Header list of 2cpf.pdb file
Complete list - r 9 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 19-MAY-05 2CPF
TITLE SOLUTION STRUCTURE OF THE PENULTIMATE RNA RECOGNITION MOTIF OF
TITLE 2 HYPOTHETICAL RNA-BINDING PROTEIN RBM19
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RNA BINDING MOTIF PROTEIN 19;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RNA RECOGNITION MOTIF;
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: RBM19;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040705-03;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS RNA RECOGNITION MOTIF, RRM, RNP, STRUCTURAL GENOMICS, NPPSFA,
KEYWDS 2 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES,
KEYWDS 3 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, UNKNOWN
KEYWDS 4 FUNCTION
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 09-MAR-22 2CPF 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2CPF 1 VERSN
REVDAT 1 19-NOV-05 2CPF 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 PENULTIMATE RNA RECOGNITION MOTIF
JRNL TITL 2 OF HYPOTHETICAL RNA-BINDING PROTEIN RBM19
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 2CPF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024478.
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 : 1.28MM 13C/15N-PROTEIN; 20MM D
REMARK 210 -TRIS-HCL(PH7.0); 100MM NACL;
REMARK 210 1MM D-DTT; 0.02% NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20030801/20031121,
REMARK 210 NMRVIEW 5.0.4, KUJIRA 0.925,
REMARK 210 CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYANAMICS,
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,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 SER A 356 112.24 -165.22
REMARK 500 1 SER A 392 91.61 -60.78
REMARK 500 1 SER A 439 154.54 -41.23
REMARK 500 1 GLU A 440 30.28 71.04
REMARK 500 1 SER A 450 -53.08 -128.53
REMARK 500 2 ASN A 366 32.53 72.49
REMARK 500 2 GLN A 423 -39.16 -39.94
REMARK 500 2 THR A 428 97.37 -69.66
REMARK 500 2 ALA A 442 170.43 -59.83
REMARK 500 2 THR A 443 99.98 -68.99
REMARK 500 2 ALA A 446 52.91 37.48
REMARK 500 2 PRO A 449 0.69 -69.75
REMARK 500 4 LEU A 421 -70.18 -53.76
REMARK 500 4 ALA A 446 83.19 -54.29
REMARK 500 4 SER A 450 46.90 34.39
REMARK 500 5 ASN A 366 37.03 72.73
REMARK 500 5 PRO A 445 0.96 -69.81
REMARK 500 5 SER A 447 170.33 -46.70
REMARK 500 5 PRO A 449 0.98 -69.70
REMARK 500 6 SER A 356 101.60 -59.02
REMARK 500 6 LEU A 421 -70.19 -51.52
REMARK 500 6 GLU A 440 37.59 -98.80
REMARK 500 6 ALA A 446 100.02 -39.41
REMARK 500 6 SER A 447 115.65 -174.98
REMARK 500 6 SER A 450 100.68 -48.18
REMARK 500 7 SER A 392 107.62 -58.30
REMARK 500 7 GLN A 423 -39.51 -38.59
REMARK 500 8 ASN A 366 44.93 74.72
REMARK 500 8 GLN A 425 142.28 -38.61
REMARK 500 8 ALA A 446 38.77 73.78
REMARK 500 8 PRO A 449 85.83 -69.71
REMARK 500 9 ASN A 366 34.46 70.33
REMARK 500 9 PRO A 445 95.60 -69.75
REMARK 500 9 SER A 447 164.11 -42.99
REMARK 500 10 SER A 356 37.65 36.86
REMARK 500 10 ASN A 366 40.61 71.18
REMARK 500 10 GLN A 416 -38.14 -37.91
REMARK 500 10 GLN A 423 -36.27 -38.62
REMARK 500 10 GLN A 425 150.64 -43.60
REMARK 500 10 THR A 443 164.14 -45.53
REMARK 500 10 PRO A 449 2.80 -69.76
REMARK 500 11 SER A 392 99.62 -57.55
REMARK 500 11 ALA A 442 161.04 -42.39
REMARK 500 11 SER A 450 167.17 -48.49
REMARK 500 12 PHE A 369 -38.13 -39.27
REMARK 500 12 SER A 388 117.66 -162.48
REMARK 500 12 SER A 392 89.44 -58.35
REMARK 500 12 PRO A 445 97.81 -69.73
REMARK 500 12 SER A 451 102.46 -42.32
REMARK 500 13 ASN A 366 30.26 71.19
REMARK 500
REMARK 500 THIS ENTRY HAS 85 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MMT007011210.12 RELATED DB: TARGETDB
DBREF 2CPF A 362 446 UNP Q8R3C6 RBM19_MOUSE 724 808
SEQADV 2CPF GLY A 355 UNP Q8R3C6 CLONING ARTIFACT
SEQADV 2CPF SER A 356 UNP Q8R3C6 CLONING ARTIFACT
SEQADV 2CPF SER A 357 UNP Q8R3C6 CLONING ARTIFACT
SEQADV 2CPF GLY A 358 UNP Q8R3C6 CLONING ARTIFACT
SEQADV 2CPF SER A 359 UNP Q8R3C6 CLONING ARTIFACT
SEQADV 2CPF SER A 360 UNP Q8R3C6 CLONING ARTIFACT
SEQADV 2CPF GLY A 361 UNP Q8R3C6 CLONING ARTIFACT
SEQADV 2CPF SER A 447 UNP Q8R3C6 CLONING ARTIFACT
SEQADV 2CPF GLY A 448 UNP Q8R3C6 CLONING ARTIFACT
SEQADV 2CPF PRO A 449 UNP Q8R3C6 CLONING ARTIFACT
SEQADV 2CPF SER A 450 UNP Q8R3C6 CLONING ARTIFACT
SEQADV 2CPF SER A 451 UNP Q8R3C6 CLONING ARTIFACT
SEQADV 2CPF GLY A 452 UNP Q8R3C6 CLONING ARTIFACT
SEQRES 1 A 98 GLY SER SER GLY SER SER GLY LEU PHE ILE LYS ASN LEU
SEQRES 2 A 98 ASN PHE SER THR THR GLU GLU THR LEU LYS GLY VAL PHE
SEQRES 3 A 98 SER LYS VAL GLY ALA ILE LYS SER CYS THR ILE SER LYS
SEQRES 4 A 98 LYS LYS ASN LYS ALA GLY VAL LEU LEU SER MET GLY PHE
SEQRES 5 A 98 GLY PHE VAL GLU TYR LYS LYS PRO GLU GLN ALA GLN LYS
SEQRES 6 A 98 ALA LEU LYS GLN LEU GLN GLY HIS THR VAL ASP GLY HIS
SEQRES 7 A 98 LYS LEU GLU VAL ARG ILE SER GLU ARG ALA THR LYS PRO
SEQRES 8 A 98 ALA SER GLY PRO SER SER GLY
HELIX 1 1 GLU A 373 PHE A 380 1 8
HELIX 2 2 PRO A 414 ALA A 420 1 7
SHEET 1 A 4 ILE A 386 SER A 392 0
SHEET 2 A 4 PHE A 406 TYR A 411 -1
SHEET 3 A 4 LEU A 362 LYS A 365 -1
SHEET 4 A 4 GLU A 435 ARG A 437 -1
SHEET 1 B 2 THR A 428 VAL A 429 0
SHEET 2 B 2 HIS A 432 LYS A 433 -1
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