Header list of 2azs.pdb file
Complete list - 9 20 Bytes
HEADER SIGNALING PROTEIN 12-SEP-05 2AZS TITLE NMR STRUCTURE OF THE N-TERMINAL SH3 DOMAIN OF DRK (CALCULATED WITHOUT TITLE 2 NOE RESTRAINTS) COMPND MOL_ID: 1; COMPND 2 MOLECULE: SH2-SH3 ADAPTER PROTEIN DRK; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: N-TERMINAL SH3 DOMAIN, RESIDUES 1-59; COMPND 5 SYNONYM: PROTEIN ENHANCER OF SEVENLESS 2B, DOWNSTREAM OF RECEPTOR COMPND 6 KINASE, PROTEIN ESEV 2B; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER; SOURCE 3 ORGANISM_COMMON: FRUIT FLY; SOURCE 4 ORGANISM_TAXID: 7227; SOURCE 5 GENE: DRK, E SEV 2B; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HMS174; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-11A KEYWDS DROSOPHILA MELANOGASTER, SH3 FRAGMENT, DRK, SIGNALING PROTEIN EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR I.BEZSONOVA,A.U.SINGER,W.-Y.CHOY,M.TOLLINGER,J.D.FORMAN-KAY REVDAT 3 09-MAR-22 2AZS 1 REMARK REVDAT 2 24-FEB-09 2AZS 1 VERSN REVDAT 1 13-DEC-05 2AZS 0 JRNL AUTH I.BEZSONOVA,A.SINGER,W.-Y.CHOY,M.TOLLINGER,J.D.FORMAN-KAY JRNL TITL STRUCTURAL COMPARISON OF THE UNSTABLE DRKN SH3 DOMAIN AND A JRNL TITL 2 STABLE MUTANT JRNL REF BIOCHEMISTRY V. 44 15550 2005 JRNL REFN ISSN 0006-2960 JRNL PMID 16300404 JRNL DOI 10.1021/BI0512795 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.0 REMARK 3 AUTHORS : BRUNGER, A.T. ET AL. REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON RESIDUAL REMARK 3 DIPOLAR COUPLING RESTRAINTS,CARBONYL CHEMICAL SHIFT ANISOTROPY REMARK 3 RESTRAINTS, DIHEDRAL ANGLE RESTRAINTS AND HYDROGEN BOND REMARK 3 RESTRAINTS REMARK 4 REMARK 4 2AZS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-SEP-05. REMARK 100 THE DEPOSITION ID IS D_1000034497. 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 : 500 MM REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 1MM DRKN SH3 DOMAIN 15N, 13C, REMARK 210 500 MM NA2SO4, 50MM PHOSPHATE, REMARK 210 90% H2O, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : H/D AMIDE EXCHANGE; HNCO-BASED REMARK 210 3D EXPERIMENTS (NON-TROSY); 2D REMARK 210 CA-CB RDC EXPERIMENT; CA-HA RDC REMARK 210 EXPERIMENT; HNCO EXPERIMENT; HN- REMARK 210 HA J-COUPLING EXPERIMENT; 3D REMARK 210 HN(CO)HB REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : CNS 1.0 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY 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: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A 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 HA LYS A 6 H THR A 22 1.11 REMARK 500 O LYS A 26 H GLU A 40 1.60 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 HIS A 7 117.12 -164.68 REMARK 500 1 ALA A 11 159.99 -20.77 REMARK 500 1 THR A 12 -65.87 -100.54 REMARK 500 1 PHE A 19 -173.84 -173.36 REMARK 500 1 LEU A 28 -60.80 -91.17 REMARK 500 1 GLU A 31 -58.14 164.36 REMARK 500 1 ASP A 42 19.88 50.85 REMARK 500 1 LYS A 56 41.40 -88.92 REMARK 500 2 PHE A 9 113.53 -164.06 REMARK 500 2 ASP A 14 