Header list of 1n7t.pdb file
Complete list - b 23 2 Bytes
HEADER SIGNALING PROTEIN 16-NOV-02 1N7T TITLE ERBIN PDZ DOMAIN BOUND TO A PHAGE-DERIVED PEPTIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: 99-MER PEPTIDE OF DENSIN-180-LIKE PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: ERBIN PDZ DOMAIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: PHAGE-DERIVED PEPTIDE; COMPND 8 CHAIN: B; COMPND 9 ENGINEERED: YES; COMPND 10 OTHER_DETAILS: THE PEPTIDE IS RELATED TO THE C-TERMINI OF THE P120- COMPND 11 LIKE CATENINS. SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: ERBIN; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B; SOURCE 11 MOL_ID: 2; SOURCE 12 SYNTHETIC: YES; SOURCE 13 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. IT WAS SOURCE 14 SELECTED FROM A PHAGE DISPLAY LIBRARY. KEYWDS PDZ DOMAIN, C-TERMINAL PEPTIDE COMPLEX, HIGH AFFNITY LIGAND, KEYWDS 2 SIGNALING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR N.J.SKELTON,M.F.T.KOEHLER,K.ZOBEL,W.L.WONG,S.YEH,M.T.PISABARRO, AUTHOR 2 J.P.YIN,L.A.LASKY,S.S.SIDHU REVDAT 4 23-FEB-22 1N7T 1 REMARK SEQADV REVDAT 3 24-FEB-09 1N7T 1 VERSN REVDAT 2 15-FEB-05 1N7T 1 JRNL REVDAT 1 28-JAN-03 1N7T 0 JRNL AUTH N.J.SKELTON,M.F.T.KOEHLER,K.ZOBEL,W.L.WONG,S.YEH, JRNL AUTH 2 M.T.PISABARRO,J.P.YIN,L.A.LASKY,S.S.SIDHU JRNL TITL ORIGINS OF PDZ DOMAIN LIGAND SPECIFICITY. STRUCTURE JRNL TITL 2 DETERMINATION AND MUTAGENESIS OF THE ERBIN PDZ DOMAIN. JRNL REF J.BIOL.CHEM. V. 278 7645 2003 JRNL REFN ISSN 0021-9258 JRNL PMID 12446668 JRNL DOI 10.1074/JBC.M209751200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.1, CNS 2000.1 REMARK 3 AUTHORS : BRUKER (XWINNMR), ACCELRYS (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE COMPLEX WAS DETERMINED USING A TOTAL OF 1717 NOE DISTANCE REMARK 3 RESTRAINTS REMARK 3 (148 INTRA RESIDUE, 339 SEQUENTIAL, 328 MEDIUM RANGE, 699 LONG- REMARK 3 RANGE AND 203 INTERMOLECULAR), REMARK 3 36 HYDROGEN BOND RESTRAINTS, REMARK 3 156 DIHEDRAL ANGLE RESTRAINTS (86 PHI, 44 PSI AND 26 CHI-1) REMARK 3 AND 82 15N RESIDUAL DIPOLAR COUPLING RESTRAINTS. REMARK 3 THE BEST 20 CONFORMERS (OF 100) HAD NO DISTANCE VIOLATIONS GREATER REMARK 3 THAN 0.12A REMARK 3 AND NO DIHEDRAL ANGLE VIOLATIONS GREATER THAN 3.0 DEGREES. REMARK 3 RMSD FROM EXPERIMENTAL DISTANCE RESTRAINTS WAS 0.0055+/-0.0007. REMARK 3 THE MEAN BACKBONE RMSD FROM THE MEAN STRUCTURE WAS 0.40+/- 0.05 A REMARK 3 FOR N, CA AND C ATOMS OF RESIDUES 10-100. REMARK 3 74% (25%) OF RESIDUES WERE IN THE MOST FAVOURED (ALLOWED) REGION REMARK 3 OF PHI/PSI SPACE; REMARK 3 NO RESIDUES WERE IN THE DISALLOWED REGION. REMARK 4 REMARK 4 1N7T COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-NOV-02. REMARK 100 THE DEPOSITION ID IS D_1000017626. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298; 298; 298; 298 REMARK 210 PH : 6.5; 6.5; 6.5; 6.5 REMARK 210 IONIC STRENGTH : 250 MM; 250 MM; 250 MM; 250 MM REMARK 210 PRESSURE : 1 ATM; 1 ATM; 1 ATM; 1 ATM REMARK 210 SAMPLE CONTENTS : 2 MM ERBIN PDZ (15N) + 2.2 MM REMARK 210 PEPTIDE; 25 MM SODIUM PHOSPHATE REMARK 210 PH 6.5; 50 MM SODIUM CHLORIDE; 2 REMARK 210 MM ERBIN PDZ (15N,13C) + 2.2 MM REMARK 210 PEPTIDE; 25 MM SODIUM PHOSPHATE REMARK 210 PH 6.5; 50 MM SODIUM CHLORIDE; 2 REMARK 210 MM ERBIN PDZ (15N,13C) + 2.2 MM REMARK 210 PEPTIDE; 25 MM SODIUM PHOSPHATE REMARK 210 PH 6.5; 50 MM SODIUM CHLORIDE; 2 REMARK 210 MM ERBIN PDZ (15N) + 2.2 MM REMARK 210 PEPTIDE; 25 MM SODIUM PHOSPHATE REMARK 210 PH 6.5; 50 MM SODIUM CHLORIDE; REMARK 210 15 MG/ML PF1 PHAGE REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; HNHA; 3D REMARK 210 HNHB; 3D 15N-SEPARATED LOW REMARK 210 MIXING TIME TOCSY; 2D-15N- REMARK 210 FILTERED NOESY; 3D_13C-SEPARATED_ REMARK 210 NOESY; 3D-13_FILTERED, 13C- REMARK 210 EDITED NOESY; 2D-13C-FILTERED REMARK 210 NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : FELIX 98 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS, REMARK 210 SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST VIOLATION OF EXPERIMENTAL REMARK 210 RESTRAINTS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 2 REMARK 210 REMARK 210 REMARK: THE RESONANCE ASSIGNMENTS WERE DETERMINED USING TRIPLE REMARK 210 -RESONANCE NMR 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 ALA A 9 -171.17 -171.00 REMARK 500 1 ASP A 20 89.06 -166.98 REMARK 500 1 PRO A 37 34.90 -92.85 REMARK 500 1 GLN A 51 -68.09 -103.91 REMARK 500 1 PRO A 55 -70.03 -60.20 REMARK 500 1 ALA A 56 43.40 -99.02 REMARK 500 1 LEU A 59 -69.52 -91.62 REMARK 500 1 ASN A 70 29.00 46.47 REMARK 500 1 GLN A 90 -137.75 -65.65 REMARK 500 1 TRP B 303 -42.25 -169.89 REMARK 500 2 SER A 2 -47.28 -162.44 REMARK 500 2 ALA A 9 44.20 -144.48 REMARK 500 2 LYS A 10 -179.27 -174.65 REMARK 500 2 ASP A 20 84.02 -175.29 REMARK 500 2 GLN A 51 -67.89 -102.66 REMARK 500 2 PRO A 55 -76.43 -58.26 REMARK 500 2 SER A 57 -67.25 -107.35 REMARK 500 2 ASN A 76 62.36 61.23 REMARK 500 2 PHE A 89 172.70 -48.98 REMARK 500 2 GLN A 90 -143.46 -84.31 REMARK 500 3 ALA A 9 -158.43 -102.14 REMARK 500 3 ASP A 20 85.52 -173.97 REMARK 500 3 GLN A 51 -69.95 -102.86 REMARK 500 3 LEU A 59 -65.11 -92.23 REMARK 500 3 GLN A 90 -131.40 -62.59 REMARK 500 3 ASN A 91 -72.28 -82.59 REMARK 500 4 GLU A 7 66.80 -113.90 REMARK 500 4 ALA A 9 47.88 -102.25 REMARK 500 4 ASP A 20 84.87 -175.10 REMARK 500 4 ASN A 36 142.30 -173.54 REMARK 500 4 PRO A 37 39.87 -90.42 REMARK 500 4 PHE A 38 -53.44 -125.62 REMARK 500 4 GLN A 51 -70.41 -97.13 REMARK 500 4 LEU A 59 -72.61 -92.04 REMARK 500 4 ASN A 76 73.78 62.54 REMARK 500 4 PHE A 89 172.81 -47.87 REMARK 500 4 GLN A 90 -138.00 -92.50 REMARK 500 4 ASN A 91 -74.97 -78.96 REMARK 500 5 LEU A 8 -84.74 -106.79 REMARK 500 5 ALA A 9 35.58 -174.96 REMARK 500 5 ASP A 20 86.87 -163.59 REMARK 500 5 ASN A 36 132.69 -170.74 REMARK 500 5 PRO A 37 44.15 -91.52 REMARK 500 5 PHE A 38 -57.77 -122.84 REMARK 500 5 GLN A 51 -68.17 -104.87 REMARK 500 5 PRO A 55 -76.11 -57.05 REMARK 500 5 SER A 57 -63.27 -99.73 REMARK 500 5 PRO A 62 79.06 -63.79 REMARK 500 5 ASP A 64 -158.25 -96.24 REMARK 500 5 ASN A 70 29.27 46.72 REMARK 500 REMARK 500 THIS ENTRY HAS 213 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE PHAGE-DERIVED PEPTIDE, CHAIN B, REMARK 999 IS DE NOVO DESIGN. NO SEQUENCE REMARK 999 DATABASE REFERENCE IS AVAILABLE FOR REMARK 999 THE PEPTIDE. DBREF 1N7T A 5 103 UNP Q96RT1 LAP2_HUMAN 1314 1412 DBREF 1N7T B 301 307 PDB 1N7T 1N7T 301 307 SEQADV 1N7T GLY A 1 UNP Q96RT1 CLONING ARTIFACT SEQADV 1N7T SER A 2 UNP Q96RT1 CLONING ARTIFACT SEQADV 1N7T HIS A 3 UNP Q96RT1 CLONING ARTIFACT SEQADV 1N7T MET A 4 UNP Q96RT1 CLONING ARTIFACT SEQRES 1 A 103 GLY SER HIS MET GLY HIS GLU LEU ALA LYS GLN GLU ILE SEQRES 2 A 103 ARG VAL ARG VAL GLU LYS ASP PRO GLU LEU GLY PHE SER SEQRES 3 A 103 ILE SER GLY GLY VAL GLY GLY ARG GLY ASN PRO PHE ARG SEQRES 4 A 103 PRO ASP ASP ASP GLY ILE PHE VAL THR ARG VAL GLN PRO SEQRES 5 A 103 GLU GLY PRO ALA SER LYS LEU LEU GLN PRO GLY ASP LYS SEQRES 6 A 103 ILE ILE GLN ALA ASN GLY TYR SER PHE ILE ASN ILE GLU SEQRES 7 A 103 HIS GLY GLN ALA VAL SER LEU LEU LYS THR PHE GLN ASN SEQRES 8 A 103 THR VAL GLU LEU ILE ILE VAL ARG GLU VAL SER SER SEQRES 1 B 7 THR GLY TRP GLU THR TRP VAL HELIX 1 1 GLU A 78 PHE A 89 1 12 SHEET 1 A 4 ILE A 13 GLU A 18 0 SHEET 2 A 4 THR A 92 VAL A 98 -1 O LEU A 95 N VAL A 15 SHEET 3 A 4 LYS A 65 ALA A 69 -1 N GLN A 68 O ILE A 96 SHEET 4 A 4 TYR A 72 SER A 73 -1 O TYR A 72 N ALA A 69 SHEET 1 B 3 ILE A 45 PHE A 46 0 SHEET 2 B 3 SER A 26 GLY A 29 -1 N SER A 28 O PHE A 46 SHEET 3 B 3 THR B 305 TRP B 306 -1 O THR B 305 N ILE A 27 CISPEP 1 ASP A 20 PRO A 21 1 0.51 CISPEP 2 ASP A 20 PRO A 21 2 0.42 CISPEP 3 ASP A 20 PRO A 21 3 0.46 CISPEP 4 ASP A 20 PRO A 21 4 0.37 CISPEP 5 ASP A 20 PRO A 21 5 0.47 CISPEP 6 ASP A 20 PRO A 21 6 0.51 CISPEP 7 ASP A 20 PRO A 21 7 0.42 CISPEP 8 ASP A 20 PRO A 21 8 0.24 CISPEP 9 ASP A 20 PRO A 21 9 0.54 CISPEP 10 ASP A 20 PRO A 21 10 0.41 CISPEP 11 ASP A 20 PRO A 21 11 0.65 CISPEP 12 ASP A 20 PRO A 21 12 0.68 CISPEP 13 ASP A 20 PRO A 21 13 0.45 CISPEP 14 ASP A 20 PRO A 21 14 0.50 CISPEP 15 ASP A 20 PRO A 21 15 0.41 CISPEP 16 ASP A 20 PRO A 21 16 0.43 CISPEP 17 ASP A 20 PRO A 21 17 0.62 CISPEP 18 ASP A 20 PRO A 21 18 0.31 CISPEP 19 ASP A 20 PRO A 21 19 0.23 CISPEP 20 ASP A 20 PRO A 21 20 0.19 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 23 2 Bytes