HEADER TRANSFERASE/TRANSFERASE INHIBITOR 23-SEP-11 3TXO
TITLE PKC ETA KINASE IN COMPLEX WITH A NAPHTHYRIDINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN KINASE C ETA TYPE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE DOMAIN, RESIDUES 333-683;
COMPND 5 SYNONYM: PKC-L, NPKC-ETA;
COMPND 6 EC: 2.7.11.13;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PRKCH, PKCL, PRKCL;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS KINASE, PHOSPHOTRANSFERASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR W.STARK,G.RUMMEL,S.W.COWAN-JACOB
REVDAT 2 07-DEC-11 3TXO 1 JRNL
REVDAT 1 30-NOV-11 3TXO 0
JRNL AUTH M.J.VAN EIS,J.P.EVENOU,P.FLOERSHEIM,C.GAUL,S.W.COWAN-JACOB,
JRNL AUTH 2 L.MONOVICH,G.RUMMEL,W.SCHULER,W.STARK,A.STRAUSS,A.MATT,
JRNL AUTH 3 E.VANGREVELINGHE,J.WAGNER,N.SOLDERMANN
JRNL TITL 2,6-NAPHTHYRIDINES AS POTENT AND SELECTIVE INHIBITORS OF THE
JRNL TITL 2 NOVEL PROTEIN KINASE C ISOZYMES.
JRNL REF BIOORG.MED.CHEM.LETT. V. 21 7367 2011
JRNL REFN ISSN 0960-894X
JRNL PMID 22078216
JRNL DOI 10.1016/J.BMCL.2011.10.025
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 56.89
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 25157
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1325
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.05
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.10
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1834
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.2610
REMARK 3 BIN FREE R VALUE SET COUNT : 97
REMARK 3 BIN FREE R VALUE : 0.2830
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2594
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 22
REMARK 3 SOLVENT ATOMS : 139
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.37
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.79000
REMARK 3 B22 (A**2) : -0.44000
REMARK 3 B33 (A**2) : 1.23000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.166
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.117
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.274
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2684 ; 0.023 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3630 ; 1.982 ; 1.972
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 316 ; 6.556 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 137 ;38.954 ;24.088
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 461 ;17.061 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;17.611 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 382 ; 0.143 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2066 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1586 ; 1.328 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2563 ; 2.336 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1098 ; 3.432 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1067 ; 5.388 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3TXO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-OCT-11.
REMARK 100 THE RCSB ID CODE IS RCSB068049.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-NOV-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99180
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25157
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 63.370
