Header list of 1jnt.pdb file
Complete list - 23 20 Bytes
HEADER ISOMERASE 25-JUL-01 1JNT
TITLE NMR STRUCTURE OF THE E. COLI PEPTIDYL-PROLYL CIS/TRANS-ISOMERASE
TITLE 2 PARVULIN 10
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE C;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PARVULIN, PPIASE C, ROTAMASE C;
COMPND 5 EC: 5.2.1.8;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: PARA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: M15[PREP4];
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PSEP612
KEYWDS ALPHA-BETA SANDWICH, CIS PEPTIDE BOND, ISOMERASE
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR A.KUEHLEWEIN,G.VOLL,B.SCHELBERT,H.KESSLER,G.FISCHER,J.U.RAHFELD,
AUTHOR 2 G.GEMMECKER
REVDAT 4 23-FEB-22 1JNT 1 REMARK
REVDAT 3 24-FEB-09 1JNT 1 VERSN
REVDAT 2 05-APR-05 1JNT 1 JRNL
REVDAT 1 17-JUN-03 1JNT 0
JRNL AUTH A.KUEHLEWEIN,G.VOLL,B.H.ALVAREZ,H.KESSLER,G.FISCHER,
JRNL AUTH 2 J.U.RAHFELD,G.GEMMECKER
JRNL TITL SOLUTION STRUCTURE OF ESCHERICHIA COLI PAR10: THE PROTOTYPIC
JRNL TITL 2 MEMBER OF THE PARVULIN FAMILY OF PEPTIDYL-PROLYL CIS/TRANS
JRNL TITL 3 ISOMERASES.
JRNL REF PROTEIN SCI. V. 13 2378 2004
JRNL REFN ISSN 0961-8368
JRNL PMID 15322281
JRNL DOI 10.1110/PS.04756704
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, X-PLOR 3.851
REMARK 3 AUTHORS : BRUKER, KARLSRUHE (XWINNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 1097 NOE
REMARK 3 -DERIVED DISTANCE CONSTRAINTS, 68 DIHEDRAL RESTRAINTS FOR CSI-
REMARK 3 DERIVED HELICAL REGIONS, 42 3J(HN,HA) RESTRAINTS, 30 DISTANCE
REMARK 3 CONSTRAINTS FOR HYDROGEN BONDS BASED ON CSI AND MEXICO DATA.
REMARK 4
REMARK 4 1JNT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-AUG-01.
REMARK 100 THE DEPOSITION ID IS D_1000013983.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 297.6
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 100 MM KCL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.8 MM [U-15N] PARVULIN 10, 10
REMARK 210 MM PHOSPHATE BUFFER, PH 6.0, 100
REMARK 210 MM KCL, 1 MM EDTA, 1 MM DTE; 0.8
REMARK 210 MM [U-13C, 15N] PARVULIN 10, 10
REMARK 210 MM PHOSPHATE BUFFER, PH 6.0, 100
REMARK 210 MM KCL, 1 MM EDTA, 1 MM DTE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNHA; 3D_15N-SEPARATED_NOESY;
REMARK 210 3D_13C-SEPARATED_NOESY; 3D_13C/
REMARK 210 13C-SEPARATED_NOESY; 3D_13C/15N-
REMARK 210 SEPARATED_NOESY; 2D_MEXICO
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.6, TRIAD 6.6, ARIA
REMARK 210 0.53, CNS 0.5, X-PLOR 3.851
REMARK 210 METHOD USED : THE AVERAGED STRUCTURE OF THE
REMARK 210 ENSEMBLE (1JNS) WAS REGULARIZED
REMARK 210 UNDER EXPERIMENTAL CONSTRAINTS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O PRO A 59 H ASP A 62 1.53
REMARK 500 O VAL A 64 H SER A 67 1.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA A 28 96.61 89.77
REMARK 500 ASP A 29 83.04 -178.05
REMARK 500 ILE A 39 29.60 37.60
REMARK 500 ASP A 48 78.01 -170.38
REMARK 500 GLN A 56 -61.96 -132.92
REMARK 500 MET A 57 -66.03 -106.16
REMARK 500 ALA A 60 -29.64 -35.53
REMARK 500 SER A 67 -70.54 -94.76
REMARK 500 VAL A 70 170.56 -57.13
REMARK 500 GLU A 72 93.48 -163.47
REMARK 500 TYR A 90 -86.73 32.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JNS RELATED DB: PDB
REMARK 900 SAME PROTEIN, ENSEMBLE OF 18 STRUCTURES
DBREF 1JNT A 1 92 UNP P0A9L5 PPIC_ECOLI 1 92
SEQRES 1 A 92 ALA LYS THR ALA ALA ALA LEU HIS ILE LEU VAL LYS GLU
SEQRES 2 A 92 GLU LYS LEU ALA LEU ASP LEU LEU GLU GLN ILE LYS ASN
SEQRES 3 A 92 GLY ALA ASP PHE GLY LYS LEU ALA LYS LYS HIS SER ILE
SEQRES 4 A 92 CYS PRO SER GLY LYS ARG GLY GLY ASP LEU GLY GLU PHE
SEQRES 5 A 92 ARG GLN GLY GLN MET VAL PRO ALA PHE ASP LYS VAL VAL
SEQRES 6 A 92 PHE SER CYS PRO VAL LEU GLU PRO THR GLY PRO LEU HIS
SEQRES 7 A 92 THR GLN PHE GLY TYR HIS ILE ILE LYS VAL LEU TYR ARG
SEQRES 8 A 92 ASN
HELIX 1 1 GLU A 14 GLY A 27 1 14
HELIX 2 2 PHE A 30 LYS A 36 1 7
HELIX 3 3 GLY A 43 GLY A 47 5 5
HELIX 4 4 ALA A 60 SER A 67 1 8
SHEET 1 A 4 GLY A 50 ARG A 53 0
SHEET 2 A 4 THR A 3 VAL A 11 -1 N ALA A 4 O PHE A 52
SHEET 3 A 4 GLY A 82 LEU A 89 -1 N TYR A 83 O VAL A 11
SHEET 4 A 4 THR A 74 THR A 79 -1 O THR A 74 N ILE A 86
CISPEP 1 GLY A 75 PRO A 76 0 -1.45
CRYST1 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
Complete list - 23 20 Bytes