HEADER TRANSFERASE 29-MAY-08 3DAE
TITLE CRYSTAL STRUCTURE OF PHOSPHORYLATED SNF1 KINASE DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBON CATABOLITE-DEREPRESSING PROTEIN KINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: KINASE DOMAIN, UNP RESIDUE 41-315;
COMPND 5 SYNONYM: SNF1;
COMPND 6 EC: 2.7.11.1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: SNF1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21B
KEYWDS KINASE, AMPK, SNF1, ATP-BINDING, CARBOHYDRATE METABOLISM, MEMBRANE,
KEYWDS 2 NUCLEOTIDE-BINDING, NUCLEUS, PHOSPHOPROTEIN, SERINE/THREONINE-
KEYWDS 3 PROTEIN KINASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.-S.ZHENG,L.CHEN,Z.-H.JIAO,J.-W.WU
REVDAT 4 01-NOV-23 3DAE 1 SEQADV
REVDAT 3 30-JUN-09 3DAE 1 JRNL
REVDAT 2 09-JUN-09 3DAE 1 JRNL
REVDAT 1 02-JUN-09 3DAE 0
JRNL AUTH L.CHEN,Z.-H.JIAO,L.-S.ZHENG,Y.-Y.ZHANG,S.-T.XIE,Z.-X.WANG,
JRNL AUTH 2 J.-W.WU
JRNL TITL STRUCTURAL INSIGHT INTO THE AUTOINHIBITION MECHANISM OF
JRNL TITL 2 AMP-ACTIVATED PROTEIN KINASE
JRNL REF NATURE V. 459 1146 2009
JRNL REFN ISSN 0028-0836
JRNL PMID 19474788
JRNL DOI 10.1038/NATURE08075
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.19
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 14082
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.229
REMARK 3 R VALUE (WORKING SET) : 0.227
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 706
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 47.1980 - 4.9550 1.00 2802 144 0.2380 0.2880
REMARK 3 2 4.9550 - 3.9340 1.00 2693 132 0.1820 0.1880
REMARK 3 3 3.9340 - 3.4360 1.00 2654 142 0.2040 0.2640
REMARK 3 4 3.4360 - 3.1220 1.00 2639 139 0.2530 0.2750
REMARK 3 5 3.1220 - 2.8980 1.00 2588 149 0.2850 0.3460
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.32
REMARK 3 B_SOL : 30.14
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 50.35
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.73
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 9.18200
REMARK 3 B22 (A**2) : 6.52000
REMARK 3 B33 (A**2) : -1.48300
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.013 4080
REMARK 3 ANGLE : 1.419 5512
REMARK 3 CHIRALITY : 0.092 619
REMARK 3 PLANARITY : 0.008 697
REMARK 3 DIHEDRAL : 18.777 1516
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3DAE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-JUN-08.
REMARK 100 THE DEPOSITION ID IS D_1000047792.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-JUN-07
REMARK 200 TEMPERATURE (KELVIN) : 150
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BSRF
REMARK 200 BEAMLINE : 3W1A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00001
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14122
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.899
REMARK 200 RESOLUTION RANGE LOW (A) : 47.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.08700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.20
REMARK 200 R MERGE FOR SHELL (I) : 0.38200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.290
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 2EUE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS PH 8.5, 3.2-3.6M NH4AC, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 37.30350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.46000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.18500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 56.46000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.30350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.18500
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 300 REMARK: THE DEPOSITORS THINK THE SOFTWARE PREDICTED QUATERNARY
REMARK 300 STRUCTURE IS NOT CONSISTENT WITH BIOCHEMICAL DATA AND MONOMER IS
REMARK 300 THE BIOLOGICAL UNIT. THE DIMER FORMATION MAY BE DUE TO CRYSTAL
REMARK 300 PACKING.
