Header list of 1b28.pdb file
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HEADER TRANSLATION/REGULATION 05-DEC-98 1B28 TITLE ARC REPRESSOR MYL MUTANT FROM SALMONELLA BACTERIOPHAGE P22 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (REGULATORY PROTEIN ARC); COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES; COMPND 5 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE P22; SOURCE 3 ORGANISM_TAXID: 10754; SOURCE 4 GENE: MUTATED ARC GENE; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: X90; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PSA300-MYL KEYWDS TRANSCRIPTION REGULATION, HYPERSTABLE MUTANT, ARC REPRESSOR, KEYWDS 2 TRANSLATION-REGULATION COMPLEX EXPDTA SOLUTION NMR NUMMDL 14 AUTHOR A.W.M.RIETVELD,I.M.A.NOOREN,R.T.SAUER,R.KAPTEIN,R.BOELENS REVDAT 4 03-NOV-21 1B28 1 REMARK SEQADV REVDAT 3 24-FEB-09 1B28 1 VERSN REVDAT 2 01-APR-03 1B28 1 JRNL REVDAT 1 03-NOV-99 1B28 0 JRNL AUTH I.M.NOOREN,A.W.RIETVELD,G.MELACINI,R.T.SAUER,R.KAPTEIN, JRNL AUTH 2 R.BOELENS JRNL TITL THE SOLUTION STRUCTURE AND DYNAMICS OF AN ARC REPRESSOR JRNL TITL 2 MUTANT REVEAL PREMELTING CONFORMATIONAL CHANGES RELATED TO JRNL TITL 3 DNA BINDING. JRNL REF BIOCHEMISTRY V. 38 6035 1999 JRNL REFN ISSN 0006-2960 JRNL PMID 10320329 JRNL DOI 10.1021/BI982677T REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH C.D.WALDBURGER,J.F.SCHILDBACH,R.T.SAUER REMARK 1 TITL ARE BURIED SALT BRIDGES IMPORTANT FOR PROTEIN STABILITY AND REMARK 1 TITL 2 CONFORMATIONAL SPECIFICITY? REMARK 1 REF NAT.STRUCT.BIOL. V. 2 122 1995 REMARK 1 REFN ISSN 1072-8368 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DISCOVER REMARK 3 AUTHORS : BIOSYM REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1B28 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-DEC-98. REMARK 100 THE DEPOSITION ID IS D_1000000225. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 4.5 REMARK 210 IONIC STRENGTH : 50 MM KPI, 150 MM NACL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; ROESY; 3D-NOESY REMARK 210 -HSQC; 3D TOCSY-HSQC REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : AMX500; DMX600 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DISCOVER REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 40 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 14 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION AND REMARK 210 TOTAL ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING MULTI-DIMENSIONAL NMR REMARK 210 SPECTROCOPY ON 15N LABELED ARC-MYL 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 HA LYS A 6 HB3 ARG B 113 1.02 REMARK 500 HB2 LYS A 46 HH21 ARG A 50 1.25 REMARK 