HEADER TRANSFERASE 22-JUN-09 3HYH
TITLE CRYSTAL STRUCTURE OF THE PROTEIN KINASE DOMAIN OF YEAST AMP-ACTIVATED
TITLE 2 PROTEIN KINASE SNF1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBON CATABOLITE-DEREPRESSING PROTEIN KINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: KINASE DOMAIN;
COMPND 5 EC: 2.7.11.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: CAT1, CCR1, D8035.20, GLC2, PAS14, SNF1, YDR477W;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS KINASE DOMAIN, TRANSFERASE, ATP-BINDING, CARBOHYDRATE METABOLISM,
KEYWDS 2 KINASE, MEMBRANE, NUCLEOTIDE-BINDING, NUCLEUS, PHOSPHOPROTEIN,
KEYWDS 3 SERINE/THREONINE-PROTEIN KINASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.J.RUDOLPH,G.A.AMODEO,Y.BAI,L.TONG
REVDAT 4 21-FEB-24 3HYH 1 REMARK
REVDAT 3 01-NOV-17 3HYH 1 REMARK
REVDAT 2 13-JUL-11 3HYH 1 VERSN
REVDAT 1 30-JUN-09 3HYH 0
SPRSDE 30-JUN-09 3HYH 3FAM
JRNL AUTH M.J.RUDOLPH,G.A.AMODEO,Y.BAI,L.TONG
JRNL TITL CRYSTAL STRUCTURE OF THE PROTEIN KINASE DOMAIN OF YEAST
JRNL TITL 2 AMP-ACTIVATED PROTEIN KINASE SNF1
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 337 1224 2005
JRNL REFN ISSN 0006-291X
JRNL PMID 16236260
JRNL DOI 10.1016/J.BBRC.2005.09.181
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.73
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 29853
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) : 0.241
REMARK 3 R VALUE (WORKING SET) : 0.239
REMARK 3 FREE R VALUE : 0.280
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1570
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2123
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.47
REMARK 3 BIN R VALUE (WORKING SET) : 0.2440
REMARK 3 BIN FREE R VALUE SET COUNT : 111
REMARK 3 BIN FREE R VALUE : 0.3090
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3851
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 107
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) : 45.68
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.29000
REMARK 3 B22 (A**2) : -0.20000
REMARK 3 B33 (A**2) : -0.09000
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): 0.285
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.229
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.164
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.431
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.927
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.903
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3931 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5299 ; 1.229 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 463 ; 5.374 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 179 ;37.326 ;23.799
