Header list of 1whn.pdb file
Complete list - r 2 2 Bytes
HEADER RNA BINDING PROTEIN 28-MAY-04 1WHN
TITLE SOLUTION STRUCTURE OF THE DSRBD FROM HYPOTHETICAL PROTEIN BAB26260
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN RIKEN CDNA 2310016K04;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DOUBLE-STRANDED RNA BINDING DOMAIN;
COMPND 5 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 2310016K04;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P021209-40;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS DOUBLE-STRANDED RNA BINDING DOMAIN, DSRBD, DSRM, RIKEN STRUCTURAL
KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, STRUCTURAL GENOMICS, 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 1WHN 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WHN 1 VERSN
REVDAT 1 28-NOV-04 1WHN 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 DSRBD FROM HYPOTHETICAL PROTEIN
JRNL TITL 2 BAB26260
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 1WHN 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_1000023590.
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 : 1.28MM 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 PHE A 359 124.55 -39.92
REMARK 500 1 LYS A 382 26.01 45.31
REMARK 500 1 PRO A 386 -178.88 -69.78
REMARK 500 1 ARG A 397 31.46 35.72
REMARK 500 1 ALA A 426 -72.48 -34.48
REMARK 500 1 PRO A 437 2.01 -69.76
REMARK 500 1 GLU A 438 45.79 -80.69
REMARK 500 1 ARG A 440 -36.09 -36.51
REMARK 500 1 SER A 445 142.23 -170.41
REMARK 500 1 LEU A 448 48.14 -105.38
REMARK 500 1 PRO A 460 -179.48 -69.82
REMARK 500 1 PRO A 463 -163.82 -69.78
REMARK 500 1 ARG A 464 67.43 -107.67
REMARK 500 1 SER A 465 96.90 -58.80
REMARK 500 2 SER A 348 105.21 -43.21
REMARK 500 2 SER A 350 136.65 -174.38
REMARK 500 2 ARG A 440 -39.58 -38.78
REMARK 500 2 ASN A 449 109.72 -38.30
REMARK 500 2 ASP A 457 134.91 -36.88
REMARK 500 2 SER A 465 109.71 -167.83
REMARK 500 3 SER A 344 107.63 -34.60
REMARK 500 3 PRO A 366 0.99 -69.72
REMARK 500 3 PRO A 386 -179.44 -69.74
REMARK 500 3 ALA A 427 -70.73 -34.54
REMARK 500 3 PRO A 437 2.96 -69.80
REMARK 500 3 GLU A 438 47.16 -77.26
REMARK 500 3 ARG A 440 -31.50 -38.81
REMARK 500 3 GLU A 444 161.06 -43.57
REMARK 500 3 SER A 445 52.65 39.13
REMARK 500 3 LEU A 448 121.12 -171.75
REMARK 500 3 ARG A 453 132.27 -174.99
REMARK 500 3 ARG A 464 77.82 -118.80
REMARK 500 4 SER A 348 41.91 -87.21
REMARK 500 4 SER A 350 45.18 -104.62
REMARK 500 4 PHE A 359 126.81 -36.64
REMARK 500 4 PRO A 366 0.99 -69.73
REMARK 500 4 LYS A 382 36.47 38.85
REMARK 500 4 PRO A 386 -179.20 -69.80
REMARK 500 4 ARG A 397 28.22 44.54
REMARK 500 4 ALA A 426 -72.56 -35.21
REMARK 500 4 PRO A 437 2.88 -69.80
REMARK 500 4 GLU A 438 40.91 -81.57
REMARK 500 4 ARG A 440 -38.94 -36.01
REMARK 500 4 GLU A 444 113.93 -34.58
REMARK 500 4 SER A 447 150.65 -41.98
REMARK 500 4 ARG A 464 159.29 -47.09
REMARK 500 5 SER A 344 42.61 -81.31
REMARK 500 5 SER A 345 -59.85 -125.64
REMARK 500 5 SER A 347 94.17 -65.90
REMARK 500 5 SER A 350 49.32 -82.67
REMARK 500
REMARK 500 THIS ENTRY HAS 221 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MMT007002726.1 RELATED DB: TARGETDB
DBREF 1WHN A 350 464 UNP Q9D7B1 DUS2L_MOUSE 350 464
SEQADV 1WHN GLY A 343 UNP Q9D7B1 CLONING ARTIFACT
SEQADV 1WHN SER A 344 UNP Q9D7B1 CLONING ARTIFACT
SEQADV 1WHN SER A 345 UNP Q9D7B1 CLONING ARTIFACT
SEQADV 1WHN GLY A 346 UNP Q9D7B1 CLONING ARTIFACT
SEQADV 1WHN SER A 347 UNP Q9D7B1 CLONING ARTIFACT
SEQADV 1WHN SER A 348 UNP Q9D7B1 CLONING ARTIFACT
SEQADV 1WHN GLY A 349 UNP Q9D7B1 CLONING ARTIFACT
SEQADV 1WHN SER A 465 UNP Q9D7B1 CLONING ARTIFACT
SEQADV 1WHN GLY A 466 UNP Q9D7B1 CLONING ARTIFACT
SEQADV 1WHN PRO A 467 UNP Q9D7B1 CLONING ARTIFACT
SEQADV 1WHN SER A 468 UNP Q9D7B1 CLONING ARTIFACT
SEQADV 1WHN SER A 469 UNP Q9D7B1 CLONING ARTIFACT
SEQADV 1WHN GLY A 470 UNP Q9D7B1 CLONING ARTIFACT
SEQRES 1 A 128 GLY SER SER GLY SER SER GLY SER GLY ILE ILE LYS MET
SEQRES 2 A 128 ALA ILE ARG PHE ASP ARG ARG ALA TYR PRO PRO GLN ILE
SEQRES 3 A 128 THR PRO LYS MET CYS LEU LEU GLU TRP CYS ARG ARG GLU
SEQRES 4 A 128 LYS LEU PRO GLN PRO VAL TYR GLU THR VAL GLN ARG THR
SEQRES 5 A 128 ILE ASP ARG MET PHE CYS SER VAL VAL THR VAL ALA GLU
SEQRES 6 A 128 GLN LYS TYR GLN SER THR LEU TRP ASP LYS SER LYS LYS
SEQRES 7 A 128 LEU ALA GLU GLN THR ALA ALA ILE VAL CYS LEU ARG SER
SEQRES 8 A 128 GLN GLY LEU PRO GLU GLY ARG LEU GLY GLU GLU SER PRO
SEQRES 9 A 128 SER LEU ASN LYS ARG LYS ARG GLU ALA PRO ASP GLN ASP
SEQRES 10 A 128 PRO GLY GLY PRO ARG SER GLY PRO SER SER GLY
HELIX 1 1 ARG A 361 ALA A 363 5 3
HELIX 2 2 PRO A 370 ARG A 380 1 11
HELIX 3 3 LYS A 419 GLN A 434 1 16
SHEET 1 A 4 ILE A 353 MET A 355 0
SHEET 2 A 4 GLN A 408 SER A 412 1 O LYS A 409 N ILE A 353
SHEET 3 A 4 PHE A 399 VAL A 405 -1 N VAL A 403 O TYR A 410
SHEET 4 A 4 THR A 390 GLN A 392 -1 N VAL A 391 O CYS 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 - r 2 2 Bytes