Header list of 1imt.pdb file
Complete list - b 23 2 Bytes
HEADER TOXIN 14-APR-98 1IMT TITLE MAMBA INTESTINAL TOXIN 1, NMR, 39 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: INTESTINAL TOXIN 1; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: MIT1 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: DENDROASPIS POLYLEPIS POLYLEPIS; SOURCE 3 ORGANISM_COMMON: BLACK MAMBA; SOURCE 4 ORGANISM_TAXID: 8620; SOURCE 5 STRAIN: POLYLEPIS; SOURCE 6 SECRETION: VENOM KEYWDS VENOM, STRUCTURAL HOMOLOGUE OF COLIPASE, RESISTANCE TO ENDOPROTEASES, KEYWDS 2 CONTRACT GUINEA PIG ILEUM, TOXIN EXPDTA SOLUTION NMR NUMMDL 39 AUTHOR J.BOISBOUVIER,J.-P.ALBRAND,M.BLACKLEDGE,M.JAQUINOD,H.SCHWEITZ, AUTHOR 2 M.LAZDUNSKI,D.MARION REVDAT 3 23-FEB-22 1IMT 1 REMARK SEQADV REVDAT 2 24-FEB-09 1IMT 1 VERSN REVDAT 1 20-APR-99 1IMT 0 JRNL AUTH J.BOISBOUVIER,J.P.ALBRAND,M.BLACKLEDGE,M.JAQUINOD, JRNL AUTH 2 H.SCHWEITZ,M.LAZDUNSKI,D.MARION JRNL TITL A STRUCTURAL HOMOLOGUE OF COLIPASE IN BLACK MAMBA VENOM JRNL TITL 2 REVEALED BY NMR FLOATING DISULPHIDE BRIDGE ANALYSIS. JRNL REF J.MOL.BIOL. V. 283 205 1998 JRNL REFN ISSN 0022-2836 JRNL PMID 9761684 JRNL DOI 10.1006/JMBI.1998.2057 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DISCOVER REMARK 3 AUTHORS : BIOSYM/MSI REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE REMARK 3 JRNL CITATION: BLACKLEDGE, M. ET AL. (1995). J. MOL. BIOL. 245, REMARK 3 PP661-681 REMARK 4 REMARK 4 1IMT 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_1000174202. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 305 REMARK 210 PH : 4.5 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : H2O OR D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; COSY; HSQC; HSQC REMARK 210 -TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : AMX600 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DISCOVER REMARK 210 METHOD USED : RESTRAINED SIMULATED ANNEALING REMARK 210 AND RESTRAINED MOLECULAR REMARK 210 DYNAMICS ENERGY REFINEMENT REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 110 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 39 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION AND REMARK 210 BEST PHYSICAL ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 2 REMARK 210 REMARK 210 REMARK: MODEL NUMBER 2 WAS DETERMINED USING 2D NMR SPECTROSCOPY ON REMARK 210 PURIFIED TOXIN. 