HEADER HYDROLASE/HYDROLASE INHIBITOR 16-DEC-13 4O21
TITLE PRODUCT COMPLEX OF METAL-FREE PKAC, ATP-GAMMA-S AND SP20.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC SUBUNIT, UNP RESIDUES 16-351;
COMPND 5 SYNONYM: PKA C-ALPHA;
COMPND 6 EC: 2.7.11.11;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: THIO-PHOSPHORYLATED PEPTIDE PSP20;
COMPND 10 CHAIN: S;
COMPND 11 FRAGMENT: UNP RESIDUES 6-25;
COMPND 12 SYNONYM: PKI-ALPHA, CAMP-DEPENDENT PROTEIN KINASE INHIBITOR ALPHA,
COMPND 13 CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, MUSCLE/BRAIN ISOFORM;
COMPND 14 ENGINEERED: YES;
COMPND 15 MUTATION: 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, PRKACA PKACA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: PKIA, PKIA PRKACN1, PRKACN1;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SER/THR KINASE, PHOSPHORYL TRANSFER, NUCLEOTIDE, HYDROLASE-HYDROLASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.DAS,A.Y.KOVALEVSKY,O.GERLITS,P.LANGAN,W.T.HELLER,M.KESHWANI,
AUTHOR 2 S.TAYLOR
REVDAT 1 28-MAY-14 4O21 0
JRNL AUTH O.GERLITS,A.DAS,M.M.KESHWANI,S.TAYLOR,M.J.WALTMAN,P.LANGAN,
JRNL AUTH 2 W.T.HELLER,A.KOVALEVSKY
JRNL TITL METAL-FREE CAMP-DEPENDENT PROTEIN KINASE CAN CATALYZE
JRNL TITL 2 PHOSPHORYL TRANSFER.
JRNL REF BIOCHEMISTRY V. 53 3179 2014
JRNL REFN ISSN 0006-2960
JRNL PMID 24786636
JRNL DOI 10.1021/BI5000965
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_1370)
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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.12
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 84.8
REMARK 3 NUMBER OF REFLECTIONS : 27971
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.860
REMARK 3 FREE R VALUE TEST SET COUNT : 1919
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 37.1304 - 4.6970 1.00 2347 172 0.1689 0.2007
REMARK 3 2 4.6970 - 3.7293 1.00 2255 165 0.1400 0.1828
REMARK 3 3 3.7293 - 3.2582 0.99 2206 161 0.1513 0.2143
REMARK 3 4 3.2582 - 2.9604 0.98 2155 160 0.1661 0.2053
REMARK 3 5 2.9604 - 2.7483 0.98 2154 159 0.1854 0.2655
REMARK 3 6 2.7483 - 2.5863 0.97 2101 154 0.1834 0.2371
REMARK 3 7 2.5863 - 2.4568 0.95 2073 156 0.1787 0.2136
REMARK 3 8 2.4568 - 2.3499 0.96 2088 156 0.1803 0.2465
REMARK 3 9 2.3499 - 2.2595 0.93 2033 152 0.1790 0.2034
REMARK 3 10 2.2595 - 2.1815 0.90 1931 139 0.1732 0.2310
REMARK 3 11 2.1815 - 2.1133 0.78 1703 123 0.1843 0.2226
REMARK 3 12 2.1133 - 2.0529 0.60 1297 96 0.1698 0.2172
REMARK 3 13 2.0529 - 1.9988 0.46 991 74 0.1839 0.2382
REMARK 3 14 1.9988 - 1.9501 0.33 718 52 0.1949 0.2312
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) : 0.130
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.680
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 : 0.005 3072
REMARK 3 ANGLE : 0.941 4161
REMARK 3 CHIRALITY : 0.063 429
REMARK 3 PLANARITY : 0.004 524
REMARK 3 DIHEDRAL : 15.898 1175
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 4O21 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JAN-14.
REMARK 100 THE RCSB ID CODE IS RCSB083942.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-SEP-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : CU ANODE, CU-KA LINE.
