HEADER TRANSFERASE 22-JUN-16 5LCU
TITLE COCRYSTAL STRUCTURE OF CAMP-DEPENDENT PROTEIN KINASE (PKA) IN COMPLEX
TITLE 2 WITH A S-METHYL-PIPERAZINE SUBSTITUTED FASUDIL-DERIVATIVE (LIGAND 01)
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 OTHER_DETAILS: PHOSPHORYLATED AT SER11, THR198, SER339;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE INHIBITOR ALPHA;
COMPND 10 CHAIN: B;
COMPND 11 SYNONYM: PKI-ALPHA,CAMP-DEPENDENT PROTEIN KINASE INHIBITOR,
COMPND 12 MUSCLE/BRAIN ISOFORM;
COMPND 13 ENGINEERED: YES;
COMPND 14 OTHER_DETAILS: AMINO ACIDS 5-24 FROM CAMP-DEPENDENT PROTEIN KINASE
COMPND 15 INHIBITOR ALPHA FROM SIGMA (ORDER ID: P7739)
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CRICETULUS GRISEUS;
SOURCE 3 ORGANISM_COMMON: CHINESE HAMSTER;
SOURCE 4 ORGANISM_TAXID: 10029;
SOURCE 5 GENE: PRKACA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606
KEYWDS PKA, KINASE, FASUDIL, INHIBITION, COCRYSTAL, 3X-PHOSPHORYLATED,
KEYWDS 2 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.WIENEN-SCHMIDT,A.HEINE,G.KLEBE
REVDAT 2 10-JAN-24 5LCU 1 REMARK
REVDAT 1 17-JAN-18 5LCU 0
JRNL AUTH B.WIENEN,H.R.A.JONKER,T.WULSDORF,H.-D.GERBER,K.SAXENA,
JRNL AUTH 2 D.KUDLINZKI,S.SREERAMULU,G.PARIGI,C.LUCHINAT,A.HEINE,
JRNL AUTH 3 H.SCHWALBE,G.KLEBE
JRNL TITL COCRYSTAL STRUCTURE OF CAMP-DEPENDENT PROTEIN KINASE (PKA)
JRNL TITL 2 IN COMPLEX WITH DIFFERENT FASUDIL-DERIVATIVES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.58 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.58
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.77
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.9
REMARK 3 NUMBER OF REFLECTIONS : 61631
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.154
REMARK 3 R VALUE (WORKING SET) : 0.152
REMARK 3 FREE R VALUE : 0.192
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3082
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 43.7904 - 4.4242 0.97 2934 155 0.1441 0.1619
REMARK 3 2 4.4242 - 3.5121 0.97 2802 147 0.1317 0.1470
REMARK 3 3 3.5121 - 3.0683 0.96 2722 144 0.1507 0.1788
REMARK 3 4 3.0683 - 2.7878 0.96 2729 143 0.1555 0.2018
REMARK 3 5 2.7878 - 2.5880 0.96 2702 142 0.1590 0.2013
REMARK 3 6 2.5880 - 2.4354 0.96 2665 141 0.1513 0.1716
REMARK 3 7 2.4354 - 2.3135 0.95 2701 142 0.1471 0.2204
REMARK 3 8 2.3135 - 2.2128 0.96 2675 141 0.1468 0.2015
REMARK 3 9 2.2128 - 2.1276 0.95 2666 140 0.1492 0.1969
REMARK 3 10 2.1276 - 2.0542 0.97 2703 142 0.1556 0.1964
REMARK 3 11 2.0542 - 1.9900 0.97 2669 141 0.1571 0.2232
REMARK 3 12 1.9900 - 1.9331 0.97 2699 142 0.1599 0.2212
REMARK 3 13 1.9331 - 1.8822 0.96 2680 141 0.1618 0.2248
REMARK 3 14 1.8822 - 1.8363 0.95 2641 139 0.1625 0.1940
REMARK 3 15 1.8363 - 1.7945 0.93 2594 136 0.1584 0.2190
REMARK 3 16 1.7945 - 1.7563 0.94 2602 137 0.1578 0.2040
REMARK 3 17 1.7563 - 1.7212 0.93 2581 136 0.1647 0.2500
REMARK 3 18 1.7212 - 1.6887 0.92 2554 135 0.1682 0.2490
REMARK 3 19 1.6887 - 1.6586 0.93 2581 135 0.1752 0.2484
REMARK 3 20 1.6586 - 1.6304 0.93 2578 136 0.1774 0.2096
REMARK 3 21 1.6304 - 1.6041 0.92 2549 134 0.1847 0.2520
REMARK 3 22 1.6041 - 1.5795 0.91 2522 133 0.1954 0.2555
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.410
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 : 0.009 3137
REMARK 3 ANGLE : 0.951 4256
REMARK 3 CHIRALITY : 0.052 451
REMARK 3 PLANARITY : 0.006 560
REMARK 3 DIHEDRAL : 15.003 1856
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 5LCU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-JUN-16.
