Header list of 1clh.pdb file
Complete list - b 16 2 Bytes
HEADER ISOMERASE(PEPTIDYL-PROLYL CIS-TRANS) 20-DEC-93 1CLH
TITLE THREE-DIMENSIONAL SOLUTION STRUCTURE OF ESCHERICHIA COLI PERIPLASMIC
TITLE 2 CYCLOPHILIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYCLOPHILIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: CYCLOPHILIN;
SOURCE 5 EXPRESSION_SYSTEM_GENE: CYCLOPHILIN
KEYWDS ISOMERASE(PEPTIDYL-PROLYL CIS-TRANS)
EXPDTA SOLUTION NMR
NUMMDL 12
AUTHOR R.T.CLUBB,G.WAGNER
REVDAT 3 16-FEB-22 1CLH 1 REMARK
REVDAT 2 24-FEB-09 1CLH 1 VERSN
REVDAT 1 31-MAY-94 1CLH 0
JRNL AUTH R.T.CLUBB,S.B.FERGUSON,C.T.WALSH,G.WAGNER
JRNL TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF ESCHERICHIA COLI
JRNL TITL 2 PERIPLASMIC CYCLOPHILIN
JRNL REF BIOCHEMISTRY V. 33 2761 1994
JRNL REFN ISSN 0006-2960
JRNL PMID 8130188
JRNL DOI 10.1021/BI00176A004
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CLH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000172374.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 12
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
DBREF 1CLH A 1 166 UNP P20752 PPIA_ECOLI 25 190
SEQRES 1 A 166 ALA LYS GLY ASP PRO HIS VAL LEU LEU THR THR SER ALA
SEQRES 2 A 166 GLY ASN ILE GLU LEU GLU LEU ASP LYS GLN LYS ALA PRO
SEQRES 3 A 166 VAL SER VAL GLN ASN PHE VAL ASP TYR VAL ASN SER GLY
SEQRES 4 A 166 PHE TYR ASN ASN THR THR PHE HIS ARG VAL ILE PRO GLY
SEQRES 5 A 166 PHE MET ILE GLN GLY GLY GLY PHE THR GLU GLN MET GLN
SEQRES 6 A 166 GLN LYS LYS PRO ASN PRO PRO ILE LYS ASN GLU ALA ASP
SEQRES 7 A 166 ASN GLY LEU ARG ASN THR ARG GLY THR ILE ALA MET ALA
SEQRES 8 A 166 ARG THR ALA ASP LYS ASP SER ALA THR SER GLN PHE PHE
SEQRES 9 A 166 ILE ASN VAL ALA ASP ASN ALA PHE LEU ASP HIS GLY GLN
SEQRES 10 A 166 ARG ASP PHE GLY TYR ALA VAL PHE GLY LYS VAL VAL LYS
SEQRES 11 A 166 GLY MET ASP VAL ALA ASP LYS ILE SER GLN VAL PRO THR
SEQRES 12 A 166 HIS ASP VAL GLY PRO TYR GLN ASN VAL PRO SER LYS PRO
SEQRES 13 A 166 VAL VAL ILE LEU SER ALA LYS VAL LEU PRO
HELIX 1 1 ALA A 25 ASN A 37 1 13
HELIX 2 2 PHE A 40 THR A 44 5 5
HELIX 3 3 GLY A 131 SER A 139 1 9
SHEET 1 A 4 GLY A 126 VAL A 128 0
SHEET 2 A 4 ASN A 15 LEU A 20 -1 N GLU A 19 O LYS A 127
SHEET 3 A 4 HIS A 6 THR A 11 -1 O VAL A 7 N LEU A 18
SHEET 4 A 4 ILE A 159 LEU A 165 -1 N LEU A 160 O THR A 10
SHEET 1 B 2 VAL A 49 ILE A 50 0
SHEET 2 B 2 MET A 54 ILE A 55 -1 N MET A 54 O ILE A 50
SHEET 1 C 2 ILE A 88 MET A 90 0
SHEET 2 C 2 PHE A 103 ILE A 105 -1 N PHE A 104 O ALA A 89
CISPEP 1 GLN A 56 GLY A 57 1 3.22
CISPEP 2 GLN A 56 GLY A 57 4 4.37
CISPEP 3 SER A 98 ALA A 99 4 -2.41
CISPEP 4 GLN A 56 GLY A 57 6 0.36
CISPEP 5 ASN A 79 GLY A 80 6 -1.15
CISPEP 6 PRO A 71 PRO A 72 7 -2.49
CISPEP 7 ARG A 85 GLY A 86 7 3.69
CISPEP 8 PRO A 71 PRO A 72 8 -2.45
CISPEP 9 LYS A 130 GLY A 131 8 0.92
CISPEP 10 LYS A 130 GLY A 131 9 -4.23
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - b 16 2 Bytes