data_wwPDB_remediated_restraints_file_for_PDB_entry_1pba

# This wwPDB archive file contains, for PDB entry 1pba:
#
# - Sequence information from the PDB mmCIF file
# - NMR restraints from the PDB MR file
#
# In this file, the NMR restraints share the same atom names as in the coordinate 
# file, and in this way can differ from the data deposited at the wwPDB. To achieve
# this aim, the NMR restraints were parsed from their original format files, and
# the coordinates and NMR restraints information were subsequently harmonized.
#
# Due to the complexity of this harmonization process, minor modifications could
# have occurred to the NMR restraints information, or data could have been lost
# because of parsing or conversion errors. The PDB file remains the
# authoritative reference for the atomic coordinates and the originally deposited
# restraints files remain the primary reference for these data.
#
# This file is generated as part of the wwPDB at the BioMagResBank (BMRB) in
# collaboration with the PDBe (formerly MSD) group at the European
# Bioinformatics Institute (EBI) and the CMBI/IMM group at the Radboud
# University of Nijmegen.
#
# Several software packages were used to produce this file:
#
# - Wattos (BMRB and CMBI/IMM).
# - FormatConverter and NMRStarExport (PDBe).
# - CCPN framework (http://www.ccpn.ac.uk/).
#
# More information about this process can be found in the references below.
# Please cite the original reference for this PDB entry.
#
# JF Doreleijers, A Nederveen, W Vranken, J Lin, AM Bonvin, R Kaptein, JL
# Markley, and EL Ulrich (2005). BioMagResBank databases DOCR and FRED
# containing converted and filtered sets of experimental NMR restraints and
# coordinates from over 500 protein PDB structures. J. Biomol. NMR 32, 1-12.
#
# WF Vranken, W Boucher, TJ Stevens, RH Fogh, A Pajon, M Llinas, EL Ulrich, JL
# Markley, J Ionides, ED Laue (2005). The CCPN data model for NMR spectroscopy:
# development of a software pipeline. Proteins 59, 687-696.
#
# JF Doreleijers, WF Vranken, C Schulte, J Lin, JR Wedell, CJ Penkett, GW Vuister,
# G Vriend, JL Markley, and EL Ulrich (2009). The NMR Restraints Grid at BMRB for
# 5,266 Protein and Nucleic Acid PDB Entries. J Biomol. NMR 45, 389–396.


save_entry_information
   _Entry.Sf_category                   entry_information
   _Entry.Sf_framecode                  entry_information
   _Entry.ID                            rr_1pba
   _Entry.Title                        "wwPDB remediated NMR restraints for PDB entry 1pba"
   _Entry.NMR_STAR_version              3.1
   _Entry.Experimental_method           NMR
   _Entry.Experimental_method_subtype   solution
   _Entry.Details                      "Contains the remediated restraint lists and coordinates for PDB entry 1pba"

save_


save_assembly
   _Assembly.Sf_category            assembly
   _Assembly.Sf_framecode           assembly
   _Assembly.Entry_ID               rr_1pba
   _Assembly.ID                     1
   _Assembly.Name                   1pba
   _Assembly.Number_of_components   1
   _Assembly.Organic_ligands        0
   _Assembly.Metal_ions             0
   _Assembly.Non_standard_bonds     no
   _Assembly.Paramagnetic           no
   _Assembly.Thiol_state           "not present"
   _Assembly.Molecular_mass         9494.2732

   loop_
      _Entity_assembly.ID
      _Entity_assembly.Entity_assembly_name
      _Entity_assembly.Entity_ID
      _Entity_assembly.Entity_label
      _Entity_assembly.Asym_ID
      _Entity_assembly.PDB_chain_ID
      _Entity_assembly.Experimental_data_reported
      _Entity_assembly.Physical_state
      _Entity_assembly.Conformational_isomer
      _Entity_assembly.Chemical_exchange_state
      _Entity_assembly.Magnetic_equivalence_group_code
      _Entity_assembly.Role
      _Entity_assembly.Details
      _Entity_assembly.Entry_ID
      _Entity_assembly.Assembly_ID

