Header list of 1bby.pdb file
Complete list - 16 20 Bytes
HEADER TRANSCRIPTION REGULATION 26-APR-98 1BBY
TITLE DNA-BINDING DOMAIN FROM HUMAN RAP30, NMR, MINIMIZED AVERAGE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RAP30;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DNA-BINDING DOMAIN;
COMPND 5 SYNONYM: TRANSCRIPTION INITIATION FACTOR RAP30;
COMPND 6 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: HMS174 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET11D
KEYWDS AVERAGE STRUCTURE TRANSCRIPTION REGULATION, RAP30, DNA-BINDING
KEYWDS 2 DOMAIN, TRANSCRIPTION, TRANSCRIPTION REGULATION
EXPDTA SOLUTION NMR
AUTHOR C.M.GROFT,S.N.ULJON,R.WANG,M.H.WERNER
REVDAT 4 16-FEB-22 1BBY 1 REMARK
REVDAT 3 24-FEB-09 1BBY 1 VERSN
REVDAT 2 13-JAN-99 1BBY 1 SOURCE COMPND REMARK TITLE
REVDAT 2 2 1 EXPDTA KEYWDS HEADER
REVDAT 1 25-NOV-98 1BBY 0
JRNL AUTH C.M.GROFT,S.N.ULJON,R.WANG,M.H.WERNER
JRNL TITL STRUCTURAL HOMOLOGY BETWEEN THE RAP30 DNA-BINDING DOMAIN AND
JRNL TITL 2 LINKER HISTONE H5: IMPLICATIONS FOR PREINITIATION COMPLEX
JRNL TITL 3 ASSEMBLY.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 95 9117 1998
JRNL REFN ISSN 0027-8424
JRNL PMID 9689043
JRNL DOI 10.1073/PNAS.95.16.9117
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: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE.
REMARK 4
REMARK 4 1BBY 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_1000171571.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 297
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : 10MM PHOSPHATE, 50MM NACL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : AQUEOUS
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D/4D HETERONUCLEAR NOESY/ROESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX500; DMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.851
REMARK 210 METHOD USED : DYNAMICAL SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 150
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT AND ANGULAR
REMARK 210 VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: STRUCTURE DETERMINED USING STANDARD MULTI-NUCLEAR 3D/4D
REMARK 210 SPECTROSCOPY
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 HE21 GLN A 223 H ASN A 224 1.35
REMARK 500 O ASP A 179 H VAL A 183 1.46
REMARK 500 O ILE A 220 H LYS A 236 1.51
REMARK 500 O LEU A 187 H PHE A 191 1.55
REMARK 500 O VAL A 210 H LYS A 214 1.58
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 LYS A 207 30.16 -79.07
REMARK 500 LYS A 226 -166.65 -127.09
REMARK 500 ILE A 228 21.80 -78.70
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2BBY RELATED DB: PDB
DBREF 1BBY A 175 243 UNP P13984 T2FB_HUMAN 175 243
SEQRES 1 A 69 ARG ALA ARG ALA ASP LYS GLN HIS VAL LEU ASP MET LEU
SEQRES 2 A 69 PHE SER ALA PHE GLU LYS HIS GLN TYR TYR ASN LEU LYS
SEQRES 3 A 69 ASP LEU VAL ASP ILE THR LYS GLN PRO VAL VAL TYR LEU
SEQRES 4 A 69 LYS GLU ILE LEU LYS GLU ILE GLY VAL GLN ASN VAL LYS
SEQRES 5 A 69 GLY ILE HIS LYS ASN THR TRP GLU LEU LYS PRO GLU TYR
SEQRES 6 A 69 ARG HIS TYR GLN
HELIX 1 1 ASP A 179 LYS A 193 1 15
HELIX 2 2 LEU A 199 ILE A 205 1 7
HELIX 3 3 VAL A 210 GLU A 219 1 10
SHEET 1 S1 1 TYR A 196 TYR A 197 0
SHEET 1 S2 1 ILE A 220 VAL A 225 0
SHEET 1 S3 1 ASN A 231 GLU A 234 0
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 - 16 20 Bytes