Header list of 1qhk.pdb file
Complete list - r 2 2 Bytes
HEADER HYDROLASE 17-MAY-99 1QHK TITLE N-TERMINAL DOMAIN OF SACCHAROMYCES CEREVISIAE RNASE HI REVEALS A FOLD TITLE 2 WITH A RESEMBLANCE TO THE N-TERMINAL DOMAIN OF RIBOSOMAL PROTEIN L9 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (RIBONUCLEASE HI); COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: N-TERMINAL DOMAIN; COMPND 5 SYNONYM: RNASE HI; COMPND 6 EC: 3.1.26.4; COMPND 7 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: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)C41; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PRSETA KEYWDS RIBONUCLEASE HI N-TERMINAL DOMAIN, HYDROLASE EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR S.P.EVANS,M.BYCROFT REVDAT 4 02-MAR-22 1QHK 1 REMARK REVDAT 3 24-FEB-09 1QHK 1 VERSN REVDAT 2 20-MAR-00 1QHK 1 DBREF REVDAT 1 31-AUG-99 1QHK 0 JRNL AUTH S.P.EVANS,M.BYCROFT JRNL TITL NMR STRUCTURE OF THE N-TERMINAL DOMAIN OF SACCHAROMYCES JRNL TITL 2 CEREVISIAE RNASE HI REVEALS A FOLD WITH A STRONG RESEMBLANCE JRNL TITL 3 TO THE N-TERMINAL DOMAIN OF RIBOSOMAL PROTEIN L9. JRNL REF J.MOL.BIOL. V. 291 661 1999 JRNL REFN ISSN 0022-2836 JRNL PMID 10448044 JRNL DOI 10.1006/JMBI.1999.2971 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH A.R.MUSHEGIAN,H.K.EDSKES,E.V.KOONIN REMARK 1 TITL EUKARYOTIC RNASE H SHARES A CONSERVED DOMAIN WITH REMARK 1 TITL 2 CAULIMOVIRUS PROTEINS THAT FACILITATE TRANSLATION OF REMARK 1 TITL 3 POLYCISTRONIC RNA REMARK 1 REF NUCLEIC ACIDS RES. V. 22 4163 1994 REMARK 1 REFN ISSN 0305-1048 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1QHK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAY-99. REMARK 100 THE DEPOSITION ID IS D_1000001069. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 3.6 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : ACETATE BUFFER (50 MM) REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; COSY; TOCSY; HBHA (CO)NH; REMARK 210 CBCA(CO)NH; HNCACB; HCCH-TOCSY; REMARK 210 HNHA; HNHB REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : AMX500 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 14 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 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 ARG A 12 34.31 -171.11 REMARK 500 1 ARG A 15 175.63 74.81 REMARK 500 1 GLU A 16 103.57 -54.98 REMARK 500 1 THR A 17 -157.69 -134.78 REMARK 500 1 ASN A 21 62.95 -166.72 REMARK 500 1 CYS A 26 -83.79 -65.71 REMARK 500 1 TYR A 33 109.61 1.10 REMARK 500 1 TYR A 38 115.09 10.43 REMARK 500 1 SER A 43 95.65 -176.04 REMARK 500 1 TYR A 44 -29.51 -36.08 REMARK 500 2 ARG A 12 -64.13 -137.17 REMARK 500 2 LYS A 13 27.46 42.65 REMARK 500 2 ARG A 15 174.96 -56.70 REMARK 500 2 GLU A 16 -150.72 66.22 REMARK 500 2 THR A 17 -145.40 49.98 REMARK 500 2 ASN A 21 59.22 -167.02 REMARK 500 2 CYS A 26 -89.62 -62.81 REMARK 500 2 VAL A 30 -91.04 -128.29 REMARK 500 2 ASP A 31 100.23 32.95 REMARK 500 2 TYR A 38 109.65 19.85 REMARK 500 2 SER A 43 100.76 167.36 REMARK 500 2 TYR A 44 -27.00 -38.86 REMARK 500 