Header list of 1dbd.pdb file
Complete list - 16 20 Bytes
HEADER GENE REGULATION 21-MAY-99 1DBD TITLE E2 DNA-BINDING DOMAIN FROM PAPILLOMAVIRUS BPV-1 CAVEAT 1DBD CHIRALITY ERRORS IN C-ALPHA CENTERS COMPND MOL_ID: 1; COMPND 2 MOLECULE: REGULATORY PROTEIN E2; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: DNA-BINDING DOMAIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BOVINE PAPILLOMAVIRUS TYPE 1; SOURCE 3 ORGANISM_TAXID: 10559; SOURCE 4 STRAIN: 1; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) PLYSS; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET32 KEYWDS DNA-BINDING DOMAIN, GENE REGULATION EXPDTA SOLUTION NMR AUTHOR S.VEERARAGHAVAN,C.C.MELLO,E.J.ANDROPHY,J.D.BALEJA REVDAT 4 16-FEB-22 1DBD 1 REMARK REVDAT 3 24-FEB-09 1DBD 1 VERSN REVDAT 2 28-FEB-00 1DBD 1 REMARK REVDAT 1 01-JAN-00 1DBD 0 JRNL AUTH S.VEERARAGHAVAN,C.C.MELLO,E.J.ANDROPHY,J.D.BALEJA JRNL TITL STRUCTURAL CORRELATES FOR ENHANCED STABILITY IN THE E2 JRNL TITL 2 DNA-BINDING DOMAIN FROM BOVINE PAPILLOMAVIRUS. JRNL REF BIOCHEMISTRY V. 38 16115 1999 JRNL REFN ISSN 0006-2960 JRNL PMID 10587434 JRNL DOI 10.1021/BI991633X REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1DBD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-MAY-99. REMARK 100 THE DEPOSITION ID IS D_1000001098. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 308.3 REMARK 210 PH : 5.75 REMARK 210 IONIC STRENGTH : 0.1 REMARK 210 PRESSURE : 1 ATM 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 : AMX; AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : INSIGHT, X-PLOR REMARK 210 METHOD USED : DG/SA REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 20 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : MINIMIZED AVERAGE 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: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ARG A 2 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES REMARK 500 THR A 3 C - N - CA ANGL. DEV. = 15.9 DEGREES REMARK 500 THR A 3 N - CA - CB ANGL. DEV. = 13.5 DEGREES REMARK 500 ARG A 40 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES 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 ARG A 2 -72.54 -89.36 REMARK 500 THR A 4 64.92 -106.64 REMARK 500 ASN A 5 -150.71 -99.95 REMARK 500 SER A 22 59.47 -95.79 REMARK 500 LYS A 37 -71.50 -55.96 REMARK 500 HIS A 41 4.48 -64.91 REMARK 500 GLU A 44 -67.32 -107.49 REMARK 500 THR A 47 -159.70 -86.38 REMARK 500 THR A 48 -151.80 -88.80 REMARK 500 ASP A 55 -72.43 -89.52 REMARK 500 ALA A 58 35.02 -71.34 REMARK 500 ARG A 60 -167.39 -117.56 REMARK 500 ARG B 2 -97.72 -66.81 REMARK 500 THR B 4 76.44 -102.59 REMARK 500 ASN B 5 -111.75 -99.88 REMARK 500 GLU B 44 -72.30 -108.14 REMARK 500 ASP B 55 -76.80 -91.27 REMARK 500 ALA B 58 26.27 -73.26 REMARK 500 ARG B 60 -162.47 -114.86 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 ASP A 6 GLY A 7 140.53 REMARK 500 ARG B 1 ARG B 2 60.91 REMARK 500 ARG B 2 THR B 3 38.39 REMARK 500 ASP B 6 GLY B 7 86.43 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 42 0.10 SIDE CHAIN REMARK 500 ARG A 60 0.14 SIDE CHAIN REMARK 500 ARG B 2 0.15 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1DBD A 1 100 UNP P03122 VE2_BPV1 311 410 DBREF 1DBD B 1 100 UNP P03122 VE2_BPV1 311 410 SEQRES 1 A 100 ARG ARG THR THR ASN ASP GLY PHE HIS LEU LEU LYS ALA SEQRES 2 A 100 GLY GLY SER CYS PHE ALA LEU ILE SER GLY THR ALA ASN SEQRES 3 A 100 GLN VAL LYS CYS TYR ARG PHE ARG VAL LYS LYS ASN HIS SEQRES 4 A 100 ARG HIS ARG TYR GLU ASN CYS THR THR THR TRP PHE THR SEQRES 5 A 100 VAL ALA ASP ASN GLY ALA GLU ARG GLN GLY GLN ALA GLN SEQRES 6 A 100 ILE LEU ILE THR PHE GLY SER PRO SER GLN ARG GLN ASP SEQRES 7 A 100 PHE LEU LYS HIS VAL PRO LEU PRO PRO GLY MET ASN ILE SEQRES 8 A 100 SER GLY PHE THR ALA SER LEU ASP PHE SEQRES 1 B 100 ARG ARG THR THR ASN ASP GLY PHE HIS LEU LEU LYS ALA SEQRES 2 B 100 GLY GLY SER CYS PHE ALA LEU ILE SER GLY THR ALA ASN SEQRES 3 B 100 GLN VAL LYS CYS TYR ARG PHE ARG VAL LYS LYS ASN HIS SEQRES 4 B 100 ARG HIS ARG TYR GLU ASN CYS THR THR THR TRP PHE THR SEQRES 5 B 100 VAL ALA ASP ASN GLY ALA GLU ARG GLN GLY GLN ALA GLN SEQRES 6 B 100 ILE LEU ILE THR PHE GLY SER PRO SER GLN ARG GLN ASP SEQRES 7 B 100 PHE LEU LYS HIS VAL PRO LEU PRO PRO GLY MET ASN ILE SEQRES 8 B 100 SER GLY PHE THR ALA SER LEU ASP PHE HELIX 1 1 ALA A 25 ARG A 42 1 18 HELIX 2 2 PRO A 73 HIS A 82 1 10 HELIX 3 3 ALA B 25 VAL B 35 1 11 HELIX 4 4 HIS B 39 ARG B 42 5 4 HELIX 5 5 PRO B 73 HIS B 82 1 10 SHEET 1 A 3 ALA A 64 PHE A 70 0 SHEET 2 A 3 CYS A 17 GLY A 23 -1 N GLY A 23 O ALA A 64 SHEET 3 A 3 ILE A 91 PHE A 94 -1 N PHE A 94 O PHE A 18 SHEET 1 B 3 ILE B 91 PHE B 94 0 SHEET 2 B 3 PHE B 18 GLY B 23 -1 N LEU B 20 O SER B 92 SHEET 3 B 3 ALA B 64 ILE B 68 -1 N ILE B 68 O ALA B 19 CISPEP 1 ARG A 2 THR A 3 0 17.41 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