      1 "PROCARBOXYPEPTIDASE B" 1 $PROCARBOXYPEPTIDASE_B A . no . . . . . . rr_1pba 1 

   stop_

save_


save_PROCARBOXYPEPTIDASE_B
   _Entity.Sf_category                       entity
   _Entity.Sf_framecode                      PROCARBOXYPEPTIDASE_B
   _Entity.Entry_ID                          rr_1pba
   _Entity.ID                                1
   _Entity.Name                              PROCARBOXYPEPTIDASE_B
   _Entity.Type                              polymer
   _Entity.Polymer_type                      polypeptide(L)
   _Entity.Polymer_strand_ID                 A
   _Entity.Polymer_seq_one_letter_code      
;
HHSGEHFEGEKVFRVNVEDE
NDISELHELASTRQIDFWKP
DSVTQIKPHSTVDFRVKAED
ILAVEDFLEQNELQYEVLIN
N
;
   _Entity.Ambiguous_conformational_states   no
   _Entity.Ambiguous_chem_comp_sites         no
   _Entity.Nstd_monomer                      no
   _Entity.Nstd_chirality                    no
   _Entity.Nstd_linkage                      no
   _Entity.Number_of_monomers                81
   _Entity.Paramagnetic                      no
   _Entity.Thiol_state                      "not present"
   _Entity.Parent_entity_ID                  1
   _Entity.Formula_weight                    9494.2732

   loop_
      _Entity_comp_index.ID
      _Entity_comp_index.Auth_seq_ID
      _Entity_comp_index.Comp_ID
      _Entity_comp_index.Comp_label
      _Entity_comp_index.Entry_ID
      _Entity_comp_index.Entity_ID

       1 . HIS . rr_1pba 1 
       2 . HIS . rr_1pba 1 
       3 . SER . rr_1pba 1 
       4 . GLY . rr_1pba 1 
       5 . GLU . rr_1pba 1 
       6 . HIS . rr_1pba 1 
       7 . PHE . rr_1pba 1 
       8 . GLU . rr_1pba 1 
       9 . GLY . rr_1pba 1 
      10 . GLU . rr_1pba 1 
      11 . LYS . rr_1pba 1 
      12 . VAL . rr_1pba 1 
      13 . PHE . rr_1pba 1 
      14 . ARG . rr_1pba 1 
      15 . VAL . rr_1pba 1 
      16 . ASN . rr_1pba 1 
      17 . VAL . rr_1pba 1 
      18 . GLU . rr_1pba 1 
      19 . ASP . rr_1pba 1 
      20 . GLU . rr_1pba 1 
      21 . ASN . rr_1pba 1 
      22 . ASP . rr_1pba 1 
      23 . ILE . rr_1pba 1 
      24 . SER . rr_1pba 1 
      25 . GLU . rr_1pba 1 
      26 . LEU . rr_1pba 1 
      27 . HIS . rr_1pba 1 
      28 . GLU . rr_1pba 1 
      29 . LEU . rr_1pba 1 
      30 . ALA . rr_1pba 1 
      31 . SER . rr_1pba 1 
      32 . THR . rr_1pba 1 
      33 . ARG . rr_1pba 1 
      34 . GLN . rr_1pba 1 
      35 . ILE . rr_1pba 1 
      36 . ASP . rr_1pba 1 
      37 . PHE . rr_1pba 1 
      38 . TRP . rr_1pba 1 
      39 . LYS . rr_1pba 1 
      40 . PRO . rr_1pba 1 
      41 . ASP . rr_1pba 1 
      42 . SER . rr_1pba 1 
      43 . VAL . rr_1pba 1 
      44 . THR . rr_1pba 1 
      45 . GLN . rr_1pba 1 
      46 . ILE . rr_1pba 1 
      47 . LYS . rr_1pba 1 
      48 . PRO . rr_1pba 1 
      49 . HIS . rr_1pba 1 
      50 . SER . rr_1pba 1 
      51 . THR . rr_1pba 1 
      52 . VAL . rr_1pba 1 
      53 . ASP . rr_1pba 1 
      54 . PHE . rr_1pba 1 
      55 . ARG . rr_1pba 1 
      56 . VAL . rr_1pba 1 
      57 . LYS . rr_1pba 1 
      58 . ALA . rr_1pba 1 
      59 . GLU . rr_1pba 1 
      60 . ASP . rr_1pba 1 
      61 . ILE . rr_1pba 1 
      62 . LEU . rr_1pba 1 
      63 . ALA . rr_1pba 1 
      64 . VAL . rr_1pba 1 
      65 . GLU . rr_1pba 1 
      66 . ASP . rr_1pba 1 
      67 . PHE . rr_1pba 1 
      68 . LEU . rr_1pba 1 
      69 . GLU . rr_1pba 1 
      70 . GLN . rr_1pba 1 
      71 . ASN . rr_1pba 1 
      72 . GLU . rr_1pba 1 
      73 . LEU . rr_1pba 1 
      74 . GLN . rr_1pba 1 
      75 . TYR . rr_1pba 1 
      76 . GLU . rr_1pba 1 
      77 . VAL . rr_1pba 1 
      78 . LEU . rr_1pba 1 
      79 . ILE . rr_1pba 1 
      80 . ASN . rr_1pba 1 
      81 . ASN . rr_1pba 1 

