HEADER SIGNALING PROTEIN 12-SEP-05 2AZV
TITLE SOLUTION STRUCTURE OF THE T22G MUTANT OF N-TERMINAL SH3 DOMAIN OF DRK
TITLE 2 (CALCULATED WITHOUT NOES)
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;
COMPND 8 MUTATION: 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 BETA-BARREL, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR I.BEZSONOVA,A.U.SINGER,W.-Y.CHOY,M.TOLLINGER,J.D.FORMAN-KAY
REVDAT 3 20-OCT-21 2AZV 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2AZV 1 VERSN
REVDAT 1 13-DEC-05 2AZV 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 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 2AZV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-SEP-05.
REMARK 100 THE DEPOSITION ID IS D_1000034499.
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 : 50 MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : T22G DRKN SH3 DOMAIN 15N, 13C,
REMARK 210 50MM PHOSPHATE BUFFER, 90% H2O,
REMARK 210 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : CLENEX EXPERIMENT; HNCO-BASED 3D
REMARK 210 EXPERIMENTS (NON-TROSY); 2D CA-
REMARK 210 CB RDC EXPERIMENTS; CA-HA RDC
REMARK 210 EXPERIMENTS; HNCO EXPERIMENT; HN-
REMARK 210 HA J-COUPLING EXPERIMENT
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 HZ1 LYS A 26 HD12 LEU A 28 1.13
REMARK 500 HB1 ALA A 11 HB3 GLU A 16 1.26
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 THR A 12 -76.75 -111.45
REMARK 500 1 ASP A 14 -131.84 47.53
REMARK 500 1 LEU A 28 34.23 -150.92
REMARK 500 1 ASN A 29 -148.84 -80.48
REMARK 500 1 MET A 30 -137.80 -105.66
REMARK 500 1 ASP A 33 66.74 61.16
REMARK 500 1 SER A 34 -151.02 -155.46
REMARK 500 1 ASN A 57 -165.66 63.84
REMARK 500 1 HIS A 58 -108.36 57.21
REMARK 500 2 MET A 30 -146.01 -127.38
REMARK 500 2 GLU A 31 -52.05 44.57
REMARK 500 2 ASP A 33 -60.17 -90.19
REMARK 500 2 SER A 34 -66.02 96.52
REMARK 500 2 LYS A 56 -83.10 47.09
REMARK 500 2 HIS A 58 99.31 88.33
REMARK 500 3 GLU A 2 86.70 -160.69
REMARK 500 3 ALA A 3 -159.94 -111.13
REMARK 500 3 ASP A 15 -4.65 86.79
REMARK 500 3 LEU A 17 -167.38 -114.18
REMARK 500 3 MET A 30 -131.47 -125.42
REMARK 500 3 GLU A 31 -34.76 -131.85
REMARK 500 3 ASP A 33 -64.82 -93.99
REMARK 500 3 SER A 34 -60.08 101.89
REMARK 500 3 GLU A 54 -167.01 -161.01
REMARK 500 3 MET A 55 6.80 -154.53
REMARK 500 3 LYS A 56 -28.03 -148.66
REMARK 500 3 ASN A 57 109.77 72.38
REMARK 500 3 HIS A 58 42.68 -106.38
REMARK 500 4 LYS A 21 -173.94 -50.03
REMARK 500 4 ASN A 29 135.50 152.71
REMARK 500 4 GLU A 31 -42.94 108.72
REMARK 500 4 SER A 34 -72.39 -83.32
REMARK 500 4 LYS A 56 -115.92 -111.91
REMARK 500 4 ASN A 57 77.94 48.16
REMARK 500 4 HIS A 58 -129.94 62.36
REMARK 500 5 ALA A 13 -149.35 -164.48
REMARK 500 5 ASP A 14 95.63 -12.84
REMARK 500 5 ASP A 15 87.04 1.28
REMARK 500 5 MET A 30 42.82 -95.92
REMARK 500 5 GLU A 31 45.82 74.70
REMARK 500 5 ASP A 33 -117.87 64.30
REMARK 500 5 SER A 34 -148.97 22.65
REMARK 500 5 LYS A 56 -119.54 -91.04
REMARK 500 5 ASN A 57 -1.95 84.55
REMARK 500 5 HIS A 58 159.65 174.25
REMARK 500 6 ASP A 15 4.58 86.17
REMARK 500 6 ASN A 29 103.60 24.47
REMARK 500 6 GLU A 31 -32.65 108.38
REMARK 500 6 ASP A 33 -63.32 -93.80
REMARK 500 6 SER A 34 -57.25 100.91
REMARK 500
REMARK 500 THIS ENTRY HAS 84 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5923 RELATED DB: BMRB
REMARK 900 HN, N, CO CHEMICAL SHIFTS OF THE T22G MUTANT OF THE DRKN SH3 DOMAIN
REMARK 900 RELATED ID: 2A37 RELATED DB: PDB
REMARK 900 NMR SOLUTION STRUCTURE OF THE T22G DRKN SH3 DOMAIN CALCULATED WITH
REMARK 900 NOES
REMARK 900 RELATED ID: 2A36 RELATED DB: PDB
REMARK 900 NMR SOLUTION STRUCTURE OF THE WT DRKN SH3 DOMAIN CALCULATED WITH
REMARK 900 NOES
REMARK 900 RELATED ID: 2AZS RELATED DB: PDB
REMARK 900 NMR SOLUTION STRUCTURE OF THE WT DRKN SH3 DOMAIN CALCULATED WITHOUT
REMARK 900 NOES
REMARK 900 RELATED ID: 5925 RELATED DB: BMRB
REMARK 900 HN, N, CO CHEMICAL SHIFTS OF THE WT DRKN SH3 DOMAIN
DBREF 2AZV A 1 59 UNP Q08012 DRK_DROME 1 59
SEQADV 2AZV GLY A 22 UNP Q08012 THR 22 ENGINEERED MUTATION
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 GLY 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 ILE A 24 ILE A 27 -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 GLU A 54 -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
(ATOM LINES ARE NOT SHOWN.)
END
