Header list of 2cpx.pdb file
Complete list - r 9 2 Bytes
HEADER TRANSCRIPTION 19-MAY-05 2CPX TITLE SOLUTION STRUCTURE OF RNA BINDING DOMAIN IN HYPOTHETICAL PROTEIN TITLE 2 FLJ11016 COMPND MOL_ID: 1; COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN FLJ11016; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RNA RECOGNITION MOTIF; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: FLJ11016; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040816-17; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS RRM DOMAIN, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN KEYWDS 2 STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, TRANSCRIPTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR K.TSUDA,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,S.YOKOYAMA,RIKEN AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 09-MAR-22 2CPX 1 REMARK SEQADV REVDAT 2 24-FEB-09 2CPX 1 VERSN REVDAT 1 19-NOV-05 2CPX 0 JRNL AUTH K.TSUDA,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU, JRNL AUTH 2 S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF RNA BINDING DOMAIN IN HYPOTHETICAL JRNL TITL 2 PROTEIN FLJ11016 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 2.0.17 REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2CPX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-MAY-05. REMARK 100 THE DEPOSITION ID IS D_1000024488. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : 120MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.7MM 13C/15N-PROTEIN, 20MM D REMARK 210 -TRIS-HCL (PH 7.0), 100MM NACL, REMARK 210 1MM D-DTT, 0.02% NAN3, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C 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 : NMRPIPE 20030801, NMRVIEW 5.0.4, REMARK 210 KUJIRA 0.9297, CYANA 2.0.17 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS, REMARK 210 RESTRAINTED MOLECULAR DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION, STRUCTURES WITH REMARK 210 THE LOWEST ENERGY, STRUCTURES REMARK 210 WITH THE LEAST RESTRAINT REMARK 210 VIOLATIONS 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 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 ARG A 294 42.66 -85.98 REMARK 500 1 SER A 301 -177.17 -64.90 REMARK 500 1 TYR A 302 158.71 -41.30 REMARK 500 1 LYS A 335 150.48 -38.47 REMARK 500 1 PRO A 338 154.44 -47.37 REMARK 500 1 VAL A 370 33.00 -98.41 REMARK 500 1 SER A 392 45.91 -105.12 REMARK 500 1 SER A 396 156.96 -40.00 REMARK 500 2 SER A 289 160.97 -41.00 REMARK 500 2 PRO A 307 103.50 -47.15 REMARK 500 2 LYS A 335 -175.96 -172.89 REMARK 500 2 THR A 346 -63.11 -127.81 REMARK 500 2 SER A 396 -63.90 -92.40 REMARK 500 3 SER A 286 170.44 -48.70 REMARK 500 3 ILE A 293 33.76 -83.61 REMARK 500 3 PHE A 332 32.10 -94.22 REMARK 500 3 LYS A 336 92.49 -57.41 REMARK 500 3 PRO A 338 165.28 -45.23 REMARK 500 4 TYR A 302 170.82 -49.30 REMARK 500 4 PRO A 307 107.02 -47.21 REMARK 500 4 PRO A 