Header list of 1uta.pdb file
Complete list - n 24 2 Bytes
HEADER CELL DIVISION 04-DEC-03 1UTA TITLE SOLUTION STRUCTURE OF THE C-TERMINAL RNP DOMAIN FROM THE DIVISOME TITLE 2 PROTEIN FTSN COMPND MOL_ID: 1; COMPND 2 MOLECULE: CELL DIVISION PROTEIN FTSN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RNP DOMAIN, RESIDUES 239-319; COMPND 5 SYNONYM: FTSN, MSGA; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 562; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 6 EXPRESSION_SYSTEM_VARIANT: C41; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PHIS17 KEYWDS BACTERIAL CELL DIVISION PROTEIN, RNP DOMAIN, CELL DIVISION, KEYWDS 2 TRANSMEMBRANE, INNER MEMBRANE EXPDTA SOLUTION NMR NUMMDL 45 AUTHOR J.-C.YANG,F.VAN DEN ENT,D.NEUHAUS,J.BREVIER,J.LOWE REVDAT 3 24-JAN-18 1UTA 1 SOURCE AUTHOR JRNL REVDAT 2 24-FEB-09 1UTA 1 VERSN REVDAT 1 24-SEP-04 1UTA 0 JRNL AUTH J.-C.YANG,F.VAN DEN ENT,D.NEUHAUS,J.BREVIER,J.LOWE JRNL TITL SOLUTION STRUCTURE AND DOMAIN ARCHITECTURE OF THE DIVISOME JRNL TITL 2 PROTEIN FTSN JRNL REF MOL.MICROBIOL. V. 52 651 2004 JRNL REFN ISSN 0950-382X JRNL PMID 15101973 JRNL DOI 10.1111/J.1365-2958.2004.03991.X 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: AS DESCRIBED IN CITATION REMARK 4 REMARK 4 1UTA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-DEC-03. REMARK 100 THE DEPOSITION ID IS D_1290014112. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 300 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D (1H; 1H) NOESY; 1H) TOCSY; REMARK 210 1H) DQF-COSY; 2D 15N-HSQC; 3D REMARK 210 15N NOESY-HSQC; 3D 15N TOCSY- REMARK 210 HSQC; 3D 15N-HSQC-NOESY-HSQC REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE; DMX; DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : CNS REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 45 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOW NOE ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING 15N LABELLED PROTEIN REMARK 210 AND STANDARD PROTOCOLS 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 400 REMARK 400 COMPOUND REMARK 400 FUNCTION: ESSENTIAL CELL DIVISION PROTEIN. 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 1-45 REMARK 465 RES C SSSEQI REMARK 465 PHE A 239 REMARK 465 THR A 240 REMARK 465 SER A 241 REMARK 465 ASN A 242 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 O GLY A 257 H ALA A 261 1.39 REMARK 500 H LYS A 276 O VAL A 287 1.54 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 ASP A 244 114.14 61.45 REMARK 500 1 GLU A 245 30.85 -98.73 REMARK 500 1 ARG A 246 128.85 63.16 REMARK 500 1 MET A 249 70.32 -165.20 REMARK 500 1 VAL A 250 154.15 -41.14 REMARK 500 1 GLN A 251 77.70 -151.37 REMARK 500 1 ALA A 258 -36.50 -37.59 REMARK 500 1 ASP A 274 91.01 -51.72 REMARK 500 1 THR A 278 122.68 177.38 REMARK 500 1 ASN A 280 -50.95 -177.17 REMARK 500 1 ASN A 284 92.63 -59.50 REMARK 500 1 PRO A 290 100.81 -39.92 REMARK 500 1 LYS A 294 -50.93 -178.69 REMARK 500 1 GLU A 295 -31.13 -172.78 REMARK 500 1 ASN A 311 111.25 93.80 REMARK 500 2 GLU A 245 49.56 -168.96 REMARK 500 2 ARG A 247 172.37 50.06 REMARK 500 2 MET A 249 75.05 -163.14 REMARK 500 2 VAL A 250 155.60 -44.88 REMARK 500 2 GLN A 251 68.36 -155.99 REMARK 500 2 ALA A 258 -35.69 -38.45 REMARK 500 2 PHE A 273 90.85 -161.90 REMARK 500 2 THR A 278 124.05 -179.94 REMARK 500 2 ASN A 280 -54.93 -175.94 REMARK 500 2 ASN A 284 99.95 -60.79 REMARK 500 2 ILE A 288 67.55 -111.98 REMARK 500 2 LYS A 294 -55.85 76.63 REMARK 500 2 ASN A 311 106.56 168.90 REMARK 500 2 ALA A 317 176.25 -58.37 REMARK 500 3 GLU A 245 63.33 -153.92 REMARK 500 3 MET A 249 74.39 -161.73 REMARK 500 3 VAL A 250 150.89 -43.30 REMARK 500 3 GLN A 251 53.83 -145.47 REMARK 500 3 CYS A 252 52.39 -97.24 REMARK 500 3 SER A 254 72.07 71.37 REMARK 500 3 PHE A 273 74.38 -151.75 REMARK 500 3 THR A 278 121.84 172.40 REMARK 500 3 ASN A 280 -56.97 -168.08 REMARK 500 3 ASN A 284 106.55 -52.71 REMARK 500 3 PRO A 290 97.17 -42.13 REMARK 500 3 LYS A 294 -56.03 77.01 REMARK 500 3 ASN A 311 106.42 81.73 REMARK 500 3 ILE A 313 116.97 -164.28 REMARK 500 4 GLU A 245 30.82 -151.91 REMARK 500 4 MET A 249 77.81 -154.46 REMARK 500 4 ALA A 258 -35.11 -37.70 REMARK 500 4 PHE A 273 91.25 -162.95 REMARK 500 4 THR A 278 121.01 -173.14 REMARK 500 4 ASN A 280 127.38 -176.87 REMARK 500 4 PRO A 290 95.71 -46.30 REMARK 500 REMARK 500 THIS ENTRY HAS 639 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1UTA A 239 319 UNP P29131 FTSN_ECOLI 239 319 SEQRES 1 A 81 PHE THR SER ASN LYS ASP GLU ARG ARG TRP MET VAL GLN SEQRES 2 A 81 CYS GLY SER PHE ARG GLY ALA GLU GLN ALA GLU THR VAL SEQRES 3 A 81 ARG ALA GLN LEU ALA PHE GLU GLY PHE ASP SER LYS ILE SEQRES 4 A 81 THR THR ASN ASN GLY TRP ASN ARG VAL VAL ILE GLY PRO SEQRES 5 A 81 VAL LYS GLY LYS GLU ASN ALA ASP SER THR LEU ASN ARG SEQRES 6 A 81 LEU LYS MET ALA GLY HIS THR ASN CYS ILE ARG LEU ALA SEQRES 7 A 81 ALA GLY GLY HELIX 1 1 GLY A 257 GLY A 272 1 16 HELIX 2 2 GLU A 295 GLY A 308 1 14 SHEET 1 AA 3 SER A 254 PHE A 255 0 SHEET 2 AA 3 ASN A 284 ILE A 288 -1 O ASN A 284 N PHE A 255 SHEET 3 AA 3 SER A 275 THR A 279 -1 O LYS A 276 N VAL A 287 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 - n 24 2 Bytes