HEADER TRANSFERASE 14-MAY-09 3HGK
TITLE CRYSTAL STRUCTURE OF EFFECT PROTEIN AVRPTOB COMPLEXED WITH KINASE PTO
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN KINASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: PTO, PTO DISEASE RESISTANCE PROTEIN, PTO KINASE,
COMPND 5 SERINE/THREONINE PROTEIN KINASE PTO;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: EFFECTOR PROTEIN HOPAB2;
COMPND 10 CHAIN: E, F, G, H;
COMPND 11 FRAGMENT: UNP RESIDUES 121-205;
COMPND 12 SYNONYM: AVRPTOB, AVIRULENCE PROTEIN AVRPTOB, E3 UBIQUITIN-PROTEIN
COMPND 13 LIGASE;
COMPND 14 EC: 6.3.2.-;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SOLANUM PIMPINELLIFOLIUM;
SOURCE 3 ORGANISM_COMMON: CURRANT TOMATO;
SOURCE 4 ORGANISM_TAXID: 4084;
SOURCE 5 GENE: PTO;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-30A;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: PSEUDOMONAS SYRINGAE PV. TOMATO;
SOURCE 12 ORGANISM_TAXID: 323;
SOURCE 13 GENE: HOPAB2, AVRPTOB, PSPTO_3087;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FIVE HELICES, PTO P+1 LOOP, ATP-BINDING, KINASE, NUCLEOTIDE-BINDING,
KEYWDS 2 SERINE/THREONINE-PROTEIN KINASE, HYPERSENSITIVE RESPONSE
KEYWDS 3 ELICITATION, LIGASE, SECRETED, UBL CONJUGATION, UBL CONJUGATION
KEYWDS 4 PATHWAY, VIRULENCE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.DONG,F.FAN,L.GU,J.CHAI
REVDAT 4 01-NOV-23 3HGK 1 REMARK
REVDAT 3 10-NOV-21 3HGK 1 SEQADV LINK
REVDAT 2 18-AUG-09 3HGK 1 JRNL
REVDAT 1 23-JUN-09 3HGK 0
JRNL AUTH J.DONG,F.XIAO,F.FAN,L.GU,H.CANG,G.B.MARTIN,J.CHAI
JRNL TITL CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN PSEUDOMONAS
JRNL TITL 2 EFFECTOR AVRPTOB AND THE TOMATO PTO KINASE REVEALS BOTH A
JRNL TITL 3 SHARED AND A UNIQUE INTERFACE COMPARED WITH AVRPTO-PTO
JRNL REF PLANT CELL V. 21 1846 2009
JRNL REFN ISSN 1040-4651
JRNL PMID 19509331
JRNL DOI 10.1105/TPC.109.066878
REMARK 2
REMARK 2 RESOLUTION. 3.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 28059
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) : 0.318
REMARK 3 R VALUE (WORKING SET) : 0.317
REMARK 3 FREE R VALUE : 0.331
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1506
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) : 3.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.38
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1976
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.15
REMARK 3 BIN R VALUE (WORKING SET) : 0.4820
REMARK 3 BIN FREE R VALUE SET COUNT : 94
REMARK 3 BIN FREE R VALUE : 0.4620
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11599
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 81.81
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.99000
REMARK 3 B22 (A**2) : 14.94000
REMARK 3 B33 (A**2) : -8.95000
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): 0.714
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.790
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 120.055
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.916
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.907
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11823 ; 0.009 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 15960 ; 1.320 ; 1.961
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1450 ; 4.641 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 576 ;42.746 ;23.611
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2124 ;17.929 ;15.028
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 100 ;16.832 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1763 ; 0.089 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8912 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 6563 ; 0.272 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 8047 ; 0.312 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 511 ; 0.191 ; 0.200
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): 123 ; 0.270 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 4 ; 0.060 ; 0.200
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): 7457 ; 2.485 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11635 ; 3.856 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4856 ; 1.725 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4325 ; 2.401 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 1.10
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3HGK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-MAY-09.
