Header list of 1io6.pdb file
Complete list - 23 20 Bytes
HEADER SIGNALING PROTEIN 25-JAN-01 1IO6 TITLE GROWTH FACTOR RECEPTOR-BOUND PROTEIN 2 (GRB2) C-TERMINAL SH3 DOMAIN TITLE 2 COMPLEXED WITH A LIGAND PEPTIDE (NMR, MINIMIZED MEAN STRUCTURE) COMPND MOL_ID: 1; COMPND 2 MOLECULE: GROWTH FACTOR RECEPTOR-BOUND PROTEIN 2; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: C-TERMINAL SH3(RESIDUE 159-215); COMPND 5 SYNONYM: GRB2-C-SH3; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: A LIGAND PEPTIDE; COMPND 9 CHAIN: B; COMPND 10 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; 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: PGEX-2T; SOURCE 10 MOL_ID: 2; SOURCE 11 SYNTHETIC: YES; SOURCE 12 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED BY THE SOLID- SOURCE 13 PHASE FMOC STRATEGY. THE SEQUENCE OF THIS PEPTIDE IS ARTIFICIAL AND SOURCE 14 IS NOT NATURALLY FOUND. KEYWDS SIGNAL TRANSDUCTION, SH3 DOMAIN, PROLINE-RICH PEPTIDE, COMPLEX (SH3 KEYWDS 2 DOMAIN-PEPTIDE), SIGNALING PROTEIN EXPDTA SOLUTION NMR MDLTYP MINIMIZED AVERAGE AUTHOR M.KAWASAKI,K.OGURA,H.HATANAKA,F.INAGAKI REVDAT 5 23-FEB-22 1IO6 1 REMARK SEQADV REVDAT 4 24-FEB-09 1IO6 1 VERSN REVDAT 3 21-JAN-03 1IO6 1 REMARK REVDAT 2 14-MAR-01 1IO6 1 EXPDTA REVDAT 1 14-FEB-01 1IO6 0 JRNL AUTH M.KAWASAKI,K.OGURA,S.YUZAWA,H.TERASAWA,H.HATANAKA, JRNL AUTH 2 V.MANDIYAN,J.SCHLESSINGER,F.INAGAKI JRNL TITL SOLUTION STRUCTURE OF THE C-TERMINAL SH3 DOMAIN OF GRB2 JRNL TITL 2 COMPLEXED WITH A LIGAND PEPTIDE: A LIGAND EXCHANGE MODEL OF JRNL TITL 3 THE SH3 DOMAIN JRNL REF TO BE PUBLISHED JRNL REFN REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH D.KOHDA,H.TERASAWA,S.ICHIKAWA,K.OGURA,H.HATANAKA,V.MANDIYAN, REMARK 1 AUTH 2 A.ULLRICH,J.SCHLESSINGER,F.INAGAKI REMARK 1 TITL SOLUTION STRUCTURE AND LIGAND-BINDING SITE OF THE C-TERMINAL REMARK 1 TITL 2 SH3 DOMAIN OF GRB2 REMARK 1 REF STRUCTURE V. 2 1029 1994 REMARK 1 REFN ISSN 0969-2126 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1IO6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-JAN-01. REMARK 100 THE DEPOSITION ID IS D_1000005113. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298. REMARK 210 PH : 7.20 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : NULL REMARK 210 SPECTROMETER MODEL : NULL REMARK 210 SPECTROMETER MANUFACTURER : NULL REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR 3.1 REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: MEAN STRUCTURE. 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: 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 THR A 3 92.45 -45.68 REMARK 500 VAL A 5 -145.39 -151.37 REMARK 500 GLN A 6 118.58 -167.29 REMARK 500 ALA A 7 98.24 -60.11 REMARK 500 GLU A 15 -146.91 -113.39 REMARK 500 ARG A 23 125.37 -38.07 REMARK 500 VAL A 29 103.63 -41.10 REMARK 500 ASP A 31 88.81 -160.09 REMARK 500 ASN A 32 32.42 -85.19 REMARK 500 ALA A 41 -167.24 -114.06 REMARK 500 CYS A 42 -52.87 -158.92 REMARK 500 HIS A 43 47.98 -159.76 REMARK 500 ASN A 58 139.81 77.57 REMARK 500 ARG B 4 145.82 73.58 REMARK 500 LEU B 6 121.85 -33.34 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 ARG A 22 0.21 SIDE CHAIN REMARK 500 ARG A 23 0.13 SIDE CHAIN REMARK 500 ARG A 51 0.29 SIDE CHAIN REMARK 500 ARG A 59 0.12 SIDE CHAIN REMARK 500 ARG B 1 0.17 SIDE CHAIN REMARK 500 ARG B 4 0.24 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1IO6 A 3 59 UNP P62993 GRB2_HUMAN 159 215 DBREF 1IO6 B 1 10 PDB 1IO6 1IO6 1 10 SEQADV 1IO6 GLY A 1 UNP P62993 CLONING ARTIFACT SEQADV 1IO6 SER A 2 UNP P62993 CLONING ARTIFACT SEQRES 1 A 59 GLY SER THR TYR VAL GLN ALA LEU PHE ASP PHE ASP PRO SEQRES 2 A 59 GLN GLU ASP GLY GLU LEU GLY PHE ARG ARG GLY ASP PHE SEQRES 3 A 59 ILE HIS VAL MET ASP ASN SER ASP PRO ASN TRP TRP LYS SEQRES 4 A 59 GLY ALA CYS HIS GLY GLN THR GLY MET PHE PRO ARG ASN SEQRES 5 A 59 TYR VAL THR PRO VAL ASN ARG SEQRES 1 B 10 ARG HIS TYR ARG PRO LEU PRO PRO LEU PRO HELIX 1 GH ARG A 51 TYR A 53 53/10 HELIX 3 SHEET 1 B1 3 ASP A 25 VAL A 29 0 SHEET 2 B1 3 TYR A 4 ALA A 7 -1 O VAL A 5 N ILE A 27 SHEET 3 B1 3 VAL A 54 PRO A 56 -1 O THR A 55 N GLN A 6 SHEET 1 B2 2 PHE A 9 ASP A 12 0 SHEET 2 B2 2 GLY A 20 ARG A 22 -1 O PHE A 21 N PHE A 11 SHEET 1 B3 3 ASP A 31 ASN A 32 0 SHEET 2 B3 3 TRP A 37 CYS A 42 -1 N LYS A 39 O ASP A 31 SHEET 3 B3 3 GLN A 45 PRO A 50 -1 N PHE A 49 O TRP 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
Complete list - 23 20 Bytes