HEADER TRANSFERASE/PEPTIDE 02-JAN-15 3X2U
TITLE MICHAELIS-LIKE INITIAL COMPLEX OF CAMP-DEPENDENT PROTEIN KINASE
TITLE 2 CATALYTIC SUBUNIT.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PKA C-ALPHA;
COMPND 5 EC: 2.7.11.11;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: SUBSTRATE PEPTIDE;
COMPND 9 CHAIN: S;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: PKACA, PRKACA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 14 ORGANISM_TAXID: 32630;
SOURCE 15 OTHER_DETAILS: PEPTIDE CHEMICAL SYNTHESIS
KEYWDS MICHAELIS-LIKE COMPLEX, PROTEIN-SUBSTRATE, PKAC-ATPMG2 TERNARY,
KEYWDS 2 SER/THR KINASE, ATP BINDING, PHOSPHORYLATION, TRANSFERASE-PEPTIDE
KEYWDS 3 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.DAS,P.LANGAN,O.GERLITS,A.Y.KOVALEVSKY,W.T.HELLER
REVDAT 1 16-DEC-15 3X2U 0
JRNL AUTH A.DAS,O.GERLITS,J.M.PARKS,P.LANGAN,A.KOVALEVSKY,W.T.HELLER
JRNL TITL PROTEIN KINASE A CATALYTIC SUBUNIT PRIMED FOR ACTION:
JRNL TITL 2 TIME-LAPSE CRYSTALLOGRAPHY OF MICHAELIS COMPLEX FORMATION.
JRNL REF STRUCTURE V. 23 2331 2015
JRNL REFN ISSN 0969-2126
JRNL PMID 26585512
JRNL DOI 10.1016/J.STR.2015.10.005
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_1692)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.95
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 17258
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 860
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 39.9605 - 4.3596 0.99 2866 154 0.1658 0.1888
REMARK 3 2 4.3596 - 3.4609 0.99 2711 148 0.1718 0.2088
REMARK 3 3 3.4609 - 3.0236 1.00 2739 138 0.2186 0.2631
REMARK 3 4 3.0236 - 2.7472 1.00 2705 139 0.2522 0.3454
REMARK 3 5 2.7472 - 2.5504 1.00 2690 141 0.2849 0.3417
REMARK 3 6 2.5504 - 2.4000 1.00 2687 140 0.2868 0.3216
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.880
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 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 : 0.022 3115
REMARK 3 ANGLE : 1.217 4206
REMARK 3 CHIRALITY : 0.042 436
REMARK 3 PLANARITY : 0.007 533
REMARK 3 DIHEDRAL : 16.678 1182
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 3X2U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-JAN-15.
REMARK 100 THE RCSB ID CODE IS RCSB097108.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-MAR-14
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9798
REMARK 200 MONOCHROMATOR : ROSENBAUM-ROCK HIGH-RESOLUTION
REMARK 200 SI(111) DOUBLE-CRYSTAL
REMARK 200 MONOCHROMATOR. LN2 COOLED FIRST
REMARK 200 CRYSTAL, SAGITTAL FOCUSING 2ND
REMARK 200 CRYSTAL.
