Header list of 1fj7.pdb file
Complete list - b 23 2 Bytes
HEADER STRUCTURAL PROTEIN 07-AUG-00 1FJ7 TITLE SOLUTION STRUCTURE OF NUCLEOLIN RBD1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: NUCLEOLIN RBD1; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: PROTEIN C23; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MESOCRICETUS AURATUS; SOURCE 3 ORGANISM_COMMON: GOLDEN HAMSTER; SOURCE 4 ORGANISM_TAXID: 10036; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: BL21(DE3)PLYSS KEYWDS RNP, RBD, RRM, RNA BINDING DOMAIN, NUCLEOLUS, STRUCTURAL PROTEIN EXPDTA SOLUTION NMR NUMMDL 34 AUTHOR F.H.-T.ALLAIN,D.E.GILBERT,P.BOUVET,J.FEIGON REVDAT 4 23-FEB-22 1FJ7 1 REMARK SEQADV REVDAT 3 24-FEB-09 1FJ7 1 VERSN REVDAT 2 01-APR-03 1FJ7 1 JRNL REVDAT 1 16-OCT-00 1FJ7 0 JRNL AUTH F.H.ALLAIN,D.E.GILBERT,P.BOUVET,J.FEIGON JRNL TITL SOLUTION STRUCTURE OF THE TWO N-TERMINAL RNA-BINDING DOMAINS JRNL TITL 2 OF NUCLEOLIN AND NMR STUDY OF THE INTERACTION WITH ITS RNA JRNL TITL 3 TARGET. JRNL REF J.MOL.BIOL. V. 303 227 2000 JRNL REFN ISSN 0022-2836 JRNL PMID 11023788 JRNL DOI 10.1006/JMBI.2000.4118 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.841 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURES ARE BASED ON 1391 REMARK 3 RESTRAINTS, 1335 ARE NOE-DERIVED AND 56 ARE FROM HYDROGEN BONDS REMARK 4 REMARK 4 1FJ7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-AUG-00. REMARK 100 THE DEPOSITION ID IS D_1000011633. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 293 REMARK 210 PH : 6.2 REMARK 210 IONIC STRENGTH : 150 REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1MM U-15N,13C; 50MM POTASSIUM REMARK 210 PHOSPHATE BUFFER; 100 MM KCL, REMARK 210 5MM DEUTERATED DTT, PH 6.2 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR 3.841, DYANA 1 REMARK 210 METHOD USED : SIMULATED ANNEALING USING X-PLOR REMARK 210 3.841 REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 34 REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES REMARK 210 SUBMITTED 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: 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 18 H PHE A 65 1.50 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 HIS A 3 77.68 -110.44 REMARK 500 1 GLU A 13 26.06 46.53 REMARK 500 1 ASN A 24 70.59 65.64 REMARK 500 1 ASN A 26 107.99 -54.15 REMARK 500 1 LYS A 29 -157.24 -117.57 REMARK 500 1 ASP A 46 29.95 91.21 REMARK 500 1 LEU A 47 -139.26 -84.11 REMARK 500 1 ALA A 48 58.41 -177.21 REMARK 500 1 THR A 56 170.99 60.72 REMARK 500 1 ARG A 58 51.24 172.45 REMARK 500 1 SER A 67 179.42 178.88 