318 -19.37 -47.04 REMARK 500 4 LYS A 335 -71.52 -68.95 REMARK 500 4 PRO A 338 157.58 -48.08 REMARK 500 4 PRO A 339 105.93 -47.10 REMARK 500 4 MET A 349 42.95 -102.27 REMARK 500 4 ARG A 350 177.97 -48.51 REMARK 500 4 LYS A 388 59.84 -103.83 REMARK 500 4 SER A 392 91.43 -65.69 REMARK 500 5 SER A 285 -62.22 -133.42 REMARK 500 5 SER A 289 100.06 -57.92 REMARK 500 5 ARG A 294 -63.79 -133.50 REMARK 500 5 TYR A 302 161.64 -49.36 REMARK 500 5 PRO A 307 99.41 -47.14 REMARK 500 5 PRO A 318 -19.50 -46.72 REMARK 500 5 LYS A 336 102.81 -38.48 REMARK 500 5 PRO A 338 156.50 -47.52 REMARK 500 5 PRO A 339 164.26 -45.92 REMARK 500 5 ARG A 348 150.36 -34.55 REMARK 500 5 VAL A 370 31.99 -84.10 REMARK 500 6 ARG A 294 -60.08 -91.08 REMARK 500 6 GLU A 334 -176.12 -51.56 REMARK 500 6 LYS A 335 46.61 -80.91 REMARK 500 6 LYS A 336 36.10 -93.42 REMARK 500 6 PRO A 338 162.90 -43.79 REMARK 500 6 GLN A 390 -64.13 -92.11 REMARK 500 6 SER A 393 130.35 -35.05 REMARK 500 7 ARG A 294 63.99 -102.29 REMARK 500 7 LYS A 335 41.80 34.49 REMARK 500 7 VAL A 370 30.06 -97.37 REMARK 500 7 PHE A 384 151.74 -47.15 REMARK 500 REMARK 500 THIS ENTRY HAS 180 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSI002007170.1 RELATED DB: TARGETDB DBREF 2CPX A 291 392 UNP Q96IZ5 Q96IZ5_HUMAN 291 392 SEQADV 2CPX GLY A 284 UNP Q96IZ5 CLONING ARTIFACT SEQADV 2CPX SER A 285 UNP Q96IZ5 CLONING ARTIFACT SEQADV 2CPX SER A 286 UNP Q96IZ5 CLONING ARTIFACT SEQADV 2CPX GLY A 287 UNP Q96IZ5 CLONING ARTIFACT SEQADV 2CPX SER A 288 UNP Q96IZ5 CLONING ARTIFACT SEQADV 2CPX SER A 289 UNP Q96IZ5 CLONING ARTIFACT SEQADV 2CPX GLY A 290 UNP Q96IZ5 CLONING ARTIFACT SEQADV 2CPX SER A 393 UNP Q96IZ5 CLONING ARTIFACT SEQADV 2CPX GLY A 394 UNP Q96IZ5 CLONING ARTIFACT SEQADV 2CPX PRO A 395 UNP Q96IZ5 CLONING ARTIFACT SEQADV 2CPX SER A 396 UNP Q96IZ5 CLONING ARTIFACT SEQADV 2CPX SER A 397 UNP Q96IZ5 CLONING ARTIFACT SEQADV 2CPX GLY A 398 UNP Q96IZ5 CLONING ARTIFACT SEQRES 1 A 115 GLY SER SER GLY SER SER GLY GLU GLU ILE ARG LYS ILE SEQRES 2 A 115 PRO MET PHE SER SER TYR ASN PRO GLY GLU PRO ASN LYS SEQRES 3 A 115 VAL LEU TYR LEU LYS ASN LEU SER PRO ARG VAL THR GLU SEQRES 4 A 115 ARG ASP LEU VAL SER LEU PHE ALA ARG PHE GLN GLU LYS SEQRES 5 A 115 LYS GLY PRO PRO ILE GLN PHE ARG MET MET THR GLY ARG SEQRES 6 A 115 MET ARG GLY GLN ALA PHE ILE THR PHE PRO ASN LYS GLU SEQRES 7 A 115 ILE ALA TRP GLN ALA LEU HIS LEU VAL ASN GLY TYR LYS SEQRES 8 A 115 LEU TYR GLY LYS ILE LEU VAL ILE GLU PHE GLY LYS ASN SEQRES 9 A 115 LYS LYS GLN ARG SER SER GLY PRO SER SER GLY HELIX 1 1 THR A 321 PHE A 329 1 9 HELIX 2 2 PHE A 329 LYS A 335 1 7 HELIX 3 3 ASN A 359 VAL A 370 1 12 SHEET 1 A 4 GLN A 341 MET A 345 0 SHEET 2 A 4 GLN A 352 THR A 356 -1 O PHE A 354 N ARG A 343 SHEET 3 A 4 VAL A 310 LYS A 314 -1 N LEU A 313 O ALA A 353 SHEET 4 A 4 VAL A 381 PHE A 384 -1 O GLU A 383 N TYR A 312 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 9 2 Bytes