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17258
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 39.960
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.5
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: PHENIX
REMARK 200 STARTING MODEL: PDB ENTRY 4O22
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM MES PH 6.5, 5MM DTT, 15-20% PEG
REMARK 280 3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
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 35.83000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.95500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.34000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.95500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.83000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.34000
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, S
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 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 MET A 0
REMARK 465 GLY A 1
REMARK 465 ASN A 2
REMARK 465 ALA A 3
REMARK 465 ALA A 4
REMARK 465 ALA A 5
REMARK 465 ALA A 6
REMARK 465 LYS A 7
REMARK 465 LYS A 8
REMARK 465 GLY A 9
REMARK 465 SER A 10
REMARK 465 GLU A 11
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 GLN A 12 CG CD OE1 NE2
REMARK 470 GLU A 13 CG CD OE1 OE2
REMARK 470 SER A 14 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 NH2 ARG A 144 O HOH A 728 1.90
REMARK 500 O HOH A 713 O HOH A 714 2.17
REMARK 500 O HOH A 716 O HOH A 717 2.17
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 GLU A 13 -45.78 -142.73
REMARK 500 ILE A 46 -54.00 -120.61
REMARK 500 ASP A 112 -160.53 -129.09
REMARK 500 ASP A 166 46.21 -153.39
REMARK 500 ASP A 184 87.70 59.36
REMARK 500 ALA A 240 -165.81 -162.85
REMARK 500 LEU A 273 41.86 -84.07
REMARK 500 VAL A 310 172.10 -59.62
REMARK 500 LYS A 319 37.16 -157.03
REMARK 500 GLU A 334 163.57 -38.89
REMARK 500 HIS S 623 131.74 -171.06
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 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 660 DISTANCE = 6.40 ANGSTROMS
REMARK 525 HOH A 731 DISTANCE = 8.12 ANGSTROMS
REMARK 525 HOH A 758 DISTANCE = 5.19 ANGSTROMS
REMARK 525 HOH A 767 DISTANCE = 5.42 ANGSTROMS
REMARK 525 HOH A 769 DISTANCE = 7.68 ANGSTROMS
REMARK 525 HOH A 770 DISTANCE = 7.76 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ATP A 501 O3G
REMARK 620 2 ASP A 184 OD2 114.3
REMARK 620 3 HOH A 649 O 89.3 94.8
REMARK 620 4 ATP A 501 O1B 77.8 110.8 154.2
REMARK 620 5 ASP A 184 OD1 173.8 59.6 92.4 102.9
REMARK 620 6 ATP A 501 O2G 58.5 56.1 88.3 103.1 115.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 503 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ATP A 501 O2A
REMARK 620 2 ATP A 501 O2G 116.0
REMARK 620 3 ASN A 171 OD1 103.6 133.0
REMARK 620 4 HOH A 607 O 87.7 140.5 60.5
REMARK 620 5 ASP A 184 OD2 77.5 62.0 106.3 157.5
