HEADER TRANSFERASE 20-AUG-07 2V92
TITLE CRYSTAL STRUCTURE OF THE REGULATORY FRAGMENT OF MAMMALIAN
TITLE 2 AMPK IN COMPLEXES WITH ATP-AMP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC
COMPND 3 SUBUNIT ALPHA-1;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: RESIDUES 396-548;
COMPND 6 SYNONYM: AMPK ALPHA-1 CHAIN, AMP-ACTIVATED PROTEIN KINASE;
COMPND 7 EC: 2.7.11.1;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT GAMMA-1;
COMPND 11 CHAIN: E;
COMPND 12 SYNONYM: AMPK GAMMA-1 CHAIN, AMPKG, AMP-ACTIVATED PROTEIN
COMPND 13 KINASE;
COMPND 14 ENGINEERED: YES;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT BETA-2;
COMPND 17 CHAIN: B;
COMPND 18 FRAGMENT: RESIDUES 187-272;
COMPND 19 SYNONYM: AMPK BETA-2 CHAIN, AMP-ACTIVATED PROTEIN KINASE;
COMPND 20 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 9 ORGANISM_COMMON: RAT;
SOURCE 10 ORGANISM_TAXID: 10116;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 13 MOL_ID: 3;
SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 15 ORGANISM_COMMON: HUMAN;
SOURCE 16 ORGANISM_TAXID: 9606;
SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PHOSPHORYLATION, NUCLEOTIDE-BINDING,
KEYWDS 2 SERINE/THREONINE-PROTEIN KINASE, ATP-BINDING, KINASE,
KEYWDS 3 MAGNESIUM, CBS DOMAIN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.XIAO,R.HEATH,P.SAIU,F.C.LEIPER,P.LEONE,C.JING,P.A.WALKER,
AUTHOR 2 L.HAIRE,J.F.ECCLESTON,C.T.DAVIS,S.R.MARTIN,D.CARLING,
AUTHOR 3 S.J.GAMBLIN
REVDAT 3 24-FEB-09 2V92 1 VERSN
REVDAT 2 02-OCT-07 2V92 1 JRNL
REVDAT 1 25-SEP-07 2V92 0
JRNL AUTH B.XIAO,R.HEATH,P.SAIU,F.C.LEIPER,P.LEONE,C.JING,
JRNL AUTH 2 P.A.WALKER,L.HAIRE,J.F.ECCLESTON,C.T.DAVIS,
JRNL AUTH 3 S.R.MARTIN,D.CARLING,S.J.GAMBLIN
JRNL TITL STRUCTURAL BASIS FOR AMP BINDING TO MAMMALIAN AMP-
JRNL TITL 2 ACTIVATED PROTEIN KINASE
JRNL REF NATURE V. 449 496 2007
JRNL REFN ISSN 0028-0836
JRNL PMID 17851531
JRNL DOI 10.1038/NATURE06161
REMARK 2
REMARK 2 RESOLUTION. 2.40 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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 30415
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 REFLECTION IN BIN (WORKING SET) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE SET COUNT : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3878
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 85
REMARK 3 SOLVENT ATOMS : 361
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL
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): NULL ; NULL ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED 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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 2V92 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-AUG-07.
