 -0.222 206 GLY LLL N   
11589 C CA  . GLY H 206 ? 2.033 2.832 1.367 0.043  -0.093 -0.213 206 GLY LLL CA  
11590 C C   . GLY H 206 ? 2.098 2.940 1.396 0.054  -0.112 -0.220 206 GLY LLL C   
11591 O O   . GLY H 206 ? 2.174 3.089 1.410 0.106  -0.117 -0.251 206 GLY LLL O   
11592 N N   . LEU H 207 ? 2.090 2.890 1.421 0.013  -0.122 -0.195 207 LEU LLL N   
11593 C CA  . LEU H 207 ? 2.134 2.976 1.436 0.017  -0.140 -0.190 207 LEU LLL CA  
11594 C C   . LEU H 207 ? 2.197 2.978 1.487 0.040  -0.197 -0.257 207 LEU LLL C   
11595 O O   . LEU H 207 ? 2.167 2.854 1.519 0.007  -0.220 -0.264 207 LEU LLL O   
11596 C CB  . LEU H 207 ? 2.083 2.911 1.436 -0.039 -0.124 -0.129 207 LEU LLL CB  
11597 C CG  . LEU H 207 ? 2.057 2.958 1.420 -0.057 -0.079 -0.063 207 LEU LLL CG  
11598 C CD1 . LEU H 207 ? 1.987 2.843 1.414 -0.110 -0.070 -0.015 207 LEU LLL CD1 
11599 C CD2 . LEU H 207 ? 2.117 3.128 1.426 -0.030 -0.070 -0.041 207 LEU LLL CD2 
11600 N N   . SER H 208 ? 2.275 3.113 1.491 0.096  -0.220 -0.301 208 SER LLL N   
11601 C CA  . SER H 208 ? 2.356 3.151 1.548 0.129  -0.287 -0.371 208 SER LLL CA  
11602 C C   . SER H 208 ? 2.322 3.058 1.576 0.080  -0.314 -0.352 208 SER LLL C   
11603 O O   . SER H 208 ? 2.314 2.953 1.644 0.051  -0.342 -0.370 208 SER LLL O   
11604 C CB  . SER H 208 ? 2.440 3.331 1.528 0.197  -0.297 -0.402 208 SER LLL CB  
11605 O OG  . SER H 208 ? 2.396 3.387 1.456 0.186  -0.250 -0.330 208 SER LLL OG  
11606 N N   . SER H 209 ? 2.295 3.094 1.526 0.071  -0.304 -0.312 209 SER LLL N   
11607 C CA  . SER H 209 ? 2.258 3.019 1.547 0.027  -0.326 -0.287 209 SER LLL CA  
11608 C C   . SER H 209 ? 2.158 2.914 1.510 -0.032 -0.273 -0.210 209 SER LLL C   
11609 O O   . SER H 209 ? 2.143 2.965 1.468 -0.034 -0.226 -0.163 209 SER LLL O   
11610 C CB  . SER H 209 ? 2.301 3.126 1.526 0.056  -0.351 -0.290 209 SER LLL CB  
11611 O OG  . SER H 209 ? 2.284 3.057 1.569 0.026  -0.395 -0.293 209 SER LLL OG  
11612 N N   . PRO H 210 ? 2.090 2.770 1.531 -0.079 -0.281 -0.195 210 PRO LLL N   
11613 C CA  . PRO H 210 ? 1.986 2.657 1.481 -0.126 -0.236 -0.130 210 PRO LLL CA  
11614 C C   . PRO H 210 ? 1.954 2.699 1.422 -0.135 -0.212 -0.076 210 PRO LLL C   
11615 O O   . PRO H 210 ? 1.998 2.786 1.426 -0.115 -0.238 -0.082 210 PRO LLL O   
11616 C CB  . PRO H 210 ? 1.968 2.567 1.551 -0.161 -0.261 -0.130 210 PRO LLL CB  
11617 C CG  . PRO H 210 ? 2.038 2.583 1.634 -0.140 -0.308 -0.194 210 PRO LLL CG  
11618 C CD  . PRO H 210 ? 2.117 2.717 1.618 -0.086 -0.334 -0.240 210 PRO LLL CD  
11619 N N   . VAL H 211 ? 1.893 2.648 1.386 -0.162 -0.169 -0.024 211 VAL LLL N   
11620 C CA  . VAL H 211 ? 1.886 2.706 1.369 -0.174 -0.145 0.036  211 VAL LLL CA  
11621 C C   . VAL H 211 ? 1.851 2.630 1.404 -0.215 -0.142 0.074  211 VAL LLL C   
11622 O O   . VAL H 211 ? 1.854 2.581 1.451 -0.235 -0.124 0.081  211 VAL LLL O   
11623 C CB  . VAL H 211 ? 1.857 2.724 1.326 -0.170 -0.105 0.065  211 VAL LLL CB  
11624 C CG1 . VAL H 211 ? 1.807 2.712 1.304 -0.197 -0.083 0.134  211 VAL LLL CG1 
11625 C CG2 . VAL H 211 ? 1.934 2.871 1.329 -0.122 -0.102 0.039  211 VAL LLL CG2 
11626 N N   . THR H 212 ? 1.860 2.665 1.416 -0.223 -0.159 0.099  212 THR LLL N   
11627 C CA  . THR H 212 ? 1.802 2.580 1.421 -0.256 -0.156 0.140  212 THR LLL CA  
11628 C C   . THR H 212 ? 1.809 2.642 1.418 -0.265 -0.139 0.200  212 THR LLL C   
11629 O O   . THR H 212 ? 1.916 2.815 1.473 -0.245 -0.147 0.214  212 THR LLL O   
11630 C CB  . THR H 212 ? 1.802 2.559 1.450 -0.261 -0.194 0.124  212 THR LLL CB  
11631 O OG1 . THR H 212 ? 1.805 2.517 1.468 -0.252 -0.217 0.070  212 THR LLL OG1 
11632 C CG2 . THR H 212 ? 1.753 2.477 1.475 -0.291 -0.189 0.157  212 THR LLL CG2 
11633 N N   . LYS H 213 ? 1.759 2.568 1.418 -0.290 -0.120 0.233  213 LYS LLL N   
11634 C CA  . LYS H 213 ? 1.778 2.620 1.457 -0.306 -0.112 0.294  213 LYS LLL CA  
11635 C C   . LYS H 213 ? 1.749 2.538 1.491 -0.328 -0.125 0.309  213 LYS LLL C   
11636 O O   . LYS H 213 ? 1.736 2.468 1.509 -0.333 -0.118 0.283  213 LYS LLL O   
11637 C CB  . LYS H 213 ? 1.786 2.646 1.473 -0.310 -0.086 0.315  213 LYS LLL CB  
11638 C CG  . LYS H 213 ? 1.860 2.791 1.491 -0.285 -0.069 0.311  213 LYS LLL CG  
11639 C CD  . LYS H 213 ? 1.909 2.927 1.534 -0.286 -0.058 0.376  213 LYS LLL CD  
11640 C CE  . LYS H 213 ? 1.889 2.913 1.578 -0.311 -0.042 0.422  213 LYS LLL CE  
11641 N NZ  . LYS H 213 ? 1.920 3.046 1.604 -0.304 -0.019 0.477  213 LYS LLL NZ  
11642 N N   . SER H 214 ? 1.792 2.603 1.549 -0.337 -0.141 0.350  214 SER LLL N   
11643 C CA  . SER H 214 ? 1.794 2.561 1.608 -0.350 -0.160 0.359  214 SER LLL CA  
11644 C C   . SER H 214 ? 1.801 2.589 1.641 -0.363 -0.172 0.420  214 SER LLL C   
11645 O O   . SER H 214 ? 1.849 2.696 1.658 -0.361 -0.167 0.459  214 SER LLL O   
11646 C CB  . SER H 214 ? 1.825 2.586 1.637 -0.342 -0.184 0.328  214 SER LLL CB  
11647 O OG  . SER H 214 ? 1.889 2.700 1.665 -0.332 -0.207 0.350  214 SER LLL OG  
11648 N N   . PHE H 215 ? 1.765 2.509 1.663 -0.374 -0.187 0.429  215 PHE LLL N   
11649 C CA  . PHE H 215 ? 1.772 2.521 1.706 -0.385 -0.210 0.482  215 PHE LLL CA  
11650 C C   . PHE H 215 ? 1.776 2.492 1.749 -0.382 -0.235 0.468  215 PHE LLL C   
11651 O O   . PHE H 215 ? 1.750 2.424 1.752 -0.377 -0.227 0.428  215 PHE LLL O   
11652 C CB  . PHE H 215 ? 1.749 2.470 1.732 -0.399 -0.209 0.512  215 PHE LLL CB  
11653 C CG  . PHE H 215 ? 1.710 2.363 1.733 -0.395 -0.207 0.475  215 PHE LLL CG  
11654 C CD1 . PHE H 215 ? 1.659 2.292 1.662 -0.387 -0.182 0.434  215 PHE LLL CD1 
11655 C CD2 . PHE H 215 ? 1.723 2.333 1.799 -0.394 -0.231 0.480  215 PHE LLL CD2 
11656 C CE1 . PHE H 215 ? 1.635 2.211 1.663 -0.376 -0.179 0.403  215 PHE LLL CE1 
11657 C CE2 . PHE H 215 ? 1.688 2.243 1.791 -0.380 -0.227 0.444  215 PHE LLL CE2 
11658 C CZ  . PHE H 215 ? 1.647 2.186 1.722 -0.370 -0.200 0.407  215 PHE LLL CZ  
11659 N N   . ASN H 216 ? 1.834 2.575 1.810 -0.382 -0.262 0.503  216 ASN LLL N   
11660 C CA  . ASN H 216 ? 1.841 2.551 1.873 -0.381 -0.290 0.504  216 ASN LLL CA  
11661 C C   . ASN H 216 ? 1.803 2.470 1.892 -0.390 -0.296 0.532  216 ASN LLL C   
11662 O O   . ASN H 216 ? 1.764 2.441 1.850 -0.402 -0.290 0.569  216 ASN LLL O   
11663 C CB  . ASN H 216 ? 1.921 2.670 1.931 -0.374 -0.322 0.532  216 ASN LLL CB  
11664 C CG  . ASN H 216 ? 1.967 2.756 1.912 -0.359 -0.324 0.498  216 ASN LLL CG  
11665 O OD1 . ASN H 216 ? 1.985 2.797 1.879 -0.354 -0.300 0.481  216 ASN LLL OD1 
11666 N ND2 . ASN H 216 ? 2.010 2.808 1.959 -0.348 -0.358 0.484  216 ASN LLL ND2 
11667 N N   . ARG H 217 ? 1.793 2.416 1.938 -0.382 -0.308 0.513  217 ARG LLL N   
11668 C CA  . ARG H 217 ? 1.807 2.379 2.008 -0.382 -0.324 0.526  217 ARG LLL CA  
11669 C C   . ARG H 217 ? 1.879 2.458 2.107 -0.394 -0.360 0.589  217 ARG LLL C   
11670 O O   . ARG H 217 ? 1.899 2.510 2.114 -0.392 -0.377 0.608  217 ARG LLL O   
11671 C CB  . ARG H 217 ? 1.777 2.313 2.023 -0.361 -0.325 0.486  217 ARG LLL CB  
11672 C CG  . ARG H 217 ? 1.790 2.268 2.075 -0.348 -0.333 0.475  217 ARG LLL CG  
11673 C CD  . ARG H 217 ? 1.795 2.255 2.092 -0.319 -0.309 0.424  217 ARG LLL CD  
11674 N NE  . ARG H 217 ? 1.819 2.303 2.148 -0.310 -0.314 0.418  217 ARG LLL NE  
11675 C CZ  . ARG H 217 ? 1.869 2.340 2.252 -0.294 -0.342 0.423  217 ARG LLL CZ  
11676 N NH1 . ARG H 217 ? 1.897 2.322 2.307 -0.284 -0.372 0.433  217 ARG LLL NH1 
11677 N NH2 . ARG H 217 ? 1.895 2.395 2.313 -0.287 -0.345 0.417  217 ARG LLL NH2 
11678 N N   . GLY H 218 ? 1.937 2.486 2.203 -0.405 -0.374 0.621  218 GLY LLL N   
11679 C CA  . GLY H 218 ? 2.034 2.582 2.340 -0.421 -0.409 0.691  218 GLY LLL CA  
11680 C C   . GLY H 218 ? 2.117 2.730 2.387 -0.441 -0.394 0.752  218 GLY LLL C   
11681 O O   . GLY H 218 ? 2.180 2.811 2.472 -0.453 -0.418 0.822  218 GLY LLL O   
11682 N N   . GLU H 219 ? 2.146 2.796 2.364 -0.443 -0.355 0.731  219 GLU LLL N   
11683 C CA  . GLU H 219 ? 2.185 2.911 2.360 -0.454 -0.331 0.782  219 GLU LLL CA  
11684 C C   . GLU H 219 ? 2.157 2.887 2.327 -0.459 -0.300 0.756  219 GLU LLL C   
11685 O O   . GLU H 219 ? 2.182 2.968 2.343 -0.470 -0.280 0.799  219 GLU LLL O   
11686 C CB  . GLU H 219 ? 2.204 2.990 2.292 -0.435 -0.318 0.770  219 GLU LLL CB  
11687 C CG  . GLU H 219 ? 2.251 3.045 2.337 -0.427 -0.351 0.803  219 GLU LLL CG  
11688 C CD  . GLU H 219 ? 2.257 3.071 2.282 -0.403 -0.357 0.752  219 GLU LLL CD  
11689 O OE1 . GLU H 219 ? 2.243 3.099 2.197 -0.390 -0.333 0.720  219 GLU LLL OE1 
11690 O OE2 . GLU H 219 ? 2.264 3.049 2.319 -0.395 -0.389 0.741  219 GLU LLL OE2 
# 
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   PRO 1   330 ?   ?   ?   AAA . n 
A 1 2   ASN 2   331 ?   ?   ?   AAA . n 
A 1 3   ILE 3   332 ?   ?   ?   AAA . n 
A 1 4   THR 4   333 ?   ?   ?   AAA . n 
A 1 5   ASN 5   334 334 ASN ASN AAA . n 
A 1 6   LEU 6   335 335 LEU LEU AAA . n 
A 1 7   CYS 7   336 336 CYS CYS AAA . n 
A 1 8   PRO 8   337 337 PRO PRO AAA . n 
A 1 9   PHE 9   338 338 PHE PHE AAA . n 
A 1 10  GLY 10  339 339 GLY GLY AAA . n 
A 1 11  GLU 11  340 340 GLU GLU AAA . n 
A 1 12  VAL 12  341 341 VAL VAL AAA . n 
A 1 13  PHE 13  342 342 PHE PHE AAA . n 
A 1 14  ASN 14  343 343 ASN ASN AAA . n 
A 1 15  ALA 15  344 344 ALA ALA AAA . n 
A 1 16  THR 16  345 345 THR THR AAA . n 
A 1 17  ARG 17  346 346 ARG ARG AAA . n 
A 1 18  PHE 18  347 347 PHE PHE AAA . n 
A 1 19  ALA 19  348 348 ALA ALA AAA . n 
A 1 20  SER 20  349 349 SER SER AAA . n 
A 1 21  VAL 21  350 350 VAL VAL AAA . n 
A 1 22  TYR 22  351 351 TYR TYR AAA . n 
A 1 23  ALA 23  352 352 ALA ALA AAA . n 
A 1 24  TRP 24  353 353 TRP TRP AAA . n 
A 1 25  ASN 25  354 354 ASN ASN AAA . n 
A 1 26  ARG 26  355 355 ARG ARG AAA . n 
A 1 27  LYS 27  356 356 LYS LYS AAA . n 
A 1 28  ARG 28  357 357 ARG ARG AAA . n 
A 1 29  ILE 29  358 358 ILE ILE AAA . n 
A 1 30  SER 30  359 359 SER SER AAA . n 
A 1 31  ASN 31  360 360 ASN ASN AAA . n 
A 1 32  CYS 32  361 361 CYS CYS AAA . n 
A 1 33  VAL 33  362 362 VAL VAL AAA . n 
A 1 34  ALA 34  363 363 ALA ALA AAA . n 
A 1 35  ASP 35  364 364 ASP ASP AAA . n 
A 1 36  TYR 36  365 365 TYR TYR AAA . n 
A 1 37  SER 37  366 366 SER SER AAA . n 
A 1 38  VAL 38  367 367 VAL VAL AAA . n 
A 1 39  LEU 39  368 368 LEU LEU AAA . n 
A 1 40  TYR 40  369 369 TYR TYR AAA . n 
A 1 41  ASN 41  370 370 ASN ASN AAA . n 
A 1 42  SER 42  371 371 SER SER AAA . n 
A 1 43  ALA 43  372 372 ALA ALA AAA . n 
A 1 44  SER 44  373 373 SER SER AAA . n 
A 1 45  PHE 45  374 374 PHE PHE AAA . n 
A 1 46  SER 46  375 375 SER SER AAA . n 
A 1 47  THR 47  376 376 THR THR AAA . n 
A 1 48  PHE 48  377 377 PHE PHE AAA . n 
A 1 49  LYS 49  378 378 LYS LYS AAA . n 
A 1 50  CYS 50  379 379 CYS CYS AAA . n 
A 1 51  TYR 51  380 380 TYR TYR AAA . n 
A 1 52  GLY 52  381 381 GLY GLY AAA . n 
A 1 53  VAL 53  382 382 VAL VAL AAA . n 
A 1 54  SER 54  383 383 SER SER AAA . n 
A 1 55  PRO 55  384 384 PRO PRO AAA . n 
A 1 56  THR 56  385 385 THR THR AAA . n 
A 1 57  LYS 57  386 386 LYS LYS AAA . n 
A 1 58  LEU 58  387 387 LEU LEU AAA . n 
A 1 59  ASN 59  388 388 ASN ASN AAA . n 
A 1 60  ASP 60  389 389 ASP ASP AAA . n 
A 1 61  LEU 61  390 390 LEU LEU AAA . n 
A 1 62  CYS 62  391 391 CYS CYS AAA . n 
A 1 63  PHE 63  392 392 PHE PHE AAA . n 
A 1 64  THR 64  393 393 THR THR AAA . n 
A 1 65  ASN 65  394 394 ASN ASN AAA . n 
A 1 66  VAL 66  395 395 VAL VAL AAA . n 
A 1 67  TYR 67  396 396 TYR TYR AAA . n 
A 1 68  ALA 68  397 397 ALA ALA AAA . n 
A 1 69  ASP 69  398 398 ASP ASP AAA . n 
A 1 70  SER 70  399 399 SER SER AAA . n 
A 1 71  PHE 71  400 400 PHE PHE AAA . n 