REMARK 620 6 ATP A 501 O3B 64.6 58.7 167.8 113.8 75.1
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3X2V RELATED DB: PDB
REMARK 900 RELATED ID: 3X2W RELATED DB: PDB
DBREF 3X2U A 0 350 UNP P05132 KAPCA_MOUSE 1 351
DBREF 3X2U S 605 624 PDB 3X2U 3X2U 605 624
SEQADV 3X2U HIS A -6 UNP P05132 EXPRESSION TAG
SEQADV 3X2U HIS A -5 UNP P05132 EXPRESSION TAG
SEQADV 3X2U HIS A -4 UNP P05132 EXPRESSION TAG
SEQADV 3X2U HIS A -3 UNP P05132 EXPRESSION TAG
SEQADV 3X2U HIS A -2 UNP P05132 EXPRESSION TAG
SEQADV 3X2U HIS A -1 UNP P05132 EXPRESSION TAG
SEQRES 1 A 357 HIS HIS HIS HIS HIS HIS MET GLY ASN ALA ALA ALA ALA
SEQRES 2 A 357 LYS LYS GLY SER GLU GLN GLU SER VAL LYS GLU PHE LEU
SEQRES 3 A 357 ALA LYS ALA LYS GLU ASP PHE LEU LYS LYS TRP GLU THR
SEQRES 4 A 357 PRO SER GLN ASN THR ALA GLN LEU ASP GLN PHE ASP ARG
SEQRES 5 A 357 ILE LYS THR LEU GLY THR GLY SER PHE GLY ARG VAL MET
SEQRES 6 A 357 LEU VAL LYS HIS LYS GLU SER GLY ASN HIS TYR ALA MET
SEQRES 7 A 357 LYS ILE LEU ASP LYS GLN LYS VAL VAL LYS LEU LYS GLN
SEQRES 8 A 357 ILE GLU HIS THR LEU ASN GLU LYS ARG ILE LEU GLN ALA
SEQRES 9 A 357 VAL ASN PHE PRO PHE LEU VAL LYS LEU GLU PHE SER PHE
SEQRES 10 A 357 LYS ASP ASN SER ASN LEU TYR MET VAL MET GLU TYR VAL
SEQRES 11 A 357 ALA GLY GLY GLU MET PHE SER HIS LEU ARG ARG ILE GLY
SEQRES 12 A 357 ARG PHE SEP GLU PRO HIS ALA ARG PHE TYR ALA ALA GLN
SEQRES 13 A 357 ILE VAL LEU THR PHE GLU TYR LEU HIS SER LEU ASP LEU
SEQRES 14 A 357 ILE TYR ARG ASP LEU LYS PRO GLU ASN LEU LEU ILE ASP
SEQRES 15 A 357 GLN GLN GLY TYR ILE GLN VAL THR ASP PHE GLY PHE ALA
SEQRES 16 A 357 LYS ARG VAL LYS GLY ARG THR TRP TPO LEU CYS GLY THR
SEQRES 17 A 357 PRO GLU TYR LEU ALA PRO GLU ILE ILE LEU SER LYS GLY
SEQRES 18 A 357 TYR ASN LYS ALA VAL ASP TRP TRP ALA LEU GLY VAL LEU
SEQRES 19 A 357 ILE TYR GLU MET ALA ALA GLY TYR PRO PRO PHE PHE ALA
SEQRES 20 A 357 ASP GLN PRO ILE GLN ILE TYR GLU LYS ILE VAL SER GLY
SEQRES 21 A 357 LYS VAL ARG PHE PRO SER HIS PHE SER SER ASP LEU LYS
SEQRES 22 A 357 ASP LEU LEU ARG ASN LEU LEU GLN VAL ASP LEU THR LYS
SEQRES 23 A 357 ARG PHE GLY ASN LEU LYS ASN GLY VAL ASN ASP ILE LYS
SEQRES 24 A 357 ASN HIS LYS TRP PHE ALA THR THR ASP TRP ILE ALA ILE
SEQRES 25 A 357 TYR GLN ARG LYS VAL GLU ALA PRO PHE ILE PRO LYS PHE
SEQRES 26 A 357 LYS GLY PRO GLY ASP THR SER ASN PHE ASP ASP TYR GLU
SEQRES 27 A 357 GLU GLU GLU ILE ARG VAL SEP ILE ASN GLU LYS CYS GLY
SEQRES 28 A 357 LYS GLU PHE THR GLU PHE
SEQRES 1 S 20 THR THR TYR ALA ASP PHE ILE ALA SER GLY ARG THR GLY
SEQRES 2 S 20 ARG ARG ALA SER ILE HIS ASP
MODRES 3X2U SEP A 139 SER PHOSPHOSERINE
MODRES 3X2U TPO A 197 THR PHOSPHOTHREONINE
MODRES 3X2U SEP A 338 SER PHOSPHOSERINE
HET SEP A 139 10
HET TPO A 197 11
HET SEP A 338 10
HET ATP A 501 31
HET MG A 502 1
HET MG A 503 1
HETNAM SEP PHOSPHOSERINE
HETNAM TPO PHOSPHOTHREONINE
