Header list of 2bjc.pdb file
Complete list - n 15 2 Bytes
HEADER TRANSCRIPTION REGULATOR 01-FEB-05 2BJC TITLE NMR STRUCTURE OF A PROTEIN-DNA COMPLEX OF AN ALTERED SPECIFICITY TITLE 2 MUTANT OF THE LAC REPRESSOR HEADPIECE THAT MIMICS THE GAL REPRESSOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: LACTOSE OPERON REPRESSOR; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: DNA BINDING DOMAIN, LAC HEADPIECE RESIDUES 1-62; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 OTHER_DETAILS: THE PROTEIN IS A DIMER. DISULFIDE BOND BETWEEN CYS52 COMPND 8 IN TWO MONOMERS FORMS A COVALENT DIMER; COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: 5'-D(*GP*AP*AP*TP*TP*GP*TP*AP*AP*GP COMPND 11 *CP*GP*CP*TP*TP*AP*CP*AP*AP*TP*TP*C)-3'; COMPND 12 CHAIN: C, D; COMPND 13 SYNONYM: LAC-GAL OPERATOR; COMPND 14 ENGINEERED: YES; COMPND 15 OTHER_DETAILS: ALTERED LAC SYML OPERATOR SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 562; SOURCE 4 STRAIN: DH9; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: DH9; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET3A / PGP1-2; SOURCE 9 MOL_ID: 2; SOURCE 10 SYNTHETIC: YES KEYWDS TRANSCRIPTION REGULATOR, SYMMETRIC DNA-BINDING, DNA-BINDING, HTH, LAC KEYWDS 2 OPERON, LAC REPRESSOR, ALTERED SPECIFICITY, MUTANT, REPRESSOR, KEYWDS 3 TRANSCRIPTION REGULATION, TRANSCRIPTION REGULATOR/DNA, GAL KEYWDS 4 REPRESSOR, GAL OPERON, LAC HEADPIECE, SYMMETRIC DIMER EXPDTA SOLUTION NMR NUMMDL 16 AUTHOR R.K.SALINAS,G.E.FOLKERS,A.M.J.J.BONVIN,D.DAS,R.BOELENS,R.KAPTEIN REVDAT 3 15-JAN-20 2BJC 1 REMARK REVDAT 2 24-FEB-09 2BJC 1 VERSN REVDAT 1 18-OCT-05 2BJC 0 JRNL AUTH R.K.SALINAS,G.E.FOLKERS,A.M.J.J.BONVIN,D.DAS,R.BOELENS, JRNL AUTH 2 R.KAPTEIN JRNL TITL ALTERED SPECIFICITY IN DNA BINDING BY THE LAC REPRESSOR: A JRNL TITL 2 MUTANT LAC HEADPIECE THAT MIMICS THE GAL REPRESSOR JRNL REF CHEMBIOCHEM V. 6 1628 2005 JRNL REFN ISSN 1439-4227 JRNL PMID 16094693 JRNL DOI 10.1002/CBIC.200500049 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH C.G.KALODIMOS,A.M.J.J.BONVIN,R.K.SALINAS,R.WECHSELBERGER, REMARK 1 AUTH 2 R.BOELENS,R.KAPTEIN REMARK 1 TITL PLASTICITY IN PROTEIN-DNA RECOGNITION: LAC REPRESSOR REMARK 1 TITL 2 INTERACTS WITH ITS NATURAL OPERATOR O1 THROUGH ALTERNATIVE REMARK 1 TITL 3 CONFORMATIONS OF ITS DNA BINDING DOMAIN REMARK 1 REF EMBO J. V. 21 2866 2002 REMARK 1 REFN ISSN 0261-4189 REMARK 1 PMID 12065400 REMARK 1 DOI 10.1093/EMBOJ/CDF318 REMARK 1 REFERENCE 2 REMARK 1 AUTH N.LEHMING,J.SARTORIUS,M.NIEMOLER,G.GENENGER, REMARK 1 AUTH 2 B.WILCKEN-BERGMANN,B.MULLER-HILL REMARK 1 TITL THE INTERACTION OF THE RECOGNITION HELIX OF LAC REPRESSOR REMARK 1 TITL 2 WITH LAC OPERATOR REMARK 1 REF EMBO J. V. 6 3145 1987 REMARK 1 REFN ISSN 0261-4189 REMARK 1 PMID 2826131 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: REFINEMENT DETAILS CAN BE FOUND IN THE REMARK 3 JRNL CITATION ABOVE REMARK 4 REMARK 4 2BJC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-FEB-05. REMARK 100 THE DEPOSITION ID IS D_1290022790. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 315.0 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : 20 REMARK 210 PRESSURE : 1.0 ATM REMARK 210 SAMPLE CONTENTS : 95% WATER/5% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D 15N NOESY-HSQC 3D 13C NOESY REMARK 210 -HSQC 2D NOESY 2D NOESY WITH X- REMARK 210 FILTERS 3D CBCACONH 3D HNCO 3D REMARK 210 HBHACONH 3D HCCCONH 3D HCCH- REMARK 210 TOCSY 2D 1H-13C HSQC 2D 1H-15N REMARK 210 HSQC 2D 1H-15N J- MODULATED HSQC REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ REMARK 210 SPECTROMETER MODEL : DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : CNS REMARK 210 METHOD USED : HADDOCK REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 16 REMARK 210 CONFORMERS, SELECTION CRITERIA : RMSD TO AVERAGE STRUCTURE AND REMARK 210 LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 3 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE RESONANCE NMR REMARK 210 SPECTROSCOPY ON A 13C, 15N LABELED PROTEIN AND UNLABELED DNA. 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D 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 400 REMARK 400 COMPOUND REMARK 400 ENGINEERED RESIDUES TYR 17 VAL, GLN 18 ALA AND VAL 52 REMARK 400 CYS IN CHAINS A AND B 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 H21 DG C 10 O2 DC D 113 1.47 REMARK 500 O2 DC C 13 H21 DG D 110 1.49 REMARK 500 O4 DT C 7 H61 DA D 116 1.59 REMARK 500 O2 DC C 22 H21 DG D 101 1.60 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 3 -161.83 -76.13 REMARK 500 1 ALA A 27 -80.06 21.16 REMARK 500 1 SER A 28 -84.04 64.82 REMARK 500 1 ASN A 46 63.55 75.55 REMARK 500 1 PRO B 103 -164.53 -78.23 REMARK 500 1 VAL B 115 -168.26 -44.81 REMARK 500 1 ALA B 127 -79.69 21.30 REMARK 500 1 SER B 128 -84.22 66.02 REMARK 500 1 ASN B 146 65.43 78.03 REMARK 500 2 LYS A 2 86.61 -167.79 REMARK 500 2 PRO A 3 -167.27 -79.44 REMARK 500 2 GLN A 26 59.92 70.29 REMARK 500 2 ALA A 27 -72.11 4.54 REMARK 500 2 SER A 28 -77.40 63.16 REMARK 500 2 SER A 31 156.69 97.17 REMARK 500 2 ASN A 46 61.31 75.39 REMARK 500 2 SER A 61 -64.04 -152.08 REMARK 500 2 LYS B 102 87.21 -165.26 REMARK 500 2 PRO B 103 -167.28 -79.55 REMARK 500 2 GLN B 126 60.25 69.18 REMARK 500 2 ALA B 127 -71.08 7.07 REMARK 500 2 SER B 128 -80.89 63.96 REMARK 500 2 SER B 131 156.86 95.94 REMARK 500 2 ASN