Header list of 1whx.pdb file
Complete list - r 2 2 Bytes
HEADER RNA BINDING PROTEIN 28-MAY-04 1WHX TITLE SOLUTION STRUCTURE OF THE SECOND RNA BINDING DOMAIN FROM HYPOTHETICAL TITLE 2 PROTEIN BAB23448 COMPND MOL_ID: 1; COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN RIKEN CDNA 1200009A02; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RNA RECOGNITION MOTIF; COMPND 5 SYNONYM: HYPOTHETICAL PROTEIN BAB23448; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 GENE: RIKEN CDNA 1200009A02; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P030811-91; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS RNA RECOGNITION MOTIF, RRM, RNA BINDING DOMAIN, RBD, RNP, STRUCTURAL KEYWDS 2 GENOMICS, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, RNA KEYWDS 3 BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR T.NAGATA,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,S.YOKOYAMA,RIKEN AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 02-MAR-22 1WHX 1 REMARK SEQADV REVDAT 2 24-FEB-09 1WHX 1 VERSN REVDAT 1 28-NOV-04 1WHX 0 JRNL AUTH T.NAGATA,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU, JRNL AUTH 2 S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE SECOND RNA BINDING DOMAIN FROM JRNL TITL 2 HYPOTHETICAL PROTEIN BAB23448 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRVIEW 5.0.4, CYANA 2.0 REMARK 3 AUTHORS : JOHNSON (NMRVIEW), GUENTERT (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1WHX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-JUN-04. REMARK 100 THE DEPOSITION ID IS D_1000023596. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : 100MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.08MM PROTEIN U-15N, 13C; 20MM REMARK 210 PHOSPHATE BUFFER NA; 100MM NACL; REMARK 210 1MM DTT; 0.02% NAN3; 90% H2O; 10% REMARK 210 D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : CYANA 2.0, NMRPIPE 2.3, KUJIRA REMARK 210 0.901 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS, REMARK 210 SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR REMARK 210 SPECTROSCOPY. 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 ASN A 228 52.91 70.75 REMARK 500 1 HIS A 276 -70.98 -57.28 REMARK 500 1 PHE A 282 -73.74 -69.63 REMARK 500 1 HIS A 283 -71.76 -110.41 REMARK 500 1 GLU A 309 151.45 -44.12 REMARK 500 1 SER A 317 120.61 -38.55 REMARK 500 1 PRO A 319 -178.86 -69.78 REMARK 500 2 SER A 213 -60.28 -101.70 REMARK 500 2 ASN A 228 52.85 72.65 REMARK 500 2 HIS A 283 -75.53 -123.94 REMARK 500 2 PHE A 297 -62.72 -96.06 REMARK 500 2 PRO A 301 -175.59 -69.79 REMARK 500 2 GLN A 302 45.95 -109.68 REMARK 500 2 GLU A 309 119.94 -34.69 REMARK 500 2 PRO A 319 -174.71 -69.76 REMARK 500 3 SER A 214 -66.63 -95.79 REMARK 500 3 ASN A 228 53.97 74.33 REMARK 500 3 THR A 233 155.67 -46.62 REMARK 500 3 PHE A 282 -74.96 -69.84 REMARK 500 3 HIS A 283 -70.17 -116.02 REMARK 500 