HEADER TRANSFERASE/SIGNALING PROTEIN 11-MAR-08 3CIK
TITLE HUMAN GRK2 IN COMPLEX WITH GBETAGAMMA SUBUNITS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-ADRENERGIC RECEPTOR KINASE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BETA-ARK-1, G-PROTEIN COUPLED RECEPTOR KINASE 2;
COMPND 5 EC: 2.7.11.15;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT
COMPND 9 BETA-1;
COMPND 10 CHAIN: B;
COMPND 11 SYNONYM: TRANSDUCIN BETA CHAIN 1;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT
COMPND 15 GAMMA-2;
COMPND 16 CHAIN: G;
COMPND 17 SYNONYM: G GAMMA-I;
COMPND 18 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ADRBK1, BARK, BARK1, GRK2;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 11 ORGANISM_COMMON: BOVINE;
SOURCE 12 ORGANISM_TAXID: 9913;
SOURCE 13 GENE: GNB1;
SOURCE 14 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 15 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 17 MOL_ID: 3;
SOURCE 18 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 19 ORGANISM_COMMON: BOVINE;
SOURCE 20 ORGANISM_TAXID: 9913;
SOURCE 21 GENE: GNG2;
SOURCE 22 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 23 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 24 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS PROTEIN KINASE, COMPLEX, G PROTEIN, RECEPTOR, WD40 REPEAT, ATP-
KEYWDS 2 BINDING, NUCLEOTIDE-BINDING, SERINE/THREONINE-PROTEIN KINASE,
KEYWDS 3 TRANSFERASE, TRANSDUCER, WD REPEAT, LIPOPROTEIN, MEMBRANE,
KEYWDS 4 PHOSPHOPROTEIN, PRENYLATION, TRANSFERASE-SIGNALING PROTEIN COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.J.G.TESMER,D.T.LODOWSKI
REVDAT 3 07-MAR-12 3CIK 1 JRNL
REVDAT 2 13-JUL-11 3CIK 1 VERSN
REVDAT 1 17-FEB-09 3CIK 0
JRNL AUTH J.J.TESMER,V.M.TESMER,D.T.LODOWSKI,H.STEINHAGEN,J.HUBER
JRNL TITL STRUCTURE OF HUMAN G PROTEIN-COUPLED RECEPTOR KINASE 2 IN
JRNL TITL 2 COMPLEX WITH THE KINASE INHIBITOR BALANOL.
JRNL REF J.MED.CHEM. V. 53 1867 2010
JRNL REFN ISSN 0022-2623
JRNL PMID 20128603
JRNL DOI 10.1021/JM9017515
REMARK 2
REMARK 2 RESOLUTION. 2.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 38772
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 + TEST SET) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1949
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) : 2.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.82
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2780
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.58
REMARK 3 BIN R VALUE (WORKING SET) : 0.3110
REMARK 3 BIN FREE R VALUE SET COUNT : 152
REMARK 3 BIN FREE R VALUE : 0.4240
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8165
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 19
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.33
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.03000
REMARK 3 B22 (A**2) : 3.35000
REMARK 3 B33 (A**2) : -4.17000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.18000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.668
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.183
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.966
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.939
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8337 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 5845 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11223 ; 1.310 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): 14168 ; 0.860 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1013 ; 6.638 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 404 ;33.018 ;23.663
