HEADER TRANSFERASE 24-JAN-12 4DFY
TITLE CRYSTAL STRUCTURE OF R194A MUTANT OF CAMP-DEPENDENT PROTEIN KINASE
TITLE 2 WITH UNPHOSPHORYLATED ACTIVATION LOOP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;
COMPND 3 CHAIN: A, E;
COMPND 4 SYNONYM: PKA C-ALPHA;
COMPND 5 EC: 2.7.11.11;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: PRKACA, PKACA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PROTEIN KINASE FOLD, SERINE/THREONINE KINASE ACTIVITY, CAMP-DEPENDENT
KEYWDS 2 PROTEIN KINASE REGULATORY SUBUNIT, PKI, PHOSPHORYLATION, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.STEICHEN,M.KUCHINSKAS,J.YANG,S.S.TAYLOR
REVDAT 3 16-MAY-12 4DFY 1 JRNL
REVDAT 2 29-FEB-12 4DFY 1 JRNL
REVDAT 1 15-FEB-12 4DFY 0
JRNL AUTH J.M.STEICHEN,M.KUCHINSKAS,M.M.KESHWANI,J.YANG,J.A.ADAMS,
JRNL AUTH 2 S.S.TAYLOR
JRNL TITL STRUCTURAL BASIS FOR THE REGULATION OF PROTEIN KINASE A BY
JRNL TITL 2 ACTIVATION LOOP PHOSPHORYLATION.
JRNL REF J.BIOL.CHEM. V. 287 14672 2012
JRNL REFN ISSN 0021-9258
JRNL PMID 22334660
JRNL DOI 10.1074/JBC.M111.335091
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.52
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.5
REMARK 3 NUMBER OF REFLECTIONS : 16987
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) : 0.253
REMARK 3 R VALUE (WORKING SET) : 0.252
REMARK 3 FREE R VALUE : 0.286
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 915
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) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.07
REMARK 3 REFLECTION IN BIN (WORKING SET) : 699
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 53.24
REMARK 3 BIN R VALUE (WORKING SET) : 0.3840
REMARK 3 BIN FREE R VALUE SET COUNT : 40
REMARK 3 BIN FREE R VALUE : 0.4090
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4984
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 7
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 104.57
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.05000
REMARK 3 B22 (A**2) : 0.05000
REMARK 3 B33 (A**2) : -0.08000
REMARK 3 B12 (A**2) : 0.03000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.484
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.471
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 61.726
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.927
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.917
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5103 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6912 ; 1.328 ; 1.954
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 618 ; 5.590 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 241 ;39.075 ;24.315
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 861 ;19.104 ;15.035
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 23 ;18.044 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 755 ; 0.081 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3870 ; 0.006 ; 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): 3107 ; 0.586 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4979 ; 1.143 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1996 ; 1.377 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1933 ; 2.462 ; 4.500