B 146 63.25 74.49 REMARK 500 2 SER B 161 -62.11 -151.94 REMARK 500 3 VAL A 15 -167.06 -45.34 REMARK 500 3 ALA A 27 -92.28 33.87 REMARK 500 3 SER A 28 -37.50 72.28 REMARK 500 3 ASN A 46 64.67 74.98 REMARK 500 3 LYS A 59 50.50 -109.08 REMARK 500 3 GLN A 60 -77.13 -61.99 REMARK 500 3 ALA B 127 -92.26 32.30 REMARK 500 3 SER B 128 -38.87 71.01 REMARK 500 3 ASN B 146 63.09 75.09 REMARK 500 3 LYS B 159 52.43 -105.29 REMARK 500 3 GLN B 160 -73.07 -63.40 REMARK 500 4 ALA A 27 -87.07 26.45 REMARK 500 4 SER A 28 -83.25 70.26 REMARK 500 4 HIS A 29 35.01 -83.63 REMARK 500 4 ASN A 46 62.03 72.58 REMARK 500 4 SER A 61 -67.35 -146.58 REMARK 500 4 GLN B 126 -25.85 99.81 REMARK 500 4 ALA B 127 -70.83 105.53 REMARK 500 4 SER B 128 -89.66 56.01 REMARK 500 4 ASN B 146 64.06 73.19 REMARK 500 4 SER B 161 -71.08 -151.48 REMARK 500 5 PRO A 3 -174.91 -67.07 REMARK 500 5 GLN A 26 -38.84 94.69 REMARK 500 5 ALA A 27 112.59 58.08 REMARK 500 5 ASN A 46 71.82 82.91 REMARK 500 REMARK 500 THIS ENTRY HAS 187 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED. REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1CJG RELATED DB: PDB REMARK 900 NMR STRUCTURE OF LAC REPRESSOR HP62- DEOXYRIBONUCLEIC ACID COMPLEX REMARK 900 RELATED ID: 1EFA RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE LAC REPRESSOR DIMER BOUND TO OPERATOR AND REMARK 900 THE ANTI-INDUCER ONPF REMARK 900 RELATED ID: 1JWL RELATED DB: PDB REMARK 900 STRUCTURE OF THE DIMERIC LAC REPRESSOR/ OPERATOR O1/ONPFCOMPLEX REMARK 900 RELATED ID: 1JYE RELATED DB: PDB REMARK 900 STRUCTURE OF A DIMERIC LAC REPRESSOR WITH C-TERMINALDELETION AND REMARK 900 K84L SUBSTITUTION REMARK 900 RELATED ID: 1JYF RELATED DB: PDB REMARK 900 STRUCTURE OF THE DIMERIC LAC REPRESSOR WITH AN 11-RESIDUE C- REMARK 900 TERMINAL DELETION. REMARK 900 RELATED ID: 1L1M RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF A DIMER OF LAC REPRESSOR DNA-BINDINGDOMAIN REMARK 900 COMPLEXED TO ITS NATURAL OPERATOR O1 REMARK 900 RELATED ID: 1LBG RELATED DB: PDB REMARK 900 LACTOSE OPERON REPRESSOR BOUND TO 21-BASE PAIR SYMMETRIC OPERATOR REMARK 900 DEOXYRIBONUCLEIC ACID, ALPHA CARBONS ONLY REMARK 900 RELATED ID: 1LBH RELATED DB: PDB REMARK 900 INTACT LACTOSE OPERON REPRESSOR WITH GRATUITOUS INDUCER IPTG REMARK 900 RELATED ID: 1LBI RELATED DB: PDB REMARK 900 LAC REPRESSOR REMARK 900 RELATED ID: 1LCC RELATED DB: PDB REMARK 900 LAC REPRESSOR ("HEADPIECE") COMPLEX WITH AN 11 BASE-PAIR HALF- REMARK 900 OPERATOR CORRESPONDING TO THE LEFT HALF OF THE WILD TYPE LAC REMARK 900 OPERATOR (NMR, BEST STRUCTURE) REMARK 900 RELATED ID: 1LCD RELATED DB: PDB REMARK 900 LAC REPRESSOR ("HEADPIECE") COMPLEX WITH AN 11 BASE-PAIR