Header list of 2bey.pdb file
Complete list - 21 20 Bytes
HEADER INHIBITOR 01-DEC-04 2BEY TITLE SOLUTION STRUCTURE OF A NOVEL C2 SYMMETRICAL TITLE 2 BIFUNCTIONAL BICYCLIC INHIBITOR BASED ON SFTI-1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: BIKK; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: DUPLICATED AND FUSED REACTIVE SITE LOOP OF COMPND 5 SFTI-1; COMPND 6 OTHER_DETAILS: THE PEPTIDE IS BACKBONE CYCLIZED COMPND 7 (CYS1-ILE16) AND HAS AN INTRAMOLECULAR DISULFIDE BOND COMPND 8 (CYS1-CYS9) SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES SOURCE 3 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 4 ORGANISM_TAXID: 32630; KEYWDS INHIBITOR, BIKK, C2 SYMMETRICAL BIFUNCTIONAL BICYCLIC KEYWDS 2 TRYPSIN INHIBITOR, PEPTIDE, SYMMETRY, SFTI1 EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR A.M.JAULENT,A.B.E.BRAUER,S.J.MATTHEWS,R.J.LEATHERBARROW REVDAT 3 21-DEC-16 2BEY 1 SOURCE REMARK VERSN REVDAT 2 24-FEB-09 2BEY 1 VERSN REVDAT 1 17-OCT-05 2BEY 0 JRNL AUTH A.M.JAULENT,A.B.E.BRAUER,S.J.MATTHEWS, JRNL AUTH 2 R.J.LEATHERBARROW JRNL TITL SOLUTION STRUCTURE OF A NOVEL C2-SYMMETRICAL JRNL TITL 2 BIFUNCTIONAL BICYCLIC INHIBITOR BASED ON SFTI-1 JRNL REF J.BIOMOL.NMR V. 33 57 2005 JRNL REFN ISSN 0925-2738 JRNL PMID 16222558 JRNL DOI 10.1007/S10858-005-1210-9 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH A.M.JAULENT,R.J.LEATHERBARROW REMARK 1 TITL DESIGN, SYNTHESIS AND ANALYSIS OF NOVEL BICYCLIC REMARK 1 TITL 2 AND BIFUNCTIONAL PROTEASE INHIBITORS REMARK 1 REF PROTEIN ENG.DES.SEL. V. 17 681 2004 REMARK 1 REFN ISSN 1741-0126 REMARK 1 PMID 15486024 REMARK 1 DOI 10.1093/PROTEIN/GZH077 REMARK 1 REFERENCE 2 REMARK 1 AUTH S.LUCKETT,R.S.GARCIA,J.J.BARKER,A.V.KONAREV, REMARK 1 AUTH 2 P.R.SHEWRY,A.R.CLARKE,R.L.BRADY REMARK 1 TITL HIGH-RESOLUTION STRUCTURE OF A POTENT, CYCLIC REMARK 1 TITL 2 PROTEINASE INHIBITOR FROM SUNFLOWER SEEDS REMARK 1 REF J.MOL.BIOL. V. 290 525 1999 REMARK 1 REFN ISSN 0022-2836 REMARK 1 PMID 10390350 REMARK 1 DOI 10.1006/JMBI.1999.2891 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : TINKER/DISTGEOM REMARK 3 AUTHORS : J.W.PONDER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2BEY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-DEC-04. REMARK 100 THE PDBE ID CODE IS EBI-16227. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 305 REMARK 210 PH : 3.8 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : TOCSY, NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : AMX 600 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : TINKER/ISTGEOM REMARK 210 METHOD USED : DISTANCE GEOMETRY, REMARK 210 SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING 1H-NMR. REMARK 210 NO HYDROGEN BOND RESTRAINTS WERE USED IN THE REMARK 210 STRUCTURE CALCULATIONS. 