Header list of 1x9a.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 20-AUG-04 1X9A TITLE SOLUTION NMR STRUCTURE OF PROTEIN TM0979 FROM THERMOTOGA MARITIMA. TITLE 2 ONTARIO CENTER FOR STRUCTURAL PROTEOMICS TARGET TM0979_1_87; TITLE 3 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET VT98. COMPND MOL_ID: 1; COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN TM0979; COMPND 3 CHAIN: A, B SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA; SOURCE 3 ORGANISM_TAXID: 2336 KEYWDS STRUCTURAL GENOMICS, PROTEIN STRUCTURE INITIATIVE, PSI, NORTHEAST KEYWDS 2 STRUCTURAL GENOMICS CONSORTIUM, NESG, OCSP, HYPOTHETICAL PROTEIN, KEYWDS 3 BETA-ALPHA PROTEIN, DIMER, UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR J.A.GASPAR,C.LIU,K.A.VASSALL,P.B.STATHOPULOS,G.MEGLEI,R.STEPHEN, AUTHOR 2 A.PINEDA-LUCENA,B.WU,A.YEE,C.H.ARROWSMITH,E.M.MEIERING,NORTHEAST AUTHOR 3 STRUCTURAL GENOMICS CONSORTIUM (NESG) REVDAT 4 02-MAR-22 1X9A 1 REMARK SEQADV REVDAT 3 24-FEB-09 1X9A 1 VERSN REVDAT 2 25-JAN-05 1X9A 1 JRNL REVDAT 1 07-DEC-04 1X9A 0 JRNL AUTH J.A.GASPAR,C.LIU,K.A.VASSALL,G.MEGLEI,R.STEPHEN, JRNL AUTH 2 P.B.STATHOPULOS,A.PINEDA-LUCENA,B.WU,A.YEE,C.H.ARROWSMITH, JRNL AUTH 3 E.M.MEIERING JRNL TITL A NOVEL MEMBER OF THE YCHN-LIKE FOLD: SOLUTION STRUCTURE OF JRNL TITL 2 THE HYPOTHETICAL PROTEIN TM0979 FROM THERMOTOGA MARITIMA. JRNL REF PROTEIN SCI. V. 14 216 2005 JRNL REFN ISSN 0961-8368 JRNL PMID 15608123 JRNL DOI 10.1110/PS.041068605 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA, CNS REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE, REMARK 3 SIMONSON,WARREN (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1X9A COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-AUG-04. REMARK 100 THE DEPOSITION ID IS D_1000030100. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 300 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1MM 15N, 13C PROTEIN, 25MM REMARK 210 SODIUM PHOSPHATE PH 6.5, 450MM REMARK 210 NACL, 0.01% SODIUM AZIDE, 5% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED REMARK 210 ANNEALING, MOLECULAR DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 20 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 9 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 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 1-10 REMARK 465 RES C SSSEQI REMARK 465 MET A -19 REMARK 465 GLY A -18 REMARK 465 SER A -17 REMARK 465 SER A -16 REMARK 465 HIS A -15 REMARK 465 HIS A -14 REMARK 465 HIS A -13 REMARK 465 HIS A -12 REMARK 465 HIS A -11 REMARK 465 HIS A -10 REMARK 465 SER A -9 REMARK 465 SER A -8 REMARK 465 GLY A -7 REMARK 465 LEU A -6 REMARK 465 VAL A -5 REMARK 465 PRO A -4 REMARK 465 ARG A -3 REMARK 465 GLY A -2 REMARK 465 SER A -1 REMARK 465 HIS A 0 REMARK 465 MET B 181 REMARK 465 GLY B 182 REMARK 465 SER B 183 REMARK 465 SER B 184 REMARK 465 HIS B 185 REMARK 465 HIS B 186 REMARK 465 HIS B 187 REMARK 465 HIS B 188 REMARK 465 HIS B 189 REMARK 465 HIS B 190 REMARK 465 SER B 191 REMARK 465 SER B 192 REMARK 465 GLY B 193 REMARK 465 LEU B 194 REMARK 465 VAL B 195 REMARK 465 PRO B 196 REMARK 465 ARG B 197 REMARK 465 GLY B 198 REMARK 465 SER B 199 REMARK 465 HIS B 200 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 OE2 GLU A 41 HZ2 LYS A 66 1.56 REMARK 500 OE1 GLU A 80 HZ1 LYS A 84 1.58 