REMARK 100 THE DEPOSITION ID IS D_1200000539.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-NOV-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 61633
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.579
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.6
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.3900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.58
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.68
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.47900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.090
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1Q8W
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: DROP: 10 MG/ML PKA (0.240 MM) 30 MM
REMARK 280 MBT (MES/BIS-TRIS PUFFER PH 6.9) 1 MM DTT 0.1 MM EDTA 75 MM LICL
REMARK 280 0.03 MM MEGA 8 0.07MM PKI (SIGMA: P7739) 1.2 MM LIGAND SOLVED IN
REMARK 280 DMSO (50 MM STOCK) RESERVOIR: 16% METHANOL 0.003 ML DROP VOLUME,
REMARK 280 0.4 ML RESERVOIR VOLUME, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277.15K
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 29.24500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 54.71400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.48150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 54.71400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.24500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.48150
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16950 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
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 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 A 21 CG CD CE NZ
REMARK 470 LYS A 28 CD CE NZ
REMARK 470 ARG A 45 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 61 NZ
REMARK 470 LYS A 81 CD CE NZ
REMARK 470 LYS A 83 CG CD CE NZ
REMARK 470 LYS A 192 CE NZ
REMARK 470 LYS A 213 CE NZ
REMARK 470 LYS A 285 CD CE NZ
REMARK 470 LYS A 317 CD CE NZ
REMARK 470 PHE A 318 CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 319 CG CD CE NZ
REMARK 470 GLU A 331 CG CD OE1 OE2
REMARK 470 GLU A 333 CD OE1 OE2
REMARK 470 GLU A 334 CG CD OE1 OE2
REMARK 470 ARG A 336 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 339 CG1 CG2 CD1
REMARK 470 LYS A 342 CG CD CE NZ
REMARK 470 LYS A 345 CG CD CE NZ
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 LEU A 273 49.68 -87.67
REMARK 500 LYS A 319 47.11 -90.13
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 870 DISTANCE = 6.21 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IQP A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD A 405
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5LCP RELATED DB: PDB
