Header list of 2cjk.pdb file
Complete list - y 2 2 Bytes
HEADER RNA BINDING PROTEIN 04-APR-06 2CJK
TITLE STRUCTURE OF THE RNA BINDING DOMAIN OF HRP1 IN COMPLEX WITH RNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NUCLEAR POLYADENYLATED RNA-BINDING PROTEIN 4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RNA-BINDING DOMAIN, RESIDUES 156-322;
COMPND 5 SYNONYM: HRP1, CLEAVAGE FACTOR IB, CFIB;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: 5'-R(*UP*AP*UP*AP*UP*AP*UP*AP)-3';
COMPND 9 CHAIN: B;
COMPND 10 SYNONYM: POLYADENYLATION ENHANCEMENT ELEMENT;
COMPND 11 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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 12 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 13 ORGANISM_TAXID: 4932
KEYWDS HRP1, RNA-BINDING, RNA PROCESSING, MRNA PROCESSING, NONSENSE-MEDIATED
KEYWDS 2 MRNA DECAY, CLEAVAGE, POLYADENYLATION, NUCLEAR PROTEIN, RNA-BINDING
KEYWDS 3 PROTEIN, RNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR J.M.PEREZ-CANADILLAS
REVDAT 4 02-MAY-18 2CJK 1 JRNL REMARK
REVDAT 3 24-FEB-09 2CJK 1 VERSN
REVDAT 2 20-DEC-06 2CJK 1 JRNL
REVDAT 1 28-JUN-06 2CJK 0
JRNL AUTH J.M.PEREZ-CANADILLAS
JRNL TITL GRABBING THE MESSAGE: STRUCTURAL BASIS OF MRNA 3'UTR
JRNL TITL 2 RECOGNITION BY HRP1.
JRNL REF EMBO J. V. 25 3167 2006
JRNL REFN ISSN 0261-4189
JRNL PMID 16794580
JRNL DOI 10.1038/SJ.EMBOJ.7601190
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XPLOR-NIH
REMARK 3 AUTHORS : SCHWIETERS
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2CJK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-APR-06.
REMARK 100 THE DEPOSITION ID IS D_1290028407.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298.0; 298.0; 298.0
REMARK 210 PH : 6.0; 6.0; 6.0
REMARK 210 IONIC STRENGTH : 25; 25; 25
REMARK 210 PRESSURE : 1.0 ATM; 1.0 ATM; 1.0 ATM
REMARK 210 SAMPLE CONTENTS : 95% WATER/5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N-NOESY-HSQC; 13C-NOESY- HSQC;
REMARK 210 TOCSY AND COSY; HNCA; HNCOCA;
REMARK 210 CBCACOHN; HCCH-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, ANSIG, XWIN-NMR
REMARK 210 METHOD USED : XPLOR-NIH, CNS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : COMPARISON BETWEEN ENERGY-
REMARK 210 ORDERED RMSD PROFILES AND TOTAL
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NONE
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 VAL A 216 HE2 HIS A 221 1.24
REMARK 500 H PHE A 162 O LYS A 231 1.56
REMARK 500 H MET A 161 O LEU A 205 1.57
REMARK 500 H ILE A 163 O GLY A 203 1.58
REMARK 500 O VAL A 216 NE2 HIS A 221 2.13
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 MET A 191 55.38 73.13
REMARK 500 1 HIS A 221 111.20 81.65
REMARK 500 1 ASP A 253 -3.70 74.16
REMARK 500 1 ARG A 255 115.25 54.56
REMARK 500 1 ILE A 269 86.99 67.55
REMARK 500 1 MET A 275 -80.28 71.02
REMARK 500 1 LEU A 276 49.42 37.95
REMARK 500 1 ASN A 303 70.58 -100.54
REMARK 500 1 PHE A 308 -72.57 -107.40
REMARK 500 1 ARG A 311 7.86 -150.78
REMARK 500 1 LYS A 312 138.53 56.71
REMARK 500 2 VAL A 185 102.87 64.99
REMARK 500 2 MET A 191 -71.09 67.21
