HEADER TRANSFERASE 06-JUN-14 4UOO
TITLE STRUCTURE OF LIPOTEICHOIC ACID SYNTHASE LTAS FROM LISTERIA
TITLE 2 MONOCYTOGENES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPOTEICHOIC ACID SYNTHASE;
COMPND 3 CHAIN: A, B, C, D, E;
COMPND 4 FRAGMENT: EXTRACELLULAR CATALYTIC DOMAIN, RESIDUES 226-653;
COMPND 5 SYNONYM: LMO0927 PROTEIN;
COMPND 6 EC: 2.7.8.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LISTERIA MONOCYTOGENES;
SOURCE 3 ORGANISM_TAXID: 169963;
SOURCE 4 STRAIN: EGD-E;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: ROSETTA
KEYWDS TRANSFERASE, LIPOTEICHOIC ACID SYNTHESIS, CELL WALL, GRAM POSITIVE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.CAMPEOTTO,P.FREEMONT,A.GRUNDLING
REVDAT 5 10-JAN-24 4UOO 1 REMARK LINK
REVDAT 4 28-FEB-18 4UOO 1 JRNL
REVDAT 3 22-OCT-14 4UOO 1 JRNL
REVDAT 2 03-SEP-14 4UOO 1 REMARK
REVDAT 1 27-AUG-14 4UOO 0
JRNL AUTH I.CAMPEOTTO,M.G.PERCY,J.T.MACDONALD,A.FORSTER,P.S.FREEMONT,
JRNL AUTH 2 A.GRUNDLING
JRNL TITL STRUCTURAL AND MECHANISTIC INSIGHT INTO THE LISTERIA
JRNL TITL 2 MONOCYTOGENES TWO-ENZYME LIPOTEICHOIC ACID SYNTHESIS SYSTEM.
JRNL REF J. BIOL. CHEM. V. 289 28054 2014
JRNL REFN ESSN 1083-351X
JRNL PMID 25128528
JRNL DOI 10.1074/JBC.M114.590570
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0071
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 108.88
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.7
REMARK 3 NUMBER OF REFLECTIONS : 60591
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) : 0.224
REMARK 3 R VALUE (WORKING SET) : 0.222
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3201
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) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4057
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.30
REMARK 3 BIN R VALUE (WORKING SET) : 0.3190
REMARK 3 BIN FREE R VALUE SET COUNT : 212
REMARK 3 BIN FREE R VALUE : 0.3760
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 16740
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
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) : 49.48
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.17000
REMARK 3 B22 (A**2) : 1.17000
REMARK 3 B33 (A**2) : -2.34000
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): 0.431
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.906
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.875
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 17170 ; 0.004 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 15510 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 23245 ; 0.790 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): 35875 ; 3.575 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2070 ; 4.285 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 890 ;36.055 ;25.562
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2860 ;12.980 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;16.485 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2415 ; 0.030 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 19825 ; 0.002 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 4110 ; 0.003 ; 0.020
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): 8295 ; 5.176 ; 4.958
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 8294 ; 5.174 ; 4.958
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10360 ; 7.252 ; 7.425
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 8875 ; 6.701 ; 5.093
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D E
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 230 A 644 1
REMARK 3 1 B 230 B 644 1
REMARK 3 1 C 230 C 644 1
REMARK 3 1 D 230 D 644 1
REMARK 3 1 E 230 E 644 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 1 A (A**2): 6450 ; 8.34 ; 0.50
REMARK 3 TIGHT THERMAL 1 B (A**2): 6450 ; 11.56 ; 0.50
REMARK 3 TIGHT THERMAL 1 C (A**2): 6450 ; 6.65 ; 0.50
REMARK 3 TIGHT THERMAL 1 D (A**2): 6450 ; 11.34 ; 0.50
REMARK 3 TIGHT THERMAL 1 E (A**2): 6450 ; 7.47 ; 0.50
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 : 1.20
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. U VALUES REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4UOO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-JUN-14.