REMARK 100 THE DEPOSITION ID IS D_1000053107.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-JAN-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.9
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI(111) DOUBLE-CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29886
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300
REMARK 200 RESOLUTION RANGE LOW (A) : 99.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.900
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.08100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 5.30
REMARK 200 R MERGE FOR SHELL (I) : 0.53000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: SOLVE, MOLREP
REMARK 200 STARTING MODEL: PDB ENTRIES 3HGL FOR AVRPTOB AND 2QKW FOR PTO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRI-SODIUM CITRATE DIHYDRATE,
REMARK 280 17.5% (W/V) POLYETHYLENE GLYCOL 3350, 0.1MM TRIS-HCL PH 7.9,
REMARK 280 10.0MM PHENOL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 30.53500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 149.43000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.23500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 149.43000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.53500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.23500
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, 3, 4
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: 1790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E
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: 3
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: 1930 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, G
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: 4
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: 1800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, H
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 MET A 1
REMARK 465 GLY A 2
REMARK 465 SER A 3
REMARK 465 LYS A 4
REMARK 465 TYR A 5
REMARK 465 SER A 6
REMARK 465 LYS A 7
REMARK 465 ALA A 8
REMARK 465 THR A 9
REMARK 465 ASN A 10
REMARK 465 SER A 11
REMARK 465 ILE A 12
REMARK 465 ASN A 13
REMARK 465 ASP A 14
REMARK 465 ALA A 15
REMARK 465 LEU A 16
REMARK 465 SER A 17
REMARK 465 SER A 18
REMARK 465 SER A 19
REMARK 465 TYR A 20
REMARK 465 LEU A 21
REMARK 465 VAL A 22
REMARK 465 PRO A 23
REMARK 465 PHE A 24
REMARK 465 GLU A 25
REMARK 465 SER A 26
REMARK 465 TYR A 27
REMARK 465 ARG A 28
REMARK 465 VAL A 29
REMARK 465 PRO A 30
REMARK 465 SER A 319
REMARK 465 VAL A 320
REMARK 465 ILE A 321
REMARK 465 HIS A 322
REMARK 465 HIS A 323
REMARK 465 HIS A 324
REMARK 465 HIS A 325
REMARK 465 HIS A 326
REMARK 465 HIS A 327
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 SER B 3
REMARK 465 LYS B 4
REMARK 465 TYR B 5
REMARK 465 SER B 6
REMARK 465 LYS B 7
REMARK 465 ALA B 8
REMARK 465 THR B 9
REMARK 465 ASN B 10
REMARK 465 SER B 11
REMARK 465 ILE B 12
REMARK 465 ASN B 13
REMARK 465 ASP B 14
REMARK 465 ALA B 15
REMARK 465 LEU B 16
REMARK 465 SER B 17
REMARK 465 SER B 18
REMARK 465 SER B 19
REMARK 465 TYR B 20
REMARK 465 LEU B 21
REMARK 465 VAL B 22
REMARK 465 PRO B 23
REMARK 465 PHE B 24
REMARK 465 GLU B 25
REMARK 465 SER B 26
REMARK 465 TYR B 27
REMARK 465 ARG B 28
REMARK 465 VAL B 29
REMARK 465 PRO B 30
REMARK 465 LEU B 31
REMARK 465 VAL B 320
REMARK 465 ILE B 321
REMARK 465 HIS B 322
REMARK 465 HIS B 323
REMARK 465 HIS B 324
REMARK 465 HIS B 325
REMARK 465 HIS B 326
