Header list of 1b22.pdb file
Complete list - b 16 2 Bytes
HEADER DNA BINDING PROTEIN 04-DEC-98 1B22 TITLE RAD51 (N-TERMINAL DOMAIN) COMPND MOL_ID: 1; COMPND 2 MOLECULE: DNA REPAIR PROTEIN RAD51; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: N-TERMINAL DOMAIN; 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; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: JM109(DE3); SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET3A; SOURCE 9 EXPRESSION_SYSTEM_GENE: RAD51(1-114) KEYWDS DNA BINDING, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, KEYWDS 2 STRUCTURAL GENOMICS, DNA BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 30 AUTHOR H.AIHARA,Y.ITO,H.KURUMIZAKA,S.YOKOYAMA,T.SHIBATA,RIKEN STRUCTURAL AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 4 16-FEB-22 1B22 1 REMARK REVDAT 3 24-FEB-09 1B22 1 VERSN REVDAT 2 01-APR-03 1B22 1 JRNL REVDAT 1 03-DEC-99 1B22 0 JRNL AUTH H.AIHARA,Y.ITO,H.KURUMIZAKA,S.YOKOYAMA,T.SHIBATA JRNL TITL THE N-TERMINAL DOMAIN OF THE HUMAN RAD51 PROTEIN BINDS DNA: JRNL TITL 2 STRUCTURE AND A DNA BINDING SURFACE AS REVEALED BY NMR. JRNL REF J.MOL.BIOL. V. 290 495 1999 JRNL REFN ISSN 0022-2836 JRNL PMID 10390347 JRNL DOI 10.1006/JMBI.1999.2904 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: SIMULATED ANNEALING REFINEMENT REMARK 4 REMARK 4 1B22 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-DEC-98. REMARK 100 THE DEPOSITION ID IS D_1000000206. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 100MM NACL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : DOUBLE; TRIPLE RESONANCE REMARK 210 EXPERIMENTS REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : DRX600 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR REMARK 210 METHOD USED : RANDOM SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 140 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST TARGET FUNCTION VALUES 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 HUMAN RAD51(1-114). 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 MODELS 1-30 REMARK 465 RES C SSSEQI REMARK 465 MET A 1 REMARK 465 ALA A 2 REMARK 465 MET A 3 REMARK 465 GLN A 4 REMARK 465 MET A 5 REMARK 465 GLN A 6 REMARK 465 LEU A 7 REMARK 465 GLU A 8 REMARK 465 ALA A 9 REMARK 465 ASN A 10 REMARK 465 ALA A 11 REMARK 465 ASP A 12 REMARK 465 THR A 13 REMARK 465 SER A 14 REMARK 465 VAL A 15 REMARK 465 PHE A 86 REMARK 465 THR A 87 REMARK 465 THR A 88 REMARK 465 ALA A 89 REMARK 465 THR A 90 REMARK 465 GLU A 91 REMARK 465 PHE A 92 REMARK 465 HIS A 93 REMARK 465 GLN A 94 REMARK 465 ARG A 95 REMARK 465 ARG A 96 REMARK 465 SER A 97 REMARK 465 GLU A 98 REMARK 465 ILE A 99 REMARK 465 ILE A 100 REMARK 465 GLN A 101 REMARK 465 ILE A 102 REMARK 465 THR A 103 REMARK 465 THR A 104 REMARK 465 GLY A 105 REMARK 465 SER A 106 REMARK 465 LYS A 107 REMARK 465 GLU A 108 REMARK 465 LEU A 109 REMARK 465 ASP A 110 REMARK 465 LYS A 111 REMARK 465 LEU A 112 REMARK 465 LEU A 113 REMARK 465 GLN A 114 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 O PRO