Header list of 2b87.pdb file
Complete list - b 26 2 Bytes
HEADER PROTEIN BINDING 06-OCT-05 2B87 TITLE STRUCTURAL BASIS FOR MOLECULAR RECOGNITION IN AN AFFIBODY:AFFIBODY TITLE 2 COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: ZTAQ AFFIBODY; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: ANTI-ZTAQ AFFIBODY; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS; SOURCE 3 ORGANISM_TAXID: 1280; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21 DE3; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28A(+); SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS; SOURCE 11 ORGANISM_TAXID: 1280; SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 13 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 14 EXPRESSION_SYSTEM_STRAIN: BL21 DE3; SOURCE 15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PET28A(+) KEYWDS PROTEIN-PROTEIN INTERACTIONS PROTEIN ENGINEERING, MOLECULAR KEYWDS 2 RECOGNITION, NMR SPECTROSCOPY, INDUCED FIT, AFFIBODY, PROTEIN KEYWDS 3 BINDING EXPDTA SOLUTION NMR NUMMDL 40 AUTHOR C.LENDEL,J.DOGAN,T.HARD REVDAT 4 26-FEB-20 2B87 1 REMARK REVDAT 3 24-FEB-09 2B87 1 VERSN REVDAT 2 04-JUL-06 2B87 1 JRNL REVDAT 1 23-MAY-06 2B87 0 JRNL AUTH C.LENDEL,J.DOGAN,T.HARD JRNL TITL STRUCTURAL BASIS FOR MOLECULAR RECOGNITION IN AN JRNL TITL 2 AFFIBODY:AFFIBODY COMPLEX. JRNL REF J.MOL.BIOL. V. 359 1293 2006 JRNL REFN ISSN 0022-2836 JRNL PMID 16750222 JRNL DOI 10.1016/J.JMB.2006.04.043 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR, X-PLOR REMARK 3 AUTHORS : BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2B87 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-OCT-05. REMARK 100 THE DEPOSITION ID IS D_1000034796. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : NULL REMARK 210 PH : NULL REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : 2.0MM ZTAQ, 1.5MM [U-13C; U-15N] REMARK 210 ANTI-ZTAQ; 1.3MM [U-13C; U-15N] REMARK 210 ZTAQ, 1.6MM ANTIZTAQ REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; 3D_15N- REMARK 210 SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE; INOVA REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE, ANSIG, X-PLOR REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 40 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES REMARK 210 WITH THE LOWEST ENERGY, GOOD REMARK 210 RAMACHANDRAN PLOTS 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: 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: 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 PHE B 5 H ARG B 9 1.49 REMARK 500 O ALA A 48 H ASN A 52 1.55 REMARK 500 O GLU