REMARK 465 HIS B 327
REMARK 465 MET C 1
REMARK 465 GLY C 2
REMARK 465 SER C 3
REMARK 465 LYS C 4
REMARK 465 TYR C 5
REMARK 465 SER C 6
REMARK 465 LYS C 7
REMARK 465 ALA C 8
REMARK 465 THR C 9
REMARK 465 ASN C 10
REMARK 465 SER C 11
REMARK 465 ILE C 12
REMARK 465 ASN C 13
REMARK 465 ASP C 14
REMARK 465 ALA C 15
REMARK 465 LEU C 16
REMARK 465 SER C 17
REMARK 465 SER C 18
REMARK 465 SER C 19
REMARK 465 TYR C 20
REMARK 465 LEU C 21
REMARK 465 VAL C 22
REMARK 465 PRO C 23
REMARK 465 PHE C 24
REMARK 465 GLU C 25
REMARK 465 SER C 26
REMARK 465 TYR C 27
REMARK 465 ARG C 28
REMARK 465 VAL C 29
REMARK 465 PRO C 30
REMARK 465 LEU C 31
REMARK 465 VAL C 32
REMARK 465 SER C 319
REMARK 465 VAL C 320
REMARK 465 ILE C 321
REMARK 465 HIS C 322
REMARK 465 HIS C 323
REMARK 465 HIS C 324
REMARK 465 HIS C 325
REMARK 465 HIS C 326
REMARK 465 HIS C 327
REMARK 465 MET D 1
REMARK 465 GLY D 2
REMARK 465 SER D 3
REMARK 465 LYS D 4
REMARK 465 TYR D 5
REMARK 465 SER D 6
REMARK 465 LYS D 7
REMARK 465 ALA D 8
REMARK 465 THR D 9
REMARK 465 ASN D 10
REMARK 465 SER D 11
REMARK 465 ILE D 12
REMARK 465 ASN D 13
REMARK 465 ASP D 14
REMARK 465 ALA D 15
REMARK 465 LEU D 16
REMARK 465 SER D 17
REMARK 465 SER D 18
REMARK 465 SER D 19
REMARK 465 TYR D 20
REMARK 465 LEU D 21
REMARK 465 VAL D 22
REMARK 465 PRO D 23
REMARK 465 PHE D 24
REMARK 465 GLU D 25
REMARK 465 SER D 26
REMARK 465 TYR D 27
REMARK 465 ARG D 28
REMARK 465 VAL D 29
REMARK 465 PRO D 30
REMARK 465 SER D 319
REMARK 465 VAL D 320
REMARK 465 ILE D 321
REMARK 465 HIS D 322
REMARK 465 HIS D 323
REMARK 465 HIS D 324
REMARK 465 HIS D 325
REMARK 465 HIS D 326
REMARK 465 HIS D 327
REMARK 465 PRO E 121
REMARK 465 ARG E 122
REMARK 465 ARG E 123
REMARK 465 GLN E 201
REMARK 465 GLN E 202
REMARK 465 ALA E 203
REMARK 465 ALA E 204
REMARK 465 SER E 205
REMARK 465 PRO F 121
REMARK 465 ARG F 122
REMARK 465 ARG F 123
REMARK 465 GLN F 201
REMARK 465 GLN F 202
REMARK 465 ALA F 203
REMARK 465 ALA F 204
REMARK 465 SER F 205
REMARK 465 PRO G 121
REMARK 465 ARG G 122
REMARK 465 ARG G 123
REMARK 465 GLN G 201
REMARK 465 GLN G 202
REMARK 465 ALA G 203
REMARK 465 ALA G 204
REMARK 465 SER G 205
REMARK 465 PRO H 121
REMARK 465 ARG H 122
REMARK 465 ARG H 123
REMARK 465 GLN H 201
REMARK 465 GLN H 202
REMARK 465 ALA H 203
REMARK 465 ALA H 204
REMARK 465 SER H 205
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 GLY G 124 C GLY G 124 O -0.112
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 ILE B 47 N - CA - C ANGL. DEV. = 17.4 DEGREES
REMARK 500 GLY G 124 N - CA - C ANGL. DEV. = -18.7 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 LEU A 34 29.94 -155.59
REMARK 500 GLU A 35 59.79 -91.53
REMARK 500 ASN A 39 105.88 14.55
REMARK 500 ASN A 40 -121.48 -84.85
REMARK 500 PHE A 41 -165.79 -101.39
REMARK 500 PHE A 45 113.91 -36.37
REMARK 500 ILE A 47 -86.50 24.11
REMARK 500 LYS A 69 67.87 -102.29
REMARK 500 GLU A 74 76.35 53.35
REMARK 500 SER A 90 1.67 -69.79
REMARK 500 CYS A 92 71.58 -46.89
REMARK 500 ASN A 108 -26.45 66.82
REMARK 500 ARG A 124 -5.71 -57.06
REMARK 500 TYR A 127 -89.54 -145.67
REMARK 500 SER A 129 132.37 163.67
REMARK 500 ASP A 130 -155.50 72.94
REMARK 500 LEU A 131 91.42 79.62
REMARK 500 PRO A 132 -172.25 -62.14
REMARK 500 MET A 134 -136.23 50.02
REMARK 500 SER A 135 -169.49 -113.65
REMARK 500 ARG A 158 42.01 -99.30
REMARK 500 ALA A 159 5.32 49.85
REMARK 500 ARG A 163 -17.83 57.40
REMARK 500 ILE A 170 51.79 -113.17
REMARK 500 LEU A 171 153.07 -36.37
