Header list of 1aa3.pdb file
Complete list - 25 201 Bytes
HEADER DOUBLE-STRANDED DNA BINDING DOMAIN 22-JAN-97 1AA3
TITLE C-TERMINAL DOMAIN OF THE E. COLI RECA, NMR, MINIMIZED AVERAGE
TITLE 2 STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RECA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12
KEYWDS DOUBLE-STRANDED DNA BINDING DOMAIN, RIKEN STRUCTURAL
KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, STRUCTURAL GENOMICS
EXPDTA SOLUTION NMR
AUTHOR H.AIHARA,Y.ITO,H.KURUMIZAKA,T.TERADA,S.YOKOYAMA,T.SHIBATA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 13-JUL-11 1AA3 1 VERSN
REVDAT 2 24-FEB-09 1AA3 1 VERSN
REVDAT 1 23-JUL-97 1AA3 0
JRNL AUTH H.AIHARA,Y.ITO,H.KURUMIZAKA,T.TERADA,S.YOKOYAMA,T.SHIBATA
JRNL TITL AN INTERACTION BETWEEN A SPECIFIED SURFACE OF THE C-TERMINAL
JRNL TITL 2 DOMAIN OF RECA PROTEIN AND DOUBLE-STRANDED DNA FOR
JRNL TITL 3 HOMOLOGOUS PAIRING.
JRNL REF J.MOL.BIOL. V. 274 213 1997
JRNL REFN ISSN 0022-2836
JRNL PMID 9398528
JRNL DOI 10.1006/JMBI.1997.1403
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SIMULATED ANNEALING REFINEMENT FOR NMR
REMARK 3 STRUCTURE DETERMINATION
REMARK 4
REMARK 4 1AA3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
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 : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 1H-1H NOESY; 1H-1H TOCSY; 1H-15N
REMARK 210 HSQC; HMQC-J; 3D 15N-SEPARATED
REMARK 210 TOCSY; 15N-SEPARATED NOESY; HNHB
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX600; ARX400
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AZARA 1.0, FELIX 2.3, X-PLOR 3.1
REMARK 210 METHOD USED : HYBRID DISTANCE GEOMETRY-
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : AVERAGED MINIMIZED STRUCTURE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: 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 TYR A 293 H GLY A 295 1.50
REMARK 500 O GLU A 318 H LYS A 322 1.50
REMARK 500 O LYS A 321 H GLU A 325 1.50
REMARK 500 HZ1 LYS A 286 O GLY A 288 1.52
REMARK 500 O GLU A 320 H ARG A 324 1.58
REMARK 500 O ASN A 312 H ALA A 316 1.60
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 ASN A 269 -100.10 43.89
REMARK 500 PHE A 270 -97.34 160.96
REMARK 500 TYR A 271 -2.24 82.21
REMARK 500 GLU A 281 -76.72 -96.96
REMARK 500 LYS A 282 39.18 167.51
REMARK 500 LYS A 294 52.40 -61.33
REMARK 500 GLN A 300 172.39 -46.75
REMARK 500 ASN A 304 32.94 -161.44
REMARK 500 ASN A 312 61.01 -106.35
REMARK 500 ALA A 316 -22.92 -36.63
REMARK 500 ILE A 319 -70.97 -66.31
REMARK 500 SER A 329 44.28 -86.72
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 324 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MY_001000015.1 RELATED DB: TARGETDB
DBREF 1AA3 A 268 330 UNP P0A7G6 RECA_ECOLI 268 330
SEQRES 1 A 63 ILE ASN PHE TYR GLY GLU LEU VAL ASP LEU GLY VAL LYS
SEQRES 2 A 63 GLU LYS LEU ILE GLU LYS ALA GLY ALA TRP TYR SER TYR
SEQRES 3 A 63 LYS GLY GLU LYS ILE GLY GLN GLY LYS ALA ASN ALA THR
SEQRES 4 A 63 ALA TRP LEU LYS ASP ASN PRO GLU THR ALA LYS GLU ILE
SEQRES 5 A 63 GLU LYS LYS VAL ARG GLU LEU LEU LEU SER ASN
HELIX 1 H1 PHE A 270 LYS A 280 1 11
HELIX 2 H2 ASN A 304 ASP A 311 1 8
HELIX 3 H3 GLU A 314 GLU A 325 1 12
SHEET 1 S1 2 ILE A 284 ALA A 287 0
SHEET 2 S1 2 TRP A 290 TYR A 293 -1 N SER A 292 O GLU A 285
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 - 25 201 Bytes