REMARK 100 THE DEPOSITION ID IS D_1290060889.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JUL-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I24
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
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 : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63877
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 106.880
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.7
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.56000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: BALBES
REMARK 200 STARTING MODEL: PDB ENTRY 2W8D
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.64M NA ACETATE PH 4.6, 4% PEG3350,
REMARK 280 100 MM MGCL2
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 236.95500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 59.88000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 59.88000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 118.47750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 59.88000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 59.88000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 355.43250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 59.88000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 59.88000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 118.47750
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 59.88000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 59.88000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 355.43250
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 236.95500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 195
REMARK 465 SER A 196
REMARK 465 TYR A 197
REMARK 465 TYR A 198
REMARK 465 HIS A 199
REMARK 465 HIS A 200
REMARK 465 HIS A 201
REMARK 465 HIS A 202
REMARK 465 HIS A 203
REMARK 465 HIS A 204
REMARK 465 ASP A 205
REMARK 465 TYR A 206
REMARK 465 ASP A 207
REMARK 465 ILE A 208
REMARK 465 PRO A 209
REMARK 465 THR A 210
REMARK 465 THR A 211
REMARK 465 GLU A 212
REMARK 465 ASN A 213
REMARK 465 LEU A 214
REMARK 465 TYR A 215
REMARK 465 PHE A 216
REMARK 465 GLN A 217
REMARK 465 GLY A 218
REMARK 465 ALA A 219
REMARK 465 MET A 220
REMARK 465 GLY A 221
REMARK 465 SER A 222
REMARK 465 GLY A 223
REMARK 465 ILE A 224
REMARK 465 GLN A 225
REMARK 465 ASP A 226
REMARK 465 SER A 227
REMARK 465 SER A 228
REMARK 465 ASP A 229
REMARK 465 LYS A 645
REMARK 465 LYS A 646
REMARK 465 SER A 647
REMARK 465 THR A 648
REMARK 465 ASP A 649
REMARK 465 SER A 650
REMARK 465 SER A 651
REMARK 465 ASP A 652
REMARK 465 LYS A 653
REMARK 465 MET B 195
REMARK 465 SER B 196
REMARK 465 TYR B 197
REMARK 465 TYR B 198
REMARK 465 HIS B 199
REMARK 465 HIS B 200
REMARK 465 HIS B 201
REMARK 465 HIS B 202
REMARK 465 HIS B 203
REMARK 465 HIS B 204
REMARK 465 ASP B 205
REMARK 465 TYR B 206
REMARK 465 ASP B 207
REMARK 465 ILE B 208
REMARK 465 PRO B 209
REMARK 465 THR B 210
REMARK 465 THR B 211
REMARK 465 GLU B 212
REMARK 465 ASN B 213
REMARK 465 LEU B 214
REMARK 465 TYR B 215
REMARK 465 PHE B 216
REMARK 465 GLN B 217
REMARK 465 GLY B 218
REMARK 465 ALA B 219
REMARK 465 MET B 220
REMARK 465 GLY B 221
REMARK 465 SER B 222
REMARK 465 GLY B 223
REMARK 465 ILE B 224
REMARK 465 GLN B 225
REMARK 465 ASP B 226
REMARK 465 SER B 227
REMARK 465 SER B 228
REMARK 465 ASP B 229
REMARK 465 LYS B 645
REMARK 465 LYS B 646
REMARK 465 SER B 647
REMARK 465 THR B 648
REMARK 465 ASP B 649
REMARK 465 SER B 650
REMARK 465 SER B 651
REMARK 465 ASP B 652
REMARK 465 LYS B 653
REMARK 465 MET C 195
REMARK 465 SER C 196
REMARK 465 TYR C 197
REMARK 465 TYR C 198
REMARK 465 HIS C 199
REMARK 465 HIS C 200
REMARK 465 HIS C 201
REMARK 465 HIS C 202
REMARK 465 HIS C 203
REMARK 465 HIS C 204
REMARK 465 ASP C 205
REMARK 465 TYR C 206
REMARK 465 ASP C 207
REMARK 465 ILE C 208
REMARK 465 PRO C 209
REMARK 465 THR C 210
REMARK 465 THR C 211
REMARK 465 GLU C 212
REMARK 465 ASN C 213
REMARK 465 LEU C 214
REMARK 465 TYR C 215
REMARK 465 PHE C 216
REMARK 465 GLN C 217
REMARK 465 GLY C 218
REMARK 465 ALA C 219
REMARK 465 MET C 220
REMARK 465 GLY C 221
REMARK 465 SER C 222
REMARK 465 GLY C 223
REMARK 465 ILE C 224