REMARK 500 ASP A 173 -166.32 -109.44
REMARK 500 ASP A 182 81.23 38.32
REMARK 500 GLU A 191 0.44 -59.91
REMARK 500 LEU A 192 77.18 55.80
REMARK 500 HIS A 196 50.40 -118.21
REMARK 500 GLU A 233 -13.81 -46.42
REMARK 500 ALA A 237 4.40 80.67
REMARK 500 SER A 239 32.43 -60.60
REMARK 500 ILE A 241 -61.79 46.88
REMARK 500 SER A 244 50.26 -95.01
REMARK 500 LEU A 245 -49.30 -134.65
REMARK 500 PRO A 246 -167.33 -59.53
REMARK 500 ARG A 247 -135.98 -75.15
REMARK 500 TRP A 255 -72.24 -81.04
REMARK 500 ASN A 262 -72.01 -153.59
REMARK 500 GLN A 264 -0.54 -176.90
REMARK 500 PRO A 271 -145.12 -78.21
REMARK 500 ASN A 272 45.80 -82.96
REMARK 500 ALA A 274 -156.35 66.66
REMARK 500 MET A 303 -2.77 -54.19
REMARK 500 LEU B 34 -27.15 -141.17
REMARK 500 ASN B 39 104.05 15.82
REMARK 500 ASN B 40 -117.68 -78.48
REMARK 500 PHE B 41 -147.00 -99.04
REMARK 500 HIS B 43 97.94 -53.27
REMARK 500
REMARK 500 THIS ENTRY HAS 212 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3HGL RELATED DB: PDB
REMARK 900 AVRPTOB 121-205
DBREF 3HGK A 1 321 UNP Q40234 Q40234_SOLPI 1 321
DBREF 3HGK B 1 321 UNP Q40234 Q40234_SOLPI 1 321
DBREF 3HGK C 1 321 UNP Q40234 Q40234_SOLPI 1 321
DBREF 3HGK D 1 321 UNP Q40234 Q40234_SOLPI 1 321
DBREF 3HGK E 121 205 UNP Q8RSY1 HPAB2_PSESM 121 205
DBREF 3HGK F 121 205 UNP Q8RSY1 HPAB2_PSESM 121 205
DBREF 3HGK G 121 205 UNP Q8RSY1 HPAB2_PSESM 121 205
DBREF 3HGK H 121 205 UNP Q8RSY1 HPAB2_PSESM 121 205
SEQADV 3HGK GLY A 193 UNP Q40234 ASP 193 ENGINEERED MUTATION
SEQADV 3HGK HIS A 322 UNP Q40234 EXPRESSION TAG
SEQADV 3HGK HIS A 323 UNP Q40234 EXPRESSION TAG
SEQADV 3HGK HIS A 324 UNP Q40234 EXPRESSION TAG
SEQADV 3HGK HIS A 325 UNP Q40234 EXPRESSION TAG
SEQADV 3HGK HIS A 326 UNP Q40234 EXPRESSION TAG
SEQADV 3HGK HIS A 327 UNP Q40234 EXPRESSION TAG
SEQADV 3HGK GLY B 193 UNP Q40234 ASP 193 ENGINEERED MUTATION
SEQADV 3HGK HIS B 322 UNP Q40234 EXPRESSION TAG
SEQADV 3HGK HIS B 323 UNP Q40234 EXPRESSION TAG
SEQADV 3HGK HIS B 324 UNP Q40234 EXPRESSION TAG
SEQADV 3HGK HIS B 325 UNP Q40234 EXPRESSION TAG
SEQADV 3HGK HIS B 326 UNP Q40234 EXPRESSION TAG
SEQADV 3HGK HIS B 327 UNP Q40234 EXPRESSION TAG
SEQADV 3HGK GLY C 193 UNP Q40234 ASP 193 ENGINEERED MUTATION
SEQADV 3HGK HIS C 322 UNP Q40234 EXPRESSION TAG
SEQADV 3HGK HIS C 323 UNP Q40234 EXPRESSION TAG
SEQADV 3HGK HIS C 324 UNP Q40234 EXPRESSION TAG
SEQADV 3HGK HIS C 325 UNP Q40234 EXPRESSION TAG
SEQADV 3HGK HIS C 326 UNP Q40234 EXPRESSION TAG
SEQADV 3HGK HIS C 327 UNP Q40234 EXPRESSION TAG
SEQADV 3HGK GLY D 193 UNP Q40234 ASP 193 ENGINEERED MUTATION
SEQADV 3HGK HIS D 322 UNP Q40234 EXPRESSION TAG
SEQADV 3HGK HIS D 323 UNP Q40234 EXPRESSION TAG
SEQADV 3HGK HIS D 324 UNP Q40234 EXPRESSION TAG
SEQADV 3HGK HIS D 325 UNP Q40234 EXPRESSION TAG
SEQADV 3HGK HIS D 326 UNP Q40234 EXPRESSION TAG
SEQADV 3HGK HIS D 327 UNP Q40234 EXPRESSION TAG
SEQRES 1 A 327 MET GLY SER LYS TYR SER LYS ALA THR ASN SER ILE ASN
SEQRES 2 A 327 ASP ALA LEU SER SER SER TYR LEU VAL PRO PHE GLU SER
SEQRES 3 A 327 TYR ARG VAL PRO LEU VAL ASP LEU GLU GLU ALA THR ASN
SEQRES 4 A 327 ASN PHE ASP HIS LYS PHE LEU ILE GLY HIS GLY VAL PHE
SEQRES 5 A 327 GLY LYS VAL TYR LYS GLY VAL LEU ARG ASP GLY ALA LYS
SEQRES 6 A 327 VAL ALA LEU LYS ARG ARG THR PRO GLU SER SER GLN GLY
SEQRES 7 A 327 ILE GLU GLU PHE GLU THR GLU ILE GLU THR LEU SER PHE
SEQRES 8 A 327 CYS ARG HIS PRO HIS LEU VAL SER LEU ILE GLY PHE CYS
SEQRES 9 A 327 ASP GLU ARG ASN GLU MET ILE LEU ILE TYR LYS TYR MET