HALF- REMARK 900 OPERATOR CORRESPONDING TO THE LEFT HALF OF THE WILD TYPE LAC REMARK 900 OPERATOR (NMR, 3 STRUCTURES) REMARK 900 RELATED ID: 1LQC RELATED DB: PDB REMARK 900 LAC REPRESSOR HEADPIECE (RESIDUES 1-56), NMR, 32 STRUCTURES REMARK 900 RELATED ID: 1LTP RELATED DB: PDB REMARK 900 RELATED ID: 1OSL RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF A DIMERIC LACTOSE DNA -BINDING REMARK 900 DOMAINCOMPLEXED TO A NONSPECIFIC DNA SEQUENCE REMARK 900 RELATED ID: 1TLF RELATED DB: PDB REMARK 900 TRYPTIC CORE FRAGMENT OF THE LACTOSE REPRESSOR OF ESCHERICHIA COLI REMARK 900 RELATED ID: 7354 RELATED DB: BMRB REMARK 999 REMARK 999 SEQUENCE REMARK 999 RESIDUES 1-62 OF LAC REPRESSOR (P03023) WITH THE REMARK 999 SUBSTITUTIONS Y17V Q18A AND V52C REMARK 999 ALTERED PALINDROME OF THE LEFT SIDE OF THE LAC OPERATOR O1 REMARK 999 LACKING THE CENTRAL BASE PAIR.ORIGINAL BASE PAIR GC7 WAS REMARK 999 SUBSTITUTED BY AT DBREF 2BJC A 1 62 UNP P03023 LACI_ECOLI 1 62 DBREF 2BJC B 101 162 UNP P03023 LACI_ECOLI 1 62 DBREF 2BJC C 1 22 PDB 2BJC 2BJC 1 22 DBREF 2BJC D 101 122 PDB 2BJC 2BJC 101 122 SEQADV 2BJC VAL A 17 UNP P03023 TYR 17 ENGINEERED MUTATION SEQADV 2BJC ALA A 18 UNP P03023 GLN 18 ENGINEERED MUTATION SEQADV 2BJC CYS A 52 UNP P03023 VAL 52 ENGINEERED MUTATION SEQADV 2BJC VAL B 117 UNP P03023 TYR 17 ENGINEERED MUTATION SEQADV 2BJC ALA B 118 UNP P03023 GLN 18 ENGINEERED MUTATION SEQADV 2BJC CYS B 152 UNP P03023 VAL 52 ENGINEERED MUTATION SEQRES 1 A 62 MET LYS PRO VAL THR LEU TYR ASP VAL ALA GLU TYR ALA SEQRES 2 A 62 GLY VAL SER VAL ALA THR VAL SER ARG VAL VAL ASN GLN SEQRES 3 A 62 ALA SER HIS VAL SER ALA LYS THR ARG GLU LYS VAL GLU SEQRES 4 A 62 ALA ALA MET ALA GLU LEU ASN TYR ILE PRO ASN ARG CYS SEQRES 5 A 62 ALA GLN GLN LEU ALA GLY LYS GLN SER LEU SEQRES 1 B 62 MET LYS PRO VAL THR LEU TYR ASP VAL ALA GLU TYR ALA SEQRES 2 B 62 GLY VAL SER VAL ALA THR VAL SER ARG VAL VAL ASN GLN SEQRES 3 B 62 ALA SER HIS VAL SER ALA LYS THR ARG GLU LYS VAL GLU SEQRES 4 B 62 ALA ALA MET ALA GLU LEU ASN TYR ILE PRO ASN ARG CYS SEQRES 5 B 62 ALA GLN GLN LEU ALA GLY LYS GLN SER LEU SEQRES 1 C 22 DG DA DA DT DT DG DT DA DA DG DC DG DC SEQRES 2 C 22 DT DT DA DC DA DA DT DT DC SEQRES 1 D 22 DG DA DA DT DT DG DT DA DA DG DC DG DC SEQRES 2 D 22 DT DT DA DC DA DA DT DT DC HELIX 1 1 THR A 5 ALA A 13 1 9 HELIX 2 2 VAL A 17 ASN A 25 1 9 HELIX 3 3 ALA A 32 LEU A 45 1 14 HELIX 4 4 ALA A 53 GLY A 58 1 6 HELIX 5 5 THR B 105 ALA B 113 1 9 HELIX 6 6 VAL B 117 ASN B 125 1 9 HELIX 7 7 ALA B 132 LEU B 145 1 14 HELIX 8 8 ALA B 153 GLY B 158 1 6 SSBOND 1 CYS A 52 CYS B 152 1555 1555 2.03 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 - n 15 2 Bytes