Header list of 1whv.pdb file
Complete list - r 2 2 Bytes
HEADER HYDROLASE 28-MAY-04 1WHV
TITLE SOLUTION STRUCTURE OF THE RNA BINDING DOMAIN FROM HYPOTHETICAL PROTEIN
TITLE 2 BAB23382
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(A)-SPECIFIC RIBONUCLEASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RNA RECOGNITION MOTIF;
COMPND 5 SYNONYM: DEADENYLATION NUCLEASE, HYPOTHETICAL PROTEIN BAB23382;
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 1200003I18;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P031020-39;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS RNA RECOGNITION MOTIF, RRM, RNA BINDING DOMAIN, RBD, RNP, POLY(A)-
KEYWDS 2 SPECIFIC RIBONUCLEASE, PARN, STRUCTURAL GENOMICS, RIKEN STRUCTURAL
KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, HYDROLASE
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 1WHV 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WHV 1 VERSN
REVDAT 1 28-NOV-04 1WHV 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 RNA BINDING DOMAIN FROM
JRNL TITL 2 HYPOTHETICAL PROTEIN BAB23382
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 1WHV 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_1000023594.
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 : 0.94MM PROTEIN U-15N, 13C; 20MM
REMARK 210 PHOSPHATE BUFFER NA; 100MM NACL;
REMARK 210 1MM D-DTT; 0.02% NAN3; 90% H2O;
REMARK 210 10% 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 TRP A 449 -175.31 -66.60
REMARK 500 1 ILE A 469 -66.20 -90.60
REMARK 500 1 VAL A 515 141.96 -39.41
REMARK 500 1 SER A 521 108.32 -39.21
REMARK 500 2 ASP A 432 177.21 -54.32
REMARK 500 2 LYS A 436 106.15 -165.00
REMARK 500 2 GLU A 448 -37.22 -36.77
REMARK 500 2 TRP A 449 172.80 -55.25
REMARK 500 2 GLN A 514 132.02 -174.02
REMARK 500 2 SER A 520 115.96 -163.09
REMARK 500 3 PRO A 431 1.49 -69.78
REMARK 500 3 LYS A 436 41.32 -96.97
REMARK 500 3 ARG A 437 78.02 -64.73
REMARK 500 3 TRP A 449 -178.08 -65.66
REMARK 500 3 SER A 459 -31.77 -36.16
REMARK 500 3 THR A 472 -33.02 -132.14
REMARK 500 3 VAL A 515 164.02 -48.45
REMARK 500 4 SER A 425 -60.64 -96.59
REMARK 500 4 PRO A 431 1.48 -69.76
REMARK 500 4 LEU A 433 159.03 -47.00
REMARK 500 4 PRO A 435 -175.29 -69.73
REMARK 500 4 LYS A 436 150.57 -35.91
REMARK 500 4 TRP A 449 179.37 -50.35
REMARK 500 4 SER A 459 -33.30 -38.25
REMARK 500 4 ILE A 469 -64.27 -90.87
REMARK 500 4 TYR A 505 -75.00 -83.89
REMARK 500 4 LYS A 509 -71.10 -55.14
REMARK 500 4 LYS A 513 110.40 -168.33
REMARK 500 4 LYS A 516 92.39 -58.72
REMARK 500 4 SER A 520 113.21 -173.11
REMARK 500 5 GLN A 514 134.55 -171.65
REMARK 500 6 LYS A 436 47.64 -84.12
REMARK 500 6 ARG A 437 41.03 -87.53
REMARK 500 6 TRP A 449 -176.31 -68.76
REMARK 500 6 ALA A 460 -36.19 -36.28
REMARK 500 6 ILE A 469 -64.20 -90.70
REMARK 500 6 LYS A 509 -72.17 -40.87
REMARK 500 6 LYS A 513 110.02 -173.70
REMARK 500 6 SER A 520 124.29 -170.38
REMARK 500 7 LEU A 433 173.01 -51.29
REMARK 500 7 GLN A 434 144.11 -35.93
REMARK 500 7 TRP A 449 -176.54 -69.26
REMARK 500 7 ILE A 469 -70.57 -90.54
REMARK 500 7 LYS A 513 116.70 -168.25
REMARK 500 8 SER A 425 133.62 -171.87
REMARK 500 8 THR A 472 -38.07 -131.97
REMARK 500 8 GLN A 510 173.74 -54.75
REMARK 500 8 PRO A 519 94.17 -69.72
REMARK 500 9 SER A 428 176.98 -52.01
REMARK 500 9 LEU A 433 86.38 -59.88
REMARK 500
REMARK 500 THIS ENTRY HAS 124 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MMT007011199.1 RELATED DB: TARGETDB
DBREF 1WHV A 430 516 UNP Q8VDG3 PARN_MOUSE 430 516
SEQADV 1WHV GLY A 423 UNP Q8VDG3 CLONING ARTIFACT
SEQADV 1WHV SER A 424 UNP Q8VDG3 CLONING ARTIFACT
SEQADV 1WHV SER A 425 UNP Q8VDG3 CLONING ARTIFACT
SEQADV 1WHV GLY A 426 UNP Q8VDG3 CLONING ARTIFACT
SEQADV 1WHV SER A 427 UNP Q8VDG3 CLONING ARTIFACT
SEQADV 1WHV SER A 428 UNP Q8VDG3 CLONING ARTIFACT
SEQADV 1WHV GLY A 429 UNP Q8VDG3 CLONING ARTIFACT
SEQADV 1WHV SER A 517 UNP Q8VDG3 CLONING ARTIFACT
SEQADV 1WHV GLY A 518 UNP Q8VDG3 CLONING ARTIFACT
SEQADV 1WHV PRO A 519 UNP Q8VDG3 CLONING ARTIFACT
SEQADV 1WHV SER A 520 UNP Q8VDG3 CLONING ARTIFACT
SEQADV 1WHV SER A 521 UNP Q8VDG3 CLONING ARTIFACT
SEQADV 1WHV GLY A 522 UNP Q8VDG3 CLONING ARTIFACT
SEQRES 1 A 100 GLY SER SER GLY SER SER GLY GLY PRO ASP LEU GLN PRO
SEQRES 2 A 100 LYS ARG ASP HIS VAL LEU HIS VAL THR PHE PRO LYS GLU
SEQRES 3 A 100 TRP LYS THR SER ASP LEU TYR GLN LEU PHE SER ALA PHE
SEQRES 4 A 100 GLY ASN ILE GLN ILE SER TRP ILE ASP ASP THR SER ALA
SEQRES 5 A 100 PHE VAL SER LEU SER GLN PRO GLU GLN VAL GLN ILE ALA
SEQRES 6 A 100 VAL ASN THR SER LYS TYR ALA GLU SER TYR ARG ILE GLN
SEQRES 7 A 100 THR TYR ALA GLU TYR VAL GLY LYS LYS GLN LYS GLY LYS
SEQRES 8 A 100 GLN VAL LYS SER GLY PRO SER SER GLY
HELIX 1 1 THR A 451 PHE A 458 1 8
HELIX 2 2 PRO A 481 TYR A 493 1 13
HELIX 3 3 TYR A 502 LYS A 509 1 8
SHEET 1 A 4 GLN A 465 TRP A 468 0
SHEET 2 A 4 ALA A 474 SER A 477 -1 O PHE A 475 N SER A 467
SHEET 3 A 4 VAL A 440 THR A 444 -1 N LEU A 441 O VAL A 476
SHEET 4 A 4 ARG A 498 THR A 501 -1 O GLN A 500 N HIS A 442
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