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 744 ;16.530 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;20.439 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 599 ; 0.089 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2870 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1759 ; 0.216 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2642 ; 0.302 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 161 ; 0.177 ; 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): 42 ; 0.132 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.113 ; 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): 2455 ; 0.833 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3820 ; 1.073 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1695 ; 1.562 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1479 ; 2.377 ; 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 48 A 315 6
REMARK 3 1 B 48 B 315 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 1 A (A): 1865 ; NULL ; NULL
REMARK 3 LOOSE THERMAL 1 A (A**2): 1865 ; NULL ; 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 : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 54 B 135
REMARK 3 ORIGIN FOR THE GROUP (A): 41.6802 33.9391 61.5094
REMARK 3 T TENSOR
REMARK 3 T11: -0.2292 T22: 0.0719
REMARK 3 T33: -0.0478 T12: 0.0017
REMARK 3 T13: 0.0391 T23: 0.0196
REMARK 3 L TENSOR
REMARK 3 L11: 3.5795 L22: 2.6166
REMARK 3 L33: 3.0679 L12: 1.3943
REMARK 3 L13: -1.4782 L23: -0.8210
REMARK 3 S TENSOR
REMARK 3 S11: -0.1976 S12: -0.2021 S13: -0.4769
REMARK 3 S21: -0.1034 S22: 0.0369 S23: -0.0580
REMARK 3 S31: 0.0709 S32: -0.6516 S33: 0.1607
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 : B 136 B 315
REMARK 3 ORIGIN FOR THE GROUP (A): 62.0971 47.5390 53.5342
REMARK 3 T TENSOR
REMARK 3 T11: -0.0028 T22: -0.1495
REMARK 3 T33: -0.1235 T12: -0.0352
REMARK 3 T13: -0.0454 T23: 0.0353
REMARK 3 L TENSOR
REMARK 3 L11: 4.1301 L22: 0.5683
REMARK 3 L33: 4.0468 L12: 0.5864
REMARK 3 L13: 2.6527 L23: 0.6676
REMARK 3 S TENSOR
REMARK 3 S11: -0.4019 S12: 0.2667 S13: -0.0500
REMARK 3 S21: -0.1431 S22: 0.1266 S23: -0.0543
REMARK 3 S31: -0.5808 S32: 0.1793 S33: 0.2753
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 54 A 135
REMARK 3 ORIGIN FOR THE GROUP (A): 91.2489 30.8360 72.0716
REMARK 3 T TENSOR
REMARK 3 T11: -0.2328 T22: 0.0534
REMARK 3 T33: 0.0788 T12: -0.0395
REMARK 3 T13: 0.0745 T23: -0.0234
REMARK 3 L TENSOR
REMARK 3 L11: 4.6282 L22: 0.6053
REMARK 3 L33: 3.0452 L12: -1.0560
REMARK 3 L13: -2.0027 L23: 0.7347
REMARK 3 S TENSOR
REMARK 3 S11: -0.1684 S12: 0.3866 S13: -0.4722
REMARK 3 S21: 0.0707 S22: -0.0765 S23: -0.1581
REMARK 3 S31: 0.2286 S32: 0.3359 S33: 0.2449
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 136 A 315
REMARK 3 ORIGIN FOR THE GROUP (A): 70.5534 38.8586 85.6162
REMARK 3 T TENSOR
REMARK 3 T11: -0.0297 T22: -0.1373
REMARK 3 T33: -0.0776 T12: -0.0070
REMARK 3 T13: -0.0190 T23: 0.0137
REMARK 3 L TENSOR
REMARK 3 L11: 2.0409 L22: 1.2655
REMARK 3 L33: 2.0935 L12: -0.2164
REMARK 3 L13: -0.0918 L23: -0.4876
REMARK 3 S TENSOR
REMARK 3 S11: -0.0309 S12: -0.0511 S13: 0.0002
