Header list of 1lmz.pdb file
Complete list - r 25 2 Bytes
HEADER HYDROLASE 02-MAY-02 1LMZ
TITLE SOLUTION STRUCTURE OF 3-METHYLADENINE DNA GLYCOSYLASE I (TAG)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 3-METHYLADENINE DNA GLYCOSYLASE I (TAG);
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.2.2.20;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 37762;
SOURCE 4 STRAIN: B;
SOURCE 5 GENE: TAG;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21A (NOVAGEN)
KEYWDS HELIX-HAIRPIN-HELIX SUPERFAMILY, DNA GLYCOSYLASE, ENZYME, TAG, 3-
KEYWDS 2 METHYLADENINE, SOLUTION STRUCTURE, NMR SPECTROSCOPY, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR A.C.DROHAT,K.KWON,D.J.KROSKY,J.T.STIVERS
REVDAT 3 13-JUL-11 1LMZ 1 VERSN
REVDAT 2 24-FEB-09 1LMZ 1 VERSN
REVDAT 1 28-AUG-02 1LMZ 0
JRNL AUTH A.C.DROHAT,K.KWON,D.J.KROSKY,J.T.STIVERS
JRNL TITL 3-METHYLADENINE DNA GLYCOSYLASE I IS AN UNEXPECTED
JRNL TITL 2 HELIX-HAIRPIN-HELIX SUPERFAMILY MEMBER.
JRNL REF NAT.STRUCT.BIOL. V. 9 659 2002
JRNL REFN ISSN 1072-8368
JRNL PMID 12161745
JRNL DOI 10.1038/NSB829
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XPLOR-NIH 1.1.2
REMARK 3 AUTHORS : CLORE, G.M., KUSZEWSKI, J., SCHWIETERS, C.D.,
REMARK 3 TJANDRA, N.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1LMZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAY-02.
REMARK 100 THE RCSB ID CODE IS RCSB016094.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 6.6
REMARK 210 IONIC STRENGTH : 100 MM NACL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : UNLABELED TAG 10 MM PHOSPHATE PH
REMARK 210 6.6 100 MM NACL 3 MM DTT 0.34 MM
REMARK 210 NAN3; U-15N-LABELED TAG 10 MM
REMARK 210 PHOSPHATE PH 6.6 100 MM NACL 3 MM
REMARK 210 DTT 0.34 MM NAN3; U-13C,15N-
REMARK 210 LABLED TAG 10 MM PHOSPHATE PH 6.6
REMARK 210 100 MM NACL 3 MM DTT 0.34 MM NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D_15N-
REMARK 210 SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY; 4D_13C-
REMARK 210 SEPARATED_NOESY; HNCO; HNCA;
REMARK 210 CBCA(CO)NH; HNCACB; HCCH-TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; DMX; UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS 1.1, NMRPIPE 2.0, SPARKY 3
REMARK 210 METHOD USED : STRUCTURES WERE CALCULATED FROM
REMARK 210 AN EXTENDED STRAND USING CNS 1.1,
REMARK 210 AND REFINED USING XPLOR-NIH 1.1.2
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES WITH
REMARK 210 THE LEAST RESTRAINT VIOLATIONS,
REMARK 210 STRUCTURES WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 8
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 HG1 THR A 131 H SER A 133 1.40
REMARK 500 O HIS A 88 H GLY A 90 1.41
REMARK 500 O CYS A 179 H CYS A 181 1.49
REMARK 500 O GLU A 106 H GLY A 109 1.55
REMARK 500 H HIS A 88 H ARG A 89 1.56
REMARK 500 O GLU A 38 H GLN A 41 1.56
REMARK 500 O LYS A 52 H TYR A 56 1.59
REMARK 500 HZ1 LYS A 151 HH11 ARG A 152 1.59
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 CYS A 4 -162.99 46.96
REMARK 500 1 GLN A 9 179.14 50.53
REMARK 500 1 ASP A 10 77.12 48.31
REMARK 500 1 PRO A 11 -10.41 -47.69
REMARK 500 1 GLU A 20 -131.83 -141.97
REMARK 500 1 TRP A 21 110.96 56.56