REMARK 500 H MET B 201 OD1 ASP B 226 1.59 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 LYS A 7 62.98 -151.59 REMARK 500 1 TYR A 8 39.77 -148.73 REMARK 500 1 GLN A 32 -125.84 67.30 REMARK 500 1 GLU A 82 -33.94 171.73 REMARK 500 1 LYS A 84 91.51 34.09 REMARK 500 1 PHE A 85 70.52 -102.14 REMARK 500 1 THR B 210 -49.13 64.20 REMARK 500 1 GLN B 232 -118.97 66.44 REMARK 500 1 LEU B 242 103.77 61.50 REMARK 500 1 ASP B 264 51.27 -90.47 REMARK 500 1 GLU B 282 -90.62 -100.40 REMARK 500 1 GLU B 283 -46.30 -169.52 REMARK 500 1 LYS B 284 -140.62 51.19 REMARK 500 2 HIS A 12 86.66 -164.11 REMARK 500 2 GLN A 32 -114.18 64.37 REMARK 500 2 GLU A 41 30.46 -81.97 REMARK 500 2 GLU A 82 -63.68 174.82 REMARK 500 2 LYS A 84 167.78 57.46 REMARK 500 2 TYR B 208 -78.57 -124.13 REMARK 500 2 ASP B 211 -65.01 -98.14 REMARK 500 2 PRO B 213 -19.46 -47.99 REMARK 500 2 GLN B 232 -102.45 59.11 REMARK 500 2 LEU B 242 107.73 65.38 REMARK 500 2 GLU B 283 -32.49 -172.73 REMARK 500 2 ILE B 286 118.86 71.68 REMARK 500 3 ALA A 2 -67.37 176.62 REMARK 500 3 LYS A 7 61.56 -150.56 REMARK 500 3 GLN A 32 -136.40 67.13 REMARK 500 3 GLU A 40 -80.14 -79.95 REMARK 500 3 GLU A 41 -26.21 166.40 REMARK 500 3 LEU A 42 120.56 -37.72 REMARK 500 3 TYR A 60 -165.68 -77.46 REMARK 500 3 GLU A 82 -64.26 73.33 REMARK 500 3 LYS A 84 149.53 70.42 REMARK 500 3 ILE A 86 89.02 -68.27 REMARK 500 3 LYS B 223 -168.80 -109.98 REMARK 500 3 GLN B 232 -109.73 58.65 REMARK 500 3 GLU B 241 -73.56 -60.25 REMARK 500 3 LEU B 242 78.23 50.55 REMARK 500 3 GLU B 283 -38.40 -155.68 REMARK 500 4 ALA A 2 -66.84 -148.37 REMARK 500 4 GLN A 32 -117.87 68.48 REMARK 500 4 GLU A 82 -41.79 70.19 REMARK 500 4 LYS A 84 101.86 44.51 REMARK 500 4 TYR B 208 -55.56 -145.72 REMARK 500 4 THR B 210 14.99 56.74 REMARK 500 4 SER B 221 76.97 -113.08 REMARK 500 4 GLN B 232 -129.66 64.43 REMARK 500 4 GLU B 240 -86.09 -72.36 REMARK 500 4 GLU B 241 -74.69 177.45 REMARK 500 REMARK 500 THIS ENTRY HAS 125 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: VT98 RELATED DB: TARGETDB DBREF 1X9A A 1 87 UNP Q9X074 Q9X074_THEMA 1 87 DBREF 1X9A B 201 287 UNP Q9X074 Q9X074_THEMA 1 87 SEQADV 1X9A MET A -19 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A GLY A -18 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A SER A -17 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A SER A -16 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A HIS A -15 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A HIS A -14 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A HIS A -13 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A HIS A -12 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A HIS A -11 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A HIS A -10 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A SER A -9 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A SER A -8 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A GLY A -7 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A LEU A -6 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A VAL A -5 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A PRO A -4 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A ARG A -3 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A GLY A -2 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A