HEADER TRANSCRIPTION 30-MAR-13 4BH9
TITLE A STRUCTURAL MODEL OF CAP MUTANT (T127L AND S128I) IN THE APO STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAMP-ACTIVATED GLOBAL TRANSCRIPTIONAL REGULATOR CRP;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CATABOLITE ACTIVATOR PROTEIN,CAP,CATABOLITE GENE ACTIVATOR,
COMPND 5 CAMP RECEPTOR PROTEIN,CRP,CAMP REGULATORY PROTEIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: CRP, CAP, CSM;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.R.TZENG,C.G.KALODIMOS
REVDAT 5 14-JUN-23 4BH9 1 REMARK
REVDAT 4 21-NOV-18 4BH9 1 COMPND SOURCE JRNL REMARK
REVDAT 4 2 1 DBREF
REVDAT 3 03-JUL-13 4BH9 1 JRNL
REVDAT 2 15-MAY-13 4BH9 1 COMPND JRNL ATOM MASTER
REVDAT 1 08-MAY-13 4BH9 0
JRNL AUTH S.R.TZENG,C.G.KALODIMOS
JRNL TITL ALLOSTERIC INHIBITION THROUGH SUPPRESSION OF TRANSIENT
JRNL TITL 2 CONFORMATIONAL STATES.
JRNL REF NAT. CHEM. BIOL. V. 9 462 2013
JRNL REFN ESSN 1552-4469
JRNL PMID 23644478
JRNL DOI 10.1038/NCHEMBIO.1250
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: NULL
REMARK 4
REMARK 4 4BH9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-MAR-13.
REMARK 100 THE DEPOSITION ID IS D_1290056340.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 305.0
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 500
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 10% WATER/90% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCA; HNCACB; HNCO; HNCOCA; 3D
REMARK 210 -15N-NOESY; 3D-13C-NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 700 MHZ
REMARK 210 SPECTROMETER MODEL : VNMRS; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CYANA, CNS
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS;
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NONE
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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: 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 LEU A 2 -177.38 63.81
REMARK 500 1 THR A 7 55.25 -100.44
REMARK 500 1 HIS A 21 164.43 176.63
REMARK 500 1 LYS A 22 -119.30 -167.60
REMARK 500 1 SER A 25 -168.59 57.31
REMARK 500 1 LYS A 26 -41.38 79.14
REMARK 500 1 HIS A 31 100.71 178.62
REMARK 500 1 GLN A 32 -57.37 179.28
REMARK 500 1 LYS A 35 106.03 -39.23
REMARK 500 1 GLU A 37 -58.37 70.87
REMARK 500 1 ILE A 42 96.70 -68.20
REMARK 500 1 GLN A 66 103.12 -55.10
REMARK 500 1 GLU A 81 54.55 -151.29
REMARK 500 1 ARG A 82 90.88 -32.92
REMARK 500 1 ALA A 84 153.79 175.86
REMARK 500 1 TRP A 85 -49.04 174.41
REMARK 500 1 ALA A 88 99.31 -67.90
REMARK 500 1 ALA A 91 108.06 -51.01
REMARK 500 1 THR A 140 101.23 -59.05
REMARK 500 1 ASP A 192 32.31 -82.86
REMARK 500 1 GLN A 193 35.52 70.82
REMARK 500 1 LEU A 195 -87.01 -138.35
REMARK 500 1 HIS A 199 24.60 -146.99
REMARK 500 2 GLN A 6 87.84 58.05
REMARK 500 2 THR A 7 -71.83 -71.38
REMARK 500 2 HIS A 21 142.23 -178.13
REMARK 500 2 LYS A 22 -132.81 -144.93
REMARK 500 2 SER A 25 -174.49 63.80
REMARK 500 2 LYS A 26 -20.24 72.29
REMARK 500 2 LEU A 29 -52.76 -142.31
REMARK 500 2 HIS A 31 -76.48 -162.86
REMARK 500 2 ALA A 36 -74.84 50.27
REMARK 500 2 GLU A 37 -50.78 81.37