   stop_

   loop_
      _Entity_poly_seq.Hetero
      _Entity_poly_seq.Mon_ID
      _Entity_poly_seq.Num
      _Entity_poly_seq.Comp_index_ID
      _Entity_poly_seq.Entry_ID
      _Entity_poly_seq.Entity_ID

      . HIS  1  1 rr_1pba 1 
      . HIS  2  2 rr_1pba 1 
      . SER  3  3 rr_1pba 1 
      . GLY  4  4 rr_1pba 1 
      . GLU  5  5 rr_1pba 1 
      . HIS  6  6 rr_1pba 1 
      . PHE  7  7 rr_1pba 1 
      . GLU  8  8 rr_1pba 1 
      . GLY  9  9 rr_1pba 1 
      . GLU 10 10 rr_1pba 1 
      . LYS 11 11 rr_1pba 1 
      . VAL 12 12 rr_1pba 1 
      . PHE 13 13 rr_1pba 1 
      . ARG 14 14 rr_1pba 1 
      . VAL 15 15 rr_1pba 1 
      . ASN 16 16 rr_1pba 1 
      . VAL 17 17 rr_1pba 1 
      . GLU 18 18 rr_1pba 1 
      . ASP 19 19 rr_1pba 1 
      . GLU 20 20 rr_1pba 1 
      . ASN 21 21 rr_1pba 1 
      . ASP 22 22 rr_1pba 1 
      . ILE 23 23 rr_1pba 1 
      . SER 24 24 rr_1pba 1 
      . GLU 25 25 rr_1pba 1 
      . LEU 26 26 rr_1pba 1 
      . HIS 27 27 rr_1pba 1 
      . GLU 28 28 rr_1pba 1 
      . LEU 29 29 rr_1pba 1 
      . ALA 30 30 rr_1pba 1 
      . SER 31 31 rr_1pba 1 
      . THR 32 32 rr_1pba 1 
      . ARG 33 33 rr_1pba 1 
      . GLN 34 34 rr_1pba 1 
      . ILE 35 35 rr_1pba 1 
      . ASP 36 36 rr_1pba 1 
      . PHE 37 37 rr_1pba 1 
      . TRP 38 38 rr_1pba 1 
      . LYS 39 39 rr_1pba 1 
      . PRO 40 40 rr_1pba 1 
      . ASP 41 41 rr_1pba 1 
      . SER 42 42 rr_1pba 1 
      . VAL 43 43 rr_1pba 1 
      . THR 44 44 rr_1pba 1 
      . GLN 45 45 rr_1pba 1 
      . ILE 46 46 rr_1pba 1 
      . LYS 47 47 rr_1pba 1 
      . PRO 48 48 rr_1pba 1 
      . HIS 49 49 rr_1pba 1 
      . SER 50 50 rr_1pba 1 
      . THR 51 51 rr_1pba 1 
      . VAL 52 52 rr_1pba 1 
      . ASP 53 53 rr_1pba 1 
      . PHE 54 54 rr_1pba 1 
      . ARG 55 55 rr_1pba 1 
      . VAL 56 56 rr_1pba 1 
      . LYS 57 57 rr_1pba 1 
      . ALA 58 58 rr_1pba 1 
      . GLU 59 59 rr_1pba 1 
      . ASP 60 60 rr_1pba 1 
      . ILE 61 61 rr_1pba 1 
      . LEU 62 62 rr_1pba 1 
      . ALA 63 63 rr_1pba 1 
      . VAL 64 64 rr_1pba 1 
      . GLU 65 65 rr_1pba 1 
      . ASP 66 66 rr_1pba 1 
      . PHE 67 67 rr_1pba 1 
      . LEU 68 68 rr_1pba 1 
      . GLU 69 69 rr_1pba 1 
      . GLN 70 70 rr_1pba 1 
      . ASN 71 71 rr_1pba 1 
      . GLU 72 72 rr_1pba 1 
      . LEU 73 73 rr_1pba 1 
      . GLN 74 74 rr_1pba 1 
      . TYR 75 75 rr_1pba 1 
      . GLU 76 76 rr_1pba 1 
      . VAL 77 77 rr_1pba 1 
      . LEU 78 78 rr_1pba 1 
      . ILE 79 79 rr_1pba 1 
      . ASN 80 80 rr_1pba 1 
      . ASN 81 81 rr_1pba 1 