A 1 72  VAL 72  401 401 VAL VAL AAA . n 
A 1 73  ILE 73  402 402 ILE ILE AAA . n 
A 1 74  ARG 74  403 403 ARG ARG AAA . n 
A 1 75  GLY 75  404 404 GLY GLY AAA . n 
A 1 76  ASP 76  405 405 ASP ASP AAA . n 
A 1 77  GLU 77  406 406 GLU GLU AAA . n 
A 1 78  VAL 78  407 407 VAL VAL AAA . n 
A 1 79  ARG 79  408 408 ARG ARG AAA . n 
A 1 80  GLN 80  409 409 GLN GLN AAA . n 
A 1 81  ILE 81  410 410 ILE ILE AAA . n 
A 1 82  ALA 82  411 411 ALA ALA AAA . n 
A 1 83  PRO 83  412 412 PRO PRO AAA . n 
A 1 84  GLY 84  413 413 GLY GLY AAA . n 
A 1 85  GLN 85  414 414 GLN GLN AAA . n 
A 1 86  THR 86  415 415 THR THR AAA . n 
A 1 87  GLY 87  416 416 GLY GLY AAA . n 
A 1 88  LYS 88  417 417 LYS LYS AAA . n 
A 1 89  ILE 89  418 418 ILE ILE AAA . n 
A 1 90  ALA 90  419 419 ALA ALA AAA . n 
A 1 91  ASP 91  420 420 ASP ASP AAA . n 
A 1 92  TYR 92  421 421 TYR TYR AAA . n 
A 1 93  ASN 93  422 422 ASN ASN AAA . n 
A 1 94  TYR 94  423 423 TYR TYR AAA . n 
A 1 95  LYS 95  424 424 LYS LYS AAA . n 
A 1 96  LEU 96  425 425 LEU LEU AAA . n 
A 1 97  PRO 97  426 426 PRO PRO AAA . n 
A 1 98  ASP 98  427 427 ASP ASP AAA . n 
A 1 99  ASP 99  428 428 ASP ASP AAA . n 
A 1 100 PHE 100 429 429 PHE PHE AAA . n 
A 1 101 THR 101 430 430 THR THR AAA . n 
A 1 102 GLY 102 431 431 GLY GLY AAA . n 
A 1 103 CYS 103 432 432 CYS CYS AAA . n 
A 1 104 VAL 104 433 433 VAL VAL AAA . n 
A 1 105 ILE 105 434 434 ILE ILE AAA . n 
A 1 106 ALA 106 435 435 ALA ALA AAA . n 
A 1 107 TRP 107 436 436 TRP TRP AAA . n 
A 1 108 ASN 108 437 437 ASN ASN AAA . n 
A 1 109 SER 109 438 438 SER SER AAA . n 
A 1 110 ASN 110 439 439 ASN ASN AAA . n 
A 1 111 ASN 111 440 440 ASN ASN AAA . n 
A 1 112 LEU 112 441 441 LEU LEU AAA . n 
A 1 113 ASP 113 442 442 ASP ASP AAA . n 
A 1 114 SER 114 443 443 SER SER AAA . n 
A 1 115 LYS 115 444 444 LYS LYS AAA . n 
A 1 116 VAL 116 445 445 VAL VAL AAA . n 
A 1 117 GLY 117 446 446 GLY GLY AAA . n 
A 1 118 GLY 118 447 447 GLY GLY AAA . n 
A 1 119 ASN 119 448 448 ASN ASN AAA . n 
A 1 120 TYR 120 449 449 TYR TYR AAA . n 
A 1 121 ASN 121 450 450 ASN ASN AAA . n 
A 1 122 TYR 122 451 451 TYR TYR AAA . n 
A 1 123 LEU 123 452 452 LEU LEU AAA . n 
A 1 124 TYR 124 453 453 TYR TYR AAA . n 
A 1 125 ARG 125 454 454 ARG ARG AAA . n 
A 1 126 LEU 126 455 455 LEU LEU AAA . n 
A 1 127 PHE 127 456 456 PHE PHE AAA . n 
A 1 128 ARG 128 457 457 ARG ARG AAA . n 
A 1 129 LYS 129 458 458 LYS LYS AAA . n 
A 1 130 SER 130 459 459 SER SER AAA . n 
A 1 131 ASN 131 460 460 ASN ASN AAA . n 
A 1 132 LEU 132 461 461 LEU LEU AAA . n 
A 1 133 LYS 133 462 462 LYS LYS AAA . n 
A 1 134 PRO 134 463 463 PRO PRO AAA . n 
A 1 135 PHE 135 464 464 PHE PHE AAA . n 
A 1 136 GLU 136 465 465 GLU GLU AAA . n 
A 1 137 ARG 137 466 466 ARG ARG AAA . n 
A 1 138 ASP 138 467 467 ASP ASP AAA . n 
A 1 139 ILE 139 468 468 ILE ILE AAA . n 
A 1 140 SER 140 469 469 SER SER AAA . n 
A 1 141 THR 141 470 470 THR THR AAA . n 
A 1 142 GLU 142 471 471 GLU GLU AAA . n 
A 1 143 ILE 143 472 472 ILE ILE AAA . n 
A 1 144 TYR 144 473 473 TYR TYR AAA . n 
A 1 145 GLN 145 474 474 GLN GLN AAA . n 
A 1 146 ALA 146 475 475 ALA ALA AAA . n 
A 1 147 GLY 147 476 476 GLY GLY AAA . n 
A 1 148 SER 148 477 477 SER SER AAA . n 
A 1 149 THR 149 478 478 THR THR AAA . n 
A 1 150 PRO 150 479 479 PRO PRO AAA . n 
A 1 151 CYS 151 480 480 CYS CYS AAA . n 
A 1 152 ASN 152 481 481 ASN ASN AAA . n 
A 1 153 GLY 153 482 482 GLY GLY AAA . n 
A 1 154 VAL 154 483 483 VAL VAL AAA . n 
A 1 155 GLU 155 484 484 GLU GLU AAA . n 
A 1 156 GLY 156 485 485 GLY GLY AAA . n 
A 1 157 PHE 157 486 486 PHE PHE AAA . n 
A 1 158 ASN 158 487 487 ASN ASN AAA . n 
A 1 159 CYS 159 488 488 CYS CYS AAA . n 
A 1 160 TYR 160 489 489 TYR TYR AAA . n 
A 1 161 PHE 161 490 490 PHE PHE AAA . n 
A 1 162 PRO 162 491 491 PRO PRO AAA . n 
A 1 163 LEU 163 492 492 LEU LEU AAA . n 
A 1 164 GLN 164 493 493 GLN GLN AAA . n 
A 1 165 SER 165 494 494 SER SER AAA . n 
A 1 166 TYR 166 495 495 TYR TYR AAA . n 
A 1 167 GLY 167 496 496 GLY GLY AAA . n 
A 1 168 PHE 168 497 497 PHE PHE AAA . n 
A 1 169 GLN 169 498 498 GLN GLN AAA . n 
A 1 170 PRO 170 499 499 PRO PRO AAA . n 
A 1 171 THR 171 500 500 THR THR AAA . n 
A 1 172 ASN 172 501 501 ASN ASN AAA . n 
A 1 173 GLY 173 502 502 GLY GLY AAA . n 
A 1 174 VAL 174 503 503 VAL VAL AAA . n 
A 1 175 GLY 175 504 504 GLY GLY AAA . n 
A 1 176 TYR 176 505 505 TYR TYR AAA . n 
A 1 177 GLN 177 506 506 GLN GLN AAA . n 
A 1 178 PRO 178 507 507 PRO PRO AAA . n 
A 1 179 TYR 179 508 508 TYR TYR AAA . n 
A 1 180 ARG 180 509 509 ARG ARG AAA . n 
A 1 181 VAL 181 510 510 VAL VAL AAA . n 
A 1 182 VAL 182 511 511 VAL VAL AAA . n 
A 1 183 VAL 183 512 512 VAL VAL AAA . n 
A 1 184 LEU 184 513 513 LEU LEU AAA . n 
A 1 185 SER 185 514 514 SER SER AAA . n 
A 1 186 PHE 186 515 515 PHE PHE AAA . n 
A 1 187 GLU 187 516 516 GLU GLU AAA . n 
A 1 188 LEU 188 517 517 LEU LEU AAA . n 
A 1 189 LEU 189 518 518 LEU LEU AAA . n 
A 1 190 HIS 190 519 519 HIS HIS AAA . n 
A 1 191 ALA 191 520 520 ALA ALA AAA . n 
A 1 192 PRO 192 521 521 PRO PRO AAA . n 
A 1 193 ALA 193 522 522 ALA ALA AAA . n 
A 1 194 THR 194 523 523 THR THR AAA . n 
A 1 195 VAL 195 524 524 VAL VAL AAA . n 
A 1 196 CYS 196 525 525 CYS CYS AAA . n 
A 1 197 GLY 197 526 526 GLY GLY AAA . n 
A 1 198 PRO 198 527 527 PRO PRO AAA . n 
A 1 199 LYS 199 528 528 LYS LYS AAA . n 
A 1 200 LYS 200 529 ?   ?   ?   AAA . n 
A 1 201 SER 201 530 ?   ?   ?   AAA . n 
A 1 202 THR 202 531 ?   ?   ?   AAA . n 
A 1 203 ASN 203 532 ?   ?   ?   AAA . n 
A 1 204 LYS 204 533 ?   ?   ?   AAA . n 
A 1 205 HIS 205 534 ?   ?   ?   AAA . n 
A 1 206 HIS 206 535 ?   ?   ?   AAA . n 
A 1 207 HIS 207 536 ?   ?   ?   AAA . n 
A 1 208 HIS 208 537 ?   ?   ?   AAA . n 
A 1 209 HIS 209 538 ?   ?   ?   AAA . n 
A 1 210 HIS 210 539 ?   ?   ?   AAA . n 
B 2 1   THR 1   0   0   THR THR BBB . n 
B 2 2   GLN 2   1   1   GLN GLN BBB . n 
B 2 3   MET 3   2   2   MET MET BBB . n 
B 2 4   GLN 4   3   3   GLN GLN BBB . n 
B 2 5   LEU 5   4   4   LEU LEU BBB . n 
B 2 6   VAL 6   5   5   VAL VAL BBB . n 
B 2 7   GLN 7   6   6   GLN GLN BBB . n 
B 2 8   SER 8   7   7   SER SER BBB . n 
B 2 9   GLY 9   8   8   GLY GLY BBB . n 
B 2 10  THR 10  9   9   THR THR BBB . n 
B 2 11  GLU 11  10  10  GLU GLU BBB . n 
B 2 12  VAL 12  11  11  VAL VAL BBB . n 
B 2 13  LYS 13  12  12  LYS LYS BBB . n 
B 2 14  LYS 14  13  13  LYS LYS BBB . n 
B 2 15  PRO 15  14  14  PRO PRO BBB . n 
B 2 16  GLY 16  15  15  GLY GLY BBB . n 
B 2 17  GLU 17  16  16  GLU GLU BBB . n 
B 2 18  SER 18  17  17  SER SER BBB . n 
B 2 19  LEU 19  18  18  LEU LEU BBB . n 
B 2 20  LYS 20  19  19  LYS LYS BBB . n 
B 2 21  ILE 21  20  20  ILE ILE BBB . n 
B 2 22  SER 22  21  21  SER SER BBB . n 
B 2 23  CYS 23  22  22  CYS CYS BBB . n 
B 2 24  LYS 24  23  23  LYS LYS BBB . n 
B 2 25  GLY 25  24  24  GLY GLY BBB . n 
B 2 26  SER 26  25  25  SER SER BBB . n 
B 2 27  GLY 27  26  26  GLY GLY BBB . n 
B 2 28  TYR 28  27  27  TYR TYR BBB . n 
B 2 29  GLY 29  28  28  GLY GLY BBB . n 
B 2 30  PHE 30  29  29  PHE PHE BBB . n 
B 2 31  ILE 31  30  30  ILE ILE BBB . n 
B 2 32  THR 32  31  31  THR THR BBB . n 
B 2 33  TYR 33  32  32  TYR TYR BBB . n 
B 2 34  TRP 34  33  33  TRP TRP BBB . n 
B 2 35  ILE 35  34  34  ILE ILE BBB . n 
B 2 36  GLY 36  35  35  GLY GLY BBB . n 
B 2 37  TRP 37  36  36  TRP TRP BBB . n 
B 2 38  VAL 38  37  37  VAL VAL BBB . n 
B 2 39  ARG 39  38  38  ARG ARG BBB . n 
B 2 40  GLN 40  39  39  GLN GLN BBB . n 
B 2 41  MET 41  40  40  MET MET BBB . n 
B 2 42  PRO 42  41  41  PRO PRO BBB . n 
B 2 43  GLY 43  42  42  GLY GLY BBB . n 
B 2 44  LYS 44  43  43  LYS LYS BBB . n 
B 2 45  GLY 45  44  44  GLY GLY BBB . n 
B 2 46  LEU 46  45  45  LEU LEU BBB . n 
B 2 47  GLU 47  46  46  GLU GLU BBB . n 
B 2 48  TRP 48  47  47  TRP TRP BBB . n 
B 2 49  MET 49  48  48  MET MET BBB . n 
B 2 50  GLY 50  49  49  GLY GLY BBB . n 
B 2 51  ILE 51  50  50  ILE ILE BBB . n 
B 2 52  ILE 52  51  51  ILE ILE BBB . n 
B 2 53  TYR 53  52  52  TYR TYR BBB . n 
B 2 54  PRO 54  53  53  PRO PRO BBB . n 
B 2 55  GLY 55  54  54  GLY GLY BBB . n 
B 2 56  ASP 56  55  55  ASP ASP BBB . n 
B 2 57  SER 57  56  56  SER SER BBB . n 
B 2 58  GLU 58  57  57  GLU GLU BBB . n 
B 2 59  THR 59  58  58  THR THR BBB . n 
B 2 60  ARG 60  59  59  ARG ARG BBB . n 
B 2 61  TYR 61  60  60  TYR TYR BBB . n 
B 2 62  SER 62  61  61  SER SER BBB . n 
B 2 63  PRO 63  62  62  PRO PRO BBB . n 
B 2 64  SER 64  63  63  SER SER BBB . n 
B 2 65  PHE 65  64  64  PHE PHE BBB . n 
B 2 66  GLN 66  65  65  GLN GLN BBB . n 
B 2 67  GLY 67  66  66  GLY GLY BBB . n 
B 2 68  GLN 68  67  67  GLN GLN BBB . n 
B 2 69  VAL 69  68  68  VAL VAL BBB . n 
B 2 70  THR 70  69  69  THR THR BBB . n 
B 2 71  ILE 71  70  70  ILE ILE BBB . n 
B 2 72  SER 72  71  71  SER SER BBB . n 
B 2 73  ALA 73  72  72  ALA ALA BBB . n 
B 2 74  ASP 74  73  73  ASP ASP BBB . n 
B 2 75  LYS 75  74  74  LYS LYS BBB . n 
B 2 76  SER 76  75  75  SER SER BBB . n 
B 2 77  ILE 77  76  76  ILE ILE BBB . n 
B 2 78  ASN 78  77  77  ASN ASN BBB . n 
B 2 79  THR 79  78  78  THR THR BBB . n 
B 2 80  ALA 80  79  79  ALA ALA BBB . n 
B 2 81  TYR 81  80  80  TYR TYR BBB . n 
B 2 82  LEU 82  81  81  LEU LEU BBB . n 
B 2 83  GLN 83  82  82  GLN GLN BBB . n 
B 2 84  TRP 84  83  83  TRP TRP BBB . n 
B 2 85  SER 85  84  84  SER SER BBB . n 
B 2 86  SER 86  85  85  SER SER BBB . n 
B 2 87  LEU 87  86  86  LEU LEU BBB . n 
B 2 88  LYS 88  87  87  LYS LYS BBB . n 
B 2 89  ALA 89  88  88  ALA ALA BBB . n 
B 2 90  SER 90  89  89  SER SER BBB . n 
B 2 91  ASP 91  90  90  ASP ASP BBB . n 
B 2 92  THR 92  91  91  THR THR BBB . n 
B 2 93  ALA 93  92  92  ALA ALA BBB . n 
B 2 94  ILE 94  93  93  ILE ILE BBB . n 
B 2 95  TYR 95  94  94  TYR TYR BBB . n 
B 2 96  TYR 96  95  95  TYR TYR BBB . n 
B 2 97  CYS 97  96  96  CYS CYS BBB . n 
B 2 98  ALA 98  97  97  ALA ALA BBB . n 
B 2 99  GLY 99  98  98  GLY GLY BBB . n 
B 2 100 GLY 100 99  99  GLY GLY BBB . n 
B 2 101 SER 101 100 100 SER SER BBB . n 
B 2 102 GLY 102 101 101 GLY GLY BBB . n 
B 2 103 ILE 103 102 102 ILE ILE BBB . n 
B 2 104 SER 104 103 103 SER SER BBB . n 
B 2 105 THR 105 104 104 THR THR BBB . n 
B 2 106 PRO 106 105 105 PRO PRO BBB . n 
B 2 107 MET 107 106 106 MET MET BBB . n 
B 2 108 ASP 108 107 107 ASP ASP BBB . n 
B 2 109 VAL 109 108 108 VAL VAL BBB . n 
B 2 110 TRP 110 109 109 TRP TRP BBB . n 
B 2 111 GLY 111 110 110 GLY GLY BBB . n 
B 2 112 GLN 112 111 111 GLN GLN BBB . n 
B 2 113 GLY 113 112 112 GLY GLY BBB . n 
B 2 114 THR 114 113 113 THR THR BBB . n 
B 2 115 THR 115 114 114 THR THR BBB . n 
B 2 116 VAL 116 115 115 VAL VAL BBB . n 
B 2 117 THR 117 116 116 THR THR BBB . n 
B 2 118 VAL 118 117 117 VAL VAL BBB . n 
B 2 119 ALA 119 118 118 ALA ALA BBB . n 
B 2 120 SER 120 119 119 SER SER BBB . n 
B 2 121 THR 121 120 120 THR THR BBB . n 
B 2 122 LYS 122 121 121 LYS LYS BBB . n 
B 2 123 GLY 123 122 122 GLY GLY BBB . n 
B 2 124 PRO 124 123 123 PRO PRO BBB . n 
B 2 125 SER 125 124 124 SER SER BBB . n 
B 2 126 VAL 126 125 125 VAL VAL BBB . n 
B 2 127 PHE 127 126 126 PHE PHE BBB . n 
B 2 128 PRO 128 127 127 PRO PRO BBB . n 
B 2 129 LEU 129 128 128 LEU LEU BBB . n 
B 2 130 ALA 130 129 129 ALA ALA BBB . n 
B 2 131 PRO 131 130 130 PRO PRO BBB . n 
B 2 132 SER 132 131 131 SER SER BBB . n 
B 2 133 SER 133 132 132 SER SER BBB . n 
B 2 134 LYS 134 133 ?   ?   ?   BBB . n 
B 2 135 SER 135 134 ?   ?   ?   BBB . n 
B 2 136 THR 136 135 ?   ?   ?   BBB . n 
B 2 137 SER 137 136 ?   ?   ?   BBB . n 