500 REMARK 500 REMARK: NULL 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 1 TRP A 14 CD1 - NE1 - CE2 ANGL. DEV. = -5.5 DEGREES REMARK 500 1 TRP B 114 CD1 - NE1 - CE2 ANGL. DEV. = -5.7 DEGREES REMARK 500 2 TRP A 14 CD1 - NE1 - CE2 ANGL. DEV. = -5.7 DEGREES REMARK 500 2 TRP B 114 CD1 - NE1 - CE2 ANGL. DEV. = -5.6 DEGREES REMARK 500 3 TRP A 14 CD1 - NE1 - CE2 ANGL. DEV. = -5.7 DEGREES REMARK 500 3 TRP B 114 CD1 - NE1 - CE2 ANGL. DEV. = -5.7 DEGREES REMARK 500 4 TRP A 14 CD1 - NE1 - CE2 ANGL. DEV. = -5.6 DEGREES REMARK 500 4 TRP B 114 CD1 - NE1 - CE2 ANGL. DEV. = -5.7 DEGREES REMARK 500 5 TRP A 14 CD1 - NE1 - CE2 ANGL. DEV. = -5.7 DEGREES REMARK 500 5 TRP B 114 CD1 - NE1 - CE2 ANGL. DEV. = -5.7 DEGREES REMARK 500 6 TRP A 14 CD1 - NE1 - CE2 ANGL. DEV. = -5.7 DEGREES REMARK 500 6 TRP B 114 CD1 - NE1 - CE2 ANGL. DEV. = -5.5 DEGREES REMARK 500 7 TRP A 14 CD1 - NE1 - CE2 ANGL. DEV. = -5.7 DEGREES REMARK 500 7 TRP B 114 CD1 - NE1 - CE2 ANGL. DEV. = -5.6 DEGREES REMARK 500 8 TRP A 14 CD1 - NE1 - CE2 ANGL. DEV. = -5.6 DEGREES REMARK 500 8 TRP B 114 CD1 - NE1 - CE2 ANGL. DEV. = -5.7 DEGREES REMARK 500 9 TRP A 14 CD1 - NE1 - CE2 ANGL. DEV. = -5.6 DEGREES REMARK 500 9 TRP B 114 CD1 - NE1 - CE2 ANGL. DEV. = -5.6 DEGREES REMARK 500 10 TRP A 14 CD1 - NE1 - CE2 ANGL. DEV. = -5.6 DEGREES REMARK 500 10 TRP B 114 CD1 - NE1 - CE2 ANGL. DEV. = -5.7 DEGREES REMARK 500 11 TRP A 14 CD1 - NE1 - CE2 ANGL. DEV. = -5.6 DEGREES REMARK 500 11 TRP B 114 CD1 - NE1 - CE2 ANGL. DEV. = -5.7 DEGREES REMARK 500 12 TRP A 14 CD1 - NE1 - CE2 ANGL. DEV. = -5.8 DEGREES REMARK 500 12 TRP B 114 CD1 - NE1 - CE2 ANGL. DEV. = -5.6 DEGREES REMARK 500 13 TRP A 14 CD1 - NE1 - CE2 ANGL. DEV. = -5.4 DEGREES REMARK 500 13 TRP B 114 CD1 - NE1 - CE2 ANGL. DEV. = -5.7 DEGREES REMARK 500 14 TRP A 14 CD1 - NE1 - CE2 ANGL. DEV. = -5.7 DEGREES REMARK 500 14 TRP B 114 CD1 - NE1 - CE2 ANGL. DEV. = -5.6 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 1 LYS A 2 112.26 84.22 REMARK 500 1 MET A 4 -52.75 -135.80 REMARK 500 1 SER A 5 -56.04 -146.51 REMARK 500 1 MET A 7 -60.51 -137.26 REMARK 500 1 PHE A 45 69.09 -103.40 REMARK 500 1 LYS A 47 33.28 118.44 REMARK 500 1 ARG A 50 -87.81 -112.38 REMARK 500 1 LYS B 102 109.44 -171.88 REMARK 500 1 MET B 104 -64.32 -101.25 REMARK 500 1 SER B 105 -71.81 -85.50 REMARK 500 1 LYS B 106 -86.96 -145.11 REMARK 500 1 LYS B 146 -36.94 165.69 REMARK 500 1 GLU B 148 -32.85 169.70 REMARK 500 1 ARG B 150 -84.21 -105.49 REMARK 500 2 LYS A 2 103.71 -169.37 REMARK 500 2 SER A 5 -95.17 -77.59 REMARK 500 2 LYS A 6 -54.33 -126.83 REMARK 500 2 PHE A 45 67.35 -152.26 REMARK 500 2 LYS A 47 33.58 126.67 