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: 1560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24680 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 MET A 40
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 LYS A 93
REMARK 465 SER A 94
REMARK 465 ASP A 95
REMARK 465 MET A 96
REMARK 465 GLY A 197
REMARK 465 LEU A 198
REMARK 465 SER A 199
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 GLU A 316
REMARK 465 HIS A 317
REMARK 465 HIS A 318
REMARK 465 HIS A 319
REMARK 465 HIS A 320
REMARK 465 HIS A 321
REMARK 465 HIS A 322
REMARK 465 MET B 40
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 LYS B 93
REMARK 465 SER B 94
REMARK 465 ASP B 95
REMARK 465 MET B 96
REMARK 465 GLY B 197
REMARK 465 LEU B 198
REMARK 465 SER B 199
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 GLU B 316
REMARK 465 HIS B 317
REMARK 465 HIS B 318
REMARK 465 HIS B 319
REMARK 465 HIS B 320
REMARK 465 HIS B 321
REMARK 465 HIS B 322
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 226 CG CD CE NZ
REMARK 470 LYS B 226 CG CD CE NZ
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 OD2 ASP B 186 N GLU B 187 1.78
REMARK 500 O HOH A 364 O HOH A 405 1.81
REMARK 500 O ASP A 195 O HOH A 383 1.83
REMARK 500 NH2 ARG B 156 O HOH B 393 1.84
REMARK 500 O LEU A 91 O HOH A 381 1.93
REMARK 500 N GLY A 136 O HOH A 355 1.93
REMARK 500 O HOH A 340 O HOH A 373 1.95
REMARK 500 O SER A 124 O HOH A 388 1.97
REMARK 500 CE LYS A 117 O HOH A 358 1.97
REMARK 500 NH2 ARG A 102 O HOH A 362 1.97
REMARK 500 CD2 HIS B 188 O HOH B 362 1.99
REMARK 500 O HOH A 398 O HOH B 400 2.00
REMARK 500 CD LYS A 88 O HOH A 392 2.00
REMARK 500 OD1 ASP B 253 O HOH B 365 2.00
REMARK 500 OD1 ASP B 147 O HOH B 377 2.02
REMARK 500 O HOH A 410 O HOH A 411 2.03
REMARK 500 O LYS B 88 O HOH B 335 2.04
REMARK 500 O LEU A 227 O HOH A 347 2.05
REMARK 500 NZ LYS B 125 O HOH B 387 2.06
REMARK 500 O LEU A 315 O HOH A 390 2.08
REMARK 500 O ALA A 194 O HOH A 383 2.08
REMARK 500 OH TYR A 228 O HOH A 393 2.08
REMARK 500 OE2 GLU B 151 O HOH B 366 2.09
REMARK 500 CA ASP A 195 O HOH A 383 2.11
REMARK 500 O GLY A 278 O HOH A 344 2.11
REMARK 500 CD2 TYR B 106 O HOH B 350 2.14
REMARK 500 OE2 GLU A 151 O HOH A 351 2.14
REMARK 500 CB LYS A 88 O HOH A 392 2.16
REMARK 500 CE2 PHE B 140 O HOH B 386 2.18
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 GLY A 213 C GLY A 213 O 0.109
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 B 215 C - N - CD ANGL. DEV. = -16.6 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 ALA A 50 28.64 37.77
REMARK 500 HIS A 51 157.03 160.74
REMARK 500 ILE A 52 73.93 -174.00
REMARK 500 ASN A 54 -23.02 102.70
REMARK 500 SER A 65 -89.82 -50.63
REMARK 500 LYS A 68 99.71 44.70
REMARK 500 ASN A 87 -157.11 -163.70
REMARK 500 VAL A 90 -21.64 -39.21
REMARK 500 ASP A 126 -67.93 -120.68
REMARK 500 ASP A 147 -147.27 -81.44
REMARK 500 ARG A 176 -19.80 81.75
REMARK 500 LYS A 179 157.41 179.81
REMARK 500 GLU A 181 -14.00 108.83
REMARK 500 ASP A 195 -93.42 -94.07
REMARK 500 SER A 224 -101.12 -83.70
REMARK 500 ASP A 253 116.69 -19.20
REMARK 500 LEU A 287 60.25 -103.08
REMARK 500 HIS B 51 156.45 -46.43