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32471
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
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) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.8
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 PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES PH 6.5, 5 MM DTT, 15-20%
REMARK 280 PEG 4000., 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 28.48100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.94650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.63000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 48.94650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.48100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.63000
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: 2170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 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 9
REMARK 465 HIS A 10
REMARK 465 HIS A 11
REMARK 465 HIS A 12
REMARK 465 HIS A 13
REMARK 465 HIS A 14
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 HOH A 825 O HOH S 631 2.17
REMARK 500 O HOH A 831 O HOH A 878 2.18
REMARK 500 O SER A 53 O HOH A 756 2.19
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 ASN A 99 110.12 -160.74
REMARK 500 ASP A 112 -159.99 -129.43
REMARK 500 ASP A 166 35.32 -144.53
REMARK 500 ASP A 184 83.75 70.53
REMARK 500 ASN A 216 -158.56 -130.08
REMARK 500 LYS A 319 -134.53 -82.35
REMARK 500 HIS S 519 -125.62 -133.42
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4O22 RELATED DB: PDB
DBREF 4O21 A 15 350 UNP P05132 KAPCA_MOUSE 16 351
DBREF 4O21 S 501 520 UNP P61925 IPKA_HUMAN 6 25
SEQADV 4O21 HIS A 9 UNP P05132 EXPRESSION TAG
SEQADV 4O21 HIS A 10 UNP P05132 EXPRESSION TAG
SEQADV 4O21 HIS A 11 UNP P05132 EXPRESSION TAG
SEQADV 4O21 HIS A 12 UNP P05132 EXPRESSION TAG
SEQADV 4O21 HIS A 13 UNP P05132 EXPRESSION TAG
SEQADV 4O21 HIS A 14 UNP P05132 EXPRESSION TAG
SEQADV 4O21 ALA S 516 UNP P61925 ASN 21 ENGINEERED MUTATION
SEQADV 4O21 2RX S 517 UNP P61925 ALA 22 ENGINEERED MUTATION
SEQRES 1 A 342 HIS HIS HIS HIS HIS HIS VAL LYS GLU PHE LEU ALA LYS
SEQRES 2 A 342 ALA LYS GLU ASP PHE LEU LYS LYS TRP GLU THR PRO SER
SEQRES 3 A 342 GLN ASN THR ALA GLN LEU ASP GLN PHE ASP ARG ILE LYS
SEQRES 4 A 342 THR LEU GLY THR GLY SER PHE GLY ARG VAL MET LEU VAL
SEQRES 5 A 342 LYS HIS LYS GLU SER GLY ASN HIS TYR ALA MET LYS ILE
SEQRES 6 A 342 LEU ASP LYS GLN LYS VAL VAL LYS LEU LYS GLN ILE GLU
SEQRES 7 A 342 HIS THR LEU ASN GLU LYS ARG ILE LEU GLN ALA VAL ASN
SEQRES 8 A 342 PHE PRO PHE LEU VAL LYS LEU GLU PHE SER PHE LYS ASP
SEQRES 9 A 342 ASN SER ASN LEU TYR MET VAL MET GLU TYR VAL ALA GLY
SEQRES 10 A 342 GLY GLU MET PHE SER HIS LEU ARG ARG ILE GLY ARG PHE
SEQRES 11 A 342 SEP GLU PRO HIS ALA ARG PHE TYR ALA ALA GLN ILE VAL
SEQRES 12 A 342 LEU THR PHE GLU TYR LEU HIS SER LEU ASP LEU ILE TYR
