HEADER TRANSFERASE 26-FEB-07 2JO8
TITLE SOLUTION STRUCTURE OF C-TERMINAL DOMAIN OF HUMAN MAMMALIAN STERILE 20-
TITLE 2 LIKE KINASE 1 (MST1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE 4;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: C-TERMINAL SARAH DOMAIN, DATABASE RESIDUES 432-480;
COMPND 5 SYNONYM: STE20-LIKE KINASE MST1, MST-1, MAMMALIAN STE20-LIKE PROTEIN
COMPND 6 KINASE 1, SERINE/THREONINE-PROTEIN KINASE KRS-2;
COMPND 7 EC: 2.7.11.1;
COMPND 8 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: STK4, MST1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PGEX4T-1
KEYWDS PROTEIN, C-TERMINAL DOMAIN, HUMAN MAMMALIAN STERILE 20-LIKE KINASE 1,
KEYWDS 2 DIMER, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR E.HWANG,K.-S.RYU,K.PAAKKONEN,P.GUNTERT,H.-K.CHEONG,D.-S.LIM,J.O.LEE,
AUTHOR 2 Y.H.JEON,C.CHEONG
REVDAT 5 20-DEC-23 2JO8 1 REMARK
REVDAT 4 09-MAR-22 2JO8 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2JO8 1 VERSN
REVDAT 2 19-JUN-07 2JO8 1 JRNL
REVDAT 1 15-MAY-07 2JO8 0
JRNL AUTH E.HWANG,K.-S.RYU,K.PAAKKONEN,P.GUNTERT,H.-K.CHEONG,D.-S.LIM,
JRNL AUTH 2 J.-O.LEE,Y.H.JEON,C.CHEONG
JRNL TITL STRUCTURAL INSIGHT INTO DIMERIC INTERACTION OF THE SARAH
JRNL TITL 2 DOMAINS FROM MST1 AND RASSF FAMILY PROTEINS IN THE APOPTOSIS
JRNL TITL 3 PATHWAY
JRNL REF PROC.NATL.ACAD.SCI.USA V. 104 9236 2007
JRNL REFN ISSN 0027-8424
JRNL PMID 17517604
JRNL DOI 10.1073/PNAS.0610716104
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 2.1, OPAL
REMARK 3 AUTHORS : P.GUNTERT ET AL. (CYANA), LUGINBUHL, GUNTERT,
REMARK 3 BILLETER AND WUTHRICH (OPAL)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2JO8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAR-07.
REMARK 100 THE DEPOSITION ID IS D_1000100080.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7
REMARK 210 IONIC STRENGTH : 125
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM [U-13C; U-15N] C-TERMINAL
REMARK 210 DOMAIN OF MAMMALIAN STERILE 20-
REMARK 210 LIKE KINASE 1, 100 MM SODIUM
REMARK 210 CHLORIDE, 2 MM DTT, 25 MM HEPES,
REMARK 210 90% H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D CBCA(CO)NH; 3D CBCANH; 3D
REMARK 210 HN(CA)CO; 3D HNCO; 3D HNCA; 3D
REMARK 210 HBHA(CO)NH; 3D H(CCO)NH; 3D
REMARK 210 C(CCO)NH; 3D HCCH-COSY; 3D CCH-
REMARK 210 TOCSY; 3D HCCH-TOCSY; 3D 1H-15N
REMARK 210 NOESY; 3D 1H-13C NOESY; 2D 1H-
REMARK 210 15N HSQC; 2D 1H-13C HSQC; 3D
REMARK 210 FILTER-EDITED 1H-15N NOESY; 3D
REMARK 210 FILTER-EDITED 1H-13C NOESY; 2D
REMARK 210 IPAP-1H-15N HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ; 900 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; AVANCE II
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CYANA 2.1, NMRPIPE, SPARKY,
REMARK 210 TALOS, TOPSPIN
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
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: DIMERIC
