Header list of 1sbu.pdb file
Complete list - 24 20 Bytes
HEADER TOXIN 11-FEB-04 1SBU TITLE NMR STRUCTURE OF A PEPTIDE CONTAINING A DIMETYLTHIAZOLIDINE : AN TITLE 2 ANALOG OF DELTA CONOTOXIN EVIA LOOP 2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: DELTA-CONOTOXIN EVIA; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 ORGANISM_SCIENTIFIC: CONUS ERMINEUS; SOURCE 4 ORGANISM_COMMON: ATLANTIC FISH-HUNTING CONE; SOURCE 5 ORGANISM_TAXID: 55423; SOURCE 6 OTHER_DETAILS: THE SOLID PHASE SYNTHESIS OF THE PEPTIDE WAS CARRIED SOURCE 7 OUT USING THE FMOC CHEMISTRY KEYWDS CIS LEU-(DMT)THIAZOLIDINE AMIDE BOND, DIMETHYL-THIAZOLIDINE, VI BETA KEYWDS 2 TURN, NMR SPECTROSCOPY, MOLECULAR DYNAMICS SIMULATIONS, TOXIN EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR M.FIGUET,S.CHIERICI,M.JOURDAN,P.DUMY REVDAT 5 24-JUN-20 1SBU 1 COMPND SOURCE REMARK DBREF REVDAT 5 2 1 LINK REVDAT 4 24-FEB-09 1SBU 1 VERSN REVDAT 3 07-SEP-04 1SBU 1 JRNL REVDAT 2 06-APR-04 1SBU 1 TITLE REVDAT 1 24-FEB-04 1SBU 0 JRNL AUTH S.CHIERICI,M.JOURDAN,M.FIGUET,P.DUMY JRNL TITL A CASE STUDY OF 2,2-DIMETHYLTHIAZOLIDINE AS LOCKED CIS JRNL TITL 2 PROLINE AMIDE BOND: SYNTHESIS, NMR AND MOLECULAR MODELING JRNL TITL 3 STUDIES OF A [SMALL DELTA]-CONOTOXIN EVIA PEPTIDE ANALOG. JRNL REF ORG.BIOMOL.CHEM. V. 2 2437 2004 JRNL REFN ISSN 1477-0520 JRNL PMID 15326523 JRNL DOI 10.1039/B408325C REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.6, IRMA 200 REMARK 3 AUTHORS : BOELENS R, KONING TMG, KAPTEIN R (IRMA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: IRMA WAS USED TO REFINE THE STRUCTURE REMARK 4 REMARK 4 1SBU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-FEB-04. REMARK 100 THE DEPOSITION ID IS D_1000021584. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 283 REMARK 210 PH : 3 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : PEPTIDE CONCENTRATION : 2MM REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE; UNITYPLUS REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : VNMR 2000 (6.1), FELIX 2000, REMARK 210 DISCOVER 2.98 REMARK 210 METHOD USED : THE PEPTIDE WAS SUBJECTED TO REMARK 210 SIMULATED ANNEALING RESTRAINTS REMARK 210 MOLECULAR DYNAMICS USING THE REMARK 210 CVFF FORCEFIELD REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES REMARK 210 WITH THE LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 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 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 1 GLY A 11 C GLY A 11 OXT 0.143 REMARK 500 2 GLY A 11 C GLY A 11 OXT 0.143 REMARK 500 3 GLY A 11 C GLY A 11 OXT 0.143 REMARK 500 4 GLY A 11 C GLY A 11 OXT 0.142 REMARK 500 5 GLY A 11 C GLY A 11 OXT 0.143 REMARK 500 6 GLY A 11 C GLY A 11 OXT 0.143 REMARK 500 7 GLY A 11 C GLY A 11 OXT 0.143 REMARK 500 8 GLY A 11 C GLY A 11 OXT 0.143 REMARK 500 9 GLY A 11 C GLY A 11 OXT 0.143 REMARK 500 10 GLY A 11 C GLY A 11 OXT 0.144 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 2 LEU A 8 CB - CG - CD1 ANGL. DEV. = 10.5 DEGREES REMARK 500 4 LEU A 8 CB - CG - CD1 ANGL. DEV. = 10.5 DEGREES 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 1 PHE A 2 88.93 -152.86 REMARK 500 2 PHE A 2 89.28 -157.57 REMARK 500 3 PHE A 2 87.89 -153.13 REMARK 500 4 PHE A 2 89.06 -156.74 REMARK 500 4 SER A 4 117.20 -161.98 REMARK 500 5 PHE A 2 86.71 -152.43 REMARK 500 6 PHE A 2 86.93 -152.13 REMARK 500 7 PHE A 2 89.03 -164.39 REMARK 500 7 SER A 4 137.59 -173.43 REMARK 500 7 LEU A 8 77.37 -105.38 REMARK 500 8 PHE A 2 86.88 -152.61 REMARK 500 9 PHE A 2 87.77 -153.74 REMARK 500 10 PHE A 2 87.46 -154.65 REMARK 500 10 SER A 4 121.82 -171.07 REMARK 500 REMARK 500 REMARK: NULL DBREF 1SBU A 1 11 PDB 1SBU 1SBU 1 11 SEQRES 1 A 11 GLY PHE ALA SER LEU 2MT ILE LEU LYS ASN GLY MODRES 1SBU 2MT A 6 PRO HET 2MT A 6 18 HETNAM 2MT (4R)-2,2-DIMETHYL-1,3-THIAZOLIDINE-4-CARBOXYLIC ACID HETSYN 2MT 2,2-DIMETHYLTHIAZOLIDINE-4-CARBOXYLIC ACID;(DMT) HETSYN 2 2MT THIAZOLIDINE FORMUL 1 2MT C6 H11 N O2 S LINK C LEU A 5 N 2MT A 6 1555 1555 1.39 LINK C 2MT A 6 N ILE A 7 1555 1555 1.37 CISPEP 1 LEU A 5 2MT A 6 1 6.43 CISPEP 2 LEU A 5 2MT A 6 2 5.38 CISPEP 3 LEU A 5 2MT A 6 3 7.93 CISPEP 4 LEU A 5 2MT A 6 4 5.96 CISPEP 5 LEU A 5 2MT A 6 5 6.20 CISPEP 6 LEU A 5 2MT A 6 6 7.69 CISPEP 7 LEU A 5 2MT A 6 7 7.51 CISPEP 8 LEU A 5 2MT A 6 8 8.68 CISPEP 9 LEU A 5 2MT A 6 9 6.17 CISPEP 10 LEU A 5 2MT A 6 10 8.09 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 - 24 20 Bytes