Header list of 1ifw.pdb file
Complete list - b 23 2 Bytes
HEADER RNA BINDING PROTEIN 13-APR-01 1IFW
TITLE SOLUTION STRUCTURE OF C-TERMINAL DOMAIN OF POLY(A) BINDING PROTEIN
TITLE 2 FROM SACCHAROMYCES CEREVISIAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYADENYLATE-BINDING PROTEIN, CYTOPLASMIC AND NUCLEAR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN (490-576);
COMPND 5 SYNONYM: POLYADENYLATE TAIL-BINDING PROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: PAB1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 GOLD;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1
KEYWDS ALL-HELICAL DOMAIN, RNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR G.KOZLOV,N.SIDDIQUI,S.COILLET-MATILLON,T.SPRULES,I.EKIEL,K.GEHRING
REVDAT 3 23-FEB-22 1IFW 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1IFW 1 VERSN
REVDAT 1 24-JUL-02 1IFW 0
JRNL AUTH G.KOZLOV,N.SIDDIQUI,S.COILLET-MATILLON,J.F.TREMPE,I.EKIEL,
JRNL AUTH 2 T.SPRULES,K.GEHRING
JRNL TITL SOLUTION STRUCTURE OF THE ORPHAN PABC DOMAIN FROM
JRNL TITL 2 SACCHAROMYCES CEREVISIAE POLY(A)-BINDING PROTEIN.
JRNL REF J.BIOL.CHEM. V. 277 22822 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 11940585
JRNL DOI 10.1074/JBC.M201230200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.1, CNS 0.9
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON 972 NOE DISTANCE CONSTRAINTS, 69
REMARK 3 DIHEDRAL ANGLES
REMARK 3 CONSTRAINTS AND 40 HYDROGEN BONDS.
REMARK 4
REMARK 4 1IFW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-APR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013235.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.3
REMARK 210 IONIC STRENGTH : 0.2
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 3MM PROTEIN, 50MM PHOSPHATE
REMARK 210 BUFFER, 0.1M NACL, 1MM NAN3; 3MM
REMARK 210 PROTEIN, 50MM PHOSPHATE BUFFER,
REMARK 210 0.1M NACL, 1MM NAN3; 3MM PROTEIN
REMARK 210 U-15N, 50MM PHOSPHATE BUFFER,
REMARK 210 0.1M NACL, 1MM NAN3; 3MM PROTEIN
REMARK 210 U-15N,13C, 50MM PHOSPHATE BUFFER,
REMARK 210 0.1M NACL, 1MM NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : GIFA 4.31, XEASY 1.3.13, CNS
REMARK 210 0.9, ARIA 0.9
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK:
REMARK 210 THE STRUCTURE WAS DETERMINED USING STANDARD TRIPLE-RESONANCE AND
REMARK 210 HOMONUCLEAR
REMARK 210 TECHNIQUES. THE N-TERMINAL SEQUENCE GPLGS IS A CLONING ARTIFACT.
