HEADER KINASE 21-JUN-95 1RGS
TITLE REGULATORY SUBUNIT OF CAMP DEPENDENT PROTEIN KINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAMP DEPENDENT PROTEIN KINASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: REGULATORY SUBUNIT;
COMPND 5 SYNONYM: RI(ALPHA);
COMPND 6 EC: 2.7.1.37;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 GENE: BOVINE SKELETON MUSCLE;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PUC VECTOR;
SOURCE 9 EXPRESSION_SYSTEM_GENE: BOVINE SKELETON MUSCLE
KEYWDS REGULATORY SUBUNIT, KINASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.SU,W.R.G.DOSTMANN,F.W.HERBERG,K.DURICK,N.-H.XUONG,L.TEN EYCK,
AUTHOR 2 S.S.TAYLOR,K.I.VARUGHESE
REVDAT 3 14-FEB-24 1RGS 1 REMARK
REVDAT 2 24-FEB-09 1RGS 1 VERSN
REVDAT 1 07-DEC-96 1RGS 0
JRNL AUTH Y.SU,W.R.DOSTMANN,F.W.HERBERG,K.DURICK,N.H.XUONG,L.TEN EYCK,
JRNL AUTH 2 S.S.TAYLOR,K.I.VARUGHESE
JRNL TITL REGULATORY SUBUNIT OF PROTEIN KINASE A: STRUCTURE OF
JRNL TITL 2 DELETION MUTANT WITH CAMP BINDING DOMAINS.
JRNL REF SCIENCE V. 269 807 1995
JRNL REFN ISSN 0036-8075
JRNL PMID 7638597
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 10254
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2015
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 44
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 0.21
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.019
REMARK 3 BOND ANGLES (DEGREES) : 2.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1RGS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000176080.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 1993
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : XUONG-HAMLIN MULTIWIRE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : UCSD
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 6.960
REMARK 200 R MERGE (I) : 0.04800
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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 : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 119.93333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 59.96667
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 89.95000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 29.98333
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 149.91667
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 119.93333
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 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 59.96667
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 29.98333
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 89.95000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 149.91667
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 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 ARG A 92
REMARK 465 ARG A 93
REMARK 465 ARG A 94
REMARK 465 ARG A 95
REMARK 465 GLY A 96
REMARK 465 ALA A 97
REMARK 465 ILE A 98
REMARK 465 SER A 99
REMARK 465 ALA A 100
REMARK 465 GLU A 101
REMARK 465 VAL A 102
REMARK 465 TYR A 103
REMARK 465 THR A 104
REMARK 465 GLU A 105
REMARK 465 GLU A 106
REMARK 465 ASP A 107
REMARK 465 ALA A 108
REMARK 465 ALA A 109
REMARK 465 SER A 110
REMARK 465 TYR A 111
REMARK 465 VAL A 112
REMARK 465 LEU A 377
REMARK 465 SER A 378
REMARK 465 VAL A 379
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 ARG A 113 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 114 CG CD CE NZ
REMARK 470 ILE A 116 CG1 CG2 CD1
REMARK 470 ASP A 119 CG OD1 OD2
REMARK 470 LYS A 132 CG CD CE NZ
REMARK 470 THR A 212 OG1 CG2
REMARK 470 GLU A 275 CG CD OE1 OE2
REMARK 470 SER A 297 OG
REMARK 470 ARG A 303 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 304 CG CD NE CZ NH1 NH2