SEQRES 10 A 327 GLU ASN GLY ASN LEU LYS ARG HIS LEU TYR GLY SER ASP
SEQRES 11 A 327 LEU PRO THR MET SER MET SER TRP GLU GLN ARG LEU GLU
SEQRES 12 A 327 ILE CYS ILE GLY ALA ALA ARG GLY LEU HIS TYR LEU HIS
SEQRES 13 A 327 THR ARG ALA ILE ILE HIS ARG ASP VAL LYS SER ILE ASN
SEQRES 14 A 327 ILE LEU LEU ASP GLU ASN PHE VAL PRO LYS ILE THR ASP
SEQRES 15 A 327 PHE GLY ILE SER LYS LYS GLY THR GLU LEU GLY GLN THR
SEQRES 16 A 327 HIS LEU SEP TPO VAL VAL LYS GLY THR LEU GLY TYR ILE
SEQRES 17 A 327 ASP PRO GLU TYR PHE ILE LYS GLY ARG LEU THR GLU LYS
SEQRES 18 A 327 SER ASP VAL TYR SER PHE GLY VAL VAL LEU PHE GLU VAL
SEQRES 19 A 327 LEU CYS ALA ARG SER ALA ILE VAL GLN SER LEU PRO ARG
SEQRES 20 A 327 GLU MET VAL ASN LEU ALA GLU TRP ALA VAL GLU SER HIS
SEQRES 21 A 327 ASN ASN GLY GLN LEU GLU GLN ILE VAL ASP PRO ASN LEU
SEQRES 22 A 327 ALA ASP LYS ILE ARG PRO GLU SER LEU ARG LYS PHE GLY
SEQRES 23 A 327 ASP THR ALA VAL LYS CYS LEU ALA LEU SER SER GLU ASP
SEQRES 24 A 327 ARG PRO SER MET GLY ASP VAL LEU TRP LYS LEU GLU TYR
SEQRES 25 A 327 ALA LEU ARG LEU GLN GLU SER VAL ILE HIS HIS HIS HIS
SEQRES 26 A 327 HIS HIS
SEQRES 1 B 327 MET GLY SER LYS TYR SER LYS ALA THR ASN SER ILE ASN
SEQRES 2 B 327 ASP ALA LEU SER SER SER TYR LEU VAL PRO PHE GLU SER
SEQRES 3 B 327 TYR ARG VAL PRO LEU VAL ASP LEU GLU GLU ALA THR ASN
SEQRES 4 B 327 ASN PHE ASP HIS LYS PHE LEU ILE GLY HIS GLY VAL PHE
SEQRES 5 B 327 GLY LYS VAL TYR LYS GLY VAL LEU ARG ASP GLY ALA LYS
SEQRES 6 B 327 VAL ALA LEU LYS ARG ARG THR PRO GLU SER SER GLN GLY
SEQRES 7 B 327 ILE GLU GLU PHE GLU THR GLU ILE GLU THR LEU SER PHE
SEQRES 8 B 327 CYS ARG HIS PRO HIS LEU VAL SER LEU ILE GLY PHE CYS
SEQRES 9 B 327 ASP GLU ARG ASN GLU MET ILE LEU ILE TYR LYS TYR MET
SEQRES 10 B 327 GLU ASN GLY ASN LEU LYS ARG HIS LEU TYR GLY SER ASP
SEQRES 11 B 327 LEU PRO THR MET SER MET SER TRP GLU GLN ARG LEU GLU
SEQRES 12 B 327 ILE CYS ILE GLY ALA ALA ARG GLY LEU HIS TYR LEU HIS
SEQRES 13 B 327 THR ARG ALA ILE ILE HIS ARG ASP VAL LYS SER ILE ASN
SEQRES 14 B 327 ILE LEU LEU ASP GLU ASN PHE VAL PRO LYS ILE THR ASP
SEQRES 15 B 327 PHE GLY ILE SER LYS LYS GLY THR GLU LEU GLY GLN THR
SEQRES 16 B 327 HIS LEU SEP TPO VAL VAL LYS GLY THR LEU GLY TYR ILE
SEQRES 17 B 327 ASP PRO GLU TYR PHE ILE LYS GLY ARG LEU THR GLU LYS
SEQRES 18 B 327 SER ASP VAL TYR SER PHE GLY VAL VAL LEU PHE GLU VAL
SEQRES 19 B 327 LEU CYS ALA ARG SER ALA ILE VAL GLN SER LEU PRO ARG
SEQRES 20 B 327 GLU MET VAL ASN LEU ALA GLU TRP ALA VAL GLU SER HIS
SEQRES 21 B 327 ASN ASN GLY GLN LEU GLU GLN ILE VAL ASP PRO ASN LEU
SEQRES 22 B 327 ALA ASP LYS ILE ARG PRO GLU SER LEU ARG LYS PHE GLY
SEQRES 23 B 327 ASP THR ALA VAL LYS CYS LEU ALA LEU SER SER GLU ASP
SEQRES 24 B 327 ARG PRO SER MET GLY ASP VAL LEU TRP LYS LEU GLU TYR
SEQRES 25 B 327 ALA LEU ARG LEU GLN GLU SER VAL ILE HIS HIS HIS HIS
SEQRES 26 B 327 HIS HIS
SEQRES 1 C 327 MET GLY SER LYS TYR SER LYS ALA THR ASN SER ILE ASN
SEQRES 2 C 327 ASP ALA LEU SER SER SER TYR LEU VAL PRO PHE GLU SER
SEQRES 3 C 327 TYR ARG VAL PRO LEU VAL ASP LEU GLU GLU ALA THR ASN
SEQRES 4 C 327 ASN PHE ASP HIS LYS PHE LEU ILE GLY HIS GLY VAL PHE
SEQRES 5 C 327 GLY LYS VAL TYR LYS GLY VAL LEU ARG ASP GLY ALA LYS
SEQRES 6 C 327 VAL ALA LEU LYS ARG ARG THR PRO GLU SER SER GLN GLY
SEQRES 7 C 327 ILE GLU GLU PHE GLU THR GLU ILE GLU THR LEU SER PHE
SEQRES 8 C 327 CYS ARG HIS PRO HIS LEU VAL SER LEU ILE GLY PHE CYS
