Header list of 1t4n.pdb file
Complete list - v 3 2 Bytes
HEADER HYDROLASE 30-APR-04 1T4N TITLE SOLUTION STRUCTURE OF RNT1P DSRBD COMPND MOL_ID: 1; COMPND 2 MOLECULE: RIBONUCLEASE III; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: DSRBD; COMPND 5 SYNONYM: RNASE III, RNT1P; COMPND 6 EC: 3.1.26.3; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE; SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST; SOURCE 4 ORGANISM_TAXID: 4932; SOURCE 5 GENE: RNT1, YMR239C, YM9408.01C, YM9959.21; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS DSRBD, RNA-BINDING, HYDROLASE EXPDTA SOLUTION NMR NUMMDL 51 AUTHOR N.LEULLIOT,S.QUEVILLON-CHERUEL,M.GRAILLE,H.VAN TILBEURGH,T.C.LEEPER, AUTHOR 2 K.S.GODIN,T.E.EDWARDS,S.T.SIGURDSSON,N.ROZENKRANTS,R.J.NAGEL,M.ARES, AUTHOR 3 G.VARANI REVDAT 4 03-NOV-21 1T4N 1 REMARK SEQADV REVDAT 3 24-FEB-09 1T4N 1 VERSN REVDAT 2 17-AUG-04 1T4N 1 JRNL REVDAT 1 13-JUL-04 1T4N 0 JRNL AUTH N.LEULLIOT,S.QUEVILLON-CHERUEL,M.GRAILLE,H.VAN TILBEURGH, JRNL AUTH 2 T.C.LEEPER,K.S.GODIN,T.E.EDWARDS,S.T.SIGURDSSON, JRNL AUTH 3 N.ROZENKRANTS,R.J.NAGEL,M.ARES,G.VARANI JRNL TITL A NEW ALPHA-HELICAL EXTENSION PROMOTES RNA BINDING BY THE JRNL TITL 2 DSRBD OF RNT1P RNASE III JRNL REF EMBO J. V. 23 2468 2004 JRNL REFN ISSN 0261-4189 JRNL PMID 15192703 JRNL DOI 10.1038/SJ.EMBOJ.7600260 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: NULL REMARK 4 REMARK 4 1T4N COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAY-04. REMARK 100 THE DEPOSITION ID IS D_1000022306. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 310 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 50MM NACL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE; AVANCE DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : SPARKY, CNS REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 51 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 51 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE REMARK 210 COVALENT GEOMETRY 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 1-51 REMARK 465 RES C SSSEQI REMARK 465 HIS A 451 REMARK 465 HIS A 452 REMARK 465 HIS A 453 REMARK 465 HIS A 454 REMARK 465 HIS A 455 REMARK 465 HIS A 456 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 TYR A 441 H ARG A 445 1.55 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 365 -41.87 -171.17 REMARK 500 1 MET A 368 -71.36 -50.30 REMARK 500 1 ILE A 378 -34.08 -137.18 REMARK 500 1 ALA A 381 -69.13 175.28 REMARK 500 1 ARG A 384 80.79 -63.98 REMARK 500 1 LYS A 391 -80.70 -48.27 REMARK 500 1 LYS A 392 61.70 66.31 REMARK 500 1 THR A 394 -84.65 -162.89 REMARK 500 1 ALA A 395 -48.38 -134.43 REMARK 500 1 ASP A 408 -75.69 -60.43 REMARK 500 1 ASP A 434 82.04 -63.46 REMARK 500 2 LYS A 365 -42.74 -174.83 REMARK 500 2 MET A 368 -91.23 26.91 REMARK 500 2 TYR A 380 50.67 -117.47 REMARK 500 2 ALA A 381 -71.55 77.97 REMARK 500 2 ARG A 384 70.49 -68.51 REMARK 500 2 LEU A 385 102.72 -57.60 REMARK 500 2 LYS A 391 172.82 -47.02 REMARK 500 2 LYS A 392 72.96 179.40 REMARK 500 2 THR A 394 -39.93 172.44 REMARK 500 2 ALA A 395 -33.54 173.17 REMARK 500 2 ASP A 408 -40.25 -177.87 REMARK 500 2 ASP A 434 78.38 -65.21 REMARK 500 2 ALA A 448 -71.50 -59.32 REMARK 500 3 LYS A 365 131.97 -178.39 REMARK 500 3 ALA A 381 -72.75 179.73 REMARK 500 3 ARG A 384 80.84 -63.29 REMARK 500 3 LYS A 391 -91.63 33.74 REMARK 500 3 LYS A 392 61.02 66.35 REMARK 500 3 THR A 394 -45.41 -159.06 REMARK 500 3 ALA A 395 -40.45 -172.14 REMARK 500 3 ASP A 408 -0.07 78.32 REMARK 500 3 ASP A 434 85.99 -59.58 REMARK 500 3 LEU A 449 -53.91 -129.54 REMARK 500 4 LYS A 365 -29.31 90.32 REMARK 500 4 LEU A 366 32.25 -96.51 REMARK 500 4 ASP A 367 67.97 67.07 REMARK 500 4 MET A 368 59.16 -68.00 REMARK 500 4 ASN A 369 -71.37 177.33 REMARK 500 4 ALA A 381 -62.93 71.65 REMARK 500 4 ARG A 384 79.99 -64.64 REMARK 500 4 LYS A 392 144.58 -172.18 REMARK 500 4 THR A 394 -61.44 -158.25 REMARK 500 4 ALA A 395 -40.81 -173.65 REMARK 500 4 ASP A 434 80.74 -65.18 REMARK 500 5 ASN A 369 -75.98 -82.42 REMARK 500 5 ILE A 378 -34.33 -149.91 REMARK 500 5 ALA A 381 -74.25 179.42 REMARK 500 5 ARG A 384 76.81 -66.64 REMARK 500 5 LEU A 385 99.91 -57.15 REMARK 500 REMARK 500 THIS ENTRY HAS 576 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1T4O RELATED DB: PDB REMARK 900 SAME PROTEIN SOLVED BY X-RAY CRYSTALLOGRAPHY DBREF 1T4N A 364 447 UNP Q02555 RNT1_YEAST 364 447 SEQADV 1T4N MET A 363 UNP Q02555 INITIATING METHIONINE SEQADV 1T4N ALA A 448 UNP Q02555 EXPRESSION TAG SEQADV 1T4N LEU A 449 UNP Q02555 EXPRESSION TAG SEQADV 1T4N GLY A 450 UNP Q02555 EXPRESSION TAG SEQADV 1T4N HIS A 451 UNP Q02555 EXPRESSION TAG SEQADV 1T4N HIS A 452 UNP Q02555 EXPRESSION TAG SEQADV 1T4N HIS A 453 UNP Q02555 EXPRESSION TAG SEQADV 1T4N HIS A 454 UNP Q02555 EXPRESSION TAG SEQADV 1T4N HIS A 455 UNP Q02555 EXPRESSION TAG SEQADV 1T4N HIS A 456 UNP Q02555 EXPRESSION TAG SEQRES 1 A 94 MET ASP LYS LEU ASP MET ASN ALA LYS ARG GLN LEU TYR SEQRES 2 A 94 SER LEU ILE GLY TYR ALA SER LEU ARG LEU HIS TYR VAL SEQRES 3 A 94 THR VAL LYS LYS PRO THR ALA VAL ASP PRO ASN SER ILE SEQRES 4 A 94 VAL GLU CYS ARG VAL GLY ASP GLY THR VAL LEU GLY THR SEQRES 5 A 94 GLY VAL GLY ARG ASN ILE LYS ILE ALA GLY ILE ARG ALA SEQRES 6 A 94 ALA GLU ASN ALA LEU ARG ASP LYS LYS MET LEU ASP PHE SEQRES 7 A 94 TYR ALA LYS GLN ARG ALA ALA ALA LEU GLY HIS HIS HIS SEQRES 8 A 94 HIS HIS HIS HELIX 1 1 ASP A 367 ILE A 378 1 12 HELIX 2 2 ASN A 419 ASP A 434 1 16 HELIX 3 3 ASP A 434 GLY A 450 1 17 SHEET 1 A 3 HIS A 386 THR A 389 0 SHEET 2 A 3 SER A 400 ARG A 405 -1 O ARG A 405 N HIS A 386 SHEET 3 A 3 VAL A 411 GLY A 417 -1 O GLY A 417 N SER A 400 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 - v 3 2 Bytes