REMARK 100 THE PDBE ID CODE IS EBI-33523.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30415
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.40
REMARK 200 RESOLUTION RANGE LOW (A) : 20.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 9.8
REMARK 200 R MERGE (I) : 0.10
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.80
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 24.48050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 63.62350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 60.51600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 63.62350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.48050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 60.51600
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 GENERATING THE BIOMOLECULE
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 7110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.4 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 GLY A 392
REMARK 465 ILE A 470
REMARK 465 THR A 471
REMARK 465 GLU A 472
REMARK 465 ALA A 473
REMARK 465 LYS A 474
REMARK 465 SER A 475
REMARK 465 GLY A 476
REMARK 465 THR A 477
REMARK 465 ALA A 478
REMARK 465 THR A 479
REMARK 465 PRO A 480
REMARK 465 GLN A 481
REMARK 465 ARG A 482
REMARK 465 SER A 483
REMARK 465 GLY A 484
REMARK 465 SER A 485
REMARK 465 ILE A 486
REMARK 465 SER A 487
REMARK 465 ASN A 488
REMARK 465 TYR A 489
REMARK 465 ARG A 490
REMARK 465 SER A 491
REMARK 465 CYS A 492
REMARK 465 GLN A 493
REMARK 465 ARG A 494
REMARK 465 SER A 495
REMARK 465 ASP A 496
REMARK 465 SER A 497
REMARK 465 ASP A 498
REMARK 465 ALA A 499
REMARK 465 GLU A 500
REMARK 465 ALA A 501
REMARK 465 GLN A 502
REMARK 465 GLY A 503
REMARK 465 LYS A 504
REMARK 465 PRO A 505
REMARK 465 SER A 506
REMARK 465 GLU A 507
REMARK 465 VAL A 508
REMARK 465 SER A 509
REMARK 465 LEU A 510
REMARK 465 THR A 511
REMARK 465 SER A 512
REMARK 465 SER A 513
REMARK 465 VAL A 514
REMARK 465 THR A 515
REMARK 465 SER A 516
REMARK 465 LEU A 517
REMARK 465 ASP A 518
REMARK 465 SER A 519
REMARK 465 SER A 520
REMARK 465 PRO A 521
REMARK 465 VAL A 522
REMARK 465 ASP A 523
REMARK 465 MET B 186
REMARK 465 GLY B 187
REMARK 465 PRO B 188
REMARK 465 TYR B 189
REMARK 465 ILE B 223
REMARK 465 SER B 224
REMARK 465 CYS B 225
REMARK 465 ASP B 226
REMARK 465 PRO B 227
REMARK 465 ALA B 228
REMARK 465 LEU B 229
REMARK 465 LEU B 230
REMARK 465 PRO B 231
REMARK 465 GLU B 232
REMARK 465 MET E 1
REMARK 465 GLU E 2
REMARK 465 SER E 3
REMARK 465 VAL E 4
REMARK 465 ALA E 5
REMARK 465 ALA E 6
REMARK 465 GLU E 7
REMARK 465 SER E 8
REMARK 465 ALA E 9
REMARK 465 PRO E 10
REMARK 465 ALA E 11
REMARK 465 PRO E 12
REMARK 465 GLU E 13
REMARK 465 ASN E 14
REMARK 465 GLU E 15
REMARK 465 HIS E 16
REMARK 465 SER E 17
REMARK 465 GLN E 18
REMARK 465 GLU E 19
REMARK 465 THR E 20
REMARK 465 PRO E 21
REMARK 465 GLU E 22
REMARK 465 GLU E 327
REMARK 465 LYS E 328
REMARK 465 LYS E 329