SEQRES 9 C 327 ASP GLU ARG ASN GLU MET ILE LEU ILE TYR LYS TYR MET
SEQRES 10 C 327 GLU ASN GLY ASN LEU LYS ARG HIS LEU TYR GLY SER ASP
SEQRES 11 C 327 LEU PRO THR MET SER MET SER TRP GLU GLN ARG LEU GLU
SEQRES 12 C 327 ILE CYS ILE GLY ALA ALA ARG GLY LEU HIS TYR LEU HIS
SEQRES 13 C 327 THR ARG ALA ILE ILE HIS ARG ASP VAL LYS SER ILE ASN
SEQRES 14 C 327 ILE LEU LEU ASP GLU ASN PHE VAL PRO LYS ILE THR ASP
SEQRES 15 C 327 PHE GLY ILE SER LYS LYS GLY THR GLU LEU GLY GLN THR
SEQRES 16 C 327 HIS LEU SEP TPO VAL VAL LYS GLY THR LEU GLY TYR ILE
SEQRES 17 C 327 ASP PRO GLU TYR PHE ILE LYS GLY ARG LEU THR GLU LYS
SEQRES 18 C 327 SER ASP VAL TYR SER PHE GLY VAL VAL LEU PHE GLU VAL
SEQRES 19 C 327 LEU CYS ALA ARG SER ALA ILE VAL GLN SER LEU PRO ARG
SEQRES 20 C 327 GLU MET VAL ASN LEU ALA GLU TRP ALA VAL GLU SER HIS
SEQRES 21 C 327 ASN ASN GLY GLN LEU GLU GLN ILE VAL ASP PRO ASN LEU
SEQRES 22 C 327 ALA ASP LYS ILE ARG PRO GLU SER LEU ARG LYS PHE GLY
SEQRES 23 C 327 ASP THR ALA VAL LYS CYS LEU ALA LEU SER SER GLU ASP
SEQRES 24 C 327 ARG PRO SER MET GLY ASP VAL LEU TRP LYS LEU GLU TYR
SEQRES 25 C 327 ALA LEU ARG LEU GLN GLU SER VAL ILE HIS HIS HIS HIS
SEQRES 26 C 327 HIS HIS
SEQRES 1 D 327 MET GLY SER LYS TYR SER LYS ALA THR ASN SER ILE ASN
SEQRES 2 D 327 ASP ALA LEU SER SER SER TYR LEU VAL PRO PHE GLU SER
SEQRES 3 D 327 TYR ARG VAL PRO LEU VAL ASP LEU GLU GLU ALA THR ASN
SEQRES 4 D 327 ASN PHE ASP HIS LYS PHE LEU ILE GLY HIS GLY VAL PHE
SEQRES 5 D 327 GLY LYS VAL TYR LYS GLY VAL LEU ARG ASP GLY ALA LYS
SEQRES 6 D 327 VAL ALA LEU LYS ARG ARG THR PRO GLU SER SER GLN GLY
SEQRES 7 D 327 ILE GLU GLU PHE GLU THR GLU ILE GLU THR LEU SER PHE
SEQRES 8 D 327 CYS ARG HIS PRO HIS LEU VAL SER LEU ILE GLY PHE CYS
SEQRES 9 D 327 ASP GLU ARG ASN GLU MET ILE LEU ILE TYR LYS TYR MET
SEQRES 10 D 327 GLU ASN GLY ASN LEU LYS ARG HIS LEU TYR GLY SER ASP
SEQRES 11 D 327 LEU PRO THR MET SER MET SER TRP GLU GLN ARG LEU GLU
SEQRES 12 D 327 ILE CYS ILE GLY ALA ALA ARG GLY LEU HIS TYR LEU HIS
SEQRES 13 D 327 THR ARG ALA ILE ILE HIS ARG ASP VAL LYS SER ILE ASN
SEQRES 14 D 327 ILE LEU LEU ASP GLU ASN PHE VAL PRO LYS ILE THR ASP
SEQRES 15 D 327 PHE GLY ILE SER LYS LYS GLY THR GLU LEU GLY GLN THR
SEQRES 16 D 327 HIS LEU SEP TPO VAL VAL LYS GLY THR LEU GLY TYR ILE
SEQRES 17 D 327 ASP PRO GLU TYR PHE ILE LYS GLY ARG LEU THR GLU LYS
SEQRES 18 D 327 SER ASP VAL TYR SER PHE GLY VAL VAL LEU PHE GLU VAL
SEQRES 19 D 327 LEU CYS ALA ARG SER ALA ILE VAL GLN SER LEU PRO ARG
SEQRES 20 D 327 GLU MET VAL ASN LEU ALA GLU TRP ALA VAL GLU SER HIS
SEQRES 21 D 327 ASN ASN GLY GLN LEU GLU GLN ILE VAL ASP PRO ASN LEU
SEQRES 22 D 327 ALA ASP LYS ILE ARG PRO GLU SER LEU ARG LYS PHE GLY
SEQRES 23 D 327 ASP THR ALA VAL LYS CYS LEU ALA LEU SER SER GLU ASP
SEQRES 24 D 327 ARG PRO SER MET GLY ASP VAL LEU TRP LYS LEU GLU TYR
SEQRES 25 D 327 ALA LEU ARG LEU GLN GLU SER VAL ILE HIS HIS HIS HIS
SEQRES 26 D 327 HIS HIS
SEQRES 1 E 85 PRO ARG ARG GLY ALA VAL ALA HIS ALA ASN SER ILE VAL
SEQRES 2 E 85 GLN GLN LEU VAL SER GLU GLY ALA ASP ILE SER HIS THR
SEQRES 3 E 85 ARG ASN MET LEU ARG ASN ALA MET ASN GLY ASP ALA VAL
SEQRES 4 E 85 ALA PHE SER ARG VAL GLU GLN ASN ILE PHE ARG GLN HIS
SEQRES 5 E 85 PHE PRO ASN MET PRO MET HIS GLY ILE SER ARG ASP SER
SEQRES 6 E 85 GLU LEU ALA ILE GLU LEU ARG GLY ALA LEU ARG ARG ALA
SEQRES 7 E 85 VAL HIS GLN GLN ALA ALA SER
SEQRES 1 F 85 PRO ARG ARG GLY ALA VAL ALA HIS ALA ASN SER ILE VAL