REMARK 500 ILE B 52 84.65 -165.93
REMARK 500 ASN B 54 -14.97 87.76
REMARK 500 GLU B 63 -130.22 -150.23
REMARK 500 SER B 65 -96.00 -89.62
REMARK 500 LYS B 68 111.02 41.38
REMARK 500 ASN B 87 -149.74 -149.42
REMARK 500 VAL B 90 -6.35 -52.43
REMARK 500 ASP B 126 -70.18 -93.17
REMARK 500 LYS B 172 20.70 49.14
REMARK 500 ARG B 176 -11.40 84.49
REMARK 500 ASP B 177 36.82 -148.52
REMARK 500 GLU B 181 -8.57 101.19
REMARK 500 ASP B 186 -131.17 -75.89
REMARK 500 ASP B 195 -97.19 -95.64
REMARK 500 LYS B 226 -16.28 -23.14
REMARK 500 LEU B 227 -158.05 65.44
REMARK 500 TYR B 228 110.65 -15.38
REMARK 500 ASP B 253 113.71 -1.58
REMARK 500 LEU B 287 51.01 -93.38
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 ASP A 48 GLY A 49 -102.13
REMARK 500 HIS A 51 ILE A 52 -142.52
REMARK 500 GLY A 213 SER A 214 -145.27
REMARK 500 GLY B 213 SER B 214 -106.28
REMARK 500 LEU B 227 TYR B 228 -120.86
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3DAE A 41 315 UNP P06782 SNF1_YEAST 41 315
DBREF 3DAE B 41 315 UNP P06782 SNF1_YEAST 41 315
SEQADV 3DAE MET A 40 UNP P06782 INITIATING METHIONINE
SEQADV 3DAE GLU A 316 UNP P06782 EXPRESSION TAG
SEQADV 3DAE HIS A 317 UNP P06782 EXPRESSION TAG
SEQADV 3DAE HIS A 318 UNP P06782 EXPRESSION TAG
SEQADV 3DAE HIS A 319 UNP P06782 EXPRESSION TAG
SEQADV 3DAE HIS A 320 UNP P06782 EXPRESSION TAG
SEQADV 3DAE HIS A 321 UNP P06782 EXPRESSION TAG
SEQADV 3DAE HIS A 322 UNP P06782 EXPRESSION TAG
SEQADV 3DAE MET B 40 UNP P06782 INITIATING METHIONINE
SEQADV 3DAE GLU B 316 UNP P06782 EXPRESSION TAG
SEQADV 3DAE HIS B 317 UNP P06782 EXPRESSION TAG
SEQADV 3DAE HIS B 318 UNP P06782 EXPRESSION TAG
SEQADV 3DAE HIS B 319 UNP P06782 EXPRESSION TAG
SEQADV 3DAE HIS B 320 UNP P06782 EXPRESSION TAG
SEQADV 3DAE HIS B 321 UNP P06782 EXPRESSION TAG
SEQADV 3DAE HIS B 322 UNP P06782 EXPRESSION TAG
SEQRES 1 A 283 MET ASN PRO LYS SER SER LEU ALA ASP GLY ALA HIS ILE
SEQRES 2 A 283 GLY ASN TYR GLN ILE VAL LYS THR LEU GLY GLU GLY SER
SEQRES 3 A 283 PHE GLY LYS VAL LYS LEU ALA TYR HIS THR THR THR GLY
SEQRES 4 A 283 GLN LYS VAL ALA LEU LYS ILE ILE ASN LYS LYS VAL LEU
SEQRES 5 A 283 ALA LYS SER ASP MET GLN GLY ARG ILE GLU ARG GLU ILE
SEQRES 6 A 283 SER TYR LEU ARG LEU LEU ARG HIS PRO HIS ILE ILE LYS
SEQRES 7 A 283 LEU TYR ASP VAL ILE LYS SER LYS ASP GLU ILE ILE MET
SEQRES 8 A 283 VAL ILE GLU TYR ALA GLY ASN GLU LEU PHE ASP TYR ILE
SEQRES 9 A 283 VAL GLN ARG ASP LYS MET SER GLU GLN GLU ALA ARG ARG
SEQRES 10 A 283 PHE PHE GLN GLN ILE ILE SER ALA VAL GLU TYR CYS HIS
SEQRES 11 A 283 ARG HIS LYS ILE VAL HIS ARG ASP LEU LYS PRO GLU ASN
SEQRES 12 A 283 LEU LEU LEU ASP GLU HIS LEU ASN VAL LYS ILE ALA ASP
SEQRES 13 A 283 PHE GLY LEU SER ASN ILE MET THR ASP GLY ASN PHE LEU
SEQRES 14 A 283 LYS THR SER CYS GLY SER PRO ASN TYR ALA ALA PRO GLU
SEQRES 15 A 283 VAL ILE SER GLY LYS LEU TYR ALA GLY PRO GLU VAL ASP
SEQRES 16 A 283 VAL TRP SER CYS GLY VAL ILE LEU TYR VAL MET LEU CYS
SEQRES 17 A 283 ARG ARG LEU PRO PHE ASP ASP GLU SER ILE PRO VAL LEU
SEQRES 18 A 283 PHE LYS ASN ILE SER ASN GLY VAL TYR THR LEU PRO LYS
SEQRES 19 A 283 PHE LEU SER PRO GLY ALA ALA GLY LEU ILE LYS ARG MET