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1518 ;16.585 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 67 ;17.437 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1209 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9231 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1737 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1675 ; 0.216 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 5871 ; 0.185 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3932 ; 0.183 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 4525 ; 0.087 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 174 ; 0.147 ; 0.200
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): 11 ; 0.190 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 41 ; 0.207 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 1 ; 0.148 ; 0.200
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): 6545 ; 1.172 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2064 ; 0.105 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8138 ; 1.743 ; 5.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3834 ; 2.895 ; 5.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3085 ; 4.238 ;10.000
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 : 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 185 A 513
REMARK 3 RESIDUE RANGE : A 690 A 700
REMARK 3 ORIGIN FOR THE GROUP (A): 43.2610 -5.2710 47.4230
REMARK 3 T TENSOR
REMARK 3 T11: -0.0782 T22: -0.1472
REMARK 3 T33: -0.0642 T12: -0.0589
REMARK 3 T13: -0.1211 T23: -0.0357
REMARK 3 L TENSOR
REMARK 3 L11: 1.6168 L22: 2.1902
REMARK 3 L33: 3.8797 L12: -0.1001
REMARK 3 L13: 0.0888 L23: 0.6625
REMARK 3 S TENSOR
REMARK 3 S11: 0.0193 S12: -0.1444 S13: -0.2325
REMARK 3 S21: 0.2395 S22: -0.1960 S23: 0.0199
REMARK 3 S31: 0.5964 S32: -0.0002 S33: 0.1767
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 2 B 340
REMARK 3 RESIDUE RANGE : G 8 G 68
REMARK 3 RESIDUE RANGE : B 341 B 342
REMARK 3 RESIDUE RANGE : B 343 B 347
REMARK 3 ORIGIN FOR THE GROUP (A): 67.1190 43.4300 113.0120
REMARK 3 T TENSOR
REMARK 3 T11: -0.0991 T22: -0.0954
REMARK 3 T33: -0.1875 T12: -0.1120
REMARK 3 T13: 0.0059 T23: -0.0482
REMARK 3 L TENSOR
REMARK 3 L11: 2.2015 L22: 1.0448
REMARK 3 L33: 2.5809 L12: 0.0010
REMARK 3 L13: 0.8556 L23: 0.0401
REMARK 3 S TENSOR
REMARK 3 S11: -0.0643 S12: 0.1347 S13: 0.1827
REMARK 3 S21: -0.0652 S22: 0.0657 S23: -0.1747
REMARK 3 S31: -0.2102 S32: 0.3488 S33: -0.0014
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 29 A 184
REMARK 3 RESIDUE RANGE : A 514 A 545
REMARK 3 RESIDUE RANGE : A 701 A 701
REMARK 3 ORIGIN FOR THE GROUP (A): 50.8850 29.3340 53.6180
REMARK 3 T TENSOR
REMARK 3 T11: -0.0469 T22: -0.0869
REMARK 3 T33: -0.1307 T12: 0.0631
REMARK 3 T13: -0.0601 T23: -0.0446
REMARK 3 L TENSOR
REMARK 3 L11: 2.1148 L22: 2.0461
REMARK 3 L33: 4.9083 L12: 0.0637
REMARK 3 L13: -0.3417 L23: 0.0670
REMARK 3 S TENSOR
REMARK 3 S11: 0.1161 S12: 0.3342 S13: 0.3344
REMARK 3 S21: -0.1558 S22: -0.1158 S23: -0.1041
REMARK 3 S31: -0.4785 S32: 0.0406 S33: -0.0003
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 : A 546 A 669
REMARK 3 ORIGIN FOR THE GROUP (A): 48.7710 23.4280 90.6010
REMARK 3 T TENSOR
REMARK 3 T11: 0.0310 T22: -0.0208
REMARK 3 T33: -0.3145 T12: -0.1463
REMARK 3 T13: 0.0226 T23: -0.0955
REMARK 3 L TENSOR
REMARK 3 L11: 5.1611 L22: 3.5309
REMARK 3 L33: 7.2753 L12: 0.4506
REMARK 3 L13: 1.9020 L23: 1.4073
REMARK 3 S TENSOR
REMARK 3 S11: 0.3342 S12: -0.4334 S13: -0.2044
REMARK 3 S21: 0.3678 S22: -0.3088 S23: 0.2095
REMARK 3 S31: 0.9071 S32: -0.8172 S33: -0.0254
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 3CIK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAR-08.