B 2 138 GLY 138 137 137 GLY GLY BBB . n 
B 2 139 GLY 139 138 138 GLY GLY BBB . n 
B 2 140 THR 140 139 139 THR THR BBB . n 
B 2 141 ALA 141 140 140 ALA ALA BBB . n 
B 2 142 ALA 142 141 141 ALA ALA BBB . n 
B 2 143 LEU 143 142 142 LEU LEU BBB . n 
B 2 144 GLY 144 143 143 GLY GLY BBB . n 
B 2 145 CYS 145 144 144 CYS CYS BBB . n 
B 2 146 LEU 146 145 145 LEU LEU BBB . n 
B 2 147 VAL 147 146 146 VAL VAL BBB . n 
B 2 148 LYS 148 147 147 LYS LYS BBB . n 
B 2 149 ASP 149 148 148 ASP ASP BBB . n 
B 2 150 TYR 150 149 149 TYR TYR BBB . n 
B 2 151 PHE 151 150 150 PHE PHE BBB . n 
B 2 152 PRO 152 151 151 PRO PRO BBB . n 
B 2 153 GLU 153 152 152 GLU GLU BBB . n 
B 2 154 PRO 154 153 153 PRO PRO BBB . n 
B 2 155 VAL 155 154 154 VAL VAL BBB . n 
B 2 156 THR 156 155 155 THR THR BBB . n 
B 2 157 VAL 157 156 156 VAL VAL BBB . n 
B 2 158 SER 158 157 157 SER SER BBB . n 
B 2 159 TRP 159 158 158 TRP TRP BBB . n 
B 2 160 ASN 160 159 159 ASN ASN BBB . n 
B 2 161 SER 161 160 160 SER SER BBB . n 
B 2 162 GLY 162 161 161 GLY GLY BBB . n 
B 2 163 ALA 163 162 162 ALA ALA BBB . n 
B 2 164 LEU 164 163 163 LEU LEU BBB . n 
B 2 165 THR 165 164 164 THR THR BBB . n 
B 2 166 SER 166 165 165 SER SER BBB . n 
B 2 167 GLY 167 166 166 GLY GLY BBB . n 
B 2 168 VAL 168 167 167 VAL VAL BBB . n 
B 2 169 HIS 169 168 168 HIS HIS BBB . n 
B 2 170 THR 170 169 169 THR THR BBB . n 
B 2 171 PHE 171 170 170 PHE PHE BBB . n 
B 2 172 PRO 172 171 171 PRO PRO BBB . n 
B 2 173 ALA 173 172 172 ALA ALA BBB . n 
B 2 174 VAL 174 173 173 VAL VAL BBB . n 
B 2 175 LEU 175 174 174 LEU LEU BBB . n 
B 2 176 GLN 176 175 175 GLN GLN BBB . n 
B 2 177 SER 177 176 176 SER SER BBB . n 
B 2 178 SER 178 177 177 SER SER BBB . n 
B 2 179 GLY 179 178 178 GLY GLY BBB . n 
B 2 180 LEU 180 179 179 LEU LEU BBB . n 
B 2 181 TYR 181 180 180 TYR TYR BBB . n 
B 2 182 SER 182 181 181 SER SER BBB . n 
B 2 183 LEU 183 182 182 LEU LEU BBB . n 
B 2 184 SER 184 183 183 SER SER BBB . n 
B 2 185 SER 185 184 184 SER SER BBB . n 
B 2 186 VAL 186 185 185 VAL VAL BBB . n 
B 2 187 VAL 187 186 186 VAL VAL BBB . n 
B 2 188 THR 188 187 187 THR THR BBB . n 
B 2 189 VAL 189 188 188 VAL VAL BBB . n 
B 2 190 PRO 190 189 189 PRO PRO BBB . n 
B 2 191 SER 191 190 190 SER SER BBB . n 
B 2 192 SER 192 191 191 SER SER BBB . n 
B 2 193 SER 193 192 192 SER SER BBB . n 
B 2 194 LEU 194 193 193 LEU LEU BBB . n 
B 2 195 GLY 195 194 194 GLY GLY BBB . n 
B 2 196 THR 196 195 195 THR THR BBB . n 
B 2 197 GLN 197 196 196 GLN GLN BBB . n 
B 2 198 THR 198 197 197 THR THR BBB . n 
B 2 199 TYR 199 198 198 TYR TYR BBB . n 
B 2 200 ILE 200 199 199 ILE ILE BBB . n 
B 2 201 CYS 201 200 200 CYS CYS BBB . n 
B 2 202 ASN 202 201 201 ASN ASN BBB . n 
B 2 203 VAL 203 202 202 VAL VAL BBB . n 
B 2 204 ASN 204 203 203 ASN ASN BBB . n 
B 2 205 HIS 205 204 204 HIS HIS BBB . n 
B 2 206 LYS 206 205 205 LYS LYS BBB . n 
B 2 207 PRO 207 206 206 PRO PRO BBB . n 
B 2 208 SER 208 207 207 SER SER BBB . n 
B 2 209 ASN 209 208 208 ASN ASN BBB . n 
B 2 210 THR 210 209 209 THR THR BBB . n 
B 2 211 LYS 211 210 210 LYS LYS BBB . n 
B 2 212 VAL 212 211 211 VAL VAL BBB . n 
B 2 213 ASP 213 212 212 ASP ASP BBB . n 
B 2 214 LYS 214 213 213 LYS LYS BBB . n 
B 2 215 LYS 215 214 214 LYS LYS BBB . n 
B 2 216 VAL 216 215 215 VAL VAL BBB . n 
B 2 217 GLU 217 216 216 GLU GLU BBB . n 
B 2 218 PRO 218 217 217 PRO PRO BBB . n 
B 2 219 LYS 219 218 218 LYS LYS BBB . n 
B 2 220 SER 220 219 219 SER SER BBB . n 
B 2 221 CYS 221 220 ?   ?   ?   BBB . n 
B 2 222 ASP 222 221 ?   ?   ?   BBB . n 
B 2 223 LYS 223 222 ?   ?   ?   BBB . n 
B 2 224 HIS 224 223 ?   ?   ?   BBB . n 
B 2 225 HIS 225 224 ?   ?   ?   BBB . n 
B 2 226 HIS 226 225 ?   ?   ?   BBB . n 
B 2 227 HIS 227 226 ?   ?   ?   BBB . n 
B 2 228 HIS 228 227 ?   ?   ?   BBB . n 
B 2 229 HIS 229 228 ?   ?   ?   BBB . n 
C 3 1   ASP 1   1   1   ASP ASP CCC . n 
C 3 2   ILE 2   2   2   ILE ILE CCC . n 
C 3 3   GLN 3   3   3   GLN GLN CCC . n 
C 3 4   LEU 4   4   4   LEU LEU CCC . n 
C 3 5   THR 5   5   5   THR THR CCC . n 
C 3 6   GLN 6   6   6   GLN GLN CCC . n 
C 3 7   SER 7   7   7   SER SER CCC . n 
C 3 8   PRO 8   8   8   PRO PRO CCC . n 
C 3 9   ASP 9   9   9   ASP ASP CCC . n 
C 3 10  SER 10  10  10  SER SER CCC . n 
C 3 11  LEU 11  11  11  LEU LEU CCC . n 
C 3 12  ALA 12  12  12  ALA ALA CCC . n 
C 3 13  VAL 13  13  13  VAL VAL CCC . n 
C 3 14  SER 14  14  14  SER SER CCC . n 
C 3 15  LEU 15  15  15  LEU LEU CCC . n 
C 3 16  GLY 16  16  16  GLY GLY CCC . n 
C 3 17  GLU 17  17  17  GLU GLU CCC . n 
C 3 18  ARG 18  18  18  ARG ARG CCC . n 
C 3 19  ALA 19  19  19  ALA ALA CCC . n 
C 3 20  THR 20  20  20  THR THR CCC . n 
C 3 21  ILE 21  21  21  ILE ILE CCC . n 
C 3 22  ASN 22  22  22  ASN ASN CCC . n 
C 3 23  CYS 23  23  23  CYS CYS CCC . n 
C 3 24  LYS 24  24  24  LYS LYS CCC . n 
C 3 25  SER 25  25  25  SER SER CCC . n 
C 3 26  SER 26  26  26  SER SER CCC . n 
C 3 27  GLN 27  27  27  GLN GLN CCC . n 
C 3 28  SER 28  28  28  SER SER CCC . n 
C 3 29  VAL 29  29  29  VAL VAL CCC . n 
C 3 30  LEU 30  30  30  LEU LEU CCC . n 
C 3 31  TYR 31  31  31  TYR TYR CCC . n 
C 3 32  SER 32  32  32  SER SER CCC . n 
C 3 33  SER 33  33  33  SER SER CCC . n 
C 3 34  ILE 34  34  34  ILE ILE CCC . n 
C 3 35  ASN 35  35  35  ASN ASN CCC . n 
C 3 36  LYS 36  36  36  LYS LYS CCC . n 
C 3 37  ASN 37  37  37  ASN ASN CCC . n 
C 3 38  TYR 38  38  38  TYR TYR CCC . n 
C 3 39  LEU 39  39  39  LEU LEU CCC . n 
C 3 40  ALA 40  40  40  ALA ALA CCC . n 
C 3 41  TRP 41  41  41  TRP TRP CCC . n 
C 3 42  TYR 42  42  42  TYR TYR CCC . n 
C 3 43  GLN 43  43  43  GLN GLN CCC . n 
C 3 44  GLN 44  44  44  GLN GLN CCC . n 
C 3 45  LYS 45  45  45  LYS LYS CCC . n 
C 3 46  PRO 46  46  46  PRO PRO CCC . n 
C 3 47  GLY 47  47  47  GLY GLY CCC . n 
C 3 48  GLN 48  48  48  GLN GLN CCC . n 
C 3 49  PRO 49  49  49  PRO PRO CCC . n 
C 3 50  PRO 50  50  50  PRO PRO CCC . n 
C 3 51  LYS 51  51  51  LYS LYS CCC . n 
C 3 52  LEU 52  52  52  LEU LEU CCC . n 
C 3 53  LEU 53  53  53  LEU LEU CCC . n 
C 3 54  ILE 54  54  54  ILE ILE CCC . n 
C 3 55  TYR 55  55  55  TYR TYR CCC . n 
C 3 56  TRP 56  56  56  TRP TRP CCC . n 
C 3 57  ALA 57  57  57  ALA ALA CCC . n 
C 3 58  SER 58  58  58  SER SER CCC . n 
C 3 59  THR 59  59  59  THR THR CCC . n 
C 3 60  ARG 60  60  60  ARG ARG CCC . n 
C 3 61  GLU 61  61  61  GLU GLU CCC . n 
C 3 62  SER 62  62  62  SER SER CCC . n 
C 3 63  GLY 63  63  63  GLY GLY CCC . n 
C 3 64  VAL 64  64  64  VAL VAL CCC . n 
C 3 65  PRO 65  65  65  PRO PRO CCC . n 
C 3 66  ASP 66  66  66  ASP ASP CCC . n 
C 3 67  ARG 67  67  67  ARG ARG CCC . n 
C 3 68  PHE 68  68  68  PHE PHE CCC . n 
C 3 69  SER 69  69  69  SER SER CCC . n 
C 3 70  GLY 70  70  70  GLY GLY CCC . n 
C 3 71  SER 71  71  71  SER SER CCC . n 
C 3 72  GLY 72  72  72  GLY GLY CCC . n 
C 3 73  SER 73  73  73  SER SER CCC . n 
C 3 74  GLY 74  74  74  GLY GLY CCC . n 
C 3 75  THR 75  75  75  THR THR CCC . n 
C 3 76  ASP 76  76  76  ASP ASP CCC . n 
C 3 77  PHE 77  77  77  PHE PHE CCC . n 
C 3 78  THR 78  78  78  THR THR CCC . n 
C 3 79  LEU 79  79  79  LEU LEU CCC . n 
C 3 80  THR 80  80  80  THR THR CCC . n 
C 3 81  ILE 81  81  81  ILE ILE CCC . n 
C 3 82  SER 82  82  82  SER SER CCC . n 
C 3 83  SER 83  83  83  SER SER CCC . n 
C 3 84  LEU 84  84  84  LEU LEU CCC . n 
C 3 85  GLN 85  85  85  GLN GLN CCC . n 
C 3 86  ALA 86  86  86  ALA ALA CCC . n 
C 3 87  GLU 87  87  87  GLU GLU CCC . n 
C 3 88  ASP 88  88  88  ASP ASP CCC . n 
C 3 89  VAL 89  89  89  VAL VAL CCC . n 
C 3 90  ALA 90  90  90  ALA ALA CCC . n 
C 3 91  VAL 91  91  91  VAL VAL CCC . n 
C 3 92  TYR 92  92  92  TYR TYR CCC . n 
C 3 93  TYR 93  93  93  TYR TYR CCC . n 
C 3 94  CYS 94  94  94  CYS CYS CCC . n 
C 3 95  GLN 95  95  95  GLN GLN CCC . n 
C 3 96  GLN 96  96  96  GLN GLN CCC . n 
C 3 97  TYR 97  97  97  TYR TYR CCC . n 
C 3 98  TYR 98  98  98  TYR TYR CCC . n 
C 3 99  SER 99  99  99  SER SER CCC . n 
C 3 100 THR 100 100 100 THR THR CCC . n 
C 3 101 PRO 101 101 101 PRO PRO CCC . n 
C 3 102 TYR 102 102 102 TYR TYR CCC . n 
C 3 103 THR 103 103 103 THR THR CCC . n 
C 3 104 PHE 104 104 104 PHE PHE CCC . n 
C 3 105 GLY 105 105 105 GLY GLY CCC . n 
C 3 106 GLN 106 106 106 GLN GLN CCC . n 
C 3 107 GLY 107 107 107 GLY GLY CCC . n 
C 3 108 THR 108 108 108 THR THR CCC . n 
C 3 109 LYS 109 109 109 LYS LYS CCC . n 
C 3 110 VAL 110 110 110 VAL VAL CCC . n 
C 3 111 GLU 111 111 111 GLU GLU CCC . n 
C 3 112 ILE 112 112 112 ILE ILE CCC . n 
C 3 113 LYS 113 113 113 LYS LYS CCC . n 
C 3 114 ARG 114 114 114 ARG ARG CCC . n 
C 3 115 THR 115 115 115 THR THR CCC . n 
C 3 116 VAL 116 116 116 VAL VAL CCC . n 
C 3 117 ALA 117 117 117 ALA ALA CCC . n 
C 3 118 ALA 118 118 118 ALA ALA CCC . n 
C 3 119 PRO 119 119 119 PRO PRO CCC . n 
C 3 120 SER 120 120 120 SER SER CCC . n 
C 3 121 VAL 121 121 121 VAL VAL CCC . n 
C 3 122 PHE 122 122 122 PHE PHE CCC . n 
C 3 123 ILE 123 123 123 ILE ILE CCC . n 
C 3 124 PHE 124 124 124 PHE PHE CCC . n 
C 3 125 PRO 125 125 125 PRO PRO CCC . n 
C 3 126 PRO 126 126 126 PRO PRO CCC . n 
C 3 127 SER 127 127 127 SER SER CCC . n 
C 3 128 ASP 128 128 128 ASP ASP CCC . n 
C 3 129 GLU 129 129 129 GLU GLU CCC . n 
C 3 130 GLN 130 130 130 GLN GLN CCC . n 
C 3 131 LEU 131 131 131 LEU LEU CCC . n 
C 3 132 LYS 132 132 132 LYS LYS CCC . n 
C 3 133 SER 133 133 133 SER SER CCC . n 
C 3 134 GLY 134 134 134 GLY GLY CCC . n 
C 3 135 THR 135 135 135 THR THR CCC . n 
C 3 136 ALA 136 136 136 ALA ALA CCC . n 
C 3 137 SER 137 137 137 SER SER CCC . n 
C 3 138 VAL 138 138 138 VAL VAL CCC . n 
C 3 139 VAL 139 139 139 VAL VAL CCC . n 
C 3 140 CYS 140 140 140 CYS CYS CCC . n 
C 3 141 LEU 141 141 141 LEU LEU CCC . n 
C 3 142 LEU 142 142 142 LEU LEU CCC . n 
C 3 143 ASN 143 143 143 ASN ASN CCC . n 
C 3 144 ASN 144 144 144 ASN ASN CCC . n 
C 3 145 PHE 145 145 145 PHE PHE CCC . n 
C 3 146 TYR 146 146 146 TYR TYR CCC . n 
C 3 147 PRO 147 147 147 PRO PRO CCC . n 
C 3 148 ARG 148 148 148 ARG ARG CCC . n 
C 3 149 GLU 149 149 149 GLU GLU CCC . n 
C 3 150 ALA 150 150 150 ALA ALA CCC . n 
C 3 151 LYS 151 151 151 LYS LYS CCC . n 
C 3 152 VAL 152 152 152 VAL VAL CCC . n 
C 3 153 GLN 153 153 153 GLN GLN CCC . n 
C 3 154 TRP 154 154 154 TRP TRP CCC . n 
C 3 155 LYS 155 155 155 LYS LYS CCC . n 
C 3 156 VAL 156 156 156 VAL VAL CCC . n 
C 3 157 ASP 157 157 157 ASP ASP CCC . n 
C 3 158 ASN 158 158 158 ASN ASN CCC . n 
C 3 159 ALA 159 159 159 ALA ALA CCC . n 
C 3 160 LEU 160 160 160 LEU LEU CCC . n 
C 3 161 GLN 161 161 161 GLN GLN CCC . n 
C 3 162 SER 162 162 162 SER SER CCC . n 
C 3 163 GLY 163 163 163 GLY GLY CCC . n 
C 3 164 ASN 164 164 164 ASN ASN CCC . n 
C 3 165 SER 165 165 165 SER SER CCC . n 
C 3 166 GLN 166 166 166 GLN GLN CCC . n 
C 3 167 GLU 167 167 167 GLU GLU CCC . n 
C 3 168 SER 168 168 168 SER SER CCC . n 
C 3 169 VAL 169 169 169 VAL VAL CCC . n 
C 3 170 THR 170 170 170 THR THR CCC . n 
C 3 171 GLU 171 171 171 GLU GLU CCC . n 
C 3 172 GLN 172 172 172 GLN GLN CCC . n 
C 3 173 ASP 173 173 173 ASP ASP CCC . n 
C 3 174 SER 174 174 174 SER SER CCC . n 
C 3 175 LYS 175 175 175 LYS LYS CCC . n 
C 3 176 ASP 176 176 176 ASP ASP CCC . n 
C 3 177 SER 177 177 177 SER SER CCC . n 
C 3 178 THR 178 178 178 THR THR CCC . n 
C 3 179 TYR 179 179 179 TYR TYR CCC . n 
C 3 180 SER 180 180 180 SER SER CCC . n 
C 3 181 LEU 181 181 181 LEU LEU CCC . n 
C 3 182 SER 182 182 182 SER SER CCC . n 
C 3 183 SER 183 183 183 SER SER CCC . n 
C 3 184 THR 184 184 184 THR THR CCC . n 
C 3 185 LEU 185 185 185 LEU LEU CCC . n 