REMARK 465 GLN C 225
REMARK 465 ASP C 226
REMARK 465 SER C 227
REMARK 465 SER C 228
REMARK 465 ASP C 229
REMARK 465 LYS C 645
REMARK 465 LYS C 646
REMARK 465 SER C 647
REMARK 465 THR C 648
REMARK 465 ASP C 649
REMARK 465 SER C 650
REMARK 465 SER C 651
REMARK 465 ASP C 652
REMARK 465 LYS C 653
REMARK 465 MET D 195
REMARK 465 SER D 196
REMARK 465 TYR D 197
REMARK 465 TYR D 198
REMARK 465 HIS D 199
REMARK 465 HIS D 200
REMARK 465 HIS D 201
REMARK 465 HIS D 202
REMARK 465 HIS D 203
REMARK 465 HIS D 204
REMARK 465 ASP D 205
REMARK 465 TYR D 206
REMARK 465 ASP D 207
REMARK 465 ILE D 208
REMARK 465 PRO D 209
REMARK 465 THR D 210
REMARK 465 THR D 211
REMARK 465 GLU D 212
REMARK 465 ASN D 213
REMARK 465 LEU D 214
REMARK 465 TYR D 215
REMARK 465 PHE D 216
REMARK 465 GLN D 217
REMARK 465 GLY D 218
REMARK 465 ALA D 219
REMARK 465 MET D 220
REMARK 465 GLY D 221
REMARK 465 SER D 222
REMARK 465 GLY D 223
REMARK 465 ILE D 224
REMARK 465 GLN D 225
REMARK 465 ASP D 226
REMARK 465 SER D 227
REMARK 465 SER D 228
REMARK 465 ASP D 229
REMARK 465 LYS D 645
REMARK 465 LYS D 646
REMARK 465 SER D 647
REMARK 465 THR D 648
REMARK 465 ASP D 649
REMARK 465 SER D 650
REMARK 465 SER D 651
REMARK 465 ASP D 652
REMARK 465 LYS D 653
REMARK 465 MET E 195
REMARK 465 SER E 196
REMARK 465 TYR E 197
REMARK 465 TYR E 198
REMARK 465 HIS E 199
REMARK 465 HIS E 200
REMARK 465 HIS E 201
REMARK 465 HIS E 202
REMARK 465 HIS E 203
REMARK 465 HIS E 204
REMARK 465 ASP E 205
REMARK 465 TYR E 206
REMARK 465 ASP E 207
REMARK 465 ILE E 208
REMARK 465 PRO E 209
REMARK 465 THR E 210
REMARK 465 THR E 211
REMARK 465 GLU E 212
REMARK 465 ASN E 213
REMARK 465 LEU E 214
REMARK 465 TYR E 215
REMARK 465 PHE E 216
REMARK 465 GLN E 217
REMARK 465 GLY E 218
REMARK 465 ALA E 219
REMARK 465 MET E 220
REMARK 465 GLY E 221
REMARK 465 SER E 222
REMARK 465 GLY E 223
REMARK 465 ILE E 224
REMARK 465 GLN E 225
REMARK 465 ASP E 226
REMARK 465 SER E 227
REMARK 465 SER E 228
REMARK 465 ASP E 229
REMARK 465 LYS E 645
REMARK 465 LYS E 646
REMARK 465 SER E 647
REMARK 465 THR E 648
REMARK 465 ASP E 649
REMARK 465 SER E 650
REMARK 465 SER E 651
REMARK 465 ASP E 652
REMARK 465 LYS E 653
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 LEU E 419 ND1 HIS E 422 2.11
REMARK 500 NZ LYS A 238 OE2 GLU A 549 2.18
REMARK 500 OG1 THR E 575 O TYR E 578 2.19
REMARK 500 OG1 THR A 575 O TYR A 578 2.19
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 LYS A 430 CA - CB - CG ANGL. DEV. = 15.5 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 271 13.92 59.76
REMARK 500 LYS A 306 -112.93 54.23
REMARK 500 MET A 382 53.79 -92.90
REMARK 500 SER A 388 -148.08 -88.59
REMARK 500 LEU A 419 -35.24 -137.05
REMARK 500 GLN A 564 81.59 -68.85
REMARK 500 THR A 577 -61.48 -95.88
REMARK 500 ALA B 252 34.57 -93.71
REMARK 500 LYS B 306 -111.31 53.72
REMARK 500 MET B 382 56.84 -92.59
REMARK 500 SER B 388 -151.28 -88.07
REMARK 500 LEU B 419 -35.12 -137.30
REMARK 500 PRO B 424 30.49 -91.95
REMARK 500 SER B 433 33.67 -153.16
REMARK 500 SER B 486 -177.89 -69.52
REMARK 500 ASN B 488 32.22 -99.45
REMARK 500 HIS B 489 52.16 -142.54
REMARK 500 THR B 577 -68.06 -100.03
REMARK 500 LYS B 633 -161.32 -73.63
REMARK 500 THR C 280 79.59 -118.90
REMARK 500 LYS C 306 -111.84 53.74
REMARK 500 ASP C 376 -167.77 -77.99
REMARK 500 MET C 382 46.80 -88.87
REMARK 500 PRO C 424 33.38 -92.69
REMARK 500 LYS C 430 75.27 -113.61
REMARK 500 ASN C 488 30.66 -99.87
REMARK 500 HIS C 489 50.72 -141.12
REMARK 500 GLN C 564 80.07 -69.87
REMARK 500 THR C 577 -64.43 -98.04
REMARK 500 THR D 280 75.58 -118.79
REMARK 500 LYS D 306 -103.98 45.84
REMARK 500 GLU D 336 67.82 -113.07
REMARK 500 TRP D 360 16.00 59.18
REMARK 500 MET D 382 45.77 -90.82
REMARK 500 SER D 388 -160.53 -106.21
REMARK 500 LEU D 419 -32.92 -138.25
REMARK 500 PRO D 424 30.01 -89.98
REMARK 500 THR E 280 77.91 -119.87
REMARK 500 LYS E 306 -112.31 53.73
REMARK 500 TRP E 360 19.58 58.40
REMARK 500 SER E 388 -160.79 -76.46
REMARK 500 LEU E 419 -34.23 -137.29
REMARK 500 PRO E 424 30.15 -93.35
REMARK 500 THR E 577 -65.95 -105.81
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1645 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 263 OE1
