Header list of 1owa.pdb file
Complete list - b 23 2 Bytes
HEADER CYTOKINE 28-MAR-03 1OWA TITLE SOLUTION STRUCTURAL STUDIES ON HUMAN ERYTHROCYTE ALPHA SPECTRIN N TITLE 2 TERMINAL TETRAMERIZATION DOMAIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPECTRIN ALPHA CHAIN, ERYTHROCYTE; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 1-156; COMPND 5 SYNONYM: ERYTHROID ALPHA-SPECTRIN; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: SPTA1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS TRIPLE HELICAL BUNDLE, CYTOKINE EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR S.PARK,M.S.CAFFREY,M.E.JOHNSON,L.W.FUNG REVDAT 3 23-FEB-22 1OWA 1 REMARK REVDAT 2 24-FEB-09 1OWA 1 VERSN REVDAT 1 30-MAR-04 1OWA 0 JRNL AUTH S.PARK,M.S.CAFFREY,M.E.JOHNSON,L.W.FUNG JRNL TITL SOLUTION STRUCTURAL STUDIES ON HUMAN ERYTHROCYTE JRNL TITL 2 ALPHA-SPECTRIN TETRAMERIZATION SITE. JRNL REF J.BIOL.CHEM. V. 278 21837 2003 JRNL REFN ISSN 0021-9258 JRNL PMID 12672815 JRNL DOI 10.1074/JBC.M300617200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1, CNS 1.1 REMARK 3 AUTHORS : BRUNGER (CNS), BRUNGER (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1OWA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-APR-03. REMARK 100 THE DEPOSITION ID IS D_1000018731. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 293 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 5MM PHOSPHATE, 150MM NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1MM SPECTRIN, 5MM PHOSPHATE, REMARK 210 150MM NACL, 5% D2O, 95 % H2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D_13C REMARK 210 -SEPARATED_NOESY; 3D_15N- REMARK 210 SEPARATED_NOESY; 4D_13C- REMARK 210 SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : DRX; DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER 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 : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY CONFORMERS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 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 HE1 TRP A 68 HB3 GLU A 100 1.24 REMARK 500 O THR A 20 H ILE A 24 1.52 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 LEU A 49 101.01 56.64 REMARK 500 1 GLU A 50 -102.75 -162.36 REMARK 500 2 GLU A 50 -44.09 80.45 REMARK 500 2 THR A 85 -73.12 -83.30 REMARK 500 2 ILE A 87 89.20 -162.74 REMARK 500 2 PHE A 119 65.67 60.40 REMARK 500 3 LYS A 16 118.23 64.25 REMARK 500 3 GLU A 50 95.19 87.57 REMARK 500 4 ASP A 51 109.18 65.77 REMARK 500 4 GLU A 82 -79.96 -89.93 REMARK 500 4 PHE A 119 -90.14 39.46 REMARK 500 4 THR A 120 20.88 -161.29 REMARK 500 4 MET A 121 178.93 49.33 REMARK 500 5 SER A 13 -26.93 -162.58 REMARK 500 5 LYS A 16 60.27 -159.98 REMARK 500 5 GLU A 50 106.21 -178.77 REMARK 500 5 PRO A 84 156.21 -47.94 REMARK 500 5 ARG A 118 -105.48 -106.48 REMARK 500 5 THR A 120 27.89 -157.21 REMARK 500 6 GLU A 2 79.54 62.82 REMARK 500 6 LYS A 6 179.95 79.22 REMARK 500 6 LEU A 49 -80.00 -90.02 REMARK 500 6 PRO A 84 52.17 -68.45 REMARK 500 6 PHE A 119 96.16 60.09 REMARK 500 6 MET A 121 100.92 63.67 REMARK 500 7 SER A 13 9.91 -157.81 REMARK 500 7 LEU A 49 -64.67 -161.50 REMARK 500 7 ASP A 51 102.29 69.42 REMARK 500 7 THR A 85 -70.41 -79.91 REMARK 500 7 ILE A 87 87.30 -154.81 REMARK 500 8 GLU A 2 -175.44 59.29 REMARK 500 8 GLU A 11 141.32 71.32 REMARK 500 8 GLU A 82 -87.40 -126.03 REMARK 500 8 PRO A 84 -175.56 -61.13 REMARK 500 8 ILE A 87 -86.73 36.50 REMARK 500 8 THR A 120 28.26 -157.00 REMARK 500 8 MET A 121 -36.28 -152.11 REMARK 500 9 LEU A 49 -43.46 -155.40 REMARK 500 9 GLU A 50 106.39 79.50 REMARK 500 9 PRO A 84 -166.14 -78.28 REMARK 500 9 ILE A 87 -62.80 70.79 REMARK 500 9 THR A 120 -171.96 43.28 REMARK 500 10 GLU A 50 17.63 46.47 REMARK 500 10 ASP A 51 -73.05 -90.32 REMARK 500 REMARK 500 REMARK: NULL DBREF 1OWA A 1 156 UNP P02549 SPTA1_HUMAN 1 156 SEQRES 1 A 156 MET GLU GLN PHE PRO LYS GLU THR VAL VAL GLU SER SER SEQRES 2 A 156 GLY PRO LYS VAL LEU GLU THR ALA GLU GLU ILE GLN GLU SEQRES 3 A 156 ARG ARG GLN GLU VAL LEU THR ARG TYR GLN SER PHE LYS SEQRES 4 A 156 GLU ARG VAL ALA GLU ARG GLY GLN LYS LEU GLU ASP SER SEQRES 5 A 156 TYR HIS LEU GLN VAL PHE LYS ARG ASP ALA ASP ASP LEU SEQRES 6 A 156 GLY LYS TRP ILE MET GLU LYS VAL ASN ILE LEU THR ASP SEQRES 7 A 156 LYS SER TYR GLU ASP PRO THR ASN ILE GLN GLY LYS TYR SEQRES 8 A 156 GLN LYS HIS GLN SER LEU GLU ALA GLU VAL GLN THR LYS SEQRES 9 A 156 SER ARG LEU MET SER GLU LEU GLU LYS THR ARG GLU GLU SEQRES 10 A 156 ARG PHE THR MET GLY HIS SER ALA HIS GLU GLU THR LYS SEQRES 11 A 156 ALA HIS ILE GLU GLU LEU ARG HIS LEU TRP ASP LEU LEU SEQRES 12 A 156 LEU GLU LEU THR LEU GLU LYS GLY ASP GLN LEU LEU ARG HELIX 1 1 THR A 20 GLY A 46 1 27 HELIX 2 2 SER A 52 GLU A 82 1 31 HELIX 3 3 ASN A 86 ARG A 118 1 33 HELIX 4 4 GLY A 122 LEU A 155 1 34 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