HEADER SIGNALING PROTEIN/GTP-BINDING PROTEIN 28-AUG-13 4MGI
TITLE SELECTIVE ACTIVATION OF EPAC1 AND EPAC2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RAP GUANINE NUCLEOTIDE EXCHANGE FACTOR 4;
COMPND 3 CHAIN: E;
COMPND 4 FRAGMENT: UNP RESIDUES 324-1011;
COMPND 5 SYNONYM: EXCHANGE FACTOR DIRECTLY ACTIVATED BY CAMP 2, EXCHANGE
COMPND 6 PROTEIN DIRECTLY ACTIVATED BY CAMP 2, EPAC 2, CAMP-DEPENDENT RAP1
COMPND 7 GUANINE-NUCLEOTIDE EXCHANGE FACTOR, CAMP-REGULATED GUANINE NUCLEOTIDE
COMPND 8 EXCHANGE FACTOR II, CAMP-GEFII;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: RAS-RELATED PROTEIN RAP-1B;
COMPND 12 CHAIN: R;
COMPND 13 FRAGMENT: UNP RESIDUES 1-169;
COMPND 14 SYNONYM: GTP-BINDING PROTEIN SMG P21B;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: RAPGEF4, CGEF2, EPAC2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: CK600K;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLAMSID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX4T1;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: RAP1B, OK/SW-CL.11;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: CK600K;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PTAC
KEYWDS GUANINE NUCLEOTIDE EXCHANGE FACTOR, NUCLEOTIDE BINDING, SIGNALING
KEYWDS 2 PROTEIN-GTP-BINDING PROTEIN COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.REHMANN
REVDAT 3 20-SEP-23 4MGI 1 REMARK SEQADV
REVDAT 2 15-NOV-17 4MGI 1 REMARK
REVDAT 1 03-SEP-14 4MGI 0
JRNL AUTH H.REHMANN
JRNL TITL SELECTIVE ACTIVATION OF EPAC1 AND EPAC2
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.26
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 48982
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) : 0.250
REMARK 3 R VALUE (WORKING SET) : 0.249
REMARK 3 FREE R VALUE : 0.271
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 2476
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3540
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3430
REMARK 3 BIN FREE R VALUE SET COUNT : 183
REMARK 3 BIN FREE R VALUE : 0.3570
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6238
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 49
REMARK 3 SOLVENT ATOMS : 97
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.26000
REMARK 3 B22 (A**2) : 1.09000
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): 0.369
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.279
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.226
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.748
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.894
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.864
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6404 ; 0.006 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8657 ; 0.960 ; 1.972
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 770 ; 4.567 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 304 ;36.261 ;24.243
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1164 ;16.434 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 43 ;13.111 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 985 ; 0.062 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4749 ; 0.003 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 3865 ; 0.330 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6265 ; 0.617 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2539 ; 0.585 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2392 ; 1.078 ; 4.500
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: NULL
REMARK 4
REMARK 4 4MGI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-SEP-13.
REMARK 100 THE DEPOSITION ID IS D_1000081881.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-NOV-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.072252
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51460
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.450
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 3CF6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 76.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.4M (NH4)2SO4, 1.2M LI2SO4, 0.1M
REMARK 280 CITRATE, PH 5.6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y+1/2,Z
REMARK 290 7555 -X+1/2,Y,-Z
REMARK 290 8555 X,-Y,-Z+1/2
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 62.65900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 112.36000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 74.24850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 112.36000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 62.65900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 74.24850
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 62.65900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 74.24850
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 112.36000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 74.24850
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 62.65900
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 112.36000
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: 3150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35270 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, R
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: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 66900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, R
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 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 -112.36000
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 E1104 LIES ON A SPECIAL POSITION.
REMARK 375 HOH E1117 LIES ON A SPECIAL POSITION.