   stop_

save_


save_conformer_statistics
   _Conformer_stat_list.Sf_category                     conformer_statistics
   _Conformer_stat_list.Sf_framecode                    conformer_statistics
   _Conformer_stat_list.Entry_ID                        rr_1pba
   _Conformer_stat_list.ID                              1
   _Conformer_stat_list.Conf_family_coord_set_ID        1
   _Conformer_stat_list.Conf_family_coord_set_label    $Original_constraints_and_structures
   _Conformer_stat_list.Conformer_submitted_total_num   20

save_


save_global_Org_file_characteristics
   _Constraint_stat_list.Sf_framecode   global_Org_file_characteristics
   _Constraint_stat_list.Sf_category    constraint_statistics
   _Constraint_stat_list.Entry_ID       rr_1pba
   _Constraint_stat_list.ID             1

   loop_
      _Constraint_file.ID
      _Constraint_file.Constraint_filename
      _Constraint_file.Software_ID
      _Constraint_file.Software_label
      _Constraint_file.Software_name
      _Constraint_file.Block_ID
      _Constraint_file.Constraint_type
      _Constraint_file.Constraint_subtype
      _Constraint_file.Constraint_subsubtype
      _Constraint_file.Constraint_number
      _Constraint_file.Entry_ID
      _Constraint_file.Constraint_stat_list_ID

      1 1pba.mr . . "MR format" 1  comment               "Not applicable" "Not applicable" 0 rr_1pba 1 
      1 1pba.mr . . "MR format" 2 "dihedral angle"       "Not applicable" "Not applicable" 0 rr_1pba 1 
      1 1pba.mr . .  n/a        3  comment               "Not applicable" "Not applicable" 0 rr_1pba 1 
      1 1pba.mr . . "MR format" 4 "nomenclature mapping" "Not applicable" "Not applicable" 0 rr_1pba 1 