REMARK 470 SER A 305 OG
REMARK 470 GLU A 306 CG CD OE1 OE2
REMARK 470 ASN A 307 CG OD1 ND2
REMARK 470 GLU A 308 CG CD OE1 OE2
REMARK 470 GLU A 309 CG CD OE1 OE2
REMARK 470 ARG A 315 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 331 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 340 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 350 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 375 CG1 CG2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NZ LYS A 250 NZ LYS A 250 12555 2.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 131 CD GLU A 131 OE2 0.073
REMARK 500 GLU A 143 CD GLU A 143 OE2 0.069
REMARK 500 GLU A 168 CD GLU A 168 OE2 0.086
REMARK 500 GLU A 179 CD GLU A 179 OE1 0.099
REMARK 500 GLU A 194 CD GLU A 194 OE2 0.101
REMARK 500 GLU A 245 CD GLU A 245 OE1 0.124
REMARK 500 GLU A 246 CD GLU A 246 OE2 0.114
REMARK 500 GLU A 255 CD GLU A 255 OE1 0.084
REMARK 500 GLU A 285 CD GLU A 285 OE1 0.073
REMARK 500 GLU A 289 CD GLU A 289 OE1 0.078
REMARK 500 GLU A 295 CD GLU A 295 OE2 0.087
REMARK 500 GLU A 312 CD GLU A 312 OE2 0.080
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 PRO A 117 C - N - CD ANGL. DEV. = -13.5 DEGREES
REMARK 500 ASP A 141 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 141 CB - CG - OD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 ASP A 146 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP A 146 CB - CG - OD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ASP A 167 CB - CG - OD1 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ASP A 170 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP A 176 CB - CG - OD2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 ASP A 225 CB - CG - OD1 ANGL. DEV. = -6.9 DEGREES
REMARK 500 ASP A 227 CB - CG - OD1 ANGL. DEV. = -7.8 DEGREES
REMARK 500 ASP A 227 CB - CG - OD2 ANGL. DEV. = 7.6 DEGREES
REMARK 500 ARG A 231 NE - CZ - NH1 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ARG A 231 NE - CZ - NH2 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ARG A 241 NE - CZ - NH1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP A 258 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ASP A 267 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP A 276 CB - CG - OD1 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ASP A 276 CB - CG - OD2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 PRO A 332 C - N - CD ANGL. DEV. = -18.1 DEGREES
REMARK 500 LEU A 348 N - CA - CB ANGL. DEV. = -12.7 DEGREES
REMARK 500 ASP A 349 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 349 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ASP A 362 CB - CG - OD2 ANGL. DEV. = -6.4 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 ILE A 116 65.24 -159.80
REMARK 500 PRO A 117 -103.68 41.68
REMARK 500 LYS A 118 118.57 75.41
REMARK 500 ASP A 119 -166.92 -56.70
REMARK 500 MET A 151 171.68 -59.98
REMARK 500 ASP A 170 -57.67 -136.84
REMARK 500 ASN A 186 14.22 58.95
REMARK 500 GLU A 187 -105.06 -86.30
REMARK 500 TRP A 188 130.41 165.13
REMARK 500 GLU A 194 131.17 -37.76
REMARK 500 VAL A 272 135.38 -175.93
REMARK 500 ASP A 276 151.76 -32.30
REMARK 500 GLN A 283 120.53 -34.97
REMARK 500 ASP A 288 70.19 -165.99
REMARK 500 GLU A 289 129.08 179.54
REMARK 500 ARG A 303 -73.57 -77.90
REMARK 500 ARG A 304 -79.18 168.17
REMARK 500 SER A 305 -56.38 -137.73
REMARK 500 GLU A 306 -83.69 -155.20
REMARK 500 GLU A 308 162.71 152.39
REMARK 500 VAL A 313 -16.41 -155.44
REMARK 500 PRO A 318 125.80 -36.22
REMARK 500 SER A 319 -16.38 87.35
REMARK 500 ASN A 330 31.30 94.25
REMARK 500 ARG A 331 -158.44 -105.54
REMARK 500 ALA A 334 42.54 -109.91