REMARK 375 HOH E1183 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 GLY E 300
REMARK 465 SER E 301
REMARK 465 PRO E 302
REMARK 465 GLU E 303
REMARK 465 SER E 304
REMARK 465 PHE E 305
REMARK 465 PRO E 306
REMARK 465 ASP E 307
REMARK 465 ALA E 308
REMARK 465 HIS E 309
REMARK 465 PRO E 463
REMARK 465 ALA E 464
REMARK 465 GLY E 465
REMARK 465 ASN E 466
REMARK 465 ARG E 467
REMARK 465 ALA E 468
REMARK 465 ALA E 469
REMARK 465 ASN E 470
REMARK 465 GLN E 471
REMARK 465 GLY E 472
REMARK 465 ASN E 473
REMARK 465 SER E 474
REMARK 465 GLN E 475
REMARK 465 PRO E 476
REMARK 465 GLN E 477
REMARK 465 LYS E 613
REMARK 465 GLN E 614
REMARK 465 ILE E 615
REMARK 465 SER E 616
REMARK 465 GLU E 617
REMARK 465 ASP E 618
REMARK 465 ALA E 619
REMARK 465 LYS E 620
REMARK 465 ALA E 621
REMARK 465 PRO E 622
REMARK 465 GLN E 623
REMARK 465 LYS E 624
REMARK 465 LYS E 625
REMARK 465 HIS E 626
REMARK 465 LYS E 627
REMARK 465 VAL E 628
REMARK 465 LEU E 629
REMARK 465 LEU E 630
REMARK 465 GLN E 631
REMARK 465 GLN E 632
REMARK 465 PHE E 633
REMARK 465 ASN E 634
REMARK 465 THR E 635
REMARK 465 GLY E 636
REMARK 465 ASP E 637
REMARK 465 GLU E 638
REMARK 465 ARG E 639
REMARK 465 ALA E 640
REMARK 465 GLN E 641
REMARK 465 LYS E 642
REMARK 465 PRO E 953
REMARK 465 ASP E 954
REMARK 465 ALA E 955
REMARK 465 ALA E 956
REMARK 465 GLN E 957
REMARK 465 ALA E 958
REMARK 465 ASN E 959
REMARK 465 LYS E 960
REMARK 465 ASN E 961
REMARK 465 ARG E 991
REMARK 465 ARG E 992
REMARK 465 PRO E 993
REMARK 465 MET R 1
REMARK 465 ARG R 2
REMARK 465 GLU R 45
REMARK 465 VAL R 46
REMARK 465 ASP R 47
REMARK 465 ALA R 48
REMARK 465 GLN R 49
REMARK 465 ALA R 135
REMARK 465 ARG R 136
REMARK 465 GLN R 137
REMARK 465 TRP R 138
REMARK 465 ASN R 139
REMARK 465 ASN R 140
REMARK 465 CYS R 141
REMARK 465 ILE R 165
REMARK 465 ASN R 166
REMARK 465 ARG R 167
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 VAL E 353 -35.74 -140.43
REMARK 500 ASN E 424 87.92 56.42
REMARK 500 VAL E 442 -25.48 -154.60
REMARK 500 PRO E 900 -68.85 -20.43
REMARK 500 PRO E 901 92.12 -69.16
REMARK 500 GLN R 25 -52.53 -158.44
REMARK 500 PHE R 28 -54.75 75.53
REMARK 500 ARG R 102 -42.98 -173.87
REMARK 500 ASP R 105 81.01 66.05
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 CMP E 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMP E 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 R 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2BYV RELATED DB: PDB