   stop_

save_


save_MR_file_comment_1
   _Org_constr_file_comment.Sf_framecode         MR_file_comment_1
   _Org_constr_file_comment.Sf_category          org_constr_file_comment
   _Org_constr_file_comment.Entry_ID             rr_1pba
   _Org_constr_file_comment.ID                   1
   _Org_constr_file_comment.Constraint_file_ID   1
   _Org_constr_file_comment.Block_ID             1
   _Org_constr_file_comment.Details             "Generated by Wattos"
   _Org_constr_file_comment.Comment             
;
*HEADER HYDROLASE(C-TERMINAL PEPTIDASE) 18-NOV-91 1PBA *COMPND PROCARBOXYPEPTIDASE B (E.C.3.4.17.2) (ACTIVATION DOMAIN) *COMPND 2 (NMR, 19 STRUCTURES) *SOURCE PORCINE (SUS SCROFA) PANCREAS *AUTHOR J.VENDRELL,G.WIDER,M.BILLETER,F.X.AVILES,K.WUTHRICH *REVDAT 1 31-OCT-93 1PBA 0 HEADER NMR DATA FOR 1ADB 14-OCT-91 ADB. ADB. 3
COMPND ACTIVATION DOMAIN OF PROCARBOXYPEPTIDASE B 1ADB 4
SOURCE PORCINE 1ADB 5
AUTHOR J.VENDRELL,G.WIDER,M.BILLETER,F.X.AVILES,K.WUTHRICH 1ADB 6
COORDS 1ADB ADB. 6
REMARK 1 1ADB 8
REMARK 1 THIS FILE CONTAINS DATA THAT WAS USED IN THE DETERMINATION 1ADB 9
REMARK 1 OF THE THREE-DIMENSIONAL STRUCTURE OF THE ACTIVATION DOMAIN 1ADB 10
REMARK 1 OF PROCARBOXYPEPTIDASE B BY NUCLEAR MAGNETIC RESONANCE IN 1ADB 11
REMARK 1 SOLUTION. THE DIFFERENT KINDS OF DATA TOGETHER WITH THE 1ADB 12
REMARK 1 CORRESPONDING RECORD IDENTIFIERS ARE GIVEN IN THE FOLLOWING 1ADB 13
REMARK 1 TABLE. SEE REMARK 2 FOR THE DETAILS. 1ADB 14
REMARK 1 1ADB 15
REMARK 1 RECORD CONTENT UNIT 1ADB 16
REMARK 1 ------ ------------------------------------------- --------- 1ADB 17
REMARK 1 SHIFTS CHEMICAL SHIFTS OF THE ASSIGNED PROTONS PPM 1ADB 18
REMARK 1 JCOUPL VICINAL 1H-1H SCALAR COUPLING CONSTANTS HERTZ 1ADB 19
REMARK 1 NOEUPP UPPER LIMITS FOR INTERATOMIC DISTANCES ANGSTROMS 1ADB 20
REMARK 1 DETERMINED FROM NUCLEAR OVERHAUSER EFFECTS 1ADB 21
REMARK 1 HBUPP UPPER LIMITS FOR INTERATOMIC DISTANCES ANGSTROMS 1ADB 22
REMARK 1 FOR HYDROGEN BONDS 1ADB 23
REMARK 1 SSUPP UPPER LIMITS FOR INTERATOMIC DISTANCES ANGSTROMS 1ADB 24
REMARK 1 FOR DISULPHIDE BRIDGES 1ADB 25
REMARK 1 NOELOW LOWER LIMITS FOR INTERATOMIC DISTANCES ANGSTROMS 1ADB 26
REMARK 1 DETERMINED FROM NUCLEAR OVERHAUSER EFFECTS 1ADB 27
REMARK 1 (NOT USED HERE) 1ADB 28
REMARK 1 HBLOW LOWER LIMITS FOR INTERATOMIC DISTANCES ANGSTROMS 1ADB 29
REMARK 1 FOR HYDROGEN BONDS 1ADB 30
REMARK 1 SSLOW LOWER LIMITS FOR INTERATOMIC DISTANCES ANGSTROMS 1ADB 31
REMARK 1 FOR DISULPHIDE BRIDGES 1ADB 32
REMARK 1 ANGLE TORSION ANGLE CONSTRAINTS IN THE FORM OF DEGREES 1ADB 33
REMARK 1 AN ALLOWED INTERVAL 1ADB 34
REMARK 1 1ADB 35
REMARK 1 ALL EXPERIMENTAL INPUT DATA (EXCEPT THE AMINO ACID SEQUENCE) 1ADB 36
