Header list of 1z00.pdb file
Complete list - r 2 2 Bytes
HEADER HYDROLASE 01-MAR-05 1Z00
TITLE SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN OF ERCC1 COMPLEXED WITH
TITLE 2 THE C-TERMINAL DOMAIN OF XPF
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA EXCISION REPAIR PROTEIN ERCC-1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: DNA REPAIR ENDONUCLEASE XPF;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: C-TERMINAL DOMAIN;
COMPND 10 SYNONYM: DNA EXCISION REPAIR PROTEIN ERCC-4, DNA-REPAIR PROTEIN
COMPND 11 COMPLEMENTING XP-F CELL, XERODERMA PIGMENTOSUM GROUP F COMPLEMENTING
COMPND 12 PROTEIN;
COMPND 13 EC: 3.1.-.-;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(ROSETTA) NOVAGEN;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28B;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(ROSETTA) NOVAGEN;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PET28B
KEYWDS HELIX-HAIRPIN-HELIX, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.TRIPSIANES,G.FOLKERS,E.AB,D.DAS,H.ODIJK,N.G.J.JASPERS,
AUTHOR 2 J.H.J.HOEIJMAKERS,R.KAPTEIN,R.BOELENS
REVDAT 3 02-MAR-22 1Z00 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1Z00 1 VERSN
REVDAT 1 20-DEC-05 1Z00 0
JRNL AUTH K.TRIPSIANES,G.FOLKERS,E.AB,D.DAS,H.ODIJK,N.G.J.JASPERS,
JRNL AUTH 2 J.H.J.HOEIJMAKERS,R.KAPTEIN,R.BOELENS
JRNL TITL THE STRUCTURE OF THE HUMAN ERCC1/XPF INTERACTION DOMAINS
JRNL TITL 2 REVEALS A COMPLEMENTARY ROLE FOR THE TWO PROTEINS IN
JRNL TITL 3 NUCLEOTIDE EXCISION REPAIR
JRNL REF STRUCTURE V. 13 1849 2005
JRNL REFN ISSN 0969-2126
JRNL PMID 16338413
JRNL DOI 10.1016/J.STR.2005.08.014
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, CNS 1.1
REMARK 3 AUTHORS : BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 4547 NOE-DERIVED
REMARK 3 DISTANCE RESTRAINTS, 197 TALOS BASED DIHEDRAL ANGLE RESTRAINTS AND
REMARK 3 DISTANCE RESTRAINTS FOR 52 HYDROGEN BONDS
REMARK 4
REMARK 4 1Z00 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032125.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 295.5
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 50MM PHOSPHATE, 100MM NACL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1.5MM ERCC1-XPF U-15N,13C; 50MM
REMARK 210 PHOSPHATE BUFFER NA: 92% H2O, 8%
REMARK 210 D2O; 1MM ERCC1-XPF U-15N; 50MM
REMARK 210 PHOSPHATE BUFFER NA: 92% H2O, 8%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D NOESY-(13C,1H)-HSQC; 3D NOESY
REMARK 210 -(15N,1H)-HSQC; 3D (13C)-HMQC-
REMARK 210 NOESY-(13C,1H)-HSQC; 3D (13C)-
REMARK 210 HMQC-NOESY-(15N 1H)-HSQC; 2D
REMARK 210 NOESY; 2D NOESY 15N FILTERED
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ; 900 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.3, SPARKY 3.110, CYANA
REMARK 210 2.0
REMARK 210 METHOD USED : WATER REFINMENT IN CNS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 HIS A 303
REMARK 465 HIS A 304
REMARK 465 HIS A 305
REMARK 465 HIS A 306
REMARK 465 HIS A 307
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 OE1 GLU A 228 HZ3 LYS B 902 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 LEU A 223 135.01 -173.39
REMARK 500 1 PRO A 275 31.14 -66.44
REMARK 500 1 LEU A 277 -80.17 -116.73
REMARK 500 1 LYS A 295 -74.69 70.04
REMARK 500 1 ASP B 823 76.54 54.24
REMARK 500 1 GLU B 825 129.51 58.53
REMARK 500 1 PRO B 845 -70.30 -57.56
REMARK 500 2 ASP A 221 24.74 -62.21
REMARK 500 2 LEU A 277 -88.83 -127.04
REMARK 500 2 LYS A 295 -83.13 65.65
REMARK 500 2 SER B 824 83.17 69.36
REMARK 500 2 PRO B 828 31.22 -75.48
REMARK 500 2 ASN B 834 107.08 -59.17
REMARK 500 2 SER B 899 -168.72 -123.11
REMARK 500 2 LYS B 900 -66.95 68.51