A 56 H GLU A 59 1.50 REMARK 500 O ALA A 78 H VAL A 82 1.50 REMARK 500 O GLN A 23 H ILE A 25 1.52 REMARK 500 O PHE A 46 H THR A 48 1.56 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 GLU A 18 -167.86 59.97 REMARK 500 1 PRO A 24 60.57 -67.12 REMARK 500 1 SER A 26 -78.32 -43.41 REMARK 500 1 LEU A 28 -78.03 -59.85 REMARK 500 1 ILE A 33 -130.65 -82.17 REMARK 500 1 ASN A 34 -140.45 -80.24 REMARK 500 1 ASN A 36 -76.92 -39.81 REMARK 500 1 ASP A 37 -59.24 -26.63 REMARK 500 1 VAL A 38 -70.39 -50.50 REMARK 500 1 GLU A 43 -26.06 -39.50 REMARK 500 1 ALA A 44 -69.62 -151.16 REMARK 500 1 PHE A 46 6.26 -68.06 REMARK 500 1 HIS A 47 63.66 -62.76 REMARK 500 1 THR A 48 -177.57 171.37 REMARK 500 1 VAL A 49 -27.75 -35.54 REMARK 500 1 GLU A 50 -29.34 -36.37 REMARK 500 1 ASN A 62 -15.22 -49.48 REMARK 500 1 ILE A 63 -90.39 -58.47 REMARK 500 1 ILE A 66 -140.33 -81.73 REMARK 500 1 SER A 67 -134.45 168.02 REMARK 500 1 ALA A 69 -80.34 -40.52 REMARK 500 1 MET A 84 -94.44 41.05 REMARK 500 2 GLU A 18 106.81 -56.12 REMARK 500 2 SER A 19 43.11 -101.32 REMARK 500 2 GLN A 23 -65.67 -150.90 REMARK 500 2 PRO A 24 57.03 -69.92 REMARK 500 2 LEU A 28 -74.16 -87.29 REMARK 500 2 ILE A 33 -126.27 -81.62 REMARK 500 2 ASN A 34 -157.51 -90.69 REMARK 500 2 ASP A 37 -72.21 -25.88 REMARK 500 2 PHE A 46 27.71 -78.36 REMARK 500 2 THR A 48 -175.73 160.76 REMARK 500 2 VAL A 49 -30.56 -35.89 REMARK 500 2 TYR A 54 -85.81 -177.21 REMARK 500 2 ILE A 63 -79.50 -45.71 REMARK 500 2 ILE A 66 -143.77 -94.93 REMARK 500 2 SER A 67 -142.48 -179.34 REMARK 500 2 ALA A 69 -79.76 -39.23 REMARK 500 2 PRO A 83 -169.76 -73.09 REMARK 500 3 GLU A 18 -155.96 -174.78 REMARK 500 3 SER A 19 71.40 -167.41 REMARK 500 3 GLN A 23 -71.05 -134.11 REMARK 500 3 LEU A 28 -77.65 -82.62 REMARK 500 3 ILE A 33 -129.08 -98.05 REMARK 500 3 ASN A 34 -142.81 -91.55 REMARK 500 3 ASN A 36 -70.69 -54.29 REMARK 500 3 ASP A 37 -60.84 -24.69 REMARK 500 3 ALA A 44 -46.49 -176.97 REMARK 500 3 HIS A 47 72.09 -58.75 REMARK 500 3 THR A 48 -167.40 159.03 REMARK 500 REMARK 500 THIS ENTRY HAS 640 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: TRT001000204.1 RELATED DB: TARGETDB DBREF 1B22 A 1 114 UNP Q06609 RAD51_HUMAN 1 114 SEQRES 1 A 114 MET ALA MET GLN MET GLN LEU GLU ALA ASN ALA ASP THR SEQRES 2 A 114 SER VAL GLU GLU GLU SER PHE GLY PRO GLN PRO ILE SER SEQRES 3 A 114 ARG LEU GLU GLN CYS GLY ILE ASN ALA ASN ASP VAL LYS SEQRES 4 A 114 LYS LEU GLU GLU ALA GLY PHE HIS THR VAL GLU ALA VAL SEQRES 5 A 114 ALA TYR ALA PRO LYS LYS GLU LEU ILE ASN ILE LYS GLY SEQRES 6 A 114 ILE SER GLU ALA LYS ALA ASP LYS ILE LEU ALA GLU ALA SEQRES 7 A 114 ALA LYS LEU VAL PRO MET GLY PHE THR THR ALA THR GLU SEQRES 8 A 114 PHE HIS GLN ARG ARG SER GLU ILE ILE GLN ILE THR THR SEQRES 9 A 114 GLY SER LYS GLU LEU ASP LYS LEU LEU GLN HELIX 1 H1 SER A 26 GLN A 30 1 5 HELIX 2 H2 ASN A 36 GLU A 43 1 8 HELIX 3 H3 VAL A 49 ALA A 51 5 3 HELIX 4 H4 LYS A 57 ILE A 61 1 5 HELIX 5 H5 ALA A 69 LYS A 80 1 12 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 - b 16 2 Bytes