C 3 186 THR 186 186 186 THR THR CCC . n 
C 3 187 LEU 187 187 187 LEU LEU CCC . n 
C 3 188 SER 188 188 188 SER SER CCC . n 
C 3 189 LYS 189 189 189 LYS LYS CCC . n 
C 3 190 ALA 190 190 190 ALA ALA CCC . n 
C 3 191 ASP 191 191 191 ASP ASP CCC . n 
C 3 192 TYR 192 192 192 TYR TYR CCC . n 
C 3 193 GLU 193 193 193 GLU GLU CCC . n 
C 3 194 LYS 194 194 194 LYS LYS CCC . n 
C 3 195 HIS 195 195 195 HIS HIS CCC . n 
C 3 196 LYS 196 196 196 LYS LYS CCC . n 
C 3 197 VAL 197 197 197 VAL VAL CCC . n 
C 3 198 TYR 198 198 198 TYR TYR CCC . n 
C 3 199 ALA 199 199 199 ALA ALA CCC . n 
C 3 200 CYS 200 200 200 CYS CYS CCC . n 
C 3 201 GLU 201 201 201 GLU GLU CCC . n 
C 3 202 VAL 202 202 202 VAL VAL CCC . n 
C 3 203 THR 203 203 203 THR THR CCC . n 
C 3 204 HIS 204 204 204 HIS HIS CCC . n 
C 3 205 GLN 205 205 205 GLN GLN CCC . n 
C 3 206 GLY 206 206 206 GLY GLY CCC . n 
C 3 207 LEU 207 207 207 LEU LEU CCC . n 
C 3 208 SER 208 208 208 SER SER CCC . n 
C 3 209 SER 209 209 209 SER SER CCC . n 
C 3 210 PRO 210 210 210 PRO PRO CCC . n 
C 3 211 VAL 211 211 211 VAL VAL CCC . n 
C 3 212 THR 212 212 212 THR THR CCC . n 
C 3 213 LYS 213 213 213 LYS LYS CCC . n 
C 3 214 SER 214 214 214 SER SER CCC . n 
C 3 215 PHE 215 215 215 PHE PHE CCC . n 
C 3 216 ASN 216 216 216 ASN ASN CCC . n 
C 3 217 ARG 217 217 217 ARG ARG CCC . n 
C 3 218 GLY 218 218 218 GLY GLY CCC . n 
C 3 219 GLU 219 219 219 GLU GLU CCC . n 
C 3 220 CYS 220 220 ?   ?   ?   CCC . n 
D 4 1   GLN 1   1   1   GLN GLN DDD . n 
D 4 2   VAL 2   2   2   VAL VAL DDD . n 
D 4 3   GLN 3   3   3   GLN GLN DDD . n 
D 4 4   LEU 4   4   4   LEU LEU DDD . n 
D 4 5   VAL 5   5   5   VAL VAL DDD . n 
D 4 6   GLU 6   6   6   GLU GLU DDD . n 
D 4 7   SER 7   7   7   SER SER DDD . n 
D 4 8   GLY 8   8   8   GLY GLY DDD . n 
D 4 9   GLY 9   9   9   GLY GLY DDD . n 
D 4 10  GLY 10  10  10  GLY GLY DDD . n 
D 4 11  LEU 11  11  11  LEU LEU DDD . n 
D 4 12  MET 12  12  12  MET MET DDD . n 
D 4 13  GLN 13  13  13  GLN GLN DDD . n 
D 4 14  ALA 14  14  14  ALA ALA DDD . n 
D 4 15  GLY 15  15  15  GLY GLY DDD . n 
D 4 16  GLY 16  16  16  GLY GLY DDD . n 
D 4 17  SER 17  17  17  SER SER DDD . n 
D 4 18  LEU 18  18  18  LEU LEU DDD . n 
D 4 19  ARG 19  19  19  ARG ARG DDD . n 
D 4 20  LEU 20  20  20  LEU LEU DDD . n 
D 4 21  SER 21  21  21  SER SER DDD . n 
D 4 22  CYS 22  22  22  CYS CYS DDD . n 
D 4 23  ALA 23  23  23  ALA ALA DDD . n 
D 4 24  VAL 24  24  24  VAL VAL DDD . n 
D 4 25  SER 25  25  25  SER SER DDD . n 
D 4 26  GLY 26  26  26  GLY GLY DDD . n 
D 4 27  ARG 27  27  27  ARG ARG DDD . n 
D 4 28  THR 28  28  28  THR THR DDD . n 
D 4 29  PHE 29  29  29  PHE PHE DDD . n 
D 4 30  SER 30  30  30  SER SER DDD . n 
D 4 31  THR 31  31  31  THR THR DDD . n 
D 4 32  ALA 32  32  32  ALA ALA DDD . n 
D 4 33  ALA 33  33  33  ALA ALA DDD . n 
D 4 34  MET 34  34  34  MET MET DDD . n 
D 4 35  GLY 35  35  35  GLY GLY DDD . n 
D 4 36  TRP 36  36  36  TRP TRP DDD . n 
D 4 37  PHE 37  37  37  PHE PHE DDD . n 
D 4 38  ARG 38  38  38  ARG ARG DDD . n 
D 4 39  GLN 39  39  39  GLN GLN DDD . n 
D 4 40  ALA 40  40  40  ALA ALA DDD . n 
D 4 41  PRO 41  41  41  PRO PRO DDD . n 
D 4 42  GLY 42  42  42  GLY GLY DDD . n 
D 4 43  LYS 43  43  43  LYS LYS DDD . n 
D 4 44  GLU 44  44  44  GLU GLU DDD . n 
D 4 45  ARG 45  45  45  ARG ARG DDD . n 
D 4 46  GLU 46  46  46  GLU GLU DDD . n 
D 4 47  PHE 47  47  47  PHE PHE DDD . n 
D 4 48  VAL 48  48  48  VAL VAL DDD . n 
D 4 49  ALA 49  49  49  ALA ALA DDD . n 
D 4 50  ALA 50  50  50  ALA ALA DDD . n 
D 4 51  ILE 51  51  51  ILE ILE DDD . n 
D 4 52  ARG 52  52  52  ARG ARG DDD . n 
D 4 53  TRP 53  53  53  TRP TRP DDD . n 
D 4 54  SER 54  54  54  SER SER DDD . n 
D 4 55  GLY 55  55  55  GLY GLY DDD . n 
D 4 56  GLY 56  56  56  GLY GLY DDD . n 
D 4 57  SER 57  57  57  SER SER DDD . n 
D 4 58  ALA 58  58  58  ALA ALA DDD . n 
D 4 59  TYR 59  59  59  TYR TYR DDD . n 
D 4 60  TYR 60  60  60  TYR TYR DDD . n 
D 4 61  ALA 61  61  61  ALA ALA DDD . n 
D 4 62  ASP 62  62  62  ASP ASP DDD . n 
D 4 63  SER 63  63  63  SER SER DDD . n 
D 4 64  VAL 64  64  64  VAL VAL DDD . n 
D 4 65  LYS 65  65  65  LYS LYS DDD . n 
D 4 66  GLY 66  66  66  GLY GLY DDD . n 
D 4 67  ARG 67  67  67  ARG ARG DDD . n 
D 4 68  PHE 68  68  68  PHE PHE DDD . n 
D 4 69  THR 69  69  69  THR THR DDD . n 
D 4 70  ILE 70  70  70  ILE ILE DDD . n 
D 4 71  SER 71  71  71  SER SER DDD . n 
D 4 72  ARG 72  72  72  ARG ARG DDD . n 
D 4 73  ASP 73  73  73  ASP ASP DDD . n 
D 4 74  LYS 74  74  74  LYS LYS DDD . n 
D 4 75  ALA 75  75  75  ALA ALA DDD . n 
D 4 76  LYS 76  76  76  LYS LYS DDD . n 
D 4 77  ASN 77  77  77  ASN ASN DDD . n 
D 4 78  THR 78  78  78  THR THR DDD . n 
D 4 79  VAL 79  79  79  VAL VAL DDD . n 
D 4 80  TYR 80  80  80  TYR TYR DDD . n 
D 4 81  LEU 81  81  81  LEU LEU DDD . n 
D 4 82  GLN 82  82  82  GLN GLN DDD . n 
D 4 83  MET 83  83  83  MET MET DDD . n 
D 4 84  ASN 84  84  84  ASN ASN DDD . n 
D 4 85  SER 85  85  85  SER SER DDD . n 
D 4 86  LEU 86  86  86  LEU LEU DDD . n 
D 4 87  LYS 87  87  87  LYS LYS DDD . n 
D 4 88  TYR 88  88  88  TYR TYR DDD . n 
D 4 89  GLU 89  89  89  GLU GLU DDD . n 
D 4 90  ASP 90  90  90  ASP ASP DDD . n 
D 4 91  THR 91  91  91  THR THR DDD . n 
D 4 92  ALA 92  92  92  ALA ALA DDD . n 
D 4 93  VAL 93  93  93  VAL VAL DDD . n 
D 4 94  TYR 94  94  94  TYR TYR DDD . n 
D 4 95  TYR 95  95  95  TYR TYR DDD . n 
D 4 96  CYS 96  96  96  CYS CYS DDD . n 
D 4 97  ALA 97  97  97  ALA ALA DDD . n 
D 4 98  ARG 98  98  98  ARG ARG DDD . n 
D 4 99  THR 99  99  99  THR THR DDD . n 
D 4 100 GLU 100 100 100 GLU GLU DDD . n 
D 4 101 ASN 101 101 101 ASN ASN DDD . n 
D 4 102 VAL 102 102 102 VAL VAL DDD . n 
D 4 103 ARG 103 103 103 ARG ARG DDD . n 
D 4 104 SER 104 104 104 SER SER DDD . n 
D 4 105 LEU 105 105 105 LEU LEU DDD . n 
D 4 106 LEU 106 106 106 LEU LEU DDD . n 
D 4 107 SER 107 107 107 SER SER DDD . n 
D 4 108 ASP 108 108 108 ASP ASP DDD . n 
D 4 109 TYR 109 109 109 TYR TYR DDD . n 
D 4 110 ALA 110 110 110 ALA ALA DDD . n 
D 4 111 THR 111 111 111 THR THR DDD . n 
D 4 112 TRP 112 112 112 TRP TRP DDD . n 
D 4 113 PRO 113 113 113 PRO PRO DDD . n 
D 4 114 TYR 114 114 114 TYR TYR DDD . n 
D 4 115 ASP 115 115 115 ASP ASP DDD . n 
D 4 116 TYR 116 116 116 TYR TYR DDD . n 
D 4 117 TRP 117 117 117 TRP TRP DDD . n 
D 4 118 GLY 118 118 118 GLY GLY DDD . n 
D 4 119 GLN 119 119 119 GLN GLN DDD . n 
D 4 120 GLY 120 120 120 GLY GLY DDD . n 
D 4 121 THR 121 121 121 THR THR DDD . n 
D 4 122 GLN 122 122 122 GLN GLN DDD . n 
D 4 123 VAL 123 123 123 VAL VAL DDD . n 
D 4 124 THR 124 124 124 THR THR DDD . n 
D 4 125 VAL 125 125 125 VAL VAL DDD . n 
D 4 126 SER 126 126 126 SER SER DDD . n 
D 4 127 SER 127 127 127 SER SER DDD . n 
D 4 128 LYS 128 128 ?   ?   ?   DDD . n 
D 4 129 HIS 129 129 ?   ?   ?   DDD . n 
D 4 130 HIS 130 130 ?   ?   ?   DDD . n 
D 4 131 HIS 131 131 ?   ?   ?   DDD . n 
D 4 132 HIS 132 132 ?   ?   ?   DDD . n 
D 4 133 HIS 133 133 ?   ?   ?   DDD . n 
D 4 134 HIS 134 134 ?   ?   ?   DDD . n 
E 1 1   PRO 1   330 ?   ?   ?   EEE . n 
E 1 2   ASN 2   331 ?   ?   ?   EEE . n 
E 1 3   ILE 3   332 ?   ?   ?   EEE . n 
E 1 4   THR 4   333 ?   ?   ?   EEE . n 
E 1 5   ASN 5   334 334 ASN ASN EEE . n 
E 1 6   LEU 6   335 335 LEU LEU EEE . n 
E 1 7   CYS 7   336 336 CYS CYS EEE . n 
E 1 8   PRO 8   337 337 PRO PRO EEE . n 
E 1 9   PHE 9   338 338 PHE PHE EEE . n 
E 1 10  GLY 10  339 339 GLY GLY EEE . n 
E 1 11  GLU 11  340 340 GLU GLU EEE . n 
E 1 12  VAL 12  341 341 VAL VAL EEE . n 
E 1 13  PHE 13  342 342 PHE PHE EEE . n 
E 1 14  ASN 14  343 343 ASN ASN EEE . n 
E 1 15  ALA 15  344 344 ALA ALA EEE . n 
E 1 16  THR 16  345 345 THR THR EEE . n 
E 1 17  ARG 17  346 346 ARG ARG EEE . n 
E 1 18  PHE 18  347 347 PHE PHE EEE . n 
E 1 19  ALA 19  348 348 ALA ALA EEE . n 
E 1 20  SER 20  349 349 SER SER EEE . n 
E 1 21  VAL 21  350 350 VAL VAL EEE . n 
E 1 22  TYR 22  351 351 TYR TYR EEE . n 
E 1 23  ALA 23  352 352 ALA ALA EEE . n 
E 1 24  TRP 24  353 353 TRP TRP EEE . n 
E 1 25  ASN 25  354 354 ASN ASN EEE . n 
E 1 26  ARG 26  355 355 ARG ARG EEE . n 
E 1 27  LYS 27  356 356 LYS LYS EEE . n 
E 1 28  ARG 28  357 357 ARG ARG EEE . n 
E 1 29  ILE 29  358 358 ILE ILE EEE . n 
E 1 30  SER 30  359 359 SER SER EEE . n 
E 1 31  ASN 31  360 360 ASN ASN EEE . n 
E 1 32  CYS 32  361 361 CYS CYS EEE . n 
E 1 33  VAL 33  362 362 VAL VAL EEE . n 
E 1 34  ALA 34  363 363 ALA ALA EEE . n 
E 1 35  ASP 35  364 364 ASP ASP EEE . n 
E 1 36  TYR 36  365 365 TYR TYR EEE . n 
E 1 37  SER 37  366 366 SER SER EEE . n 
E 1 38  VAL 38  367 367 VAL VAL EEE . n 
E 1 39  LEU 39  368 368 LEU LEU EEE . n 
E 1 40  TYR 40  369 369 TYR TYR EEE . n 
E 1 41  ASN 41  370 370 ASN ASN EEE . n 
E 1 42  SER 42  371 371 SER SER EEE . n 
E 1 43  ALA 43  372 372 ALA ALA EEE . n 
E 1 44  SER 44  373 373 SER SER EEE . n 
E 1 45  PHE 45  374 374 PHE PHE EEE . n 
E 1 46  SER 46  375 375 SER SER EEE . n 
E 1 47  THR 47  376 376 THR THR EEE . n 
E 1 48  PHE 48  377 377 PHE PHE EEE . n 
E 1 49  LYS 49  378 378 LYS LYS EEE . n 
E 1 50  CYS 50  379 379 CYS CYS EEE . n 
E 1 51  TYR 51  380 380 TYR TYR EEE . n 
E 1 52  GLY 52  381 381 GLY GLY EEE . n 
E 1 53  VAL 53  382 382 VAL VAL EEE . n 
E 1 54  SER 54  383 383 SER SER EEE . n 
E 1 55  PRO 55  384 384 PRO PRO EEE . n 
E 1 56  THR 56  385 385 THR THR EEE . n 
E 1 57  LYS 57  386 386 LYS LYS EEE . n 
E 1 58  LEU 58  387 387 LEU LEU EEE . n 
E 1 59  ASN 59  388 388 ASN ASN EEE . n 
E 1 60  ASP 60  389 389 ASP ASP EEE . n 
E 1 61  LEU 61  390 390 LEU LEU EEE . n 
E 1 62  CYS 62  391 391 CYS CYS EEE . n 
E 1 63  PHE 63  392 392 PHE PHE EEE . n 
E 1 64  THR 64  393 393 THR THR EEE . n 
E 1 65  ASN 65  394 394 ASN ASN EEE . n 
E 1 66  VAL 66  395 395 VAL VAL EEE . n 
E 1 67  TYR 67  396 396 TYR TYR EEE . n 
E 1 68  ALA 68  397 397 ALA ALA EEE . n 
E 1 69  ASP 69  398 398 ASP ASP EEE . n 
E 1 70  SER 70  399 399 SER SER EEE . n 
E 1 71  PHE 71  400 400 PHE PHE EEE . n 
E 1 72  VAL 72  401 401 VAL VAL EEE . n 
E 1 73  ILE 73  402 402 ILE ILE EEE . n 
E 1 74  ARG 74  403 403 ARG ARG EEE . n 
E 1 75  GLY 75  404 404 GLY GLY EEE . n 
E 1 76  ASP 76  405 405 ASP ASP EEE . n 
E 1 77  GLU 77  406 406 GLU GLU EEE . n 
E 1 78  VAL 78  407 407 VAL VAL EEE . n 
E 1 79  ARG 79  408 408 ARG ARG EEE . n 
E 1 80  GLN 80  409 409 GLN GLN EEE . n 
E 1 81  ILE 81  410 410 ILE ILE EEE . n 
E 1 82  ALA 82  411 411 ALA ALA EEE . n 
E 1 83  PRO 83  412 412 PRO PRO EEE . n 
E 1 84  GLY 84  413 413 GLY GLY EEE . n 
E 1 85  GLN 85  414 414 GLN GLN EEE . n 
E 1 86  THR 86  415 415 THR THR EEE . n 
E 1 87  GLY 87  416 416 GLY GLY EEE . n 
E 1 88  LYS 88  417 417 LYS LYS EEE . n 
E 1 89  ILE 89  418 418 ILE ILE EEE . n 
E 1 90  ALA 90  419 419 ALA ALA EEE . n 
E 1 91  ASP 91  420 420 ASP ASP EEE . n 
E 1 92  TYR 92  421 421 TYR TYR EEE . n 
E 1 93  ASN 93  422 422 ASN ASN EEE . n 
E 1 94  TYR 94  423 423 TYR TYR EEE . n 
E 1 95  LYS 95  424 424 LYS LYS EEE . n 
E 1 96  LEU 96  425 425 LEU LEU EEE . n 
E 1 97  PRO 97  426 426 PRO PRO EEE . n 
E 1 98  ASP 98  427 427 ASP ASP EEE . n 
E 1 99  ASP 99  428 428 ASP ASP EEE . n 
E 1 100 PHE 100 429 429 PHE PHE EEE . n 
E 1 101 THR 101 430 430 THR THR EEE . n 
E 1 102 GLY 102 431 431 GLY GLY EEE . n 
E 1 103 CYS 103 432 432 CYS CYS EEE . n 
E 1 104 VAL 104 433 433 VAL VAL EEE . n 
E 1 105 ILE 105 434 434 ILE ILE EEE . n 
E 1 106 ALA 106 435 435 ALA ALA EEE . n 
E 1 107 TRP 107 436 436 TRP TRP EEE . n 