REMARK 100 THE RCSB ID CODE IS RCSB046817.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-FEB-05
REMARK 200 TEMPERATURE (KELVIN) : 90
REMARK 200 PH : 5.25
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.033
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38796
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.750
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.10100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.54500
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: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM NACL, 5% ETHYLENE GLYCOL, 6.3%
REMARK 280 PEG 3350, PH 5.25, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 277K, VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 92.86800
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.80200
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 92.86800
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 36.80200
REMARK 290 SMTRY3 4 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 48040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.6 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, G
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 1
REMARK 465 ALA A 2
REMARK 465 ASP A 3
REMARK 465 LEU A 4
REMARK 465 GLU A 5
REMARK 465 ALA A 6
REMARK 465 VAL A 7
REMARK 465 LEU A 8
REMARK 465 ALA A 9
REMARK 465 ASP A 10
REMARK 465 VAL A 11
REMARK 465 SER A 12
REMARK 465 TYR A 13
REMARK 465 LEU A 14
REMARK 465 MET A 15
REMARK 465 ALA A 16
REMARK 465 MET A 17
REMARK 465 GLU A 18
REMARK 465 LYS A 19
REMARK 465 SER A 20
REMARK 465 LYS A 21
REMARK 465 ALA A 22
REMARK 465 THR A 23
REMARK 465 PRO A 24
REMARK 465 ALA A 25
REMARK 465 ALA A 26
REMARK 465 ARG A 27
REMARK 465 ALA A 28
REMARK 465 GLU A 476
REMARK 465 VAL A 477
REMARK 465 ASN A 478
REMARK 465 ALA A 479
REMARK 465 ALA A 480
REMARK 465 ASP A 481
REMARK 465 ALA A 482
REMARK 465 PHE A 483
REMARK 465 ASP A 484
REMARK 465 ILE A 485
REMARK 465 GLY A 486
REMARK 465 SER A 487
REMARK 465 PHE A 488
REMARK 465 ASP A 489
REMARK 465 GLU A 490
REMARK 465 GLU A 491
REMARK 465 ASP A 492
REMARK 465 GLY A 569
REMARK 465 ASN A 570
REMARK 465 PRO A 571
REMARK 465 PHE A 572
REMARK 465 LEU A 573
REMARK 465 SER A 670
REMARK 465 PRO A 671
REMARK 465 VAL A 672
REMARK 465 VAL A 673
REMARK 465 GLU A 674
REMARK 465 LEU A 675
REMARK 465 SER A 676
REMARK 465 LYS A 677
REMARK 465 VAL A 678
REMARK 465 PRO A 679
REMARK 465 LEU A 680
REMARK 465 VAL A 681
REMARK 465 GLN A 682
REMARK 465 ARG A 683
REMARK 465 GLY A 684
REMARK 465 SER A 685
REMARK 465 ALA A 686
REMARK 465 ASN A 687
REMARK 465 GLY A 688
REMARK 465 LEU A 689
REMARK 465 MET B 1
REMARK 465 HIS G -5
REMARK 465 HIS G -4
