Header list of 1ds9.pdb file
Complete list - b 16 2 Bytes
HEADER CONTRACTILE PROTEIN 07-JAN-00 1DS9 TITLE SOLUTION STRUCTURE OF CHLAMYDOMONAS OUTER ARM DYNEIN LIGHT CHAIN 1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: OUTER ARM DYNEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: LIGHT CHAIN 1; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CHLAMYDOMONAS REINHARDTII; SOURCE 3 ORGANISM_TAXID: 3055; SOURCE 4 ORGAN: FLAGELLAE; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET16B KEYWDS LEUCINE-RICH REPEAT, BETA-BETA-ALPHA CYLINDER, DYNEIN, CHLAMYDOMONAS, KEYWDS 2 FLAGELLA, CONTRACTILE PROTEIN EXPDTA SOLUTION NMR NUMMDL 17 AUTHOR H.W.WU,M.W.MACIEJEWSKI,A.MARINTCHEV,S.E.BENASHSKI,G.P.MULLEN,S.M.KING REVDAT 4 16-FEB-22 1DS9 1 REMARK REVDAT 3 24-FEB-09 1DS9 1 VERSN REVDAT 2 01-APR-03 1DS9 1 JRNL REVDAT 1 26-JUL-00 1DS9 0 JRNL AUTH H.WU,M.W.MACIEJEWSKI,A.MARINTCHEV,S.E.BENASHSKI,G.P.MULLEN, JRNL AUTH 2 S.M.KING JRNL TITL SOLUTION STRUCTURE OF A DYNEIN MOTOR DOMAIN ASSOCIATED LIGHT JRNL TITL 2 CHAIN. JRNL REF NAT.STRUCT.BIOL. V. 7 575 2000 JRNL REFN ISSN 1072-8368 JRNL PMID 10876244 JRNL DOI 10.1038/76804 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH H.WU,M.W.MACIEJEWSKI,S.E.BENASHSKI,G.P.MULLEN,S.M.KING REMARK 1 TITL 1H, 15N AND 13C RESONANCE ASSIGNMENTS FOR THE 22 KDA LC1 REMARK 1 TITL 2 LIGHT CHAIN FROM CHLAMYDOMONAS OUTER ARM DYNEIN REMARK 1 REF J.BIOMOL.NMR V. 13 309 1999 REMARK 1 REFN ISSN 0925-2738 REMARK 1 DOI 10.1023/A:1008340420295 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : FELIX 95, X-PLOR 4.0 REMARK 3 AUTHORS : HARE, BIOSYM (FELIX), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1DS9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JAN-00. REMARK 100 THE DEPOSITION ID IS D_1000010329. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.76 REMARK 210 IONIC STRENGTH : 100 MM NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1 MM LC1 U-15N,13C; 2.5 MM REMARK 210 TRIS.CL PH6.76, 100 MM NACL;; 1 REMARK 210 MM LC1 U-15N,13C; 2.5 MM TRIS.CL REMARK 210 PH6.76, 100 MM NACL; REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C EDITED NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DYANA 1.5, XEASY 1.3.13, VNMR REMARK 210 4.3 REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION REMARK 210 ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 150 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 17 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES REMARK 210 WITH THE LOWEST ENERGY,TARGET REMARK 210 FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 8 REMARK 210 REMARK 210 REMARK: NMR EXPERIMENTAL DATA ARE DESCRIBED IN BIOMAGRESBANK REMARK 210 DEPOSITION #4265 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: 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 -162.12 -79.29 REMARK 500 1 THR A 5 -93.20 -119.55 REMARK 500 1 ARG A 17 -72.93 -94.38 REMARK 500 1 ALA A 22 -79.80 -63.54 REMARK 500 1 GLU A 38 -60.76 -145.19 REMARK 500 1 MET A 40 71.03 -100.31 REMARK 500 1 ALA A 49 43.85 -102.59 REMARK 500 1 LYS A 51 -43.93 -160.83 REMARK 500 1 SER A 56 -67.18 -121.91 REMARK 500 1 ILE A 63 109.41 -160.75 REMARK 500 1 GLU A 86 27.65 -157.66 REMARK 500 1 ASN A 87 -40.85 -160.37 REMARK 500 1 GLU A 96 -49.38 -134.71 REMARK 500 1 ASN A 103 118.30 -160.07 REMARK 500 1 ALA A 106 20.40 -152.49 REMARK 500 1 LEU A 117 -174.98 -51.56 REMARK 500 1 ARG A 118 -79.26 -78.70 REMARK 500 1 ASN A 129 59.50 -98.03 REMARK 500 1 ALA A 137 49.81 -79.67 REMARK 500 1 LYS A 141 -44.77 -160.76 REMARK 500 1 LEU A 142 112.83 -19.54 REMARK 500 1 GLU A 143 -81.39 -54.48 REMARK 500 1 ASN A 150 154.79 176.63 REMARK 500 1 LYS A 157 102.36 172.06 REMARK 500 1 GLU A 158 -72.40 -25.19 REMARK 500 1 LEU A 173 85.84 -23.55 REMARK 500 1 PRO A 174 -78.89 -90.99 REMARK 500 1 LEU A 176 140.36 -33.04 REMARK 500 1 ASP A 180 80.38 62.98 REMARK 500 1 ASP A 185 28.84 44.66 REMARK 500 1 VAL A 186 27.83 46.26 REMARK 500 2 ALA A 2 -159.64 -160.20 REMARK 500 2 THR A 5 -96.61 -106.52 REMARK 500 2 SER A 19 61.17 60.35 REMARK 500 2 VAL A 21 62.34 -115.71 REMARK 500 2 GLU A 38 -65.39 -145.17 REMARK 500 2 MET A 40 53.06 -100.38 REMARK 500 2 ALA A 49 41.54 -102.16 REMARK 500 2 LYS A 51 -49.28 -160.67 REMARK 500 2 SER A 56 -68.35 -134.18 REMARK 500 2 SER A 65 54.70 -100.38 REMARK 500 2 GLU A 70 38.61 -67.41 REMARK 500 2 ASN A 71 9.64 -150.13 REMARK 500 2 ARG A 73 -47.13 -134.26 REMARK 500 2 GLU A 86 -45.19 -158.80 REMARK 500 2 LEU A 95 -174.45 -62.50 REMARK 500 2 GLU A 96 -48.42 -160.61 REMARK 500 2 LEU A 117 176.69 -49.25 REMARK 500 2 ASN A 124 61.10 -156.83 REMARK 500 2 ASN A 129 48.34 -106.80 REMARK 500 REMARK 500 THIS ENTRY HAS 544 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4265 RELATED DB: BMRB REMARK 900 NMR EXPERIMENTAL DATA AND CHEMICAL SHIFT ASSIGNMENTS DBREF 1DS9 A 1 198 UNP Q9XHH2 Q9XHH2_CHLRE 1 198 SEQRES 1 A 198 MET ALA LYS ALA THR THR ILE LYS ASP ALA ILE ARG ILE SEQRES 2 A 198 PHE GLU GLU ARG LYS SER VAL VAL ALA THR GLU ALA GLU SEQRES 3 A 198 LYS VAL GLU LEU HIS GLY MET ILE PRO PRO ILE GLU LYS SEQRES 4 A 198 MET ASP ALA THR LEU SER THR LEU LYS ALA CYS LYS HIS SEQRES 5 A 198 LEU ALA LEU SER THR ASN ASN ILE GLU LYS ILE SER SER SEQRES 6 A 198 LEU SER GLY MET GLU ASN LEU ARG ILE LEU SER LEU GLY SEQRES 7 A 198 ARG ASN LEU ILE LYS LYS ILE GLU ASN LEU ASP ALA VAL SEQRES 8 A 198 ALA ASP THR LEU GLU GLU LEU TRP ILE SER TYR ASN GLN SEQRES 9 A 198 ILE ALA SER LEU SER GLY ILE GLU LYS LEU VAL ASN LEU SEQRES 10 A 198 ARG VAL LEU TYR MET SER ASN ASN LYS ILE THR ASN TRP SEQRES 11 A 198 GLY GLU ILE ASP LYS LEU ALA ALA LEU ASP LYS LEU GLU SEQRES 12 A 198 ASP LEU LEU LEU ALA GLY ASN PRO LEU TYR ASN ASP TYR SEQRES 13 A 198 LYS GLU ASN ASN ALA THR SER GLU TYR ARG ILE GLU VAL SEQRES 14 A 198 VAL LYS ARG LEU PRO ASN LEU LYS LYS LEU ASP GLY MET SEQRES 15 A 198 PRO VAL ASP VAL ASP GLU ARG GLU GLN ALA ASN VAL ALA SEQRES 16 A 198 ARG GLY GLY HELIX 1 1 THR A 6 ARG A 17 1 12 HELIX 2 2 MET A 40 LEU A 47 1 8 HELIX 3 3 SER A 65 GLU A 70 1 6 HELIX 4 4 ASN A 87 LEU A 95 1 9 HELIX 5 5 SER A 107 LEU A 117 1 11 HELIX 6 6 ASN A 129 ALA A 137 1 9 HELIX 7 7 ASN A 150 GLU A 158 1 9 HELIX 8 8 ALA A 161 LEU A 173 1 13 HELIX 9 9 GLY A 181 ASP A 185 5 5 HELIX 10 10 GLU A 190 GLY A 197 1 8 SHEET 1 A 7 ILE A 74 ILE A 82 0 SHEET 2 A 7 THR A 57 ILE A 60 1 O ASN A 58 N LEU A 81 SHEET 3 A 7 ILE A 74 ILE A 82 1 O ILE A 74 N LEU A 53 SHEET 4 A 7 GLU A 97 GLN A 104 1 O GLU A 97 N LEU A 75 SHEET 5 A 7 VAL A 119 MET A 122 1 O VAL A 119 N LEU A 98 SHEET 6 A 7 ASP A 144 LEU A 147 1 O ASP A 144 N LEU A 120 SHEET 7 A 7 LYS A 178 LEU A 179 1 O LYS A 178 N LEU A 145 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 16 2 Bytes