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.09100
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) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
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: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 UL PROTEIN (18MG/ML IN 0.25 M NACL,
REMARK 280 0.025 M TRIS PH 7.8, 4MM TCEP, 1MM EDTA) WITH 3-4 UL
REMARK 280 CRYSTALLISATION BUFFER (25 % PEG3350 W/V, 200 MM CITRATE), FREE
REMARK 280 INTERFACE DIFUSION, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 56.76650
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.43050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 56.76650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 28.43050
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 300 REMARK: DIMER IN CRYSTAL DUE TO DOMAIN SWAPPING
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29920 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 56.86100
REMARK 350 BIOMT3 2 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 GLY A 331
REMARK 465 PRO A 332
REMARK 465 LYS A 333
REMARK 465 GLU A 334
REMARK 465 SER A 335
REMARK 465 SER A 336
REMARK 465 LYS A 337
REMARK 465 GLU A 338
REMARK 465 GLY A 339
REMARK 465 ASN A 340
REMARK 465 GLY A 341
REMARK 465 ILE A 342
REMARK 465 GLY A 343
REMARK 465 VAL A 344
REMARK 465 ASN A 345
REMARK 465 SER A 346
REMARK 465 SER A 347
REMARK 465 ASN A 348
REMARK 465 ARG A 349
REMARK 465 LEU A 350
REMARK 465 GLY A 351
REMARK 465 ILE A 352
REMARK 465 ASN A 507
REMARK 465 GLY A 508
REMARK 465 VAL A 509
REMARK 465 THR A 510
REMARK 465 THR A 511
REMARK 465 ALA A 512
REMARK 465 THR A 513
REMARK 465 PHE A 514
REMARK 465 CYS A 515
REMARK 465 GLU A 680
REMARK 465 LEU A 681
REMARK 465 GLN A 682
REMARK 465 PRO A 683
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 12 O HOH A 125 2555 2.09
REMARK 500 O HOH A 157 O HOH A 157 2565 2.09
REMARK 500 O HOH A 156 O HOH A 156 2555 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 TYR A 545 CE2 TYR A 545 CD2 0.094
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 LEU A 409 CA - CB - CG ANGL. DEV. = 18.9 DEGREES
REMARK 500 GLU A 524 CA - CB - CG ANGL. DEV. = 15.2 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 ASN A 354 65.18 -112.03
REMARK 500 PHE A 366 6.48 -64.11
REMARK 500 ARG A 449 -56.60 76.08
REMARK 500 ARG A 478 -16.47 71.88
REMARK 500 ASP A 497 93.31 77.42
REMARK 500 MET A 589 45.50 -87.26
REMARK 500 ASN A 673 32.37 -94.89
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 07U A 1
DBREF 3TXO A 333 683 UNP P24723 KPCL_HUMAN 333 683
SEQADV 3TXO GLY A 331 UNP P24723 EXPRESSION TAG
SEQADV 3TXO PRO A 332 UNP P24723 EXPRESSION TAG
SEQADV 3TXO GLU A 675 UNP P24723 SER 675 ENGINEERED MUTATION
SEQRES 1 A 353 GLY PRO LYS GLU SER SER LYS GLU GLY ASN GLY ILE GLY
SEQRES 2 A 353 VAL ASN SER SER ASN ARG LEU GLY ILE ASP ASN PHE GLU
SEQRES 3 A 353 PHE ILE ARG VAL LEU GLY LYS GLY SER PHE GLY LYS VAL
SEQRES 4 A 353 MET LEU ALA ARG VAL LYS GLU THR GLY ASP LEU TYR ALA
SEQRES 5 A 353 VAL LYS VAL LEU LYS LYS ASP VAL ILE LEU GLN ASP ASP
SEQRES 6 A 353 ASP VAL GLU CYS THR MET THR GLU LYS ARG ILE LEU SER
SEQRES 7 A 353 LEU ALA ARG ASN HIS PRO PHE LEU THR GLN LEU PHE CYS
SEQRES 8 A 353 CYS PHE GLN THR PRO ASP ARG LEU PHE PHE VAL MET GLU