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 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 GLU A 8 -32.29 -136.13 REMARK 500 1 CYS A 13 -52.22 -138.91 REMARK 500 1 SER A 37 108.52 -38.86 REMARK 500 1 LYS A 47 161.36 -48.08 REMARK 500 1 MET A 55 -40.54 74.10 REMARK 500 1 ASN A 64 35.79 -87.40 REMARK 500 2 THR A 4 33.10 -74.85 REMARK 500 2 CYS A 13 -60.67 -99.28 REMARK 500 2 CYS A 31 99.55 -69.48 REMARK 500 2 SER A 37 111.83 -36.31 REMARK 500 2 LYS A 73 -39.81 71.48 REMARK 500 2 LYS A 74 81.73 -66.20 REMARK 500 2 SER A 79 37.79 -79.28 REMARK 500 3 ILE A 3 67.54 -118.91 REMARK 500 3 LYS A 15 -35.24 -39.17 REMARK 500 3 LYS A 26 -0.08 -57.99 REMARK 500 3 SER A 37 107.53 -41.05 REMARK 500 3 LYS A 47 156.48 -48.88 REMARK 500 3 PRO A 63 -43.49 -24.64 REMARK 500 3 LYS A 73 -44.36 71.64 REMARK 500 4 GLU A 8 -36.17 -131.12 REMARK 500 4 CYS A 13 -119.55 -104.04 REMARK 500 4 LYS A 15 83.67 -53.89 REMARK 500 4 LYS A 26 -1.38 -58.76 REMARK 500 4 CYS A 31 99.91 -65.55 REMARK 500 4 SER A 45 91.12 -67.34 REMARK 500 4 HIS A 46 134.06 -23.99 REMARK 500 4 PRO A 63 78.89 -37.27 REMARK 500 4 ASN A 64 -52.88 160.63 REMARK 500 4 THR A 70 -32.38 -131.48 REMARK 500 4 LYS A 73 -15.37 72.98 REMARK 500 5 VAL A 2 36.90 -83.68 REMARK 500 5 ILE A 3 -88.18 -0.72 REMARK 500 5 ALA A 6 145.42 133.24 REMARK 500 5 LEU A 11 -38.47 -39.70 REMARK 500 5 TRP A 24 -66.79 -99.83 REMARK 500 5 LYS A 26 -6.75 -56.04 REMARK 500 5 CYS A 31 95.38 -65.17 REMARK 500 5 SER A 37 108.53 -41.40 REMARK 500 5 SER A 45 106.89 -59.12 REMARK 500 5 LYS A 47 179.30 -59.31 REMARK 500 5 MET A 55 33.94 -78.64 REMARK 500 5 HIS A 57 37.50 -79.33 REMARK 500 5 PRO A 63 79.41 -46.64 REMARK 500 5 ASN A 64 -48.50 166.46 REMARK 500 5 LYS A 73 -34.34 72.94 REMARK 500 5 LYS A 74 85.49 -69.95 REMARK 500 6 ILE A 3 -71.21 61.68 REMARK 500 6 LYS A 15 34.18 -74.76 REMARK 500 6 VAL A 21 143.78 -38.01 REMARK 500 REMARK 500 THIS ENTRY HAS 381 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 2 ARG A 29 0.15 SIDE CHAIN REMARK 500 4 PHE A 50 0.14 SIDE CHAIN REMARK 500 4 ARG A 54 0.08 SIDE CHAIN REMARK 500 7 HIS A 46 0.09 SIDE CHAIN REMARK 500 8 ARG A 54 0.13 SIDE CHAIN REMARK 500 12 ARG A 29 0.10 SIDE CHAIN REMARK 500 12 HIS A 57 0.10 SIDE CHAIN REMARK 500 13 ARG A 54 0.10 SIDE CHAIN REMARK 500 19 HIS A 57 0.08 SIDE CHAIN REMARK 500 20 ARG A 29 0.12 SIDE CHAIN REMARK 500 22 PHE A 75 0.10 SIDE CHAIN REMARK 500 23 HIS A 57 0.10 SIDE CHAIN REMARK 500 26 HIS A 57 0.13 SIDE CHAIN REMARK 500 27 ARG A 29 0.11 SIDE CHAIN REMARK 500 27 HIS A 46 0.09 SIDE CHAIN REMARK 500 29 ARG A 29 0.11 SIDE CHAIN REMARK 500 32 ARG A 9 0.09 SIDE CHAIN REMARK 500 32 PHE A 75 0.10 SIDE CHAIN REMARK 500 33 ARG A 9 0.11 SIDE CHAIN REMARK 500 33 PHE A 75 0.13 SIDE CHAIN REMARK 500 35 ARG