REMARK 900 5LCP CONTAINS THE SAME PROTEIN IN COMPLEX WITH THE STRUCTURALLY
REMARK 900 RELATED DRUG FASUDIL (M77)
REMARK 900 RELATED ID: 5LCQ RELATED DB: PDB
REMARK 900 5LCQ CONTAINS THE SAME PROTEIN IN COMPLEX WITH A LONG-CHAINED
REMARK 900 FASUDIL-DERIVATIVE (LIGAND 08)
REMARK 900 RELATED ID: 5LCR RELATED DB: PDB
REMARK 900 5LCR CONTAINS THE SAME PROTEIN IN COMPLEX WITH AN OPEN-CHAINED
REMARK 900 FASUDIL-DERIVATIVE (LIGAND 10)
REMARK 900 RELATED ID: 5LCT RELATED DB: PDB
REMARK 900 5LCT CONTAINS THE SAME PROTEIN IN COMPLEX WITH AN R-METHYL-
REMARK 900 PIPERAZINE SUBSTITUTED FASUDIL-DERIVATIVE (LIGAND 21)
DBREF 5LCU A 0 350 UNP P25321 KAPCA_CRIGR 1 351
DBREF 5LCU B 5 24 UNP P61925 IPKA_HUMAN 6 25
SEQADV 5LCU GLY A -2 UNP P25321 EXPRESSION TAG
SEQADV 5LCU HIS A -1 UNP P25321 EXPRESSION TAG
SEQRES 1 A 353 GLY HIS MET GLY ASN ALA ALA ALA ALA LYS LYS GLY SEP
SEQRES 2 A 353 GLU GLN GLU SER VAL LYS GLU PHE LEU ALA LYS ALA LYS
SEQRES 3 A 353 GLU GLU PHE LEU LYS LYS TRP GLU SER PRO SER GLN ASN
SEQRES 4 A 353 THR ALA GLN LEU ASP HIS PHE ASP ARG ILE LYS THR LEU
SEQRES 5 A 353 GLY THR GLY SER PHE GLY ARG VAL MET LEU VAL LYS HIS
SEQRES 6 A 353 LYS GLU THR GLY ASN HIS TYR ALA MET LYS ILE LEU ASP
SEQRES 7 A 353 LYS GLN LYS VAL VAL LYS LEU LYS GLN ILE GLU HIS THR
SEQRES 8 A 353 LEU ASN GLU LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO
SEQRES 9 A 353 PHE LEU VAL LYS LEU GLU PHE SER PHE LYS ASP ASN SER
SEQRES 10 A 353 ASN LEU TYR MET VAL MET GLU TYR VAL PRO GLY GLY GLU
SEQRES 11 A 353 MET PHE SER HIS LEU ARG ARG ILE GLY ARG PHE SER GLU
SEQRES 12 A 353 PRO HIS ALA ARG PHE TYR ALA ALA GLN ILE VAL LEU THR
SEQRES 13 A 353 PHE GLU TYR LEU HIS SER LEU ASP LEU ILE TYR ARG ASP
SEQRES 14 A 353 LEU LYS PRO GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR
SEQRES 15 A 353 ILE GLN VAL THR ASP PHE GLY PHE ALA LYS ARG VAL LYS
SEQRES 16 A 353 GLY ARG THR TRP TPO LEU CYS GLY THR PRO GLU TYR LEU
SEQRES 17 A 353 ALA PRO GLU ILE ILE LEU SER LYS GLY TYR ASN LYS ALA
SEQRES 18 A 353 VAL ASP TRP TRP ALA LEU GLY VAL LEU ILE TYR GLU MET
SEQRES 19 A 353 ALA ALA GLY TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE
SEQRES 20 A 353 GLN ILE TYR GLU LYS ILE VAL SER GLY LYS VAL ARG PHE
SEQRES 21 A 353 PRO SER HIS PHE SER SER ASP LEU LYS ASP LEU LEU ARG
SEQRES 22 A 353 ASN LEU LEU GLN VAL ASP LEU THR LYS ARG PHE GLY ASN
SEQRES 23 A 353 LEU LYS ASN GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP
SEQRES 24 A 353 PHE ALA THR THR ASP TRP ILE ALA ILE TYR GLN ARG LYS
SEQRES 25 A 353 VAL GLU ALA PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY
SEQRES 26 A 353 ASP THR SER ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE
SEQRES 27 A 353 ARG VAL SEP ILE ASN GLU LYS CYS GLY LYS GLU PHE THR
SEQRES 28 A 353 GLU PHE
SEQRES 1 B 20 THR THR TYR ALA ASP PHE ILE ALA SER GLY ARG THR GLY
SEQRES 2 B 20 ARG ARG ASN ALA ILE HIS ASP
MODRES 5LCU SEP A 10 SER MODIFIED RESIDUE
MODRES 5LCU TPO A 197 THR MODIFIED RESIDUE
MODRES 5LCU SEP A 338 SER MODIFIED RESIDUE
HET SEP A 10 14
HET TPO A 197 17
HET SEP A 338 14
HET IQP A 401 20
HET MOH A 402 2
HET MOH A 403 2
HET MOH A 404 2
HET MPD A 405 8
HETNAM SEP PHOSPHOSERINE
HETNAM TPO PHOSPHOTHREONINE
HETNAM IQP 1-(5-ISOQUINOLINESULFONYL)-2-METHYLPIPERAZINE
HETNAM MOH METHANOL
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETSYN SEP PHOSPHONOSERINE
HETSYN TPO PHOSPHONOTHREONINE
HETSYN IQP H-7
FORMUL 1 SEP 2(C3 H8 N O6 P)
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 3 IQP C14 H17 N3 O2 S
FORMUL 4 MOH 3(C H4 O)
FORMUL 7 MPD C6 H14 O2
FORMUL 8 HOH *399(H2 O)
HELIX 1 AA1 GLY A 1 SER A 32 1 32
HELIX 2 AA2 GLN A 39 ASP A 41 5 3
HELIX 3 AA3 LYS A 76 LEU A 82 1 7
HELIX 4 AA4 GLN A 84 VAL A 98 1 15
HELIX 5 AA5 GLU A 127 GLY A 136 1 10
HELIX 6 AA6 SER A 139 LEU A 160 1 22
HELIX 7 AA7 LYS A 168 GLU A 170 5 3
HELIX 8 AA8 THR A 201 LEU A 205 5 5
HELIX 9 AA9 ALA A 206 LEU A 211 1 6
HELIX 10 AB1 LYS A 217 GLY A 234 1 18
HELIX 11 AB2 GLN A 242 GLY A 253 1 12
HELIX 12 AB3 SER A 262 LEU A 273 1 12
HELIX 13 AB4 ASP A 276 ARG A 280 5 5
HELIX 14 AB5 VAL A 288 ASN A 293 1 6
HELIX 15 AB6 HIS A 294 ALA A 298 5 5
HELIX 16 AB7 ASP A 301 GLN A 307 1 7
HELIX 17 AB8 GLY A 344 THR A 348 5 5
HELIX 18 AB9 THR B 6 SER B 13 1 8
SHEET 1 AA1 5 PHE A 43 GLY A 52 0
SHEET 2 AA1 5 GLY A 55 HIS A 62 -1 O LEU A 59 N LYS A 47
SHEET 3 AA1 5 HIS A 68 ASP A 75 -1 O MET A 71 N MET A 58
SHEET 4 AA1 5 ASN A 115 GLU A 121 -1 O MET A 118 N LYS A 72
SHEET 5 AA1 5 LEU A 106 LYS A 111 -1 N PHE A 108 O VAL A 119
SHEET 1 AA2 2 LEU A 162 ILE A 163 0
SHEET 2 AA2 2 LYS A 189 ARG A 190 -1 O LYS A 189 N ILE A 163
SHEET 1 AA3 2 LEU A 172 ILE A 174 0
SHEET 2 AA3 2 ILE A 180 VAL A 182 -1 O GLN A 181 N LEU A 173
LINK C GLY A 9 N SEP A 10 1555 1555 1.32
LINK C SEP A 10 N GLU A 11 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 1.34
SITE 1 AC1 12 GLY A 50 VAL A 57 ALA A 70 GLU A 121
SITE 2 AC1 12 TYR A 122 VAL A 123 LEU A 173 THR A 183
SITE 3 AC1 12 ASP A 184 PHE A 327 HOH A 671 HOH B 106
SITE 1 AC2 8 VAL A 15 PHE A 18 PHE A 100 LEU A 152
SITE 2 AC2 8 GLU A 155 TYR A 306 HOH A 589 HOH A 659
CRYST1 58.490 72.963 109.428 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 0.017097 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013706 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009138 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