REMARK 620 2 GLU A 263 OE2 48.1
REMARK 620 3 TPO A 307 OG1 91.3 112.6
REMARK 620 4 TPO A 307 O3P 109.3 81.3 62.9
REMARK 620 5 ASP A 481 OD2 74.1 114.2 94.6 156.9
REMARK 620 6 HIS A 482 NE2 163.8 126.4 104.2 82.5 99.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1645 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 263 OE2
REMARK 620 2 GLU B 263 OE1 48.6
REMARK 620 3 TPO B 307 OG1 116.0 88.9
REMARK 620 4 TPO B 307 O3P 80.9 104.5 64.6
REMARK 620 5 ASP B 481 OD2 107.9 75.5 101.8 166.3
REMARK 620 6 HIS B 482 NE2 108.8 152.9 117.4 82.8 103.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C1645 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 263 OE2
REMARK 620 2 GLU C 263 OE1 54.3
REMARK 620 3 TPO C 307 O3P 85.6 113.1
REMARK 620 4 TPO C 307 P 109.5 105.2 36.1
REMARK 620 5 TPO C 307 OG1 134.6 98.5 72.1 36.5
REMARK 620 6 ASP C 481 OD2 107.7 73.1 165.9 131.2 94.7
REMARK 620 7 HIS C 482 NE2 105.0 147.5 86.7 105.6 112.4 93.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D1645 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 263 OE2
REMARK 620 2 TPO D 307 O3P 83.2
REMARK 620 3 TPO D 307 OG1 117.9 65.1
REMARK 620 4 ASP D 481 OD2 107.7 161.1 96.0
REMARK 620 5 HIS D 482 NE2 120.1 86.0 109.7 101.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E1645 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 263 OE2
REMARK 620 2 TPO E 307 O3P 89.5
REMARK 620 3 TPO E 307 OG1 127.2 66.9
REMARK 620 4 ASP E 481 OD2 93.5 166.8 101.3
REMARK 620 5 HIS E 482 NE2 104.9 88.0 119.8 103.7
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1645
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1645
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 1645
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 1645
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 1645
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4UOP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE LIPOTEICHOIC ACID SYNTHASE LTAP FROM
REMARK 900 LISTERIA MONOCYTOGENES
REMARK 900 RELATED ID: 4UOR RELATED DB: PDB
REMARK 900 STRUCTURE OF LIPOTEICHOIC ACID SYNTHASE LTAS FROM LISTERIA
REMARK 900 MONOCYTOGENES IN COMPLEX WITH GLYCEROL PHOSPHATE
DBREF 4UOO A 226 653 UNP Q8Y8H6 Q8Y8H6_LISMO 226 653
DBREF 4UOO B 226 653 UNP Q8Y8H6 Q8Y8H6_LISMO 226 653
DBREF 4UOO C 226 653 UNP Q8Y8H6 Q8Y8H6_LISMO 226 653
DBREF 4UOO D 226 653 UNP Q8Y8H6 Q8Y8H6_LISMO 226 653
DBREF 4UOO E 226 653 UNP Q8Y8H6 Q8Y8H6_LISMO 226 653
SEQADV 4UOO MET A 195 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO SER A 196 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO TYR A 197 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO TYR A 198 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO HIS A 199 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO HIS A 200 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO HIS A 201 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO HIS A 202 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO HIS A 203 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO HIS A 204 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO ASP A 205 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO TYR A 206 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO ASP A 207 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO ILE A 208 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO PRO A 209 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO THR A 210 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO THR A 211 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO GLU A 212 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO ASN A 213 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO LEU A 214 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO TYR A 215 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO PHE A 216 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO GLN A 217 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO GLY A 218 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO ALA A 219 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO MET A 220 