REMARK 465 PRO E 330
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 B 203 CB CG CD CE NZ
REMARK 470 SER B 204 OG
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 E 176 - OG1 THR E 180 2.04
REMARK 500 O ILE E 179 - N GLU E 181 2.04
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 LEU E 40 CA - CB - CG ANGL. DEV. = 14.0 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 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 PRO A 526 -60.23 -93.05
REMARK 500 ARG A 527 -149.73 56.91
REMARK 500 GLN B 191 130.03 69.32
REMARK 500 GLU B 199 161.66 58.49
REMARK 500 GLU B 200 -156.64 55.71
REMARK 500 ARG B 201 -54.39 58.15
REMARK 500 SER B 204 128.78 71.91
REMARK 500 LEU B 208 -71.77 -63.03
REMARK 500 HIS B 211 8.93 -155.22
REMARK 500 LYS B 219 -72.75 -73.95
REMARK 500 ASP B 220 16.91 53.60
REMARK 500 HIS B 235 -84.74 -71.59
REMARK 500 ASN B 239 -0.93 76.69
REMARK 500 LYS B 260 -104.25 45.59
REMARK 500 SER E 25 -29.51 71.17
REMARK 500 SER E 26 138.96 60.99
REMARK 500 ALA E 70 128.64 61.63
REMARK 500 LEU E 121 38.41 -79.55
REMARK 500 GLN E 122 -99.22 -49.86
REMARK 500 SER E 124 106.90 -47.06
REMARK 500 THR E 180 59.52 -45.32
REMARK 500 PRO E 183 99.23 -68.38
REMARK 500 ARG E 223 71.51 55.76
REMARK 500 TYR E 254 -0.38 59.97
REMARK 500 HIS E 267 7.38 -68.18
REMARK 500 HIS E 270 165.02 117.87
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 ARG A 527 PRO A 528 -142.61
REMARK 500 PHE E 182 PRO E 183 134.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 PHE E 182 19.5 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE)
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP E1327
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP E1328
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP E1329
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2V8Q RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE REGULATORY FRAGMENT
REMARK 900 OF MAMMALIAN AMPK IN COMPLEXES WITH AMP
REMARK 900 RELATED ID: 2F15 RELATED DB: PDB
REMARK 900 GLYCOGEN-BINDING DOMAIN OF THE AMP-ACTIVATED
REMARK 900 PROTEIN KINASEBETA2 SUBUNIT
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE FIRST FOUR RESIDUES (GSMA) OF THE SEQUENCE OF CHAIN A
REMARK 999 ARE GENERATED FROM THE POST HIS-TAG CLEAVAGE
REMARK 999 THE FIRST RESIDUES (M) OF THE SEQUENCE OF CHAIN B IS
REMARK 999 GENERATED BY THE WAY IT WAS CLONED INTO THE VECTOR
DBREF 2V92 A 392 395 PDB 2V92 2V92 392 395
DBREF 2V92 A 396 548 UNP P54645 AAPK1_RAT 396 548
DBREF 2V92 E 1 330 UNP P80385 AAKG1_RAT 1 330
DBREF 2V92 B 186 186 PDB 2V92 2V92 186 186
DBREF 2V92 B 187 272 UNP O43741 AAKB2_HUMAN 187 272
SEQRES 1 A 157 GLY SER MET ALA TRP HIS LEU GLY ILE ARG SER GLN SER
SEQRES 2 A 157 ARG PRO ASN ASP ILE MET ALA GLU VAL CYS ARG ALA ILE
SEQRES 3 A 157 LYS GLN LEU ASP TYR GLU TRP LYS VAL VAL ASN PRO TYR
SEQRES 4 A 157 TYR LEU ARG VAL ARG ARG LYS ASN PRO VAL THR SER THR