3 TRP A 291 150.87 -37.48 REMARK 500 3 PRO A 293 -174.87 -69.71 REMARK 500 3 PRO A 301 -172.43 -69.77 REMARK 500 3 GLN A 302 74.54 -115.22 REMARK 500 3 GLN A 307 -31.61 -38.89 REMARK 500 3 SER A 317 43.79 34.49 REMARK 500 3 PRO A 319 -175.03 -69.78 REMARK 500 4 THR A 241 -38.97 -39.54 REMARK 500 4 PHE A 282 -73.34 -78.72 REMARK 500 4 HIS A 283 -71.99 -118.29 REMARK 500 4 TRP A 291 150.79 -49.49 REMARK 500 4 GLU A 309 127.28 -36.03 REMARK 500 4 SER A 317 103.89 -44.04 REMARK 500 4 SER A 321 147.42 -34.91 REMARK 500 5 PHE A 282 -72.25 -70.55 REMARK 500 5 HIS A 283 -74.92 -112.78 REMARK 500 5 PRO A 301 -169.19 -69.78 REMARK 500 5 HIS A 308 -32.94 -39.92 REMARK 500 5 GLU A 309 123.24 -38.63 REMARK 500 5 GLN A 310 96.96 -33.96 REMARK 500 5 SER A 317 124.52 -34.88 REMARK 500 6 SER A 220 154.32 -44.57 REMARK 500 6 THR A 233 163.41 -44.70 REMARK 500 6 ALA A 235 -36.78 -37.59 REMARK 500 6 HIS A 276 -72.10 -63.13 REMARK 500 6 TYR A 279 32.30 70.83 REMARK 500 6 PHE A 282 -72.67 -78.55 REMARK 500 6 HIS A 283 -73.05 -108.46 REMARK 500 6 TRP A 291 146.32 -38.82 REMARK 500 6 PRO A 293 -174.63 -69.75 REMARK 500 REMARK 500 THIS ENTRY HAS 188 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: MMT007011210.1 RELATED DB: TARGETDB DBREF 1WHX A 219 316 UNP Q8R3C6 RBM19_MOUSE 219 316 SEQADV 1WHX GLY A 212 UNP Q8R3C6 CLONING ARTIFACT SEQADV 1WHX SER A 213 UNP Q8R3C6 CLONING ARTIFACT SEQADV 1WHX SER A 214 UNP Q8R3C6 CLONING ARTIFACT SEQADV 1WHX GLY A 215 UNP Q8R3C6 CLONING ARTIFACT SEQADV 1WHX SER A 216 UNP Q8R3C6 CLONING ARTIFACT SEQADV 1WHX SER A 217 UNP Q8R3C6 CLONING ARTIFACT SEQADV 1WHX GLY A 218 UNP Q8R3C6 CLONING ARTIFACT SEQADV 1WHX SER A 317 UNP Q8R3C6 CLONING ARTIFACT SEQADV 1WHX GLY A 318 UNP Q8R3C6 CLONING ARTIFACT SEQADV 1WHX PRO A 319 UNP Q8R3C6 CLONING ARTIFACT SEQADV 1WHX SER A 320 UNP Q8R3C6 CLONING ARTIFACT SEQADV 1WHX SER A 321 UNP Q8R3C6 CLONING ARTIFACT SEQADV 1WHX GLY A 322 UNP Q8R3C6 CLONING ARTIFACT SEQRES 1 A 111 GLY SER SER GLY SER SER GLY ARG SER LYS THR VAL ILE SEQRES 2 A 111 LEU ALA LYS ASN LEU PRO ALA GLY THR LEU ALA ALA GLU SEQRES 3 A 111 ILE GLN GLU THR PHE SER ARG PHE GLY SER LEU GLY ARG SEQRES 4 A 111 VAL LEU LEU PRO GLU GLY GLY ILE THR ALA ILE VAL GLU SEQRES 5 A 111 PHE LEU GLU PRO LEU GLU ALA ARG LYS ALA PHE ARG HIS SEQRES 6 A 111 LEU ALA TYR SER LYS PHE HIS HIS VAL PRO LEU TYR LEU SEQRES 7 A 111 GLU TRP ALA PRO ILE GLY VAL PHE GLY ALA ALA PRO GLN SEQRES 8 A 111 LYS LYS ASP SER GLN HIS GLU GLN PRO ALA GLU LYS ALA SEQRES 9 A 111 GLU SER GLY PRO SER SER GLY HELIX 1 1 ALA A 235 SER A 243 1 9 HELIX 2 2 PRO A 267 LEU A 277 1 11 SHEET 1 A 4 LEU A 248 LEU A 252 0 SHEET 2 A 4 ALA A 260 PHE A 264 -1 O ILE A 261 N LEU A 252 SHEET 3 A 4 VAL A 223 LYS A 227 -1 N ILE A 224 O VAL A 262 SHEET 4 A 4 TYR A 288 TRP A 291 -1 O GLU A 290 N LEU A 225 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