Header list of 1xpn.pdb file
Complete list - r 25 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 08-OCT-04 1XPN TITLE NMR STRUCTURE OF P. AERUGINOSA PROTEIN PA1324: NORTHEAST STRUCTURAL TITLE 2 GENOMICS CONSORTIUM TARGET PAP1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN PA1324; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA; SOURCE 3 ORGANISM_TAXID: 208964; SOURCE 4 STRAIN: PAO1; SOURCE 5 GENE: PA1324; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET28B KEYWDS B-BARREL, STRUCTURAL GENOMICS, NORTHEAST STRUCTURAL GENOMICS KEYWDS 2 CONSORTIUM, NESG, PROTEIN STRUCTURE INITIATIVE, PSI, UNKNOWN KEYWDS 3 FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR J.R.CORT,S.NI,E.E.LOCKERT,G.T.MONTELIONE,M.A.KENNEDY,NORTHEAST AUTHOR 2 STRUCTURAL GENOMICS CONSORTIUM (NESG) REVDAT 5 13-JUL-11 1XPN 1 VERSN REVDAT 4 24-NOV-10 1XPN 1 JRNL REVDAT 3 24-FEB-09 1XPN 1 VERSN REVDAT 2 06-SEP-05 1XPN 1 AUTHOR JRNL REVDAT 1 23-NOV-04 1XPN 0 JRNL AUTH K.A.MERCIER,J.R.CORT,M.A.KENNEDY,E.E.LOCKERT,S.NI, JRNL AUTH 2 M.D.SHORTRIDGE,R.POWERS JRNL TITL STRUCTURE AND FUNCTION OF PSEUDOMONAS AERUGINOSA PROTEIN JRNL TITL 2 PA1324 (21-170). JRNL REF PROTEIN SCI. V. 18 606 2009 JRNL REFN ISSN 0961-8368 JRNL PMID 19241370 JRNL DOI 10.1002/PRO.62 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NIH-XPLOR 2.0.4, CNS 1.1 REMARK 3 AUTHORS : BRUNGER, CLORE, KUSZEWSKI, SCHWIETERS, TJANDRA REMARK 3 (NIH-XPLOR), BRUNGER, ADAMS, CLORE, DELANO, GROS, REMARK 3 GROSSE-KUNSTLEVE, JIANG, KUSZEWSKI, NILGES, PANNU, REMARK 3 READ, RICE, SIMONSON, WARREN (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NOE DISTANCE RESTRAINTS WERE DETERMINED REMARK 3 AUTOMATICALLY USING AUTOSTRUCTURE (G.T. MONTELIONE & Y.J. HUANG) REMARK 3 STARTING FROM PEAK-PICKED NOESY DATA AND CHEMICAL SHIFT REMARK 3 ASSIGNMENTS. FINAL REFINEMENT WAS CONDUCTED IN EXPLICIT SOLVENT REMARK 3 WITH LEONARD-JONES AND ELECTROSTATIC POTENTIALS. RESIDUES 1-26 REMARK 3 ARE UNRESTRAINED AND CONSTITUTE A FLEXIBLE, N-TERMINAL TAIL. THE REMARK 3 STRUCTURE OF RESIDUES 27-170 IS RESTRAINED BY 1861 NOE DISTANCE REMARK 3 RESTRAINTS (541 INTRARESIDUE, 513 SEQUENTIAL, 190 MEDIUM RANGE, REMARK 3 AND 617 LONG RANGE (N>4)), 132 DIHEDRAL RESTRAINTS (65 PHI, 67 REMARK 3 PSI), AND 70 H-BOND RESTRAINTS (FOR 35 H-BONDS). DIHEDRAL REMARK 3 RESTRAINTS WERE DERIVED FROM TALOS AND HNHA. H-BOND RESTRAINTS REMARK 3 WERE DERIVED FROM ANALYSIS OF AMIDES THAT EXCHANGE SLOWLY WITH REMARK 3 D2O SOLVENT TOGETHER WITH INITIAL STRUCTURES DERIVED FROM NOESY REMARK 3 DATA. REMARK 4 REMARK 4 1XPN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-NOV-04. REMARK 100 THE RCSB ID CODE IS RCSB030619. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.8 REMARK 210 IONIC STRENGTH : 300 MM NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1 MM U-13C,15N PA1324, 20 MM REMARK 210 BISTRISPROPANE, 90% H2O, 10% D2O; REMARK 210 1 MM U-13C,15N PA1324, 20 MM REMARK 210 BISTRISPROPANE, 100% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C- REMARK 210 SEPARATED_NOESY; 4D-13C,13C-HMQC- REMARK 210 NOESY-HMQC REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : SPARKY 3.106, AUTOSTRUCTURE REMARK 210 2.1.0, TALOS 2003 REMARK 210 METHOD USED : MOLECULAR DYNAMICS AND SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 20 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY,STRUCTURES WITH THE FEWEST REMARK 210 RESTRAINT VIOLATIONS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 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: 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 SER A 3 88.71 63.08 REMARK 500 1 HIS A 6 -160.70 -112.78 REMARK 500 1 ARG A 16 89.17 65.64 REMARK 500 1 HIS A 19 -91.39 -86.29 REMARK 500 1 ALA A 21 -31.40 71.96 REMARK 500 1 GLN A 40 110.13 178.42 REMARK 500 1 VAL A 41 109.72 -55.02 REMARK 500 1 TYR A 51 123.02 -174.74 REMARK 500 1 LYS A 61 -71.73 -71.63 REMARK 500 1 PHE A 83 -84.04 -108.28 REMARK 500 1 ASP A 114 -77.72 -61.96 REMARK 500 1 GLN A 115 -36.09 -135.95 REMARK 500 1 HIS A 123 64.90 61.32 REMARK 500 1 ASP A 142 -46.74 72.97 REMARK 500 1 PRO A 163 105.14 -43.30 REMARK 500 2 HIS A 6 147.08 177.12 REMARK 500 2 ARG A 16 -12.63 -145.04 REMARK 500 2 SER A 18 30.21 -83.65 REMARK 500 2 HIS A 19 14.46 -142.20 REMARK 500 2 MET A 20 178.46 63.96 REMARK 500 2 ASP A 26 -75.03 -54.04 REMARK 500 2 GLN A 40 113.41 79.31 REMARK 500 2 TYR A 51 109.83 -170.85 REMARK 500 2 PHE A 83 -94.48 -127.15 REMARK 500 3 ALA A 21 89.94 62.83 REMARK 500 3 PRO A 24 90.47 -64.75 REMARK 500 3 LEU A 27 93.79 67.12 REMARK 500 3 GLN A 40 -111.75 -91.61 REMARK 500 3 ILE A 59 111.40 66.99 REMARK 500 3 LYS A 61 -70.65 -70.62 REMARK 500 3 PHE A 83 -85.51 -96.84 REMARK 500 3 GLN A 115 -36.93 179.71 REMARK 500 3 SER A 141 -164.56 -107.02 REMARK 500 3 ASP A 142 95.34 -63.66 REMARK 500 4 SER A 3 -63.26 68.30 REMARK 500 4 HIS A 6 51.13 -144.05 REMARK 500 4 HIS A 8 15.02 -143.50 REMARK 500 4 SER A 11 98.83 65.00 REMARK 500 4 VAL A 14 92.53 64.34 REMARK 500 4 ASP A 26 -155.84 -125.89 REMARK 500 4 LEU A 27 96.34 54.28 REMARK 500 4 TYR A 51 114.53 -170.65 REMARK 500 4 ILE A 59 112.72 66.82 REMARK 500 4 ASN A 64 75.92 58.78 REMARK 500 4 ASN A 85 79.76 57.98 REMARK 500 4 ASP A 114 -148.71 -122.35 REMARK 500 4 ASP A 142 -83.47 65.04 REMARK 500 5 SER A 3 102.01 -59.16 REMARK 500 5 HIS A 6 64.12 -158.72 REMARK 500 5 ALA A 21 -63.42 -145.63 REMARK 500 REMARK 500 THIS ENTRY HAS 236 