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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 OE2 GLU A 29 HH TYR B 137 1.59
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 2 ARG A 18 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 2 ARG A 18 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 10 ARG B 134 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 17 ARG A 18 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 19 ARG B 141 NE - CZ - NH2 ANGL. DEV. = -3.2 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 3 TYR B 104 -0.87 -142.64
REMARK 500 5 TYR B 104 13.40 -153.60
REMARK 500 5 PHE B 106 2.27 -67.91
REMARK 500 6 SER A 2 -62.34 -106.01
REMARK 500 6 SER B 102 -144.77 -86.60
REMARK 500 7 TYR B 104 23.53 -145.92
REMARK 500 8 TYR A 4 37.45 -147.85
REMARK 500 8 TYR B 104 13.61 -140.18
REMARK 500 9 SER A 2 99.54 -41.85
REMARK 500 9 TYR B 104 -4.28 -142.55
REMARK 500 10 TYR A 4 18.13 -149.09
REMARK 500 12 ASP B 103 106.98 -52.27
REMARK 500 12 TYR B 104 4.00 -152.85
REMARK 500 13 SER A 2 65.56 -159.27
REMARK 500 14 SER A 2 126.77 -179.04
REMARK 500 14 SER B 102 132.79 -174.94
REMARK 500 15 ASP A 3 42.26 -67.26
REMARK 500 20 TYR A 4 16.97 -142.55
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 TYR A 4 0.11 SIDE CHAIN
REMARK 500 5 TYR A 4 0.07 SIDE CHAIN
REMARK 500 5 ARG A 34 0.09 SIDE CHAIN
REMARK 500 6 ARG A 41 0.08 SIDE CHAIN
REMARK 500 9 ARG A 34 0.11 SIDE CHAIN
REMARK 500 13 ARG B 118 0.09 SIDE CHAIN
REMARK 500 13 ARG B 134 0.08 SIDE CHAIN
REMARK 500 14 TYR A 4 0.07 SIDE CHAIN
REMARK 500 15 TYR B 104 0.09 SIDE CHAIN
REMARK 500 16 ARG A 34 0.09 SIDE CHAIN
REMARK 500 17 ARG A 34 0.11 SIDE CHAIN
REMARK 500 18 ARG B 118 0.10 SIDE CHAIN
REMARK 500 18 ARG B 141 0.08 SIDE CHAIN
REMARK 500 20 ARG A 34 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2JO8 A 3 51 UNP Q13043 STK4_HUMAN 432 480
DBREF 2JO8 B 103 151 UNP Q13043 STK4_HUMAN 432 480
SEQADV 2JO8 GLY A 1 UNP Q13043 CLONING ARTIFACT
SEQADV 2JO8 SER A 2 UNP Q13043 CLONING ARTIFACT
SEQADV 2JO8 GLY B 101 UNP Q13043 CLONING ARTIFACT
SEQADV 2JO8 SER B 102 UNP Q13043 CLONING ARTIFACT
SEQRES 1 A 51 GLY SER ASP TYR GLU PHE LEU LYS SER TRP THR VAL GLU
SEQRES 2 A 51 ASP LEU GLN LYS ARG LEU LEU ALA LEU ASP PRO MET MET
SEQRES 3 A 51 GLU GLN GLU ILE GLU GLU ILE ARG GLN LYS TYR GLN SER
SEQRES 4 A 51 LYS ARG GLN PRO ILE LEU ASP ALA ILE GLU ALA LYS
SEQRES 1 B 51 GLY SER ASP TYR GLU PHE LEU LYS SER TRP THR VAL GLU
SEQRES 2 B 51 ASP LEU GLN LYS ARG LEU LEU ALA LEU ASP PRO MET MET
SEQRES 3 B 51 GLU GLN GLU ILE GLU GLU ILE ARG GLN LYS TYR GLN SER
SEQRES 4 B 51 LYS ARG GLN PRO ILE LEU ASP ALA ILE GLU ALA LYS
HELIX 1 1 TYR A 4 TRP A 10 5 7
HELIX 2 2 THR A 11 GLU A 49 1 39
HELIX 3 3 GLU B 105 TRP B 110 5 6
HELIX 4 4 THR B 111 GLU B 149 1 39
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