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO GLY A 221 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO SER A 222 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO GLY A 223 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO ILE A 224 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO GLN A 225 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO MET B 195 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO SER B 196 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO TYR B 197 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO TYR B 198 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO HIS B 199 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO HIS B 200 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO HIS B 201 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO HIS B 202 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO HIS B 203 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO HIS B 204 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO ASP B 205 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO TYR B 206 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO ASP B 207 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO ILE B 208 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO PRO B 209 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO THR B 210 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO THR B 211 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO GLU B 212 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO ASN B 213 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO LEU B 214 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO TYR B 215 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO PHE B 216 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO GLN B 217 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO GLY B 218 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO ALA B 219 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO MET B 220 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO GLY B 221 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO SER B 222 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO GLY B 223 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO ILE B 224 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO GLN B 225 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO MET C 195 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO SER C 196 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO TYR C 197 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO TYR C 198 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO HIS C 199 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO HIS C 200 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO HIS C 201 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO HIS C 202 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO HIS C 203 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO HIS C 204 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO ASP C 205 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO TYR C 206 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO ASP C 207 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO ILE C 208 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO PRO C 209 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO THR C 210 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO THR C 211 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO GLU C 212 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO ASN C 213 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO LEU C 214 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO TYR C 215 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO PHE C 216 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO GLN C 217 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO GLY C 218 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO ALA C 219 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO MET C 220 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO GLY C 221 