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A E
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 14 A 350 1
REMARK 3 1 E 14 E 350 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 2455 ; 0.070 ; 0.050
REMARK 3 TIGHT THERMAL 1 A (A**2): 2455 ; 0.610 ; 0.500
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 14 A 126
REMARK 3 RESIDUE RANGE : A 333 A 350
REMARK 3 ORIGIN FOR THE GROUP (A): -60.3050 13.2430 -1.0690
REMARK 3 T TENSOR
REMARK 3 T11: 0.2838 T22: 0.5401
REMARK 3 T33: 0.3564 T12: -0.0813
REMARK 3 T13: -0.0912 T23: 0.1512
REMARK 3 L TENSOR
REMARK 3 L11: 1.6127 L22: 2.4541
REMARK 3 L33: 6.1906 L12: -1.4201
REMARK 3 L13: -0.8186 L23: 2.1914
REMARK 3 S TENSOR
REMARK 3 S11: -0.1821 S12: 0.1299 S13: 0.1439
REMARK 3 S21: -0.0760 S22: 0.0172 S23: 0.1916
REMARK 3 S31: -0.3112 S32: -1.2832 S33: 0.1649
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 127 A 318
REMARK 3 ORIGIN FOR THE GROUP (A): -61.3700 21.8770 26.3060
REMARK 3 T TENSOR
REMARK 3 T11: 0.2811 T22: 0.3622
REMARK 3 T33: 0.4042 T12: 0.2610
REMARK 3 T13: 0.0913 T23: 0.0652
REMARK 3 L TENSOR
REMARK 3 L11: 2.6291 L22: 2.0404
REMARK 3 L33: 7.9667 L12: 1.0565
REMARK 3 L13: 1.0256 L23: -0.2955
REMARK 3 S TENSOR
REMARK 3 S11: -0.0364 S12: 0.0313 S13: -0.0434
REMARK 3 S21: 0.0591 S22: -0.0380 S23: -0.0463
REMARK 3 S31: -0.0885 S32: -0.4255 S33: 0.0744
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 14 E 126
REMARK 3 RESIDUE RANGE : E 333 E 350
REMARK 3 ORIGIN FOR THE GROUP (A): -31.1230 30.0980 20.2510
REMARK 3 T TENSOR
REMARK 3 T11: 0.5210 T22: 0.2933
REMARK 3 T33: 0.2791 T12: -0.3026
REMARK 3 T13: -0.0322 T23: 0.0171
REMARK 3 L TENSOR
REMARK 3 L11: 1.2206 L22: 3.5120
REMARK 3 L33: 2.4058 L12: -0.5007
REMARK 3 L13: 0.2921 L23: -0.2957
REMARK 3 S TENSOR
REMARK 3 S11: -0.0320 S12: -0.2420 S13: -0.1088
REMARK 3 S21: 0.4712 S22: 0.1044 S23: 0.0372
REMARK 3 S31: -0.7979 S32: 0.3179 S33: -0.0723
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 127 E 318
REMARK 3 ORIGIN FOR THE GROUP (A): -30.8970 4.3770 7.8980
REMARK 3 T TENSOR
REMARK 3 T11: 0.1374 T22: 0.3322
REMARK 3 T33: 0.2947 T12: -0.0879
REMARK 3 T13: -0.0169 T23: -0.0408
REMARK 3 L TENSOR
REMARK 3 L11: 2.5068 L22: 5.9456
REMARK 3 L33: 3.4786 L12: 1.7040
REMARK 3 L13: 1.4790 L23: 1.6828
REMARK 3 S TENSOR
REMARK 3 S11: -0.0881 S12: 0.0465 S13: -0.0418
REMARK 3 S21: 0.4488 S22: 0.3722 S23: -0.0981
REMARK 3 S31: 0.1398 S32: 0.4708 S33: -0.2841
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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
REMARK 4
REMARK 4 4DFY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JAN-12.
REMARK 100 THE RCSB ID CODE IS RCSB070279.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-NOV-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL (SI 111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18017