A 29 0.11 SIDE CHAIN REMARK 500 36 ARG A 54 0.12 SIDE CHAIN REMARK 500 39 HIS A 57 0.10 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1IMT A 1 80 UNP P25687 VPRA_DENPO 1 81 SEQADV 1IMT A UNP P25687 LYS 55 DELETION SEQRES 1 A 80 ALA VAL ILE THR GLY ALA CYS GLU ARG ASP LEU GLN CYS SEQRES 2 A 80 GLY LYS GLY THR CYS CYS ALA VAL SER LEU TRP ILE LYS SEQRES 3 A 80 SER VAL ARG VAL CYS THR PRO VAL GLY THR SER GLY GLU SEQRES 4 A 80 ASP CYS HIS PRO ALA SER HIS LYS ILE PRO PHE SER GLY SEQRES 5 A 80 GLN ARG MET HIS HIS THR CYS PRO CYS ALA PRO ASN LEU SEQRES 6 A 80 ALA CYS VAL GLN THR SER PRO LYS LYS PHE LYS CYS LEU SEQRES 7 A 80 SER LYS HELIX 1 1 ASP A 10 GLN A 12 5 3 SHEET 1 A 2 THR A 17 VAL A 21 0 SHEET 2 A 2 ARG A 29 PRO A 33 -1 N THR A 32 O CYS A 18 SHEET 1 B 2 ALA A 66 SER A 71 0 SHEET 2 B 2 LYS A 74 LEU A 78 -1 N LEU A 78 O ALA A 66 SSBOND 1 CYS A 7 CYS A 19 1555 1555 2.08 SSBOND 2 CYS A 13 CYS A 31 1555 1555 2.08 SSBOND 3 CYS A 18 CYS A 59 1555 1555 2.08 SSBOND 4 CYS A 41 CYS A 67 1555 1555 2.08 SSBOND 5 CYS A 61 CYS A 77 1555 1555 2.08 CISPEP 1 ILE A 48 PRO A 49 1 2.25 CISPEP 2 ILE A 48 PRO A 49 2 -4.26 CISPEP 3 ILE A 48 PRO A 49 3 1.10 CISPEP 4 ILE A 48 PRO A 49 4 -3.69 CISPEP 5 ILE A 48 PRO A 49 5 -5.36 CISPEP 6 ILE A 48 PRO A 49 6 -6.34 CISPEP 7 ILE A 48 PRO A 49 7 -1.35 CISPEP 8 ILE A 48 PRO A 49 8 10.46 CISPEP 9 ILE A 48 PRO A 49 9 0.30 CISPEP 10 ILE A 48 PRO A 49 10 -10.34 CISPEP 11 ILE A 48 PRO A 49 11 -9.70 CISPEP 12 ILE A 48 PRO A 49 12 -8.19 CISPEP 13 ILE A 48 PRO A 49 13 -5.28 CISPEP 14 ILE A 48 PRO A 49 14 -3.24 CISPEP 15 ILE A 48 PRO A 49 15 -6.36 CISPEP 16 ILE A 48 PRO A 49 16 -3.98 CISPEP 17 ILE A 48 PRO A 49 17 -4.85 CISPEP 18 ILE A 48 PRO A 49 18 -5.21 CISPEP 19 ILE A 48 PRO A 49 19 -10.11 CISPEP 20 ILE A 48 PRO A 49 20 -9.98 CISPEP 21 ILE A 48 PRO A 49 21 -3.12 CISPEP 22 ILE A 48 PRO A 49 22 -9.28 CISPEP 23 ILE A 48 PRO A 49 23 -7.70 CISPEP 24 ILE A 48 PRO A 49 24 -3.68 CISPEP 25 ILE A 48 PRO A 49 25 -5.20 CISPEP 26 ILE A 48 PRO A 49 26 -7.39 CISPEP 27 ILE A 48 PRO A 49 27 -10.40 CISPEP 28 ILE A 48 PRO A 49 28 -10.51 CISPEP 29 ILE A 48 PRO A 49 29 -9.99 CISPEP 30 ILE A 48 PRO A 49 30 -5.87 CISPEP 31 ILE A 48 PRO A 49 31 -7.56 CISPEP 32 ILE A 48 PRO A 49 32 -7.33 CISPEP 33 ILE A 48 PRO A 49 33 -6.54 CISPEP 34 ILE A 48 PRO A 49 34 -8.89 CISPEP 35 ILE A 48 PRO A 49 35 -1.24 CISPEP 36 ILE A 48 PRO A 49 36 -7.70 CISPEP 37 ILE A 48 PRO A 49 37 -6.39 CISPEP 38 ILE A 48 PRO A 49 38 -3.43 CISPEP 39 ILE A 48 PRO A 49 39 -10.41 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 23 2 Bytes