SEQRES 13 A 342 ARG ASP LEU LYS PRO GLU ASN LEU LEU ILE ASP GLN GLN
SEQRES 14 A 342 GLY TYR ILE GLN VAL THR ASP PHE GLY PHE ALA LYS ARG
SEQRES 15 A 342 VAL LYS GLY ARG THR TRP TPO LEU CYS GLY THR PRO GLU
SEQRES 16 A 342 TYR LEU ALA PRO GLU ILE ILE LEU SER LYS GLY TYR ASN
SEQRES 17 A 342 LYS ALA VAL ASP TRP TRP ALA LEU GLY VAL LEU ILE TYR
SEQRES 18 A 342 GLU MET ALA ALA GLY TYR PRO PRO PHE PHE ALA ASP GLN
SEQRES 19 A 342 PRO ILE GLN ILE TYR GLU LYS ILE VAL SER GLY LYS VAL
SEQRES 20 A 342 ARG PHE PRO SER HIS PHE SER SER ASP LEU LYS ASP LEU
SEQRES 21 A 342 LEU ARG ASN LEU LEU GLN VAL ASP LEU THR LYS ARG PHE
SEQRES 22 A 342 GLY ASN LEU LYS ASN GLY VAL ASN ASP ILE LYS ASN HIS
SEQRES 23 A 342 LYS TRP PHE ALA THR THR ASP TRP ILE ALA ILE TYR GLN
SEQRES 24 A 342 ARG LYS VAL GLU ALA PRO PHE ILE PRO LYS PHE LYS GLY
SEQRES 25 A 342 PRO GLY ASP THR SER ASN PHE ASP ASP TYR GLU GLU GLU
SEQRES 26 A 342 GLU ILE ARG VAL SEP ILE ASN GLU LYS CYS GLY LYS GLU
SEQRES 27 A 342 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 2RX ILE HIS ASP
MODRES 4O21 SEP A 139 SER PHOSPHOSERINE
MODRES 4O21 TPO A 197 THR PHOSPHOTHREONINE
MODRES 4O21 SEP A 338 SER PHOSPHOSERINE
MODRES 4O21 2RX S 517 SER O-THIOPHOSPHONO-L-SERINE
HET SEP A 139 10
HET TPO A 197 11
HET SEP A 338 10
HET 2RX S 517 17
HET ADP A 401 27
HETNAM SEP PHOSPHOSERINE
HETNAM TPO PHOSPHOTHREONINE
HETNAM 2RX O-THIOPHOSPHONO-L-SERINE
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETSYN SEP PHOSPHONOSERINE
HETSYN TPO PHOSPHONOTHREONINE
FORMUL 1 SEP 2(C3 H8 N O6 P)
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 2 2RX C3 H8 N O5 P S
FORMUL 3 ADP C10 H15 N5 O10 P2
FORMUL 4 HOH *421(H2 O)
HELIX 1 1 VAL A 15 THR A 32 1 18
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 502 ALA S 508 1 7
SHEET 1 A 5 PHE A 43 GLY A 52 0
SHEET 2 A 5 GLY A 55 HIS A 62 -1 O LEU A 59 N LYS A 47
SHEET 3 A 5 HIS A 68 ASP A 75 -1 O MET A 71 N MET A 58
SHEET 4 A 5 ASN A 115 GLU A 121 -1 O LEU A 116 N LEU A 74
SHEET 5 A 5 LEU A 106 LYS A 111 -1 N GLU A 107 O VAL A 119
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
LINK C PHE A 138 N SEP A 139 1555 1555 1.33
LINK C SEP A 139 N GLU A 140 1555 1555 1.32
LINK C TRP A 196 N TPO A 197 1555 1555 1.33
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 C 2RX S 517 N ILE S 518 1555 1555 1.33
LINK C ALA S 516 N 2RX S 517 1555 1555 1.32
SITE 1 AC1 21 GLY A 50 GLY A 52 PHE A 54 GLY A 55
SITE 2 AC1 21 VAL A 57 ALA A 70 LYS A 72 VAL A 104
SITE 3 AC1 21 MET A 120 GLU A 121 VAL A 123 GLU A 127
SITE 4 AC1 21 GLU A 170 LEU A 173 THR A 183 ASP A 184
SITE 5 AC1 21 PHE A 327 HOH A 671 HOH A 864 ARG S 514
SITE 6 AC1 21 2RX S 517
CRYST1 56.962 79.260 97.893 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 0.017556 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012617 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010215 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