E 1 108 ASN 108 437 437 ASN ASN EEE . n 
E 1 109 SER 109 438 438 SER SER EEE . n 
E 1 110 ASN 110 439 439 ASN ASN EEE . n 
E 1 111 ASN 111 440 440 ASN ASN EEE . n 
E 1 112 LEU 112 441 441 LEU LEU EEE . n 
E 1 113 ASP 113 442 442 ASP ASP EEE . n 
E 1 114 SER 114 443 443 SER SER EEE . n 
E 1 115 LYS 115 444 444 LYS LYS EEE . n 
E 1 116 VAL 116 445 445 VAL VAL EEE . n 
E 1 117 GLY 117 446 446 GLY GLY EEE . n 
E 1 118 GLY 118 447 447 GLY GLY EEE . n 
E 1 119 ASN 119 448 448 ASN ASN EEE . n 
E 1 120 TYR 120 449 449 TYR TYR EEE . n 
E 1 121 ASN 121 450 450 ASN ASN EEE . n 
E 1 122 TYR 122 451 451 TYR TYR EEE . n 
E 1 123 LEU 123 452 452 LEU LEU EEE . n 
E 1 124 TYR 124 453 453 TYR TYR EEE . n 
E 1 125 ARG 125 454 454 ARG ARG EEE . n 
E 1 126 LEU 126 455 455 LEU LEU EEE . n 
E 1 127 PHE 127 456 456 PHE PHE EEE . n 
E 1 128 ARG 128 457 457 ARG ARG EEE . n 
E 1 129 LYS 129 458 458 LYS LYS EEE . n 
E 1 130 SER 130 459 459 SER SER EEE . n 
E 1 131 ASN 131 460 460 ASN ASN EEE . n 
E 1 132 LEU 132 461 461 LEU LEU EEE . n 
E 1 133 LYS 133 462 462 LYS LYS EEE . n 
E 1 134 PRO 134 463 463 PRO PRO EEE . n 
E 1 135 PHE 135 464 464 PHE PHE EEE . n 
E 1 136 GLU 136 465 465 GLU GLU EEE . n 
E 1 137 ARG 137 466 466 ARG ARG EEE . n 
E 1 138 ASP 138 467 467 ASP ASP EEE . n 
E 1 139 ILE 139 468 468 ILE ILE EEE . n 
E 1 140 SER 140 469 469 SER SER EEE . n 
E 1 141 THR 141 470 470 THR THR EEE . n 
E 1 142 GLU 142 471 471 GLU GLU EEE . n 
E 1 143 ILE 143 472 472 ILE ILE EEE . n 
E 1 144 TYR 144 473 473 TYR TYR EEE . n 
E 1 145 GLN 145 474 474 GLN GLN EEE . n 
E 1 146 ALA 146 475 475 ALA ALA EEE . n 
E 1 147 GLY 147 476 476 GLY GLY EEE . n 
E 1 148 SER 148 477 477 SER SER EEE . n 
E 1 149 THR 149 478 478 THR THR EEE . n 
E 1 150 PRO 150 479 479 PRO PRO EEE . n 
E 1 151 CYS 151 480 480 CYS CYS EEE . n 
E 1 152 ASN 152 481 481 ASN ASN EEE . n 
E 1 153 GLY 153 482 482 GLY GLY EEE . n 
E 1 154 VAL 154 483 483 VAL VAL EEE . n 
E 1 155 GLU 155 484 484 GLU GLU EEE . n 
E 1 156 GLY 156 485 485 GLY GLY EEE . n 
E 1 157 PHE 157 486 486 PHE PHE EEE . n 
E 1 158 ASN 158 487 487 ASN ASN EEE . n 
E 1 159 CYS 159 488 488 CYS CYS EEE . n 
E 1 160 TYR 160 489 489 TYR TYR EEE . n 
E 1 161 PHE 161 490 490 PHE PHE EEE . n 
E 1 162 PRO 162 491 491 PRO PRO EEE . n 
E 1 163 LEU 163 492 492 LEU LEU EEE . n 
E 1 164 GLN 164 493 493 GLN GLN EEE . n 
E 1 165 SER 165 494 494 SER SER EEE . n 
E 1 166 TYR 166 495 495 TYR TYR EEE . n 
E 1 167 GLY 167 496 496 GLY GLY EEE . n 
E 1 168 PHE 168 497 497 PHE PHE EEE . n 
E 1 169 GLN 169 498 498 GLN GLN EEE . n 
E 1 170 PRO 170 499 499 PRO PRO EEE . n 
E 1 171 THR 171 500 500 THR THR EEE . n 
E 1 172 ASN 172 501 501 ASN ASN EEE . n 
E 1 173 GLY 173 502 502 GLY GLY EEE . n 
E 1 174 VAL 174 503 503 VAL VAL EEE . n 
E 1 175 GLY 175 504 504 GLY GLY EEE . n 
E 1 176 TYR 176 505 505 TYR TYR EEE . n 
E 1 177 GLN 177 506 506 GLN GLN EEE . n 
E 1 178 PRO 178 507 507 PRO PRO EEE . n 
E 1 179 TYR 179 508 508 TYR TYR EEE . n 
E 1 180 ARG 180 509 509 ARG ARG EEE . n 
E 1 181 VAL 181 510 510 VAL VAL EEE . n 
E 1 182 VAL 182 511 511 VAL VAL EEE . n 
E 1 183 VAL 183 512 512 VAL VAL EEE . n 
E 1 184 LEU 184 513 513 LEU LEU EEE . n 
E 1 185 SER 185 514 514 SER SER EEE . n 
E 1 186 PHE 186 515 515 PHE PHE EEE . n 
E 1 187 GLU 187 516 516 GLU GLU EEE . n 
E 1 188 LEU 188 517 517 LEU LEU EEE . n 
E 1 189 LEU 189 518 518 LEU LEU EEE . n 
E 1 190 HIS 190 519 519 HIS HIS EEE . n 
E 1 191 ALA 191 520 520 ALA ALA EEE . n 
E 1 192 PRO 192 521 521 PRO PRO EEE . n 
E 1 193 ALA 193 522 522 ALA ALA EEE . n 
E 1 194 THR 194 523 523 THR THR EEE . n 
E 1 195 VAL 195 524 524 VAL VAL EEE . n 
E 1 196 CYS 196 525 525 CYS CYS EEE . n 
E 1 197 GLY 197 526 526 GLY GLY EEE . n 
E 1 198 PRO 198 527 527 PRO PRO EEE . n 
E 1 199 LYS 199 528 528 LYS LYS EEE . n 
E 1 200 LYS 200 529 ?   ?   ?   EEE . n 
E 1 201 SER 201 530 ?   ?   ?   EEE . n 
E 1 202 THR 202 531 ?   ?   ?   EEE . n 
E 1 203 ASN 203 532 ?   ?   ?   EEE . n 
E 1 204 LYS 204 533 ?   ?   ?   EEE . n 
E 1 205 HIS 205 534 ?   ?   ?   EEE . n 
E 1 206 HIS 206 535 ?   ?   ?   EEE . n 
E 1 207 HIS 207 536 ?   ?   ?   EEE . n 
E 1 208 HIS 208 537 ?   ?   ?   EEE . n 
E 1 209 HIS 209 538 ?   ?   ?   EEE . n 
E 1 210 HIS 210 539 ?   ?   ?   EEE . n 
F 4 1   GLN 1   1   1   GLN GLN FFF . n 
F 4 2   VAL 2   2   2   VAL VAL FFF . n 
F 4 3   GLN 3   3   3   GLN GLN FFF . n 
F 4 4   LEU 4   4   4   LEU LEU FFF . n 
F 4 5   VAL 5   5   5   VAL VAL FFF . n 
F 4 6   GLU 6   6   6   GLU GLU FFF . n 
F 4 7   SER 7   7   7   SER SER FFF . n 
F 4 8   GLY 8   8   8   GLY GLY FFF . n 
F 4 9   GLY 9   9   9   GLY GLY FFF . n 
F 4 10  GLY 10  10  10  GLY GLY FFF . n 
F 4 11  LEU 11  11  11  LEU LEU FFF . n 
F 4 12  MET 12  12  12  MET MET FFF . n 
F 4 13  GLN 13  13  13  GLN GLN FFF . n 
F 4 14  ALA 14  14  14  ALA ALA FFF . n 
F 4 15  GLY 15  15  15  GLY GLY FFF . n 
F 4 16  GLY 16  16  16  GLY GLY FFF . n 
F 4 17  SER 17  17  17  SER SER FFF . n 
F 4 18  LEU 18  18  18  LEU LEU FFF . n 
F 4 19  ARG 19  19  19  ARG ARG FFF . n 
F 4 20  LEU 20  20  20  LEU LEU FFF . n 
F 4 21  SER 21  21  21  SER SER FFF . n 
F 4 22  CYS 22  22  22  CYS CYS FFF . n 
F 4 23  ALA 23  23  23  ALA ALA FFF . n 
F 4 24  VAL 24  24  24  VAL VAL FFF . n 
F 4 25  SER 25  25  25  SER SER FFF . n 
F 4 26  GLY 26  26  26  GLY GLY FFF . n 
F 4 27  ARG 27  27  27  ARG ARG FFF . n 
F 4 28  THR 28  28  28  THR THR FFF . n 
F 4 29  PHE 29  29  29  PHE PHE FFF . n 
F 4 30  SER 30  30  30  SER SER FFF . n 
F 4 31  THR 31  31  31  THR THR FFF . n 
F 4 32  ALA 32  32  32  ALA ALA FFF . n 
F 4 33  ALA 33  33  33  ALA ALA FFF . n 
F 4 34  MET 34  34  34  MET MET FFF . n 
F 4 35  GLY 35  35  35  GLY GLY FFF . n 
F 4 36  TRP 36  36  36  TRP TRP FFF . n 
F 4 37  PHE 37  37  37  PHE PHE FFF . n 
F 4 38  ARG 38  38  38  ARG ARG FFF . n 
F 4 39  GLN 39  39  39  GLN GLN FFF . n 
F 4 40  ALA 40  40  40  ALA ALA FFF . n 
F 4 41  PRO 41  41  41  PRO PRO FFF . n 
F 4 42  GLY 42  42  42  GLY GLY FFF . n 
F 4 43  LYS 43  43  43  LYS LYS FFF . n 
F 4 44  GLU 44  44  44  GLU GLU FFF . n 
F 4 45  ARG 45  45  45  ARG ARG FFF . n 
F 4 46  GLU 46  46  46  GLU GLU FFF . n 
F 4 47  PHE 47  47  47  PHE PHE FFF . n 
F 4 48  VAL 48  48  48  VAL VAL FFF . n 
F 4 49  ALA 49  49  49  ALA ALA FFF . n 
F 4 50  ALA 50  50  50  ALA ALA FFF . n 
F 4 51  ILE 51  51  51  ILE ILE FFF . n 
F 4 52  ARG 52  52  52  ARG ARG FFF . n 
F 4 53  TRP 53  53  53  TRP TRP FFF . n 
F 4 54  SER 54  54  54  SER SER FFF . n 
F 4 55  GLY 55  55  55  GLY GLY FFF . n 
F 4 56  GLY 56  56  56  GLY GLY FFF . n 
F 4 57  SER 57  57  57  SER SER FFF . n 
F 4 58  ALA 58  58  58  ALA ALA FFF . n 
F 4 59  TYR 59  59  59  TYR TYR FFF . n 
F 4 60  TYR 60  60  60  TYR TYR FFF . n 
F 4 61  ALA 61  61  61  ALA ALA FFF . n 
F 4 62  ASP 62  62  62  ASP ASP FFF . n 
F 4 63  SER 63  63  63  SER SER FFF . n 
F 4 64  VAL 64  64  64  VAL VAL FFF . n 
F 4 65  LYS 65  65  65  LYS LYS FFF . n 
F 4 66  GLY 66  66  66  GLY GLY FFF . n 
F 4 67  ARG 67  67  67  ARG ARG FFF . n 
F 4 68  PHE 68  68  68  PHE PHE FFF . n 
F 4 69  THR 69  69  69  THR THR FFF . n 
F 4 70  ILE 70  70  70  ILE ILE FFF . n 
F 4 71  SER 71  71  71  SER SER FFF . n 
F 4 72  ARG 72  72  72  ARG ARG FFF . n 
F 4 73  ASP 73  73  73  ASP ASP FFF . n 
F 4 74  LYS 74  74  74  LYS LYS FFF . n 
F 4 75  ALA 75  75  75  ALA ALA FFF . n 
F 4 76  LYS 76  76  76  LYS LYS FFF . n 
F 4 77  ASN 77  77  77  ASN ASN FFF . n 
F 4 78  THR 78  78  78  THR THR FFF . n 
F 4 79  VAL 79  79  79  VAL VAL FFF . n 
F 4 80  TYR 80  80  80  TYR TYR FFF . n 
F 4 81  LEU 81  81  81  LEU LEU FFF . n 
F 4 82  GLN 82  82  82  GLN GLN FFF . n 
F 4 83  MET 83  83  83  MET MET FFF . n 
F 4 84  ASN 84  84  84  ASN ASN FFF . n 
F 4 85  SER 85  85  85  SER SER FFF . n 
F 4 86  LEU 86  86  86  LEU LEU FFF . n 
F 4 87  LYS 87  87  87  LYS LYS FFF . n 
F 4 88  TYR 88  88  88  TYR TYR FFF . n 
F 4 89  GLU 89  89  89  GLU GLU FFF . n 
F 4 90  ASP 90  90  90  ASP ASP FFF . n 
F 4 91  THR 91  91  91  THR THR FFF . n 
F 4 92  ALA 92  92  92  ALA ALA FFF . n 
F 4 93  VAL 93  93  93  VAL VAL FFF . n 
F 4 94  TYR 94  94  94  TYR TYR FFF . n 
F 4 95  TYR 95  95  95  TYR TYR FFF . n 
F 4 96  CYS 96  96  96  CYS CYS FFF . n 
F 4 97  ALA 97  97  97  ALA ALA FFF . n 
F 4 98  ARG 98  98  98  ARG ARG FFF . n 
F 4 99  THR 99  99  99  THR THR FFF . n 
F 4 100 GLU 100 100 100 GLU GLU FFF . n 
F 4 101 ASN 101 101 101 ASN ASN FFF . n 
F 4 102 VAL 102 102 102 VAL VAL FFF . n 
F 4 103 ARG 103 103 103 ARG ARG FFF . n 
F 4 104 SER 104 104 104 SER SER FFF . n 
F 4 105 LEU 105 105 105 LEU LEU FFF . n 
F 4 106 LEU 106 106 106 LEU LEU FFF . n 
F 4 107 SER 107 107 107 SER SER FFF . n 
F 4 108 ASP 108 108 108 ASP ASP FFF . n 
F 4 109 TYR 109 109 109 TYR TYR FFF . n 
F 4 110 ALA 110 110 110 ALA ALA FFF . n 
F 4 111 THR 111 111 111 THR THR FFF . n 
F 4 112 TRP 112 112 112 TRP TRP FFF . n 
F 4 113 PRO 113 113 113 PRO PRO FFF . n 
F 4 114 TYR 114 114 114 TYR TYR FFF . n 
F 4 115 ASP 115 115 115 ASP ASP FFF . n 
F 4 116 TYR 116 116 116 TYR TYR FFF . n 
F 4 117 TRP 117 117 117 TRP TRP FFF . n 
F 4 118 GLY 118 118 118 GLY GLY FFF . n 
F 4 119 GLN 119 119 119 GLN GLN FFF . n 
F 4 120 GLY 120 120 120 GLY GLY FFF . n 
F 4 121 THR 121 121 121 THR THR FFF . n 
F 4 122 GLN 122 122 122 GLN GLN FFF . n 
F 4 123 VAL 123 123 123 VAL VAL FFF . n 
F 4 124 THR 124 124 124 THR THR FFF . n 
F 4 125 VAL 125 125 125 VAL VAL FFF . n 
F 4 126 SER 126 126 126 SER SER FFF . n 
F 4 127 SER 127 127 127 SER SER FFF . n 
F 4 128 LYS 128 128 ?   ?   ?   FFF . n 
F 4 129 HIS 129 129 ?   ?   ?   FFF . n 
F 4 130 HIS 130 130 ?   ?   ?   FFF . n 
F 4 131 HIS 131 131 ?   ?   ?   FFF . n 
F 4 132 HIS 132 132 ?   ?   ?   FFF . n 
F 4 133 HIS 133 133 ?   ?   ?   FFF . n 
F 4 134 HIS 134 134 ?   ?   ?   FFF . n 
G 2 1   THR 1   0   0   THR THR HHH . n 
G 2 2   GLN 2   1   1   GLN GLN HHH . n 
G 2 3   MET 3   2   2   MET MET HHH . n 
G 2 4   GLN 4   3   3   GLN GLN HHH . n 
G 2 5   LEU 5   4   4   LEU LEU HHH . n 
G 2 6   VAL 6   5   5   VAL VAL HHH . n 
G 2 7   GLN 7   6   6   GLN GLN HHH . n 
G 2 8   SER 8   7   7   SER SER HHH . n 
G 2 9   GLY 9   8   8   GLY GLY HHH . n 
G 2 10  THR 10  9   9   THR THR HHH . n 
G 2 11  GLU 11  10  10  GLU GLU HHH . n 
G 2 12  VAL 12  11  11  VAL VAL HHH . n 
G 2 13  LYS 13  12  12  LYS LYS HHH . n 
G 2 14  LYS 14  13  13  LYS LYS HHH . n 
G 2 15  PRO 15  14  14  PRO PRO HHH . n 
G 2 16  GLY 16  15  15  GLY GLY HHH . n 
G 2 17  GLU 17  16  16  GLU GLU HHH . n 
G 2 18  SER 18  17  17  SER SER HHH . n 
G 2 19  LEU 19  18  18  LEU LEU HHH . n 
G 2 20  LYS 20  19  19  LYS LYS HHH . n 
G 2 21  ILE 21  20  20  ILE ILE HHH . n 
G 2 22  SER 22  21  21  SER SER HHH . n 
G 2 23  CYS 23  22  22  CYS CYS HHH . n 
G 2 24  LYS 24  23  23  LYS LYS HHH . n 
G 2 25  GLY 25  24  24  GLY GLY HHH . n 
G 2 26  SER 26  25  25  SER SER HHH . n 
G 2 27  GLY 27  26  26  GLY GLY HHH . n 
G 2 28  TYR 28  27  27  TYR TYR HHH . n 
G 2 29  GLY 29  28  28  GLY GLY HHH . n 
G 2 30  PHE 30  29  29  PHE PHE HHH . n 
G 2 31  ILE 31  30  30  ILE ILE HHH . n 
G 2 32  THR 32  31  31  THR THR HHH . n 
G 2 33  TYR 33  32  32  TYR TYR HHH . n 
G 2 34  TRP 34  33  33  TRP TRP HHH . n 
G 2 35  ILE 35  34  34  ILE ILE HHH . n 
G 2 36  GLY 36  35  35  GLY GLY HHH . n 
G 2 37  TRP 37  36  36  TRP TRP HHH . n 
G 2 38  VAL 38  37  37  VAL VAL HHH . n 
G 2 39  ARG 39  38  38  ARG ARG HHH . n 
G 2 40  GLN 40  39  39  GLN GLN HHH . n 
