Header list of 1imu.pdb file
Complete list - b 23 2 Bytes
HEADER RNA BINDING PROTEIN 11-MAY-01 1IMU TITLE SOLUTION STRUCTURE OF HI0257, A RIBOSOME BINDING PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN HI0257; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HAEMOPHILUS INFLUENZAE; SOURCE 3 ORGANISM_TAXID: 727; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET-15B KEYWDS DSRNA BINDING PROTEIN, PROTEOME, SOLUTION STRUCTURE, RIBOSOME, KEYWDS 2 STRUCTURE 2 FUNCTION PROJECT, S2F, STRUCTURAL GENOMICS, RNA BINDING KEYWDS 3 PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR L.PARSONS,E.EISENSTEIN,J.ORBAN,STRUCTURE 2 FUNCTION PROJECT (S2F) REVDAT 3 23-FEB-22 1IMU 1 REMARK REVDAT 2 24-FEB-09 1IMU 1 VERSN REVDAT 1 03-OCT-01 1IMU 0 JRNL AUTH L.PARSONS,E.EISENSTEIN,J.ORBAN JRNL TITL SOLUTION STRUCTURE OF HI0257, A BACTERIAL RIBOSOME BINDING JRNL TITL 2 PROTEIN. JRNL REF BIOCHEMISTRY V. 40 10979 2001 JRNL REFN ISSN 0006-2960 JRNL PMID 11551193 JRNL DOI 10.1021/BI011077I REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.0 REMARK 3 AUTHORS : BRUNGER, ADAMS, CLORE, DELANO, GROS,GROSSE REMARK 3 -KUNSTLEVE, JIANG, KUSZEWSKI,NILGES, PANNU, READ, REMARK 3 RICE, SIMONSON,WARREN REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1IMU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAY-01. REMARK 100 THE DEPOSITION ID IS D_1000013414. 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 : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : 1.3MM HI0257, 15N,13C; 50MM REMARK 210 NAPO4, 100MM NACL, 3MM DTT PH 7.0 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; HNHA; 3D REMARK 210 HNCACB; 3D CBCA(CO)NH; 3D HNCO; REMARK 210 3D HBHA(CO)NH; 3D_15N TOCSY-HSQC; REMARK 210 3D HCCH-TOCSY; 2D_TOCSY; 2D_ REMARK 210 NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRDRAW, SPARKY REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 39 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES REMARK 210 WITH THE LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL 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: 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 H PHE A 48 O SER A 67 1.60 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 THR A 6 -53.58 -126.31 REMARK 500 1 SER A 7 96.23 42.86 REMARK 500 1 GLN A 9 -93.39 -118.15 REMARK 500 1 ALA A 15 -73.57 -53.24 REMARK 500 1 GLN A 31 67.15 -61.51 REMARK 500 1 LEU A 34 96.79 -48.54 REMARK 500 1 SER A 36 94.01 59.51 REMARK 500 1 MET A 70 -70.14 -38.63 REMARK 500 1 LYS A 91 -175.32 47.26 REMARK 500 1 GLU A 93 30.04 -98.88 REMARK 500 1 SER A 94 61.46 -170.12 REMARK 500 1 ARG A 95 73.66 -68.36 REMARK 500 1 ARG A 96 -75.56 66.33 REMARK 500 1 ASP A 98 175.31 55.44 REMARK 500 1 ARG A 100 167.78 67.50 REMARK 500 1 SER A 104 -39.60 -178.25 REMARK 500 1 PHE A 105 -44.30 -156.73 REMARK 500 1 GLU A 106 70.78 63.45 REMARK 500 2 LEU A 3 107.33 58.20 REMARK 500 2 GLN A 9 -53.77 -141.64 REMARK 500 2 ASP A 11 178.62 -51.45 REMARK 500 2 ALA A 15 -75.02 -50.14 REMARK 500 2 GLN A 31 84.10 -38.80 REMARK 500 2 ILE A 35 109.88 -59.69 REMARK 500 2 SER A 36 90.54 46.58 REMARK 500 2 MET A 70 -70.27 -38.85 REMARK 500 2 SER A 92 163.86 66.90 REMARK 500 2 ALA A 97 110.22 60.71 REMARK 500 2 GLU A 99 108.65 60.20 REMARK 500 3 THR A 6 -64.57 -149.45 REMARK 500 3 SER A 7 97.99 56.42 REMARK 500 3 GLN A 9 -89.29 -131.03 REMARK 500 3 MET A 10 107.48 -56.58 REMARK 500 3 ASP A 11 -173.65 -61.06 REMARK 500 3 ALA A 15 -82.02 -73.30 REMARK 500 3 GLN A 31 71.24 -18.69 REMARK 500 3 LEU A 34 96.34 -59.07 REMARK 500 3 SER A 36 94.81 -168.36 REMARK 500 3 MET A 70 -71.88 -39.47 REMARK 500 3 LYS A 91 -171.82 -54.58 REMARK 500 3 SER A 92 88.75 -159.12 REMARK 500 3 ALA A 97 132.89 -174.83 REMARK 500 3 ASP A 98 165.57 60.03 REMARK 500 3 GLU A 99 37.12 -175.59 REMARK 500 3 LEU A 101 61.70 -100.06 REMARK 500 3 LYS A 102 -79.49 63.55 REMARK 500 3 ASP A 103 -53.54 -155.13 REMARK 500 3 SER A 104 153.38 61.62 REMARK 500 3 PHE A 105 171.62 60.13 REMARK 500 4 LEU A 3 102.79 64.19 REMARK 500 REMARK 500 THIS ENTRY HAS 348 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HI0257 RELATED DB: TARGETDB DBREF 1IMU A 1 107 UNP P71346 Y257_HAEIN 0 106 SEQRES 1 A 107 MET THR LEU ASN ILE THR SER LYS GLN MET ASP ILE THR SEQRES 2 A 107 PRO ALA ILE ARG GLU HIS LEU GLU GLU ARG LEU ALA LYS SEQRES 3 A 107 LEU GLY LYS TRP GLN THR GLN LEU ILE SER PRO HIS PHE SEQRES 4 A 107 VAL LEU ASN LYS VAL PRO ASN GLY PHE SER VAL GLU ALA SEQRES 5 A 107 SER ILE GLY THR PRO LEU GLY ASN LEU LEU ALA SER ALA SEQRES 6 A 107 THR SER ASP ASP MET TYR LYS ALA ILE ASN GLU VAL GLU SEQRES 7 A 107 GLU LYS LEU GLU ARG GLN LEU ASN LYS LEU GLN HIS LYS SEQRES 8 A 107 SER GLU SER ARG ARG ALA ASP GLU ARG LEU LYS ASP SER SEQRES 9 A 107 PHE GLU ASN HELIX 1 1 THR A 13 LYS A 29 1 17 HELIX 2 2 ASP A 69 LYS A 91 1 23 SHEET 1 A 4 ASN A 4 ILE A 5 0 SHEET 2 A 4 HIS A 38 VAL A 44 1 N PHE A 39 O ASN A 4 SHEET 3 A 4 GLY A 47 ILE A 54 -1 O GLY A 47 N VAL A 44 SHEET 4 A 4 LEU A 61 SER A 67 -1 N LEU A 61 O ILE A 54 CRYST1 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