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETSYN SEP PHOSPHONOSERINE
HETSYN TPO PHOSPHONOTHREONINE
FORMUL 1 SEP 2(C3 H8 N O6 P)
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 3 ATP C10 H16 N5 O13 P3
FORMUL 4 MG 2(MG 2+)
FORMUL 6 HOH *197(H2 O)
HELIX 1 1 GLU A 13 THR A 32 1 20
HELIX 2 2 GLN A 39 ASP A 41 5 3
HELIX 3 3 LYS A 76 LEU A 82 1 7
HELIX 4 4 GLN A 84 GLN A 96 1 13
HELIX 5 5 GLU A 127 GLY A 136 1 10
HELIX 6 6 SEP A 139 LEU A 160 1 22
HELIX 7 7 LYS A 168 GLU A 170 5 3
HELIX 8 8 THR A 201 LEU A 205 5 5
HELIX 9 9 ALA A 206 LEU A 211 1 6
HELIX 10 10 LYS A 217 GLY A 234 1 18
HELIX 11 11 GLN A 242 GLY A 253 1 12
HELIX 12 12 SER A 262 LEU A 273 1 12
HELIX 13 13 VAL A 288 ASN A 293 1 6
HELIX 14 14 HIS A 294 ALA A 298 5 5
HELIX 15 15 ASP A 301 GLN A 307 1 7
HELIX 16 16 THR S 606 ALA S 612 1 7
SHEET 1 A 5 PHE A 43 THR A 51 0
SHEET 2 A 5 ARG A 56 HIS A 62 -1 O LEU A 59 N LYS A 47
SHEET 3 A 5 HIS A 68 ASP A 75 -1 O TYR A 69 N VAL A 60
SHEET 4 A 5 ASN A 115 GLU A 121 -1 O MET A 120 N ALA A 70
SHEET 5 A 5 LEU A 106 LYS A 111 -1 N PHE A 110 O TYR A 117
SHEET 1 B 2 LEU A 162 ILE A 163 0
SHEET 2 B 2 LYS A 189 ARG A 190 -1 O LYS A 189 N ILE A 163
SHEET 1 C 2 LEU A 172 ILE A 174 0
SHEET 2 C 2 ILE A 180 VAL A 182 -1 O GLN A 181 N LEU A 173
SHEET 1 D 2 CYS A 199 GLY A 200 0
SHEET 2 D 2 ILE S 622 HIS S 623 -1 O ILE S 622 N GLY A 200
LINK C PHE A 138 N SEP A 139 1555 1555 1.33
LINK C SEP A 139 N GLU A 140 1555 1555 1.33
LINK C TRP A 196 N TPO A 197 1555 1555 1.32
LINK C TPO A 197 N LEU A 198 1555 1555 1.33
LINK C VAL A 337 N SEP A 338 1555 1555 1.33
LINK C SEP A 338 N ILE A 339 1555 1555 1.33
LINK O3G ATP A 501 MG MG A 502 1555 1555 1.86
LINK OD2 ASP A 184 MG MG A 502 1555 1555 1.86
LINK O2A ATP A 501 MG MG A 503 1555 1555 2.02
LINK MG MG A 502 O HOH A 649 1555 1555 2.08
LINK O2G ATP A 501 MG MG A 503 1555 1555 2.15
LINK O1B ATP A 501 MG MG A 502 1555 1555 2.26
LINK OD1 ASN A 171 MG MG A 503 1555 1555 2.27
LINK MG MG A 503 O HOH A 607 1555 1555 2.33
LINK OD1 ASP A 184 MG MG A 502 1555 1555 2.35
LINK OD2 ASP A 184 MG MG A 503 1555 1555 2.48
LINK O3B ATP A 501 MG MG A 503 1555 1555 2.65
LINK O2G ATP A 501 MG MG A 502 1555 1555 2.88
SITE 1 AC1 25 LEU A 49 THR A 51 GLY A 52 VAL A 57
SITE 2 AC1 25 ALA A 70 LYS A 72 VAL A 104 MET A 120
SITE 3 AC1 25 GLU A 121 TYR A 122 VAL A 123 GLU A 127
SITE 4 AC1 25 GLU A 170 ASN A 171 LEU A 173 THR A 183
SITE 5 AC1 25 ASP A 184 PHE A 327 MG A 502 MG A 503
SITE 6 AC1 25 HOH A 602 HOH A 607 HOH A 649 ARG S 618
SITE 7 AC1 25 SER S 621
SITE 1 AC2 3 ASP A 184 ATP A 501 HOH A 649
SITE 1 AC3 4 ASN A 171 ASP A 184 ATP A 501 HOH A 607
CRYST1 71.660 74.680 79.910 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 0.013955 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013390 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012514 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
