Header list of 1hsn.pdb file
Complete list - b 23 2 Bytes
HEADER DNA-BINDING 17-NOV-94 1HSN
TITLE THE STRUCTURE OF THE HMG BOX AND ITS INTERACTION WITH DNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HIGH MOBILITY GROUP PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CRICETULUS GRISEUS;
SOURCE 3 ORGANISM_COMMON: CHINESE HAMSTER;
SOURCE 4 ORGANISM_TAXID: 10029;
SOURCE 5 GENE: INSERT DERIVED BY PCR;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: DH5 ALPHA;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PGEX-2T;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-2T GENE: INSERT DERIVED BY PCR
KEYWDS DNA-BINDING
EXPDTA SOLUTION NMR
NUMMDL 49
AUTHOR C.M.READ,P.D.CARY,C.CRANE-ROBINSON,P.C.DRISCOLL,M.O.M.CARILLO,
AUTHOR 2 D.G.NORMAN
REVDAT 3 23-FEB-22 1HSN 1 REMARK LINK
REVDAT 2 24-FEB-09 1HSN 1 VERSN
REVDAT 1 07-FEB-95 1HSN 0
JRNL AUTH C.M.READ,P.D.CARY,C.CRANE-ROBINSON,P.C.DRISCOLL,
JRNL AUTH 2 M.O.M.CARILLO,D.G.NORMAN
JRNL TITL THE STRUCTURE OF THE HMG BOX AND ITS INTERACTION WITH DNA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.M.READ,P.D.CARY,C.CRANE-ROBINSON,P.C.DRISCOLL,D.G.NORMAN
REMARK 1 TITL SOLUTION STRUCTURE OF A DNA-BINDING DOMAIN FROM HMG1
REMARK 1 REF NUCLEIC ACIDS RES. V. 21 3427 1993
REMARK 1 REFN ISSN 0305-1048
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.0
REMARK 3 AUTHORS : NILGES (SIMULATED ANNEALING), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1HSN 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_1000173999.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
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 : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 49
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: 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 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 82
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HSM RELATED DB: PDB
DBREF 1HSN A 3 81 UNP P07156 HMG1_CRIGR 92 170
SEQRES 1 A 79 ASN ALA PRO LYS ARG PRO PRO SER ALA PHE PHE LEU PHE
SEQRES 2 A 79 CYS SER GLU TYR ARG PRO LYS ILE LYS GLY GLU HIS PRO
SEQRES 3 A 79 GLY LEU SER ILE GLY ASP VAL ALA LYS LYS LEU GLY GLU
SEQRES 4 A 79 MET TRP ASN ASN THR ALA ALA ASP ASP LYS GLN PRO TYR
SEQRES 5 A 79 GLU LYS LYS ALA ALA LYS LEU LYS GLU LYS TYR GLU LYS
SEQRES 6 A 79 ASP ILE ALA ALA TYR ARG ALA LYS GLY LYS PRO ASP ALA
SEQRES 7 A 79 ALA
HET BME A 82 9
HETNAM BME BETA-MERCAPTOETHANOL
FORMUL 2 BME C2 H6 O S
HELIX 1 H1 PHE A 12 GLU A 18 1 7
HELIX 2 H1' PRO A 21 GLU A 26 1H1 AND H1' BEND AROUND H2 6
HELIX 3 H2 GLY A 33 ASN A 44 1 12
HELIX 4 H3 PRO A 53 ARG A 73 1 21
LINK SG CYS A 16 S2 BME A 82 1555 1555 2.02
SITE 1 AC1 4 PHE A 13 CYS A 16 SER A 17 ARG A 20
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 23 2 Bytes