G 2 41  MET 41  40  40  MET MET HHH . n 
G 2 42  PRO 42  41  41  PRO PRO HHH . n 
G 2 43  GLY 43  42  42  GLY GLY HHH . n 
G 2 44  LYS 44  43  43  LYS LYS HHH . n 
G 2 45  GLY 45  44  44  GLY GLY HHH . n 
G 2 46  LEU 46  45  45  LEU LEU HHH . n 
G 2 47  GLU 47  46  46  GLU GLU HHH . n 
G 2 48  TRP 48  47  47  TRP TRP HHH . n 
G 2 49  MET 49  48  48  MET MET HHH . n 
G 2 50  GLY 50  49  49  GLY GLY HHH . n 
G 2 51  ILE 51  50  50  ILE ILE HHH . n 
G 2 52  ILE 52  51  51  ILE ILE HHH . n 
G 2 53  TYR 53  52  52  TYR TYR HHH . n 
G 2 54  PRO 54  53  53  PRO PRO HHH . n 
G 2 55  GLY 55  54  54  GLY GLY HHH . n 
G 2 56  ASP 56  55  55  ASP ASP HHH . n 
G 2 57  SER 57  56  56  SER SER HHH . n 
G 2 58  GLU 58  57  57  GLU GLU HHH . n 
G 2 59  THR 59  58  58  THR THR HHH . n 
G 2 60  ARG 60  59  59  ARG ARG HHH . n 
G 2 61  TYR 61  60  60  TYR TYR HHH . n 
G 2 62  SER 62  61  61  SER SER HHH . n 
G 2 63  PRO 63  62  62  PRO PRO HHH . n 
G 2 64  SER 64  63  63  SER SER HHH . n 
G 2 65  PHE 65  64  64  PHE PHE HHH . n 
G 2 66  GLN 66  65  65  GLN GLN HHH . n 
G 2 67  GLY 67  66  66  GLY GLY HHH . n 
G 2 68  GLN 68  67  67  GLN GLN HHH . n 
G 2 69  VAL 69  68  68  VAL VAL HHH . n 
G 2 70  THR 70  69  69  THR THR HHH . n 
G 2 71  ILE 71  70  70  ILE ILE HHH . n 
G 2 72  SER 72  71  71  SER SER HHH . n 
G 2 73  ALA 73  72  72  ALA ALA HHH . n 
G 2 74  ASP 74  73  73  ASP ASP HHH . n 
G 2 75  LYS 75  74  74  LYS LYS HHH . n 
G 2 76  SER 76  75  75  SER SER HHH . n 
G 2 77  ILE 77  76  76  ILE ILE HHH . n 
G 2 78  ASN 78  77  77  ASN ASN HHH . n 
G 2 79  THR 79  78  78  THR THR HHH . n 
G 2 80  ALA 80  79  79  ALA ALA HHH . n 
G 2 81  TYR 81  80  80  TYR TYR HHH . n 
G 2 82  LEU 82  81  81  LEU LEU HHH . n 
G 2 83  GLN 83  82  82  GLN GLN HHH . n 
G 2 84  TRP 84  83  83  TRP TRP HHH . n 
G 2 85  SER 85  84  84  SER SER HHH . n 
G 2 86  SER 86  85  85  SER SER HHH . n 
G 2 87  LEU 87  86  86  LEU LEU HHH . n 
G 2 88  LYS 88  87  87  LYS LYS HHH . n 
G 2 89  ALA 89  88  88  ALA ALA HHH . n 
G 2 90  SER 90  89  89  SER SER HHH . n 
G 2 91  ASP 91  90  90  ASP ASP HHH . n 
G 2 92  THR 92  91  91  THR THR HHH . n 
G 2 93  ALA 93  92  92  ALA ALA HHH . n 
G 2 94  ILE 94  93  93  ILE ILE HHH . n 
G 2 95  TYR 95  94  94  TYR TYR HHH . n 
G 2 96  TYR 96  95  95  TYR TYR HHH . n 
G 2 97  CYS 97  96  96  CYS CYS HHH . n 
G 2 98  ALA 98  97  97  ALA ALA HHH . n 
G 2 99  GLY 99  98  98  GLY GLY HHH . n 
G 2 100 GLY 100 99  99  GLY GLY HHH . n 
G 2 101 SER 101 100 100 SER SER HHH . n 
G 2 102 GLY 102 101 101 GLY GLY HHH . n 
G 2 103 ILE 103 102 102 ILE ILE HHH . n 
G 2 104 SER 104 103 103 SER SER HHH . n 
G 2 105 THR 105 104 104 THR THR HHH . n 
G 2 106 PRO 106 105 105 PRO PRO HHH . n 
G 2 107 MET 107 106 106 MET MET HHH . n 
G 2 108 ASP 108 107 107 ASP ASP HHH . n 
G 2 109 VAL 109 108 108 VAL VAL HHH . n 
G 2 110 TRP 110 109 109 TRP TRP HHH . n 
G 2 111 GLY 111 110 110 GLY GLY HHH . n 
G 2 112 GLN 112 111 111 GLN GLN HHH . n 
G 2 113 GLY 113 112 112 GLY GLY HHH . n 
G 2 114 THR 114 113 113 THR THR HHH . n 
G 2 115 THR 115 114 114 THR THR HHH . n 
G 2 116 VAL 116 115 115 VAL VAL HHH . n 
G 2 117 THR 117 116 116 THR THR HHH . n 
G 2 118 VAL 118 117 117 VAL VAL HHH . n 
G 2 119 ALA 119 118 118 ALA ALA HHH . n 
G 2 120 SER 120 119 119 SER SER HHH . n 
G 2 121 THR 121 120 120 THR THR HHH . n 
G 2 122 LYS 122 121 121 LYS LYS HHH . n 
G 2 123 GLY 123 122 122 GLY GLY HHH . n 
G 2 124 PRO 124 123 123 PRO PRO HHH . n 
G 2 125 SER 125 124 124 SER SER HHH . n 
G 2 126 VAL 126 125 125 VAL VAL HHH . n 
G 2 127 PHE 127 126 126 PHE PHE HHH . n 
G 2 128 PRO 128 127 127 PRO PRO HHH . n 
G 2 129 LEU 129 128 128 LEU LEU HHH . n 
G 2 130 ALA 130 129 129 ALA ALA HHH . n 
G 2 131 PRO 131 130 130 PRO PRO HHH . n 
G 2 132 SER 132 131 131 SER SER HHH . n 
G 2 133 SER 133 132 132 SER SER HHH . n 
G 2 134 LYS 134 133 ?   ?   ?   HHH . n 
G 2 135 SER 135 134 ?   ?   ?   HHH . n 
G 2 136 THR 136 135 ?   ?   ?   HHH . n 
G 2 137 SER 137 136 ?   ?   ?   HHH . n 
G 2 138 GLY 138 137 137 GLY GLY HHH . n 
G 2 139 GLY 139 138 138 GLY GLY HHH . n 
G 2 140 THR 140 139 139 THR THR HHH . n 
G 2 141 ALA 141 140 140 ALA ALA HHH . n 
G 2 142 ALA 142 141 141 ALA ALA HHH . n 
G 2 143 LEU 143 142 142 LEU LEU HHH . n 
G 2 144 GLY 144 143 143 GLY GLY HHH . n 
G 2 145 CYS 145 144 144 CYS CYS HHH . n 
G 2 146 LEU 146 145 145 LEU LEU HHH . n 
G 2 147 VAL 147 146 146 VAL VAL HHH . n 
G 2 148 LYS 148 147 147 LYS LYS HHH . n 
G 2 149 ASP 149 148 148 ASP ASP HHH . n 
G 2 150 TYR 150 149 149 TYR TYR HHH . n 
G 2 151 PHE 151 150 150 PHE PHE HHH . n 
G 2 152 PRO 152 151 151 PRO PRO HHH . n 
G 2 153 GLU 153 152 152 GLU GLU HHH . n 
G 2 154 PRO 154 153 153 PRO PRO HHH . n 
G 2 155 VAL 155 154 154 VAL VAL HHH . n 
G 2 156 THR 156 155 155 THR THR HHH . n 
G 2 157 VAL 157 156 156 VAL VAL HHH . n 
G 2 158 SER 158 157 157 SER SER HHH . n 
G 2 159 TRP 159 158 158 TRP TRP HHH . n 
G 2 160 ASN 160 159 159 ASN ASN HHH . n 
G 2 161 SER 161 160 160 SER SER HHH . n 
G 2 162 GLY 162 161 161 GLY GLY HHH . n 
G 2 163 ALA 163 162 162 ALA ALA HHH . n 
G 2 164 LEU 164 163 163 LEU LEU HHH . n 
G 2 165 THR 165 164 164 THR THR HHH . n 
G 2 166 SER 166 165 165 SER SER HHH . n 
G 2 167 GLY 167 166 166 GLY GLY HHH . n 
G 2 168 VAL 168 167 167 VAL VAL HHH . n 
G 2 169 HIS 169 168 168 HIS HIS HHH . n 
G 2 170 THR 170 169 169 THR THR HHH . n 
G 2 171 PHE 171 170 170 PHE PHE HHH . n 
G 2 172 PRO 172 171 171 PRO PRO HHH . n 
G 2 173 ALA 173 172 172 ALA ALA HHH . n 
G 2 174 VAL 174 173 173 VAL VAL HHH . n 
G 2 175 LEU 175 174 174 LEU LEU HHH . n 
G 2 176 GLN 176 175 175 GLN GLN HHH . n 
G 2 177 SER 177 176 176 SER SER HHH . n 
G 2 178 SER 178 177 177 SER SER HHH . n 
G 2 179 GLY 179 178 178 GLY GLY HHH . n 
G 2 180 LEU 180 179 179 LEU LEU HHH . n 
G 2 181 TYR 181 180 180 TYR TYR HHH . n 
G 2 182 SER 182 181 181 SER SER HHH . n 
G 2 183 LEU 183 182 182 LEU LEU HHH . n 
G 2 184 SER 184 183 183 SER SER HHH . n 
G 2 185 SER 185 184 184 SER SER HHH . n 
G 2 186 VAL 186 185 185 VAL VAL HHH . n 
G 2 187 VAL 187 186 186 VAL VAL HHH . n 
G 2 188 THR 188 187 187 THR THR HHH . n 
G 2 189 VAL 189 188 188 VAL VAL HHH . n 
G 2 190 PRO 190 189 189 PRO PRO HHH . n 
G 2 191 SER 191 190 190 SER SER HHH . n 
G 2 192 SER 192 191 191 SER SER HHH . n 
G 2 193 SER 193 192 192 SER SER HHH . n 
G 2 194 LEU 194 193 193 LEU LEU HHH . n 
G 2 195 GLY 195 194 194 GLY GLY HHH . n 
G 2 196 THR 196 195 195 THR THR HHH . n 
G 2 197 GLN 197 196 196 GLN GLN HHH . n 
G 2 198 THR 198 197 197 THR THR HHH . n 
G 2 199 TYR 199 198 198 TYR TYR HHH . n 
G 2 200 ILE 200 199 199 ILE ILE HHH . n 
G 2 201 CYS 201 200 200 CYS CYS HHH . n 
G 2 202 ASN 202 201 201 ASN ASN HHH . n 
G 2 203 VAL 203 202 202 VAL VAL HHH . n 
G 2 204 ASN 204 203 203 ASN ASN HHH . n 
G 2 205 HIS 205 204 204 HIS HIS HHH . n 
G 2 206 LYS 206 205 205 LYS LYS HHH . n 
G 2 207 PRO 207 206 206 PRO PRO HHH . n 
G 2 208 SER 208 207 207 SER SER HHH . n 
G 2 209 ASN 209 208 208 ASN ASN HHH . n 
G 2 210 THR 210 209 209 THR THR HHH . n 
G 2 211 LYS 211 210 210 LYS LYS HHH . n 
G 2 212 VAL 212 211 211 VAL VAL HHH . n 
G 2 213 ASP 213 212 212 ASP ASP HHH . n 
G 2 214 LYS 214 213 213 LYS LYS HHH . n 
G 2 215 LYS 215 214 214 LYS LYS HHH . n 
G 2 216 VAL 216 215 215 VAL VAL HHH . n 
G 2 217 GLU 217 216 216 GLU GLU HHH . n 
G 2 218 PRO 218 217 217 PRO PRO HHH . n 
G 2 219 LYS 219 218 218 LYS LYS HHH . n 
G 2 220 SER 220 219 219 SER SER HHH . n 
G 2 221 CYS 221 220 ?   ?   ?   HHH . n 
G 2 222 ASP 222 221 ?   ?   ?   HHH . n 
G 2 223 LYS 223 222 ?   ?   ?   HHH . n 
G 2 224 HIS 224 223 ?   ?   ?   HHH . n 
G 2 225 HIS 225 224 ?   ?   ?   HHH . n 
G 2 226 HIS 226 225 ?   ?   ?   HHH . n 
G 2 227 HIS 227 226 ?   ?   ?   HHH . n 
G 2 228 HIS 228 227 ?   ?   ?   HHH . n 
G 2 229 HIS 229 228 ?   ?   ?   HHH . n 
H 3 1   ASP 1   1   1   ASP ASP LLL . n 
H 3 2   ILE 2   2   2   ILE ILE LLL . n 
H 3 3   GLN 3   3   3   GLN GLN LLL . n 
H 3 4   LEU 4   4   4   LEU LEU LLL . n 
H 3 5   THR 5   5   5   THR THR LLL . n 
H 3 6   GLN 6   6   6   GLN GLN LLL . n 
H 3 7   SER 7   7   7   SER SER LLL . n 
H 3 8   PRO 8   8   8   PRO PRO LLL . n 
H 3 9   ASP 9   9   9   ASP ASP LLL . n 
H 3 10  SER 10  10  10  SER SER LLL . n 
H 3 11  LEU 11  11  11  LEU LEU LLL . n 
H 3 12  ALA 12  12  12  ALA ALA LLL . n 
H 3 13  VAL 13  13  13  VAL VAL LLL . n 
H 3 14  SER 14  14  14  SER SER LLL . n 
H 3 15  LEU 15  15  15  LEU LEU LLL . n 
H 3 16  GLY 16  16  16  GLY GLY LLL . n 
H 3 17  GLU 17  17  17  GLU GLU LLL . n 
H 3 18  ARG 18  18  18  ARG ARG LLL . n 
H 3 19  ALA 19  19  19  ALA ALA LLL . n 
H 3 20  THR 20  20  20  THR THR LLL . n 
H 3 21  ILE 21  21  21  ILE ILE LLL . n 
H 3 22  ASN 22  22  22  ASN ASN LLL . n 
H 3 23  CYS 23  23  23  CYS CYS LLL . n 
H 3 24  LYS 24  24  24  LYS LYS LLL . n 
H 3 25  SER 25  25  25  SER SER LLL . n 
H 3 26  SER 26  26  26  SER SER LLL . n 
H 3 27  GLN 27  27  27  GLN GLN LLL . n 
H 3 28  SER 28  28  28  SER SER LLL . n 
H 3 29  VAL 29  29  29  VAL VAL LLL . n 
H 3 30  LEU 30  30  30  LEU LEU LLL . n 
H 3 31  TYR 31  31  31  TYR TYR LLL . n 
H 3 32  SER 32  32  32  SER SER LLL . n 
H 3 33  SER 33  33  33  SER SER LLL . n 
H 3 34  ILE 34  34  34  ILE ILE LLL . n 
H 3 35  ASN 35  35  35  ASN ASN LLL . n 
H 3 36  LYS 36  36  36  LYS LYS LLL . n 
H 3 37  ASN 37  37  37  ASN ASN LLL . n 
H 3 38  TYR 38  38  38  TYR TYR LLL . n 
H 3 39  LEU 39  39  39  LEU LEU LLL . n 
H 3 40  ALA 40  40  40  ALA ALA LLL . n 
H 3 41  TRP 41  41  41  TRP TRP LLL . n 
H 3 42  TYR 42  42  42  TYR TYR LLL . n 
H 3 43  GLN 43  43  43  GLN GLN LLL . n 
H 3 44  GLN 44  44  44  GLN GLN LLL . n 
H 3 45  LYS 45  45  45  LYS LYS LLL . n 
H 3 46  PRO 46  46  46  PRO PRO LLL . n 
H 3 47  GLY 47  47  47  GLY GLY LLL . n 
H 3 48  GLN 48  48  48  GLN GLN LLL . n 
H 3 49  PRO 49  49  49  PRO PRO LLL . n 
H 3 50  PRO 50  50  50  PRO PRO LLL . n 
H 3 51  LYS 51  51  51  LYS LYS LLL . n 
H 3 52  LEU 52  52  52  LEU LEU LLL . n 
H 3 53  LEU 53  53  53  LEU LEU LLL . n 
H 3 54  ILE 54  54  54  ILE ILE LLL . n 
H 3 55  TYR 55  55  55  TYR TYR LLL . n 
H 3 56  TRP 56  56  56  TRP TRP LLL . n 
H 3 57  ALA 57  57  57  ALA ALA LLL . n 
H 3 58  SER 58  58  58  SER SER LLL . n 
H 3 59  THR 59  59  59  THR THR LLL . n 
H 3 60  ARG 60  60  60  ARG ARG LLL . n 
H 3 61  GLU 61  61  61  GLU GLU LLL . n 
H 3 62  SER 62  62  62  SER SER LLL . n 
H 3 63  GLY 63  63  63  GLY GLY LLL . n 
H 3 64  VAL 64  64  64  VAL VAL LLL . n 
H 3 65  PRO 65  65  65  PRO PRO LLL . n 
H 3 66  ASP 66  66  66  ASP ASP LLL . n 
H 3 67  ARG 67  67  67  ARG ARG LLL . n 
H 3 68  PHE 68  68  68  PHE PHE LLL . n 
H 3 69  SER 69  69  69  SER SER LLL . n 
H 3 70  GLY 70  70  70  GLY GLY LLL . n 
H 3 71  SER 71  71  71  SER SER LLL . n 
H 3 72  GLY 72  72  72  GLY GLY LLL . n 
H 3 73  SER 73  73  73  SER SER LLL . n 
H 3 74  GLY 74  74  74  GLY GLY LLL . n 
H 3 75  THR 75  75  75  THR THR LLL . n 
H 3 76  ASP 76  76  76  ASP ASP LLL . n 
H 3 77  PHE 77  77  77  PHE PHE LLL . n 
H 3 78  THR 78  78  78  THR THR LLL . n 
H 3 79  LEU 79  79  79  LEU LEU LLL . n 
H 3 80  THR 80  80  80  THR THR LLL . n 
H 3 81  ILE 81  81  81  ILE ILE LLL . n 
H 3 82  SER 82  82  82  SER SER LLL . n 
H 3 83  SER 83  83  83  SER SER LLL . n 
H 3 84  LEU 84  84  84  LEU LEU LLL . n 
H 3 85  GLN 85  85  85  GLN GLN LLL . n 
H 3 86  ALA 86  86  86  ALA ALA LLL . n 
H 3 87  GLU 87  87  87  GLU GLU LLL . n 