REMARK 500 2 LYS B 902 -76.90 -106.06
REMARK 500 2 LYS B 904 148.70 73.11
REMARK 500 3 LEU A 222 -68.13 175.45
REMARK 500 3 LEU A 223 160.31 173.67
REMARK 500 3 LEU A 277 -89.98 -131.72
REMARK 500 3 LYS A 295 -84.92 65.93
REMARK 500 3 LEU A 300 58.45 -105.67
REMARK 500 3 PRO B 828 38.63 -77.31
REMARK 500 3 LYS B 902 9.98 -154.96
REMARK 500 3 LYS B 904 162.07 71.62
REMARK 500 4 ASP A 221 24.74 -70.84
REMARK 500 4 LEU A 222 -53.97 70.70
REMARK 500 4 PRO A 275 7.04 -67.68
REMARK 500 4 LEU A 277 -92.21 -120.29
REMARK 500 4 LYS A 295 -83.05 64.99
REMARK 500 4 ASP B 823 -69.69 67.72
REMARK 500 4 PRO B 828 35.78 -76.42
REMARK 500 5 LEU A 223 141.17 174.34
REMARK 500 5 PRO A 275 20.83 -63.04
REMARK 500 5 LEU A 277 -85.36 -107.96
REMARK 500 5 LYS A 295 -78.00 66.68
REMARK 500 5 ASP B 823 -79.00 -131.55
REMARK 500 5 PRO B 828 29.73 -78.41
REMARK 500 5 SER B 830 -10.57 -49.46
REMARK 500 5 LYS B 902 -71.13 -92.36
REMARK 500 6 LEU A 222 -43.56 68.79
REMARK 500 6 SER A 267 -166.64 -107.27
REMARK 500 6 LEU A 277 -84.08 -123.40
REMARK 500 6 LYS A 295 -80.08 67.52
REMARK 500 6 ASP B 823 -76.37 -139.74
REMARK 500 6 PRO B 828 32.93 -73.68
REMARK 500 6 SER B 830 -19.41 -48.01
REMARK 500 6 LYS B 902 178.86 61.15
REMARK 500 7 PRO A 275 -8.10 -56.02
REMARK 500 7 LEU A 277 -91.52 -108.33
REMARK 500
REMARK 500 THIS ENTRY HAS 140 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 3 ARG A 234 0.10 SIDE CHAIN
REMARK 500 13 ARG A 234 0.07 SIDE CHAIN
REMARK 500 14 ARG A 283 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1Z00 A 220 297 UNP P07992 ERCC1_HUMAN 220 297
DBREF 1Z00 B 823 905 UNP Q92889 ERCC4_HUMAN 823 905
SEQADV 1Z00 MET A 219 UNP P07992 INITIATING METHIONINE
SEQADV 1Z00 GLY A 298 UNP P07992 EXPRESSION TAG
SEQADV 1Z00 GLY A 299 UNP P07992 EXPRESSION TAG
SEQADV 1Z00 LEU A 300 UNP P07992 EXPRESSION TAG
SEQADV 1Z00 GLU A 301 UNP P07992 EXPRESSION TAG
SEQADV 1Z00 HIS A 302 UNP P07992 EXPRESSION TAG
SEQADV 1Z00 HIS A 303 UNP P07992 EXPRESSION TAG
SEQADV 1Z00 HIS A 304 UNP P07992 EXPRESSION TAG
SEQADV 1Z00 HIS A 305 UNP P07992 EXPRESSION TAG
SEQADV 1Z00 HIS A 306 UNP P07992 EXPRESSION TAG
SEQADV 1Z00 HIS A 307 UNP P07992 EXPRESSION TAG
SEQADV 1Z00 MET B 822 UNP Q92889 INITIATING METHIONINE
SEQRES 1 A 89 MET ALA ASP LEU LEU MET GLU LYS LEU GLU GLN ASP PHE
SEQRES 2 A 89 VAL SER ARG VAL THR GLU CYS LEU THR THR VAL LYS SER
SEQRES 3 A 89 VAL ASN LYS THR ASP SER GLN THR LEU LEU THR THR PHE
SEQRES 4 A 89 GLY SER LEU GLU GLN LEU ILE ALA ALA SER ARG GLU ASP
SEQRES 5 A 89 LEU ALA LEU CYS PRO GLY LEU GLY PRO GLN LYS ALA ARG
SEQRES 6 A 89 ARG LEU PHE ASP VAL LEU HIS GLU PRO PHE LEU LYS VAL
SEQRES 7 A 89 PRO GLY GLY LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 84 MET ASP SER GLU THR LEU PRO GLU SER GLU LYS TYR ASN
SEQRES 2 B 84 PRO GLY PRO GLN ASP PHE LEU LEU LYS MET PRO GLY VAL
SEQRES 3 B 84 ASN ALA LYS ASN CYS ARG SER LEU MET HIS HIS VAL LYS
SEQRES 4 B 84 ASN ILE ALA GLU LEU ALA ALA LEU SER GLN ASP GLU LEU
SEQRES 5 B 84 THR SER ILE LEU GLY ASN ALA ALA ASN ALA LYS GLN LEU
SEQRES 6 B 84 TYR ASP PHE ILE HIS THR SER PHE ALA GLU VAL VAL SER
SEQRES 7 B 84 LYS GLY LYS GLY LYS LYS
HELIX 1 1 LEU A 223 THR A 240 1 18
HELIX 2 2 ASN A 246 PHE A 257 1 12
HELIX 3 3 SER A 259 ALA A 266 1 8
HELIX 4 4 SER A 267 LEU A 273 1 7
HELIX 5 5 GLY A 278 GLU A 291 1 14
HELIX 6 6 LEU B 827 LYS B 832 5 6
HELIX 7 7 ASN B 834 LYS B 843 1 10
HELIX 8 8 ASN B 848 VAL B 859 1 12
HELIX 9 9 ASN B 861 LEU B 868 1 8
HELIX 10 10 SER B 869 GLY B 878 1 10
HELIX 11 11 ASN B 879 HIS B 891 1 13
HELIX 12 12 SER B 893 VAL B 898 1 6
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