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.997
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 (%) : 94.9
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 : 28.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 59.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.33200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
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: PDB ENTRY 1RDQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS, 800 MM SODIUM FORMATE,
REMARK 280 10% PEG 8000, 10% PEG 1000, PH 7.5, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 277.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
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 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 115.97267
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 57.98633
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 57.98633
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 115.97267
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 56470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E
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 57.98633
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E
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 MET A -20
REMARK 465 GLY A -19
REMARK 465 SER A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 GLY A -8
REMARK 465 LEU A -7
REMARK 465 VAL A -6
REMARK 465 PRO A -5
REMARK 465 ARG A -4
REMARK 465 GLY A -3
REMARK 465 SER A -2
REMARK 465 HIS A -1
REMARK 465 MET A 0
REMARK 465 GLY A 1
REMARK 465 ASN A 2
REMARK 465 ALA A 3
REMARK 465 ALA A 4
REMARK 465 ALA A 5
REMARK 465 ALA A 6
REMARK 465 LYS A 7
REMARK 465 LYS A 8
REMARK 465 GLY A 9
REMARK 465 SER A 10
REMARK 465 GLU A 11
REMARK 465 GLN A 12
REMARK 465 GLU A 13
REMARK 465 LYS A 189
REMARK 465 ARG A 190
REMARK 465 VAL A 191
REMARK 465 LYS A 192
REMARK 465 GLY A 193
REMARK 465 ALA A 194
REMARK 465 THR A 195
REMARK 465 TRP A 196
REMARK 465 THR A 197
REMARK 465 LEU A 198
REMARK 465 CYS A 199
REMARK 465 GLY A 200
REMARK 465 LYS A 319
REMARK 465 GLY A 320
REMARK 465 PRO A 321
REMARK 465 GLY A 322
REMARK 465 ASP A 323
REMARK 465 THR A 324
REMARK 465 SER A 325
REMARK 465 ASN A 326
REMARK 465 PHE A 327
REMARK 465 ASP A 328
REMARK 465 ASP A 329
REMARK 465 TYR A 330
REMARK 465 GLU A 331
REMARK 465 GLU A 332
REMARK 465 MET E -20
REMARK 465 GLY E -19
REMARK 465 SER E -18
REMARK 465 SER E -17
REMARK 465 HIS E -16
REMARK 465 HIS E -15
REMARK 465 HIS E -14
REMARK 465 HIS E -13
REMARK 465 HIS E -12
REMARK 465 HIS E -11
REMARK 465 SER E -10
REMARK 465 SER E -9
REMARK 465 GLY E -8
REMARK 465 LEU E -7
REMARK 465 VAL E -6
REMARK 465 PRO E -5
REMARK 465 ARG E -4
REMARK 465 GLY E -3
REMARK 465 SER E -2
REMARK 465 HIS E -1
REMARK 465 MET E 0
REMARK 465 GLY E 1
REMARK 465 ASN E 2
REMARK 465 ALA E 3
REMARK 465 ALA E 4
REMARK 465 ALA E 5
REMARK 465 ALA E 6
REMARK 465 LYS E 7
REMARK 465 LYS E 8
REMARK 465 GLY E 9
