HEADER TRANSCRIPTION ACTIVATOR 27-JUN-12 4FT8
TITLE E. COLI CATABOLITE ACTIVATOR PROTEIN WITH COBALT AND SULFATE LIGANDS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATABOLITE GENE ACTIVATOR;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CAMP RECEPTOR PROTEIN, CAMP REGULATORY PROTEIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: B3357, CAP, CRP, CSM, JW5702;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET
KEYWDS WINGED HELIX-TURN-HELIX, DNA BINDING PROTEIN, COBALT BINDING, SULFATE
KEYWDS 2 BINDING, TRANSCRIPTION ACTIVATOR
EXPDTA X-RAY DIFFRACTION
AUTHOR R.RAO,C.L.LAWSON
REVDAT 4 13-SEP-23 4FT8 1 REMARK LINK
REVDAT 3 24-SEP-14 4FT8 1 JRNL
REVDAT 2 07-MAY-14 4FT8 1 JRNL
REVDAT 1 18-DEC-13 4FT8 0
JRNL AUTH R.R.RAO,C.L.LAWSON
JRNL TITL STRUCTURE OF CATABOLITE ACTIVATOR PROTEIN WITH COBALT(II)
JRNL TITL 2 AND SULFATE.
JRNL REF ACTA CRYSTALLOGR F STRUCT V. 70 560 2014
JRNL REF 2 BIOL COMMUN
JRNL REFN ESSN 1744-3091
JRNL PMID 24817710
JRNL DOI 10.1107/S2053230X14005366
REMARK 2
REMARK 2 RESOLUTION. 1.97 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.97
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.78
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 35596
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 1774
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 40.7895 - 4.6212 0.98 0 141 0.1950 0.2049
REMARK 3 2 2.0194 - 1.9663 0.92 0 113 0.2865 0.3216
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.37
REMARK 3 B_SOL : 59.42
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.280
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.29
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.66410
REMARK 3 B22 (A**2) : -0.47290
REMARK 3 B33 (A**2) : -0.19120
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.005 NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : 16.888 NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4FT8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUL-12.
REMARK 100 THE DEPOSITION ID IS D_1000073326.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-NOV-07
REMARK 200 TEMPERATURE (KELVIN) : 108
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X8C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.07
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35645
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.960
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.96
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.77800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: SEARCH 1: 1ZRC CAP N-TERMINAL DOMAIN DIMER;
REMARK 200 SEARCHES 2,3: 1ZRC CAP INDIVIDUAL C-TERMINAL DOMAIN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: A CAP-DNA COMPLEX WAS SCREENED BY
REMARK 280 HANGING-DROP VAPOR DIFFUSION WITH HAMPTON RESEARCH CRYSTAL
REMARK 280 SCREENS AND PREGREASED VDX PLATES. OPTIMIZATION OF CRYSTAL
REMARK 280 SCREEN 2 CONDITION #25 YIELDED RUBY-RED COLORED CRYSTALS
REMARK 280 APPEARING WITHIN 3 DAYS AT 20 C IN 0.01 M COCL2.6H2O, 0.1 M MES
REMARK 280 MONOHYDRATE PH 6.5 AND 2.5 M (NH4)2SO4. THE CRYSTALLIZATION
REMARK 280 PROCESS YIELDED CRYSTALS CONTAINING ONLY CAP PROTEIN WITHOUT DNA,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 52.07150
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.22600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 52.07150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.22600
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7060 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -201.0 KCAL/MOL
