Header list of 1r57.pdb file
Complete list - v 6 2 Bytes
HEADER TRANSFERASE 09-OCT-03 1R57
TITLE NMR SOLUTION STRUCTURE OF A GCN5-LIKE PUTATIVE N-ACETYLTRANSFERASE
TITLE 2 FROM STAPHYLOCOCCUS AUREUS. NORTHEAST STRUCTURAL GENOMICS CONSORTIUM
TITLE 3 TARGET ZR31
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CONSERVED HYPOTHETICAL PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.3.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 1280;
SOURCE 4 GENE: SA2309 OR MW2441 OR SAV2521;
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: PET21
KEYWDS GCN5, N-ACETYLTRANSFERASE, STRUCTURAL GENOMICS, PSI, PROTEIN
KEYWDS 2 STRUCTURE INITIATIVE, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM,
KEYWDS 3 NESG, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.R.CORT,T.B.ACTON,L.MA,R.B.XIAO,G.T.MONTELIONE,M.A.KENNEDY,NORTHEAST
AUTHOR 2 STRUCTURAL GENOMICS CONSORTIUM (NESG)
REVDAT 8 06-NOV-19 1R57 1 REMARK SEQADV SEQRES
REVDAT 7 09-JUN-09 1R57 1 REVDAT
REVDAT 6 24-FEB-09 1R57 1 VERSN
REVDAT 5 23-DEC-08 1R57 1 JRNL
REVDAT 4 30-SEP-08 1R57 1 JRNL
REVDAT 3 01-JAN-08 1R57 1 AUTHOR JRNL
REVDAT 2 25-JAN-05 1R57 1 AUTHOR KEYWDS REMARK
REVDAT 1 09-MAR-04 1R57 0
JRNL AUTH J.R.CORT,T.A.RAMELOT,D.MURRAY,T.B.ACTON,L.C.MA,R.XIAO,
JRNL AUTH 2 G.T.MONTELIONE,M.A.KENNEDY
JRNL TITL STRUCTURE OF AN ACETYL-COA BINDING PROTEIN FROM
JRNL TITL 2 STAPHYLOCOCCUS AUREUS REPRESENTING A NOVEL SUBFAMILY OF
JRNL TITL 3 GCN5-RELATED N-ACETYLTRANSFERASE-LIKE PROTEINS.
JRNL REF J.STRUCT.FUNCT.GENOM. V. 9 7 2008
JRNL REFN ISSN 1345-711X
JRNL PMID 18709443
JRNL DOI 10.1007/S10969-008-9041-Z
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AUTOSTRUCTURE 1.1, CNS 1.1
REMARK 3 AUTHORS : HUANG, TEJERO, MONTELIONE (AUTOSTRUCTURE), BRUNGER
REMARK 3 (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 BACKBONE AND SIDECHAIN ASSIGNMENTS WERE DETERMINED MANUALLY FROM
REMARK 3 TRIPLE-RESONANCE NMR DATA.
REMARK 3 NOE DISTANCE RESTRAINTS WERE DERIVED AUTOMATICALLY FROM PEAK-
REMARK 3 PICKED DATA WITH AUTOSTRUCTURE, THEN ERROR-CHECKED AND CORRECTED
REMARK 3 MANUALLY.
REMARK 3 THE STRUCTURE IS BASED ON 848 RESTRAINTS: 710 MEANINGFUL DISTANCE
REMARK 3 RESTRAINTS, 58 HYDROGEN BOND RESTRAINTS, AND 80 DIHEDRAL ANGLE
REMARK 3 RESTRAINTS.
REMARK 3 THERE ARE 9.5 RESTRAINTS PER RESTRAINED RESIDUE.
REMARK 3 PHI DIHEDRAL RESTRAINTS WERE DERIVED FROM THE HNHA EXPERIMENT AND
REMARK 3 TALOS.
REMARK 3 PSI DIHEDRAL RESTRAINTS WERE DERIVED FROM NOE RATIOS, SECONDARY
REMARK 3 STRUCTURE PROPENSITIES EVIDENT IN PRELIMINARY STRUCTURES, ALPHA
REMARK 3 CARBON CHEMICAL SHIFTS, AND TALOS.
REMARK 3 RESIDUES 44-51 COMPRISE A POORLY-DEFINED LOOP IN THIS ENSEMBLE OF
REMARK 3 STRUCTURES.
REMARK 3 RESIDUES 1-3 AND 94-102 ARE UNSTRUCTURED TERMINI.
REMARK 4
REMARK 4 1R57 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-OCT-03.