SEQRES 2 F 85 GLN GLN LEU VAL SER GLU GLY ALA ASP ILE SER HIS THR
SEQRES 3 F 85 ARG ASN MET LEU ARG ASN ALA MET ASN GLY ASP ALA VAL
SEQRES 4 F 85 ALA PHE SER ARG VAL GLU GLN ASN ILE PHE ARG GLN HIS
SEQRES 5 F 85 PHE PRO ASN MET PRO MET HIS GLY ILE SER ARG ASP SER
SEQRES 6 F 85 GLU LEU ALA ILE GLU LEU ARG GLY ALA LEU ARG ARG ALA
SEQRES 7 F 85 VAL HIS GLN GLN ALA ALA SER
SEQRES 1 G 85 PRO ARG ARG GLY ALA VAL ALA HIS ALA ASN SER ILE VAL
SEQRES 2 G 85 GLN GLN LEU VAL SER GLU GLY ALA ASP ILE SER HIS THR
SEQRES 3 G 85 ARG ASN MET LEU ARG ASN ALA MET ASN GLY ASP ALA VAL
SEQRES 4 G 85 ALA PHE SER ARG VAL GLU GLN ASN ILE PHE ARG GLN HIS
SEQRES 5 G 85 PHE PRO ASN MET PRO MET HIS GLY ILE SER ARG ASP SER
SEQRES 6 G 85 GLU LEU ALA ILE GLU LEU ARG GLY ALA LEU ARG ARG ALA
SEQRES 7 G 85 VAL HIS GLN GLN ALA ALA SER
SEQRES 1 H 85 PRO ARG ARG GLY ALA VAL ALA HIS ALA ASN SER ILE VAL
SEQRES 2 H 85 GLN GLN LEU VAL SER GLU GLY ALA ASP ILE SER HIS THR
SEQRES 3 H 85 ARG ASN MET LEU ARG ASN ALA MET ASN GLY ASP ALA VAL
SEQRES 4 H 85 ALA PHE SER ARG VAL GLU GLN ASN ILE PHE ARG GLN HIS
SEQRES 5 H 85 PHE PRO ASN MET PRO MET HIS GLY ILE SER ARG ASP SER
SEQRES 6 H 85 GLU LEU ALA ILE GLU LEU ARG GLY ALA LEU ARG ARG ALA
SEQRES 7 H 85 VAL HIS GLN GLN ALA ALA SER
MODRES 3HGK SEP A 198 SER PHOSPHOSERINE
MODRES 3HGK TPO A 199 THR PHOSPHOTHREONINE
MODRES 3HGK SEP B 198 SER PHOSPHOSERINE
MODRES 3HGK TPO B 199 THR PHOSPHOTHREONINE
MODRES 3HGK SEP C 198 SER PHOSPHOSERINE
MODRES 3HGK TPO C 199 THR PHOSPHOTHREONINE
MODRES 3HGK SEP D 198 SER PHOSPHOSERINE
MODRES 3HGK TPO D 199 THR PHOSPHOTHREONINE
HET SEP A 198 10
HET TPO A 199 11
HET SEP B 198 10
HET TPO B 199 11
HET SEP C 198 10
HET TPO C 199 11
HET SEP D 198 10
HET TPO D 199 11
HETNAM SEP PHOSPHOSERINE
HETNAM TPO PHOSPHOTHREONINE
HETSYN SEP PHOSPHONOSERINE
HETSYN TPO PHOSPHONOTHREONINE
FORMUL 1 SEP 4(C3 H8 N O6 P)
FORMUL 1 TPO 4(C4 H10 N O6 P)
HELIX 1 1 GLN A 77 THR A 88 1 12
HELIX 2 2 ASP A 105 GLU A 109 5 5
HELIX 3 3 LEU A 122 LEU A 126 5 5
HELIX 4 4 TRP A 138 ARG A 158 1 21
HELIX 5 5 LYS A 166 ILE A 170 5 5
HELIX 6 6 ASP A 209 GLY A 216 1 8
HELIX 7 7 LYS A 221 CYS A 236 1 16
HELIX 8 8 ASN A 251 ASN A 261 1 11
HELIX 9 9 ARG A 278 LEU A 293 1 16
HELIX 10 10 SER A 296 ARG A 300 5 5
HELIX 11 11 SER A 302 GLU A 318 1 17
HELIX 12 12 ILE B 79 PHE B 91 1 13
HELIX 13 13 ASP B 105 GLU B 109 5 5
HELIX 14 14 LEU B 122 TYR B 127 1 6
HELIX 15 15 SER B 137 THR B 157 1 21
HELIX 16 16 LYS B 166 ILE B 168 5 3
HELIX 17 17 ASP B 209 GLY B 216 1 8
HELIX 18 18 LYS B 221 ALA B 237 1 17
HELIX 19 19 ASN B 251 HIS B 260 1 10
HELIX 20 20 ARG B 278 ALA B 294 1 17
HELIX 21 21 SER B 296 ARG B 300 5 5
HELIX 22 22 SER B 302 SER B 319 1 18
HELIX 23 23 GLN C 77 PHE C 91 1 15
HELIX 24 24 ASP C 105 GLU C 109 5 5
HELIX 25 25 LEU C 122 TYR C 127 1 6
HELIX 26 26 SER C 137 THR C 157 1 21
HELIX 27 27 LYS C 166 ILE C 168 5 3
HELIX 28 28 ASP C 209 GLY C 216 1 8
HELIX 29 29 LYS C 221 ALA C 237 1 17
HELIX 30 30 ASN C 251 ASN C 261 1 11
HELIX 31 31 ARG C 278 LEU C 293 1 16
HELIX 32 32 SER C 296 ARG C 300 5 5
HELIX 33 33 SER C 302 GLU C 318 1 17
HELIX 34 34 GLN D 77 THR D 88 1 12
HELIX 35 35 ASP D 105 GLU D 109 5 5
HELIX 36 36 LEU D 122 TYR D 127 1 6
HELIX 37 37 SER D 137 ARG D 158 1 22
HELIX 38 38 ASP D 209 GLY D 216 1 8
HELIX 39 39 GLU D 220 CYS D 236 1 17
HELIX 40 40 ASN D 251 ASN D 261 1 11
HELIX 41 41 ARG D 278 CYS D 292 1 15
HELIX 42 42 SER D 296 ARG D 300 5 5
HELIX 43 43 SER D 302 LEU D 316 1 15
