Header list of 1qg1.pdb file
Complete list - 2 20 Bytes
HEADER HORMONE/GROWTH FACTOR 19-APR-99 1QG1 TITLE GROWTH FACTOR RECEPTOR BINDING PROTEIN SH2 DOMAIN COMPLEXED WITH AN TITLE 2 SHC-DERIVED PEPTIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (GROWTH FACTOR RECEPTOR BINDING PROTEIN); COMPND 3 CHAIN: E; COMPND 4 FRAGMENT: SH2; COMPND 5 SYNONYM: GRB2-SH2; COMPND 6 ENGINEERED: YES; COMPND 7 OTHER_DETAILS: RESIDUES HIS-58 - THR-159 AND THE EXTRINSIC N-TERMINAL COMPND 8 TWO RESIDUES, GLY-56 AND SER-57; COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: PROTEIN (SHC-DERIVED PEPTIDE); COMPND 11 CHAIN: I; COMPND 12 FRAGMENT: 423-435; COMPND 13 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; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PGEX-4T-2; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: BL21 (DE3); SOURCE 9 EXPRESSION_SYSTEM_GENE: PROTEIN WAS EXPRESSED WITH PGEX-4T-2 VECTOR SOURCE 10 AND BL21 (DE3) CELL AS GST-FUSION PROTEIN, AND CLEAVED WITH TRYPSIN; SOURCE 11 MOL_ID: 2; SOURCE 12 SYNTHETIC: YES; SOURCE 13 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED BY THE SOLID- SOURCE 14 PHASE FMOC STRATEGY. THE SEQUENCE OF THIS PEPTIDE IS NATURALLY FOUND SOURCE 15 IN HOMO SAPIENS (HUMAN). KEYWDS SIGNAL TRANSDUCTION, SH2 DOMAIN, PHOSPHOTYROSYL PEPTIDE, COMPLEX KEYWDS 2 (SIGNAL TRANSDUCTION-PEPTIDE), HORMONE-GROWTH FACTOR COMPLEX EXPDTA SOLUTION NMR AUTHOR K.OGURA REVDAT 5 02-MAR-22 1QG1 1 REMARK SEQADV LINK REVDAT 4 24-FEB-09 1QG1 1 VERSN REVDAT 3 01-APR-03 1QG1 1 JRNL REVDAT 2 17-JUN-99 1QG1 1 JRNL REVDAT 1 27-APR-99 1QG1 0 JRNL AUTH K.OGURA,S.TSUCHIYA,H.TERASAWA,S.YUZAWA,H.HATANAKA, JRNL AUTH 2 V.MANDIYAN,J.SCHLESSINGER,F.INAGAKI JRNL TITL SOLUTION STRUCTURE OF THE SH2 DOMAIN OF GRB2 COMPLEXED WITH JRNL TITL 2 THE SHC-DERIVED PHOSPHOTYROSINE-CONTAINING PEPTIDE. JRNL REF J.MOL.BIOL. V. 289 439 1999 JRNL REFN ISSN 0022-2836 JRNL PMID 10356320 JRNL DOI 10.1006/JMBI.1999.2792 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 1QG1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-APR-99. REMARK 100 THE DEPOSITION ID IS D_1000000886. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 301 REMARK 210 PH : 6.3 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 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 : NULL 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: E, I 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 ANGLES 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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) 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 ATM2 ATM3 REMARK 500 GLY E 1 N - CA - C ANGL. DEV. = 24.3 DEGREES 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 SER E 2 -147.83 -162.15 REMARK 500 TRP E 5 -37.80 -149.88 REMARK 500 LYS E 9 68.77 -118.72 REMARK 500 GLN E 22 177.35 -51.53 REMARK 500 ALA E 27 137.34 -36.48 REMARK 500 GLU E 32 57.66 -96.62 REMARK 500 SER E 33 94.84 34.53 REMARK 500 SER E 41 -177.85 -170.71 REMARK 500 ASN E 48 -23.33 158.47 REMARK 500 LEU E 65 57.22 -176.41 REMARK 500 TRP E 66 -78.01 159.18 REMARK 500 VAL E 67 -74.02 -133.58 REMARK 500 SER E 84 -170.55 -52.55 REMARK 500 VAL E 85 -36.62 -138.93 REMARK 500 GLU E 97 -175.93 41.34 REMARK 500 GLN E 98 -14.05 73.99 REMARK 500 VAL E 99 169.47 48.12 REMARK 500 GLN E 101 112.33 1.10 REMARK 500 GLN E 102 10.73 98.69 REMARK 500 SER I 4 -177.27 77.53 REMARK 500 VAL I 6 -68.82 -5.77 REMARK 500 VAL I 8 123.18 -9.30 REMARK 500 ASN I 10 166.57 -43.03 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 E 12 0.32 SIDE CHAIN REMARK 500 ARG E 81 0.28 SIDE CHAIN REMARK 500 ARG E 87 0.22 SIDE CHAIN REMARK 500 ARG E 94 0.27 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1QG1 E 3 104 UNP P62993 GRB2_HUMAN 58 159 DBREF 1QG1 I 1 13 UNP P29353 SHC1_HUMAN 423 435 SEQADV 1QG1 GLY E 1 UNP P62993 CLONING ARTIFACT SEQADV 1QG1 SER E 2 UNP P62993 CLONING ARTIFACT SEQADV 1QG1 PTR I 5 UNP P29353 TYR 427 MODIFIED RESIDUE SEQRES 1 E 104 GLY SER HIS PRO TRP PHE PHE GLY LYS ILE PRO ARG ALA SEQRES 2 E 104 LYS ALA GLU GLU MET LEU SER LYS GLN ARG HIS ASP GLY SEQRES 3 E 104 ALA PHE LEU ILE ARG GLU SER GLU SER ALA PRO GLY ASP SEQRES 4 E 104 PHE SER LEU SER VAL LYS PHE GLY ASN ASP VAL GLN HIS SEQRES 5 E 104 PHE LYS VAL LEU ARG ASP GLY ALA GLY LYS TYR PHE LEU SEQRES 6 E 104 TRP VAL VAL LYS PHE ASN SER LEU ASN GLU LEU VAL ASP SEQRES 7 E 104 TYR HIS ARG SER THR SER VAL SER ARG ASN GLN GLN ILE SEQRES 8 E 104 PHE LEU ARG ASP ILE GLU GLN VAL PRO GLN GLN PRO THR SEQRES 1 I 13 ASP ASP PRO SER PTR VAL ASN VAL GLN ASN LEU ASP LYS MODRES 1QG1 PTR I 5 TYR O-PHOSPHOTYROSINE HET PTR I 5 24 HETNAM PTR O-PHOSPHOTYROSINE HETSYN PTR PHOSPHONOTYROSINE FORMUL 2 PTR C9 H12 N O6 P HELIX 1 1 PRO E 11 LEU E 19 1 9 HELIX 2 2 SER E 72 THR E 83 1 12 SHEET 1 A 4 ASP E 49 LYS E 54 0 SHEET 2 A 4 SER E 41 PHE E 46 -1 O LEU E 42 N PHE E 53 SHEET 3 A 4 ALA E 27 ARG E 31 -1 O ALA E 27 N LYS E 45 SHEET 4 A 4 PHE E 6 GLY E 8 1 N PHE E 7 O ILE E 30 SHEET 1 A1 4 ASP E 49 LYS E 54 0 SHEET 2 A1 4 SER E 41 PHE E 46 -1 O LEU E 42 N PHE E 53 SHEET 3 A1 4 ALA E 27 ARG E 31 -1 O ALA E 27 N LYS E 45 SHEET 4 A1 4 ARG E 94 ASP E 95 1 O ARG E 94 N PHE E 28 SHEET 1 B 3 LEU E 56 ARG E 57 0 SHEET 2 B 3 TYR E 63 PHE E 64 -1 O PHE E 64 N LEU E 56 SHEET 3 B 3 LYS E 69 PHE E 70 -1 O PHE E 70 N TYR E 63 LINK C SER I 4 N PTR I 5 1555 1555 1.30 LINK C PTR I 5 N VAL I 6 1555 1555 1.31 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 - 2 20 Bytes