Header list of 1imq.pdb file
Complete list - 23 20 Bytes
HEADER BACTERIOCIN 30-MAY-96 1IMQ TITLE COLICIN E9 IMMUNITY PROTEIN IM9, NMR, MINIMIZED AVERAGE STRUCTURE COMPND MOL_ID: 1; COMPND 2 MOLECULE: IM9; COMPND 3 CHAIN: A SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 562; SOURCE 4 STRAIN: JM105 KEYWDS IMMUNITY PROTEIN, BACTERIOCIN, PLASMID, COLICIN EXPDTA SOLUTION NMR AUTHOR M.J.OSBORNE,A.L.BREEZE,L.Y.LIAN,A.REILLY,R.JAMES,C.KLEANTHOUS, AUTHOR 2 G.R.MOORE REVDAT 4 23-FEB-22 1IMQ 1 REMARK REVDAT 3 24-FEB-09 1IMQ 1 VERSN REVDAT 2 22-MAR-05 1IMQ 1 TITLE AUTHOR REVDAT 1 07-JUL-97 1IMQ 0 JRNL AUTH M.J.OSBORNE,A.L.BREEZE,L.Y.LIAN,A.REILLY,R.JAMES, JRNL AUTH 2 C.KLEANTHOUS,G.R.MOORE JRNL TITL THREE-DIMENSIONAL SOLUTION STRUCTURE AND 13C NUCLEAR JRNL TITL 2 MAGNETIC RESONANCE ASSIGNMENTS OF THE COLICIN E9 IMMUNITY JRNL TITL 3 PROTEIN IM9. JRNL REF BIOCHEMISTRY V. 35 9505 1996 JRNL REFN ISSN 0006-2960 JRNL PMID 8755730 JRNL DOI 10.1021/BI960401K REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH M.J.OSBORNE,L.Y.LIAN,R.WALLIS,A.REILLY,R.JAMES,C.KLEANTHOUS, REMARK 1 AUTH 2 G.R.MOORE REMARK 1 TITL SEQUENTIAL ASSIGNMENTS AND IDENTIFICATION OF SECONDARY REMARK 1 TITL 2 STRUCTURE ELEMENTS OF THE COLICIN E9 IMMUNITY PROTEIN IN REMARK 1 TITL 3 SOLUTION BY HOMONUCLEAR AND HETERONUCLEAR NMR REMARK 1 REF BIOCHEMISTRY V. 33 12347 1994 REMARK 1 REFN ISSN 0006-2960 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DIANA REMARK 3 AUTHORS : WUTHRICH REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1IMQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000174199. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : NULL REMARK 210 PH : NULL REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : NULL REMARK 210 SPECTROMETER MODEL : NULL REMARK 210 SPECTROMETER MANUFACTURER : NULL REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : NULL 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: 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: 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 HB3 ARG A 75 HB2 LYS A 80 0.43 REMARK 500 HD3 LYS A 4 OD1 ASP A 9 0.86 REMARK 500 HG22 VAL A 37 HD11 ILE A 53 1.03 REMARK 500 HD3 LYS A 4 CG ASP A 9 1.05 REMARK 500 OG SER A 48 HB3 ASP A 51 1.16 REMARK 500 CB ARG A 75 HB2 LYS A 80 1.22 REMARK 500 HA ALA A 25 HD12 LEU A 33 1.23 REMARK 500 HD21 LEU A 3 H LYS A 4 1.23 REMARK 500 HA SER A 6 HE1 MET A 43 1.27 REMARK 500 HB3 ARG A 75 CB LYS A 80 1.30 REMARK 500 HG LEU A 16 HG23 VAL A 68 1.30 REMARK 500 HG2 GLU A 41 HA3 GLY A 49 1.31 REMARK 500 O THR A 44 H HIS A 46 1.32 REMARK 500 HA LEU A 16 HG23 VAL A 68 1.33 REMARK 500 O SER A 63 HG13 ILE A 67 1.40 REMARK 500 O ILE A 22 HD23 LEU A 33 1.42 REMARK 500 O THR A 20 HB2 ASN A 24 1.46 REMARK 500 CG HIS A 46 HD2 PRO A 47 1.51 REMARK 500 ND1 HIS A 46 HD2 PRO A 47 1.54 REMARK 500 O VAL A 71 H TRP A 74 1.55 REMARK 500 HG LEU A 16 CG2 VAL A 68 1.56 REMARK 500 CD LYS A 4 OD1 ASP A 9 1.56 REMARK 500 OD1 ASP A 51 HB2 TYR A 55 1.57 REMARK 500 O SER A 65 H VAL A 68 1.58 REMARK 500 O ARG A 75 H LYS A 80 1.58 REMARK 500 O GLU A 45 O HIS A 46 1.65 REMARK 500 OG SER A 48 CB ASP A 51 1.86 REMARK 500 CE LYS A 4 OD1 ASP A 9 1.93 REMARK 500 O THR A 44 N HIS A 46 1.95 REMARK 500 O ILE A 22 CD2 LEU A 33 2.07 REMARK 500 NZ LYS A 4 OD1 ASP A 9 2.07 REMARK 500 CD2 LEU A 3 OH TYR A 10 2.10 REMARK 500 CD LYS A 4 CG ASP A 9 2.11 REMARK 500 O SER A 65 N ILE A 67 2.13 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 GLU A 2 107.59 -172.79 REMARK 500 LEU A 3 -152.88 -83.12 REMARK 500 LYS A 4 -161.55 -106.32 REMARK 500 SER A 6 -161.25 -164.00 REMARK 500 SER A 29 -178.36 144.97 REMARK 500 MET A 43 -70.56 -88.52 REMARK 500 GLU A 45 -11.07 44.27 REMARK 500 HIS A 46 163.42 -16.28 REMARK 500 TYR A 55 61.67 -151.91 REMARK 500 LYS A 57 149.31 -36.47 REMARK 500 ASP A 60 -143.87 -89.97 REMARK 500 SER A 63 162.33 -32.47 REMARK 500 SER A 65 -76.64 -74.02 REMARK 500 PHE A 83 -168.74 -79.18 REMARK 500 LYS A 84 -139.05 -68.62 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1IMP RELATED DB: PDB DBREF 1IMQ A 1 86 UNP P13479 IMM9_ECOLI 1 86 SEQRES 1 A 86 MET GLU LEU LYS HIS SER ILE SER ASP TYR THR GLU ALA SEQRES 2 A 86 GLU PHE LEU GLN LEU VAL THR THR ILE CYS ASN ALA ASP SEQRES 3 A 86 THR SER SER GLU GLU GLU LEU VAL LYS LEU VAL THR HIS SEQRES 4 A 86 PHE GLU GLU MET THR GLU HIS PRO SER GLY SER ASP LEU SEQRES 5 A 86 ILE TYR TYR PRO LYS GLU GLY ASP ASP ASP SER PRO SER SEQRES 6 A 86 GLY ILE VAL ASN THR VAL LYS GLN TRP ARG ALA ALA ASN SEQRES 7 A 86 GLY LYS SER GLY PHE LYS GLN GLY HELIX 1 1 GLU A 12 CYS A 23 1 12 HELIX 2 2 GLU A 30 THR A 44 1 15 HELIX 3 3 GLY A 49 TYR A 54 5 6 HELIX 4 4 SER A 65 ALA A 77 1 13 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 - 23 20 Bytes