Header list of 1aze.pdb file
Complete list - 3 20 Bytes
HEADER COMPLEX (ADAPTOR PROTEIN/PEPTIDE) 17-NOV-97 1AZE TITLE NMR STRUCTURE OF THE COMPLEX BETWEEN THE C32S-Y7V MUTANT OF THE NSH3 TITLE 2 DOMAIN OF GRB2 WITH A PEPTIDE FROM SOS, 10 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: GRB2; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: N-TERMINAL SH3 DOMAIN, RESIDUES 1 - 55; COMPND 5 SYNONYM: ASH, GROWTH FACTOR RECEPTOR-BOUND PROTEIN 2; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: SOS; COMPND 10 CHAIN: B; COMPND 11 FRAGMENT: BINDING SITE IN H-SOS, PEPTIDE VPPPVPPRRR; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 ORGAN: FRUIT; SOURCE 6 GENE: GRB2; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER; SOURCE 9 ORGANISM_COMMON: FRUIT FLY; SOURCE 10 ORGANISM_TAXID: 7227 KEYWDS COMPLEX (ADAPTOR PROTEIN-PEPTIDE), SH3 DOMAIN, GUANINE-NUCLEOTIDE KEYWDS 2 RELEASING FACTOR, COMPLEX (ADAPTOR PROTEIN-PEPTIDE) COMPLEX EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR M.VIDAL,E.GINCEL,N.GOUDREAU,F.CORNILLE,F.PARKER,M.DUCHESNE,B.TOCQUE, AUTHOR 2 C.GARBAY,B.P.ROQUES REVDAT 3 03-NOV-21 1AZE 1 REMARK SEQADV REVDAT 2 24-FEB-09 1AZE 1 VERSN REVDAT 1 18-MAY-99 1AZE 0 JRNL AUTH M.VIDAL,N.GOUDREAU,F.CORNILLE,D.CUSSAC,E.GINCEL,C.GARBAY JRNL TITL MOLECULAR AND CELLULAR ANALYSIS OF GRB2 SH3 DOMAIN MUTANTS: JRNL TITL 2 INTERACTION WITH SOS AND DYNAMIN. JRNL REF J.MOL.BIOL. V. 290 717 1999 JRNL REFN ISSN 0022-2836 JRNL PMID 10395825 JRNL DOI 10.1006/JMBI.1999.2899 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH N.GOUDREAU,F.CORNILLE,M.DUCHESNE,F.PARKER,B.TOCQUE,C.GARBAY, REMARK 1 AUTH 2 B.P.ROQUES REMARK 1 TITL NMR STRUCTURE OF THE N-TERMINAL SH3 DOMAIN OF GRB2 AND ITS REMARK 1 TITL 2 COMPLEX WITH A PROLINE-RICH PEPTIDE FROM SOS REMARK 1 REF NAT.STRUCT.BIOL. V. 1 898 1994 REMARK 1 REFN ISSN 1072-8368 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DISCOVER 2.95 REMARK 3 AUTHORS : BIOSYM REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1AZE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000171441. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 293 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : NACL 100MM REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : H2O, PHOSPHATE BUFFER 20MM, NACL REMARK 210 100MM REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : AMX600 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : BRUKER UXNMR + DISCOVER DISCOVER REMARK 210 METHOD USED : SIMULATED ANNEALING ENERGY REMARK 210 MINIMIZATION REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : BEST ENERGY, LEAST RESTRAINT REMARK 210 VIOLATION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL 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: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 1 LYS A 56 C LYS A 56 OXT 0.134 REMARK 500 2 LYS A 56 C LYS A 56 OXT 0.134 REMARK 500 3 LYS A 56 C LYS A 56 OXT 0.135 REMARK 500 4 LYS A 56 C LYS A 56 OXT 0.136 REMARK 500 5 LYS A 56 C LYS A 56 OXT 0.137 REMARK 500 6 LYS A 56 C LYS A 56 OXT 0.133 REMARK 500 7 LYS