Header list of 1hbw.pdb file
Complete list - g 9 2 Bytes
HEADER TRANSCRIPTIONAL ACTIVATOR 20-APR-01 1HBW TITLE SOLUTION NMR STRUCTURE OF THE DIMERIZATION DOMAIN OF THE YEAST TITLE 2 TRANSCRIPTIONAL ACTIVATOR GAL4 (RESIDUES 50-106) COMPND MOL_ID: 1; COMPND 2 MOLECULE: REGULATORY PROTEIN GAL4; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: DIMERIZATION DOMAIN RESIDUES 50-106; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE; SOURCE 4 ORGANISM_COMMON: YEAST; SOURCE 5 ORGANISM_TAXID: 4932 KEYWDS TRANSCRIPTIONAL ACTIVATOR, GALACTOSE AND MELIBIOSE METABOLISM, KEYWDS 2 DIMERIZATION DOMAIN, COILED-COIL DIMERIC EXPDTA SOLUTION NMR NUMMDL 17 AUTHOR P.HIDALGO,A.Z.ANSARI,P.SCHMIDT,B.HARE,N.SIMKOVIC,S.FARRELL,E.J.SHIN, AUTHOR 2 M.PTASHNE,G.WAGNER REVDAT 4 14-JUN-23 1HBW 1 REMARK REVDAT 3 15-JAN-20 1HBW 1 REMARK ATOM REVDAT 2 24-FEB-09 1HBW 1 VERSN REVDAT 1 10-MAY-01 1HBW 0 JRNL AUTH P.HIDALGO,A.Z.ANSARI,P.SCHMIDT,B.HARE,N.SIMKOVICH,S.FARRELL, JRNL AUTH 2 E.J.SHIN,M.PTASHNE,G.WAGNER JRNL TITL RECRUITMENT OF THE TRANSCRIPTIONAL MACHINERY THROUGH GAL11P: JRNL TITL 2 STRUCTURE AND INTERACTIONS OF THE GAL4 DIMERIZATION DOMAIN JRNL REF GENES DEV. V. 15 1007 2001 JRNL REFN ISSN 0890-9369 JRNL PMID 11316794 JRNL DOI 10.1101/GAD.873901 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE- REMARK 3 KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ, RICE, REMARK 3 SIMONSON,WARREN REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: C2 SYMMETRY WAS ENFORCED IN THE REMARK 3 STRUCTURE CALCULATIONS. REMARK 4 REMARK 4 1HBW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-APR-01. REMARK 100 THE DEPOSITION ID IS D_1290005904. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 308 REMARK 210 PH : 7.4 REMARK 210 IONIC STRENGTH : 50 MM SODIUM PHOSPHATE REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY (1H; 13C; 15N); HNHA; REMARK 210 HNHB; HNCA; HN(CO)CA REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 600 MHZ; 500 MHZ; 400 REMARK 210 MHZ REMARK 210 SPECTROMETER MODEL : UP 750; UP 400; AMX; INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : CNS REMARK 210 METHOD USED : SIMULATED ANNEALING PROTOCOL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 300 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 17 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY AND MINIMAL NOE REMARK 210 DERIVED DISTANCE RESTRAINTS REMARK 210 VIOLATIONS 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 400 REMARK 400 COMPOUND REMARK 400 CHAIN A, B ENGINEERED MUTATION GLN87ARG, LYS90GLU REMARK 400 GAL4 IS A POSITIVE REGULATOR FOR THE GALACTOSE-INDUCED GENES 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 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 ALA A 52 -162.61 -176.84 REMARK 500 1 HIS A 53 153.51 65.23 REMARK 500 1 LEU A 54 -137.52 64.26 REMARK 500 1 THR A 55 -84.94 27.94 REMARK 500 1 ARG A 60 -73.85 -73.04 REMARK 500 1 PHE A 68 175.65 63.76 REMARK 500 1 LEU A 69 -66.90 -129.71 REMARK 500 1 ILE A 71 -58.05 -128.18 REMARK 500 1 ARG