REMARK 900 INACTIVE EPAC2
REMARK 900 RELATED ID: 3CF6 RELATED DB: PDB
REMARK 900 COMPLEX WITH SP1 / SP-CAMPS / 6-(6-AMINO-PURIN-9-YL)-2-THIOXO-
REMARK 900 TETRAHYDRO-2-FURO[3,2- D][1,3,2]DIOXAPHOSPHININE-2,7-DIOL / SP-
REMARK 900 ADENOSINE-3',5'-CYCLIC-MONOPHOSPHOROTHIOATE
REMARK 900 RELATED ID: 4MGK RELATED DB: PDB
REMARK 900 COMPLEX OF MUTANT K405Q WITH CMP / CAMP / CYCLIC AMP / ADENOSINE-3',
REMARK 900 5'-CYCLIC-MONOPHOSPHATE
REMARK 900 RELATED ID: 4MGY RELATED DB: PDB
REMARK 900 COMPLEX OF MUTANT K405Q WITH 8-PPCT-2 -O-ME-CAMP / 8-(4-
REMARK 900 CHLOROPHENYLTHIO)-2'-O-METHYLADENOSINE-3',5'-CYCLIC MONOPHOSPHATE
REMARK 900 RELATED ID: 4MGZ RELATED DB: PDB
REMARK 900 COMPLEX WITH SP-8-BNT-CAMPS / 8-BENZYLTHIOADENOSINE-3',5'-CYCLIC
REMARK 900 MONOPHOSPHOROTHIOATE, SP- ISOMER
REMARK 900 RELATED ID: 4MH0 RELATED DB: PDB
DBREF 4MGI E 306 993 UNP Q9EQZ6 RPGF4_MOUSE 324 1011
DBREF 4MGI R 1 167 UNP P61224 RAP1B_HUMAN 1 167
SEQADV 4MGI GLY E 300 UNP Q9EQZ6 EXPRESSION TAG
SEQADV 4MGI SER E 301 UNP Q9EQZ6 EXPRESSION TAG
SEQADV 4MGI PRO E 302 UNP Q9EQZ6 EXPRESSION TAG
SEQADV 4MGI GLU E 303 UNP Q9EQZ6 EXPRESSION TAG
SEQADV 4MGI SER E 304 UNP Q9EQZ6 EXPRESSION TAG
SEQADV 4MGI PHE E 305 UNP Q9EQZ6 EXPRESSION TAG
SEQRES 1 E 694 GLY SER PRO GLU SER PHE PRO ASP ALA HIS MET ARG MET
SEQRES 2 E 694 ILE LEU ARG LYS PRO PRO GLY GLN ARG THR VAL ASP ASP
SEQRES 3 E 694 LEU GLU ILE ILE TYR ASP GLU LEU LEU HIS ILE LYS ALA
SEQRES 4 E 694 LEU SER HIS LEU SER THR THR VAL LYS ARG GLU LEU ALA
SEQRES 5 E 694 GLY VAL LEU ILE PHE GLU SER HIS ALA LYS GLY GLY THR
SEQRES 6 E 694 VAL LEU PHE ASN GLN GLY GLU GLU GLY THR SER TRP TYR
SEQRES 7 E 694 ILE ILE LEU LYS GLY SER VAL ASN VAL VAL ILE TYR GLY
SEQRES 8 E 694 LYS GLY VAL VAL CYS THR LEU HIS GLU GLY ASP ASP PHE
SEQRES 9 E 694 GLY LYS LEU ALA LEU VAL ASN ASP ALA PRO ARG ALA ALA
SEQRES 10 E 694 SER ILE VAL LEU ARG GLU ASP ASN CYS HIS PHE LEU ARG
SEQRES 11 E 694 VAL ASP LYS GLU ASP PHE ASN ARG ILE LEU ARG ASP VAL
SEQRES 12 E 694 GLU ALA ASN THR VAL ARG LEU LYS GLU HIS ASP GLN ASP
SEQRES 13 E 694 VAL LEU VAL LEU GLU LYS VAL PRO ALA GLY ASN ARG ALA
SEQRES 14 E 694 ALA ASN GLN GLY ASN SER GLN PRO GLN GLN LYS TYR THR
SEQRES 15 E 694 VAL MET SER GLY THR PRO GLU LYS ILE LEU GLU HIS PHE
SEQRES 16 E 694 LEU GLU THR ILE ARG LEU GLU PRO SER LEU ASN GLU ALA