REMARK 500 1 ALA A 42 108.64 -43.62
REMARK 500 1 ASP A 64 129.83 61.75
REMARK 500 1 MET A 71 -160.63 -75.22
REMARK 500 1 GLN A 81 -63.45 -91.36
REMARK 500 1 ALA A 83 -46.36 -172.49
REMARK 500 1 HIS A 88 1.98 -158.21
REMARK 500 1 ARG A 89 -60.65 59.48
REMARK 500 1 PHE A 119 -15.98 -45.12
REMARK 500 1 PRO A 124 155.19 -47.16
REMARK 500 1 GLN A 128 43.72 -141.28
REMARK 500 1 HIS A 175 100.28 -160.90
REMARK 500 1 CYS A 180 -57.18 65.63
REMARK 500 1 CYS A 181 60.81 -173.07
REMARK 500 2 CYS A 4 26.99 -150.91
REMARK 500 2 SER A 8 48.22 -149.94
REMARK 500 2 GLN A 9 -125.77 -152.96
REMARK 500 2 GLU A 20 -131.09 -142.48
REMARK 500 2 TRP A 21 138.97 58.76
REMARK 500 2 GLN A 41 -15.39 58.34
REMARK 500 2 LEU A 44 -135.53 -116.87
REMARK 500 2 PHE A 60 -43.26 -132.84
REMARK 500 2 ASP A 64 131.48 69.62
REMARK 500 2 PRO A 65 -37.24 -39.90
REMARK 500 2 ALA A 83 -45.35 -176.72
REMARK 500 2 HIS A 88 91.17 170.44
REMARK 500 2 PHE A 119 -12.80 -46.07
REMARK 500 2 PRO A 124 151.89 -45.34
REMARK 500 2 GLN A 128 43.41 -149.06
REMARK 500 2 ALA A 129 -150.61 -82.05
REMARK 500 2 THR A 130 -33.72 -138.72
REMARK 500 2 HIS A 175 48.68 -146.22
REMARK 500 2 PRO A 183 41.43 -85.58
REMARK 500 3 CYS A 4 171.95 53.94
REMARK 500 3 TRP A 6 46.05 -148.30
REMARK 500 3 GLU A 20 -156.57 -144.54
REMARK 500 3 TRP A 21 125.73 59.76
REMARK 500 3 ALA A 42 109.75 -44.43
REMARK 500 3 PHE A 60 -54.22 -120.95
REMARK 500 3 ASP A 64 162.58 57.70
REMARK 500 3 ALA A 83 -61.97 -170.27
REMARK 500 3 ILE A 85 -169.06 -100.30
REMARK 500 3 HIS A 88 81.71 -177.60
REMARK 500 3 PHE A 119 -11.32 -45.13
REMARK 500 3 ASN A 121 -50.45 77.51
REMARK 500
REMARK 500 THIS ENTRY HAS 385 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1LMZ A 1 187 UNP P05100 3MG1_ECOLI 1 187
SEQRES 1 A 187 MET GLU ARG CYS GLY TRP VAL SER GLN ASP PRO LEU TYR
SEQRES 2 A 187 ILE ALA TYR HIS ASP ASN GLU TRP GLY VAL PRO GLU THR
SEQRES 3 A 187 ASP SER LYS LYS LEU PHE GLU MET ILE CYS LEU GLU GLY
SEQRES 4 A 187 GLN GLN ALA GLY LEU SER TRP ILE THR VAL LEU LYS LYS
SEQRES 5 A 187 ARG GLU ASN TYR ARG ALA CYS PHE HIS GLN PHE ASP PRO
SEQRES 6 A 187 VAL LYS VAL ALA ALA MET GLN GLU GLU ASP VAL GLU ARG
SEQRES 7 A 187 LEU VAL GLN ASP ALA GLY ILE ILE ARG HIS ARG GLY LYS
SEQRES 8 A 187 ILE GLN ALA ILE ILE GLY ASN ALA ARG ALA TYR LEU GLN
SEQRES 9 A 187 MET GLU GLN ASN GLY GLU PRO PHE ALA ASP PHE VAL TRP
SEQRES 10 A 187 SER PHE VAL ASN HIS GLN PRO GLN MET THR GLN ALA THR
SEQRES 11 A 187 THR LEU SER GLU ILE PRO THR SER THR PRO ALA SER ASP
SEQRES 12 A 187 ALA LEU SER LYS ALA LEU LYS LYS ARG GLY PHE LYS PHE
SEQRES 13 A 187 VAL GLY THR THR ILE CYS TYR SER PHE MET GLN ALA CYS
SEQRES 14 A 187 GLY LEU VAL ASN ASP HIS VAL VAL GLY CYS CYS CYS TYR
SEQRES 15 A 187 PRO GLY ASN LYS PRO
HELIX 1 1 PRO A 11 GLU A 20 1 10
HELIX 2 2 ASP A 27 GLN A 40 1 14
HELIX 3 3 SER A 45 MET A 71 1 27
HELIX 4 4 GLN A 72 ASP A 82 1 11
HELIX 5 5 ARG A 89 ASN A 108 1 20
HELIX 6 6 PRO A 111 PHE A 119 1 9
HELIX 7 7 THR A 139 GLY A 153 1 15
HELIX 8 8 GLY A 158 GLY A 170 1 13
SHEET 1 A 2 GLN A 125 MET A 126 0
SHEET 2 A 2 VAL A 172 ASN A 173 1 O ASN A 173 N GLN A 125
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 - r 25 2 Bytes