Header list of 1ixu.pdb file
Complete list - 25 201 Bytes
HEADER PROTEIN BINDING 04-JUL-02 1IXU TITLE SOLUTION STRUCTURE OF MARINOSTATIN, A PROTEASE INHIBITOR, CONTAINING TITLE 2 TWO ESTER LINKAGES COMPND MOL_ID: 1; COMPND 2 MOLECULE: MARINOSTATIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: MARINOSTATIN ACTIVE FRAGMENT; COMPND 5 SYNONYM: MSTI SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ALTEROMONAS SP.; SOURCE 3 ORGANISM_TAXID: 29456; SOURCE 4 STRAIN: B-10-31; SOURCE 5 OTHER_DETAILS: MARINE MICROORGANISM KEYWDS PROTEASE INHIBITOR, ESTER LINKAGE, PROTEIN BINDING EXPDTA SOLUTION NMR AUTHOR K.KANAORI,K.KAMEI,T.KOYAMA,T.YASUI,R.TAKANO,C.IMADA,K.TAJIMA,S.HARA REVDAT 4 13-JUL-11 1IXU 1 VERSN REVDAT 3 24-FEB-09 1IXU 1 VERSN REVDAT 2 08-MAR-05 1IXU 1 JRNL REVDAT 1 17-FEB-04 1IXU 0 JRNL AUTH K.KANAORI,K.KAMEI,M.TANIGUCHI,T.KOYAMA,T.YASUI,R.TAKANO, JRNL AUTH 2 C.IMADA,K.TAJIMA,S.HARA JRNL TITL SOLUTION STRUCTURE OF MARINOSTATIN, A NATURAL ESTER-LINKED JRNL TITL 2 PROTEIN PROTEASE INHIBITOR JRNL REF BIOCHEMISTRY V. 44 2462 2005 JRNL REFN ISSN 0006-2960 JRNL PMID 15709758 JRNL DOI 10.1021/BI048034X REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRCHITECT 2.0 REMARK 3 AUTHORS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THERE ARE TWO ESTER LINKAGES. ONE IS LOCATED BETWEEN REMARK 3 THE SIDE-CHAINS OF THR 3-ASP 9, THE OTHER BETWEEN REMARK 3 SER 8-ASP 11. REMARK 4 REMARK 4 1IXU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-JUL-02. REMARK 100 THE RCSB ID CODE IS RCSB005385. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 278 REMARK 210 PH : 3.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1MM MARINOSTATIN REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : ARX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : UXNMR 9410001.2, FELIX 2.3 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 VIOLATION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D REMARK 210 HOMONUCLEAR TECHNIQUES. 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 GLU A 12 CD GLU A 12 OE2 0.113 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 SER A 10 26.02 -148.02 REMARK 500 REMARK 500 REMARK: NULL DBREF 1IXU A 1 12 UNP P29399 MARI_ALTSP 45 56 SEQRES 1 A 12 PHE ALA THR MET ARG TYR PRO SER ASP SER ASP GLU LINK OG1 THR A 3 CG ASP A 9 1555 1555 1.37 LINK OG SER A 8 CG ASP A 11 1555 1555 1.37 CISPEP 1 TYR A 6 PRO A 7 0 -11.19 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
Complete list - 25 201 Bytes