Header list of 2d9p.pdb file
Complete list - r 9 2 Bytes
HEADER RNA BINDING PROTEIN 12-DEC-05 2D9P
TITLE SOLUTION STRUCTURE OF RNA BINDING DOMAIN 4 IN POLYADENYLATION BINDING
TITLE 2 PROTEIN 3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYADENYLATE-BINDING PROTEIN 3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RNA RECOGNITION MOTIF;
COMPND 5 SYNONYM: POLYA, -BINDING PROTEIN 3, PABP 3, TESTIS-SPECIFIC POLYA, -
COMPND 6 BINDING PROTEIN;
COMPND 7 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: PABP3;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P050516-01;
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, RNA BINDING PROTEIN
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 2D9P 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2D9P 1 VERSN
REVDAT 1 12-JUN-06 2D9P 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 4 IN
JRNL TITL 2 POLYADENYLATION BINDING PROTEIN 3
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
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2D9P COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-DEC-05.
REMARK 100 THE DEPOSITION ID IS D_1000025160.
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 : 100MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 20MM D-TRIS-HCL(PH 7.0), 100MM
REMARK 210 NACL, 1MM D-DTT, 0.02% NAN3, 90%
REMARK 210 H2O, 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 0.9321, CYANA 2.0
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 287 38.15 35.49
REMARK 500 1 GLN A 292 95.71 -59.83
REMARK 500 1 PRO A 316 -17.34 -47.97
REMARK 500 1 GLU A 328 34.31 -94.67
REMARK 500 1 PHE A 335 147.54 -171.32
REMARK 500 1 GLU A 352 -19.19 -49.94
REMARK 500 1 ASN A 354 111.01 -36.30
REMARK 500 1 ALA A 359 -73.09 -116.43
REMARK 500 1 THR A 360 -47.62 -132.98
REMARK 500 1 TYR A 364 96.82 -68.43
REMARK 500 1 SER A 379 91.44 -60.95
REMARK 500 2 ASN A 300 37.87 74.50
REMARK 500 2 LEU A 310 -71.12 -67.61
REMARK 500 2 PRO A 316 -17.04 -48.02
REMARK 500 2 MET A 326 95.58 -68.39
REMARK 500 2 GLU A 352 -27.90 -39.99
REMARK 500 2 VAL A 358 -40.90 -131.95
REMARK 500 2 ALA A 359 -66.82 -130.21
REMARK 500 2 THR A 360 -54.52 -133.00
REMARK 500 2 LYS A 371 116.70 -161.86
REMARK 500 2 PRO A 378 150.37 -45.60
REMARK 500 3 ARG A 309 -36.49 -35.19
REMARK 500 3 LEU A 310 -75.12 -68.05
REMARK 500 3 PHE A 314 -30.41 -130.22
REMARK 500 3 PRO A 316 -17.59 -47.95
REMARK 500 3 ASN A 354 111.96 -34.25
REMARK 500 3 THR A 360 -53.23 -131.60
REMARK 500 3 LYS A 371 105.04 -170.25
REMARK 500 4 ASP A 302 157.93 -44.79
REMARK 500 4 LEU A 310 -74.50 -55.42
REMARK 500 4 PRO A 316 -17.88 -48.03
REMARK 500 4 PHE A 317 -61.09 -100.45
REMARK 500 4 ASN A 354 115.95 -34.02
REMARK 500 4 ALA A 359 -72.83 -118.55
REMARK 500 4 THR A 360 -51.74 -132.14
REMARK 500 4 GLN A 369 78.72 -101.06
REMARK 500 4 LYS A 371 -70.84 -106.73
REMARK 500 5 SER A 280 44.01 35.61
REMARK 500 5 LEU A 310 -70.53 -57.28
REMARK 500 5 PRO A 316 -17.10 -47.92
REMARK 500 5 ASN A 354 110.18 -34.89
REMARK 500 5 ALA A 359 -70.63 -125.11
REMARK 500 5 THR A 360 -52.91 -132.03
REMARK 500 5 ALA A 368 -61.41 -105.18
REMARK 500 5 GLU A 373 153.59 -44.99
REMARK 500 5 PRO A 378 156.48 -46.17
REMARK 500 6 SER A 283 147.26 -173.06
REMARK 500 6 LEU A 310 -70.29 -60.22
REMARK 500 6 PRO A 316 -17.02 -48.07
REMARK 500 6 GLU A 328 64.50 -113.37
REMARK 500
REMARK 500 THIS ENTRY HAS 177 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSI002012034.1 RELATED DB: TARGETDB
DBREF 2D9P A 286 375 UNP Q9H361 PABP3_HUMAN 286 375
SEQADV 2D9P GLY A 279 UNP Q9H361 CLONING ARTIFACT
SEQADV 2D9P SER A 280 UNP Q9H361 CLONING ARTIFACT
SEQADV 2D9P SER A 281 UNP Q9H361 CLONING ARTIFACT
SEQADV 2D9P GLY A 282 UNP Q9H361 CLONING ARTIFACT
SEQADV 2D9P SER A 283 UNP Q9H361 CLONING ARTIFACT
SEQADV 2D9P SER A 284 UNP Q9H361 CLONING ARTIFACT
SEQADV 2D9P GLY A 285 UNP Q9H361 CLONING ARTIFACT
SEQADV 2D9P SER A 376 UNP Q9H361 CLONING ARTIFACT
SEQADV 2D9P GLY A 377 UNP Q9H361 CLONING ARTIFACT
SEQADV 2D9P PRO A 378 UNP Q9H361 CLONING ARTIFACT
SEQADV 2D9P SER A 379 UNP Q9H361 CLONING ARTIFACT
SEQADV 2D9P SER A 380 UNP Q9H361 CLONING ARTIFACT
SEQADV 2D9P GLY A 381 UNP Q9H361 CLONING ARTIFACT
SEQRES 1 A 103 GLY SER SER GLY SER SER GLY ASP ARG ILE THR ARG TYR
SEQRES 2 A 103 GLN VAL VAL ASN LEU TYR VAL LYS ASN LEU ASP ASP GLY
SEQRES 3 A 103 ILE ASP ASP GLU ARG LEU ARG LYS ALA PHE SER PRO PHE
SEQRES 4 A 103 GLY THR ILE THR SER ALA LYS VAL MET MET GLU GLY GLY
SEQRES 5 A 103 ARG SER LYS GLY PHE GLY PHE VAL CYS PHE SER SER PRO
SEQRES 6 A 103 GLU GLU ALA THR LYS ALA VAL THR GLU MET ASN GLY ARG
SEQRES 7 A 103 ILE VAL ALA THR LYS PRO LEU TYR VAL ALA LEU ALA GLN
SEQRES 8 A 103 ARG LYS GLU GLU ARG GLN SER GLY PRO SER SER GLY
HELIX 1 1 ASP A 306 ALA A 313 1 8
HELIX 2 2 SER A 342 ASN A 354 1 13
SHEET 1 A 4 ILE A 320 MET A 327 0
SHEET 2 A 4 SER A 332 PHE A 340 -1 O PHE A 337 N LYS A 324
SHEET 3 A 4 LEU A 296 LYS A 299 -1 N LEU A 296 O VAL A 338
SHEET 4 A 4 TYR A 364 LEU A 367 -1 O ALA A 366 N TYR A 297
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