Header list of 1xna.pdb file
Complete list - 2 20 Bytes
HEADER DNA BINDING PROTEIN 27-FEB-99 1XNA
TITLE NMR SOLUTION STRUCTURE OF THE SINGLE-STRAND BREAK REPAIR PROTEIN
TITLE 2 XRCC1-N-TERMINAL DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (DNA-REPAIR PROTEIN XRCC1);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN, RESIDUES 1-183. RESIDUES 152-183 ARE
COMPND 5 DISORDERED AND NOT SHOWN.;
COMPND 6 SYNONYM: XRCC1-NTD;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELLULAR_LOCATION: NUCLEUS;
SOURCE 6 GENE: XRCC1;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21[DE3]PLYSS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET23A
KEYWDS XRCC1, 3D NMR, DNA REPAIR, SINGLE-STRAND BREAK DNA BINDING, DNA
KEYWDS 2 POLYMERASE-BETA BINDING, BETA SANDWICH, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
AUTHOR A.MARINTCHEV,G.P.MULLEN
REVDAT 4 02-MAR-22 1XNA 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1XNA 1 VERSN
REVDAT 2 01-APR-03 1XNA 1 JRNL
REVDAT 1 01-SEP-99 1XNA 0
JRNL AUTH A.MARINTCHEV,M.A.MULLEN,M.W.MACIEJEWSKI,B.PAN,M.R.GRYK,
JRNL AUTH 2 G.P.MULLEN
JRNL TITL SOLUTION STRUCTURE OF THE SINGLE-STRAND BREAK REPAIR PROTEIN
JRNL TITL 2 XRCC1 N-TERMINAL DOMAIN.
JRNL REF NAT.STRUCT.BIOL. V. 6 884 1999
JRNL REFN ISSN 1072-8368
JRNL PMID 10467102
JRNL DOI 10.1038/12347
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JOURNAL CITATION ABOVE.
REMARK 4
REMARK 4 1XNA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000558.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : 0.4
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : H2O AND D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D HNCACB; CBCA(CO)NH; HN(CO)CA;
REMARK 210 15N-EDITED TOCSY; HCC(CO)NH;
REMARK 210 HCCH TOCSY; HNCO; HNHA; HNHB; 2D
REMARK 210 (HB)CB(CGCD)HD; 1H-15N-HSQC; 1H-
REMARK 210 13C-HSQC; 1H-TOCSY; AROMATIC 1H-
REMARK 210 13C-HSQC; HMQC-J; 3D 15N-NOESY;
REMARK 210 3D 13C-NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA 1.5
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : MINIMIZED AVERAGE STRUCTURE OF
REMARK 210 23 CONFORMERS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-AND DOUBLE
REMARK 210 -RESONANCE NMR SPECTROSCOPY ON 13C-, 15N-LABELED XRCC1-N-
REMARK 210 TERMINAL DOMAIN
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 RES C SSSEQI
REMARK 465 PRO A 152
REMARK 465 PRO A 153
REMARK 465 ASP A 154
REMARK 465 LYS A 155
REMARK 465 ASP A 156
REMARK 465 GLU A 157
REMARK 465 ALA A 158
REMARK 465 GLU A 159
REMARK 465 ALA A 160
REMARK 465 PRO A 161
REMARK 465 SER A 162
REMARK 465 GLN A 163
REMARK 465 LYS A 164
REMARK 465 VAL A 165
REMARK 465 THR A 166
REMARK 465 VAL A 167
REMARK 465 THR A 168
REMARK 465 LYS A 169
REMARK 465 LEU A 170
REMARK 465 GLY A 171
REMARK 465 GLN A 172
REMARK 465 PHE A 173
REMARK 465 ARG A 174