A 8 H ALA A 12 1.59 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 ASN A 21 -5.82 -144.44 REMARK 500 1 ASN B 3 -173.26 -177.88 REMARK 500 2 ASN A 21 -3.73 -142.96 REMARK 500 2 PRO A 57 150.24 -42.01 REMARK 500 2 PHE B 5 7.21 -69.62 REMARK 500 3 ASP B 37 108.58 -167.93 REMARK 500 4 ASN A 21 -4.98 -144.20 REMARK 500 4 PRO A 57 83.90 -46.20 REMARK 500 4 PHE B 5 5.11 -69.11 REMARK 500 5 ASN A 21 -4.42 -144.04 REMARK 500 5 ASP B 37 110.15 -163.64 REMARK 500 6 ASN A 21 -1.99 -144.03 REMARK 500 6 PRO A 57 38.05 -81.97 REMARK 500 7 ASN A 3 74.09 54.06 REMARK 500 7 ASN A 21 -4.34 -143.93 REMARK 500 7 PRO A 57 41.26 -81.49 REMARK 500 7 PRO B 57 41.15 -79.06 REMARK 500 8 ASN A 21 -3.86 -144.31 REMARK 500 8 PHE B 5 8.03 -63.39 REMARK 500 8 PRO B 57 41.19 -82.57 REMARK 500 9 ASN A 21 -2.95 -143.88 REMARK 500 9 PHE B 5 18.65 -66.66 REMARK 500 10 ASN A 21 -2.94 -145.30 REMARK 500 10 PHE B 5 11.60 -66.84 REMARK 500 10 ASP B 37 101.41 -169.24 REMARK 500 10 PRO B 57 35.56 -79.84 REMARK 500 11 ASN A 21 -5.27 -144.32 REMARK 500 11 ASN B 3 -176.16 -63.77 REMARK 500 12 ASN A 21 -2.04 -144.04 REMARK 500 12 PHE B 5 9.70 -63.79 REMARK 500 12 PRO B 57 33.88 -79.65 REMARK 500 13 ASN A 21 -1.08 -145.83 REMARK 500 13 PRO A 57 106.79 -42.80 REMARK 500 13 ASN B 3 -173.85 -179.63 REMARK 500 13 PRO B 57 41.40 -82.24 REMARK 500 14 ASN A 21 -3.13 -144.03 REMARK 500 16 ASN A 21 -4.66 -145.70 REMARK 500 17 LYS B 4 -7.82 -59.72 REMARK 500 17 PHE B 5 7.83 -69.33 REMARK 500 18 ASN A 21 -2.85 -144.09 REMARK 500 18 PHE B 5 21.71 -74.65 REMARK 500 18 ASP B 37 107.11 -169.89 REMARK 500 19 ASN A 21 -3.19 -144.87 REMARK 500 20 ASN A 21 -4.31 -144.42 REMARK 500 20 PRO A 57 93.10 -41.26 REMARK 500 20 ASN B 3 -165.29 -65.74 REMARK 500 20 PRO B 57 40.67 -79.59 REMARK 500 21 ASN A 21 -0.63 -145.36 REMARK 500 21 PRO B 57 37.22 -80.07 REMARK 500 22 ASN A 21 -3.09 -144.54 REMARK 500 REMARK 500 THIS ENTRY HAS 109 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 35 0.31 SIDE CHAIN REMARK 500 1 ARG B 9 0.17 SIDE CHAIN REMARK 500 1 ARG B 18 0.31 SIDE CHAIN REMARK 500 1 ARG B 35 0.31 SIDE CHAIN REMARK 500 2 ARG A 35 0.08 SIDE CHAIN REMARK 500 2 ARG B 9 0.22 SIDE CHAIN REMARK 500 2 ARG B 18 0.31 SIDE CHAIN REMARK 500 2 ARG B 35 0.16 SIDE CHAIN REMARK 500 3 ARG B 9 0.21 SIDE CHAIN REMARK 500 3 ARG B 18 0.28 SIDE CHAIN REMARK 500 3 ARG B 35 0.31 SIDE CHAIN REMARK 500 4 ARG A 35 0.30 SIDE CHAIN REMARK 500 4 ARG B 9 0.29 SIDE CHAIN REMARK 500 4 ARG B 18 0.31 SIDE CHAIN REMARK 500 4 ARG B 35 0.31 SIDE CHAIN REMARK 500 5 ARG B 9 0.23 SIDE CHAIN REMARK 500 5 ARG B 18 