HEADER TRANSFERASE 01-JUN-12 2LTU
TITLE SOLUTION STRUCTURE OF AUTOINHIBITORY DOMAIN OF HUMAN AMP-ACTIVATED
TITLE 2 PROTEIN KINASE CATALYTIC SUBUNIT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC SUBUNIT ALPHA-2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: AMPK SUBUNIT ALPHA-2;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX
KEYWDS AMPK, AID, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR B.XIA,J.HU
REVDAT 2 14-JUN-23 2LTU 1 REMARK SEQADV
REVDAT 1 12-JUN-13 2LTU 0
JRNL AUTH B.XIA,J.HU
JRNL TITL SOLUTION STRUCTURE OF AUTOINHIBITORY DOMAIN OF HUMAN
JRNL TITL 2 AMP-ACTIVATED PROTEIN KINASE CATALYTIC SUBUNIT
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE, AMBER
REMARK 3 AUTHORS : DELAGLIO, GRZESIEK, VUISTER, ZHU, PFEIFER AND BAX
REMARK 3 (NMRPIPE), CASE, DARDEN, CHEATHAM, III, SIMMERLING,
REMARK 3 WANG, DUKE, LUO, ... AND KOLLMAN (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2LTU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JUN-12.
REMARK 100 THE DEPOSITION ID IS D_1000102825.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 50
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.2 MM [U-100% 13C; U-100% 15N]
REMARK 210 AID PROTEIN, 50 MM SODIUM
REMARK 210 PHOSPHATE, 10 % [U-100% 2H] D2O,
REMARK 210 90 % H2O, 1 MM EDTA, 90% H2O/10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D 1H-13C HSQC;
REMARK 210 3D CBCA(CO)NH; 3D HNCACB; 3D
REMARK 210 HN(CO)CA; 3D HNCO; 3D HCACO; 3D
REMARK 210 H(CCO)NH; 3D HCCH-TOCSY; 3D
REMARK 210 HBHA(CO)NH; 3D 1H-15N TOCSY; 3D
REMARK 210 1H-15N NOESY; 3D 1H-13C NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW, TOPSPIN, NMRDRAW,
REMARK 210 CYANA, DYANA, PROCHECKNMR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: 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 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 1 ARG A 54 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 2 ARG A 54 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 3 ARG A 54 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 5 ARG A 55 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 8 ARG A 54 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 10 ARG A 54 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 13 ARG A 54 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 14 ARG A 54 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 16 ARG A 54 NE - CZ - NH1 ANGL. DEV. = 3.3 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 1 GLU A 24 71.60 71.66
REMARK 500 1 ILE A 56 -60.59 -91.51
REMARK 500 2 SER A 5 128.97 177.49
REMARK 500 2 VAL A 10 88.40 78.58
REMARK 500 2 CYS A 25 -151.72 -102.67
REMARK 500 3 SER A 36 -5.67 -144.16
REMARK 500 4 VAL A 10 85.75 69.41
REMARK 500 4 CYS A 25 -157.24 -102.93
REMARK 500 4 PRO A 39 -5.26 -57.43
REMARK 500 4 MET A 57 31.56 -93.89
REMARK 500 5 VAL A 10 31.33 -83.48
REMARK 500 5 PRO A 39 5.53 -54.77
REMARK 500 7 CYS A 25 -148.87 -102.72
REMARK 500 8 VAL A 10 24.43 -77.81
REMARK 500 8 SER A 36 -20.11 -142.75
REMARK 500 8 MET A 57 -29.62 112.83
REMARK 500 9 MET A 57 53.53 82.78
REMARK 500 9 ASN A 58 135.18 81.30
REMARK 500 10 MET A 4 -43.41 72.47
REMARK 500 10 GLU A 24 71.51 71.69
REMARK 500 10 CYS A 25 -146.58 -145.51
REMARK 500 11 VAL A 10 93.63 74.04
REMARK 500 11 GLU A 24 70.97 67.54
REMARK 500 12 GLU A 24 74.63 70.81
REMARK 500 12 PRO A 39 -9.74 -57.79
REMARK 500 13 GLU A 24 70.19 71.67
REMARK 500 13 MET A 57 -23.83 95.93
REMARK 500 13 ASN A 58 -51.46 73.57
REMARK 500 15 MET A 4 108.67 -52.80
REMARK 500 15 SER A 5 -26.43 -142.04
REMARK 500 15 SER A 36 -11.68 -141.83
REMARK 500 15 MET A 57 128.19 -175.61
REMARK 500 16 CYS A 25 -163.40 -102.72
REMARK 500 17 MET A 4 -19.56 59.13
REMARK 500 17 VAL A 10 115.42 77.32
REMARK 500 17 GLU A 24 77.29 66.51
REMARK 500 17 CYS A 25 -148.61 -149.23
REMARK 500 17 PRO A 39 20.93 -59.85
REMARK 500 18 ASN A 58 -30.00 66.70
REMARK 500 19 SER A 5 27.70 -78.27
REMARK 500 19 MET A 57 141.53 -178.91
REMARK 500 20 MET A 57 -39.20 113.41
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 18497 RELATED DB: BMRB
DBREF 2LTU A 5 62 UNP P54646 AAPK2_HUMAN 282 339
SEQADV 2LTU GLY A 1 UNP P54646 EXPRESSION TAG
SEQADV 2LTU PRO A 2 UNP P54646 EXPRESSION TAG
SEQADV 2LTU HIS A 3 UNP P54646 EXPRESSION TAG
SEQADV 2LTU MET A 4 UNP P54646 EXPRESSION TAG
SEQRES 1 A 62 GLY PRO HIS MET SER TYR ASP ALA ASN VAL ILE ASP ASP
SEQRES 2 A 62 GLU ALA VAL LYS GLU VAL CYS GLU LYS PHE GLU CYS THR
SEQRES 3 A 62 GLU SER GLU VAL MET ASN SER LEU TYR SER GLY ASP PRO
SEQRES 4 A 62 GLN ASP GLN LEU ALA VAL ALA TYR HIS LEU ILE ILE ASP
SEQRES 5 A 62 ASN ARG ARG ILE MET ASN GLN ALA SER GLU
HELIX 1 1 ASP A 7 ILE A 11 5 5
HELIX 2 2 ASP A 12 GLU A 24 1 13
HELIX 3 3 THR A 26 SER A 36 1 11
HELIX 4 4 ASP A 41 ILE A 56 1 16
HELIX 5 5 ILE A 56 SER A 61 1 6
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END