SER A -1 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A HIS A 0 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A MET B 181 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A GLY B 182 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A SER B 183 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A SER B 184 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A HIS B 185 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A HIS B 186 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A HIS B 187 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A HIS B 188 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A HIS B 189 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A HIS B 190 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A SER B 191 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A SER B 192 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A GLY B 193 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A LEU B 194 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A VAL B 195 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A PRO B 196 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A ARG B 197 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A GLY B 198 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A SER B 199 UNP Q9X074 EXPRESSION TAG SEQADV 1X9A HIS B 200 UNP Q9X074 EXPRESSION TAG SEQRES 1 A 107 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY SEQRES 2 A 107 LEU VAL PRO ARG GLY SER HIS MET ALA LEU VAL LEU VAL SEQRES 3 A 107 LYS TYR GLY THR ASP HIS PRO VAL GLU LYS LEU LYS ILE SEQRES 4 A 107 ARG SER ALA LYS ALA GLU ASP LYS ILE VAL LEU ILE GLN SEQRES 5 A 107 ASN GLY VAL PHE TRP ALA LEU GLU GLU LEU GLU THR PRO SEQRES 6 A 107 ALA LYS VAL TYR ALA ILE LYS ASP ASP PHE LEU ALA ARG SEQRES 7 A 107 GLY TYR SER GLU GLU ASP SER LYS VAL PRO LEU ILE THR SEQRES 8 A 107 TYR SER GLU PHE ILE ASP LEU LEU GLU GLY GLU GLU LYS SEQRES 9 A 107 PHE ILE GLY SEQRES 1 B 107 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY SEQRES 2 B 107 LEU VAL PRO ARG GLY SER HIS MET ALA LEU VAL LEU VAL SEQRES 3 B 107 LYS TYR GLY THR ASP HIS PRO VAL GLU LYS LEU LYS ILE SEQRES 4 B 107 ARG SER ALA LYS ALA GLU ASP LYS ILE VAL LEU ILE GLN SEQRES 5 B 107 ASN GLY VAL PHE TRP ALA LEU GLU GLU LEU GLU THR PRO SEQRES 6 B 107 ALA LYS VAL TYR ALA ILE LYS ASP ASP PHE LEU ALA ARG SEQRES 7 B 107 GLY TYR SER GLU GLU ASP SER LYS VAL PRO LEU ILE THR SEQRES 8 B 107 TYR SER GLU PHE ILE ASP LEU LEU GLU GLY GLU GLU LYS SEQRES 9 B 107 PHE ILE GLY HELIX 1 1 PRO A 13 SER A 21 1 9 HELIX 2 2 GLN A 32 GLU A 40 5 9 HELIX 3 3 LYS A 52 ARG A 58 1 7 HELIX 4 4 SER A 61 SER A 65 5 5 HELIX 5 5 THR A 71 GLY A 81 1 11 HELIX 6 6 VAL B 214 ALA B 222 1 9 HELIX 7 7 GLN B 232 GLU B 240 5 9 HELIX 8 8 LYS B 252 ARG B 258 1 7 HELIX 9 9 THR B 271 GLY B 281 1 11 SHEET 1 A 4 LEU A 3 VAL A 6 0 SHEET 2 A 4 LYS A 27 LEU A 30 1 O LYS A 27 N VAL A 4 SHEET 3 A 4 LYS A 47 ILE A 51 1 O LYS A 47 N ILE A 28 SHEET 4 A 4 LEU A 69 ILE A 70 1 O ILE A 70 N ALA A 50 SHEET 1 B 4 LEU B 203 VAL B 206 0 SHEET 2 B 4 LYS B 227 LEU B 230 1 O LYS B 227 N VAL B 204 SHEET 3 B 4 LYS B 247 ILE B 251 1 O LYS B 247 N ILE B 228 SHEET 4 B 4 LEU B 269 ILE B 270 1 O ILE B 270 N ALA B 250 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 2 2 Bytes