Header list of 2ezx.pdb file
Complete list - 9 20 Bytes
HEADER DNA BINDING PROTEIN 26-JUL-98 2EZX
TITLE SOLUTION STRUCTURE OF HUMAN BARRIER-TO-AUTOINTEGRATION FACTOR BAF,
TITLE 2 NMR, REGULARIZED MEAN STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BARRIER-TO-AUTOINTEGRATION FACTOR;
COMPND 3 CHAIN: A, B;
COMPND 4 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
KEYWDS DNA-BINDING PROTEIN, INTEGRATION, AIDS, RETROVIRUSES, DNA BINDING
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
AUTHOR G.M.CLORE,M.CAI,A.M.GRONENBORN
REVDAT 3 09-MAR-22 2EZX 1 KEYWDS REMARK
REVDAT 2 24-FEB-09 2EZX 1 VERSN
REVDAT 1 13-JAN-99 2EZX 0
JRNL AUTH M.CAI,Y.HUANG,R.ZHENG,S.Q.WEI,R.GHIRLANDO,M.S.LEE,R.CRAIGIE,
JRNL AUTH 2 A.M.GRONENBORN,G.M.CLORE
JRNL TITL SOLUTION STRUCTURE OF THE CELLULAR FACTOR BAF RESPONSIBLE
JRNL TITL 2 FOR PROTECTING RETROVIRAL DNA FROM AUTOINTEGRATION.
JRNL REF NAT.STRUCT.BIOL. V. 5 903 1998
JRNL REFN ISSN 1072-8368
JRNL PMID 9783751
JRNL DOI 10.1038/2345
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE
REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,
REMARK 3 SIMONSON,WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES WERE CALCULATED USING THE SIMULATED
REMARK 3 ANNEALING PROTOCOL OF NILGES ET AL. (1988) FEBS LETT.
REMARK 3 229, 129 - 136 USING THE PROGRAM X-PLOR 3.1 (BRUNGER)
REMARK 3 MODIFIED TO INCORPORATE COUPLING CONSTANT (GARRETT ET AL.
REMARK 3 (1984) J.MAGN.RESON. SERIES B 104, 99 - 103), CARBON
REMARK 3 CHEMICAL SHIFT (KUSZEWSKI ET AL. (1995) J.MAGN.RESON.
REMARK 3 SERIES B 106, 92 - 96) RESTRAINTS, 1H CHEMICAL SHIFT
REMARK 3 RESTRAINTS (KUSZEWSKI ET AL. (1995) J.MAGN.RESON. SERIES
REMARK 3 B 107, 293-297; (1996) J.MAGN.RESON. SERIES B 112,
REMARK 3 79-81), AND A CONFORMATIONAL DATABASE POTENTIAL
REMARK 3 (KUSZWESKI ET AL. (1996) PROTEIN SCI. 5, 1067-108 AND
REMARK 3 (1997) J.MAGN.RESON. 125, 171-177).
REMARK 3
REMARK 3 THE 3D STRUCTURE OF THE 21 KDA BAF DIMER WAS SOLVED BY
REMARK 3 MULTI-DIMENSIONAL HETERONUCLEAR-EDITED AND -FILTERED NMR
REMARK 3 BASED ON 1655 EXPERIMENTAL RESTRAINTS (PER MONOMER):
REMARK 3 (A) INTRASUBUNIT: 288 SEQUENTIAL (|I-J|=1), 267 MEDIUM
REMARK 3 RANGE (1 < |I-J| >=5) AND 190 LONG RANGE (|I-J| >5)
REMARK 3 INTERRESIDUE, AND 7 INTRARESIDUE APPROXIMATE INTERPROTON
REMARK 3 DISTANCE RESTRAINTS; 64 DISTANCE RESTRAINTS FOR 32
REMARK 3 HYDROGEN BONDS; 257 TORSION ANGLE (84 PHI, 78 PSI, 60 CHI1
REMARK 3 29 CHI2 AND 6 CHI3) RESTRAINTS; 66 THREE-BOND HN-HA
REMARK 3 COUPLING CONSTANT RESTRAINTS; 165 (87 CALPHA AND 78 CBETA)
REMARK 3 13C SHIFT RESTRAINTS; 44 1H METHYL PROTON CHEMICAL SHIFTS;
REMARK 3 259 DIPOLAR COUPLINGS (76 N-H, 76 CALPHA-C', 55 N-C'
REMARK 3 AND 52 HN-C').
REMARK 3 (B) 48 INTERSUBUNIT INTERPROTON DISTANCE RESTRAINTS.
REMARK 3
REMARK 3 RMS DEVIATIONS.