REMARK 465 SER E 10
REMARK 465 GLU E 11
REMARK 465 GLN E 12
REMARK 465 GLU E 13
REMARK 465 LYS E 189
REMARK 465 ARG E 190
REMARK 465 VAL E 191
REMARK 465 LYS E 192
REMARK 465 GLY E 193
REMARK 465 ALA E 194
REMARK 465 THR E 195
REMARK 465 TRP E 196
REMARK 465 THR E 197
REMARK 465 LEU E 198
REMARK 465 LYS E 319
REMARK 465 GLY E 320
REMARK 465 PRO E 321
REMARK 465 GLY E 322
REMARK 465 ASP E 323
REMARK 465 THR E 324
REMARK 465 SER E 325
REMARK 465 ASN E 326
REMARK 465 PHE E 327
REMARK 465 ASP E 328
REMARK 465 ASP E 329
REMARK 465 TYR E 330
REMARK 465 GLU E 331
REMARK 465 GLU E 332
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 LYS A 16 CG CD CE NZ
REMARK 470 LYS A 28 CG CD CE NZ
REMARK 470 LYS A 72 CG CD CE NZ
REMARK 470 LYS A 78 CG CD CE NZ
REMARK 470 LYS A 81 CG CD CE NZ
REMARK 470 LYS A 83 CE NZ
REMARK 470 GLU A 91 CD OE1 OE2
REMARK 470 LYS A 105 CG CD CE NZ
REMARK 470 HIS A 131 CG ND1 CD2 CE1 NE2
REMARK 470 HIS A 142 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 168 CG CD CE NZ
REMARK 470 GLN A 176 CG CD OE1 NE2
REMARK 470 PHE A 185 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE A 187 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 256 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 295 CG CD CE NZ
REMARK 470 PHE A 314 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE A 315 CG1 CG2 CD1
REMARK 470 LYS A 317 CG CD CE NZ
REMARK 470 PHE A 318 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS E 16 CG CD CE NZ
REMARK 470 GLU E 24 CG CD OE1 OE2
REMARK 470 LYS E 78 CG CD CE NZ
REMARK 470 LYS E 83 CE NZ
REMARK 470 GLU E 86 CG CD OE1 OE2
REMARK 470 ARG E 165 CG CD NE CZ NH1 NH2
REMARK 470 ASP E 166 CG OD1 OD2
REMARK 470 LYS E 168 CG CD CE NZ
REMARK 470 GLN E 176 CG CD OE1 NE2
REMARK 470 PHE E 185 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 CYS E 199 SG
REMARK 470 ARG E 256 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 279 CG CD CE NZ
REMARK 470 LYS E 285 CG CD CE NZ
REMARK 470 LYS E 295 CD CE NZ
REMARK 470 PHE E 314 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE E 315 CG1 CG2 CD1
REMARK 470 LYS E 317 CG CD CE NZ
REMARK 470 PHE E 318 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU E 333 CG CD OE1 OE2
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 TYR E 164 CE1 TYR E 164 CZ 0.095
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 ASN A 36 70.66 50.44
REMARK 500 ALA A 38 -170.37 -174.96
REMARK 500 ILE A 46 -61.94 -96.65
REMARK 500 ARG A 165 -71.89 74.17
REMARK 500 ASP A 184 66.58 33.76
REMARK 500 ASN A 216 -179.74 -172.02
REMARK 500 ASP A 241 -70.68 -65.52
REMARK 500 SER A 259 -34.47 -32.20
REMARK 500 LEU A 273 46.25 -87.92
REMARK 500 ASP A 276 95.50 -63.12
REMARK 500 ARG A 308 16.33 82.15
REMARK 500 ASN E 36 71.74 46.23
REMARK 500 ILE E 46 -66.54 -94.41
REMARK 500 ARG E 165 -78.98 73.48
REMARK 500 ASP E 184 65.83 34.83
REMARK 500 LYS E 217 -31.94 -33.20
REMARK 500 ASP E 241 -70.42 -64.80
REMARK 500 SER E 259 -34.42 -34.68
REMARK 500 LEU E 273 48.42 -86.79
