Header list of 1qxf.pdb file
Complete list - r 2 2 Bytes
HEADER RIBOSOME 05-SEP-03 1QXF TITLE SOLUTION STRUCTURE OF 30S RIBOSOMAL PROTEIN S27E FROM ARCHAEOGLOBUS TITLE 2 FULGIDUS: GR2, A NESG TARGET PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: 30S RIBOSOMAL PROTEIN S27E; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: GR2; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ARCHAEOGLOBUS FULGIDUS; SOURCE 3 ORGANISM_TAXID: 2234; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS STRUCTURAL GENOMICS, BETA SHEET, PSI, PROTEIN STRUCTURE INITIATIVE, KEYWDS 2 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG, RIBOSOME EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR C.HERVE DU PENHOAT,H.S.ATREYA,Y.SHEN,G.LIU,T.B.ACTON,R.XIAO, AUTHOR 2 G.T.MONTELIONE,T.SZYPERSKI,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM AUTHOR 3 (NESG) REVDAT 5 02-MAR-22 1QXF 1 REMARK SEQADV REVDAT 4 24-FEB-09 1QXF 1 VERSN REVDAT 3 25-JAN-05 1QXF 1 AUTHOR KEYWDS REMARK REVDAT 2 04-MAY-04 1QXF 1 JRNL REVDAT 1 16-SEP-03 1QXF 0 SPRSDE 16-SEP-03 1QXF 1NVH JRNL AUTH C.HERVE DU PENHOAT,H.S.ATREYA,Y.SHEN,G.LIU,T.B.ACTON,R.XIAO, JRNL AUTH 2 Z.LI,D.MURRAY,G.T.MONTELIONE,T.SZYPERSKI JRNL TITL THE NMR SOLUTION STRUCTURE OF THE 30S RIBOSOMAL PROTEIN S27E JRNL TITL 2 ENCODED IN GENE RS27_ARCFU OF ARCHAEOGLOBUS FULGIDIS REVEALS JRNL TITL 3 A NOVEL PROTEIN FOLD JRNL REF PROTEIN SCI. V. 13 1407 2004 JRNL REFN ISSN 0961-8368 JRNL PMID 15096641 JRNL DOI 10.1110/PS.03589204 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CYANA 1.05 REMARK 3 AUTHORS : GUNTERT, P. REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1QXF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-SEP-03. REMARK 100 THE DEPOSITION ID IS D_1000020185. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : 1.0 ATM REMARK 210 SAMPLE CONTENTS : 0.8 MM GR2 (100% 15N, 100% 13C), REMARK 210 20 MM MES, 100 MM NACL, 5 MM REMARK 210 CACL2, 10 MM DTT, 0.02% NAN3; REMARK 210 0.8 MM, GR2 (100% 15N, 5% 13C), REMARK 210 20 MM MES, 100 MM NACL, 5 MM REMARK 210 CACL2, 10 MM DTT, 0.02% NAN3 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_ 15N REMARK 210 -SEPARATED_NOESY; 3D HNCACB; 3D REMARK 210 HCCH-COSY RD; 3D HABCAB(CO)NH RD; REMARK 210 3D HNHA; 3D HNCO; 2D 1H-1H REMARK 210 NOESY; 2D C13HSQC; CONSTANT TIME REMARK 210 GCHSQC; NON-CONSTANT TIME GCHSQC REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DYANA 1.5, MOLMOL 1.0, XEASY REMARK 210 1.3.3 REMARK 210 METHOD USED : DYANA 1.5 WITH 30,000 TAD STEPS REMARK 210 AND SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE RD (REDUCED DIMENSIONALITY) EXPERIMENTS ARE FROM REMARK 210 SZYPERSKI ET AL., PROC. NATL. ACAD. SCI. USA, VOL. 99, PP 8014 REMARK 210 (2002) 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 MODELS 1-20 REMARK 465 RES C SSSEQI REMARK 465 LEU A 59 REMARK 465 GLU A 60 REMARK 465 HIS A 61 REMARK 465 HIS A 62 REMARK 465 HIS A 63 REMARK 465 HIS A 64 REMARK 465 HIS A 65 REMARK 465 HIS A 66 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 8 H GLN A 17 1.52 