REMARK 500 2 SER A 62 -166.50 -165.08
REMARK 500 2 GLN A 66 108.75 -40.61
REMARK 500 2 GLN A 80 39.07 -82.68
REMARK 500 2 ARG A 82 -36.69 -180.00
REMARK 500 2 SER A 83 -63.90 67.32
REMARK 500 2 ALA A 84 127.59 72.36
REMARK 500 2 TRP A 85 -27.84 177.88
REMARK 500 2 ALA A 91 96.33 -60.79
REMARK 500 2 LEU A 127 -65.26 -91.02
REMARK 500 2 LYS A 130 -68.46 -99.62
REMARK 500 2 VAL A 131 4.60 48.67
REMARK 500 2 ASN A 133 -42.79 -157.43
REMARK 500 2 LEU A 137 -45.84 81.19
REMARK 500 2 CYS A 178 -161.27 -107.41
REMARK 500 2 LEU A 195 -80.00 -122.32
REMARK 500 2 SER A 197 73.11 -115.39
REMARK 500 2 THR A 208 47.92 -90.35
REMARK 500
REMARK 500 THIS ENTRY HAS 498 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4BHP RELATED DB: PDB
REMARK 900 A STRUCTURAL MODEL OF CAP MUTANT (T127L AND S128I) IN CGMP-BOUND
REMARK 900 STATE
REMARK 900 RELATED ID: 19144 RELATED DB: BMRB
DBREF 4BH9 A 1 209 UNP P0ACJ8 CRP_ECOLI 2 210
SEQADV 4BH9 LEU A 127 UNP P0ACJ8 THR 128 ENGINEERED MUTATION
SEQADV 4BH9 ILE A 128 UNP P0ACJ8 SER 129 ENGINEERED MUTATION
SEQRES 1 A 209 VAL LEU GLY LYS PRO GLN THR ASP PRO THR LEU GLU TRP
SEQRES 2 A 209 PHE LEU SER HIS CYS HIS ILE HIS LYS TYR PRO SER LYS
SEQRES 3 A 209 SER THR LEU ILE HIS GLN GLY GLU LYS ALA GLU THR LEU
SEQRES 4 A 209 TYR TYR ILE VAL LYS GLY SER VAL ALA VAL LEU ILE LYS
SEQRES 5 A 209 ASP GLU GLU GLY LYS GLU MET ILE LEU SER TYR LEU ASN
SEQRES 6 A 209 GLN GLY ASP PHE ILE GLY GLU LEU GLY LEU PHE GLU GLU
SEQRES 7 A 209 GLY GLN GLU ARG SER ALA TRP VAL ARG ALA LYS THR ALA
SEQRES 8 A 209 CYS GLU VAL ALA GLU ILE SER TYR LYS LYS PHE ARG GLN
SEQRES 9 A 209 LEU ILE GLN VAL ASN PRO ASP ILE LEU MET ARG LEU SER
SEQRES 10 A 209 ALA GLN MET ALA ARG ARG LEU GLN VAL LEU ILE GLU LYS
SEQRES 11 A 209 VAL GLY ASN LEU ALA PHE LEU ASP VAL THR GLY ARG ILE
SEQRES 12 A 209 ALA GLN THR LEU LEU ASN LEU ALA LYS GLN PRO ASP ALA
SEQRES 13 A 209 MET THR HIS PRO ASP GLY MET GLN ILE LYS ILE THR ARG
SEQRES 14 A 209 GLN GLU ILE GLY GLN ILE VAL GLY CYS SER ARG GLU THR
SEQRES 15 A 209 VAL GLY ARG ILE LEU LYS MET LEU GLU ASP GLN ASN LEU
SEQRES 16 A 209 ILE SER ALA HIS GLY LYS THR ILE VAL VAL TYR GLY THR
SEQRES 17 A 209 ARG
HELIX 1 1 ASP A 8 SER A 16 1 9
HELIX 2 2 GLY A 71 PHE A 76 1 6
HELIX 3 3 TYR A 99 ASN A 109 1 11
HELIX 4 4 PRO A 110 VAL A 131 1 22
HELIX 5 5 GLY A 141 LEU A 150 1 10
HELIX 6 6 ALA A 151 GLN A 153 5 3
HELIX 7 7 THR A 168 VAL A 176 1 9
HELIX 8 8 SER A 179 ASP A 192 1 14
SHEET 1 AA 4 HIS A 19 TYR A 23 0
SHEET 2 AA 4 CYS A 92 SER A 98 -1 O CYS A 92 N TYR A 23
SHEET 3 AA 4 THR A 38 LYS A 44 -1 O LEU A 39 N ILE A 97
SHEET 4 AA 4 PHE A 69 ILE A 70 -1 O ILE A 70 N TYR A 40
SHEET 1 AB 4 THR A 28 ILE A 30 0
SHEET 2 AB 4 TRP A 85 ARG A 87 -1 N TRP A 85 O ILE A 30
SHEET 3 AB 4 SER A 46 LYS A 52 -1 O ALA A 48 N ARG A 87
SHEET 4 AB 4 GLU A 58 ASN A 65 -1 O MET A 59 N ILE A 51
SHEET 1 AC 4 ALA A 156 THR A 158 0
SHEET 2 AC 4 MET A 163 ILE A 165 -1 O GLN A 164 N MET A 157
SHEET 3 AC 4 ILE A 203 VAL A 205 -1 O ILE A 203 N ILE A 165
SHEET 4 AC 4 SER A 197 ALA A 198 -1 O SER A 197 N VAL A 204
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
(ATOM LINES ARE NOT SHOWN.)
END