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -204.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 44.32000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 488 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 543 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 VAL A 1
REMARK 465 LEU A 2
REMARK 465 GLY A 3
REMARK 465 LYS A 4
REMARK 465 PRO A 5
REMARK 465 GLN A 6
REMARK 465 THR A 7
REMARK 465 THR A 208
REMARK 465 ARG A 209
REMARK 465 VAL B 1
REMARK 465 LEU B 2
REMARK 465 GLY B 3
REMARK 465 LYS B 4
REMARK 465 PRO B 5
REMARK 465 GLN B 6
REMARK 465 GLY B 207
REMARK 465 THR B 208
REMARK 465 ARG B 209
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 26 -5.62 78.26
REMARK 500 GLU A 37 -1.95 -141.85
REMARK 500 HIS A 199 45.37 -150.97
REMARK 500 LYS B 26 -2.18 75.09
REMARK 500 ASP B 155 39.14 -78.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CO A 308 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 19 NE2
REMARK 620 2 HIS A 21 NE2 92.6
REMARK 620 3 GLU A 96 OE2 112.8 81.7
REMARK 620 4 HOH A 402 O 100.3 167.1 92.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CO B 309 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 19 NE2
REMARK 620 2 HIS B 21 NE2 92.6
REMARK 620 3 GLU B 96 OE1 106.5 85.9
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMP A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO A 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMP B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO B 309
DBREF 4FT8 A 1 209 UNP P0ACJ8 CRP_ECOLI 2 210
DBREF 4FT8 B 1 209 UNP P0ACJ8 CRP_ECOLI 2 210
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 THR SER 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
SEQRES 1 B 209 VAL LEU GLY LYS PRO GLN THR ASP PRO THR LEU GLU TRP
SEQRES 2 B 209 PHE LEU SER HIS CYS HIS ILE HIS LYS TYR PRO SER LYS
SEQRES 3 B 209 SER THR LEU ILE HIS GLN GLY GLU LYS ALA GLU THR LEU
SEQRES 4 B 209 TYR TYR ILE VAL LYS GLY SER VAL ALA VAL LEU ILE LYS
SEQRES 5 B 209 ASP GLU GLU GLY LYS GLU MET ILE LEU SER TYR LEU ASN
SEQRES 6 B 209 GLN GLY ASP PHE ILE GLY GLU LEU GLY LEU PHE GLU GLU
SEQRES 7 B 209 GLY GLN GLU ARG SER ALA TRP VAL ARG ALA LYS THR ALA
SEQRES 8 B 209 CYS GLU VAL ALA GLU ILE SER TYR LYS LYS PHE ARG GLN
SEQRES 9 B 209 LEU ILE GLN VAL ASN PRO ASP ILE LEU MET ARG LEU SER
SEQRES 10 B 209 ALA GLN MET ALA ARG ARG LEU GLN VAL THR SER GLU LYS
SEQRES 11 B 209 VAL GLY ASN LEU ALA PHE LEU ASP VAL THR GLY ARG ILE
SEQRES 12 B 209 ALA GLN THR LEU LEU ASN LEU ALA LYS GLN PRO ASP ALA
SEQRES 13 B 209 MET THR HIS PRO ASP GLY MET GLN ILE LYS ILE THR ARG
SEQRES 14 B 209 GLN GLU ILE GLY GLN ILE VAL GLY CYS SER ARG GLU THR
SEQRES 15 B 209 VAL GLY ARG ILE LEU LYS MET LEU GLU ASP GLN ASN LEU
SEQRES 16 B 209 ILE SER ALA HIS GLY LYS THR ILE VAL VAL TYR GLY THR
SEQRES 17 B 209 ARG
HET CMP A 301 22
HET SO4 A 302 5
HET SO4 A 303 5
HET SO4 A 304 5
HET SO4 A 305 5
HET SO4 A 306 5
HET SO4 A 307 5
HET CO A 308 1
HET CMP B 301 22
HET SO4 B 302 5
HET SO4 B 303 5
HET SO4 B 304 5
HET SO4 B 305 5
HET SO4 B 306 5
HET SO4 B 307 5
HET SO4 B 308 5
HET CO B 309 1
HETNAM CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE
HETNAM SO4 SULFATE ION
HETNAM CO COBALT (II) ION
HETSYN CMP CYCLIC AMP; CAMP
FORMUL 3 CMP 2(C10 H12 N5 O6 P)
FORMUL 4 SO4 13(O4 S 2-)
FORMUL 10 CO 2(CO 2+)
FORMUL 20 HOH *409(H2 O)
HELIX 1 1 ASP A 8 HIS A 17 1 10
HELIX 2 2 TYR A 99 ASN A 109 1 11
HELIX 3 3 PRO A 110 LEU A 137 1 28
HELIX 4 4 ASP A 138 LYS A 152 1 15
HELIX 5 5 THR A 168 GLY A 177 1 10
HELIX 6 6 SER A 179 GLN A 193 1 15