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO SER C 222 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO GLY C 223 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO ILE C 224 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO GLN C 225 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO MET D 195 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO SER D 196 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO TYR D 197 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO TYR D 198 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO HIS D 199 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO HIS D 200 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO HIS D 201 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO HIS D 202 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO HIS D 203 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO HIS D 204 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO ASP D 205 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO TYR D 206 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO ASP D 207 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO ILE D 208 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO PRO D 209 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO THR D 210 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO THR D 211 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO GLU D 212 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO ASN D 213 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO LEU D 214 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO TYR D 215 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO PHE D 216 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO GLN D 217 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO GLY D 218 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO ALA D 219 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO MET D 220 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO GLY D 221 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO SER D 222 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO GLY D 223 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO ILE D 224 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO GLN D 225 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO MET E 195 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO SER E 196 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO TYR E 197 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO TYR E 198 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO HIS E 199 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO HIS E 200 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO HIS E 201 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO HIS E 202 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO HIS E 203 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO HIS E 204 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO ASP E 205 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO TYR E 206 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO ASP E 207 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO ILE E 208 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO PRO E 209 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO THR E 210 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO THR E 211 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO GLU E 212 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO ASN E 213 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO LEU E 214 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO TYR E 215 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO PHE E 216 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO GLN E 217 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO GLY E 218 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO ALA E 219 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO MET E 220 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO GLY E 221 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO SER E 222 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO GLY E 223 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO ILE E 224 UNP Q8Y8H6 EXPRESSION TAG