H 3 88  ASP 88  88  88  ASP ASP LLL . n 
H 3 89  VAL 89  89  89  VAL VAL LLL . n 
H 3 90  ALA 90  90  90  ALA ALA LLL . n 
H 3 91  VAL 91  91  91  VAL VAL LLL . n 
H 3 92  TYR 92  92  92  TYR TYR LLL . n 
H 3 93  TYR 93  93  93  TYR TYR LLL . n 
H 3 94  CYS 94  94  94  CYS CYS LLL . n 
H 3 95  GLN 95  95  95  GLN GLN LLL . n 
H 3 96  GLN 96  96  96  GLN GLN LLL . n 
H 3 97  TYR 97  97  97  TYR TYR LLL . n 
H 3 98  TYR 98  98  98  TYR TYR LLL . n 
H 3 99  SER 99  99  99  SER SER LLL . n 
H 3 100 THR 100 100 100 THR THR LLL . n 
H 3 101 PRO 101 101 101 PRO PRO LLL . n 
H 3 102 TYR 102 102 102 TYR TYR LLL . n 
H 3 103 THR 103 103 103 THR THR LLL . n 
H 3 104 PHE 104 104 104 PHE PHE LLL . n 
H 3 105 GLY 105 105 105 GLY GLY LLL . n 
H 3 106 GLN 106 106 106 GLN GLN LLL . n 
H 3 107 GLY 107 107 107 GLY GLY LLL . n 
H 3 108 THR 108 108 108 THR THR LLL . n 
H 3 109 LYS 109 109 109 LYS LYS LLL . n 
H 3 110 VAL 110 110 110 VAL VAL LLL . n 
H 3 111 GLU 111 111 111 GLU GLU LLL . n 
H 3 112 ILE 112 112 112 ILE ILE LLL . n 
H 3 113 LYS 113 113 113 LYS LYS LLL . n 
H 3 114 ARG 114 114 114 ARG ARG LLL . n 
H 3 115 THR 115 115 115 THR THR LLL . n 
H 3 116 VAL 116 116 116 VAL VAL LLL . n 
H 3 117 ALA 117 117 117 ALA ALA LLL . n 
H 3 118 ALA 118 118 118 ALA ALA LLL . n 
H 3 119 PRO 119 119 119 PRO PRO LLL . n 
H 3 120 SER 120 120 120 SER SER LLL . n 
H 3 121 VAL 121 121 121 VAL VAL LLL . n 
H 3 122 PHE 122 122 122 PHE PHE LLL . n 
H 3 123 ILE 123 123 123 ILE ILE LLL . n 
H 3 124 PHE 124 124 124 PHE PHE LLL . n 
H 3 125 PRO 125 125 125 PRO PRO LLL . n 
H 3 126 PRO 126 126 126 PRO PRO LLL . n 
H 3 127 SER 127 127 127 SER SER LLL . n 
H 3 128 ASP 128 128 128 ASP ASP LLL . n 
H 3 129 GLU 129 129 129 GLU GLU LLL . n 
H 3 130 GLN 130 130 130 GLN GLN LLL . n 
H 3 131 LEU 131 131 131 LEU LEU LLL . n 
H 3 132 LYS 132 132 132 LYS LYS LLL . n 
H 3 133 SER 133 133 133 SER SER LLL . n 
H 3 134 GLY 134 134 134 GLY GLY LLL . n 
H 3 135 THR 135 135 135 THR THR LLL . n 
H 3 136 ALA 136 136 136 ALA ALA LLL . n 
H 3 137 SER 137 137 137 SER SER LLL . n 
H 3 138 VAL 138 138 138 VAL VAL LLL . n 
H 3 139 VAL 139 139 139 VAL VAL LLL . n 
H 3 140 CYS 140 140 140 CYS CYS LLL . n 
H 3 141 LEU 141 141 141 LEU LEU LLL . n 
H 3 142 LEU 142 142 142 LEU LEU LLL . n 
H 3 143 ASN 143 143 143 ASN ASN LLL . n 
H 3 144 ASN 144 144 144 ASN ASN LLL . n 
H 3 145 PHE 145 145 145 PHE PHE LLL . n 
H 3 146 TYR 146 146 146 TYR TYR LLL . n 
H 3 147 PRO 147 147 147 PRO PRO LLL . n 
H 3 148 ARG 148 148 148 ARG ARG LLL . n 
H 3 149 GLU 149 149 149 GLU GLU LLL . n 
H 3 150 ALA 150 150 150 ALA ALA LLL . n 
H 3 151 LYS 151 151 151 LYS LYS LLL . n 
H 3 152 VAL 152 152 152 VAL VAL LLL . n 
H 3 153 GLN 153 153 153 GLN GLN LLL . n 
H 3 154 TRP 154 154 154 TRP TRP LLL . n 
H 3 155 LYS 155 155 155 LYS LYS LLL . n 
H 3 156 VAL 156 156 156 VAL VAL LLL . n 
H 3 157 ASP 157 157 157 ASP ASP LLL . n 
H 3 158 ASN 158 158 158 ASN ASN LLL . n 
H 3 159 ALA 159 159 159 ALA ALA LLL . n 
H 3 160 LEU 160 160 160 LEU LEU LLL . n 
H 3 161 GLN 161 161 161 GLN GLN LLL . n 
H 3 162 SER 162 162 162 SER SER LLL . n 
H 3 163 GLY 163 163 163 GLY GLY LLL . n 
H 3 164 ASN 164 164 164 ASN ASN LLL . n 
H 3 165 SER 165 165 165 SER SER LLL . n 
H 3 166 GLN 166 166 166 GLN GLN LLL . n 
H 3 167 GLU 167 167 167 GLU GLU LLL . n 
H 3 168 SER 168 168 168 SER SER LLL . n 
H 3 169 VAL 169 169 169 VAL VAL LLL . n 
H 3 170 THR 170 170 170 THR THR LLL . n 
H 3 171 GLU 171 171 171 GLU GLU LLL . n 
H 3 172 GLN 172 172 172 GLN GLN LLL . n 
H 3 173 ASP 173 173 173 ASP ASP LLL . n 
H 3 174 SER 174 174 174 SER SER LLL . n 
H 3 175 LYS 175 175 175 LYS LYS LLL . n 
H 3 176 ASP 176 176 176 ASP ASP LLL . n 
H 3 177 SER 177 177 177 SER SER LLL . n 
H 3 178 THR 178 178 178 THR THR LLL . n 
H 3 179 TYR 179 179 179 TYR TYR LLL . n 
H 3 180 SER 180 180 180 SER SER LLL . n 
H 3 181 LEU 181 181 181 LEU LEU LLL . n 
H 3 182 SER 182 182 182 SER SER LLL . n 
H 3 183 SER 183 183 183 SER SER LLL . n 
H 3 184 THR 184 184 184 THR THR LLL . n 
H 3 185 LEU 185 185 185 LEU LEU LLL . n 
H 3 186 THR 186 186 186 THR THR LLL . n 
H 3 187 LEU 187 187 187 LEU LEU LLL . n 
H 3 188 SER 188 188 188 SER SER LLL . n 
H 3 189 LYS 189 189 189 LYS LYS LLL . n 
H 3 190 ALA 190 190 190 ALA ALA LLL . n 
H 3 191 ASP 191 191 191 ASP ASP LLL . n 
H 3 192 TYR 192 192 192 TYR TYR LLL . n 
H 3 193 GLU 193 193 193 GLU GLU LLL . n 
H 3 194 LYS 194 194 194 LYS LYS LLL . n 
H 3 195 HIS 195 195 195 HIS HIS LLL . n 
H 3 196 LYS 196 196 196 LYS LYS LLL . n 
H 3 197 VAL 197 197 197 VAL VAL LLL . n 
H 3 198 TYR 198 198 198 TYR TYR LLL . n 
H 3 199 ALA 199 199 199 ALA ALA LLL . n 
H 3 200 CYS 200 200 200 CYS CYS LLL . n 
H 3 201 GLU 201 201 201 GLU GLU LLL . n 
H 3 202 VAL 202 202 202 VAL VAL LLL . n 
H 3 203 THR 203 203 203 THR THR LLL . n 
H 3 204 HIS 204 204 204 HIS HIS LLL . n 
H 3 205 GLN 205 205 205 GLN GLN LLL . n 
H 3 206 GLY 206 206 206 GLY GLY LLL . n 
H 3 207 LEU 207 207 207 LEU LEU LLL . n 
H 3 208 SER 208 208 208 SER SER LLL . n 
H 3 209 SER 209 209 209 SER SER LLL . n 
H 3 210 PRO 210 210 210 PRO PRO LLL . n 
H 3 211 VAL 211 211 211 VAL VAL LLL . n 
H 3 212 THR 212 212 212 THR THR LLL . n 
H 3 213 LYS 213 213 213 LYS LYS LLL . n 
H 3 214 SER 214 214 214 SER SER LLL . n 
H 3 215 PHE 215 215 215 PHE PHE LLL . n 
H 3 216 ASN 216 216 216 ASN ASN LLL . n 
H 3 217 ARG 217 217 217 ARG ARG LLL . n 
H 3 218 GLY 218 218 218 GLY GLY LLL . n 
H 3 219 GLU 219 219 219 GLU GLU LLL . n 
H 3 220 CYS 220 220 ?   ?   ?   LLL . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
I 5 NAG 1 601 601 NAG NAG AAA . 
J 5 NAG 1 601 601 NAG NAG EEE . 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? tetrameric 4 
2 author_defined_assembly ? tetrameric 4 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,C,D,I 
2 1 E,F,G,H,J 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
_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       2020-06-03 
# 
_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             ? 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined -55.3770 -30.5620 42.1650  0.4631 ? 0.2067  ? 0.1472  ? 0.9313 ? 0.0554  ? 0.7458 ? 7.3659 ? 
-2.6568 ? -4.4313 ? 6.6534 ? 3.0509   ? 4.7085  ? 0.1805  ? -0.3527 ? 1.6956  ? -0.8589 ? 0.3432  ? -0.5248 ? -0.6016 ? -0.3872 ? 
-0.5238 ? 
2  'X-RAY DIFFRACTION' ? refined -60.4080 -42.2160 59.5660  0.5946 ? 0.1167  ? 0.1039  ? 1.1689 ? 0.0617  ? 0.3966 ? 3.5821 ? 
0.9232  ? -2.6271 ? 3.7845 ? 0.3642   ? 4.4103  ? -0.1016 ? -1.0358 ? -0.1034 ? 1.0771  ? 0.2374  ? -0.1497 ? 0.6998  ? -0.0586 ? 
-0.1358 ? 
3  'X-RAY DIFFRACTION' ? refined -54.2670 -34.4780 47.6050  0.2106 ? 0.1083  ? 0.2430  ? 0.8388 ? -0.0669 ? 0.4238 ? 6.5974 ? 
-0.4703 ? 4.9164  ? 5.7711 ? -1.0515  ? 10.3103 ? 0.2222  ? 0.0143  ? 0.8048  ? -0.2827 ? -0.3062 ? -0.1503 ? -0.0172 ? 0.0335  ? 
0.0840  ? 
4  'X-RAY DIFFRACTION' ? refined -35.9670 -55.0050 28.1100  0.2356 ? -0.0382 ? -0.1112 ? 0.3703 ? 0.0795  ? 0.2196 ? 2.7805 ? 
-0.6427 ? -2.0569 ? 2.8859 ? 1.8810   ? 5.0671  ? -0.0843 ? -0.3390 ? -0.3405 ? 0.0482  ? 0.4072  ? 0.2592  ? 0.5864  ? 0.1540  ? 
-0.3229 ? 
5  'X-RAY DIFFRACTION' ? refined -21.3260 -62.3100 3.8940   1.0624 ? 0.0089  ? -0.2575 ? 0.4927 ? -0.2275 ? 0.5663 ? 4.8000 ? 
0.1641  ? -0.2146 ? 4.5180 ? -1.6880  ? 5.4693  ? -0.4964 ? -0.2188 ? 0.4779  ? -0.1836 ? -0.0324 ? -0.5064 ? -0.4729 ? 0.5245  ? 
0.5288  ? 
6  'X-RAY DIFFRACTION' ? refined -54.4660 -49.4690 16.8770  0.1903 ? -0.0710 ? -0.1512 ? 0.4044 ? 0.0478  ? 0.3306 ? 3.3937 ? 
-1.1327 ? -0.8560 ? 5.2558 ? 0.1408   ? 8.6397  ? 0.3145  ? 0.0610  ? -0.5631 ? -0.4611 ? -0.0364 ? 0.9338  ? 0.0898  ? -0.8631 ? 
-0.2780 ? 
7  'X-RAY DIFFRACTION' ? refined -32.2900 -71.2750 -5.2190  0.7983 ? -0.1589 ? -0.0858 ? 0.3851 ? -0.2053 ? 0.3180 ? 3.6834 ? 
-3.9389 ? 0.0460  ? 8.8523 ? 1.0055   ? 3.9715  ? -0.0797 ? -0.1292 ? -0.1720 ? -0.4094 ? 0.0450  ? -0.3587 ? 0.0797  ? -0.0509 ? 
0.0347  ? 
8  'X-RAY DIFFRACTION' ? refined -60.1950 -27.2090 88.5180  2.6458 ? -0.3482 ? 0.0915  ? 2.9929 ? -0.4970 ? 1.2371 ? 1.5746 ? 
-2.4941 ? -1.1441 ? 4.0038 ? 1.8430   ? 0.8572  ? -0.4197 ? -0.1082 ? -0.0806 ? 0.9266  ? 0.0308  ? 0.2628  ? 0.5461  ? -0.1624 ? 
0.3889  ? 
9  'X-RAY DIFFRACTION' ? refined -62.5460 -34.8320 88.1220  2.5035 ? -0.0195 ? 0.2266  ? 2.9429 ? -0.4292 ? 1.1242 ? 1.0142 ? 
0.5009  ? 0.6158  ? 0.3498 ? 0.1893   ? 0.5202  ? 0.5110  ? -0.7812 ? 0.5297  ? 0.7008  ? -0.5872 ? 0.3174  ? -0.0245 ? -0.2516 ? 
0.0762  ? 
10 'X-RAY DIFFRACTION' ? refined -56.7230 -34.5680 87.2280  2.0234 ? -0.1349 ? 0.1048  ? 2.1143 ? -0.1330 ? 0.7944 ? 1.4054 ? 
0.8449  ? -0.1904 ? 2.0189 ? -0.3175  ? 0.0658  ? 0.3227  ? -0.1790 ? 0.3625  ? 0.2958  ? -0.2347 ? 0.4205  ? -0.2141 ? 0.0647  ? 
-0.0880 ? 
11 'X-RAY DIFFRACTION' ? refined -46.6100 -22.8480 2.4000   0.3292 ? 0.1961  ? 0.0743  ? 0.3256 ? 0.1293  ? 0.3974 ? 2.0964 ? 
-0.3363 ? 0.8500  ? 6.6741 ? -1.4968  ? 7.9488  ? 0.4019  ? -0.1540 ? -0.3645 ? 0.0206  ? -0.0904 ? 1.2801  ? -0.6056 ? -0.6456 ? 
-0.3115 ? 
12 'X-RAY DIFFRACTION' ? refined -36.1950 -19.9770 -1.1030  0.2733 ? 0.1162  ? 0.0828  ? 0.2509 ? 0.0185  ? 0.2271 ? 4.2888 ? 
0.4570  ? 0.9881  ? 6.0627 ? 0.3154   ? 8.1297  ? -0.0780 ? -0.1960 ? -0.2323 ? -0.0264 ? 0.3723  ? -0.0029 ? 0.2347  ? 0.5514  ? 
-0.2943 ? 
13 'X-RAY DIFFRACTION' ? refined -34.9760 -17.4400 -12.9780 0.4506 ? 0.0289  ? 0.0780  ? 0.3837 ? -0.0299 ? 0.0263 ? 2.6087 ? 
0.1828  ? -0.1091 ? 3.9155 ? -2.3449  ? 5.5265  ? 0.0102  ? 0.2476  ? -0.0933 ? -0.4895 ? 0.2590  ? 0.0212  ? -0.5938 ? 0.5329  ? 
-0.2691 ? 
14 'X-RAY DIFFRACTION' ? refined -48.0370 -14.2760 15.5540  1.0633 ? 0.1367  ? 0.2143  ? 0.9298 ? -0.1111 ? 0.9123 ? 4.9019 ? 
-5.4758 ? 7.5365  ? 8.4776 ? -10.0419 ? 13.3374 ? -0.4790 ? -0.9285 ? 0.4616  ? 0.3924  ? 0.3693  ? 0.7057  ? 0.1901  ? -0.8893 ? 
0.1097  ? 
15 'X-RAY DIFFRACTION' ? refined -39.2730 -13.4190 -41.6480 0.5324 ? 0.0706  ? 0.0312  ? 0.3326 ? 0.0357  ? 0.3196 ? 4.2686 ? 
-0.9124 ? 0.0010  ? 2.6393 ? 1.1319   ? 9.1706  ? 0.0604  ? -0.2508 ? -0.3141 ? 0.0407  ? 0.1145  ? 0.4671  ? -0.4515 ? -0.3597 ? 
-0.1749 ? 
16 'X-RAY DIFFRACTION' ? refined -38.2750 -13.5710 -41.1650 0.4776 ? 0.1206  ? 0.0700  ? 0.3789 ? -0.0397 ? 0.2466 ? 1.4734 ? 
-0.1329 ? 1.2640  ? 3.1358 ? 0.8990   ? 10.1624 ? 0.1378  ? -0.1427 ? -0.1111 ? -0.0738 ? 0.0305  ? 0.2805  ? -0.6603 ? 0.0394  ? 
-0.1683 ? 
17 'X-RAY DIFFRACTION' ? refined -22.8100 -40.4530 16.8470  0.2476 ? 0.0343  ? 0.0468  ? 0.2960 ? -0.0560 ? 0.0637 ? 2.9787 ? 
-0.8579 ? 2.0651  ? 3.8086 ? -2.9297  ? 4.4577  ? 0.6177  ? 0.0563  ? -0.0042 ? -0.3061 ? -0.4770 ? -0.1607 ? 0.2232  ? 0.4146  ? 
-0.1407 ? 
18 'X-RAY DIFFRACTION' ? refined -16.1870 -54.2900 45.2530  0.5251 ? -0.3069 ? -0.2098 ? 0.9176 ? 0.2721  ? 0.5202 ? 3.6002 ? 
-2.2155 ? 0.7137  ? 3.5959 ? -0.6495  ? 6.1543  ? 0.4697  ? -0.8352 ? -0.8912 ? 0.2945  ? 0.0310  ? 0.4851  ? 0.6584  ? -0.4535 ? 
-0.5007 ? 
19 'X-RAY DIFFRACTION' ? refined -28.0290 -22.5260 30.2390  0.3051 ? -0.0521 ? 0.0793  ? 0.3366 ? -0.1360 ? 0.1354 ? 5.0720 ? 
-1.2448 ? 0.9174  ? 4.1141 ? -1.7829  ? 6.8563  ? 0.0089  ? -0.4313 ? 0.6287  ? 0.3993  ? 0.0257  ? -0.3094 ? -0.8755 ? -0.2193 ? 
-0.0346 ? 
20 'X-RAY DIFFRACTION' ? refined -6.3220  -44.1130 52.7160  0.3336 ? -0.3074 ? -0.0433 ? 0.8456 ? 0.2187  ? 0.1468 ? 8.7459 ? 
-4.3604 ? 3.5194  ? 6.7445 ? -1.1786  ? 4.1406  ? 0.3969  ? -1.0501 ? -0.5119 ? 0.0148  ? -0.1924 ? -0.4298 ? -0.0925 ? -0.3568 ? 
-0.2045 ? 
