Header list of 1ija.pdb file
Complete list - b 5 2 Bytes
HEADER PROTEIN BINDING 25-APR-01 1IJA TITLE STRUCTURE OF SORTASE COMPND MOL_ID: 1; COMPND 2 MOLECULE: SORTASE; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: CATALYTIC DOMAIN (RESIDUES 60-206); COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS; SOURCE 3 ORGANISM_TAXID: 1280; SOURCE 4 STRAIN: OS2; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET9A KEYWDS EIGHT STRANDED BETA BARREL, TRANSPEPTIDASE, PROTEIN BINDING EXPDTA SOLUTION NMR NUMMDL 25 AUTHOR U.ILANGOVAN,H.TON-THAT,J.IWAHARA,O.SCHNEEWIND,R.T.CLUBB REVDAT 4 05-FEB-20 1IJA 1 REMARK SEQADV REVDAT 3 24-FEB-09 1IJA 1 VERSN REVDAT 2 16-MAY-01 1IJA 1 JRNL REVDAT 1 09-MAY-01 1IJA 0 JRNL AUTH U.ILANGOVAN,H.TON-THAT,J.IWAHARA,O.SCHNEEWIND,R.T.CLUBB JRNL TITL STRUCTURE OF SORTASE, THE TRANSPEPTIDASE THAT ANCHORS JRNL TITL 2 PROTEINS TO THE CELL WALL OF STAPHYLOCOCCUS AUREUS. JRNL REF PROC.NATL.ACAD.SCI.USA V. 98 6056 2001 JRNL REFN ISSN 0027-8424 JRNL PMID 11371637 JRNL DOI 10.1073/PNAS.101064198 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.6, X-PLOR 3.843 REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER, T.A. (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF REMARK 3 2105 EXPERIMENTAL RESTRAINTS, 1852 NOE-DERIVED DISTANCE REMARK 3 RESTRAINTS, 195 DIHEDRAL ANGLE RESTRAINTS, 58 COUPLING CONSTANT REMARK 3 RESTAINTS REMARK 4 REMARK 4 1IJA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-APR-01. REMARK 100 THE DEPOSITION ID IS D_1000013326. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 308 REMARK 210 PH : 6.2 REMARK 210 IONIC STRENGTH : 100 MM NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 2.5 MM SORTASE 15N,13C; 50 MM REMARK 210 TRIS (PH 6.2); 20 MM CACL2; 100 REMARK 210 MM NACL; 3 MM DTT; 93 % H2O; 7 % REMARK 210 D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N_EDITED_NOESY; REMARK 210 4D_15N/13C_EDITED_NOESY; 3D_13C_ REMARK 210 EDITED_NOESY; 4D_13C/13C_EDITED_ REMARK 210 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 : NMRPIPE 1.7, NMRVIEW 4.1.3, X REMARK 210 -PLOR 3.843 REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 150 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE REMARK 210 COVALENT GEOMETRY,STRUCTURES REMARK 210 WITH FAVORABLE NON-BOND ENERGY, REMARK 210 STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THIS 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 HG1 THR A 63 HZ1 LYS A 76 1.34 REMARK 500 O THR A 73 HZ3 LYS A 76 1.41 REMARK 500 O GLN A 38 H ARG A 41 1.46 REMARK 500 O ASP A 107 H GLY A 109 1.53 REMARK 500 OG1 THR A 63 HZ1 LYS A 76 1.55 REMARK 500 O TYR A 30 HG SER A 44 1.58 REMARK 500 H ALA A 46 O SER A 58 1.58 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 LYS A 4 58.16 -152.14 REMARK 500 1 PRO A 5 -160.31 -69.44 REMARK 500 1 LYS A 9 -7.55 -59.48 REMARK 500 1 LYS A 11 -5.68 -57.21 REMARK 500 1 LYS A 26 80.58 -164.64 REMARK 500 1 ALA A 34 88.04 -43.22 REMARK 500 1 GLN A 38 -62.39 -93.34 REMARK 500 1 LEU A 39 -18.66 -46.26 REMARK 500 1 GLN A 55 -20.00 -42.31 REMARK 500 1 THR A 63 87.36 -153.06 REMARK 500 1 ARG A 67 70.01 -150.05 REMARK 500 1 PRO A 68 18.64 -54.38 