REMARK 465 VAL A 175
REMARK 465 LYS A 176
REMARK 465 GLU A 177
REMARK 465 GLU A 178
REMARK 465 GLU A 179
REMARK 465 GLU A 180
REMARK 465 SER A 181
REMARK 465 ALA A 182
REMARK 465 ASN A 183
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 SER A 14 90.04 153.86
REMARK 500 LYS A 26 65.33 -114.99
REMARK 500 THR A 29 -87.95 -155.53
REMARK 500 TYR A 30 35.06 -178.04
REMARK 500 LYS A 32 -164.08 -127.33
REMARK 500 GLU A 40 88.26 -52.12
REMARK 500 GLU A 50 -9.96 -51.35
REMARK 500 ASP A 63 77.29 -113.31
REMARK 500 ALA A 66 -51.61 -139.29
REMARK 500 ASP A 83 34.16 -97.05
REMARK 500 VAL A 86 89.37 -58.65
REMARK 500 VAL A 89 179.10 -53.03
REMARK 500 SER A 97 -51.73 -120.18
REMARK 500 ARG A 100 -82.28 -82.36
REMARK 500 SER A 101 38.83 -161.66
REMARK 500 SER A 103 -154.17 -150.98
REMARK 500 ASN A 104 109.48 -54.27
REMARK 500 GLN A 134 128.33 149.70
REMARK 500 LYS A 138 -40.47 -170.66
REMARK 500 PHE A 142 -165.90 -167.76
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1XNA A 1 183 UNP P18887 XRCC1_HUMAN 1 183
SEQADV 1XNA GLU A 179 UNP P18887 ASP 179 CLONING ARTIFACT
SEQRES 1 A 183 MET PRO GLU ILE ARG LEU ARG HIS VAL VAL SER CYS SER
SEQRES 2 A 183 SER GLN ASP SER THR HIS CYS ALA GLU ASN LEU LEU LYS
SEQRES 3 A 183 ALA ASP THR TYR ARG LYS TRP ARG ALA ALA LYS ALA GLY
SEQRES 4 A 183 GLU LYS THR ILE SER VAL VAL LEU GLN LEU GLU LYS GLU
SEQRES 5 A 183 GLU GLN ILE HIS SER VAL ASP ILE GLY ASN ASP GLY SER
SEQRES 6 A 183 ALA PHE VAL GLU VAL LEU VAL GLY SER SER ALA GLY GLY
SEQRES 7 A 183 ALA GLY GLU GLN ASP TYR GLU VAL LEU LEU VAL THR SER
SEQRES 8 A 183 SER PHE MET SER PRO SER GLU SER ARG SER GLY SER ASN
SEQRES 9 A 183 PRO ASN ARG VAL ARG MET PHE GLY PRO ASP LYS LEU VAL
SEQRES 10 A 183 ARG ALA ALA ALA GLU LYS ARG TRP ASP ARG VAL LYS ILE
SEQRES 11 A 183 VAL CYS SER GLN PRO TYR SER LYS ASP SER PRO PHE GLY
SEQRES 12 A 183 LEU SER PHE VAL ARG PHE HIS SER PRO PRO ASP LYS ASP
SEQRES 13 A 183 GLU ALA GLU ALA PRO SER GLN LYS VAL THR VAL THR LYS
SEQRES 14 A 183 LEU GLY GLN PHE ARG VAL LYS GLU GLU GLU GLU SER ALA
SEQRES 15 A 183 ASN
HELIX 1 1 ALA A 21 LEU A 25 5 5
HELIX 2 2 PRO A 96 ARG A 100 1 5
HELIX 3 3 ARG A 118 GLU A 122 1 5
SHEET 1 1 5 HIS A 8 SER A 13 0
SHEET 2 1 5 THR A 42 LEU A 49 -1 N VAL A 46 O SER A 11
SHEET 3 1 5 ARG A 127 SER A 133 -1 N CYS A 132 O ILE A 43
SHEET 4 1 5 PHE A 67 SER A 74 -1 N GLY A 73 O ARG A 127
SHEET 5 1 5 TYR A 84 SER A 92 -1 N LEU A 88 O VAL A 72
SHEET 1 2 3 ARG A 107 GLY A 112 0
SHEET 2 2 3 SER A 57 ASN A 62 -1 N ASN A 62 O ARG A 107
SHEET 3 2 3 PHE A 146 HIS A 150 -1 N HIS A 150 O SER A 57
SHEET 1 3 2 TRP A 33 ALA A 35 0
SHEET 2 3 2 PHE A 142 LEU A 144 -1 N LEU A 144 O TRP A 33
SHEET 1 4 2 GLU A 52 ILE A 55 0
SHEET 2 4 2 ARG A 124 TRP A 125 -1 N TRP A 125 O GLU A 53
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
Complete list - 2 20 Bytes