REMARK 3 S21: 0.0698 S22: -0.0481 S23: -0.0824
REMARK 3 S31: -0.1548 S32: -0.0821 S33: 0.0790
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3HYH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUN-09.
REMARK 100 THE DEPOSITION ID IS D_1000053737.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31518
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.06200
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) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.60500
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: SAD
REMARK 200 SOFTWARE USED: SOLVE 2.06
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS (PH 8.5), 25% (W/V)
REMARK 280 PEG3350, AND 300 MM (NH4)2SO4, VAPOR DIFFUSION, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 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
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 35.51400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.84950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.56850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 56.84950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.51400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.56850
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: B
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: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 ASN A 41
REMARK 465 PRO A 42
REMARK 465 LYS A 43
REMARK 465 SER A 44
REMARK 465 SER A 45
REMARK 465 LEU A 46
REMARK 465 ALA A 47
REMARK 465 ASP A 48
REMARK 465 GLY A 49
REMARK 465 ALA A 50
REMARK 465 HIS A 51
REMARK 465 ILE A 52
REMARK 465 GLY A 53
REMARK 465 GLY A 64
REMARK 465 SER A 65
REMARK 465 PHE A 66
REMARK 465 VAL A 90
REMARK 465 LEU A 91
REMARK 465 ALA A 92
REMARK 465 LYS A 93
REMARK 465 SER A 94
REMARK 465 ASP A 95
REMARK 465 ASN A 200
REMARK 465 ILE A 201
REMARK 465 MET A 202
REMARK 465 THR A 203
REMARK 465 ASP A 204
REMARK 465 GLY A 205
REMARK 465 ASN A 206
REMARK 465 PHE A 207
REMARK 465 LEU A 208
REMARK 465 LYS A 209
REMARK 465 THR A 210
REMARK 465 SER A 211
REMARK 465 CYS A 212
REMARK 465 GLY A 213
REMARK 465 SER A 214
REMARK 465 ASN B 41
REMARK 465 PRO B 42
REMARK 465 LYS B 43
REMARK 465 SER B 44
REMARK 465 SER B 45
REMARK 465 LEU B 46
REMARK 465 ALA B 47
REMARK 465 ASP B 48
REMARK 465 GLY B 49
REMARK 465 ALA B 50
REMARK 465 HIS B 51
REMARK 465 ILE B 52
REMARK 465 GLY B 53
REMARK 465 GLY B 64
REMARK 465 SER B 65
REMARK 465 PHE B 66
REMARK 465 GLY B 67
REMARK 465 LEU B 91
REMARK 465 ALA B 92
REMARK 465 LYS B 93
REMARK 465 SER B 94
REMARK 465 ASP B 95
REMARK 465 ASN B 200
REMARK 465 ILE B 201
REMARK 465 MET B 202
REMARK 465 THR B 203
REMARK 465 ASP B 204
REMARK 465 GLY B 205
REMARK 465 ASN B 206
REMARK 465 PHE B 207
REMARK 465 LEU B 208
REMARK 465 LYS B 209
REMARK 465 THR B 210
REMARK 465 SER B 211
REMARK 465 CYS B 212
REMARK 465 GLY B 213
REMARK 465 SER B 214
REMARK 465 GLY B 225
REMARK 465 LYS B 226