REMARK 500 ASP E 276 96.25 -58.56
REMARK 500 ARG E 308 14.02 81.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ATP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CATALYTIC SUBUNIT OF CAMP-DEPENDENT
REMARK 900 PROTEIN KINASE COMPLEXED WITH ATP AND IP20.
REMARK 900 RELATED ID: 1J3H RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF APO CAMP-DEPENDENT PROTEIN KINASE.
DBREF 4DFY A 0 350 UNP P05132 KAPCA_MOUSE 1 351
DBREF 4DFY E 0 350 UNP P05132 KAPCA_MOUSE 1 351
SEQADV 4DFY MET A -20 UNP P05132 EXPRESSION TAG
SEQADV 4DFY GLY A -19 UNP P05132 EXPRESSION TAG
SEQADV 4DFY SER A -18 UNP P05132 EXPRESSION TAG
SEQADV 4DFY SER A -17 UNP P05132 EXPRESSION TAG
SEQADV 4DFY HIS A -16 UNP P05132 EXPRESSION TAG
SEQADV 4DFY HIS A -15 UNP P05132 EXPRESSION TAG
SEQADV 4DFY HIS A -14 UNP P05132 EXPRESSION TAG
SEQADV 4DFY HIS A -13 UNP P05132 EXPRESSION TAG
SEQADV 4DFY HIS A -12 UNP P05132 EXPRESSION TAG
SEQADV 4DFY HIS A -11 UNP P05132 EXPRESSION TAG
SEQADV 4DFY SER A -10 UNP P05132 EXPRESSION TAG
SEQADV 4DFY SER A -9 UNP P05132 EXPRESSION TAG
SEQADV 4DFY GLY A -8 UNP P05132 EXPRESSION TAG
SEQADV 4DFY LEU A -7 UNP P05132 EXPRESSION TAG
SEQADV 4DFY VAL A -6 UNP P05132 EXPRESSION TAG
SEQADV 4DFY PRO A -5 UNP P05132 EXPRESSION TAG
SEQADV 4DFY ARG A -4 UNP P05132 EXPRESSION TAG
SEQADV 4DFY GLY A -3 UNP P05132 EXPRESSION TAG
SEQADV 4DFY SER A -2 UNP P05132 EXPRESSION TAG
SEQADV 4DFY HIS A -1 UNP P05132 EXPRESSION TAG
SEQADV 4DFY ALA A 194 UNP P05132 ARG 195 ENGINEERED MUTATION
SEQADV 4DFY MET E -20 UNP P05132 EXPRESSION TAG
SEQADV 4DFY GLY E -19 UNP P05132 EXPRESSION TAG
SEQADV 4DFY SER E -18 UNP P05132 EXPRESSION TAG
SEQADV 4DFY SER E -17 UNP P05132 EXPRESSION TAG
SEQADV 4DFY HIS E -16 UNP P05132 EXPRESSION TAG
SEQADV 4DFY HIS E -15 UNP P05132 EXPRESSION TAG
SEQADV 4DFY HIS E -14 UNP P05132 EXPRESSION TAG
SEQADV 4DFY HIS E -13 UNP P05132 EXPRESSION TAG
SEQADV 4DFY HIS E -12 UNP P05132 EXPRESSION TAG
SEQADV 4DFY HIS E -11 UNP P05132 EXPRESSION TAG
SEQADV 4DFY SER E -10 UNP P05132 EXPRESSION TAG
SEQADV 4DFY SER E -9 UNP P05132 EXPRESSION TAG
SEQADV 4DFY GLY E -8 UNP P05132 EXPRESSION TAG
SEQADV 4DFY LEU E -7 UNP P05132 EXPRESSION TAG
SEQADV 4DFY VAL E -6 UNP P05132 EXPRESSION TAG
SEQADV 4DFY PRO E -5 UNP P05132 EXPRESSION TAG
SEQADV 4DFY ARG E -4 UNP P05132 EXPRESSION TAG
SEQADV 4DFY GLY E -3 UNP P05132 EXPRESSION TAG
SEQADV 4DFY SER E -2 UNP P05132 EXPRESSION TAG
SEQADV 4DFY HIS E -1 UNP P05132 EXPRESSION TAG
SEQADV 4DFY ALA E 194 UNP P05132 ARG 195 ENGINEERED MUTATION
SEQRES 1 A 371 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 371 LEU VAL PRO ARG GLY SER HIS MET GLY ASN ALA ALA ALA
SEQRES 3 A 371 ALA LYS LYS GLY SER GLU GLN GLU SER VAL LYS GLU PHE
SEQRES 4 A 371 LEU ALA LYS ALA LYS GLU ASP PHE LEU LYS LYS TRP GLU
SEQRES 5 A 371 THR PRO SER GLN ASN THR ALA GLN LEU ASP GLN PHE ASP
SEQRES 6 A 371 ARG ILE LYS THR LEU GLY THR GLY SER PHE GLY ARG VAL
SEQRES 7 A 371 MET LEU VAL LYS HIS LYS GLU SER GLY ASN HIS TYR ALA