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 22 64.63 68.14 REMARK 500 1 PRO A 23 -169.48 -75.04 REMARK 500 1 ILE A 31 -78.97 -76.40 REMARK 500 1 THR A 40 -159.22 39.01 REMARK 500 1 LYS A 43 100.82 63.35 REMARK 500 1 LYS A 47 39.44 -92.00 REMARK 500 1 ILE A 51 -63.01 -95.12 REMARK 500 1 GLU A 52 -170.49 -179.25 REMARK 500 2 SER A 3 132.46 61.82 REMARK 500 2 HIS A 22 64.86 65.40 REMARK 500 2 ILE A 31 -79.98 -77.81 REMARK 500 2 THR A 40 -163.78 42.59 REMARK 500 2 LYS A 43 107.97 -169.08 REMARK 500 2 LYS A 47 41.13 -94.03 REMARK 500 2 GLU A 52 -166.73 171.71 REMARK 500 3 SER A 3 118.07 -38.76 REMARK 500 3 HIS A 22 64.19 68.44 REMARK 500 3 PRO A 23 -167.46 -74.98 REMARK 500 3 ILE A 31 -82.46 -80.36 REMARK 500 3 THR A 40 169.50 -45.99 REMARK 500 3 LYS A 47 37.15 -91.29 REMARK 500 3 GLU A 52 -172.13 177.35 REMARK 500 4 SER A 3 121.48 -39.57 REMARK 500 4 HIS A 22 70.87 -156.33 REMARK 500 4 ILE A 31 -80.65 -77.73 REMARK 500 4 LYS A 47 40.76 -95.52 REMARK 500 4 ILE A 51 -69.78 -102.49 REMARK 500 5 SER A 24 -35.45 89.32 REMARK 500 5 ILE A 31 -77.91 -77.76 REMARK 500 5 LYS A 43 110.28 72.48 REMARK 500 5 LYS A 47 39.69 -94.15 REMARK 500 5 GLU A 52 -168.52 177.57 REMARK 500 6 SER A 3 158.46 -43.92 REMARK 500 6 HIS A 22 64.17 68.17 REMARK 500 6 SER A 24 -34.53 89.25 REMARK 500 6 ILE A 31 -84.16 -82.82 REMARK 500 6 LYS A 43 68.44 -161.42 REMARK 500 6 LYS A 47 42.00 -95.08 REMARK 500 6 ILE A 51 -69.64 -100.43 REMARK 500 6 GLU A 52 -175.25 -174.36 REMARK 500 7 SER A 3 127.53 75.77 REMARK 500 7 ASP A 21 37.76 -87.92 REMARK 500 7 HIS A 22 63.09 176.98 REMARK 500 7 SER A 24 -37.12 88.99 REMARK 500 7 ILE A 31 -82.30 -79.79 REMARK 500 7 LYS A 43 41.56 -167.99 REMARK 500 7 LYS A 47 41.67 -91.22 REMARK 500 7 GLU A 52 -168.91 175.43 REMARK 500 8 SER A 3 157.41 64.45 REMARK 500 8 HIS A 22 63.66 -157.33 REMARK 500 REMARK 500 THIS ENTRY HAS 140 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: GR2 RELATED DB: TARGETDB DBREF 1QXF A 1 58 UNP O28935 RS27_ARCFU 1 58 SEQADV 1QXF LEU A 59 UNP O28935 CLONING ARTIFACT SEQADV 1QXF GLU A 60 UNP O28935 CLONING ARTIFACT SEQADV 1QXF HIS A 61 UNP O28935 EXPRESSION TAG SEQADV 1QXF HIS A 62 UNP O28935 EXPRESSION TAG SEQADV 1QXF HIS A 63 UNP O28935 EXPRESSION TAG SEQADV 1QXF HIS A 64 UNP O28935 EXPRESSION TAG SEQADV 1QXF HIS A 65 UNP O28935 EXPRESSION TAG SEQADV 1QXF HIS A 66 UNP O28935 EXPRESSION TAG SEQRES 1 A 66 MET HIS SER ARG PHE VAL LYS VAL LYS CYS PRO ASP CYS SEQRES 2 A 66 GLU HIS GLU GLN VAL ILE PHE ASP HIS PRO SER THR ILE SEQRES 3 A 66 VAL LYS CYS ILE ILE CYS GLY ARG THR VAL ALA GLU PRO SEQRES 4 A 66 THR GLY GLY LYS GLY ASN ILE LYS ALA GLU ILE ILE GLU SEQRES 5 A 66 TYR VAL ASP GLN ILE GLU LEU GLU HIS HIS HIS HIS HIS SEQRES 6 A 66 HIS SHEET 1 A 3 GLU A 16 PHE A 20 0 SHEET 2 A 3 PHE A 5 LYS A 9 -1 N VAL A 8 O GLN A 17 SHEET 3 A 3 GLU A 49 GLU A 52 -1 O GLU A 52 N LYS A 7 SHEET 1 B 3 VAL A 27 LYS A 28 0 SHEET 2 B 3 THR A 35 GLU A 38 -1 O VAL A 36 N VAL A 27 SHEET 3 B 3 ASN A 45 ILE A 46 -1 O ASN A 45 N GLU A 38 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