REMARK 500 2 LYS A 192 133.71 59.81
REMARK 500 2 ALA A 195 -75.63 -75.46
REMARK 500 2 ARG A 200 -41.88 74.94
REMARK 500 2 HIS A 221 122.30 77.61
REMARK 500 2 ARG A 255 125.68 56.34
REMARK 500 2 ILE A 269 97.78 28.91
REMARK 500 2 ASP A 271 94.02 -164.83
REMARK 500 2 MET A 275 114.75 93.32
REMARK 500 2 THR A 280 46.30 169.66
REMARK 500 2 LYS A 304 -74.89 67.47
REMARK 500 2 PHE A 308 -107.98 -140.62
REMARK 500 2 ASP A 310 -29.59 176.70
REMARK 500 3 SER A 158 8.61 -150.50
REMARK 500 3 TRP A 168 35.05 33.32
REMARK 500 3 ASP A 169 22.48 -175.72
REMARK 500 3 THR A 171 131.23 62.33
REMARK 500 3 THR A 242 -75.57 -31.31
REMARK 500 3 ARG A 255 124.29 62.21
REMARK 500 3 ILE A 269 80.68 69.39
REMARK 500 3 ASP A 271 86.48 -157.86
REMARK 500 3 MET A 275 119.92 81.24
REMARK 500 3 LYS A 278 -46.94 -161.77
REMARK 500 3 ASP A 279 -79.93 -131.19
REMARK 500 3 LYS A 304 -72.76 69.20
REMARK 500 3 LYS A 309 -165.04 -109.87
REMARK 500 4 TRP A 168 75.95 -60.27
REMARK 500 4 ASP A 169 -22.31 178.28
REMARK 500 4 VAL A 185 89.86 67.47
REMARK 500 4 ARG A 255 141.84 60.97
REMARK 500 4 ILE A 269 83.99 69.70
REMARK 500 4 ASP A 271 93.10 -161.63
REMARK 500 4 MET A 275 115.48 95.00
REMARK 500 4 LYS A 278 -49.38 -150.39
REMARK 500 4 ASP A 279 -54.32 -150.38
REMARK 500 4 LYS A 304 -81.57 37.62
REMARK 500 4 PHE A 308 -109.37 -106.16
REMARK 500 4 ASP A 310 -27.57 -179.60
REMARK 500
REMARK 500 THIS ENTRY HAS 382 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2CJK A 156 322 UNP Q99383 HRP1_YEAST 156 322
DBREF 2CJK B 1 8 PDB 2CJK 2CJK 1 8
SEQRES 1 A 167 LYS GLU SER CYS LYS MET PHE ILE GLY GLY LEU ASN TRP
SEQRES 2 A 167 ASP THR THR GLU ASP ASN LEU ARG GLU TYR PHE GLY LYS
SEQRES 3 A 167 TYR GLY THR VAL THR ASP LEU LYS ILE MET LYS ASP PRO
SEQRES 4 A 167 ALA THR GLY ARG SER ARG GLY PHE GLY PHE LEU SER PHE
SEQRES 5 A 167 GLU LYS PRO SER SER VAL ASP GLU VAL VAL LYS THR GLN
SEQRES 6 A 167 HIS ILE LEU ASP GLY LYS VAL ILE ASP PRO LYS ARG ALA
SEQRES 7 A 167 ILE PRO ARG ASP GLU GLN ASP LYS THR GLY LYS ILE PHE
SEQRES 8 A 167 VAL GLY GLY ILE GLY PRO ASP VAL ARG PRO LYS GLU PHE
SEQRES 9 A 167 GLU GLU PHE PHE SER GLN TRP GLY THR ILE ILE ASP ALA
SEQRES 10 A 167 GLN LEU MET LEU ASP LYS ASP THR GLY GLN SER ARG GLY
SEQRES 11 A 167 PHE GLY PHE VAL THR TYR ASP SER ALA ASP ALA VAL ASP
SEQRES 12 A 167 ARG VAL CYS GLN ASN LYS PHE ILE ASP PHE LYS ASP ARG
SEQRES 13 A 167 LYS ILE GLU ILE LYS ARG ALA GLU PRO ARG HIS
SEQRES 1 B 8 U A U A U A U A
HELIX 1 1 THR A 171 GLY A 180 1 10
HELIX 2 2 PRO A 210 THR A 219 1 10
HELIX 3 3 PRO A 235 THR A 242 1 8
HELIX 4 4 ARG A 255 GLN A 265 1 11
HELIX 5 5 SER A 293 ASN A 303 1 11
SHEET 1 AA 4 VAL A 185 LYS A 189 0
SHEET 2 AA 4 GLY A 203 PHE A 207 -1 O PHE A 204 N LYS A 189
SHEET 3 AA 4 LYS A 160 ILE A 163 -1 O MET A 161 N LEU A 205
SHEET 4 AA 4 ILE A 228 LYS A 231 -1 O LYS A 231 N PHE A 162
SHEET 1 AB 4 ASP A 271 GLN A 273 0
SHEET 2 AB 4 GLY A 285 TYR A 291 -1 O PHE A 288 N GLN A 273
SHEET 3 AB 4 GLY A 243 ILE A 250 -1 O GLY A 243 N TYR A 291
SHEET 4 AB 4 ILE A 313 ARG A 317 -1 O GLU A 314 N GLY A 248
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 - y 2 2 Bytes