Header list of 2i18.pdb file
Complete list - n 31 2 Bytes
HEADER METAL BINDING PROTEIN 13-AUG-06 2I18 TITLE THE REFINED STRUCTURE OF C-TERMINAL DOMAIN OF AN EF-HAND CALCIUM TITLE 2 BINDING PROTEIN FROM ENTAMOEBA HISTOLYTICA COMPND MOL_ID: 1; COMPND 2 MOLECULE: CALCIUM-BINDING PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: C-TERMINAL DOMAIN, RESIDUES 71-134; COMPND 5 SYNONYM: CABP SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ENTAMOEBA HISTOLYTICA; SOURCE 3 ORGANISM_TAXID: 5759 KEYWDS BETA SHEET, ALPHA HELIX, CALCIUM BINDING LOOPS, METAL BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 16 AUTHOR S.M.MUSTAFI,S.MUKHERJEE,K.V.R.CHARY REVDAT 4 31-JAN-18 2I18 1 AUTHOR REMARK REVDAT 3 24-FEB-09 2I18 1 VERSN REVDAT 2 28-NOV-06 2I18 1 JRNL REVDAT 1 22-AUG-06 2I18 0 SPRSDE 22-AUG-06 2I18 2EV7 JRNL AUTH S.M.MUSTAFI,S.MUKHERJEE,K.V.CHARY,G.CAVALLARO JRNL TITL STRUCTURAL BASIS FOR THE OBSERVED DIFFERENTIAL MAGNETIC JRNL TITL 2 ANISOTROPIC TENSORIAL VALUES IN CALCIUM BINDING PROTEINS. JRNL REF PROTEINS V. 65 656 2006 JRNL REFN ISSN 0887-3585 JRNL PMID 16981203 JRNL DOI 10.1002/PROT.21121 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PSEUDYANA 1.5 REMARK 3 AUTHORS : BANCI,L REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2I18 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-AUG-06. REMARK 100 THE DEPOSITION ID IS D_1000039009. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 308 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : 4.5 REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 1MM EHCABP U-15, 13C, 50MM TRIS REMARK 210 BUFFER, 90% H2O, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; 15N-1H HSQC REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE; INOVA REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 16 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE REFINEMENT IS DONE USING 6 LANTHANIDE IONS 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 O VAL A 27 H PHE A 31 1.38 REMARK 500 O LYS A 8 H LYS A 12 1.47 REMARK 500 O THR A 55 H PHE A 59 1.48 REMARK 500 O GLY A 35 H VAL A 39 1.51 REMARK 500 O VAL A 39 H VAL A 43 1.53 REMARK 500 OE1 GLU A 26 LA LA A 226 2.17 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 LYS A 4 33.32 -170.30 REMARK 500 1 ASP A 15 96.62 -40.34 REMARK 500 1 ASP A 17 -78.59 -38.87 REMARK 500 1 ASP A 19 -49.04 -159.56 REMARK 500 1 VAL A 27 -71.29 -67.16 REMARK 500 1 HIS A 34 -130.67 -67.04 REMARK 500 1 ILE A 36 -33.12 -36.37 REMARK 500 1 GLU A 37 -70.51 -65.33 REMARK 500 1 ALA A 48 49.58 39.05 REMARK 500 1 ASN A 49 -46.95 -146.70 REMARK 500 1 ASP A 51 66.78 176.38 REMARK 500 2 ASP A 3 49.19 -80.80 REMARK 500 2 LYS A 4 -32.26 173.51 REMARK 500 2 ASP A 15 98.04 -38.20 REMARK 500 2 ASP A 17 -71.79 -38.74 REMARK 500 2 VAL A 27 -71.14 -68.69 REMARK 500 2 HIS A 34 -132.77 -106.22 REMARK 500 2 ILE A 36 -44.62 -29.80 REMARK 500 2 ASP A 51 70.27 159.07 REMARK 500 3 ASP A 15 90.49 -53.22 REMARK 500 3 ASP A 17 -34.02 -39.43 REMARK 500 3 ASP A 19 -53.90 -161.00 REMARK 500 3 VAL A 27 -70.93 -70.09 REMARK 500 3 HIS A 34 -129.90 -93.84 REMARK 500 3 ILE A 36 -53.58 -29.86 REMARK 500 3 ASP A 47 56.00 -101.78 REMARK 500 3 ASP A 51 57.36 175.69 REMARK 500 4 ASP A 15 96.85 -43.55 REMARK 500 4 ASP A 17 -57.15 -148.87 REMARK 500 4 ASP A 19 -48.09 -137.40 REMARK 500 4 VAL A 27 -71.25 -67.45 REMARK 500 4 HIS A 34 -129.40 -79.32 REMARK 500 4 LYS A 38 -70.14 -61.64 REMARK 500 4 ALA A 48 79.49 -101.83 REMARK 500 4 ASN A 49 -41.87 -169.79 REMARK 500 4 ASP A 51 70.44 156.15 REMARK 500 5 ASP A 2 -56.03 76.53 REMARK 500 5 ASP A 3 -27.21 158.38 REMARK 500 5 LYS A 4 28.31 -162.86 REMARK 500 5 ASP A 15 94.06 -52.16 REMARK 500 5 VAL A 27 -70.24 -69.46 REMARK 500 5 HIS A 34 -129.04 -104.50 REMARK 500 5 ILE A 36 -34.97 -34.97 REMARK 500 5 GLU A 37 -70.90 -48.83 REMARK 500 5 ASP A 47 61.27 -104.80 REMARK 500 5 ASP A 51 60.82 173.38 REMARK 500 6 LYS A 4 -35.24 178.14 REMARK 500 6 ILE A 5 -31.11 -39.19 REMARK 500 6 ASP A 15 97.83 -39.46 REMARK 500 6 ASP A 17 -61.93 -174.78 REMARK 500 REMARK 500 THIS ENTRY HAS 149 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LA A 226 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1JFK RELATED DB: PDB REMARK 900 MINIMUM ENERGY REPRESENTATIVE STRUCTURE OF A CALCIUM BOUND EF-HAND REMARK 900 PROTEIN FROM ENTAMOEBA HISTOLYTICA REMARK 900 RELATED ID: 1JFJ RELATED DB: PDB REMARK 900 NMR SOLUTION STRUCTURE OF AN EF-HAND CALCIUM BINDING PROTEIN FROM REMARK 900 ENTAMOEBA HISTOLYTICA DBREF 2I18 A 1 64 UNP P38505 CALBP_ENTHI 71 134 SEQRES 1 A 64 SER ASP ASP LYS ILE GLY LEU LYS VAL LEU TYR LYS LEU SEQRES 2 A 64 MET ASP VAL ASP GLY ASP GLY LYS LEU THR LYS GLU GLU SEQRES 3 A 64 VAL THR SER PHE PHE LYS LYS HIS GLY ILE GLU LYS VAL SEQRES 4 A 64 ALA GLU GLN VAL MET LYS ALA ASP ALA ASN GLY ASP GLY SEQRES 5 A 64 TYR ILE THR LEU GLU GLU PHE LEU GLU PHE SER LEU HET LA A 226 1 HETNAM LA LANTHANUM (III) ION FORMUL 2 LA LA 3+ HELIX 1 1 LYS A 4 ASP A 15 1 12 HELIX 2 2 LYS A 24 LYS A 32 1 9 HELIX 3 3 GLY A 35 ALA A 48 1 14 HELIX 4 4 LEU A 56 LEU A 64 1 9 SHEET 1 A 2 LYS A 21 THR A 23 0 SHEET 2 A 2 TYR A 53 THR A 55 -1 O ILE A 54 N LEU A 22 SITE 1 AC1 6 ASP A 15 ASP A 17 GLY A 18 ASP A 19 SITE 2 AC1 6 LYS A 21 GLU A 26 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 - n 31 2 Bytes