3 ARG A 12 -55.37 -132.76 REMARK 500 3 LYS A 13 -73.44 62.95 REMARK 500 3 ARG A 15 -72.12 -59.33 REMARK 500 3 ASN A 21 57.41 -163.28 REMARK 500 3 CYS A 26 -91.04 -65.44 REMARK 500 3 TYR A 38 138.49 -172.98 REMARK 500 3 LYS A 40 150.15 -47.72 REMARK 500 3 SER A 43 97.18 178.75 REMARK 500 3 TYR A 44 -27.44 -37.80 REMARK 500 4 ARG A 12 -15.60 -146.34 REMARK 500 4 LYS A 13 -94.17 43.71 REMARK 500 4 ASN A 21 64.48 -158.49 REMARK 500 4 CYS A 26 -83.31 -47.26 REMARK 500 4 TYR A 38 140.70 -174.66 REMARK 500 4 LYS A 39 77.69 -111.74 REMARK 500 4 SER A 43 93.10 -171.83 REMARK 500 4 TYR A 44 -36.84 -30.89 REMARK 500 5 ARG A 12 -73.35 -163.87 REMARK 500 5 LYS A 13 -33.23 172.83 REMARK 500 5 GLU A 16 129.95 65.93 REMARK 500 5 THR A 17 3.79 -170.33 REMARK 500 5 ASN A 21 62.08 -160.45 REMARK 500 5 CYS A 26 -86.49 -66.28 REMARK 500 5 TYR A 33 116.97 -1.85 REMARK 500 5 LYS A 40 151.58 -47.75 REMARK 500 5 SER A 43 88.59 -160.42 REMARK 500 5 TYR A 44 -27.80 -37.68 REMARK 500 5 LEU A 51 -70.68 -45.25 REMARK 500 REMARK 500 THIS ENTRY HAS 203 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 12 0.30 SIDE CHAIN REMARK 500 1 ARG A 15 0.27 SIDE CHAIN REMARK 500 2 ARG A 12 0.17 SIDE CHAIN REMARK 500 2 ARG A 15 0.21 SIDE CHAIN REMARK 500 3 ARG A 12 0.26 SIDE CHAIN REMARK 500 3 ARG A 15 0.08 SIDE CHAIN REMARK 500 4 ARG A 12 0.30 SIDE CHAIN REMARK 500 4 ARG A 15 0.27 SIDE CHAIN REMARK 500 5 ARG A 12 0.22 SIDE CHAIN REMARK 500 6 ARG A 15 0.29 SIDE CHAIN REMARK 500 7 ARG A 12 0.16 SIDE CHAIN REMARK 500 7 ARG A 15 0.32 SIDE CHAIN REMARK 500 8 ARG A 15 0.25 SIDE CHAIN REMARK 500 9 ARG A 12 0.17 SIDE CHAIN REMARK 500 9 ARG A 15 0.22 SIDE CHAIN REMARK 500 10 ARG A 12 0.29 SIDE CHAIN REMARK 500 10 ARG A 15 0.26 SIDE CHAIN REMARK 500 11 ARG A 12 0.18 SIDE CHAIN REMARK 500 11 ARG A 15 0.32 SIDE CHAIN REMARK 500 12 ARG A 12 0.22 SIDE CHAIN REMARK 500 12 ARG A 15 0.13 SIDE CHAIN REMARK 500 13 ARG A 12 0.20 SIDE CHAIN REMARK 500 13 ARG A 15 0.22 SIDE CHAIN REMARK 500 14 ARG A 12 0.21 SIDE CHAIN REMARK 500 14 ARG A 15 0.21 SIDE CHAIN REMARK 500 15 ARG A 12 0.31 SIDE CHAIN REMARK 500 15 ARG A 15 0.18 SIDE CHAIN REMARK 500 16 ARG A 15 0.21 SIDE CHAIN REMARK 500 17 ARG A 12 0.17 SIDE CHAIN REMARK 500 17 ARG A 15 0.31 SIDE CHAIN REMARK 500 18 ARG A 12 0.25 SIDE CHAIN REMARK 500 18 ARG A 15 0.32 SIDE CHAIN REMARK 500 19 ARG A 12 0.31 SIDE CHAIN REMARK 500 19 ARG A 15 0.24 SIDE CHAIN REMARK 500 20 ARG A 12 0.31 SIDE CHAIN REMARK 500 20 ARG A 15 0.27 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1QHK A 6 52 UNP Q04740 RNH1_YEAST 6 52 SEQRES 1 A 47 GLY ASN PHE TYR ALA VAL ARG LYS GLY ARG GLU THR GLY SEQRES 2 A 47 ILE TYR ASN THR TRP ASN GLU CYS LYS ASN GLN VAL ASP SEQRES 3 A 47 GLY TYR GLY GLY ALA ILE TYR LYS LYS PHE ASN SER TYR SEQRES 4 A 47 GLU GLN ALA LYS SER PHE LEU GLY HELIX 1 H1 ASN A 24 GLN A 29 1 6 HELIX 2 H2 TYR A 44 LEU A 51 1 8 SHEET 1 S2 1 GLY A 18 THR A 22 0 SHEET 1 S1 1 ASN A 7 VAL A 11 0 SHEET 1 S3 1 TYR A 38 ASN A 42 0 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 2 2 Bytes