REMARK 465 HIS G -3
REMARK 465 HIS G -2
REMARK 465 HIS G -1
REMARK 465 HIS G 0
REMARK 465 MET G 1
REMARK 465 ALA G 2
REMARK 465 SER G 3
REMARK 465 ASN G 4
REMARK 465 ASN G 5
REMARK 465 THR G 6
REMARK 465 ALA G 7
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 123 C - N - CA ANGL. DEV. = -9.2 DEGREES
REMARK 500 VAL B 71 CB - CA - C ANGL. DEV. = -11.8 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 VAL A 53 70.51 -101.30
REMARK 500 PHE A 109 24.36 -68.38
REMARK 500 ASP A 110 -67.58 -121.36
REMARK 500 SER A 121 -13.15 61.74
REMARK 500 LYS A 139 15.92 57.94
REMARK 500 ILE A 197 27.20 -148.99
REMARK 500 ARG A 316 -16.37 69.81
REMARK 500 SER A 334 -84.39 -113.38
REMARK 500 LYS A 344 -78.28 -93.84
REMARK 500 HIS A 348 -22.89 -145.04
REMARK 500 ASP A 369 -145.89 -127.35
REMARK 500 HIS A 394 54.41 39.98
REMARK 500 LYS A 395 74.79 45.60
REMARK 500 PRO A 473 -83.05 -88.23
REMARK 500 ARG A 474 110.13 -171.17
REMARK 500 THR A 524 -80.83 -128.90
REMARK 500 HIS A 549 128.05 -35.53
REMARK 500 GLU A 551 112.60 -28.24
REMARK 500 ASP A 552 123.68 -35.00
REMARK 500 LYS A 557 -149.10 -125.37
REMARK 500 GLN A 575 73.59 -172.99
REMARK 500 LYS A 615 -108.18 61.15
REMARK 500 ARG A 625 -65.02 18.29
REMARK 500 PRO A 668 99.16 -44.15
REMARK 500 ALA B 56 -166.61 -163.38
REMARK 500 ARG B 68 -56.88 -129.34
REMARK 500 THR B 87 -6.12 86.56
REMARK 500 TRP B 99 34.74 -96.44
REMARK 500 ARG B 137 132.93 -171.54
REMARK 500 THR B 164 -0.43 92.18
REMARK 500 THR B 196 26.65 49.65
REMARK 500 HIS B 266 133.49 -172.73
REMARK 500 PHE B 292 -12.32 94.33
REMARK 500 ALA B 302 -8.51 74.50
REMARK 500 ARG B 314 132.78 -29.00
REMARK 500 SER B 334 -3.03 93.56
REMARK 500 ARG G 62 -75.24 -111.63
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PHE G 67 CMT G 68 149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 PHE G 67 -15.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 690 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 348 O
REMARK 620 2 GLU A 360 O 146.3
REMARK 620 3 GLN A 363 O 105.6 98.6
REMARK 620 4 VAL A 366 O 97.9 92.6 115.0
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 690
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OMW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN G PROTEIN-COUPLED
REMARK 900 RECEPTOR KINASE 2 AND HETEROTRIMERIC G PROTEIN BETA 1 AND
REMARK 900 GAMMA 2 SUBUNITS
REMARK 900 RELATED ID: 1BX6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE POTENT NATURAL PRODUCT INHIBITOR
REMARK 900 BALANOL IN COMPLEX WITH THE CATALYTIC SUBUNIT OF CAMP-
REMARK 900 DEPENDENT PROTEIN KINASE
REMARK 900 RELATED ID: 3CIL RELATED DB: PDB
REMARK 900 HUMAN GRK2 IN COMPLEX WITH GBETAGAMMA SUBUNITS AND BALANOL