SEQRES 17 E 694 THR ASP SER VAL LEU ASN ASP PHE VAL MET MET HIS CYS
SEQRES 18 E 694 VAL PHE MET PRO ASN THR GLN LEU CYS PRO ALA LEU VAL
SEQRES 19 E 694 ALA HIS TYR HIS ALA GLN PRO SER GLN GLY THR GLU GLN
SEQRES 20 E 694 GLU ARG MET ASP TYR ALA LEU ASN ASN LYS ARG ARG VAL
SEQRES 21 E 694 ILE ARG LEU VAL LEU GLN TRP ALA ALA MET TYR GLY ASP
SEQRES 22 E 694 LEU LEU GLN GLU ASP ASP VAL ALA MET ALA PHE LEU GLU
SEQRES 23 E 694 GLU PHE TYR VAL SER VAL SER ASP ASP ALA ARG MET MET
SEQRES 24 E 694 ALA ALA PHE LYS GLU GLN LEU PRO GLU LEU GLU LYS ILE
SEQRES 25 E 694 VAL LYS GLN ILE SER GLU ASP ALA LYS ALA PRO GLN LYS
SEQRES 26 E 694 LYS HIS LYS VAL LEU LEU GLN GLN PHE ASN THR GLY ASP
SEQRES 27 E 694 GLU ARG ALA GLN LYS ARG GLN PRO ILE ARG GLY SER ASP
SEQRES 28 E 694 GLU VAL LEU PHE LYS VAL TYR CYS ILE ASP HIS THR TYR
SEQRES 29 E 694 THR THR ILE ARG VAL PRO VAL ALA ALA SER VAL LYS GLU
SEQRES 30 E 694 VAL ILE SER ALA VAL ALA ASP LYS LEU GLY SER GLY GLU
SEQRES 31 E 694 GLY LEU ILE ILE VAL LYS MET ASN SER GLY GLY GLU LYS
SEQRES 32 E 694 VAL VAL LEU LYS SER ASN ASP VAL SER VAL PHE THR THR
SEQRES 33 E 694 LEU THR ILE ASN GLY ARG LEU PHE ALA CYS PRO ARG GLU
SEQRES 34 E 694 GLN PHE ASP SER LEU THR PRO LEU PRO GLU GLN GLU GLY
SEQRES 35 E 694 PRO THR THR GLY THR VAL GLY THR PHE GLU LEU MET SER
SEQRES 36 E 694 SER LYS ASP LEU ALA TYR GLN MET THR THR TYR ASP TRP
SEQRES 37 E 694 GLU LEU PHE ASN CYS VAL HIS GLU LEU GLU LEU ILE TYR
SEQRES 38 E 694 HIS THR PHE GLY ARG HIS ASN PHE LYS LYS THR THR ALA
SEQRES 39 E 694 ASN LEU ASP LEU PHE LEU ARG ARG PHE ASN GLU ILE GLN
SEQRES 40 E 694 PHE TRP VAL VAL THR GLU VAL CYS LEU CYS SER GLN LEU
SEQRES 41 E 694 SER LYS ARG VAL GLN LEU LEU LYS LYS PHE ILE LYS ILE
SEQRES 42 E 694 ALA ALA HIS CYS LYS GLU TYR LYS ASN LEU ASN SER PHE
SEQRES 43 E 694 PHE ALA ILE VAL MET GLY LEU SER ASN VAL ALA VAL SER
SEQRES 44 E 694 ARG LEU ALA LEU THR TRP GLU LYS LEU PRO SER LYS PHE
SEQRES 45 E 694 LYS LYS PHE TYR ALA GLU PHE GLU SER LEU MET ASP PRO
SEQRES 46 E 694 SER ARG ASN HIS ARG ALA TYR ARG LEU THR ALA ALA LYS
SEQRES 47 E 694 LEU GLU PRO PRO LEU ILE PRO PHE MET PRO LEU LEU ILE
SEQRES 48 E 694 LYS ASP MET THR PHE THR HIS GLU GLY ASN LYS THR PHE
SEQRES 49 E 694 ILE ASP ASN LEU VAL ASN PHE GLU LYS MET ARG MET ILE
SEQRES 50 E 694 ALA ASN THR ALA ARG THR VAL ARG TYR TYR ARG SER GLN
SEQRES 51 E 694 PRO PHE ASN PRO ASP ALA ALA GLN ALA ASN LYS ASN HIS
