HEADER TRANSFERASE 29-SEP-15 5E16
TITLE CO-CRYSTAL STRUCTURE OF THE N-TERMIAL CGMP BINDING DOMAIN OF
TITLE 2 PLASMODIUM FALCIPARUM PKG WITH CGMP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CGMP-DEPENDENT PROTEIN KINASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CGMP BINDING DOMAIN (UNP RESIDUES 21-162);
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM;
SOURCE 3 ORGANISM_TAXID: 5833;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET15-MHL
KEYWDS KINASE, CGMP BINDING DOMAIN, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS
KEYWDS 2 CONSORTIUM, SGC, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.EL BAKKOURI,J.R.WALKER,P.LOPPNAU,C.H.ARROWSMITH,A.M.EDWARDS,
AUTHOR 2 C.BOUNTRA,R.HUI,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 5 27-SEP-23 5E16 1 REMARK
REVDAT 4 13-NOV-19 5E16 1 JRNL
REVDAT 3 03-JUL-19 5E16 1 JRNL REMARK
REVDAT 2 11-NOV-15 5E16 1 REMARK
REVDAT 1 04-NOV-15 5E16 0
JRNL AUTH M.EL BAKKOURI,I.KOUIDMI,A.K.WERNIMONT,M.AMANI,A.HUTCHINSON,
JRNL AUTH 2 P.LOPPNAU,J.J.KIM,C.FLUECK,J.R.WALKER,A.SEITOVA,
JRNL AUTH 3 G.SENISTERRA,Y.KAKIHARA,C.KIM,M.J.BLACKMAN,C.CALMETTES,
JRNL AUTH 4 D.A.BAKER,R.HUI
JRNL TITL STRUCTURES OF THE CGMP-DEPENDENT PROTEIN KINASE IN MALARIA
JRNL TITL 2 PARASITES REVEAL A UNIQUE STRUCTURAL RELAY MECHANISM FOR
JRNL TITL 3 ACTIVATION.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 116 14164 2019
JRNL REFN ESSN 1091-6490
JRNL PMID 31239348
JRNL DOI 10.1073/PNAS.1905558116
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0131
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.18
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 14851
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 813
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.69
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1062
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.96
REMARK 3 BIN R VALUE (WORKING SET) : 0.2710
REMARK 3 BIN FREE R VALUE SET COUNT : 53
REMARK 3 BIN FREE R VALUE : 0.3000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1078
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 23
REMARK 3 SOLVENT ATOMS : 104
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.09
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.71000
REMARK 3 B22 (A**2) : 0.64000
REMARK 3 B33 (A**2) : -1.35000
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.117
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.111
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.081
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.358
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.956
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1170 ; 0.013 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1091 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1589 ; 1.592 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2514 ; 0.951 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 149 ; 5.985 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 54 ;35.808 ;25.370
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 212 ;11.899 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 5 ;16.009 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 180 ; 0.093 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1352 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 277 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 578 ; 2.006 ; 2.530
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 577 ; 1.994 ; 2.522
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 730 ; 3.015 ; 3.782
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5E16 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-SEP-15.
REMARK 100 THE DEPOSITION ID IS D_1000214068.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-JUL-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN A200
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15745
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.04300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.68
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.8
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 0.30300
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: 4MYJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25 % PEG3350, 0.2 M NACL, 0.1 M HEPES,
REMARK 280 PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 46.17550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 46.17550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 25.63300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 26.92350
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 25.63300
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 26.92350
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 46.17550
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 25.63300
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 26.92350
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 46.17550
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 25.63300
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 26.92350
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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: MONOMERIC
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 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 GLY A 20
REMARK 465 LEU A 159
REMARK 465 SER A 160
REMARK 465 ASN A 161
REMARK 465 ARG A 162
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 SER A 21 OG
REMARK 470 GLU A 40 CG CD OE1 OE2
REMARK 470 ASP A 109 CG OD1 OD2
REMARK 470 LYS A 157 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 ND2 ASN A 55 O HOH A 701 1.81
REMARK 500 OD1 ASP A 29 O HOH A 702 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PCG A 601
DBREF 5E16 A 21 162 UNP Q8MMZ4 Q8MMZ4_PLAFA 21 162
SEQADV 5E16 GLY A 20 UNP Q8MMZ4 EXPRESSION TAG
SEQRES 1 A 143 GLY SER ASN ASP ASP PHE THR GLY GLU ASP SER LEU MET
SEQRES 2 A 143 GLU ASP HIS LEU GLU LEU ARG GLU LYS LEU SER GLU ASP
SEQRES 3 A 143 ILE ASP MET ILE LYS THR SER LEU LYS ASN ASN LEU VAL
SEQRES 4 A 143 CYS SER THR LEU ASN ASP ASN GLU ILE LEU THR LEU SER
SEQRES 5 A 143 ASN TYR MET GLN PHE PHE VAL PHE LYS SER GLY ASN LEU
SEQRES 6 A 143 VAL ILE LYS GLN GLY GLU LYS GLY SER TYR PHE PHE ILE
SEQRES 7 A 143 ILE ASN SER GLY LYS PHE ASP VAL TYR VAL ASN ASP LYS
SEQRES 8 A 143 LYS VAL LYS THR MET GLY LYS GLY SER SER PHE GLY GLU
SEQRES 9 A 143 ALA ALA LEU ILE HIS ASN THR GLN ARG SER ALA THR ILE
SEQRES 10 A 143 ILE ALA GLU THR ASP GLY THR LEU TRP GLY VAL GLN ARG
SEQRES 11 A 143 SER THR PHE ARG ALA THR LEU LYS GLN LEU SER ASN ARG
HET PCG A 601 23
HETNAM PCG CYCLIC GUANOSINE MONOPHOSPHATE
FORMUL 2 PCG C10 H12 N5 O7 P
FORMUL 3 HOH *104(H2 O)
HELIX 1 AA1 GLY A 27 HIS A 35 1 9
HELIX 2 AA2 LEU A 42 ASN A 56 1 15
HELIX 3 AA3 ASN A 63 MET A 74 1 12
HELIX 4 AA4 GLY A 122 ASN A 129 1 8
HELIX 5 AA5 ARG A 149 GLN A 158 1 10
SHEET 1 AA1 5 LEU A 36 GLU A 37 0
SHEET 2 AA1 5 GLN A 75 PHE A 79 -1 O PHE A 76 N GLU A 37
SHEET 3 AA1 5 GLY A 142 GLN A 148 -1 O GLY A 142 N PHE A 79
SHEET 4 AA1 5 TYR A 94 SER A 100 -1 N ILE A 97 O TRP A 145
SHEET 5 AA1 5 SER A 120 PHE A 121 -1 O PHE A 121 N PHE A 96
SHEET 1 AA2 4 LEU A 84 ILE A 86 0
SHEET 2 AA2 4 THR A 135 ALA A 138 -1 O ILE A 136 N VAL A 85
SHEET 3 AA2 4 PHE A 103 VAL A 107 -1 N TYR A 106 O THR A 135
SHEET 4 AA2 4 LYS A 110 MET A 115 -1 O MET A 115 N PHE A 103
SITE 1 AC1 14 ASN A 55 VAL A 107 LYS A 113 PHE A 121
SITE 2 AC1 14 GLY A 122 GLU A 123 ALA A 124 ALA A 125
SITE 3 AC1 14 ARG A 132 SER A 133 ALA A 134 ILE A 136
SITE 4 AC1 14 HOH A 760 HOH A 767
CRYST1 51.266 53.847 92.351 90.00 90.00 90.00 C 2 2 21 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 0.019506 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018571 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010828 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
