Header list of 1x51.pdb file
Complete list - r 2 2 Bytes
HEADER HYDROLASE, DNA BINDING PROTEIN 15-MAY-05 1X51
TITLE SOLUTION STRUCTURE OF THE NUDIX DOMAIN FROM HUMAN A/G-SPECIFIC ADENINE
TITLE 2 DNA GLYCOSYLASE ALPHA-3 SPLICE ISOFORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: A/G-SPECIFIC ADENINE DNA GLYCOSYLASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: NUDIX DOMAIN;
COMPND 5 SYNONYM: A/G-SPECIFIC ADENINE DNA GLYCOSYLASE ISOFORM ALPHA-3, MUTY
COMPND 6 HOMOLOG, HMYH;
COMPND 7 EC: 3.2.2.-;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: MUTYH;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040906-16;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS NUDIX DOMAIN, DNA REPAIR, ALPHA-3 ISOFORM, STRUCTURAL GENOMICS,
KEYWDS 2 NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL
KEYWDS 3 ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI,
KEYWDS 4 HYDROLASE, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.TOMIZAWA,T.KIGAWA,S.KOSHIBA,M.INOUE,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1X51 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1X51 1 VERSN
REVDAT 1 15-NOV-05 1X51 0
JRNL AUTH T.TOMIZAWA,T.KIGAWA,S.KOSHIBA,M.INOUE,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE NUDIX DOMAIN FROM HUMAN
JRNL TITL 2 A/G-SPECIFIC ADENINE DNA GLYCOSYLASE ALPHA-3 SPLICE ISOFORM
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1X51 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024387.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.32MM NUDIX DOMAIN U-15N, 13C;
REMARK 210 20MM D-TRIS-HCL; 100MM NACL; 1MM
REMARK 210 D-DTT; 0.02% NAN3; 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20030801, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9295, CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 RESTRAINTED MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION,STRUCTURES WITH
REMARK 210 THE LOWEST ENERGY,STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS
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: 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 SER A 2 102.29 -58.98
REMARK 500 1 PRO A 8 1.51 -69.77
REMARK 500 1 LYS A 10 179.77 -54.34
REMARK 500 1 ALA A 11 125.35 -35.58
REMARK 500 1 SER A 12 107.04 -55.74
REMARK 500 1 ARG A 13 -51.47 -130.47
REMARK 500 1 ALA A 34 125.02 -170.04
REMARK 500 1 ASN A 43 153.52 -43.57
REMARK 500 1 LEU A 47 28.45 39.26
REMARK 500 1 TRP A 76 -71.57 -87.24
REMARK 500 1 ALA A 77 -70.99 -74.98
REMARK 500 1 PRO A 81 -179.82 -69.75
REMARK 500 1 ALA A 82 -54.09 -125.94
REMARK 500 1 PRO A 114 -173.79 -69.74
REMARK 500 1 VAL A 118 136.20 -171.88
REMARK 500 1 PRO A 120 1.24 -69.71
REMARK 500 1 ALA A 134 99.04 -66.89
REMARK 500 1 SER A 150 115.32 -164.41
REMARK 500 1 SER A 153 153.09 -39.94
REMARK 500 1 SER A 154 171.27 -46.06
REMARK 500 2 SER A 12 168.93 -45.47
REMARK 500 2 ALA A 34 139.36 -172.99
REMARK 500 2 LEU A 46 132.29 -35.17
REMARK 500 2 ALA A 77 -71.18 -79.67
REMARK 500 2 ALA A 82 -70.06 -101.35
REMARK 500 2 SER A 96 -72.52 -49.09
REMARK 500 2 PRO A 114 -179.36 -69.71