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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O PHE A 67 H TYR A 71 1.58
REMARK 500
REMARK 500 REMARK: NULL
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 15 44.85 -86.04
REMARK 500 1 ALA A 23 -73.19 -60.76
REMARK 500 1 SER A 37 40.00 -91.71
REMARK 500 1 ALA A 41 -70.50 -75.42
REMARK 500 1 PRO A 53 168.30 -47.80
REMARK 500 1 GLU A 84 44.94 -88.52
REMARK 500 2 ALA A 23 -71.63 -61.52
REMARK 500 2 THR A 36 167.63 176.31
REMARK 500 2 SER A 37 36.56 -98.34
REMARK 500 2 PRO A 53 172.32 -47.58
REMARK 500 3 LEU A 3 -69.48 -91.70
REMARK 500 3 ALA A 9 81.95 -62.05
REMARK 500 3 GLN A 17 38.18 -88.91
REMARK 500 3 ALA A 23 -72.66 -66.62
REMARK 500 3 SER A 37 39.41 -87.18
REMARK 500 3 PRO A 53 175.62 -46.45
REMARK 500 3 THR A 89 79.06 -100.58
REMARK 500 4 PHE A 15 46.70 -80.61
REMARK 500 4 ALA A 23 -75.49 -68.80
REMARK 500 4 THR A 36 161.95 179.62
REMARK 500 4 SER A 37 38.51 -97.28
REMARK 500 4 LYS A 44 -70.12 -72.99
REMARK 500 4 PRO A 53 172.76 -53.24
REMARK 500 4 GLU A 84 39.98 -83.86
REMARK 500 4 GLN A 87 -60.76 -98.03
REMARK 500 4 THR A 89 73.02 -111.03
REMARK 500 5 ASN A 13 94.82 -57.72
REMARK 500 5 ALA A 23 -71.40 -65.99
REMARK 500 5 SER A 37 37.33 -86.60
REMARK 500 5 PRO A 53 175.77 -48.07
REMARK 500 5 PRO A 54 -70.28 -58.08
REMARK 500 5 GLU A 84 37.86 -85.16
REMARK 500 6 PRO A 2 94.08 -55.70
REMARK 500 6 ALA A 23 -71.93 -69.04
REMARK 500 6 ALA A 34 -7.40 -59.14
REMARK 500 6 SER A 37 38.19 -89.01
REMARK 500 6 PRO A 53 170.67 -50.91
REMARK 500 6 GLU A 90 -173.07 -66.02
REMARK 500 7 ALA A 23 -73.93 -65.33
REMARK 500 7 SER A 37 38.57 -98.18
REMARK 500 8 GLN A 14 40.36 -95.08
REMARK 500 8 ALA A 23 -72.32 -64.06
REMARK 500 8 SER A 37 38.34 -92.57
REMARK 500 8 ALA A 41 -70.73 -79.55
REMARK 500 8 PRO A 53 166.96 -45.74
REMARK 500 8 GLN A 85 86.03 -65.10
REMARK 500 8 THR A 89 -147.98 -113.34
REMARK 500 9 ALA A 23 -74.56 -61.54
REMARK 500 9 THR A 36 166.42 178.98
REMARK 500 9 SER A 37 37.03 -89.55
REMARK 500
REMARK 500 THIS ENTRY HAS 195 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1IFW A 6 92 UNP P04147 PABP_YEAST 490 576
SEQADV 1IFW GLY A 1 UNP P04147 CLONING ARTIFACT
SEQADV 1IFW PRO A 2 UNP P04147 CLONING ARTIFACT
SEQADV 1IFW LEU A 3 UNP P04147 CLONING ARTIFACT
SEQADV 1IFW GLY A 4 UNP P04147 CLONING ARTIFACT
SEQADV 1IFW SER A 5 UNP P04147 CLONING ARTIFACT
SEQRES 1 A 92 GLY PRO LEU GLY SER PRO ARG ASN ALA ASN ASP ASN ASN
SEQRES 2 A 92 GLN PHE TYR GLN GLN LYS GLN ARG GLN ALA LEU GLY GLU
SEQRES 3 A 92 GLN LEU TYR LYS LYS VAL SER ALA LYS THR SER ASN GLU
SEQRES 4 A 92 GLU ALA ALA GLY LYS ILE THR GLY MET ILE LEU ASP LEU
SEQRES 5 A 92 PRO PRO GLN GLU VAL PHE PRO LEU LEU GLU SER ASP GLU
SEQRES 6 A 92 LEU PHE GLU GLN HIS TYR LYS GLU ALA SER ALA ALA TYR
SEQRES 7 A 92 GLU SER PHE LYS LYS GLU GLN GLU GLN GLN THR GLU GLN
SEQRES 8 A 92 ALA
HELIX 1 1 PHE A 15 LYS A 19 5 5
HELIX 2 2 GLN A 20 SER A 33 1 14
HELIX 3 3 ALA A 34 THR A 36 5 3
HELIX 4 4 ASN A 38 LEU A 50 1 13
HELIX 5 5 PRO A 59 GLU A 62 5 4
HELIX 6 6 SER A 63 GLN A 85 1 23
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 - b 23 2 Bytes