DBREF 3CIK A 1 689 UNP P25098 ARBK1_HUMAN 1 689
DBREF 3CIK B 1 340 UNP P62871 GBB1_BOVIN 1 340
DBREF 3CIK G 1 68 UNP P63212 GBG2_BOVIN 1 68
SEQADV 3CIK HIS G -5 UNP P63212 EXPRESSION TAG
SEQADV 3CIK HIS G -4 UNP P63212 EXPRESSION TAG
SEQADV 3CIK HIS G -3 UNP P63212 EXPRESSION TAG
SEQADV 3CIK HIS G -2 UNP P63212 EXPRESSION TAG
SEQADV 3CIK HIS G -1 UNP P63212 EXPRESSION TAG
SEQADV 3CIK HIS G 0 UNP P63212 EXPRESSION TAG
SEQRES 1 A 689 MET ALA ASP LEU GLU ALA VAL LEU ALA ASP VAL SER TYR
SEQRES 2 A 689 LEU MET ALA MET GLU LYS SER LYS ALA THR PRO ALA ALA
SEQRES 3 A 689 ARG ALA SER LYS LYS ILE LEU LEU PRO GLU PRO SER ILE
SEQRES 4 A 689 ARG SER VAL MET GLN LYS TYR LEU GLU ASP ARG GLY GLU
SEQRES 5 A 689 VAL THR PHE GLU LYS ILE PHE SER GLN LYS LEU GLY TYR
SEQRES 6 A 689 LEU LEU PHE ARG ASP PHE CYS LEU ASN HIS LEU GLU GLU
SEQRES 7 A 689 ALA ARG PRO LEU VAL GLU PHE TYR GLU GLU ILE LYS LYS
SEQRES 8 A 689 TYR GLU LYS LEU GLU THR GLU GLU GLU ARG VAL ALA ARG
SEQRES 9 A 689 SER ARG GLU ILE PHE ASP SER TYR ILE MET LYS GLU LEU
SEQRES 10 A 689 LEU ALA CYS SER HIS PRO PHE SER LYS SER ALA THR GLU
SEQRES 11 A 689 HIS VAL GLN GLY HIS LEU GLY LYS LYS GLN VAL PRO PRO
SEQRES 12 A 689 ASP LEU PHE GLN PRO TYR ILE GLU GLU ILE CYS GLN ASN
SEQRES 13 A 689 LEU ARG GLY ASP VAL PHE GLN LYS PHE ILE GLU SER ASP
SEQRES 14 A 689 LYS PHE THR ARG PHE CYS GLN TRP LYS ASN VAL GLU LEU
SEQRES 15 A 689 ASN ILE HIS LEU THR MET ASN ASP PHE SER VAL HIS ARG
SEQRES 16 A 689 ILE ILE GLY ARG GLY GLY PHE GLY GLU VAL TYR GLY CYS
SEQRES 17 A 689 ARG LYS ALA ASP THR GLY LYS MET TYR ALA MET LYS CYS
SEQRES 18 A 689 LEU ASP LYS LYS ARG ILE LYS MET LYS GLN GLY GLU THR
SEQRES 19 A 689 LEU ALA LEU ASN GLU ARG ILE MET LEU SER LEU VAL SER
SEQRES 20 A 689 THR GLY ASP CYS PRO PHE ILE VAL CYS MET SER TYR ALA
SEQRES 21 A 689 PHE HIS THR PRO ASP LYS LEU SER PHE ILE LEU ASP LEU
SEQRES 22 A 689 MET ASN GLY GLY ASP LEU HIS TYR HIS LEU SER GLN HIS
SEQRES 23 A 689 GLY VAL PHE SER GLU ALA ASP MET ARG PHE TYR ALA ALA
SEQRES 24 A 689 GLU ILE ILE LEU GLY LEU GLU HIS MET HIS ASN ARG PHE
SEQRES 25 A 689 VAL VAL TYR ARG ASP LEU LYS PRO ALA ASN ILE LEU LEU
SEQRES 26 A 689 ASP GLU HIS GLY HIS VAL ARG ILE SER ASP LEU GLY LEU
SEQRES 27 A 689 ALA CYS ASP PHE SER LYS LYS LYS PRO HIS ALA SER VAL
SEQRES 28 A 689 GLY THR HIS GLY TYR MET ALA PRO GLU VAL LEU GLN LYS
SEQRES 29 A 689 GLY VAL ALA TYR ASP SER SER ALA ASP TRP PHE SER LEU
SEQRES 30 A 689 GLY CYS MET LEU PHE LYS LEU LEU ARG GLY HIS SER PRO
SEQRES 31 A 689 PHE ARG GLN HIS LYS THR LYS ASP LYS HIS GLU ILE ASP
SEQRES 32 A 689 ARG MET THR LEU THR MET ALA VAL GLU LEU PRO ASP SER
SEQRES 33 A 689 PHE SER PRO GLU LEU ARG SER LEU LEU GLU GLY LEU LEU