REMARK 3 BOND LENGTHS : 0.004931
REMARK 3 BOND ANGLES : 0.543143
REMARK 3 IMPROPER ANGLES : 0.551732
REMARK 3 CDIH : 0.128297
REMARK 3 NOE : 0.022087
REMARK 3 COUP : 0.943946
REMARK 3 13C SHIFTS RMS CA, CB (PPM): 1.04812, 1.20411
REMARK 3 JHNHA RMS (HZ): 0.943946 0
REMARK 3 DIPOLAR COUPLINGS NH CACO NCO HNCO
REMARK 3 RMS DIPOLAR (HZ): 0.421677 1.31903 0.483471 1.20095
REMARK 3 1H METHYL SHIFTS: 0.118116
REMARK 3
REMARK 3 THE STRUCTURE IN THIS ENTRY IS THE RESTRAINED REGULARIZED
REMARK 3 MEAN STRUCTURE AND THE LAST NUMERIC COLUMN REPRESENTS THE
REMARK 3 RMS OF THE 40 INDIVIDUAL SIMULATED ANNEALING STRUCTURES
REMARK 3 FOUND IN PDB ENTRY 2EZY ABOUT THE MEAN COORDINATE
REMARK 3 POSITIONS. THE LAST NUMERIC COLUMN IN THE INDIVIDUAL SA
REMARK 3 STRUCTURES HAS NO MEANING.
REMARK 4
REMARK 4 2EZX 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_1000178070.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313
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 : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX600; DMX500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS MODIFIED MODIFIED
REMARK 210 METHOD USED : SEE REMARK 3
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : REGULARIZED MEAN STRUCTURE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE IN THIS ENTRY IS THE RESTRAINED REGULARIZED
REMARK 210 MEAN STRUCTURE.
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 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 PRO A 14 159.98 -41.59
REMARK 500 PHE A 39 74.47 -105.21
REMARK 500 CYS A 67 -30.02 -131.52
REMARK 500 PRO B 14 159.98 -41.51
REMARK 500 PHE B 39 74.55 -105.26
REMARK 500 CYS B 67 -30.05 -131.58
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2EZX A 1 89 UNP O75531 BAF_HUMAN 1 89
DBREF 2EZX B 1 89 UNP O75531 BAF_HUMAN 1 89
SEQRES 1 A 89 MET THR THR SER GLN LYS HIS ARG ASP PHE VAL ALA GLU
SEQRES 2 A 89 PRO MET GLY GLU LYS PRO VAL GLY SER LEU ALA GLY ILE
SEQRES 3 A 89 GLY GLU VAL LEU GLY LYS LYS LEU GLU GLU ARG GLY PHE
SEQRES 4 A 89 ASP LYS ALA TYR VAL VAL LEU GLY GLN PHE LEU VAL LEU
SEQRES 5 A 89 LYS LYS ASP GLU ASP LEU PHE ARG GLU TRP LEU LYS ASP
SEQRES 6 A 89 THR CYS GLY ALA ASN ALA LYS GLN SER ARG ASP CYS PHE
SEQRES 7 A 89 GLY CYS LEU ARG GLU TRP CYS ASP ALA PHE LEU
SEQRES 1 B 89 MET THR THR SER GLN LYS HIS ARG ASP PHE VAL ALA GLU
SEQRES 2 B 89 PRO MET GLY GLU LYS PRO VAL GLY SER LEU ALA GLY ILE
SEQRES 3 B 89 GLY GLU VAL LEU GLY LYS LYS LEU GLU GLU ARG GLY PHE
SEQRES 4 B 89 ASP LYS ALA TYR VAL VAL LEU GLY GLN PHE LEU VAL LEU
SEQRES 5 B 89 LYS LYS ASP GLU ASP LEU PHE ARG GLU TRP LEU LYS ASP
SEQRES 6 B 89 THR CYS GLY ALA ASN ALA LYS GLN SER ARG ASP CYS PHE
SEQRES 7 B 89 GLY CYS LEU ARG GLU TRP CYS ASP ALA PHE LEU
HELIX 1 1 GLN A 5 ALA A 12 1 8
HELIX 2 2 VAL A 20 SER A 22 5 3
HELIX 3 3 GLU A 28 ARG A 37 1 10
HELIX 4 4 ALA A 42 VAL A 51 1 10
HELIX 5 5 GLU A 56 CYS A 67 1 12
HELIX 6 6 ALA A 71 ALA A 87 1 17
HELIX 7 7 GLN B 5 ALA B 12 1 8
HELIX 8 8 VAL B 20 SER B 22 5 3
HELIX 9 9 GLU B 28 ARG B 37 1 10
HELIX 10 10 ALA B 42 VAL B 51 1 10
HELIX 11 11 GLU B 56 CYS B 67 1 12
HELIX 12 12 ALA B 71 ALA B 87 1 17
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 - 9 20 Bytes