SEQRES 20 A 283 LEU ILE VAL ASN PRO LEU ASN ARG ILE SER ILE HIS GLU
SEQRES 21 A 283 ILE MET GLN ASP ASP TRP PHE LYS VAL ASP LEU PRO GLU
SEQRES 22 A 283 TYR LEU LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 283 MET ASN PRO LYS SER SER LEU ALA ASP GLY ALA HIS ILE
SEQRES 2 B 283 GLY ASN TYR GLN ILE VAL LYS THR LEU GLY GLU GLY SER
SEQRES 3 B 283 PHE GLY LYS VAL LYS LEU ALA TYR HIS THR THR THR GLY
SEQRES 4 B 283 GLN LYS VAL ALA LEU LYS ILE ILE ASN LYS LYS VAL LEU
SEQRES 5 B 283 ALA LYS SER ASP MET GLN GLY ARG ILE GLU ARG GLU ILE
SEQRES 6 B 283 SER TYR LEU ARG LEU LEU ARG HIS PRO HIS ILE ILE LYS
SEQRES 7 B 283 LEU TYR ASP VAL ILE LYS SER LYS ASP GLU ILE ILE MET
SEQRES 8 B 283 VAL ILE GLU TYR ALA GLY ASN GLU LEU PHE ASP TYR ILE
SEQRES 9 B 283 VAL GLN ARG ASP LYS MET SER GLU GLN GLU ALA ARG ARG
SEQRES 10 B 283 PHE PHE GLN GLN ILE ILE SER ALA VAL GLU TYR CYS HIS
SEQRES 11 B 283 ARG HIS LYS ILE VAL HIS ARG ASP LEU LYS PRO GLU ASN
SEQRES 12 B 283 LEU LEU LEU ASP GLU HIS LEU ASN VAL LYS ILE ALA ASP
SEQRES 13 B 283 PHE GLY LEU SER ASN ILE MET THR ASP GLY ASN PHE LEU
SEQRES 14 B 283 LYS THR SER CYS GLY SER PRO ASN TYR ALA ALA PRO GLU
SEQRES 15 B 283 VAL ILE SER GLY LYS LEU TYR ALA GLY PRO GLU VAL ASP
SEQRES 16 B 283 VAL TRP SER CYS GLY VAL ILE LEU TYR VAL MET LEU CYS
SEQRES 17 B 283 ARG ARG LEU PRO PHE ASP ASP GLU SER ILE PRO VAL LEU
SEQRES 18 B 283 PHE LYS ASN ILE SER ASN GLY VAL TYR THR LEU PRO LYS
SEQRES 19 B 283 PHE LEU SER PRO GLY ALA ALA GLY LEU ILE LYS ARG MET
SEQRES 20 B 283 LEU ILE VAL ASN PRO LEU ASN ARG ILE SER ILE HIS GLU
SEQRES 21 B 283 ILE MET GLN ASP ASP TRP PHE LYS VAL ASP LEU PRO GLU
SEQRES 22 B 283 TYR LEU LEU GLU HIS HIS HIS HIS HIS HIS
FORMUL 3 HOH *187(H2 O)
HELIX 1 1 ASN A 87 ALA A 92 5 6
HELIX 2 2 GLN A 97 LEU A 110 1 14
HELIX 3 3 LEU A 139 ARG A 146 1 8
HELIX 4 4 SER A 150 HIS A 171 1 22
HELIX 5 5 SER A 214 ALA A 218 5 5
HELIX 6 6 ALA A 219 SER A 224 1 6
HELIX 7 7 PRO A 231 ARG A 248 1 18
HELIX 8 8 SER A 256 ASN A 266 1 11
HELIX 9 9 SER A 276 LEU A 287 1 12
HELIX 10 10 SER A 296 MET A 301 1 6
HELIX 11 11 ASP A 303 VAL A 308 1 6
HELIX 12 12 ASN B 87 ALA B 92 5 6
HELIX 13 13 GLN B 97 LEU B 110 1 14
HELIX 14 14 LEU B 139 GLN B 145 1 7
HELIX 15 15 SER B 150 ARG B 170 1 21
HELIX 16 16 ALA B 219 GLY B 225 1 7
HELIX 17 17 PRO B 231 ARG B 248 1 18
HELIX 18 18 SER B 256 ASN B 266 1 11
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 LYS A 59 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 ILE A 86 -1 O VAL A 81 N ALA A 72
SHEET 4 A 5 ILE A 128 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 5 TYR B 55 GLY B 62 0
SHEET 2 C 5 VAL B 69 HIS B 74 -1 O LEU B 71 N VAL B 58
SHEET 3 C 5 LYS B 80 ILE B 86 -1 O VAL B 81 N ALA B 72
SHEET 4 C 5 ILE B 128 GLU B 133 -1 O ILE B 132 N ALA B 82
SHEET 5 C 5 LEU B 118 LYS B 123 -1 N ASP B 120 O VAL B 131
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 74.607 72.370 112.920 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 0.013404 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013818 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008856 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
