Header list of 2ezy.pdb file
Complete list - r 9 2 Bytes
HEADER DNA BINDING PROTEIN 26-JUL-98 2EZY
TITLE SOLUTION STRUCTURE OF HUMAN BARRIER-TO-AUTOINTEGRATION FACTOR BAF,
TITLE 2 NMR, ENSEMBLE OF 20 SIMULATED ANNEALING STRUCTURES
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
NUMMDL 20
AUTHOR G.M.CLORE,M.CAI,A.M.GRONENBORN
REVDAT 3 09-MAR-22 2EZY 1 KEYWDS REMARK
REVDAT 2 24-FEB-09 2EZY 1 VERSN
REVDAT 1 13-JAN-99 2EZY 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 LAST NUMERIC COLUMN IN THE INDIVIDUAL SA STRUCTURES HAS NO
REMARK 3 MEANING.
REMARK 4
REMARK 4 2EZY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000178071.
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 : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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: 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: 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 OD1 ASP A 57 HH21 ARG A 60 1.53
REMARK 500 OD1 ASP B 57 HH21 ARG B 60 1.53
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 PRO A 14 157.83 -41.99
REMARK 500 1 PHE A 39 73.51 -104.05
REMARK 500 1 PHE A 88 -86.19 -106.43
REMARK 500 1 PRO B 14 157.96 -42.10
REMARK 500 1 PHE B 39 73.28 -103.82
REMARK 500 1 PHE B 88 -86.09 -106.54
REMARK 500 2 PRO A 14 164.64 -44.53
REMARK 500 2 CYS A 67 -31.34 -132.42
REMARK 500 2 PHE A 88 -87.27 -107.51
REMARK 500 2 PRO B 14 164.52 -44.50
REMARK 500 2 CYS B 67 -31.40 -132.41
REMARK 500 2 PHE B 88 -87.59 -107.42
REMARK 500 3 PRO A 14 160.02 -41.86
REMARK 500 3 PHE A 39 75.55 -104.37
REMARK 500 3 PHE A 88 -84.65 -104.07
REMARK 500 3 PRO B 14 159.90 -41.86
REMARK 500 3 PHE B 39 75.55 -104.13
REMARK 500 3 PHE B 88 -84.68 -104.08
REMARK 500 4 PRO A 14 159.97 -41.57
REMARK 500 4 LYS A 53 19.57 59.94
REMARK 500 4 PHE A 88 -85.71 -105.32
REMARK 500 4 PRO B 14 160.02 -41.54
REMARK 500 4 LYS B 53 19.55 59.94
REMARK 500 4 PHE B 88 -85.72 -105.28
REMARK 500 5 PRO A 14 160.06 -42.74
REMARK 500 5 PHE A 39 75.49 -102.09
REMARK 500 5 CYS A 67 -31.84 -130.61
REMARK 500 5 PRO B 14 160.37 -42.70
REMARK 500 5 PHE B 39 75.50 -101.95
REMARK 500 5 CYS B 67 -31.90 -130.40
REMARK 500 6 PRO A 14 159.03 -41.21
REMARK 500 6 CYS A 67 -36.75 -131.92
REMARK 500 6 PHE A 88 -85.90 -103.93
REMARK 500 6 PRO B 14 158.97 -41.20
REMARK 500 6 CYS B 67 -36.49 -131.75
REMARK 500 6 PHE B 88 -85.78 -103.97
REMARK 500 7 PRO A 14 162.92 -40.16
REMARK 500 7 PHE A 39 74.51 -104.09
REMARK 500 7 PRO B 14 162.82 -40.24
REMARK 500 7 PHE B 39 74.46 -104.22
REMARK 500 8 THR A 2 24.19 46.41
REMARK 500 8 PRO A 14 161.43 -41.98
REMARK 500 8 PHE A 39 73.91 -104.68
REMARK 500 8 THR B 2 24.35 46.24
REMARK 500 8 PRO B 14 161.44 -42.06
REMARK 500 8 PHE B 39 73.92 -104.82
REMARK 500 9 THR A 2 -157.05 -92.05
REMARK 500 9 PRO A 14 162.34 -44.92
REMARK 500 9 PHE A 39 75.61 -104.87
REMARK 500 9 LYS A 54 19.58 59.95
REMARK 500
REMARK 500 THIS ENTRY HAS 128 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2EZY A 1 89 UNP O75531 BAF_HUMAN 1 89
DBREF 2EZY 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
MODEL 1
Complete list - r 9 2 Bytes