REMARK 465 LEU B 227
REMARK 465 TYR B 228
REMARK 465 ALA B 229
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O LYS A 179 OD1 ASN A 182 1.89
REMARK 500 OE1 GLU B 103 O ASP B 195 1.91
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 LYS A 89 C LYS A 89 O 0.218
REMARK 500 VAL B 90 C VAL B 90 O 0.118
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 LYS A 89 CA - C - O ANGL. DEV. = -13.5 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 LYS A 88 102.94 -57.97
REMARK 500 ASP A 177 28.98 -141.72
REMARK 500 ASP A 195 -61.58 -126.17
REMARK 500 LEU A 227 117.50 64.89
REMARK 500 GLN B 56 77.22 60.16
REMARK 500 VAL B 58 -72.81 -97.41
REMARK 500 ASN B 87 -102.72 -149.11
REMARK 500 LYS B 88 -73.90 -21.00
REMARK 500 HIS B 171 32.95 -99.16
REMARK 500 LYS B 172 18.66 51.51
REMARK 500 ARG B 176 -7.04 67.86
REMARK 500 ASP B 195 -49.92 -134.22
REMARK 500 LEU B 287 50.54 -94.64
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3HYH A 41 315 UNP P06782 SNF1_YEAST 41 315
DBREF 3HYH B 41 315 UNP P06782 SNF1_YEAST 41 315
SEQRES 1 A 275 ASN PRO LYS SER SER LEU ALA ASP GLY ALA HIS ILE GLY
SEQRES 2 A 275 ASN TYR GLN ILE VAL LYS THR LEU GLY GLU GLY SER PHE
SEQRES 3 A 275 GLY LYS VAL LYS LEU ALA TYR HIS THR THR THR GLY GLN
SEQRES 4 A 275 LYS VAL ALA LEU LYS ILE ILE ASN LYS LYS VAL LEU ALA
SEQRES 5 A 275 LYS SER ASP MET GLN GLY ARG ILE GLU ARG GLU ILE SER
SEQRES 6 A 275 TYR LEU ARG LEU LEU ARG HIS PRO HIS ILE ILE LYS LEU
SEQRES 7 A 275 TYR ASP VAL ILE LYS SER LYS ASP GLU ILE ILE MET VAL
SEQRES 8 A 275 ILE GLU TYR ALA GLY ASN GLU LEU PHE ASP TYR ILE VAL
SEQRES 9 A 275 GLN ARG ASP LYS MET SER GLU GLN GLU ALA ARG ARG PHE
SEQRES 10 A 275 PHE GLN GLN ILE ILE SER ALA VAL GLU TYR CYS HIS ARG
SEQRES 11 A 275 HIS LYS ILE VAL HIS ARG ASP LEU LYS PRO GLU ASN LEU
SEQRES 12 A 275 LEU LEU ASP GLU HIS LEU ASN VAL LYS ILE ALA ASP PHE
SEQRES 13 A 275 GLY LEU SER ASN ILE MET THR ASP GLY ASN PHE LEU LYS
SEQRES 14 A 275 THR SER CYS GLY SER PRO ASN TYR ALA ALA PRO GLU VAL
SEQRES 15 A 275 ILE SER GLY LYS LEU TYR ALA GLY PRO GLU VAL ASP VAL
SEQRES 16 A 275 TRP SER CYS GLY VAL ILE LEU TYR VAL MET LEU CYS ARG
SEQRES 17 A 275 ARG LEU PRO PHE ASP ASP GLU SER ILE PRO VAL LEU PHE
SEQRES 18 A 275 LYS ASN ILE SER ASN GLY VAL TYR THR LEU PRO LYS PHE
SEQRES 19 A 275 LEU SER PRO GLY ALA ALA GLY LEU ILE LYS ARG MET LEU
SEQRES 20 A 275 ILE VAL ASN PRO LEU ASN ARG ILE SER ILE HIS GLU ILE
SEQRES 21 A 275 MET GLN ASP ASP TRP PHE LYS VAL ASP LEU PRO GLU TYR
SEQRES 22 A 275 LEU LEU
SEQRES 1 B 275 ASN PRO LYS SER SER LEU ALA ASP GLY ALA HIS ILE GLY
SEQRES 2 B 275 ASN TYR GLN ILE VAL LYS THR LEU GLY GLU GLY SER PHE
SEQRES 3 B 275 GLY LYS VAL LYS LEU ALA TYR HIS THR THR THR GLY GLN
SEQRES 4 B 275 LYS VAL ALA LEU LYS ILE ILE ASN LYS LYS VAL LEU ALA
SEQRES 5 B 275 LYS SER ASP MET GLN GLY ARG ILE GLU ARG GLU ILE SER
SEQRES 6 B 275 TYR LEU ARG LEU LEU ARG HIS PRO HIS ILE ILE LYS LEU