REMARK 100 THE DEPOSITION ID IS D_1000020451.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : .115
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM PROTEIN U-15N,13C; 20 MM
REMARK 210 MES, 100 MM NACL, 5 MM CACL2,
REMARK 210 0.02% NAN3; 95% H2O, 5% D2O; 1
REMARK 210 MM PROTEIN U-15N,13C, 20 MM MES,
REMARK 210 100 MM NACL, 5 MM CACL2, 0.02%
REMARK 210 NAN3; 100% D2O; 0.4 MM PROTEIN U-
REMARK 210 15N,5%-13C; 20 MM MES, 100 MM
REMARK 210 NACL, 5 MM CACL2, 0.02% NAN3; 95%
REMARK 210 H2O, 5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA; HNHB; 4D_
REMARK 210 13C-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS 1.1, FELIX 97, SPARKY 3,
REMARK 210 TALOS
REMARK 210 METHOD USED : AUTOMATED GENERATION OF INITIAL
REMARK 210 DISTANCE RESTRAINT SET DISTANCE
REMARK 210 GEOMETRY SIMULATED ANNEALING
REMARK 210 FINAL REFINEMENT IN EXPLICIT
REMARK 210 SOLVENT
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH FEWEST RESTRAINT
REMARK 210 VIOLATIONS AND LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: AMIDE PROTON EXCHANGE WAS MEASURED BY DISSOLVING A
REMARK 210 LYOPHILIZED PROTONATED SAMPLE IN D2O
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 HZ2 LYS A 12 OE1 GLU A 25 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 GLU A 10 94.11 -64.26
REMARK 500 1 ASN A 21 31.72 -88.10
REMARK 500 1 ASP A 32 -79.44 -125.45
REMARK 500 1 ASN A 33 -86.66 -135.60
REMARK 500 1 LEU A 47 19.17 -140.94
REMARK 500 2 SER A 2 -77.45 -166.94
REMARK 500 2 LEU A 4 39.25 -85.35
REMARK 500 2 ASP A 32 78.26 -151.82
REMARK 500 2 ASN A 33 -84.20 49.17
REMARK 500 2 GLN A 50 140.69 69.84
REMARK 500 2 LEU A 93 -138.21 -94.61
REMARK 500 2 HIS A 101 -54.63 -157.36
REMARK 500 3 ASN A 21 49.87 -105.75
REMARK 500 3 ASP A 32 -159.53 -141.70
REMARK 500 4 LEU A 4 30.07 -92.76
REMARK 500 4 ASN A 21 49.60 -108.20
REMARK 500 4 ALA A 24 89.37 -154.95
REMARK 500 4 ASP A 32 -91.21 -119.62
REMARK 500 4 ASN A 33 -77.92 -128.22
REMARK 500 4 ASP A 45 33.26 -76.03
REMARK 500 4 LEU A 47 -22.17 73.34
REMARK 500 5 SER A 2 156.64 70.30
REMARK 500 5 ASN A 3 12.75 -140.04
REMARK 500 5 LEU A 4 -151.72 -121.48
REMARK 500 5 GLU A 5 -178.34 68.15
REMARK 500 5 ASP A 32 -82.43 -133.37
REMARK 500 5 ASN A 33 -64.90 -125.49
REMARK 500 5 ASN A 68 71.16 59.10
REMARK 500 5 ASP A 90 -44.09 -164.39
REMARK 500 5 HIS A 101 -35.12 -146.25
REMARK 500 6 SER A 2 -83.18 66.38
REMARK 500 6 ASN A 3 25.31 -159.58
REMARK 500 6 GLU A 10 98.88 -66.93
REMARK 500 6 ALA A 24 109.07 -161.49
REMARK 500 6 GLU A 96 -78.88 -130.28
REMARK 500 6 HIS A 100 -79.05 -84.44
REMARK 500 7 LEU A 4 -94.45 -116.29
REMARK 500 7 GLU A 5 135.08 66.56
REMARK 500 7 ASP A 32 52.59 -153.07
REMARK 500 7 ASN A 33 -77.29 66.65
REMARK 500 7 LEU A 47 -61.67 -140.53
REMARK 500 7 HIS A 98 98.03 -65.68
REMARK 500 8 SER A 2 -72.43 -133.28
REMARK 500 8 GLU A 10 85.05 -58.76
REMARK 500 8 ASN A 21 39.61 -92.87
REMARK 500 8 ASP A 32 -88.52 -122.85
REMARK 500 8 ASN A 33 -65.93 -123.91
REMARK 500 8 LEU A 95 32.10 -91.39
REMARK 500 8 HIS A 97 -37.21 174.34
REMARK 500 8 HIS A 99 -161.06 53.92
REMARK 500
REMARK 500 THIS ENTRY HAS 128 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5845 RELATED DB: BMRB
REMARK 900 CHEMICAL SHIFTS AND COUPLING CONSTANTS
REMARK 900 RELATED ID: NESG-ZR31 RELATED DB: TARGETDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE PROTEIN THAT IS THE SUBJECT OF THIS STRUCTURE
REMARK 999 DETERMINATION WAS CLONED FROM STAPHYLOCOCCUS AUREUS
REMARK 999 SUBSP. ROSENBACH. THIS STRAIN HAS NOT BEEN THE
REMARK 999 SUBJECT OF GENOME SEQUENCING, HOWEVER THREE OTHER
REMARK 999 STRAINS HAVE BEEN SEQUENCED: MW2, MU50,AND N315.