REMARK 1 FOR THE DISTANCE GEOMETRY CALCULATIONS WITH THE PROGRAM 1ADB 37
REMARK 1 DISMAN AND REFINEMENT WITH AMBER IS GIVEN IN THE RECORDS 1ADB 38
REMARK 1 NOEUPP, HBUPP, SSUPP, HBLOW,SSLOW AND ANGLE. 1ADB 39
REMARK 2 1ADB 40
REMARK 2 1ADB 41
REMARK 2 THE NEXT TABLE CONTAINS A DETAILED DESCRIPTION OF THE 1ADB 42
REMARK 2 CONTENTS AND FORMATS OF THE VARIOUS DATA RECORDS AND THE 1ADB 43
REMARK 2 MASTER RECORD. 1ADB 44
REMARK 2 1ADB 45
REMARK 2 RECORD CONTENTS (FORTRAN FORMAT) 1ADB 46
REMARK 2 ------ ----------------------------------------------------- 1ADB 47
REMARK 2 SHIFTS RESIDUE NAME, RESIDUE NUMBER, ATOM NAME, CHEMICAL 1ADB 48
REMARK 2 SHIFT(S), ATOM NAME, CHEMICAL SHIFT(S), ATOM NAME, 1ADB 49
REMARK 2 CHEMICAL SHIFT(S) 1ADB 50
REMARK 2 ('SHIFTS',2X,A4,I4,2X,3(A4,2F6.2,2X)) 1ADB 51
REMARK 2 JCOUPL RESIDUE NAME, RESIDUE NUMBER, FIRST AND SECOND ATOM 1ADB 52
REMARK 2 NAME, J-COUPLING CONSTANT, FIRST AND SECOND ATOM 1ADB 53
REMARK 2 NAME, J-COUPLING CONSTANT, FIRST AND SECOND ATOM 1ADB 54
REMARK 2 NAME, J-COUPLING CONSTANT 1ADB 55
REMARK 2 ('JCOUPL',2X,A4,I4,2X,3(A4,1X,A4,F6.2,3X)) 1ADB 56
REMARK 2 NOEUPP FIRST RESIDUE NAME, FIRST RESIDUE NUMBER, FIRST ATOM 1ADB 57
REMARK 2 NAME, SECOND RESIDUE NAME, SECOND RESIDUE NUMBER, 1ADB 58
REMARK 2 SECOND ATOM NAME, UPPER DISTANCE LIMIT, FIRST ATOM 1ADB 59
REMARK 2 NAME, SECOND RESIDUE NAME, SECOND RESIDUE NUMBER, 1ADB 60
REMARK 2 SECOND ATOM NAME, UPPER DISTANCE LIMIT 1ADB 61
REMARK 2 ('NOEUPP',2X,A4,I4,1X,2(A4,1X,A4,I4,1X,A4,F6.2,5X)) 1ADB 62
REMARK 2 HBUPP SIMILAR TO NOEUPP 1ADB 63
REMARK 2 SSUPP SIMILAR TO NOEUPP 1ADB 64
REMARK 2 NOELOW SIMILAR TO NOEUPP, BUT WITH LOWER DISTANCE LIMITS 1ADB 65
REMARK 2 HBLOW SIMILAR TO NOELOW 1ADB 66
REMARK 2 SSLOW SIMILAR TO NOELOW 1ADB 67
REMARK 2 ANGLE RESIDUE NAME, RESIDUE NUMBER, ANGLE NAME, LOWER AND 1ADB 68
REMARK 2 UPPER BOUND, ANGLE NAME, LOWER AND UPPER BOUND 1ADB 69
REMARK 2 ('ANGLE',3X,A4,I4,1X,2(A5,2F8.2,8X)) 1ADB 70
REMARK 2 MASTER NUMBER OF REMARK RECORDS, NUMBER OF FTNOTE RECORDS, 1ADB 71
REMARK 2 NUMBER OF SHIFTS RECORDS, NUMBER OF JCOUPL RECORDS, 1ADB 72
REMARK 2 NUMBER OF NOEUPP, HBUPP AND SSUPP RECORDS, NUMBER OF 1ADB 73
REMARK 2 NOELOW, HBLOW AND SSLOW RECORDS, NUMBER OF ANGLE 1ADB 74
REMARK 2 RECORDS 1ADB 75
REMARK 2 ('MASTER',4X,7I5) 1ADB 76
REMARK 3 1ADB 77
REMARK 3 ATOM NAMES HAVE BEEN ASSIGNED FOLLOWING THE RECOMMENDATIONS 1ADB 78
REMARK 3 OF THE IUPAC-IUB COMMISSION AS PUBLISHED IN BIOCHEMISTRY 1ADB 79
REMARK 3 (1970) VOL. 9, 3471-3479, EXCEPT THAT BACKBONE AMIDE 1ADB 80
REMARK 3 HYDROGENS ARE DENOTED BY HN INSTEAD OF H. THE HYDROGEN ATOM 1ADB 81