21 'X-RAY DIFFRACTION' ? refined -57.6380 -36.9750 51.6600  0.2855 ? 0.1148  ? 0.1049  ? 0.8624 ? 0.0182  ? 0.3317 ? 4.7078 ? 
0.3466  ? -2.3920 ? 4.0650 ? 1.0891   ? 4.0617  ? 0.1268  ? -0.5662 ? 0.5436  ? 0.2249  ? 0.1237  ? -0.0942 ? 0.1270  ? -0.2138 ? 
-0.2504 ? 
22 'X-RAY DIFFRACTION' ? refined -30.7650 -57.6080 19.5410  0.3675 ? -0.0690 ? -0.1564 ? 0.3769 ? -0.0110 ? 0.2610 ? 1.7108 ? 
-0.6951 ? -1.7744 ? 2.1849 ? 1.0097   ? 3.8773  ? -0.0257 ? -0.0629 ? -0.2108 ? -0.3620 ? 0.3609  ? 0.0548  ? 0.5117  ? 0.2721  ? 
-0.3353 ? 
23 'X-RAY DIFFRACTION' ? refined -43.7780 -59.9820 6.2380   0.4513 ? -0.1425 ? -0.2283 ? 0.4469 ? -0.0298 ? 0.4392 ? 1.1542 ? 
-1.3410 ? -1.7021 ? 4.1209 ? 2.0552   ? 3.5770  ? 0.1349  ? 0.1066  ? -0.2961 ? -0.6863 ? -0.0170 ? 0.4178  ? 0.0837  ? -0.3604 ? 
-0.1179 ? 
24 'X-RAY DIFFRACTION' ? refined -60.7060 -32.4480 88.0380  2.0844 ? -0.1756 ? 0.1618  ? 2.4586 ? -0.3516 ? 0.9956 ? 0.0566 ? 
0.0455  ? -0.0057 ? 0.0703 ? -0.0004  ? 0.0012  ? 0.2280  ? -0.2058 ? 0.1683  ? 0.3428  ? -0.1965 ? 0.0112  ? 0.0024  ? 0.0283  ? 
-0.0316 ? 
25 'X-RAY DIFFRACTION' ? refined -39.1790 -19.1930 -4.7330  0.2926 ? 0.1196  ? 0.0510  ? 0.2681 ? 0.0147  ? 0.1165 ? 2.2998 ? 
0.6710  ? 0.6093  ? 4.3479 ? -1.1858  ? 4.3510  ? 0.0313  ? -0.0765 ? -0.1351 ? -0.0980 ? 0.2405  ? 0.3480  ? -0.5283 ? 0.0845  ? 
-0.2718 ? 
26 'X-RAY DIFFRACTION' ? refined -38.8290 -13.4640 -41.3800 0.4215 ? 0.0809  ? 0.0489  ? 0.2279 ? -0.0113 ? 0.2249 ? 2.8021 ? 
-0.8709 ? 0.6770  ? 1.9016 ? 0.5956   ? 9.3262  ? 0.0465  ? -0.1719 ? -0.2281 ? 0.0000  ? 0.1547  ? 0.4082  ? -0.5881 ? -0.2245 ? 
-0.2012 ? 
27 'X-RAY DIFFRACTION' ? refined -20.2180 -45.8580 27.8960  0.2533 ? -0.1243 ? -0.0507 ? 0.3833 ? 0.0356  ? 0.1665 ? 2.8475 ? 
-1.0990 ? 2.0925  ? 2.4235 ? -1.8220  ? 3.9703  ? 0.5415  ? -0.4402 ? -0.4394 ? 0.0189  ? -0.2055 ? -0.0275 ? 0.3040  ? 0.1328  ? 
-0.3360 ? 
28 'X-RAY DIFFRACTION' ? refined -17.7300 -32.7620 40.9010  0.2938 ? -0.2047 ? 0.0419  ? 0.4824 ? -0.0501 ? 0.0794 ? 5.2998 ? 
-2.1719 ? 3.0614  ? 2.2289 ? -2.3104  ? 4.0605  ? -0.0055 ? -0.8523 ? 0.0684  ? 0.3194  ? -0.0243 ? -0.1608 ? -0.4402 ? -0.2494 ? 
0.0298  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.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.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  ? ? AAA 334 ? ? AAA 398 ALL ? 
2  'X-RAY DIFFRACTION' 2  ? ? AAA 399 ? ? AAA 493 ALL ? 
3  'X-RAY DIFFRACTION' 3  ? ? AAA 494 ? ? AAA 528 ALL ? 
4  'X-RAY DIFFRACTION' 4  ? ? BBB 0   ? ? BBB 143 ALL ? 
5  'X-RAY DIFFRACTION' 5  ? ? BBB 144 ? ? BBB 219 ALL ? 
6  'X-RAY DIFFRACTION' 6  ? ? CCC 1   ? ? CCC 113 ALL ? 
7  'X-RAY DIFFRACTION' 7  ? ? CCC 114 ? ? CCC 219 ALL ? 
8  'X-RAY DIFFRACTION' 8  ? ? DDD 1   ? ? DDD 42  ALL ? 
9  'X-RAY DIFFRACTION' 9  ? ? DDD 43  ? ? DDD 103 ALL ? 
10 'X-RAY DIFFRACTION' 10 ? ? DDD 104 ? ? DDD 128 ALL ? 
11 'X-RAY DIFFRACTION' 11 ? ? EEE 334 ? ? EEE 386 ALL ? 
12 'X-RAY DIFFRACTION' 12 ? ? EEE 387 ? ? EEE 423 ALL ? 
13 'X-RAY DIFFRACTION' 13 ? ? EEE 424 ? ? EEE 515 ALL ? 
14 'X-RAY DIFFRACTION' 14 ? ? EEE 516 ? ? EEE 528 ALL ? 
15 'X-RAY DIFFRACTION' 15 ? ? FFF 1   ? ? FFF 67  ALL ? 
16 'X-RAY DIFFRACTION' 16 ? ? FFF 68  ? ? FFF 128 ALL ? 
17 'X-RAY DIFFRACTION' 17 ? ? HHH 0   ? ? HHH 129 ALL ? 
18 'X-RAY DIFFRACTION' 18 ? ? HHH 130 ? ? HHH 219 ALL ? 
19 'X-RAY DIFFRACTION' 19 ? ? LLL 1   ? ? LLL 114 ALL ? 
20 'X-RAY DIFFRACTION' 20 ? ? LLL 115 ? ? LLL 219 ALL ? 
21 'X-RAY DIFFRACTION' 21 ? ? AAA 334 ? ? AAA 528 ALL ? 
22 'X-RAY DIFFRACTION' 22 ? ? BBB 0   ? ? BBB 219 ALL ? 
23 'X-RAY DIFFRACTION' 23 ? ? CCC 1   ? ? CCC 219 ALL ? 
24 'X-RAY DIFFRACTION' 24 ? ? DDD 1   ? ? DDD 128 ALL ? 
25 'X-RAY DIFFRACTION' 25 ? ? EEE 334 ? ? EEE 528 ALL ? 
26 'X-RAY DIFFRACTION' 26 ? ? FFF 1   ? ? FFF 128 ALL ? 
27 'X-RAY DIFFRACTION' 27 ? ? HHH 0   ? ? HHH 219 ALL ? 
28 'X-RAY DIFFRACTION' 28 ? ? LLL 1   ? ? LLL 219 ALL ? 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0258 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        3 
# 
_pdbx_entry_details.entry_id                 6YZ7 
_pdbx_entry_details.has_ligand_of_interest   N 
_pdbx_entry_details.compound_details         ? 
_pdbx_entry_details.source_details           ? 
_pdbx_entry_details.nonpolymer_details       ? 
_pdbx_entry_details.sequence_details         ? 
# 
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 OH DDD TYR 60 ? ? N  DDD ILE 70 ? ? 1.68 
2 1 OH FFF TYR 60 ? ? N  FFF ILE 70 ? ? 1.69 
3 1 OH FFF TYR 60 ? ? CA FFF THR 69 ? ? 1.94 
4 1 OH DDD TYR 60 ? ? CA DDD THR 69 ? ? 1.94 
5 1 OH DDD TYR 60 ? ? C  DDD THR 69 ? ? 2.02 
6 1 OH FFF TYR 60 ? ? C  FFF THR 69 ? ? 2.02 
# 
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 VAL AAA 341 ? ? -123.99 -60.26  
2  1 PHE AAA 377 ? ? -119.60 64.67   
3  1 ASP AAA 389 ? ? -151.57 38.98   
4  1 ALA AAA 411 ? ? -175.92 144.28  
5  1 ASN AAA 422 ? ? -129.23 -64.04  
6  1 ASP AAA 428 ? ? -92.02  44.67   
7  1 SER AAA 438 ? ? -140.02 39.14   
8  1 ARG AAA 457 ? ? -177.30 140.13  
9  1 ASN AAA 481 ? ? -105.23 49.82   
10 1 PHE AAA 486 ? ? -57.58  109.84  
11 1 LEU AAA 518 ? ? -81.99  -152.31 
12 1 THR AAA 523 ? ? -154.24 23.52   
13 1 PRO AAA 527 ? ? -65.03  -82.26  
14 1 PRO BBB 41  ? ? -45.38  106.17  
15 1 PHE BBB 64  ? ? -143.55 -27.84  
16 1 GLN BBB 65  ? ? -15.58  -71.87  
17 1 SER BBB 85  ? ? -172.53 124.14  
18 1 ALA BBB 92  ? ? 177.92  174.71  
19 1 SER BBB 160 ? ? 86.96   -16.66  
20 1 ALA BBB 162 ? ? -95.63  52.18   
21 1 LEU BBB 163 ? ? -171.46 84.46   
22 1 SER BBB 165 ? ? -53.93  80.82   
23 1 THR BBB 195 ? ? -137.98 -73.07  
24 1 ASN CCC 35  ? ? -39.82  72.68   
25 1 TRP CCC 56  ? ? 26.51   50.74   
26 1 ALA CCC 57  ? ? 76.85   -26.16  
27 1 SER CCC 58  ? ? -148.32 -23.43  
28 1 ILE CCC 81  ? ? -110.16 75.27   
29 1 ALA CCC 86  ? ? -34.98  -73.37  
30 1 ALA CCC 90  ? ? 175.25  179.27  
31 1 ASN CCC 144 ? ? 51.63   91.87   
32 1 GLU CCC 149 ? ? -62.76  91.23   
33 1 ASN CCC 158 ? ? 38.71   53.32   
34 1 SER CCC 162 ? ? -165.65 108.09  
35 1 SER CCC 208 ? ? -45.16  -74.47  
36 1 ARG DDD 27  ? ? -65.73  82.81   
37 1 ARG DDD 67  ? ? -125.97 -57.01  
38 1 ALA DDD 110 ? ? -98.46  -64.73  
39 1 SER DDD 126 ? ? -121.69 -148.14 
40 1 VAL EEE 341 ? ? -124.59 -60.03  
41 1 SER EEE 373 ? ? -93.58  58.88   
42 1 PHE EEE 377 ? ? -119.18 65.34   
43 1 ASP EEE 389 ? ? -151.68 40.01   
44 1 ALA EEE 411 ? ? -176.88 144.47  
45 1 ASN EEE 422 ? ? -128.81 -64.66  
46 1 ASP EEE 428 ? ? -92.55  48.27   
47 1 SER EEE 438 ? ? -140.35 39.53   
48 1 ARG EEE 457 ? ? -178.88 141.24  
49 1 ASN EEE 481 ? ? -105.00 49.19   
50 1 LEU EEE 518 ? ? -81.43  -149.25 
51 1 THR EEE 523 ? ? -154.23 22.48   
52 1 PRO EEE 527 ? ? -65.18  -82.01  
53 1 ARG FFF 27  ? ? -66.48  83.10   
54 1 SER FFF 54  ? ? -97.69  60.00   
55 1 ARG FFF 67  ? ? -126.69 -56.78  
56 1 ALA FFF 110 ? ? -97.05  -64.87  
57 1 SER FFF 126 ? ? -122.64 -147.95 
58 1 PRO HHH 41  ? ? -44.86  105.49  
59 1 PHE HHH 64  ? ? -143.10 -27.38  
60 1 GLN HHH 65  ? ? -17.53  -69.54  
61 1 GLN HHH 67  ? ? -101.00 -62.29  
62 1 SER HHH 85  ? ? -172.40 125.81  
63 1 ALA HHH 92  ? ? 176.21  174.58  
64 1 SER HHH 160 ? ? 87.66   -18.38  
65 1 ALA HHH 162 ? ? -94.85  51.50   
66 1 LEU HHH 163 ? ? -172.09 80.84   
67 1 SER HHH 165 ? ? -60.11  85.17   
68 1 THR HHH 195 ? ? -135.68 -71.91  
69 1 ASN HHH 208 ? ? 37.58   55.65   
70 1 SER LLL 33  ? ? -39.58  -70.47  
71 1 ASN LLL 35  ? ? -42.68  74.48   
72 1 TRP LLL 56  ? ? 26.75   50.89   
73 1 ALA LLL 57  ? ? 77.13   -27.09  
74 1 SER LLL 58  ? ? -148.07 -23.35  
75 1 ILE LLL 81  ? ? -109.28 75.77   
76 1 ALA LLL 86  ? ? -36.71  -71.59  
77 1 ALA LLL 90  ? ? 177.19  -179.69 
78 1 ASN LLL 144 ? ? 51.97   91.94   
79 1 GLU LLL 149 ? ? -63.59  91.43   
80 1 ASN LLL 158 ? ? 37.54   54.15   
81 1 SER LLL 162 ? ? -162.95 105.95  
82 1 SER LLL 208 ? ? -43.96  -75.58  
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   GLY 
_pdbx_validate_peptide_omega.auth_asym_id_1   BBB 
_pdbx_validate_peptide_omega.auth_seq_id_1    98 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   GLY 
_pdbx_validate_peptide_omega.auth_asym_id_2   BBB 
_pdbx_validate_peptide_omega.auth_seq_id_2    99 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            149.23 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 AAA PRO 330 ? A PRO 1   
2  1 Y 1 AAA ASN 331 ? A ASN 2   
3  1 Y 1 AAA ILE 332 ? A ILE 3   
4  1 Y 1 AAA THR 333 ? A THR 4   
5  1 Y 1 AAA LYS 529 ? A LYS 200 
6  1 Y 1 AAA SER 530 ? A SER 201 
7  1 Y 1 AAA THR 531 ? A THR 202 
8  1 Y 1 AAA ASN 532 ? A ASN 203 
9  1 Y 1 AAA LYS 533 ? A LYS 204 
10 1 Y 1 AAA HIS 534 ? A HIS 205 
11 1 Y 1 AAA HIS 535 ? A HIS 206 
12 1 Y 1 AAA HIS 536 ? A HIS 207 
13 1 Y 1 AAA HIS 537 ? A HIS 208 
14 1 Y 1 AAA HIS 538 ? A HIS 209 
15 1 Y 1 AAA HIS 539 ? A HIS 210 
16 1 Y 1 BBB LYS 133 ? B LYS 134 
17 1 Y 1 BBB SER 134 ? B SER 135 
18 1 Y 1 BBB THR 135 ? B THR 136 
19 1 Y 1 BBB SER 136 ? B SER 137 
20 1 Y 1 BBB CYS 220 ? B CYS 221 
21 1 Y 1 BBB ASP 221 ? B ASP 222 
22 1 Y 1 BBB LYS 222 ? B LYS 223 
23 1 Y 1 BBB HIS 223 ? B HIS 224 
24 1 Y 1 BBB HIS 224 ? B HIS 225 
25 1 Y 1 BBB HIS 225 ? B HIS 226 
26 1 Y 1 BBB HIS 226 ? B HIS 227 
27 1 Y 1 BBB HIS 227 ? B HIS 228 
28 1 Y 1 BBB HIS 228 ? B HIS 229 
29 1 Y 1 CCC CYS 220 ? C CYS 220 
30 1 Y 1 DDD LYS 128 ? D LYS 128 
31 1 Y 1 DDD HIS 129 ? D HIS 129 
32 1 Y 1 DDD HIS 130 ? D HIS 130 
33 1 Y 1 DDD HIS 131 ? D HIS 131 
34 1 Y 1 DDD HIS 132 ? D HIS 132 
35 1 Y 1 DDD HIS 133 ? D HIS 133 
36 1 Y 1 DDD HIS 134 ? D HIS 134 
37 1 Y 1 EEE PRO 330 ? E PRO 1   
38 1 Y 1 EEE ASN 331 ? E ASN 2   
39 1 Y 1 EEE ILE 332 ? E ILE 3   
40 1 Y 1 EEE THR 333 ? E THR 4   
41 1 Y 1 EEE LYS 529 ? E LYS 200 
42 1 Y 1 EEE SER 530 ? E SER 201 
43 1 Y 1 EEE THR 531 ? E THR 202 
44 1 Y 1 EEE ASN 532 ? E ASN 203 
45 1 Y 1 EEE LYS 533 ? E LYS 204 
46 1 Y 1 EEE HIS 534 ? E HIS 205 
47 1 Y 1 EEE HIS 535 ? E HIS 206 
48 1 Y 1 EEE HIS 536 ? E HIS 207 
49 1 Y 1 EEE HIS 537 ? E HIS 208 
50 1 Y 1 EEE HIS 538 ? E HIS 209 
51 1 Y 1 EEE HIS 539 ? E HIS 210 
52 1 Y 1 FFF LYS 128 ? F LYS 128 
53 1 Y 1 FFF HIS 129 ? F HIS 129 
54 1 Y 1 FFF HIS 130 ? F HIS 130 
55 1 Y 1 FFF HIS 131 ? F HIS 131 
56 1 Y 1 FFF HIS 132 ? F HIS 132 
57 1 Y 1 FFF HIS 133 ? F HIS 133 
58 1 Y 1 FFF HIS 134 ? F HIS 134 
59 1 Y 1 HHH LYS 133 ? G LYS 134 
60 1 Y 1 HHH SER 134 ? G SER 135 
61 1 Y 1 HHH THR 135 ? G THR 136 
62 1 Y 1 HHH SER 136 ? G SER 137 
63 1 Y 1 HHH CYS 220 ? G CYS 221 
64 1 Y 1 HHH ASP 221 ? G ASP 222 
65 1 Y 1 HHH LYS 222 ? G LYS 223 
66 1 Y 1 HHH HIS 223 ? G HIS 224 
67 1 Y 1 HHH HIS 224 ? G HIS 225 
68 1 Y 1 HHH HIS 225 ? G HIS 226 
69 1 Y 1 HHH HIS 226 ? G HIS 227 
70 1 Y 1 HHH HIS 227 ? G HIS 228 
71 1 Y 1 HHH HIS 228 ? G HIS 229 
72 1 Y 1 LLL CYS 220 ? H CYS 220 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Wellcome Trust'                                     'United Kingdom' 100209/Z/12/Z 1 
'Engineering and Physical Sciences Research Council' 'United Kingdom' EP/S025243/1. 2 
# 
_pdbx_entity_nonpoly.entity_id   5 
_pdbx_entity_nonpoly.name        N-ACETYL-D-GLUCOSAMINE 
_pdbx_entity_nonpoly.comp_id     NAG 
# 
_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                ? 
# 