REMARK 999 THE AMINO ACID RESIDUES AT THREE POSITIONS IN THE
REMARK 999 PROTEIN STRUCTURE DESCRIBED HERE DIFFER FROM THOSE
REMARK 999 AT SOME OR ALL OF THE SAME POSITIONS IN THE SEQUENCES
REMARK 999 FROM THE THREE SEQUENCED STRAINS. THESE MUTATIONS,
REMARK 999 INDICATED BY THE NOTATION XNY WHERE THE X IS THE
REMARK 999 RESIDUE IN THE SEQUENCED STRAIN, N IS THE POSITION
REMARK 999 NUMBER, AND Y IS THE RESIDUE IN THE STRUCTURE
REMARK 999 DESCRIBED HERE, ARE AS FOLLOWS:
REMARK 999 STRAIN MW2: V57L AND H68N
REMARK 999 STRAINS MU50 AND N315: H21N, V57L, AND H68N
DBREF 1R57 A 1 94 UNP Q99RB4 Q99RB4_STAAM 1 94
SEQADV 1R57 LEU A 57 UNP Q99RB4 VAL 57 SEE REMARK 999
SEQADV 1R57 ASN A 68 UNP Q99RB4 HIS 68 SEE REMARK 999
SEQADV 1R57 LEU A 95 UNP Q99RB4 EXPRESSION TAG
SEQADV 1R57 GLU A 96 UNP Q99RB4 EXPRESSION TAG
SEQADV 1R57 HIS A 97 UNP Q99RB4 EXPRESSION TAG
SEQADV 1R57 HIS A 98 UNP Q99RB4 EXPRESSION TAG
SEQADV 1R57 HIS A 99 UNP Q99RB4 EXPRESSION TAG
SEQADV 1R57 HIS A 100 UNP Q99RB4 EXPRESSION TAG
SEQADV 1R57 HIS A 101 UNP Q99RB4 EXPRESSION TAG
SEQADV 1R57 HIS A 102 UNP Q99RB4 EXPRESSION TAG
SEQRES 1 A 102 MET SER ASN LEU GLU ILE LYS GLN GLY GLU ASN LYS PHE
SEQRES 2 A 102 TYR ILE GLY ASP ASP GLU ASN ASN ALA LEU ALA GLU ILE
SEQRES 3 A 102 THR TYR ARG PHE VAL ASP ASN ASN GLU ILE ASN ILE ASP
SEQRES 4 A 102 HIS THR GLY VAL SER ASP GLU LEU GLY GLY GLN GLY VAL
SEQRES 5 A 102 GLY LYS LYS LEU LEU LYS ALA VAL VAL GLU HIS ALA ARG
SEQRES 6 A 102 GLU ASN ASN LEU LYS ILE ILE ALA SER CYS SER PHE ALA
SEQRES 7 A 102 LYS HIS MET LEU GLU LYS GLU ASP SER TYR GLN ASP VAL
SEQRES 8 A 102 TYR LEU GLY LEU GLU HIS HIS HIS HIS HIS HIS
HELIX 1 1 VAL A 52 ASN A 68 1 17
HELIX 2 2 CYS A 75 GLU A 85 1 11
HELIX 3 3 ASP A 86 GLN A 89 5 4
SHEET 1 A 5 LYS A 7 GLY A 9 0
SHEET 2 A 5 LYS A 12 GLY A 16 -1 O LYS A 12 N GLY A 9
SHEET 3 A 5 ALA A 22 PHE A 30 -1 O ALA A 24 N ILE A 15
SHEET 4 A 5 GLU A 35 VAL A 43 -1 O ASN A 37 N ARG A 29
SHEET 5 A 5 LYS A 70 ALA A 73 1 O LYS A 70 N ILE A 36
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 - v 6 2 Bytes