SEQRES 8 A 371 MET LYS ILE LEU ASP LYS GLN LYS VAL VAL LYS LEU LYS
SEQRES 9 A 371 GLN ILE GLU HIS THR LEU ASN GLU LYS ARG ILE LEU GLN
SEQRES 10 A 371 ALA VAL ASN PHE PRO PHE LEU VAL LYS LEU GLU PHE SER
SEQRES 11 A 371 PHE LYS ASP ASN SER ASN LEU TYR MET VAL MET GLU TYR
SEQRES 12 A 371 VAL ALA GLY GLY GLU MET PHE SER HIS LEU ARG ARG ILE
SEQRES 13 A 371 GLY ARG PHE SER GLU PRO HIS ALA ARG PHE TYR ALA ALA
SEQRES 14 A 371 GLN ILE VAL LEU THR PHE GLU TYR LEU HIS SER LEU ASP
SEQRES 15 A 371 LEU ILE TYR ARG ASP LEU LYS PRO GLU ASN LEU LEU ILE
SEQRES 16 A 371 ASP GLN GLN GLY TYR ILE GLN VAL THR ASP PHE GLY PHE
SEQRES 17 A 371 ALA LYS ARG VAL LYS GLY ALA THR TRP THR LEU CYS GLY
SEQRES 18 A 371 THR PRO GLU TYR LEU ALA PRO GLU ILE ILE LEU SER LYS
SEQRES 19 A 371 GLY TYR ASN LYS ALA VAL ASP TRP TRP ALA LEU GLY VAL
SEQRES 20 A 371 LEU ILE TYR GLU MET ALA ALA GLY TYR PRO PRO PHE PHE
SEQRES 21 A 371 ALA ASP GLN PRO ILE GLN ILE TYR GLU LYS ILE VAL SER
SEQRES 22 A 371 GLY LYS VAL ARG PHE PRO SER HIS PHE SER SER ASP LEU
SEQRES 23 A 371 LYS ASP LEU LEU ARG ASN LEU LEU GLN VAL ASP LEU THR
SEQRES 24 A 371 LYS ARG PHE GLY ASN LEU LYS ASN GLY VAL ASN ASP ILE
SEQRES 25 A 371 LYS ASN HIS LYS TRP PHE ALA THR THR ASP TRP ILE ALA
SEQRES 26 A 371 ILE TYR GLN ARG LYS VAL GLU ALA PRO PHE ILE PRO LYS
SEQRES 27 A 371 PHE LYS GLY PRO GLY ASP THR SER ASN PHE ASP ASP TYR
SEQRES 28 A 371 GLU GLU GLU GLU ILE ARG VAL SEP ILE ASN GLU LYS CYS
SEQRES 29 A 371 GLY LYS GLU PHE THR GLU PHE
SEQRES 1 E 371 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 E 371 LEU VAL PRO ARG GLY SER HIS MET GLY ASN ALA ALA ALA
SEQRES 3 E 371 ALA LYS LYS GLY SER GLU GLN GLU SER VAL LYS GLU PHE
SEQRES 4 E 371 LEU ALA LYS ALA LYS GLU ASP PHE LEU LYS LYS TRP GLU
SEQRES 5 E 371 THR PRO SER GLN ASN THR ALA GLN LEU ASP GLN PHE ASP
SEQRES 6 E 371 ARG ILE LYS THR LEU GLY THR GLY SER PHE GLY ARG VAL
SEQRES 7 E 371 MET LEU VAL LYS HIS LYS GLU SER GLY ASN HIS TYR ALA
SEQRES 8 E 371 MET LYS ILE LEU ASP LYS GLN LYS VAL VAL LYS LEU LYS
SEQRES 9 E 371 GLN ILE GLU HIS THR LEU ASN GLU LYS ARG ILE LEU GLN
SEQRES 10 E 371 ALA VAL ASN PHE PRO PHE LEU VAL LYS LEU GLU PHE SER
SEQRES 11 E 371 PHE LYS ASP ASN SER ASN LEU TYR MET VAL MET GLU TYR
SEQRES 12 E 371 VAL ALA GLY GLY GLU MET PHE SER HIS LEU ARG ARG ILE
SEQRES 13 E 371 GLY ARG PHE SER GLU PRO HIS ALA ARG PHE TYR ALA ALA
SEQRES 14 E 371 GLN ILE VAL LEU THR PHE GLU TYR LEU HIS SER LEU ASP
SEQRES 15 E 371 LEU ILE TYR ARG ASP LEU LYS PRO GLU ASN LEU LEU ILE
SEQRES 16 E 371 ASP GLN GLN GLY TYR ILE GLN VAL THR ASP PHE GLY PHE
SEQRES 17 E 371 ALA LYS ARG VAL LYS GLY ALA THR TRP THR LEU CYS GLY
SEQRES 18 E 371 THR PRO GLU TYR LEU ALA PRO GLU ILE ILE LEU SER LYS
SEQRES 19 E 371 GLY TYR ASN LYS ALA VAL ASP TRP TRP ALA LEU GLY VAL
SEQRES 20 E 371 LEU ILE TYR GLU MET ALA ALA GLY TYR PRO PRO PHE PHE
SEQRES 21 E 371 ALA ASP GLN PRO ILE GLN ILE TYR GLU LYS ILE VAL SER
SEQRES 22 E 371 GLY LYS VAL ARG PHE PRO SER HIS PHE SER SER ASP LEU