SEQRES 52 E 694 GLN ASP VAL ARG SER TYR VAL ARG GLN LEU ASN VAL ILE
SEQRES 53 E 694 ASP ASN GLN ARG THR LEU SER GLN MET SER HIS ARG LEU
SEQRES 54 E 694 GLU PRO ARG ARG PRO
SEQRES 1 R 167 MET ARG GLU TYR LYS LEU VAL VAL LEU GLY SER GLY GLY
SEQRES 2 R 167 VAL GLY LYS SER ALA LEU THR VAL GLN PHE VAL GLN GLY
SEQRES 3 R 167 ILE PHE VAL GLU LYS TYR ASP PRO THR ILE GLU ASP SER
SEQRES 4 R 167 TYR ARG LYS GLN VAL GLU VAL ASP ALA GLN GLN CYS MET
SEQRES 5 R 167 LEU GLU ILE LEU ASP THR ALA GLY THR GLU GLN PHE THR
SEQRES 6 R 167 ALA MET ARG ASP LEU TYR MET LYS ASN GLY GLN GLY PHE
SEQRES 7 R 167 ALA LEU VAL TYR SER ILE THR ALA GLN SER THR PHE ASN
SEQRES 8 R 167 ASP LEU GLN ASP LEU ARG GLU GLN ILE LEU ARG VAL LYS
SEQRES 9 R 167 ASP THR ASP ASP VAL PRO MET ILE LEU VAL GLY ASN LYS
SEQRES 10 R 167 CYS ASP LEU GLU ASP GLU ARG VAL VAL GLY LYS GLU GLN
SEQRES 11 R 167 GLY GLN ASN LEU ALA ARG GLN TRP ASN ASN CYS ALA PHE
SEQRES 12 R 167 LEU GLU SER SER ALA LYS SER LYS ILE ASN VAL ASN GLU
SEQRES 13 R 167 ILE PHE TYR ASP LEU VAL ARG GLN ILE ASN ARG
HET CMP E1001 22
HET CMP E1002 22
HET SO4 R 201 5
HETNAM CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE
HETNAM SO4 SULFATE ION
HETSYN CMP CYCLIC AMP; CAMP
FORMUL 3 CMP 2(C10 H12 N5 O6 P)
FORMUL 5 SO4 O4 S 2-
FORMUL 6 HOH *97(H2 O)
HELIX 1 1 MET E 310 LYS E 316 1 7
HELIX 2 2 PRO E 317 ARG E 321 5 5
HELIX 3 3 THR E 322 LEU E 334 1 13
HELIX 4 4 SER E 343 GLY E 352 1 10
HELIX 5 5 GLY E 404 ASP E 411 1 8
HELIX 6 6 LYS E 432 LEU E 439 1 8
HELIX 7 7 THR E 486 THR E 497 1 12
HELIX 8 8 GLU E 501 SER E 503 5 3
HELIX 9 9 LEU E 504 MET E 523 1 20
HELIX 10 10 PRO E 524 HIS E 537 1 14
HELIX 11 11 THR E 544 GLY E 571 1 28
HELIX 12 12 ASP E 572 GLU E 576 5 5
HELIX 13 13 ASP E 577 ALA E 599 1 23
HELIX 14 14 GLU E 603 VAL E 612 1 10
HELIX 15 15 SER E 673 LEU E 685 1 13
HELIX 16 16 VAL E 712 LEU E 716 5 5
HELIX 17 17 PRO E 726 LEU E 733 5 8
HELIX 18 18 LEU E 736 GLY E 741 5 6
HELIX 19 19 THR E 746 GLU E 751 1 6
HELIX 20 20 SER E 754 VAL E 773 1 20
HELIX 21 21 HIS E 774 GLY E 784 1 11
HELIX 22 22 ARG E 785 PHE E 788 5 4
HELIX 23 23 THR E 792 LEU E 815 1 24
HELIX 24 24 GLN E 818 TYR E 839 1 22
HELIX 25 25 ASN E 841 ASN E 854 1 14
HELIX 26 26 ASN E 854 ARG E 859 1 6
HELIX 27 27 LEU E 860 LYS E 866 1 7
HELIX 28 28 PRO E 868 LEU E 881 1 14
HELIX 29 29 PRO E 884 LEU E 898 1 15
HELIX 30 30 PHE E 905 ASN E 920 1 16
HELIX 31 31 PHE E 930 ARG E 947 1 18