HELIX 7 7 ASP B 8 HIS B 17 1 10
HELIX 8 8 TYR B 99 ASN B 109 1 11
HELIX 9 9 PRO B 110 ALA B 135 1 26
HELIX 10 10 ASP B 138 ALA B 151 1 14
HELIX 11 11 THR B 168 GLY B 177 1 10
HELIX 12 12 SER B 179 GLN B 193 1 15
SHEET 1 A 4 HIS A 19 TYR A 23 0
SHEET 2 A 4 CYS A 92 SER A 98 -1 O CYS A 92 N TYR A 23
SHEET 3 A 4 THR A 38 LYS A 44 -1 N LEU A 39 O ILE A 97
SHEET 4 A 4 PHE A 69 ILE A 70 -1 O ILE A 70 N TYR A 40
SHEET 1 B 4 THR A 28 ILE A 30 0
SHEET 2 B 4 TRP A 85 ALA A 88 -1 O VAL A 86 N LEU A 29
SHEET 3 B 4 VAL A 47 LYS A 52 -1 N LEU A 50 O TRP A 85
SHEET 4 B 4 GLU A 58 LEU A 64 -1 O SER A 62 N VAL A 49
SHEET 1 C 4 MET A 157 HIS A 159 0
SHEET 2 C 4 GLY A 162 LYS A 166 -1 O GLN A 164 N MET A 157
SHEET 3 C 4 THR A 202 VAL A 205 -1 O VAL A 205 N MET A 163
SHEET 4 C 4 ILE A 196 ALA A 198 -1 N SER A 197 O VAL A 204
SHEET 1 D 4 HIS B 19 TYR B 23 0
SHEET 2 D 4 CYS B 92 SER B 98 -1 O CYS B 92 N TYR B 23
SHEET 3 D 4 THR B 38 LYS B 44 -1 N TYR B 41 O ALA B 95
SHEET 4 D 4 PHE B 69 ILE B 70 -1 O ILE B 70 N TYR B 40
SHEET 1 E 4 THR B 28 ILE B 30 0
SHEET 2 E 4 TRP B 85 ALA B 88 -1 O VAL B 86 N ILE B 30
SHEET 3 E 4 SER B 46 LYS B 52 -1 N LEU B 50 O TRP B 85
SHEET 4 E 4 GLU B 58 ASN B 65 -1 O LEU B 61 N VAL B 49
SHEET 1 F 4 MET B 157 HIS B 159 0
SHEET 2 F 4 GLY B 162 LYS B 166 -1 O GLN B 164 N MET B 157
SHEET 3 F 4 THR B 202 VAL B 205 -1 O ILE B 203 N ILE B 165
SHEET 4 F 4 ILE B 196 HIS B 199 -1 N HIS B 199 O THR B 202
LINK NE2 HIS A 19 CO CO A 308 1555 1555 2.24
LINK NE2 HIS A 21 CO CO A 308 1555 1555 2.05
LINK OE2 GLU A 96 CO CO A 308 1555 1555 2.28
LINK CO CO A 308 O HOH A 402 1555 1555 2.17
LINK NE2 HIS B 19 CO CO B 309 1555 1555 2.08
LINK NE2 HIS B 21 CO CO B 309 1555 1555 2.15
LINK OE1 GLU B 96 CO CO B 309 1555 1555 2.21
SITE 1 AC1 15 VAL A 49 LEU A 61 ILE A 70 GLY A 71
SITE 2 AC1 15 GLU A 72 LEU A 73 ARG A 82 SER A 83
SITE 3 AC1 15 ALA A 84 THR A 127 HOH A 415 HOH A 417
SITE 4 AC1 15 HOH A 475 LEU B 124 SER B 128
SITE 1 AC2 5 HIS A 21 LYS A 22 HOH A 570 LYS B 35
SITE 2 AC2 5 GLY B 79
SITE 1 AC3 7 HIS A 31 TRP A 85 HOH A 508 HOH A 549
SITE 2 AC3 7 HIS B 31 TRP B 85 HOH B 568
SITE 1 AC4 7 GLY A 33 GLU A 81 HOH A 442 HOH A 470
SITE 2 AC4 7 HOH A 558 SER B 27 THR B 28
SITE 1 AC5 3 THR A 168 ARG A 169 GLN A 170
SITE 1 AC6 4 THR A 90 ALA A 91 HOH A 599 HOH A 601
SITE 1 AC7 4 HIS A 19 ILE A 20 HOH A 482 HOH A 566
SITE 1 AC8 5 HIS A 19 HIS A 21 GLU A 96 HOH A 402
SITE 2 AC8 5 GLU B 37
SITE 1 AC9 18 LEU A 124 SER A 128 VAL B 49 LEU B 61
SITE 2 AC9 18 SER B 62 ILE B 70 GLY B 71 GLU B 72
SITE 3 AC9 18 LEU B 73 ARG B 82 SER B 83 ALA B 84
SITE 4 AC9 18 VAL B 86 ARG B 123 THR B 127 HOH B 412
SITE 5 AC9 18 HOH B 416 HOH B 417
SITE 1 BC1 7 LYS A 35 HOH A 478 HOH A 583 ILE B 20
SITE 2 BC1 7 HIS B 21 LYS B 22 HOH B 573
SITE 1 BC2 6 ASP B 68 GLN B 119 ARG B 122 ARG B 123
SITE 2 BC2 6 HOH B 457 HOH B 460
SITE 1 BC3 3 ASP B 138 VAL B 139 ARG B 142
SITE 1 BC4 3 SER B 179 ARG B 180 HOH B 590
SITE 1 BC5 4 LYS B 57 CYS B 178 SER B 179 THR B 182
SITE 1 BC6 5 THR B 168 ARG B 169 GLN B 170 ARG B 180
SITE 2 BC6 5 HOH B 520
SITE 1 BC7 6 SER A 197 TYR A 206 HIS B 199 GLY B 200
SITE 2 BC7 6 LYS B 201 HOH B 586
SITE 1 BC8 5 GLU A 37 HOH A 412 HIS B 19 HIS B 21
SITE 2 BC8 5 GLU B 96
CRYST1 104.143 108.452 44.320 90.00 90.00 90.00 P 21 21 2 8
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 0.009602 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009221 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022563 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
