Header list of 2aby.pdb file
Complete list - r 9 2 Bytes
HEADER UNKNOWN FUNCTION 18-JUL-05 2ABY TITLE SOLUTION STRUCTURE OF TA0743 FROM THERMOPLASMA ACIDOPHILUM COMPND MOL_ID: 1; COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN TA0743; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: THERMOPLASMA ACIDOPHILUM; SOURCE 3 ORGANISM_TAXID: 2303; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS HELIX-TURN-HELIX, UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR B.KIM,J.JUNG,E.HONG,A.YEE,C.H.ARROWSMITH,W.LEE REVDAT 3 09-MAR-22 2ABY 1 REMARK SEQADV REVDAT 2 24-FEB-09 2ABY 1 VERSN REVDAT 1 08-AUG-06 2ABY 0 JRNL AUTH B.KIM,J.JUNG,E.HONG,A.YEE,C.H.ARROWSMITH,W.LEE JRNL TITL NMR STRUCTURE OF THE CONSERVED NOVEL-FOLD PROTEIN TA0743 JRNL TITL 2 FROM THERMOPLASMA ACIDOPHILUM. JRNL REF PROTEINS V. 62 819 2006 JRNL REFN ISSN 0887-3585 JRNL PMID 16374782 JRNL DOI 10.1002/PROT.20832 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE 2.3, CYANA 2.0 REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), HERRMANN (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2ABY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUL-05. REMARK 100 THE DEPOSITION ID IS D_1000033724. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : NO SALT REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 1.6MM TA0743 U-15N,13C,15N/13C REMARK 210 50MM POTASSIUM PHOSPHATE BUFFER , REMARK 210 NAN3,90% H20,10% D20 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; HNHA REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : DRX; DMX; UNITYPLUS REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : SPARKY 3.110, MARS 1.1, CYANA REMARK 210 2.0 REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY 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 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 1-20 REMARK 465 RES C SSSEQI REMARK 465 MET A -21 REMARK 465 GLY A -20 REMARK 465 THR A -19 REMARK 465 SER A -18 REMARK 465 HIS A -17 REMARK 465 HIS A -16 REMARK 465 HIS A -15 REMARK 465 HIS A -14 REMARK 465 HIS A -13 REMARK 465 HIS A -12 REMARK 465 SER A -11 REMARK 465 SER A -10 REMARK 465 GLY A -9 REMARK 465 ARG A -8 REMARK 465 GLU A -7 REMARK 465 ASN A -6 REMARK 465 LEU A -5 REMARK 465 TYR A -4 REMARK 465 PHE A -3 REMARK 465 GLN A -2 REMARK 465 SER A -1 REMARK 465 HIS A 0 REMARK 465 GLY A 123 REMARK 465 SER A 124 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 3 -176.49 -175.40 REMARK 500 1 ASN A 13 -168.42 178.96 REMARK 500 1 PHE A 31 74.09 -112.59 REMARK 500 1 LYS A 37 71.34 -105.93 REMARK 500 1 HIS A 64 71.28 63.66 REMARK 500 1 GLU A 110 -168.65 170.76 REMARK 500 1 ASP A 112 -69.19 -131.80 REMARK 500 1 LEU A 113 -168.76 -60.11 REMARK 500 1 GLU A 115 71.10 37.43 REMARK 500 1 ASP A 116 -60.57 -179.31 REMARK 500 1 GLN A 120 -74.58 -100.54 REMARK 500 2 ILE A 12 -48.65 -140.05 REMARK 500 2 PHE A 31 73.26 -112.05 REMARK 500 2 LEU A 34 19.35 59.56 REMARK 500 2 ASN A 39 168.53 179.86 REMARK 500 2 LEU A 60 107.08 -45.18 REMARK 500 2 HIS A 64 66.74 64.24 REMARK 500 2 MET A 81 157.90 -44.97 REMARK 500 2 GLU A 110 -168.07 174.44 REMARK 500 2 LEU A 113 -171.04 -59.46 REMARK 500 2 ASP A 116 -62.05 -179.02 REMARK 500 2 GLN A 120 -74.82 -85.89 REMARK 500 3 ILE A 12 -68.01 -140.75 REMARK 500 3 PHE A 31 74.50 -112.21 REMARK 500 3 LYS A 37 77.18 -113.53 REMARK 500 3 HIS A 64 67.81 60.96 REMARK 500 3 MET A 81 150.48 -41.38 