SEQRES 34 A 689 GLN ARG ASP VAL ASN ARG ARG LEU GLY CYS LEU GLY ARG
SEQRES 35 A 689 GLY ALA GLN GLU VAL LYS GLU SER PRO PHE PHE ARG SER
SEQRES 36 A 689 LEU ASP TRP GLN MET VAL PHE LEU GLN LYS TYR PRO PRO
SEQRES 37 A 689 PRO LEU ILE PRO PRO ARG GLY GLU VAL ASN ALA ALA ASP
SEQRES 38 A 689 ALA PHE ASP ILE GLY SER PHE ASP GLU GLU ASP THR LYS
SEQRES 39 A 689 GLY ILE LYS LEU LEU ASP SER ASP GLN GLU LEU TYR ARG
SEQRES 40 A 689 ASN PHE PRO LEU THR ILE SER GLU ARG TRP GLN GLN GLU
SEQRES 41 A 689 VAL ALA GLU THR VAL PHE ASP THR ILE ASN ALA GLU THR
SEQRES 42 A 689 ASP ARG LEU GLU ALA ARG LYS LYS ALA LYS ASN LYS GLN
SEQRES 43 A 689 LEU GLY HIS GLU GLU ASP TYR ALA LEU GLY LYS ASP CYS
SEQRES 44 A 689 ILE MET HIS GLY TYR MET SER LYS MET GLY ASN PRO PHE
SEQRES 45 A 689 LEU THR GLN TRP GLN ARG ARG TYR PHE TYR LEU PHE PRO
SEQRES 46 A 689 ASN ARG LEU GLU TRP ARG GLY GLU GLY GLU ALA PRO GLN
SEQRES 47 A 689 SER LEU LEU THR MET GLU GLU ILE GLN SER VAL GLU GLU
SEQRES 48 A 689 THR GLN ILE LYS GLU ARG LYS CYS LEU LEU LEU LYS ILE
SEQRES 49 A 689 ARG GLY GLY LYS GLN PHE ILE LEU GLN CYS ASP SER ASP
SEQRES 50 A 689 PRO GLU LEU VAL GLN TRP LYS LYS GLU LEU ARG ASP ALA
SEQRES 51 A 689 TYR ARG GLU ALA GLN GLN LEU VAL GLN ARG VAL PRO LYS
SEQRES 52 A 689 MET LYS ASN LYS PRO ARG SER PRO VAL VAL GLU LEU SER
SEQRES 53 A 689 LYS VAL PRO LEU VAL GLN ARG GLY SER ALA ASN GLY LEU
SEQRES 1 B 340 MET SER GLU LEU ASP GLN LEU ARG GLN GLU ALA GLU GLN
SEQRES 2 B 340 LEU LYS ASN GLN ILE ARG ASP ALA ARG LYS ALA CYS ALA
SEQRES 3 B 340 ASP ALA THR LEU SER GLN ILE THR ASN ASN ILE ASP PRO
SEQRES 4 B 340 VAL GLY ARG ILE GLN MET ARG THR ARG ARG THR LEU ARG
SEQRES 5 B 340 GLY HIS LEU ALA LYS ILE TYR ALA MET HIS TRP GLY THR
SEQRES 6 B 340 ASP SER ARG LEU LEU VAL SER ALA SER GLN ASP GLY LYS
SEQRES 7 B 340 LEU ILE ILE TRP ASP SER TYR THR THR ASN LYS VAL HIS
SEQRES 8 B 340 ALA ILE PRO LEU ARG SER SER TRP VAL MET THR CYS ALA
SEQRES 9 B 340 TYR ALA PRO SER GLY ASN TYR VAL ALA CYS GLY GLY LEU
SEQRES 10 B 340 ASP ASN ILE CYS SER ILE TYR ASN LEU LYS THR ARG GLU
SEQRES 11 B 340 GLY ASN VAL ARG VAL SER ARG GLU LEU ALA GLY HIS THR
SEQRES 12 B 340 GLY TYR LEU SER CYS CYS ARG PHE LEU ASP ASP ASN GLN
SEQRES 13 B 340 ILE VAL THR SER SER GLY ASP THR THR CYS ALA LEU TRP
SEQRES 14 B 340 ASP ILE GLU THR GLY GLN GLN THR THR THR PHE THR GLY
SEQRES 15 B 340 HIS THR GLY ASP VAL MET SER LEU SER LEU ALA PRO ASP
SEQRES 16 B 340 THR ARG LEU PHE VAL SER GLY ALA CYS ASP ALA SER ALA
SEQRES 17 B 340 LYS LEU TRP ASP VAL ARG GLU GLY MET CYS ARG GLN THR
SEQRES 18 B 340 PHE THR GLY HIS GLU SER ASP ILE ASN ALA ILE CYS PHE
SEQRES 19 B 340 PHE PRO ASN GLY ASN ALA PHE ALA THR GLY SER ASP ASP