44.78 -75.38 REMARK 500 2 ASP A 15 -39.17 -155.82 REMARK 500 2 PHE A 19 -169.61 -176.37 REMARK 500 2 THR A 22 -11.74 57.49 REMARK 500 2 GLN A 23 38.81 -68.55 REMARK 500 2 ILE A 24 116.64 41.12 REMARK 500 2 GLU A 31 72.20 42.27 REMARK 500 2 SER A 34 129.25 112.75 REMARK 500 2 ASN A 35 -30.00 94.07 REMARK 500 2 ASP A 42 -86.28 46.70 REMARK 500 3 HIS A 7 110.39 -164.07 REMARK 500 3 ASP A 14 45.62 -75.41 REMARK 500 3 ASP A 15 -39.15 -155.36 REMARK 500 3 THR A 22 -3.88 80.45 REMARK 500 3 GLU A 31 -37.57 75.33 REMARK 500 3 ASP A 33 137.51 17.87 REMARK 500 3 ASP A 42 -90.56 50.71 REMARK 500 3 LYS A 56 44.27 -88.22 REMARK 500 3 ASN A 57 -108.44 -116.98 REMARK 500 3 HIS A 58 120.32 92.42 REMARK 500 4 HIS A 7 114.65 -164.97 REMARK 500 4 PHE A 19 -178.03 -170.39 REMARK 500 4 THR A 22 6.60 80.59 REMARK 500 4 GLU A 31 -10.77 -143.38 REMARK 500 4 ASP A 32 3.14 -61.15 REMARK 500 4 ASP A 33 -110.08 -116.10 REMARK 500 4 SER A 34 -114.58 16.51 REMARK 500 4 ASN A 35 -31.73 -147.58 REMARK 500 4 ASP A 42 -78.83 57.32 REMARK 500 4 HIS A 58 -169.29 27.13 REMARK 500 5 PHE A 9 113.13 -163.06 REMARK 500 5 ASP A 14 43.02 -75.35 REMARK 500 5 ASP A 15 -39.06 -153.71 REMARK 500 5 PHE A 19 -174.90 -173.75 REMARK 500 5 THR A 22 -2.16 57.68 REMARK 500 5 GLN A 23 35.09 -71.96 REMARK 500 5 ILE A 24 125.06 40.43 REMARK 500 5 ASP A 32 -15.96 -43.98 REMARK 500 5 ASP A 33 135.14 106.05 REMARK 500 5 SER A 34 74.79 76.99 REMARK 500 5 ASN A 35 -165.48 -175.92 REMARK 500 REMARK 500 THIS ENTRY HAS 107 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2A36 RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF THE N-TERMINAL SH3 DOMAIN OF DRK (CALCULATED REMARK 900 WITH NOE RESTRAINTS) REMARK 900 RELATED ID: 5925 RELATED DB: BMRB REMARK 900 CO, N AND HN CHEMICAL SHIFTS OF THE N-TERMINAL SH3 DOMAIN OF DRK REMARK 900 RELATED ID: 2A37 RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF THE T22G MUTANT OF THE N-TERMINAL SH3 DOMAIN REMARK 900 OF DRK (CALCULATED WITH NOE RESTRAINTS) REMARK 900 RELATED ID: 5923 RELATED DB: BMRB REMARK 900 CO, N AND HN CHEMICAL SHIFTS OF THE T22G MUTANT OF THE N-TERMINAL REMARK 900 SH3 DOMAIN OF DRK REMARK 900 RELATED ID: 2AZV RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF THE T22G MUTANT OF N-TERMINAL SH3 DOMAIN OF REMARK 900 DRK (CALCULATED WITHOUT NOES) DBREF 2AZS A 1 59 UNP Q08012 DRK_DROME 1 59 SEQRES 1 A 59 MET GLU ALA ILE ALA LYS HIS ASP PHE SER ALA THR ALA SEQRES 2 A 59 ASP ASP GLU LEU SER PHE ARG LYS THR GLN ILE LEU LYS SEQRES 3 A 59 ILE LEU ASN MET GLU ASP ASP SER ASN TRP TYR ARG ALA SEQRES 4 A 59 GLU LEU ASP GLY LYS GLU GLY LEU ILE PRO SER ASN TYR SEQRES 5 A 59 ILE GLU MET LYS ASN HIS ASP SHEET 1 A 5 LYS A 44 PRO A 49 0 SHEET 2 A 5 TRP A 36 LEU A 41 -1 N LEU A 41 O LYS A 44 SHEET 3 A 5 GLN A 23 ASN A 29 -1 N LYS A 26 O GLU A 40 SHEET 4 A 5 GLU A 2 ALA A 5 -1 N ALA A 3 O LEU A 25 SHEET 5 A 5 ILE A 53 MET A 55 -1 O GLU A 54 N ILE A 4 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 - 9 20 Bytes