HELIX 44 44 ALA E 125 GLU E 139 1 15
HELIX 45 45 ASP E 142 GLY E 156 1 15
HELIX 46 46 SER E 162 PHE E 173 1 12
HELIX 47 47 SER E 185 HIS E 200 1 16
HELIX 48 48 ALA F 125 GLU F 139 1 15
HELIX 49 49 ASP F 142 GLY F 156 1 15
HELIX 50 50 SER F 162 PHE F 173 1 12
HELIX 51 51 SER F 185 HIS F 200 1 16
HELIX 52 52 ALA G 125 GLU G 139 1 15
HELIX 53 53 ASP G 142 GLY G 156 1 15
HELIX 54 54 SER G 162 PHE G 173 1 12
HELIX 55 55 SER G 185 HIS G 200 1 16
HELIX 56 56 ALA H 125 GLU H 139 1 15
HELIX 57 57 ASP H 142 GLY H 156 1 15
HELIX 58 58 SER H 162 PHE H 173 1 12
HELIX 59 59 SER H 185 HIS H 200 1 16
SHEET 1 A 2 HIS A 49 GLY A 50 0
SHEET 2 A 2 GLY A 53 LYS A 54 -1 O GLY A 53 N GLY A 50
SHEET 1 B 4 TYR A 56 VAL A 59 0
SHEET 2 B 4 LYS A 65 LEU A 68 -1 O LEU A 68 N TYR A 56
SHEET 3 B 4 ILE A 111 LYS A 115 -1 O TYR A 114 N ALA A 67
SHEET 4 B 4 LEU A 100 CYS A 104 -1 N ILE A 101 O ILE A 113
SHEET 1 C 2 ILE A 160 ILE A 161 0
SHEET 2 C 2 LYS A 187 LYS A 188 -1 O LYS A 187 N ILE A 161
SHEET 1 D 2 GLY B 48 GLY B 50 0
SHEET 2 D 2 GLY B 53 VAL B 55 -1 O GLY B 53 N GLY B 50
SHEET 1 E 3 VAL B 66 LYS B 69 0
SHEET 2 E 3 ILE B 111 LYS B 115 -1 O LEU B 112 N LYS B 69
SHEET 3 E 3 LEU B 100 CYS B 104 -1 N GLY B 102 O ILE B 113
SHEET 1 F 2 ILE B 160 ILE B 161 0
SHEET 2 F 2 LYS B 187 LYS B 188 -1 O LYS B 187 N ILE B 161
SHEET 1 G 2 ILE B 170 LEU B 172 0
SHEET 2 G 2 PRO B 178 ILE B 180 -1 O LYS B 179 N LEU B 171
SHEET 1 H 2 HIS B 196 LEU B 197 0
SHEET 2 H 2 LEU B 218 THR B 219 -1 O LEU B 218 N LEU B 197
SHEET 1 I 2 GLY B 203 THR B 204 0
SHEET 2 I 2 ALA E 158 VAL E 159 -1 O VAL E 159 N GLY B 203
SHEET 1 J 5 GLY C 48 GLY C 50 0
SHEET 2 J 5 GLY C 53 VAL C 59 -1 O GLY C 53 N GLY C 50
SHEET 3 J 5 LYS C 65 ARG C 70 -1 O LEU C 68 N TYR C 56
SHEET 4 J 5 ILE C 111 LYS C 115 -1 O TYR C 114 N ALA C 67
SHEET 5 J 5 LEU C 100 CYS C 104 -1 N CYS C 104 O ILE C 111
SHEET 1 K 2 ILE C 160 ILE C 161 0
SHEET 2 K 2 LYS C 187 LYS C 188 -1 O LYS C 187 N ILE C 161
SHEET 1 L 2 ILE C 170 LEU C 172 0
SHEET 2 L 2 PRO C 178 ILE C 180 -1 O LYS C 179 N LEU C 171
SHEET 1 M 2 HIS C 196 LEU C 197 0
SHEET 2 M 2 LEU C 218 THR C 219 -1 O LEU C 218 N LEU C 197
SHEET 1 N 2 GLY C 203 THR C 204 0
SHEET 2 N 2 ALA G 158 VAL G 159 -1 O VAL G 159 N GLY C 203
SHEET 1 O 5 GLY D 48 GLY D 50 0
SHEET 2 O 5 GLY D 53 VAL D 59 -1 O GLY D 53 N GLY D 50
SHEET 3 O 5 LYS D 65 ARG D 70 -1 O ARG D 70 N LYS D 54
SHEET 4 O 5 LEU D 112 LYS D 115 -1 O TYR D 114 N ALA D 67
SHEET 5 O 5 LEU D 100 PHE D 103 -1 N GLY D 102 O ILE D 113
SHEET 1 P 2 ILE D 170 LEU D 172 0
SHEET 2 P 2 PRO D 178 ILE D 180 -1 O LYS D 179 N LEU D 171
LINK C LEU A 197 N SEP A 198 1555 1555 1.34
LINK C SEP A 198 N TPO A 199 1555 1555 1.34
LINK C TPO A 199 N VAL A 200 1555 1555 1.34
LINK C LEU B 197 N SEP B 198 1555 1555 1.34
LINK C SEP B 198 N TPO B 199 1555 1555 1.34
LINK C TPO B 199 N VAL B 200 1555 1555 1.33
LINK C LEU C 197 N SEP C 198 1555 1555 1.34
LINK C SEP C 198 N TPO C 199 1555 1555 1.33
LINK C TPO C 199 N VAL C 200 1555 1555 1.33
LINK C LEU D 197 N SEP D 198 1555 1555 1.34
LINK C SEP D 198 N TPO D 199 1555 1555 1.34
LINK C TPO D 199 N VAL D 200 1555 1555 1.34
CRYST1 61.070 104.470 298.860 90.00 90.00 90.00 P 21 21 21 16
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 0.016375 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009572 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003346 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