REMARK 500 1 TYR A 70 -153.90 -130.07 REMARK 500 1 GLN A 71 -89.66 -62.46 REMARK 500 1 ALA A 78 170.22 -56.30 REMARK 500 1 ASN A 90 53.92 -116.16 REMARK 500 1 THR A 98 18.85 -153.11 REMARK 500 1 SER A 99 87.45 -170.14 REMARK 500 1 ASP A 102 -16.60 -43.64 REMARK 500 1 VAL A 103 -112.26 -59.50 REMARK 500 1 VAL A 108 46.61 -67.75 REMARK 500 1 LEU A 111 -33.39 -139.99 REMARK 500 1 LYS A 115 -155.68 -64.68 REMARK 500 1 LYS A 117 -121.61 -95.99 REMARK 500 1 LYS A 119 150.63 -38.52 REMARK 500 1 GLU A 137 -77.54 -40.28 REMARK 500 1 ARG A 139 79.48 -151.03 REMARK 500 1 VAL A 147 -153.19 -91.97 REMARK 500 2 PRO A 5 -125.80 -42.52 REMARK 500 2 PRO A 8 150.58 -42.33 REMARK 500 2 SER A 12 30.81 -98.48 REMARK 500 2 LYS A 26 81.35 -168.97 REMARK 500 2 ALA A 34 87.75 -40.85 REMARK 500 2 GLN A 38 -69.36 -96.98 REMARK 500 2 GLU A 50 95.77 -62.87 REMARK 500 2 GLN A 55 -14.74 -46.72 REMARK 500 2 HIS A 62 -169.29 -74.53 REMARK 500 2 THR A 63 99.99 -167.84 REMARK 500 2 ARG A 67 75.58 -151.04 REMARK 500 2 PRO A 68 24.12 -51.78 REMARK 500 2 ASN A 69 62.92 -151.70 REMARK 500 2 GLN A 71 -119.23 65.03 REMARK 500 2 PHE A 72 33.35 -87.44 REMARK 500 2 ASN A 90 29.80 -154.27 REMARK 500 2 THR A 98 20.07 -149.44 REMARK 500 2 SER A 99 123.69 -171.37 REMARK 500 2 ARG A 101 -70.80 -86.54 REMARK 500 2 ASP A 102 10.72 51.16 REMARK 500 2 VAL A 103 -93.64 -91.05 REMARK 500 2 PRO A 105 28.89 -73.06 REMARK 500 REMARK 500 THIS ENTRY HAS 753 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4879 RELATED DB: BMRB REMARK 900 4879 IS THE CHEMICAL SHIFT ASSIGNMENTS OF SORTASE DBREF 1IJA A 2 148 UNP Q9S446 Q9S446_STAAU 60 206 SEQADV 1IJA MET A 1 UNP Q9S446 INITIATING METHIONINE SEQRES 1 A 148 MET GLN ALA LYS PRO GLN ILE PRO LYS ASP LYS SER LYS SEQRES 2 A 148 VAL ALA GLY TYR ILE GLU ILE PRO ASP ALA ASP ILE LYS SEQRES 3 A 148 GLU PRO VAL TYR PRO GLY PRO ALA THR PRO GLU GLN LEU SEQRES 4 A 148 ASN ARG GLY VAL SER PHE ALA GLU GLU ASN GLU SER LEU SEQRES 5 A 148 ASP ASP GLN ASN ILE SER ILE ALA GLY HIS THR PHE ILE SEQRES 6 A 148 ASP ARG PRO ASN TYR GLN PHE THR ASN LEU LYS ALA ALA SEQRES 7 A 148 LYS LYS GLY SER MET VAL TYR PHE LYS VAL GLY ASN GLU SEQRES 8 A 148 THR ARG LYS TYR LYS MET THR SER ILE ARG ASP VAL LYS SEQRES 9 A 148 PRO THR ASP VAL GLY VAL LEU ASP GLU GLN LYS GLY LYS SEQRES 10 A 148 ASP LYS GLN LEU THR LEU ILE THR CYS ASP ASP TYR ASN SEQRES 11 A 148 GLU LYS THR GLY VAL TRP GLU LYS ARG LYS ILE PHE VAL SEQRES 12 A 148 ALA THR GLU VAL LYS HELIX 1 1 THR A 35 ASN A 40 1 6 HELIX 2 2 THR A 73 ALA A 78 5 6 SHEET 1 A 9 GLY A 16 ILE A 20 0 SHEET 2 A 9 ILE A 25 TYR A 30 -1 N ILE A 25 O ILE A 20 SHEET 3 A 9 VAL A 43 PHE A 45 1 O VAL A 43 N TYR A 30 SHEET 4 A 9 ASN A 56 HIS A 62 -1 N ALA A 60 O SER A 44 SHEET 5 A 9 GLN A 120 CYS A 126 1 O GLN A 120 N ILE A 57 SHEET 6 A 9 ILE A 141 THR A 145 -1 O PHE A 142 N LEU A 123 SHEET 7 A 9 GLU A 91 ILE A 100 -1 N LYS A 96 O THR A 145 SHEET 8 A 9 MET A 83 VAL A 88 -1 O VAL A 84 N TYR A 95 SHEET 9 A 9 GLY A 16 ILE A 20 -1 O TYR A 17 N LYS A 87 SHEET 1 B 2 TYR A 129 ASN A 130 0 SHEET 2 B 2 VAL A 135 TRP A 136 -1 O VAL A 135 N ASN A 130 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 5 2 Bytes