REMARK 500 3 GLU A 110 -168.52 171.90 REMARK 500 3 TYR A 111 77.55 -117.11 REMARK 500 3 ASP A 112 -74.28 -117.79 REMARK 500 3 LEU A 113 -175.28 -57.59 REMARK 500 3 ASP A 116 -60.37 179.37 REMARK 500 3 GLN A 120 -74.67 -88.12 REMARK 500 4 ILE A 12 -39.39 -130.81 REMARK 500 4 PHE A 31 71.64 -113.61 REMARK 500 4 LYS A 37 76.94 -111.30 REMARK 500 4 HIS A 64 71.27 51.33 REMARK 500 4 MET A 81 155.09 -43.65 REMARK 500 4 LYS A 98 -170.89 -171.21 REMARK 500 4 ASP A 101 74.33 -117.52 REMARK 500 4 TYR A 111 67.46 -175.11 REMARK 500 4 LEU A 113 -94.63 -74.95 REMARK 500 4 ASP A 116 -62.78 -179.80 REMARK 500 4 GLN A 120 -74.47 -106.20 REMARK 500 4 TYR A 121 -179.66 -170.96 REMARK 500 5 ASN A 13 102.04 -52.98 REMARK 500 5 PHE A 31 75.74 -111.79 REMARK 500 5 LYS A 37 69.02 -110.27 REMARK 500 5 ASN A 39 176.96 178.91 REMARK 500 5 LEU A 60 105.50 -45.56 REMARK 500 REMARK 500 THIS ENTRY HAS 226 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 2ABY A 1 122 UNP Q9HK62 Q9HK62_THEAC 1 122 SEQADV 2ABY MET A -21 UNP Q9HK62 CLONING ARTIFACT SEQADV 2ABY GLY A -20 UNP Q9HK62 CLONING ARTIFACT SEQADV 2ABY THR A -19 UNP Q9HK62 CLONING ARTIFACT SEQADV 2ABY SER A -18 UNP Q9HK62 CLONING ARTIFACT SEQADV 2ABY HIS A -17 UNP Q9HK62 CLONING ARTIFACT SEQADV 2ABY HIS A -16 UNP Q9HK62 CLONING ARTIFACT SEQADV 2ABY HIS A -15 UNP Q9HK62 CLONING ARTIFACT SEQADV 2ABY HIS A -14 UNP Q9HK62 CLONING ARTIFACT SEQADV 2ABY HIS A -13 UNP Q9HK62 CLONING ARTIFACT SEQADV 2ABY HIS A -12 UNP Q9HK62 CLONING ARTIFACT SEQADV 2ABY SER A -11 UNP Q9HK62 CLONING ARTIFACT SEQADV 2ABY SER A -10 UNP Q9HK62 CLONING ARTIFACT SEQADV 2ABY GLY A -9 UNP Q9HK62 CLONING ARTIFACT SEQADV 2ABY ARG A -8 UNP Q9HK62 CLONING ARTIFACT SEQADV 2ABY GLU A -7 UNP Q9HK62 CLONING ARTIFACT SEQADV 2ABY ASN A -6 UNP Q9HK62 CLONING ARTIFACT SEQADV 2ABY LEU A -5 UNP Q9HK62 CLONING ARTIFACT SEQADV 2ABY TYR A -4 UNP Q9HK62 CLONING ARTIFACT SEQADV 2ABY PHE A -3 UNP Q9HK62 CLONING ARTIFACT SEQADV 2ABY GLN A -2 UNP Q9HK62 CLONING ARTIFACT SEQADV 2ABY SER A -1 UNP Q9HK62 CLONING ARTIFACT SEQADV 2ABY HIS A 0 UNP Q9HK62 CLONING ARTIFACT SEQADV 2ABY GLY A 123 UNP Q9HK62 CLONING ARTIFACT SEQADV 2ABY SER A 124 UNP Q9HK62 CLONING ARTIFACT SEQRES 1 A 146 MET GLY THR SER HIS HIS HIS HIS HIS HIS SER SER GLY SEQRES 2 A 146 ARG GLU ASN LEU TYR PHE GLN SER HIS MET GLN LYS GLY SEQRES 3 A 146 LEU GLU ILE ALA PHE GLN THR ILE ASN GLY LEU ASP GLU SEQRES 4 A 146 SER LEU VAL GLN ALA LEU ALA GLY VAL THR ALA SER ASP SEQRES 5 A 146 PHE PRO ASP LEU ASP ILE LYS TYR ASN ILE PHE LEU VAL SEQRES 6 A 146 ASP LEU TYR GLY GLN LYS TYR PHE ARG ILE LEU PHE GLN SEQRES 7 A 146 SER LYS LYS LEU SER GLU LEU HIS PRO GLU GLU ARG LYS SEQRES 8 A 146 LYS VAL ARG GLU LYS PHE ASP GLU ASN SER ARG MET GLN SEQRES 9 A 146 TYR SER GLU LEU MET THR LYS TYR HIS ASP LEU LYS LYS SEQRES 10 A 146 GLN GLY LYS ILE LYS ASP ARG PRO VAL LYS GLU VAL HIS SEQRES 11 A 146 GLU GLU TYR ASP LEU TRP GLU ASP PRO ILE TRP GLN TYR SEQRES 12 A 146 ILE GLY SER HELIX 1 1 LEU A 15 PHE A 31 1 17 HELIX 2 2 HIS A 64 MET A 81 1 18 HELIX 3 3 GLN A 82 ASP A 92 1 11 HELIX 4 4 LEU A 93 GLN A 96 5 4 HELIX 5 5 ASP A 116 TYR A 121 1 6 SHEET 1 A 4 ILE A 7 THR A 11 0 SHEET 2 A 4 GLN A 48 GLN A 56 -1 O ILE A 53 N PHE A 9 SHEET 3 A 4 LYS A 37 LEU A 45 -1 N VAL A 43 O TYR A 50 SHEET 4 A 4 LYS A 105 VAL A 107 1 O LYS A 105 N LEU A 42 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 - r 9 2 Bytes