SEQRES 7 B 275 TYR ASP VAL ILE LYS SER LYS ASP GLU ILE ILE MET VAL
SEQRES 8 B 275 ILE GLU TYR ALA GLY ASN GLU LEU PHE ASP TYR ILE VAL
SEQRES 9 B 275 GLN ARG ASP LYS MET SER GLU GLN GLU ALA ARG ARG PHE
SEQRES 10 B 275 PHE GLN GLN ILE ILE SER ALA VAL GLU TYR CYS HIS ARG
SEQRES 11 B 275 HIS LYS ILE VAL HIS ARG ASP LEU LYS PRO GLU ASN LEU
SEQRES 12 B 275 LEU LEU ASP GLU HIS LEU ASN VAL LYS ILE ALA ASP PHE
SEQRES 13 B 275 GLY LEU SER ASN ILE MET THR ASP GLY ASN PHE LEU LYS
SEQRES 14 B 275 THR SER CYS GLY SER PRO ASN TYR ALA ALA PRO GLU VAL
SEQRES 15 B 275 ILE SER GLY LYS LEU TYR ALA GLY PRO GLU VAL ASP VAL
SEQRES 16 B 275 TRP SER CYS GLY VAL ILE LEU TYR VAL MET LEU CYS ARG
SEQRES 17 B 275 ARG LEU PRO PHE ASP ASP GLU SER ILE PRO VAL LEU PHE
SEQRES 18 B 275 LYS ASN ILE SER ASN GLY VAL TYR THR LEU PRO LYS PHE
SEQRES 19 B 275 LEU SER PRO GLY ALA ALA GLY LEU ILE LYS ARG MET LEU
SEQRES 20 B 275 ILE VAL ASN PRO LEU ASN ARG ILE SER ILE HIS GLU ILE
SEQRES 21 B 275 MET GLN ASP ASP TRP PHE LYS VAL ASP LEU PRO GLU TYR
SEQRES 22 B 275 LEU LEU
FORMUL 3 HOH *107(H2 O)
HELIX 1 1 MET A 96 LEU A 110 1 15
HELIX 2 2 LEU A 139 ARG A 146 1 8
HELIX 3 3 SER A 150 HIS A 171 1 22
HELIX 4 4 ALA A 219 SER A 224 1 6
HELIX 5 5 PRO A 231 ARG A 248 1 18
HELIX 6 6 SER A 256 GLY A 267 1 12
HELIX 7 7 SER A 276 LEU A 287 1 12
HELIX 8 8 ASN A 290 ARG A 294 5 5
HELIX 9 9 SER A 296 ASP A 303 1 8
HELIX 10 10 ASP A 303 VAL A 308 1 6
HELIX 11 11 PRO A 311 LEU A 315 5 5
HELIX 12 12 MET B 96 LEU B 110 1 15
HELIX 13 13 LEU B 139 GLN B 145 1 7
HELIX 14 14 SER B 150 HIS B 171 1 22
HELIX 15 15 LYS B 179 GLU B 181 5 3
HELIX 16 16 ALA B 219 SER B 224 1 6
HELIX 17 17 PRO B 231 ARG B 248 1 18
HELIX 18 18 SER B 256 GLY B 267 1 12
HELIX 19 19 SER B 276 LEU B 287 1 12
HELIX 20 20 SER B 296 GLN B 302 1 7
HELIX 21 21 ASP B 303 VAL B 308 1 6
HELIX 22 22 PRO B 311 LEU B 315 5 5
SHEET 1 A 5 GLN A 56 GLY A 62 0
SHEET 2 A 5 VAL A 69 TYR A 73 -1 O LEU A 71 N LYS A 59
SHEET 3 A 5 LYS A 80 ASN A 87 -1 O VAL A 81 N ALA A 72
SHEET 4 A 5 GLU A 127 GLU A 133 -1 O ILE A 132 N ALA A 82
SHEET 5 A 5 LEU A 118 LYS A 123 -1 N ILE A 122 O ILE A 129
SHEET 1 B 3 ASN A 137 GLU A 138 0
SHEET 2 B 3 LEU A 183 LEU A 185 -1 O LEU A 185 N ASN A 137
SHEET 3 B 3 VAL A 191 ILE A 193 -1 O LYS A 192 N LEU A 184
SHEET 1 C 4 VAL B 69 TYR B 73 0
SHEET 2 C 4 LYS B 80 ILE B 86 -1 O VAL B 81 N ALA B 72
SHEET 3 C 4 ILE B 128 GLU B 133 -1 O ILE B 132 N ALA B 82
SHEET 4 C 4 LEU B 118 LYS B 123 -1 N ILE B 122 O ILE B 129
SHEET 1 D 3 ASN B 137 GLU B 138 0
SHEET 2 D 3 LEU B 183 LEU B 185 -1 O LEU B 185 N ASN B 137
SHEET 3 D 3 VAL B 191 ILE B 193 -1 O LYS B 192 N LEU B 184
CRYST1 71.028 75.137 113.699 90.00 90.00 90.00 P 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 0.014079 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013309 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008795 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