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: 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 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 LYS A 3 29.65 -75.72 REMARK 500 1 LYS A 11 39.82 -82.75 REMARK 500 2 LYS A 3 30.31 -77.38 REMARK 500 2 LYS A 11 40.74 -75.00 REMARK 500 3 LYS A 3 26.77 -76.87 REMARK 500 3 LYS A 11 41.43 -80.96 REMARK 500 4 LYS A 3 29.44 -76.79 REMARK 500 4 LYS A 11 38.52 -78.83 REMARK 500 5 LYS A 3 28.24 -79.24 REMARK 500 5 LYS A 11 35.60 -78.49 REMARK 500 6 LYS A 3 27.96 -79.16 REMARK 500 6 LYS A 11 40.00 -79.36 REMARK 500 7 LYS A 3 30.83 -75.63 REMARK 500 7 LYS A 11 40.34 -79.81 REMARK 500 8 LYS A 3 29.94 -77.02 REMARK 500 8 LYS A 11 34.11 -84.59 REMARK 500 9 LYS A 3 28.60 -79.04 REMARK 500 9 LYS A 11 37.92 -85.63 REMARK 500 10 LYS A 3 27.31 -76.32 REMARK 500 10 LYS A 11 37.33 -82.54 REMARK 500 11 LYS A 3 28.46 -75.48 REMARK 500 11 LYS A 11 37.08 -80.47 REMARK 500 12 LYS A 3 33.70 -74.98 REMARK 500 12 LYS A 11 40.09 -79.76 REMARK 500 13 LYS A 3 31.50 -78.57 REMARK 500 13 LYS A 11 36.65 -82.77 REMARK 500 14 LYS A 3 32.42 -75.76 REMARK 500 14 LYS A 11 38.55 -81.29 REMARK 500 15 LYS A 3 29.23 -79.92 REMARK 500 15 LYS A 11 35.01 -81.94 REMARK 500 16 LYS A 3 32.05 -75.95 REMARK 500 16 LYS A 11 39.33 -77.10 REMARK 500 17 LYS A 3 33.07 -74.86 REMARK 500 17 LYS A 11 39.49 -80.53 REMARK 500 18 LYS A 3 30.58 -78.18 REMARK 500 18 LYS A 11 39.49 -79.59 REMARK 500 19 LYS A 3 29.91 -78.18 REMARK 500 19 LYS A 11 33.07 -82.53 REMARK 500 20 LYS A 3 30.31 -77.38 REMARK 500 20 LYS A 11 40.74 -75.00 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: P1A REMARK 800 EVIDENCE_CODE: AUTHOR REMARK 800 SITE_DESCRIPTION: SPECIFICITY DETERMINANT FOR INHIBITION REMARK 800 REMARK 800 SITE_IDENTIFIER: P1B REMARK 800 EVIDENCE_CODE: AUTHOR REMARK 800 SITE_DESCRIPTION: SPECIFICITY DETERMINANT FOR INHIBITION DBREF 2BEY A 1 16 PDB 2BEY 2BEY 1 16 SEQRES 1 A 16 CYS THR LYS SER ILE PRO PRO ILE CYS THR LYS SER ILE SEQRES 2 A 16 PRO PRO ILE SSBOND 1 CYS A 1 CYS A 9 1555 1555 2.02 CISPEP 1 ILE A 5 PRO A 6 1 1.96 CISPEP 2 ILE A 13 PRO A 14 1 0.21 CISPEP 3 ILE A 5 PRO A 6 2 1.05 CISPEP 4 ILE A 13 PRO A 14 2 0.23 CISPEP 5 ILE A 5 PRO A 6 3 1.31 CISPEP 6 ILE A 13 PRO A 14 3 0.42 CISPEP 7 ILE A 5 PRO A 6 4 -0.12 CISPEP 8 ILE A 13 PRO A 14 4 1.66 CISPEP 9 ILE A 5 PRO A 6 5 0.44 CISPEP 10 ILE A 13 PRO A 14 5 1.04 CISPEP 11 ILE A 5 PRO A 6 6 -0.44 CISPEP 12 ILE A 13 PRO A 14 6 0.75 CISPEP 13 ILE A 5 PRO A 6 7 -0.17 CISPEP 14 ILE A 13 PRO A 14 7 0.74 CISPEP 15 ILE A 5 PRO A 6 8 -0.18 CISPEP 16 ILE A 13 PRO A 14 8 -0.07 CISPEP 17 ILE A 5 PRO A 6 9 2.27 CISPEP 18 ILE A 13 PRO A 14 9 1.37 CISPEP 19 ILE A 5 PRO A 6 10 1.37 CISPEP 20 ILE A 13 PRO A 14 10 0.42 CISPEP 21 ILE A 5 PRO A 6 11 1.08 CISPEP 22 ILE A 13 PRO A 14 11 0.43 CISPEP 23 ILE A 5 PRO A 6 12 0.94 CISPEP 24 ILE A 13 PRO A 14 12 -0.29 CISPEP 25 ILE A 5 PRO A 6 13 0.47 CISPEP 26 ILE A 13 PRO A 14 13 2.03 CISPEP 27 ILE A 5 PRO A 6 14 0.58 CISPEP 28 ILE A 13 PRO A 14 14 0.59 CISPEP 29 ILE A 5 PRO A 6 15 0.18 CISPEP 30 ILE A 13 PRO A 14 15 0.88 CISPEP 31 ILE A 5 PRO A 6 16 0.04 CISPEP 32 ILE A 13 PRO A 14 16 -0.23 CISPEP 33 ILE A 5 PRO A 6 17 1.33 CISPEP 34 ILE A 13 PRO A 14 17 0.82 CISPEP 35 ILE A 5 PRO A 6 18 -0.28 CISPEP 36 ILE A 13 PRO A 14 18 -0.20 CISPEP 37 ILE A 5 PRO A 6 19 0.97 CISPEP 38 ILE A 13 PRO A 14 19 -0.44 CISPEP 39 ILE A 5 PRO A 6 20 1.05 CISPEP 40 ILE A 13 PRO A 14 20 0.23 SITE 1 P1A 1 LYS A 3 SITE 2 P1B 1 LYS A 11 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 - 21 20 Bytes