REMARK 3 NUMBERS OF THOSE HYDROGEN ATOMS WHICH ARE CONNECTED TO THE 1ADB 82
REMARK 3 SAME NON-HYDROGEN ATOM ARE WRITTEN AS THE FIRST CHARACTER 1ADB 83
REMARK 3 RATHER THAN THE LAST CHARACTER OF THE ATOM NAMES. 1ADB 84
REMARK 3 THEY ARE IDENTICAL WITH THE ATOM NAMES USED IN THE CO- 1ADB 85
REMARK 3 ORDINATE FILE 1ADB. 1ADB 86
REMARK 4 1ADB 87
REMARK 4 PSEUDO-ATOMS DESIGNATED AS Q ARE DIMENSIONLESS REFERENCE 1ADB 88
REMARK 4 POINTS REPRESENTING A GROUP OF HYDROGEN ATOMS 1ADB 89
REMARK 4 (K.WUTHRICH, M.BILLETER AND W.BRAUN, J. MOL. BIOL. (1983) 1ADB 90
REMARK 4 VOL. 169, 949-961). THEY ARE USED TO DESCRIBE ALL METHYL 1ADB 91
REMARK 4 GROUPS, AND THOSE GROUPS OF PROCHIRAL HYDROGEN ATOMS FOR 1ADB 92
REMARK 4 WHICH NO STEREOSPECIFIC ASSIGNMENTS HAD BEEN OBTAINED. 1ADB 93
REMARK 4 FOR ALL METHYLENE GROUPS, EVEN IN CASE OF IDENTICAL SHIFTS, 1ADB 94
REMARK 4 TWO CHEMICAL SHIFTS ARE LISTED FOR THE TWO PROTONS. 1ADB 95
REMARK 4 TWO CHEMICAL SHIFTS ARE ALSO ALWAYS GIVEN FOR THE TWO 1ADB 96
REMARK 4 METHYLS IN THE ISOPROPYL GROUPS. 1ADB 97
REMARK 5 1ADB 98
REMARK 5 DETAILS OF THE NOMENCLATURE FOR THE PSEUDO-ATOMS ARE 1ADB 99
REMARK 5 AS FOLLOWS: QA REPRESENTS THE TWO METHYLENE HYDROGEN 1ADB 100
REMARK 5 ATOMS OF GLY. QB, QG, ... REPRESENT BETA, GAMMA, ... 1ADB 101
REMARK 5 METHYLENE OR METHYL GROUPS IN THE SIDE CHAINS. IN CASE OF 1ADB 102
REMARK 5 BRANCHES IN THE SIDE CHAINS THE NUMBERS OF THE PSEUDO-ATOMS 1ADB 103
REMARK 5 ARE THE SAME AS THE NUMBERS OF THE CARBONS TO WHICH THE 1ADB 104
REMARK 5 HYDROGEN ATOMS ARE ATTACHED. 1ADB 105
REMARK 5 QQG AND QQD DENOTE THE PSEUDO-ATOMS FOR THE 6 HYDROGEN 1ADB 106
REMARK 5 ATOMS OF THE ISOPROPYL METHYL GROUPS OF VAL AND LEU, RESPEC- 1ADB 107
REMARK 5 TIVELY. QR IS THE PSEUDO-ATOM FOR THE DELTA AND EPSILON 1ADB 108
REMARK 5 HYDROGENS OF THE AROMATIC RINGS OF TYR AND PHE. IN THE CASE 1ADB 109
REMARK 5 THE DELTA AND EPSILON PROTONS OF THE AROMATIC RINGS 1ADB 110
REMARK 5 ARE DEGENERATE, THE CHEMICAL SHIFTS ARE LISTED UNDER CG 1ADB 111
REMARK 5 AND CZ, RESPECTIVELY. 1ADB 112
REMARK 5 1ADB 113
;

save_


save_MR_file_comment_3
   _Org_constr_file_comment.Sf_framecode         MR_file_comment_3
   _Org_constr_file_comment.Sf_category          org_constr_file_comment
   _Org_constr_file_comment.Entry_ID             rr_1pba
   _Org_constr_file_comment.ID                   2
   _Org_constr_file_comment.Constraint_file_ID   1
   _Org_constr_file_comment.Block_ID             3
   _Org_constr_file_comment.Details             "Generated by Wattos"
   _Org_constr_file_comment.Comment             
;
MASTER 0 0 0 0 401 0 0 ADB. 408
END ADB. 409 
;

save_