HELIX 32 32 GLN E 963 ARG E 970 1 8
HELIX 33 33 ASN E 977 ARG E 987 1 11
HELIX 34 34 GLY R 15 GLN R 25 1 11
HELIX 35 35 PHE R 64 GLY R 75 1 12
HELIX 36 36 ALA R 86 ASP R 92 1 7
HELIX 37 37 ASP R 92 LYS R 104 1 13
HELIX 38 38 GLY R 127 LEU R 134 1 8
HELIX 39 39 ASN R 153 GLN R 164 1 12
SHEET 1 A 4 ILE E 355 HIS E 359 0
SHEET 2 A 4 CYS E 425 ASP E 431 -1 O PHE E 427 N GLU E 357
SHEET 3 A 4 SER E 375 LYS E 381 -1 N LEU E 380 O HIS E 426
SHEET 4 A 4 ASP E 402 PHE E 403 -1 O PHE E 403 N TYR E 377
SHEET 1 B 4 VAL E 365 PHE E 367 0
SHEET 2 B 4 SER E 417 LEU E 420 -1 O ILE E 418 N LEU E 366
SHEET 3 B 4 VAL E 384 ILE E 388 -1 N ASN E 385 O VAL E 419
SHEET 4 B 4 GLY E 392 LEU E 397 -1 O CYS E 395 N VAL E 386
SHEET 1 C 5 VAL E 447 GLU E 451 0
SHEET 2 C 5 GLN E 454 LYS E 461 -1 O LEU E 459 N VAL E 447
SHEET 3 C 5 TYR E 480 GLY E 485 -1 O MET E 483 N VAL E 458
SHEET 4 C 5 LEU E 927 ASN E 929 -1 O VAL E 928 N GLY E 485
SHEET 5 C 5 PHE E 923 ILE E 924 -1 N ILE E 924 O LEU E 927
SHEET 1 D 5 TYR E 663 PRO E 669 0
SHEET 2 D 5 GLU E 651 TYR E 657 -1 N VAL E 656 O THR E 664
SHEET 3 D 5 ARG E 721 CYS E 725 1 O LEU E 722 N TYR E 657
SHEET 4 D 5 ILE E 692 MET E 696 -1 N ILE E 692 O CYS E 725
SHEET 5 D 5 LYS E 702 VAL E 704 -1 O VAL E 703 N LYS E 695
SHEET 1 E 6 ARG R 41 GLN R 43 0
SHEET 2 E 6 MET R 52 ASP R 57 -1 O LEU R 53 N LYS R 42
SHEET 3 E 6 TYR R 4 LEU R 9 1 N LEU R 6 O LEU R 56
SHEET 4 E 6 GLY R 77 SER R 83 1 O ALA R 79 N LEU R 9
SHEET 5 E 6 MET R 111 ASN R 116 1 O ILE R 112 N LEU R 80
SHEET 6 E 6 PHE R 143 GLU R 145 1 O LEU R 144 N GLY R 115
SITE 1 AC1 15 VAL E 386 ILE E 388 VAL E 394 CYS E 395
SITE 2 AC1 15 PHE E 403 GLY E 404 ALA E 407 ARG E 414
SITE 3 AC1 15 ALA E 415 LEU E 449 LYS E 450 GLU E 451
SITE 4 AC1 15 LYS E 489 HOH E1145 HOH E1169
SITE 1 AC2 13 VAL E 365 ASN E 368 VAL E 387 GLY E 392
SITE 2 AC2 13 SER E 417 VAL E 419 HIS E 537 GLN E 539
SITE 3 AC2 13 SER E 541 GLN E 542 LYS E 556 MET E 597
SITE 4 AC2 13 HOH E1148
SITE 1 AC3 10 SER R 11 GLY R 12 GLY R 13 VAL R 14
SITE 2 AC3 10 GLY R 15 LYS R 16 SER R 17 ALA R 59
SITE 3 AC3 10 GLU R 62 HOH R 304
CRYST1 125.318 148.497 224.720 90.00 90.00 90.00 I 21 21 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 0.007980 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006734 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004450 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