SEQRES 5 A 157 PHE SER LYS MET SER LEU GLN LEU TYR GLN VAL ASP SER
SEQRES 6 A 157 ARG THR TYR LEU LEU ASP PHE ARG SER ILE ASP ASP GLU
SEQRES 7 A 157 ILE THR GLU ALA LYS SER GLY THR ALA THR PRO GLN ARG
SEQRES 8 A 157 SER GLY SER ILE SER ASN TYR ARG SER CYS GLN ARG SER
SEQRES 9 A 157 ASP SER ASP ALA GLU ALA GLN GLY LYS PRO SER GLU VAL
SEQRES 10 A 157 SER LEU THR SER SER VAL THR SER LEU ASP SER SER PRO
SEQRES 11 A 157 VAL ASP VAL ALA PRO ARG PRO GLY SER HIS THR ILE GLU
SEQRES 12 A 157 PHE PHE GLU MET CYS ALA ASN LEU ILE LYS ILE LEU ALA
SEQRES 13 A 157 GLN
SEQRES 1 B 87 MET GLY PRO TYR GLY GLN GLU MET TYR ALA PHE ARG SER
SEQRES 2 B 87 GLU GLU ARG PHE LYS SER PRO PRO ILE LEU PRO PRO HIS
SEQRES 3 B 87 LEU LEU GLN VAL ILE LEU ASN LYS ASP THR ASN ILE SER
SEQRES 4 B 87 CYS ASP PRO ALA LEU LEU PRO GLU PRO ASN HIS VAL MET
SEQRES 5 B 87 LEU ASN HIS LEU TYR ALA LEU SER ILE LYS ASP SER VAL
SEQRES 6 B 87 MET VAL LEU SER ALA THR HIS ARG TYR LYS LYS LYS TYR
SEQRES 7 B 87 VAL THR THR LEU LEU TYR LYS PRO ILE
SEQRES 1 E 330 MET GLU SER VAL ALA ALA GLU SER ALA PRO ALA PRO GLU
SEQRES 2 E 330 ASN GLU HIS SER GLN GLU THR PRO GLU SER ASN SER SER
SEQRES 3 E 330 VAL TYR THR THR PHE MET LYS SER HIS ARG CYS TYR ASP
SEQRES 4 E 330 LEU ILE PRO THR SER SER LYS LEU VAL VAL PHE ASP THR
SEQRES 5 E 330 SER LEU GLN VAL LYS LYS ALA PHE PHE ALA LEU VAL THR
SEQRES 6 E 330 ASN GLY VAL ARG ALA ALA PRO LEU TRP ASP SER LYS LYS
SEQRES 7 E 330 GLN SER PHE VAL GLY MET LEU THR ILE THR ASP PHE ILE
SEQRES 8 E 330 ASN ILE LEU HIS ARG TYR TYR LYS SER ALA LEU VAL GLN
SEQRES 9 E 330 ILE TYR GLU LEU GLU GLU HIS LYS ILE GLU THR TRP ARG
SEQRES 10 E 330 GLU VAL TYR LEU GLN ASP SER PHE LYS PRO LEU VAL CYS
SEQRES 11 E 330 ILE SER PRO ASN ALA SER LEU PHE ASP ALA VAL SER SER
SEQRES 12 E 330 LEU ILE ARG ASN LYS ILE HIS ARG LEU PRO VAL ILE ASP
SEQRES 13 E 330 PRO GLU SER GLY ASN THR LEU TYR ILE LEU THR HIS LYS
SEQRES 14 E 330 ARG ILE LEU LYS PHE LEU LYS LEU PHE ILE THR GLU PHE
SEQRES 15 E 330 PRO LYS PRO GLU PHE MET SER LYS SER LEU GLU GLU LEU
SEQRES 16 E 330 GLN ILE GLY THR TYR ALA ASN ILE ALA MET VAL ARG THR
SEQRES 17 E 330 THR THR PRO VAL TYR VAL ALA LEU GLY ILE PHE VAL GLN
SEQRES 18 E 330 HIS ARG VAL SER ALA LEU PRO VAL VAL ASP GLU LYS GLY
SEQRES 19 E 330 ARG VAL VAL ASP ILE TYR SER LYS PHE ASP VAL ILE ASN
SEQRES 20 E 330 LEU ALA ALA GLU LYS THR TYR ASN ASN LEU ASP VAL SER
SEQRES 21 E 330 VAL THR LYS ALA LEU GLN HIS ARG SER HIS TYR PHE GLU
SEQRES 22 E 330 GLY VAL LEU LYS CYS TYR LEU HIS GLU THR LEU GLU ALA
SEQRES 23 E 330 ILE ILE ASN ARG LEU VAL GLU ALA GLU VAL HIS ARG LEU
SEQRES 24 E 330 VAL VAL VAL ASP GLU HIS ASP VAL VAL LYS GLY ILE VAL
SEQRES 25 E 330 SER LEU SER ASP ILE LEU GLN ALA LEU VAL LEU THR GLY
SEQRES 26 E 330 GLY GLU LYS LYS PRO
HET ATP E1327 31
HET ATP E1328 31
HET AMP E1329 23
HETNAM AMP ADENOSINE MONOPHOSPHATE
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
FORMUL 4 AMP C10 H14 N5 O7 P