A 56 C LYS A 56 OXT 0.134 REMARK 500 8 LYS A 56 C LYS A 56 OXT 0.132 REMARK 500 9 LYS A 56 C LYS A 56 OXT 0.134 REMARK 500 10 LYS A 56 C LYS A 56 OXT 0.134 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 ASP A 15 -44.52 -158.97 REMARK 500 1 SER A 32 -57.67 -168.45 REMARK 500 1 LEU A 41 -74.25 -71.04 REMARK 500 1 ASN A 42 -59.31 -167.59 REMARK 500 1 ARG B 9 130.27 83.80 REMARK 500 2 ASP A 15 39.27 -156.24 REMARK 500 2 ASP A 33 86.74 -156.13 REMARK 500 2 ASN A 35 49.47 -82.51 REMARK 500 2 ARG B 9 158.51 83.37 REMARK 500 3 ALA A 13 144.09 -170.41 REMARK 500 3 ASP A 15 -61.57 -162.12 REMARK 500 3 LYS A 20 -123.60 -97.38 REMARK 500 3 GLU A 30 -70.27 -54.88 REMARK 500 3 SER A 32 118.27 74.71 REMARK 500 3 ASN A 42 -62.53 -13.32 REMARK 500 3 MET A 55 -80.36 -63.36 REMARK 500 4 ASP A 15 -40.65 -170.09 REMARK 500 4 LYS A 20 -93.81 -100.73 REMARK 500 4 ARG A 21 127.50 -172.70 REMARK 500 4 LEU A 28 -105.81 -90.00 REMARK 500 4 ASN A 29 -75.37 -150.36 REMARK 500 4 SER A 32 -65.38 69.71 REMARK 500 4 ASN A 35 -43.05 -170.68 REMARK 500 4 TYR A 52 39.66 -85.88 REMARK 500 4 GLU A 54 -80.74 -69.80 REMARK 500 4 MET A 55 83.55 52.96 REMARK 500 5 THR A 12 -70.48 -88.77 REMARK 500 5 ASP A 15 -46.64 -155.90 REMARK 500 5 LEU A 28 -76.73 -89.79 REMARK 500 5 GLU A 31 -51.20 -123.05 REMARK 500 5 SER A 32 -82.68 -159.31 REMARK 500 5 ASN A 42 -45.22 -159.61 REMARK 500 5 ASN A 51 -53.75 -159.97 REMARK 500 5 MET A 55 94.62 -66.82 REMARK 500 6 ASP A 8 91.50 -69.92 REMARK 500 6 ASP A 15 -47.73 -165.78 REMARK 500 6 LEU A 28 -68.79 -93.68 REMARK 500 6 GLU A 30 -99.68 -173.41 REMARK 500 6 GLU A 31 -55.08 -132.34 REMARK 500 6 SER A 32 -75.17 -161.72 REMARK 500 6 ASP A 33 50.90 -148.46 REMARK 500 6 ASN A 42 -56.65 -176.41 REMARK 500 6 ASN A 51 -60.00 -165.13 REMARK 500 6 ARG B 8 -72.41 -69.31 REMARK 500 7 THR A 12 -42.28 -132.95 REMARK 500 7 GLU A 31 -73.21 -46.92 REMARK 500 7 SER A 32 -158.51 59.61 REMARK 500 7 GLN A 34 -61.05 -137.56 REMARK 500 7 ASN A 35 -12.07 104.02 REMARK 500 7 LEU A 41 -90.61 -108.79 REMARK 500 REMARK 500 THIS ENTRY HAS 77 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 TYR A 37 0.10 SIDE CHAIN REMARK 500 3 TYR A 37 0.10 SIDE CHAIN REMARK 500 4 TYR A 37 0.10 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1AZE A 1 56 UNP P62993 GRB2_HUMAN 1 56 DBREF 1AZE B 1 9 UNP P26675 SOS_DROME 1342 1350 SEQADV 1AZE VAL A 7 UNP P62993 TYR 7 ENGINEERED MUTATION SEQADV 1AZE SER A 32 UNP P62993 CYS 32 ENGINEERED MUTATION SEQRES 1 A 56 MET GLU ALA ILE ALA LYS VAL ASP PHE LYS ALA THR ALA SEQRES 2 A 56 ASP ASP GLU LEU SER PHE LYS ARG GLY ASP ILE LEU LYS SEQRES 3 A 56 VAL LEU ASN GLU GLU SER ASP GLN ASN TRP TYR LYS ALA SEQRES 4 A 56 GLU LEU ASN GLY LYS ASP GLY PHE ILE PRO LYS ASN TYR SEQRES 5 A 56 ILE GLU MET LYS SEQRES 1 B 10 VAL PRO PRO PRO VAL PRO PRO ARG ARG ARG SHEET 1 A 4 GLU A 2 ILE A 4 0 SHEET 2 A 4 ILE A 24 ASN A 29 -1 N LEU A 25 O ALA A 3 SHEET 3 A 4 TRP A 36 GLU A 40 -1 N GLU A 40 O LYS A 26 SHEET 4 A 4 ASP A 45 PRO A 49 -1 N ILE A 48 O TYR A 37 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 - 3 20 Bytes