SEQRES 20 B 340 ALA THR CYS ARG LEU PHE ASP LEU ARG ALA ASP GLN GLU
SEQRES 21 B 340 LEU MET THR TYR SER HIS ASP ASN ILE ILE CYS GLY ILE
SEQRES 22 B 340 THR SER VAL SER PHE SER LYS SER GLY ARG LEU LEU LEU
SEQRES 23 B 340 ALA GLY TYR ASP ASP PHE ASN CYS ASN VAL TRP ASP ALA
SEQRES 24 B 340 LEU LYS ALA ASP ARG ALA GLY VAL LEU ALA GLY HIS ASP
SEQRES 25 B 340 ASN ARG VAL SER CYS LEU GLY VAL THR ASP ASP GLY MET
SEQRES 26 B 340 ALA VAL ALA THR GLY SER TRP ASP SER PHE LEU LYS ILE
SEQRES 27 B 340 TRP ASN
SEQRES 1 G 74 HIS HIS HIS HIS HIS HIS MET ALA SER ASN ASN THR ALA
SEQRES 2 G 74 SER ILE ALA GLN ALA ARG LYS LEU VAL GLU GLN LEU LYS
SEQRES 3 G 74 MET GLU ALA ASN ILE ASP ARG ILE LYS VAL SER LYS ALA
SEQRES 4 G 74 ALA ALA ASP LEU MET ALA TYR CYS GLU ALA HIS ALA LYS
SEQRES 5 G 74 GLU ASP PRO LEU LEU THR PRO VAL PRO ALA SER GLU ASN
SEQRES 6 G 74 PRO PHE ARG GLU LYS LYS PHE PHE CMT
MODRES 3CIK CMT G 68 CYS O-METHYLCYSTEINE
HET CMT G 68 8
HET MG A 690 1
HETNAM CMT O-METHYLCYSTEINE
HETNAM MG MAGNESIUM ION
FORMUL 3 CMT C4 H9 N O2 S
FORMUL 4 MG MG 2+
FORMUL 5 HOH *19(H2 O)
HELIX 1 1 SER A 38 ARG A 50 1 13
HELIX 2 2 THR A 54 SER A 60 1 7
HELIX 3 3 GLN A 61 LEU A 76 1 16
HELIX 4 4 ALA A 79 LYS A 94 1 16
HELIX 5 5 THR A 97 PHE A 109 1 13
HELIX 6 6 ASP A 110 ALA A 119 1 10
HELIX 7 7 SER A 125 GLY A 137 1 13
HELIX 8 8 PRO A 142 LEU A 145 5 4
HELIX 9 9 PHE A 146 ARG A 158 1 13
HELIX 10 10 GLY A 159 SER A 168 1 10
HELIX 11 11 SER A 168 LEU A 182 1 15
HELIX 12 12 THR A 187 ASN A 189 5 3
HELIX 13 13 LYS A 224 LYS A 230 1 7
HELIX 14 14 GLY A 232 SER A 247 1 16
HELIX 15 15 ASP A 278 GLY A 287 1 10
HELIX 16 16 SER A 290 ARG A 311 1 22
HELIX 17 17 LYS A 319 ALA A 321 5 3
HELIX 18 18 ASP A 335 ALA A 339 5 5
HELIX 19 19 ALA A 358 GLN A 363 1 6
HELIX 20 20 SER A 370 GLY A 387 1 18
HELIX 21 21 ASP A 398 MET A 409 1 12
HELIX 22 22 SER A 418 LEU A 429 1 12
HELIX 23 23 ASP A 432 ARG A 436 5 5
HELIX 24 24 GLY A 443 GLU A 449 1 7
HELIX 25 25 SER A 450 ARG A 454 5 5
HELIX 26 26 ASP A 457 LEU A 463 1 7
HELIX 27 27 LEU A 499 GLU A 504 1 6
HELIX 28 28 LEU A 505 ARG A 507 5 3
HELIX 29 29 ILE A 513 GLU A 523 1 11
HELIX 30 30 VAL A 525 GLY A 548 1 24
HELIX 31 31 SER A 636 ARG A 660 1 25
HELIX 32 32 SER B 2 ALA B 26 1 25
HELIX 33 33 THR B 29 THR B 34 1 6
HELIX 34 34 ASN B 35 ILE B 37 5 3
HELIX 35 35 SER G 8 ASN G 24 1 17
HELIX 36 36 LYS G 29 HIS G 44 1 16
HELIX 37 37 PRO G 55 ASN G 59 5 5
SHEET 1 A 6 PHE A 191 ARG A 199 0
SHEET 2 A 6 GLU A 204 LYS A 210 -1 O GLY A 207 N HIS A 194
SHEET 3 A 6 MET A 216 ASP A 223 -1 O MET A 219 N TYR A 206
SHEET 4 A 6 LYS A 266 LEU A 271 -1 O LEU A 271 N ALA A 218
SHEET 5 A 6 MET A 257 HIS A 262 -1 N PHE A 261 O SER A 268