FORMUL 5 ATP 2(C10 H16 N5 O13 P3)
FORMUL 6 HOH *361(H2 O1)
HELIX 1 1 ARG A 405 LEU A 420 1 16
HELIX 2 2 SER A 530 ILE A 545 1 16
HELIX 3 3 SER E 26 SER E 34 1 9
HELIX 4 4 CYS E 37 ILE E 41 5 5
HELIX 5 5 GLN E 55 GLY E 67 1 13
HELIX 6 6 THR E 86 LEU E 102 1 17
HELIX 7 7 TYR E 106 HIS E 111 5 6
HELIX 8 8 LYS E 112 LEU E 121 1 10
HELIX 9 9 SER E 136 LYS E 148 1 13
HELIX 10 10 THR E 167 THR E 180 1 14
HELIX 11 11 PRO E 185 LYS E 190 5 6
HELIX 12 12 SER E 191 GLN E 196 1 6
HELIX 13 13 PRO E 211 ARG E 223 1 13
HELIX 14 14 PHE E 243 GLU E 251 5 9
HELIX 15 15 SER E 260 GLN E 266 1 7
HELIX 16 16 THR E 283 GLU E 295 1 13
HELIX 17 17 LEU E 314 LEU E 323 1 10
SHEET 1 BA 8 VAL B 215 LEU B 217 0
SHEET 2 BA 8 ALA A 395 LEU A 398 -1 O TRP A 396 N ILE B 216
SHEET 3 BA 8 TYR B 242 ALA B 243 -1 O ALA B 243 N HIS A 397
SHEET 4 BA 8 VAL B 250 TYR B 259 -1 O SER B 254 N TYR B 242
SHEET 5 BA 8 LYS B 262 PRO B 271 -1 O LYS B 262 N TYR B 259
SHEET 6 BA 8 SER E 44 ASP E 51 1 O SER E 45 N THR B 265
SHEET 7 BA 8 ALA E 71 ASP E 75 1 O PRO E 72 N PHE E 50
SHEET 8 BA 8 SER E 80 LEU E 85 -1 O SER E 80 N ASP E 75
SHEET 1 AA 5 ILE A 400 SER A 402 0
SHEET 2 AA 5 TYR A 459 ILE A 466 -1 O TYR A 459 N SER A 402
SHEET 3 AA 5 PHE A 444 GLN A 453 -1 O LYS A 446 N ILE A 466
SHEET 4 AA 5 TYR A 431 LYS A 437 -1 O LEU A 432 N LEU A 449
SHEET 5 AA 5 GLU A 423 ASN A 428 -1 O GLU A 423 N ARG A 435
SHEET 1 EA 2 LEU E 152 ILE E 155 0
SHEET 2 EA 2 THR E 162 LEU E 166 -1 N LEU E 163 O VAL E 154
SHEET 1 EB 3 VAL E 206 ARG E 207 0
SHEET 2 EB 3 ALA E 226 VAL E 230 1 O PRO E 228 N VAL E 206
SHEET 3 EB 3 VAL E 236 SER E 241 -1 N VAL E 237 O VAL E 229
SHEET 1 EC 3 LYS E 277 CYS E 278 0
SHEET 2 EC 3 ARG E 298 VAL E 302 1 O VAL E 300 N CYS E 278
SHEET 3 EC 3 VAL E 308 SER E 313 -1 N LYS E 309 O VAL E 301
SITE 1 AC1 21 ARG E 69 ARG E 151 LYS E 169 ILE E 239
SITE 2 AC1 21 SER E 241 PHE E 243 ASP E 244 ARG E 268
SITE 3 AC1 21 GLY E 274 VAL E 275 LEU E 276 VAL E 296
SITE 4 AC1 21 HIS E 297 ARG E 298 HOH E2229 HOH E2230
SITE 5 AC1 21 HOH E2231 HOH E2232 HOH E2233 HOH E2234
SITE 6 AC1 21 HOH E2235
SITE 1 AC2 20 ARG E 69 MET E 84 THR E 86 ILE E 87
SITE 2 AC2 20 THR E 88 ASP E 89 PRO E 127 LEU E 128
SITE 3 AC2 20 VAL E 129 ILE E 149 HIS E 150 ARG E 151
SITE 4 AC2 20 PRO E 153 SER E 225 LYS E 242 HOH E2036
SITE 5 AC2 20 HOH E2232 HOH E2236 HOH E2237 HOH E2238
SITE 1 AC3 18 ARG A 457 HIS E 150 THR E 199 ASN E 202
SITE 2 AC3 18 ILE E 203 ALA E 204 VAL E 224 SER E 225
SITE 3 AC3 18 ALA E 226 HIS E 297 ILE E 311 SER E 313
SITE 4 AC3 18 SER E 315 ASP E 316 HOH E2199 HOH E2239
SITE 5 AC3 18 HOH E2241 HOH E2242
CRYST1 48.961 121.032 127.247 90.00 90.00 90.00 P 21 21 21 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 0.020424 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008262 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007859 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