REMARK 500 2 ARG A 50 -85.78 -123.71 REMARK 500 2 LYS B 102 108.38 133.50 REMARK 500 2 MET B 104 -50.92 -139.02 REMARK 500 2 SER B 105 -33.89 -160.55 REMARK 500 2 LYS B 106 35.66 -87.02 REMARK 500 2 MET B 107 -49.47 -132.57 REMARK 500 2 SER B 144 -66.67 -97.57 REMARK 500 2 LYS B 146 -42.52 -138.15 REMARK 500 2 LYS B 147 48.18 138.64 REMARK 500 2 GLU B 148 -30.63 -151.54 REMARK 500 2 ILE B 151 -53.64 -120.65 REMARK 500 3 LYS A 2 99.39 143.87 REMARK 500 3 MET A 4 -39.30 -140.26 REMARK 500 3 SER A 5 -40.59 -159.92 REMARK 500 3 LYS A 6 30.06 -86.38 REMARK 500 3 MET A 7 -48.64 -149.68 REMARK 500 3 SER A 44 -71.94 -93.72 REMARK 500 3 LYS A 46 -58.83 169.61 REMARK 500 3 ARG A 50 -84.95 -131.57 REMARK 500 3 LYS B 102 106.93 115.96 REMARK 500 3 MET B 104 36.56 -173.71 REMARK 500 3 MET B 107 46.05 -162.07 REMARK 500 3 LYS B 146 -59.62 -166.82 REMARK 500 3 LYS B 147 23.71 163.59 REMARK 500 3 ARG B 150 -97.26 -137.92 REMARK 500 4 LYS A 2 -76.39 132.29 REMARK 500 4 MET A 4 43.81 -162.66 REMARK 500 4 SER A 5 -37.38 78.00 REMARK 500 4 MET A 7 -47.85 -151.50 REMARK 500 4 PHE A 45 99.59 -69.18 REMARK 500 4 LYS A 46 -41.66 161.21 REMARK 500 REMARK 500 THIS ENTRY HAS 207 RAMACHANDRAN OUTLIERS. 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 1 TYR A 36 0.07 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1B28 A 1 53 UNP P03050 RARC_BPP22 1 53 DBREF 1B28 B 101 153 UNP P03050 RARC_BPP22 1 53 SEQADV 1B28 MET A 31 UNP P03050 ARG 31 ENGINEERED MUTATION SEQADV 1B28 TYR A 36 UNP P03050 GLU 36 ENGINEERED MUTATION SEQADV 1B28 LEU A 40 UNP P03050 ARG 40 ENGINEERED MUTATION SEQADV 1B28 MET B 131 UNP P03050 ARG 31 ENGINEERED MUTATION SEQADV 1B28 TYR B 136 UNP P03050 GLU 36 ENGINEERED MUTATION SEQADV 1B28 LEU B 140 UNP P03050 ARG 40 ENGINEERED MUTATION SEQRES 1 A 53 MET LYS GLY MET SER LYS MET PRO GLN PHE ASN LEU ARG SEQRES 2 A 53 TRP PRO ARG GLU VAL LEU ASP LEU VAL ARG LYS VAL ALA SEQRES 3 A 53 GLU GLU ASN GLY MET SER VAL ASN SER TYR ILE TYR GLN SEQRES 4 A 53 LEU VAL MET GLU SER PHE LYS LYS GLU GLY ARG ILE GLY SEQRES 5 A 53 ALA SEQRES 1 B 53 MET LYS GLY MET SER LYS MET PRO GLN PHE ASN LEU ARG SEQRES 2 B 53 TRP PRO ARG GLU VAL LEU ASP LEU VAL ARG LYS VAL ALA SEQRES 3 B 53 GLU GLU ASN GLY MET SER VAL ASN SER TYR ILE TYR GLN SEQRES 4 B 53 LEU VAL MET GLU SER PHE LYS LYS GLU GLY ARG ILE GLY SEQRES 5 B 53 ALA HELIX 1 1 ARG A 16 GLU A 28 1 13 HELIX 2 2 VAL A 33 GLU A 43 1 11 HELIX 3 3 ARG B 116 GLU B 128 1 13 HELIX 4 4 VAL B 133 SER B 144 1 12 SHEET 1 A 2 GLN A 9 ARG A 13 0 SHEET 2 A 2 GLN B 109 ARG B 113 -1 N LEU B 112 O PHE A 10 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 - v 3 2 Bytes