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: PAP1 RELATED DB: TARGETDB DBREF 1XPN A 21 170 UNP Q9I420 Q9I420_PSEAE 21 170 SEQADV 1XPN GLY A 1 UNP Q9I420 EXPRESSION TAG SEQADV 1XPN SER A 2 UNP Q9I420 EXPRESSION TAG SEQADV 1XPN SER A 3 UNP Q9I420 EXPRESSION TAG SEQADV 1XPN HIS A 4 UNP Q9I420 EXPRESSION TAG SEQADV 1XPN HIS A 5 UNP Q9I420 EXPRESSION TAG SEQADV 1XPN HIS A 6 UNP Q9I420 EXPRESSION TAG SEQADV 1XPN HIS A 7 UNP Q9I420 EXPRESSION TAG SEQADV 1XPN HIS A 8 UNP Q9I420 EXPRESSION TAG SEQADV 1XPN HIS A 9 UNP Q9I420 EXPRESSION TAG SEQADV 1XPN SER A 10 UNP Q9I420 EXPRESSION TAG SEQADV 1XPN SER A 11 UNP Q9I420 EXPRESSION TAG SEQADV 1XPN GLY A 12 UNP Q9I420 EXPRESSION TAG SEQADV 1XPN LEU A 13 UNP Q9I420 EXPRESSION TAG SEQADV 1XPN VAL A 14 UNP Q9I420 EXPRESSION TAG SEQADV 1XPN PRO A 15 UNP Q9I420 EXPRESSION TAG SEQADV 1XPN ARG A 16 UNP Q9I420 EXPRESSION TAG SEQADV 1XPN GLY A 17 UNP Q9I420 EXPRESSION TAG SEQADV 1XPN SER A 18 UNP Q9I420 EXPRESSION TAG SEQADV 1XPN HIS A 19 UNP Q9I420 EXPRESSION TAG SEQADV 1XPN MET A 20 UNP Q9I420 EXPRESSION TAG SEQADV 1XPN GLY A 43 UNP Q9I420 GLU 43 CONFLICT SEQRES 1 A 170 GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU SEQRES 2 A 170 VAL PRO ARG GLY SER HIS MET ALA SER ASN PRO ASN ASP SEQRES 3 A 170 LEU PRO ASP PHE PRO GLU HIS GLU TYR ALA ALA THR GLN SEQRES 4 A 170 GLN VAL GLY GLY GLY VAL ILE ASN GLY ASP LEU TYR LEU SEQRES 5 A 170 THR SER ALA SER GLY ALA ILE GLN LYS GLY THR ASN THR SEQRES 6 A 170 LYS VAL ALA LEU GLU PRO ALA THR SER TYR MET LYS ALA SEQRES 7 A 170 TYR TYR ALA LYS PHE GLY ASN LEU ASP ALA ALA LYS ARG SEQRES 8 A 170 ASP PRO ASP VAL GLN PRO PRO VAL LEU ASP PRO ARG ARG SEQRES 9 A 170 ALA THR TYR VAL ARG GLU ALA THR THR ASP GLN ASN GLY SEQRES 10 A 170 ARG PHE ASP PHE ASP HIS ILE PRO ASN GLY THR TYR TYR SEQRES 11 A 170 ILE SER SER GLU LEU THR TRP SER ALA GLN SER ASP GLY SEQRES 12 A 170 LYS THR ILE THR GLU GLY GLY THR VAL THR LYS LEU VAL SEQRES 13 A 170 THR VAL SER GLY SER GLN PRO GLN LYS VAL LEU LEU THR SEQRES 14 A 170 ARG HELIX 1 1 GLU A 32 ALA A 37 5 6 HELIX 2 2 SER A 74 PHE A 83 1 10 HELIX 3 3 ALA A 89 ARG A 91 5 3 HELIX 4 4 ARG A 103 VAL A 108 1 6 SHEET 1 A 3 ARG A 118 PHE A 121 0 SHEET 2 A 3 ILE A 46 LEU A 50 -1 N GLY A 48 O PHE A 119 SHEET 3 A 3 GLN A 164 LEU A 168 1 O VAL A 166 N ASN A 47 SHEET 1 B 2 LEU A 52 THR A 53 0 SHEET 2 B 2 ILE A 59 GLN A 60 -1 O GLN A 60 N LEU A 52 SHEET 1 C 5 LEU A 86 ASP A 87 0 SHEET 2 C 5 LYS A 144 VAL A 158 -1 O THR A 151 N LEU A 86 SHEET 3 C 5 GLY A 127 SER A 141 -1 N SER A 141 O LYS A 144 SHEET 4 C 5 THR A 65 PRO A 71 -1 N GLU A 70 O TYR A 130 SHEET 5 C 5 ARG A 109 THR A 113 -1 O ALA A 111 N VAL A 67 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 25 2 Bytes