Header list of 1xpa.pdb file
Complete list - 2 20 Bytes
HEADER DNA REPAIR 06-JUL-98 1XPA
TITLE SOLUTION STRUCTURE OF THE DNA-AND RPA-BINDING DOMAIN OF THE HUMAN
TITLE 2 REPAIR FACTOR XPA, NMR, 1 STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: XPA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: MF122, RESIDUES 98-219;
COMPND 5 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 BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET16B;
SOURCE 9 EXPRESSION_SYSTEM_GENE: HUMAN XPA CDNA
KEYWDS DNA REPAIR, NUCLEOTIDE EXCISION REPAIR, ZINC-FINGER
EXPDTA SOLUTION NMR
AUTHOR T.IKEGAMI,I.KURAOKA,M.SAIJO,N.KODO,Y.KYOGOKU,K.MORIKAWA,K.TANAKA,
AUTHOR 2 M.SHIRAKAWA
REVDAT 3 02-MAR-22 1XPA 1 REMARK LINK
REVDAT 2 24-FEB-09 1XPA 1 VERSN
REVDAT 1 22-JUL-99 1XPA 0
JRNL AUTH T.IKEGAMI,I.KURAOKA,M.SAIJO,N.KODO,Y.KYOGOKU,K.MORIKAWA,
JRNL AUTH 2 K.TANAKA,M.SHIRAKAWA
JRNL TITL SOLUTION STRUCTURE OF THE DNA- AND RPA-BINDING DOMAIN OF THE
JRNL TITL 2 HUMAN REPAIR FACTOR XPA.
JRNL REF NAT.STRUCT.BIOL. V. 5 701 1998
JRNL REFN ISSN 1072-8368
JRNL PMID 9699634
JRNL DOI 10.1038/1400
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1XPA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000177300.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 7.3
REMARK 210 IONIC STRENGTH : 150MM KCL
REMARK 210 PRESSURE : 1 ATMOSPHERE
REMARK 210 SAMPLE CONTENTS : 50MM D-TRIS HCL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D-; 4D-MULTI-DIMENSIONAL
REMARK 210 EXPERIMENTS
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DMX500; DRX500; DRX800
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 140
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : THE LOWEST ENERGY AND NO
REMARK 210 VIOLATION GREATER THAN 0.3A OR
REMARK 210 5DEG
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY ON 13C, 15N-LABELED XPA. THIS MODEL IS THE CLOSEST
REMARK 210 STRUCTURE TO THE MEAN.
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 ARG A 211
REMARK 465 GLU A 212
REMARK 465 LYS A 213
REMARK 465 MET A 214
REMARK 465 LYS A 215
REMARK 465 GLN A 216
REMARK 465 LYS A 217
REMARK 465 LYS A 218
REMARK 465 PHE A 219
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 TYR A 102 33.45 -152.09
REMARK 500 GLU A 107 -50.88 -125.52
REMARK 500 SER A 115 -147.12 -157.32
REMARK 500 ASP A 134 -56.71 -160.23
REMARK 500 LYS A 135 -74.72 -46.33
REMARK 500 LYS A 137 93.46 -48.69
REMARK 500 LEU A 138 163.89 -41.88
REMARK 500 LEU A 149 26.25 43.70
REMARK 500 LYS A 151 -140.44 -123.23
REMARK 500 CYS A 153 -86.25 -127.97
REMARK 500 LEU A 155 -51.30 -125.18
REMARK 500 GLU A 159 85.21 39.13
REMARK 500 LEU A 162 99.96 22.23
REMARK 500 LYS A 163 128.72 -28.73
REMARK 500 ILE A 165 -159.22 -153.15
REMARK 500 LYS A 167 -144.64 -157.72
REMARK 500 HIS A 171 -155.47 -92.58
REMARK 500 ASP A 177 55.81 -158.61
REMARK 500 LEU A 182 105.90 -46.18
REMARK 500 SER A 196 -147.95 179.38
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 ARG A 130 0.28 SIDE CHAIN
REMARK 500 ARG A 158 0.27 SIDE CHAIN
REMARK 500 ARG A 189 0.32 SIDE CHAIN
REMARK 500 ARG A 207 0.31 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 220 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 105 SG
REMARK 620 2 CYS A 108 SG 106.3
REMARK 620 3 CYS A 126 SG 112.1 109.9
REMARK 620 4 CYS A 129 SG 106.8 112.2 109.4
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: NUL
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ZN BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 220
DBREF 1XPA A 98 219 UNP P23025 XPA_HUMAN 98 219
SEQRES 1 A 122 MET GLU PHE ASP TYR VAL ILE CYS GLU GLU CYS GLY LYS
SEQRES 2 A 122 GLU PHE MET ASP SER TYR LEU MET ASN HIS PHE ASP LEU
SEQRES 3 A 122 PRO THR CYS ASP ASN CYS ARG ASP ALA ASP ASP LYS HIS
SEQRES 4 A 122 LYS LEU ILE THR LYS THR GLU ALA LYS GLN GLU TYR LEU
SEQRES 5 A 122 LEU LYS ASP CYS ASP LEU GLU LYS ARG GLU PRO PRO LEU
SEQRES 6 A 122 LYS PHE ILE VAL LYS LYS ASN PRO HIS HIS SER GLN TRP
SEQRES 7 A 122 GLY ASP MET LYS LEU TYR LEU LYS LEU GLN ILE VAL LYS
SEQRES 8 A 122 ARG SER LEU GLU VAL TRP GLY SER GLN GLU ALA LEU GLU
SEQRES 9 A 122 GLU ALA LYS GLU VAL ARG GLN GLU ASN ARG GLU LYS MET
SEQRES 10 A 122 LYS GLN LYS LYS PHE
HET ZN A 220 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 H1 LYS A 141 GLU A 147 1 7
HELIX 2 H2 LYS A 183 TRP A 194 1 12
HELIX 3 H3 GLN A 197 GLU A 209 1 13
SHEET 1 S1 2 VAL A 103 ILE A 104 0
SHEET 2 S1 2 GLU A 111 PHE A 112 -1 N PHE A 112 O VAL A 103
SHEET 1 S2 3 ILE A 139 THR A 140 0
SHEET 2 S2 3 LEU A 180 TYR A 181 -1 N TYR A 181 O ILE A 139
SHEET 3 S2 3 PHE A 164 ILE A 165 -1 N ILE A 165 O LEU A 180
LINK SG CYS A 105 ZN ZN A 220 1555 1555 2.26
LINK SG CYS A 108 ZN ZN A 220 1555 1555 2.35
LINK SG CYS A 126 ZN ZN A 220 1555 1555 2.44
LINK SG CYS A 129 ZN ZN A 220 1555 1555 2.35
CISPEP 1 GLU A 159 PRO A 160 0 0.07
SITE 1 NUL 4 CYS A 105 CYS A 108 CYS A 126 CYS A 129
SITE 1 AC1 4 CYS A 105 CYS A 108 CYS A 126 CYS A 129
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