Header list of 1w7e.pdb file
Complete list - 22 20 Bytes
HEADER CELL ADHESION 01-SEP-04 1W7E TITLE NMR ENSEMBLE OF FASCICLIN-LIKE PROTEIN FROM RHODOBACTER SPHAEROIDES COMPND MOL_ID: 1; COMPND 2 MOLECULE: BETA-IG-H3/FASCICLIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: FASCICLIN-LIKE PROTEIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RHODOBACTER SPHAEROIDES; SOURCE 3 ORGANISM_TAXID: 1063; SOURCE 4 ATCC: NCIB 8253; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET14B KEYWDS FASCICLIN, CELL ADHESION EXPDTA SOLUTION NMR NUMMDL 6 AUTHOR R.MOODY,M.K.PHILLIPS-JONES,M.P.WILLIAMSON REVDAT 4 30-JUL-14 1W7E 1 JRNL REVDAT 3 19-JUN-13 1W7E 1 TITLE COMPND SOURCE KEYWDS REVDAT 3 2 REMARK VERSN DBREF ATOM REVDAT 3 3 TER REVDAT 2 24-FEB-09 1W7E 1 VERSN REVDAT 1 08-MAR-06 1W7E 0 JRNL AUTH R.G.MOODY,M.P.WILLIAMSON JRNL TITL STRUCTURE AND FUNCTION OF A BACTERIAL FASCICLIN I DOMAIN JRNL TITL 2 PROTEIN ELUCIDATES FUNCTION OF RELATED CELL ADHESION JRNL TITL 3 PROTEINS SUCH AS TGFBIP AND PERIOSTIN. JRNL REF FEBS OPEN BIO V. 3 71 2013 JRNL REFN ISSN 2211-5463 JRNL PMID 23772377 JRNL DOI 10.1016/J.FOB.2013.01.001 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.2 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,READ, REMARK 3 RICE,SIMONSON,WARREN REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1W7E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-SEP-04. REMARK 100 THE PDBE ID CODE IS EBI-20945. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298.0 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : 50 MM REMARK 210 PRESSURE : 1.0 ATM REMARK 210 SAMPLE CONTENTS : 90% WATER/10% D2O, REMARK 210 50MM NAPHOS REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; HNHA REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ REMARK 210 SPECTROMETER MODEL : DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : FELIX REMARK 210 METHOD USED : CNS 1.2 REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 6 REMARK 210 CONFORMERS, SELECTION CRITERIA : 6 RANDOMLY CHOSEN FROM REMARK 210 30 LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: SEE PDB ENTRY 1W7D FOR BEST STRUCTURE 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 MODELS 1-6 REMARK 465 RES C SSSEQI REMARK 465 GLU A 21 REMARK 465 THR A 22 REMARK 465 GLY A 23 REMARK 465 ALA A 157 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 LEU A 38 -45.16 -142.55 REMARK 500 1 PRO A 71 -167.92 -76.75 REMARK 500 1 LEU A 105 -79.16 -117.61 REMARK 500 1 LEU A 123 -65.15 -122.18 REMARK 500 1 SER A 135 -61.10 -27.96 REMARK 500 1 VAL A 139 -60.64 74.34 REMARK 500 1 MET A 154 157.67 59.18 REMARK 500 2 LEU A 38 -53.95 -136.20 REMARK 500 2 LEU A 70 71.75 -115.29 REMARK 500 2 PRO A 71 -159.04 -82.27 REMARK 500 2 THR A 106 179.38 179.26 REMARK 500 2 LEU A 123 -41.91 -130.04 REMARK 500 2 SER A 135 -76.11 -37.57 REMARK 500 2 VAL A 139 -67.98 68.52 REMARK 500 2 MET A 154 148.03 72.47 