REMARK 500 ALA A 335 157.25 157.10
REMARK 500 ARG A 340 75.93 -113.03
REMARK 500 LEU A 348 114.82 -164.46
REMARK 500 SER A 361 -19.20 -47.33
REMARK 500 VAL A 375 -86.51 -107.53
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 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMP A 601
DBREF 1RGS A 92 379 UNP P00514 KAP0_BOVIN 92 379
SEQRES 1 A 288 ARG ARG ARG ARG GLY ALA ILE SER ALA GLU VAL TYR THR
SEQRES 2 A 288 GLU GLU ASP ALA ALA SER TYR VAL ARG LYS VAL ILE PRO
SEQRES 3 A 288 LYS ASP TYR LYS THR MET ALA ALA LEU ALA LYS ALA ILE
SEQRES 4 A 288 GLU LYS ASN VAL LEU PHE SER HIS LEU ASP ASP ASN GLU
SEQRES 5 A 288 ARG SER ASP ILE PHE ASP ALA MET PHE PRO VAL SER PHE
SEQRES 6 A 288 ILE ALA GLY GLU THR VAL ILE GLN GLN GLY ASP GLU GLY
SEQRES 7 A 288 ASP ASN PHE TYR VAL ILE ASP GLN GLY GLU MET ASP VAL
SEQRES 8 A 288 TYR VAL ASN ASN GLU TRP ALA THR SER VAL GLY GLU GLY
SEQRES 9 A 288 GLY SER PHE GLY GLU LEU ALA LEU ILE TYR GLY THR PRO
SEQRES 10 A 288 ARG ALA ALA THR VAL LYS ALA LYS THR ASN VAL LYS LEU
SEQRES 11 A 288 TRP GLY ILE ASP ARG ASP SER TYR ARG ARG ILE LEU MET
SEQRES 12 A 288 GLY SER THR LEU ARG LYS ARG LYS MET TYR GLU GLU PHE
SEQRES 13 A 288 LEU SER LYS VAL SER ILE LEU GLU SER LEU ASP LYS TRP
SEQRES 14 A 288 GLU ARG LEU THR VAL ALA ASP ALA LEU GLU PRO VAL GLN
SEQRES 15 A 288 PHE GLU ASP GLY GLN LYS ILE VAL VAL GLN GLY GLU PRO
SEQRES 16 A 288 GLY ASP GLU PHE PHE ILE ILE LEU GLU GLY SER ALA ALA
SEQRES 17 A 288 VAL LEU GLN ARG ARG SER GLU ASN GLU GLU PHE VAL GLU
SEQRES 18 A 288 VAL GLY ARG LEU GLY PRO SER ASP TYR PHE GLY GLU ILE
SEQRES 19 A 288 ALA LEU LEU MET ASN ARG PRO ARG ALA ALA THR VAL VAL
SEQRES 20 A 288 ALA ARG GLY PRO LEU LYS CYS VAL LYS LEU ASP ARG PRO
SEQRES 21 A 288 ARG PHE GLU ARG VAL LEU GLY PRO CYS SER ASP ILE LEU
SEQRES 22 A 288 LYS ARG ASN ILE GLN GLN TYR ASN SER PHE VAL SER LEU
SEQRES 23 A 288 SER VAL
HET CMP A 401 22
HET CMP A 601 22
HETNAM CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE
HETSYN CMP CYCLIC AMP; CAMP
FORMUL 2 CMP 2(C10 H12 N5 O6 P)
HELIX 1 1 LYS A 121 LYS A 132 1 12
HELIX 2 2 VAL A 134 PHE A 136 5 3
HELIX 3 3 ASP A 141 ALA A 150 1 10
HELIX 4 4 GLU A 200 TYR A 205 1 6
HELIX 5 5 ARG A 226 ILE A 232 1 7
HELIX 6 6 MET A 234 LYS A 250 1 17
HELIX 7 7 SER A 252 SER A 256 5 5
HELIX 8 8 LYS A 259 ALA A 268 1 10
HELIX 9 9 GLU A 324 MET A 329 1 6
HELIX 10 10 ARG A 350 VAL A 356 1 7
HELIX 11 11 PRO A 359 GLN A 370 5 12
SHEET 1 A 3 PHE A 152 PHE A 156 0
SHEET 2 A 3 VAL A 219 ASP A 225 -1 N GLY A 223 O PHE A 152
SHEET 3 A 3 ASN A 171 GLN A 177 -1 N GLN A 177 O LYS A 220
SHEET 1 B 3 THR A 190 VAL A 192 0
SHEET 2 B 3 MET A 180 TYR A 183 -1 N VAL A 182 O THR A 190
SHEET 3 B 3 THR A 212 ALA A 215 -1 N LYS A 214 O ASP A 181
SHEET 1 C 4 GLN A 278 VAL A 281 0
SHEET 2 C 4 THR A 336 ALA A 339 -1 N ALA A 339 O GLN A 278
SHEET 3 C 4 SER A 297 GLN A 302 -1 N LEU A 301 O THR A 336
SHEET 4 C 4 VAL A 311 GLY A 317 -1 N LEU A 316 O ALA A 298
SHEET 1 D 2 GLU A 289 GLU A 295 0
SHEET 2 D 2 LYS A 344 ASP A 349 -1 N LEU A 348 O PHE A 290
SITE 1 AC1 9 PHE A 198 GLY A 199 GLU A 200 LEU A 201
SITE 2 AC1 9 ALA A 202 ARG A 209 ALA A 210 ALA A 211
SITE 3 AC1 9 TRP A 260
SITE 1 AC2 12 ASN A 185 PHE A 322 GLY A 323 GLU A 324
SITE 2 AC2 12 ILE A 325 ALA A 326 ARG A 333 ALA A 334
SITE 3 AC2 12 ALA A 335 TYR A 371 ASN A 372 SER A 373
CRYST1 88.900 88.900 179.900 90.00 90.00 120.00 P 65 2 2 12
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 0.011249 0.006494 0.000000 0.00000
SCALE2 0.000000 0.012989 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005559 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