A 74 -53.06 -177.57 REMARK 500 1 GLU A 75 118.22 -175.99 REMARK 500 1 ASP A 76 -63.91 -159.08 REMARK 500 1 ASP A 78 -34.04 -130.94 REMARK 500 1 PHE A 97 75.84 38.78 REMARK 500 1 VAL A 102 -45.57 -148.42 REMARK 500 1 ASN A 103 -175.75 64.85 REMARK 500 1 ASP A 105 113.37 61.28 REMARK 500 1 ARG B 51 36.96 -157.61 REMARK 500 1 ALA B 52 -162.67 -176.73 REMARK 500 1 HIS B 53 153.66 65.38 REMARK 500 1 LEU B 54 -137.50 64.13 REMARK 500 1 THR B 55 -84.83 27.88 REMARK 500 1 ARG B 60 -73.66 -73.24 REMARK 500 1 PHE B 68 175.64 63.81 REMARK 500 1 LEU B 69 -67.57 -129.59 REMARK 500 1 ILE B 71 -58.12 -128.27 REMARK 500 1 ARG B 74 -54.68 -177.66 REMARK 500 1 ASP B 76 114.46 68.93 REMARK 500 1 LEU B 77 47.62 -101.64 REMARK 500 1 PHE B 97 75.79 38.80 REMARK 500 1 VAL B 102 -45.71 -148.49 REMARK 500 1 ASN B 103 -175.70 64.90 REMARK 500 1 ASP B 105 113.41 61.35 REMARK 500 2 ARG A 51 -41.42 -170.33 REMARK 500 2 LEU A 54 -80.95 64.47 REMARK 500 2 THR A 55 -90.50 6.54 REMARK 500 2 GLU A 56 -70.05 -44.46 REMARK 500 2 ARG A 60 -74.03 -73.38 REMARK 500 2 PHE A 68 -165.57 72.34 REMARK 500 2 LEU A 69 -33.05 86.88 REMARK 500 2 LEU A 77 -80.05 -103.13 REMARK 500 2 ASP A 78 -57.58 71.85 REMARK 500 2 LEU A 86 -41.72 -169.76 REMARK 500 2 PHE A 97 139.56 -36.69 REMARK 500 2 ASN A 103 92.18 42.92 REMARK 500 2 ASP A 105 33.40 -96.58 REMARK 500 2 ARG B 51 -78.53 -123.23 REMARK 500 2 LEU B 54 -80.85 64.32 REMARK 500 2 THR B 55 -90.47 6.39 REMARK 500 2 GLU B 56 -70.17 -44.35 REMARK 500 2 ARG B 60 -74.00 -73.46 REMARK 500 REMARK 500 THIS ENTRY HAS 465 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1AW6 RELATED DB: PDB REMARK 900 GAL4 (CD), NMR, 24 STRUCTURES REMARK 900 RELATED ID: 1D66 RELATED DB: PDB REMARK 900 GAL4 (RESIDUES 1 - 65) COMPLEX WITH 19MER DEOXYRIBONUCLEIC ACID REMARK 900 RELATED ID: 5180 RELATED DB: BMRB DBREF 1HBW A 50 106 UNP P04386 GAL4_YEAST 50 106 DBREF 1HBW B 50 106 UNP P04386 GAL4_YEAST 50 106 SEQADV 1HBW ARG A 87 UNP P04386 GLN 87 ENGINEERED MUTATION SEQADV 1HBW ARG B 87 UNP P04386 GLN 87 ENGINEERED MUTATION SEQADV 1HBW GLU A 90 UNP P04386 LYS 90 ENGINEERED MUTATION SEQADV 1HBW GLU B 90 UNP P04386 LYS 90 ENGINEERED MUTATION SEQRES 1 A 57 THR ARG ALA HIS LEU THR GLU VAL GLU SER ARG LEU GLU SEQRES 2 A 57 ARG LEU GLU GLN LEU PHE LEU LEU ILE PHE PRO ARG GLU SEQRES 3 A 57 ASP LEU ASP MET ILE LEU LYS MET ASP SER LEU ARG ASP SEQRES 4 A 57 ILE GLU ALA LEU LEU THR GLY LEU PHE VAL GLN ASP ASN SEQRES 5 A 57 VAL ASN LYS ASP ALA SEQRES 1 B 57 THR ARG ALA HIS LEU THR GLU VAL GLU SER ARG LEU GLU SEQRES 2 B 57 ARG LEU GLU GLN LEU PHE LEU LEU ILE PHE PRO ARG GLU SEQRES 3 B 57 ASP LEU ASP MET ILE LEU LYS MET ASP SER LEU ARG ASP SEQRES 4 B 57 ILE GLU ALA LEU LEU THR GLY LEU PHE VAL GLN ASP ASN SEQRES 5 B 57 VAL ASN LYS ASP ALA HELIX 1 1 THR A 55 GLN A 66 1 12 HELIX 2 2 ASP A 78 ASP A 84 1 7 HELIX 3 3 ARG A 87 PHE A 97 1 11 HELIX 4 4 THR B 55 GLN B 66 1 12 HELIX 5 5 ASP B 78 ASP B 84 1 7 HELIX 6 6 ARG B 87 PHE B 97 1 11 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 - g 9 2 Bytes