SEQRES 23 E 371 LYS ASP LEU LEU ARG ASN LEU LEU GLN VAL ASP LEU THR
SEQRES 24 E 371 LYS ARG PHE GLY ASN LEU LYS ASN GLY VAL ASN ASP ILE
SEQRES 25 E 371 LYS ASN HIS LYS TRP PHE ALA THR THR ASP TRP ILE ALA
SEQRES 26 E 371 ILE TYR GLN ARG LYS VAL GLU ALA PRO PHE ILE PRO LYS
SEQRES 27 E 371 PHE LYS GLY PRO GLY ASP THR SER ASN PHE ASP ASP TYR
SEQRES 28 E 371 GLU GLU GLU GLU ILE ARG VAL SEP ILE ASN GLU LYS CYS
SEQRES 29 E 371 GLY LYS GLU PHE THR GLU PHE
MODRES 4DFY SEP A 338 SER PHOSPHOSERINE
MODRES 4DFY SEP E 338 SER PHOSPHOSERINE
HET SEP A 338 10
HET SEP E 338 10
HETNAM SEP PHOSPHOSERINE
HETSYN SEP PHOSPHONOSERINE
FORMUL 1 SEP 2(C3 H8 N O6 P)
FORMUL 3 HOH *7(H2 O)
HELIX 1 1 SER A 14 THR A 32 1 19
HELIX 2 2 GLN A 39 ASP A 41 5 3
HELIX 3 3 LYS A 76 LEU A 82 1 7
HELIX 4 4 GLN A 84 VAL A 98 1 15
HELIX 5 5 GLU A 127 GLY A 136 1 10
HELIX 6 6 SER A 139 LEU A 160 1 22
HELIX 7 7 LYS A 168 GLU A 170 5 3
HELIX 8 8 THR A 201 LEU A 205 5 5
HELIX 9 9 ALA A 206 LEU A 211 1 6
HELIX 10 10 ALA A 218 GLY A 234 1 17
HELIX 11 11 GLN A 242 GLY A 253 1 12
HELIX 12 12 SER A 262 LEU A 273 1 12
HELIX 13 13 ASP A 276 ARG A 280 5 5
HELIX 14 14 VAL A 288 HIS A 294 1 7
HELIX 15 15 LYS A 295 ALA A 298 5 4
HELIX 16 16 ASP A 301 ARG A 308 1 8
HELIX 17 17 VAL E 15 THR E 32 1 18
HELIX 18 18 GLN E 39 ASP E 41 5 3
HELIX 19 19 LYS E 76 LEU E 82 1 7
HELIX 20 20 GLN E 84 VAL E 98 1 15
HELIX 21 21 GLU E 127 GLY E 136 1 10
HELIX 22 22 SER E 139 LEU E 160 1 22
HELIX 23 23 LYS E 168 GLU E 170 5 3
HELIX 24 24 THR E 201 LEU E 205 5 5
HELIX 25 25 ALA E 206 LEU E 211 1 6
HELIX 26 26 ALA E 218 GLY E 234 1 17
HELIX 27 27 GLN E 242 GLY E 253 1 12
HELIX 28 28 SER E 262 LEU E 273 1 12
HELIX 29 29 ASP E 276 ARG E 280 5 5
HELIX 30 30 VAL E 288 ASN E 293 1 6
HELIX 31 31 HIS E 294 ALA E 298 5 5
HELIX 32 32 ASP E 301 ARG E 308 1 8
HELIX 33 33 GLY E 344 THR E 348 5 5
SHEET 1 A 5 PHE A 43 THR A 51 0
SHEET 2 A 5 ARG A 56 HIS A 62 -1 O VAL A 57 N GLY A 50
SHEET 3 A 5 HIS A 68 ASP A 75 -1 O TYR A 69 N VAL A 60
SHEET 4 A 5 ASN A 115 GLU A 121 -1 O MET A 118 N LYS A 72
SHEET 5 A 5 LEU A 106 LYS A 111 -1 N PHE A 110 O TYR A 117
SHEET 1 B 2 LEU A 172 ILE A 174 0
SHEET 2 B 2 ILE A 180 VAL A 182 -1 O GLN A 181 N LEU A 173
SHEET 1 C 5 PHE E 43 THR E 51 0
SHEET 2 C 5 ARG E 56 HIS E 62 -1 O VAL E 57 N GLY E 50
SHEET 3 C 5 HIS E 68 ASP E 75 -1 O MET E 71 N MET E 58
SHEET 4 C 5 ASN E 115 GLU E 121 -1 O MET E 118 N LYS E 72
SHEET 5 C 5 LEU E 106 LYS E 111 -1 N PHE E 108 O VAL E 119
SHEET 1 D 2 LEU E 172 ILE E 174 0
SHEET 2 D 2 ILE E 180 VAL E 182 -1 O GLN E 181 N LEU E 173
LINK C VAL A 337 N SEP A 338 1555 1555 1.32
LINK C SEP A 338 N ILE A 339 1555 1555 1.33
LINK C VAL E 337 N SEP E 338 1555 1555 1.34
LINK C SEP E 338 N ILE E 339 1555 1555 1.33
CRYST1 95.745 95.745 173.959 90.00 90.00 120.00 P 32 2 1 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 0.010444 0.006030 0.000000 0.00000
SCALE2 0.000000 0.012060 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005748 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