REMARK 500 2 THR A 116 37.12 38.94
REMARK 500 2 ALA A 133 155.11 -45.04
REMARK 500 3 SER A 2 96.52 -50.72
REMARK 500 3 SER A 5 -50.95 -128.22
REMARK 500 3 ALA A 11 175.27 -53.40
REMARK 500 3 SER A 12 49.22 -100.93
REMARK 500 3 ALA A 34 148.01 -170.91
REMARK 500 3 ASN A 43 108.39 -39.26
REMARK 500 3 LEU A 47 54.73 72.29
REMARK 500 3 GLN A 71 -31.13 -35.50
REMARK 500 3 TRP A 76 -74.68 -90.24
REMARK 500 3 ALA A 77 -72.78 -73.66
REMARK 500 3 PRO A 81 -174.14 -69.75
REMARK 500 3 ALA A 82 -52.81 -130.07
REMARK 500 3 GLN A 112 174.56 -50.83
REMARK 500 3 THR A 116 34.85 35.49
REMARK 500 3 ALA A 134 98.94 -65.62
REMARK 500 4 LYS A 10 89.57 -64.20
REMARK 500 4 SER A 12 128.33 -36.25
REMARK 500 4 ARG A 13 103.31 -38.98
REMARK 500 4 ASN A 43 106.90 -169.91
REMARK 500 4 TRP A 58 158.42 -44.70
REMARK 500 4 LYS A 67 -70.00 -54.88
REMARK 500
REMARK 500 THIS ENTRY HAS 253 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSI002005124.1 RELATED DB: TARGETDB
DBREF 1X51 A 8 149 UNP Q9UIF7 MUTYH_HUMAN 345 486
SEQADV 1X51 GLY A 1 UNP Q9UIF7 CLONING ARTIFACT
SEQADV 1X51 SER A 2 UNP Q9UIF7 CLONING ARTIFACT
SEQADV 1X51 SER A 3 UNP Q9UIF7 CLONING ARTIFACT
SEQADV 1X51 GLY A 4 UNP Q9UIF7 CLONING ARTIFACT
SEQADV 1X51 SER A 5 UNP Q9UIF7 CLONING ARTIFACT
SEQADV 1X51 SER A 6 UNP Q9UIF7 CLONING ARTIFACT
SEQADV 1X51 GLY A 7 UNP Q9UIF7 CLONING ARTIFACT
SEQADV 1X51 SER A 150 UNP Q9UIF7 CLONING ARTIFACT
SEQADV 1X51 GLY A 151 UNP Q9UIF7 CLONING ARTIFACT
SEQADV 1X51 PRO A 152 UNP Q9UIF7 CLONING ARTIFACT
SEQADV 1X51 SER A 153 UNP Q9UIF7 CLONING ARTIFACT
SEQADV 1X51 SER A 154 UNP Q9UIF7 CLONING ARTIFACT
SEQADV 1X51 GLY A 155 UNP Q9UIF7 CLONING ARTIFACT
SEQRES 1 A 155 GLY SER SER GLY SER SER GLY PRO ARG LYS ALA SER ARG
SEQRES 2 A 155 LYS PRO PRO ARG GLU GLU SER SER ALA THR CYS VAL LEU
SEQRES 3 A 155 GLU GLN PRO GLY ALA LEU GLY ALA GLN ILE LEU LEU VAL
SEQRES 4 A 155 GLN ARG PRO ASN SER GLY LEU LEU ALA GLY LEU TRP GLU
SEQRES 5 A 155 PHE PRO SER VAL THR TRP GLU PRO SER GLU GLN LEU GLN
SEQRES 6 A 155 ARG LYS ALA LEU LEU GLN GLU LEU GLN ARG TRP ALA GLY
SEQRES 7 A 155 PRO LEU PRO ALA THR HIS LEU ARG HIS LEU GLY GLU VAL
SEQRES 8 A 155 VAL HIS THR PHE SER HIS ILE LYS LEU THR TYR GLN VAL
SEQRES 9 A 155 TYR GLY LEU ALA LEU GLU GLY GLN THR PRO VAL THR THR
SEQRES 10 A 155 VAL PRO PRO GLY ALA ARG TRP LEU THR GLN GLU GLU PHE
SEQRES 11 A 155 HIS THR ALA ALA VAL SER THR ALA MET LYS LYS VAL PHE
SEQRES 12 A 155 ARG VAL TYR GLN GLY GLN SER GLY PRO SER SER GLY
HELIX 1 1 SER A 61 ALA A 77 1 17
HELIX 2 2 GLN A 127 ALA A 133 1 7
HELIX 3 3 SER A 136 GLY A 148 1 13
SHEET 1 A 5 TRP A 51 GLU A 52 0
SHEET 2 A 5 ALA A 34 GLN A 40 -1 N VAL A 39 O GLU A 52
SHEET 3 A 5 GLU A 18 PRO A 29 -1 N GLN A 28 O GLN A 35
SHEET 4 A 5 LYS A 99 ALA A 108 1 O THR A 101 N SER A 21
SHEET 5 A 5 ARG A 86 HIS A 87 -1 N ARG A 86 O GLY A 106
SHEET 1 B 4 SER A 55 THR A 57 0
SHEET 2 B 4 GLU A 18 PRO A 29 -1 N ALA A 22 O VAL A 56
SHEET 3 B 4 ALA A 34 GLN A 40 -1 O GLN A 35 N GLN A 28
SHEET 4 B 4 ALA A 122 THR A 126 -1 O ARG A 123 N LEU A 38
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 2 2 Bytes