REMARK 500 3 LEU A 38 -39.18 -143.88 REMARK 500 3 MET A 101 88.63 -60.79 REMARK 500 3 LEU A 123 -39.12 -155.98 REMARK 500 3 VAL A 129 113.88 -160.07 REMARK 500 3 SER A 135 -86.82 -14.46 REMARK 500 3 VAL A 139 -28.64 81.71 REMARK 500 3 ASP A 140 79.22 -112.27 REMARK 500 3 MET A 154 157.16 62.21 REMARK 500 4 SER A 34 -21.67 170.30 REMARK 500 4 LEU A 38 -52.44 -144.85 REMARK 500 4 LEU A 70 108.52 -54.43 REMARK 500 4 LEU A 105 -53.40 -133.21 REMARK 500 4 GLN A 136 79.67 -114.78 REMARK 500 4 VAL A 139 -38.37 81.93 REMARK 500 5 PHE A 35 49.08 -148.10 REMARK 500 5 LEU A 38 -53.94 -144.57 REMARK 500 5 PRO A 71 -159.25 -86.36 REMARK 500 5 LEU A 105 -50.48 -130.79 REMARK 500 5 THR A 106 146.29 -178.16 REMARK 500 5 SER A 135 -59.66 -20.10 REMARK 500 5 VAL A 139 -54.28 71.00 REMARK 500 5 MET A 154 148.37 62.33 REMARK 500 6 LEU A 38 -38.89 -134.39 REMARK 500 6 LEU A 70 76.51 -111.17 REMARK 500 6 PRO A 71 -158.94 -81.19 REMARK 500 6 LEU A 105 -81.17 -123.15 REMARK 500 6 LEU A 123 -54.62 -132.93 REMARK 500 6 SER A 135 -91.25 -23.50 REMARK 500 6 VAL A 139 -29.84 82.38 REMARK 500 6 MET A 154 145.20 66.68 REMARK 500 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED. REMARK 700 REMARK 700 SHEET REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED. REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1W7D RELATED DB: PDB REMARK 900 NMR STRUCTURE OF FASCICLIN-LIKE PROTEIN FROM REMARK 900 RHODOBACTER SPHAEROIDES REMARK 999 REMARK 999 SEQUENCE REMARK 999 RHODOBACTER SPHAEROIDES GENOME DATABASE DBREF 1W7E A 21 157 UNP Q3IXZ6 Q3IXZ6_RHOS4 20 156 SEQRES 1 A 137 GLU THR GLY ASP ILE VAL GLU THR ALA THR GLY ALA GLY SEQRES 2 A 137 SER PHE THR THR LEU LEU THR ALA ALA GLU ALA ALA GLY SEQRES 3 A 137 LEU VAL ASP THR LEU LYS GLY ASP GLY PRO PHE THR VAL SEQRES 4 A 137 PHE ALA PRO THR ASP ALA ALA PHE ALA ALA LEU PRO GLU SEQRES 5 A 137 GLY THR VAL GLU ASP LEU LEU LYS PRO GLU ASN LYS GLU SEQRES 6 A 137 LYS LEU THR GLU ILE LEU THR TYR HIS VAL VAL PRO GLY SEQRES 7 A 137 GLU VAL MET SER SER ASP LEU THR GLU GLY MET THR ALA SEQRES 8 A 137 GLU THR VAL GLU GLY GLY ALA LEU THR VAL THR LEU GLU SEQRES 9 A 137 GLY GLY PRO LYS VAL ASN GLY VAL SER ILE SER GLN PRO SEQRES 10 A 137 ASP VAL ASP ALA SER ASN GLY VAL ILE HIS VAL ILE ASP SEQRES 11 A 137 GLY VAL LEU MET PRO GLY ALA HELIX 1 1 ILE A 25 GLY A 31 5 7 HELIX 2 2 LEU A 39 ALA A 45 1 7 HELIX 3 3 LEU A 47 LYS A 52 1 6 HELIX 4 4 THR A 63 LEU A 70 1 8 HELIX 5 5 GLY A 73 LEU A 78 1 6 HELIX 6 6 LYS A 80 HIS A 94 1 15 SHEET 1 AA 3 VAL A 95 GLY A 98 0 SHEET 2 AA 3 PRO A 56 ALA A 61 -1 O THR A 58 N VAL A 96 SHEET 3 AA 3 GLY A 144 ILE A 149 1 O VAL A 145 N VAL A 59 SHEET 1 AB 4 GLY A 108 THR A 113 0 SHEET 2 AB 4 GLY A 117 LEU A 123 -1 O LEU A 119 N ALA A 111 SHEET 3 AB 4 LYS A 128 ASN A 130 -1 O LYS A 128 N THR A 122 SHEET 4 AB 4 VAL A 132 ILE A 134 -1 O VAL A 132 N VAL A 129 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 - 22 20 Bytes