REMARK 500 1 LYS A 81 47.90 -179.10 REMARK 500 1 PHE A 83 25.88 43.96 REMARK 500 1 GLU A 86 92.86 -53.47 REMARK 500 1 ARG A 99 -74.15 -131.77 REMARK 500 2 GLU A 6 93.42 47.73 REMARK 500 2 ASP A 7 -59.41 179.38 REMARK 500 2 SER A 12 54.92 -145.45 REMARK 500 2 GLU A 13 28.63 -168.15 REMARK 500 2 ASN A 26 102.18 -42.92 REMARK 500 2 LYS A 29 -156.31 -107.13 REMARK 500 2 ASP A 46 30.34 148.26 REMARK 500 2 LEU A 47 -158.94 -106.10 REMARK 500 2 ALA A 48 61.90 -160.41 REMARK 500 2 THR A 56 -83.48 59.43 REMARK 500 2 ASN A 57 97.09 -161.54 REMARK 500 2 ARG A 58 27.09 42.75 REMARK 500 2 LYS A 81 49.85 -170.64 REMARK 500 2 PHE A 83 29.38 42.72 REMARK 500 2 GLU A 86 100.33 -41.92 REMARK 500 2 LYS A 93 -37.51 -133.64 REMARK 500 2 ARG A 95 -56.75 -166.86 REMARK 500 2 ASP A 96 -161.20 -171.96 REMARK 500 2 THR A 98 -163.50 42.60 REMARK 500 3 HIS A 3 -149.65 -97.73 REMARK 500 3 MET A 4 -54.68 -128.95 REMARK 500 3 GLU A 6 -84.18 -74.99 REMARK 500 3 PRO A 8 -156.89 -71.37 REMARK 500 3 VAL A 9 -157.88 -109.60 REMARK 500 3 SER A 14 -173.09 -52.50 REMARK 500 3 ASN A 24 72.29 72.54 REMARK 500 3 LYS A 29 -155.27 -113.27 REMARK 500 3 ASP A 46 29.73 91.69 REMARK 500 3 LEU A 47 -140.68 -87.95 REMARK 500 3 ALA A 48 59.34 -178.28 REMARK 500 3 THR A 56 -91.33 57.68 REMARK 500 3 ARG A 58 26.80 41.92 REMARK 500 3 THR A 78 -19.81 -48.42 REMARK 500 3 LYS A 81 47.93 -169.64 REMARK 500 3 VAL A 82 125.48 -37.83 REMARK 500 REMARK 500 THIS ENTRY HAS 707 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 1 ARG A 53 0.18 SIDE CHAIN REMARK 500 1 ARG A 58 0.16 SIDE CHAIN REMARK 500 1 ARG A 95 0.11 SIDE CHAIN REMARK 500 1 ARG A 99 0.27 SIDE CHAIN REMARK 500 2 ARG A 53 0.19 SIDE CHAIN REMARK 500 2 ARG A 58 0.24 SIDE CHAIN REMARK 500 2 ARG A 95 0.23 SIDE CHAIN REMARK 500 2 ARG A 99 0.23 SIDE CHAIN REMARK 500 3 ARG A 53 0.31 SIDE CHAIN REMARK 500 3 ARG A 58 0.32 SIDE CHAIN REMARK 500 3 ARG A 95 0.19 SIDE CHAIN REMARK 500 3 ARG A 99 0.32 SIDE CHAIN REMARK 500 4 ARG A 53 0.13 SIDE CHAIN REMARK 500 4 ARG A 58 0.29 SIDE CHAIN REMARK 500 4 ARG A 95 0.24 SIDE CHAIN REMARK 500 4 ARG A 99 0.32 SIDE CHAIN REMARK 500 5 ARG A 53 0.10 SIDE CHAIN REMARK 500 5 ARG A 58 0.32 SIDE CHAIN REMARK 500 5 ARG A 95 0.29 SIDE CHAIN REMARK 500 5 ARG A 99 0.32 SIDE CHAIN REMARK 500 6 ARG A 53 0.15 SIDE CHAIN REMARK 500 6 ARG A 58 0.27 SIDE CHAIN REMARK 500 6 ARG A 95 0.30 SIDE CHAIN REMARK 500 6 ARG A 99 0.25 SIDE CHAIN REMARK 500 7 ARG A 53 0.26 SIDE CHAIN REMARK 500 7 ARG A 58 0.29 SIDE CHAIN REMARK 500 7 ARG A 95 0.30 SIDE CHAIN REMARK 500 7 ARG A 99 0.25 SIDE CHAIN REMARK 500 8 ARG