SEQRES 9 A 353 PHE VAL ASN GLY GLY ASP LEU MET PHE HIS ILE GLN LYS
SEQRES 10 A 353 SER ARG ARG PHE ASP GLU ALA ARG ALA ARG PHE TYR ALA
SEQRES 11 A 353 ALA GLU ILE ILE SER ALA LEU MET PHE LEU HIS ASP LYS
SEQRES 12 A 353 GLY ILE ILE TYR ARG ASP LEU LYS LEU ASP ASN VAL LEU
SEQRES 13 A 353 LEU ASP HIS GLU GLY HIS CYS LYS LEU ALA ASP PHE GLY
SEQRES 14 A 353 MET CYS LYS GLU GLY ILE CYS ASN GLY VAL THR THR ALA
SEQRES 15 A 353 THR PHE CYS GLY THR PRO ASP TYR ILE ALA PRO GLU ILE
SEQRES 16 A 353 LEU GLN GLU MET LEU TYR GLY PRO ALA VAL ASP TRP TRP
SEQRES 17 A 353 ALA MET GLY VAL LEU LEU TYR GLU MET LEU CYS GLY HIS
SEQRES 18 A 353 ALA PRO PHE GLU ALA GLU ASN GLU ASP ASP LEU PHE GLU
SEQRES 19 A 353 ALA ILE LEU ASN ASP GLU VAL VAL TYR PRO THR TRP LEU
SEQRES 20 A 353 HIS GLU ASP ALA THR GLY ILE LEU LYS SER PHE MET THR
SEQRES 21 A 353 LYS ASN PRO THR MET ARG LEU GLY SER LEU THR GLN GLY
SEQRES 22 A 353 GLY GLU HIS ALA ILE LEU ARG HIS PRO PHE PHE LYS GLU
SEQRES 23 A 353 ILE ASP TRP ALA GLN LEU ASN HIS ARG GLN ILE GLU PRO
SEQRES 24 A 353 PRO PHE ARG PRO ARG ILE LYS SER ARG GLU ASP VAL SER
SEQRES 25 A 353 ASN PHE ASP PRO ASP PHE ILE LYS GLU GLU PRO VAL LEU
SEQRES 26 A 353 TPO PRO ILE ASP GLU GLY HIS LEU PRO MET ILE ASN GLN
SEQRES 27 A 353 ASP GLU PHE ARG ASN PHE GLU TYR VAL SER PRO GLU LEU
SEQRES 28 A 353 GLN PRO
MODRES 3TXO TPO A 656 THR PHOSPHOTHREONINE
HET TPO A 656 11
HET 07U A 1 22
HETNAM TPO PHOSPHOTHREONINE
HETNAM 07U 2-METHYL-N~1~-[3-(PYRIDIN-4-YL)-2,6-NAPHTHYRIDIN-1-
HETNAM 2 07U YL]PROPANE-1,2-DIAMINE
HETSYN TPO PHOSPHONOTHREONINE
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 2 07U C17 H19 N5
FORMUL 3 HOH *139(H2 O)
HELIX 1 1 LYS A 388 ASP A 395 1 8
HELIX 2 2 ASP A 396 ALA A 410 1 15
HELIX 3 3 ASP A 440 ARG A 449 1 10
HELIX 4 4 ASP A 452 LYS A 473 1 22
HELIX 5 5 LYS A 481 ASP A 483 5 3
HELIX 6 6 THR A 517 ILE A 521 5 5
HELIX 7 7 ALA A 522 TYR A 531 1 10
HELIX 8 8 PRO A 533 GLY A 550 1 18
HELIX 9 9 ASN A 558 ASP A 569 1 12
HELIX 10 10 HIS A 578 MET A 589 1 12
HELIX 11 11 ASN A 592 ARG A 596 5 5
HELIX 12 12 SER A 599 GLY A 604 5 6
HELIX 13 13 GLU A 605 ARG A 610 1 6
HELIX 14 14 HIS A 611 LYS A 615 5 5
HELIX 15 15 ASP A 618 HIS A 624 1 7
HELIX 16 16 ASP A 645 LYS A 650 1 6
HELIX 17 17 HIS A 662 ILE A 666 5 5
HELIX 18 18 ASN A 667 ARG A 672 5 6
SHEET 1 A 6 PHE A 355 GLY A 364 0
SHEET 2 A 6 GLY A 367 VAL A 374 -1 O VAL A 369 N LEU A 361
SHEET 3 A 6 LEU A 380 LYS A 387 -1 O VAL A 385 N LYS A 368
SHEET 4 A 6 ARG A 428 GLU A 434 -1 O MET A 433 N ALA A 382
SHEET 5 A 6 LEU A 419 GLN A 424 -1 N CYS A 421 O VAL A 432
SHEET 6 A 6 TYR A 676 VAL A 677 -1 O TYR A 676 N CYS A 422
SHEET 1 B 2 VAL A 485 LEU A 487 0
SHEET 2 B 2 CYS A 493 LEU A 495 -1 O LYS A 494 N LEU A 486
LINK C LEU A 655 N TPO A 656 1555 1555 1.33
LINK C TPO A 656 N PRO A 657 1555 1555 1.37
SITE 1 AC1 10 PHE A 366 VAL A 369 ALA A 382 LYS A 384
SITE 2 AC1 10 GLU A 434 VAL A 436 ASP A 440 ASP A 483
SITE 3 AC1 10 LEU A 486 ASP A 497
CRYST1 113.533 56.861 63.367 90.00 90.00 90.00 P 21 21 2 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 0.008808 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017587 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015781 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