SHEET 6 A 6 LEU A 511 THR A 512 -1 O LEU A 511 N ALA A 260
SHEET 1 B 2 VAL A 313 VAL A 314 0
SHEET 2 B 2 CYS A 340 ASP A 341 -1 O CYS A 340 N VAL A 314
SHEET 1 C 2 ILE A 323 LEU A 325 0
SHEET 2 C 2 VAL A 331 ILE A 333 -1 O ARG A 332 N LEU A 324
SHEET 1 D 7 SER A 599 THR A 602 0
SHEET 2 D 7 ARG A 587 ARG A 591 -1 N LEU A 588 O LEU A 601
SHEET 3 D 7 GLN A 577 PHE A 584 -1 N PHE A 584 O ARG A 587
SHEET 4 D 7 MET A 561 MET A 568 -1 N GLY A 563 O PHE A 581
SHEET 5 D 7 LYS A 628 GLN A 633 -1 O GLN A 633 N SER A 566
SHEET 6 D 7 ARG A 617 ILE A 624 -1 N LEU A 622 O PHE A 630
SHEET 7 D 7 ILE A 606 ILE A 614 -1 N THR A 612 O CYS A 619
SHEET 1 E 4 ARG B 46 LEU B 51 0
SHEET 2 E 4 LEU B 336 ASN B 340 -1 O ILE B 338 N ARG B 48
SHEET 3 E 4 VAL B 327 SER B 331 -1 N VAL B 327 O TRP B 339
SHEET 4 E 4 VAL B 315 VAL B 320 -1 N SER B 316 O GLY B 330
SHEET 1 F 4 ILE B 58 TRP B 63 0
SHEET 2 F 4 LEU B 69 SER B 74 -1 O ALA B 73 N TYR B 59
SHEET 3 F 4 LYS B 78 ASP B 83 -1 O TRP B 82 N LEU B 70
SHEET 4 F 4 LYS B 89 PRO B 94 -1 O ILE B 93 N LEU B 79
SHEET 1 G 4 VAL B 100 TYR B 105 0
SHEET 2 G 4 TYR B 111 GLY B 116 -1 O GLY B 115 N MET B 101
SHEET 3 G 4 CYS B 121 ASN B 125 -1 O TYR B 124 N VAL B 112
SHEET 4 G 4 ARG B 134 LEU B 139 -1 O LEU B 139 N CYS B 121
SHEET 1 H 4 LEU B 146 ASP B 153 0
SHEET 2 H 4 GLN B 156 SER B 161 -1 O GLN B 156 N LEU B 152
SHEET 3 H 4 CYS B 166 ASP B 170 -1 O ALA B 167 N THR B 159
SHEET 4 H 4 GLN B 175 PHE B 180 -1 O PHE B 180 N CYS B 166
SHEET 1 I 4 VAL B 187 LEU B 192 0
SHEET 2 I 4 LEU B 198 ALA B 203 -1 O GLY B 202 N MET B 188
SHEET 3 I 4 ALA B 208 ASP B 212 -1 O TRP B 211 N PHE B 199
SHEET 4 I 4 MET B 217 PHE B 222 -1 O PHE B 222 N ALA B 208
SHEET 1 J 4 ILE B 229 PHE B 234 0
SHEET 2 J 4 ALA B 240 SER B 245 -1 O GLY B 244 N ASN B 230
SHEET 3 J 4 CYS B 250 ASP B 254 -1 O PHE B 253 N PHE B 241
SHEET 4 J 4 GLN B 259 TYR B 264 -1 O LEU B 261 N LEU B 252
SHEET 1 K 4 ILE B 273 PHE B 278 0
SHEET 2 K 4 LEU B 284 TYR B 289 -1 O LEU B 286 N SER B 277
SHEET 3 K 4 ASN B 293 ASP B 298 -1 O TRP B 297 N LEU B 285
SHEET 4 K 4 ARG B 304 ALA B 309 -1 O ALA B 305 N VAL B 296
LINK C PHE G 67 N CMT G 68 1555 1555 1.29
LINK O HIS A 348 MG MG A 690 1555 1555 2.20
LINK O GLU A 360 MG MG A 690 1555 1555 2.19
LINK O GLN A 363 MG MG A 690 1555 1555 2.20
LINK O VAL A 366 MG MG A 690 1555 1555 2.19
SITE 1 AC1 3 HIS A 348 GLU A 360 GLN A 363
CRYST1 185.736 73.604 122.914 90.00 115.22 90.00 C 1 2 1 4
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 0.005384 0.000000 0.002535 0.00000
SCALE2 0.000000 0.013586 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008993 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