A 53 0.30 SIDE CHAIN REMARK 500 8 ARG A 58 0.20 SIDE CHAIN REMARK 500 8 ARG A 95 0.29 SIDE CHAIN REMARK 500 8 ARG A 99 0.28 SIDE CHAIN REMARK 500 9 ARG A 53 0.18 SIDE CHAIN REMARK 500 9 ARG A 58 0.20 SIDE CHAIN REMARK 500 9 ARG A 95 0.15 SIDE CHAIN REMARK 500 9 ARG A 99 0.16 SIDE CHAIN REMARK 500 10 ARG A 53 0.20 SIDE CHAIN REMARK 500 10 ARG A 58 0.18 SIDE CHAIN REMARK 500 10 ARG A 95 0.09 SIDE CHAIN REMARK 500 10 ARG A 99 0.30 SIDE CHAIN REMARK 500 11 ARG A 53 0.30 SIDE CHAIN REMARK 500 11 ARG A 58 0.11 SIDE CHAIN REMARK 500 11 ARG A 95 0.20 SIDE CHAIN REMARK 500 11 ARG A 99 0.15 SIDE CHAIN REMARK 500 12 ARG A 53 0.15 SIDE CHAIN REMARK 500 12 ARG A 58 0.24 SIDE CHAIN REMARK 500 12 ARG A 95 0.28 SIDE CHAIN REMARK 500 12 ARG A 99 0.30 SIDE CHAIN REMARK 500 13 ARG A 53 0.22 SIDE CHAIN REMARK 500 13 ARG A 58 0.31 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 134 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1FJ7 A 1 101 UNP P08199 NUCL_MESAU 291 391 SEQADV 1FJ7 GLY A 1 UNP P08199 VAL 291 CONFLICT SEQADV 1FJ7 SER A 2 UNP P08199 PRO 292 CONFLICT SEQADV 1FJ7 HIS A 3 UNP P08199 GLU 293 CONFLICT SEQADV 1FJ7 MET A 4 UNP P08199 ALA 294 CONFLICT SEQADV 1FJ7 LEU A 5 UNP P08199 LYS 295 CONFLICT SEQADV 1FJ7 GLU A 6 UNP P08199 LYS 296 CONFLICT SEQADV 1FJ7 ASP A 7 UNP P08199 GLN 297 CONFLICT SEQADV 1FJ7 PRO A 8 UNP P08199 LYS 298 CONFLICT SEQADV 1FJ7 LEU A 41 UNP P08199 PRO 331 CONFLICT SEQADV 1FJ7 GLY A 97 UNP P08199 SER 387 CONFLICT SEQADV 1FJ7 THR A 98 UNP P08199 LYS 388 CONFLICT SEQADV 1FJ7 ARG A 99 UNP P08199 LYS 389 CONFLICT SEQADV 1FJ7 GLY A 100 UNP P08199 VAL 390 CONFLICT SEQADV 1FJ7 CYS A 101 UNP P08199 ARG 391 CONFLICT SEQRES 1 A 101 GLY SER HIS MET LEU GLU ASP PRO VAL GLU GLY SER GLU SEQRES 2 A 101 SER THR THR PRO PHE ASN LEU PHE ILE GLY ASN LEU ASN SEQRES 3 A 101 PRO ASN LYS SER VAL ALA GLU LEU LYS VAL ALA ILE SER SEQRES 4 A 101 GLU LEU PHE ALA LYS ASN ASP LEU ALA VAL VAL ASP VAL SEQRES 5 A 101 ARG THR GLY THR ASN ARG LYS PHE GLY TYR VAL ASP PHE SEQRES 6 A 101 GLU SER ALA GLU ASP LEU GLU LYS ALA LEU GLU LEU THR SEQRES 7 A 101 GLY LEU LYS VAL PHE GLY ASN GLU ILE LYS LEU GLU LYS SEQRES 8 A 101 PRO LYS GLY ARG ASP GLY THR ARG GLY CYS HELIX 1 1 SER A 30 ASP A 46 1 17 HELIX 2 2 SER A 67 LEU A 77 1 11 HELIX 3 3 THR A 78 LEU A 80 5 3 HELIX 4 4 LYS A 81 LYS A 81 5 1 SHEET 1 A 4 ASP A 51 GLY A 55 0 SHEET 2 A 4 PHE A 60 PHE A 65 -1 N PHE A 60 O GLY A 55 SHEET 3 A 4 PHE A 18 GLY A 23 -1 O PHE A 18 N PHE A 65 SHEET 4 A 4 LYS A 88 GLU A 90 -1 N LYS A 88 O GLY A 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