0.31 SIDE CHAIN REMARK 500 5 ARG B 35 0.31 SIDE CHAIN REMARK 500 6 ARG A 35 0.31 SIDE CHAIN REMARK 500 6 ARG B 9 0.23 SIDE CHAIN REMARK 500 6 ARG B 18 0.31 SIDE CHAIN REMARK 500 6 ARG B 35 0.31 SIDE CHAIN REMARK 500 7 ARG A 35 0.30 SIDE CHAIN REMARK 500 7 ARG B 9 0.29 SIDE CHAIN REMARK 500 7 ARG B 18 0.23 SIDE CHAIN REMARK 500 7 ARG B 35 0.31 SIDE CHAIN REMARK 500 8 ARG A 35 0.17 SIDE CHAIN REMARK 500 8 ARG B 9 0.22 SIDE CHAIN REMARK 500 8 ARG B 18 0.30 SIDE CHAIN REMARK 500 8 ARG B 35 0.30 SIDE CHAIN REMARK 500 9 ARG A 35 0.31 SIDE CHAIN REMARK 500 9 ARG B 9 0.15 SIDE CHAIN REMARK 500 9 ARG B 18 0.30 SIDE CHAIN REMARK 500 9 ARG B 35 0.31 SIDE CHAIN REMARK 500 10 ARG B 9 0.26 SIDE CHAIN REMARK 500 10 ARG B 18 0.31 SIDE CHAIN REMARK 500 10 ARG B 35 0.31 SIDE CHAIN REMARK 500 11 ARG B 9 0.20 SIDE CHAIN REMARK 500 11 ARG B 18 0.25 SIDE CHAIN REMARK 500 11 ARG B 35 0.31 SIDE CHAIN REMARK 500 12 ARG A 35 0.31 SIDE CHAIN REMARK 500 12 ARG B 9 0.19 SIDE CHAIN REMARK 500 12 ARG B 18 0.31 SIDE CHAIN REMARK 500 12 ARG B 35 0.31 SIDE CHAIN REMARK 500 13 ARG B 9 0.15 SIDE CHAIN REMARK 500 13 ARG B 18 0.27 SIDE CHAIN REMARK 500 13 ARG B 35 0.31 SIDE CHAIN REMARK 500 14 ARG A 35 0.17 SIDE CHAIN REMARK 500 14 ARG B 9 0.19 SIDE CHAIN REMARK 500 14 ARG B 18 0.31 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 147 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 6806 RELATED DB: BMRB REMARK 900 NMR ASSIGNMENT REMARK 900 RELATED ID: 2B88 RELATED DB: PDB REMARK 900 STRUCTURE FREE ZTAQ SUBUNIT REMARK 900 RELATED ID: 2B89 RELATED DB: PDB REMARK 900 STRUCTURE FREE ANTI-ZTAQ SUBUNIT DBREF 2B87 A 2 58 UNP Q70AB8 Q70AB8_STAAU 117 173 DBREF 2B87 B 2 58 UNP Q70AB8 Q70AB8_STAAU 117 173 SEQRES 1 A 58 VAL ASP ASN LYS PHE ASN LYS GLU LEU GLY TRP ALA THR SEQRES 2 A 58 TRP GLU ILE PHE ASN LEU PRO ASN LEU ASN GLY VAL GLN SEQRES 3 A 58 VAL LYS ALA PHE ILE ASP SER LEU ARG ASP ASP PRO SER SEQRES 4 A 58 GLN SER ALA ASN LEU LEU ALA GLU ALA LYS LYS LEU ASN SEQRES 5 A 58 ASP ALA GLN ALA PRO LYS SEQRES 1 B 58 VAL ASP ASN LYS PHE ASN LYS GLU ARG VAL ILE ALA ILE SEQRES 2 B 58 GLY GLU ILE MET ARG LEU PRO ASN LEU ASN SER LEU GLN SEQRES 3 B 58 VAL VAL ALA PHE ILE ASN SER LEU ARG ASP ASP PRO SER SEQRES 4 B 58 GLN SER ALA ASN LEU LEU ALA GLU ALA LYS LYS LEU ASN SEQRES 5 B 58 ASP ALA GLN ALA PRO LYS HELIX 1 1 ASN A 3 ASN A 18 1 16 HELIX 2 2 ASN A 23 ASP A 37 1 15 HELIX 3 3 GLN A 40 ALA A 56 1 17 HELIX 4 4 LYS B 4 LEU B 19 1 16 HELIX 5 5 ASN B 23 ASP B 37 1 15 HELIX 6 6 GLN B 40 ALA B 56 1 17 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 26 2 Bytes