SEQADV 4UOO GLN E 225 UNP Q8Y8H6 EXPRESSION TAG
SEQRES 1 A 459 MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP
SEQRES 2 A 459 ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET
SEQRES 3 A 459 GLY SER GLY ILE GLN ASP SER SER ASP VAL THR GLU VAL
SEQRES 4 A 459 LEU ASN TYR THR LYS SER LYS TYR ALA ALA PRO ASN PRO
SEQRES 5 A 459 GLU TYR PHE GLY LYS ALA LYS GLY LYS ASN VAL ILE TYR
SEQRES 6 A 459 ILE HIS LEU GLU SER PHE GLN GLN PHE LEU VAL ASN TYR
SEQRES 7 A 459 LYS LEU ASN GLY GLU GLU VAL THR PRO PHE ILE ASN SER
SEQRES 8 A 459 PHE PHE LYS ASP GLN ASN THR LEU SER PHE THR ASN PHE
SEQRES 9 A 459 PHE HIS GLN THR GLY GLN GLY LYS TPO ALA ASP SER GLU
SEQRES 10 A 459 MET LEU LEU GLU ASN SER LEU TYR GLY LEU PRO GLN GLY
SEQRES 11 A 459 SER ALA PHE THR THR LYS GLY GLN ASN THR TYR GLU SER
SEQRES 12 A 459 ALA SER ALA ILE LEU GLY GLN GLN GLY TYR THR SER ALA
SEQRES 13 A 459 VAL PHE HIS GLY ASN TYR LYS SER PHE TRP ASN ARG ASP
SEQRES 14 A 459 GLU ILE TYR LYS GLN PHE GLY TYR ASP ASN PHE PHE ASP
SEQRES 15 A 459 ALA SER TYR TYR ASP MET ASN GLU ALA ASP VAL SER ASN
SEQRES 16 A 459 TYR GLY LEU LYS ASP LYS PRO PHE PHE LYS GLU SER GLU
SEQRES 17 A 459 GLU TYR LEU SER SER LEU GLN GLN PRO PHE TYR THR LYS
SEQRES 18 A 459 PHE ILE THR LEU THR ASN HIS PHE PRO TYR PRO ILE ASP
SEQRES 19 A 459 GLU LYS ASP ALA SER ILE ALA PRO ALA THR THR GLY ASP
SEQRES 20 A 459 SER SER VAL ASP THR TYR PHE GLN THR ALA ARG TYR LEU
SEQRES 21 A 459 ASP GLU SER VAL LYS SER PHE VAL ASP TYR LEU LYS LYS
SEQRES 22 A 459 SER GLY LEU TYR ASP ASN SER VAL ILE ILE MET TYR GLY
SEQRES 23 A 459 ASP HIS TYR GLY ILE SER ASP ASN HIS GLU GLU ALA MET
SEQRES 24 A 459 THR LYS ILE LEU GLY LYS ASP TYR ASN THR PHE GLU ASN
SEQRES 25 A 459 ALA GLN ALA GLN ARG VAL PRO LEU MET ILE HIS VAL PRO
SEQRES 26 A 459 GLY VAL GLN GLY GLY VAL GLN GLU GLN TYR GLY GLY GLN
SEQRES 27 A 459 VAL ASP LEU LEU PRO THR LEU LEU HIS LEU LEU GLY VAL
SEQRES 28 A 459 ASP ASN LYS GLU TYR LEU GLN PHE GLY THR ASP LEU LEU
SEQRES 29 A 459 SER LYS ASP HIS LYS GLN LEU VAL PRO PHE ARG ASN GLY
SEQRES 30 A 459 ASP TYR ILE THR PRO THR TYR SER MET ILE GLY GLY ASN
SEQRES 31 A 459 MET TYR ASN GLN GLN THR GLY GLU PRO ILE ALA THR GLU
SEQRES 32 A 459 THR LYS GLU MET LYS GLU THR LYS GLU LYS VAL ALA LYS
SEQRES 33 A 459 GLU LEU GLU LEU SER ASP SER VAL LEU GLN GLY ASP LEU
SEQRES 34 A 459 LEU ARG PHE TYR ALA PRO ASP GLY PHE LYS LYS VAL ASP
SEQRES 35 A 459 PRO SER LYS TYR ASN TYR ASN LYS LYS LYS SER THR ASP
SEQRES 36 A 459 SER SER ASP LYS
SEQRES 1 B 459 MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP
SEQRES 2 B 459 ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET
SEQRES 3 B 459 GLY SER GLY ILE GLN ASP SER SER ASP VAL THR GLU VAL
SEQRES 4 B 459 LEU ASN TYR THR LYS SER LYS TYR ALA ALA PRO ASN PRO
SEQRES 5 B 459 GLU TYR PHE GLY LYS ALA LYS GLY LYS ASN VAL ILE TYR
SEQRES 6 B 459 ILE HIS LEU GLU SER PHE GLN GLN PHE LEU VAL ASN TYR
SEQRES 7 B 459 LYS LEU ASN GLY GLU GLU VAL THR PRO PHE ILE ASN SER
SEQRES 8 B 459 PHE PHE LYS ASP GLN ASN THR LEU SER PHE THR ASN PHE
SEQRES 9 B 459 PHE HIS GLN THR GLY GLN GLY LYS TPO ALA ASP SER GLU
SEQRES 10 B 459 MET LEU LEU GLU ASN SER LEU TYR GLY LEU PRO GLN GLY
SEQRES 11 B 459 SER ALA PHE THR THR LYS GLY GLN ASN THR TYR GLU SER
SEQRES 12 B 459 ALA SER ALA ILE LEU GLY GLN GLN GLY TYR THR SER ALA
SEQRES 13 B 459 VAL PHE HIS GLY ASN TYR LYS SER PHE TRP ASN ARG ASP
SEQRES 14 B 459 GLU ILE TYR LYS GLN PHE GLY TYR ASP ASN PHE PHE ASP
SEQRES 15 B 459 ALA SER TYR TYR ASP MET ASN GLU ALA ASP VAL SER ASN
SEQRES 16 B 459 TYR GLY LEU LYS ASP LYS PRO PHE PHE LYS GLU SER GLU
SEQRES 17 B 459 GLU TYR LEU SER SER LEU GLN GLN PRO PHE TYR THR LYS
SEQRES 18 B 459 PHE ILE THR LEU THR ASN HIS PHE PRO TYR PRO ILE ASP
SEQRES 19 B 459 GLU LYS ASP ALA SER ILE ALA PRO ALA THR THR GLY ASP
SEQRES 20 B 459 SER SER VAL ASP THR TYR PHE GLN THR ALA ARG TYR LEU
SEQRES 21 B 459 ASP GLU SER VAL LYS SER PHE VAL ASP TYR LEU LYS LYS
SEQRES 22 B 459 SER GLY LEU TYR ASP ASN SER VAL ILE ILE MET TYR GLY
SEQRES 23 B 459 ASP HIS TYR GLY ILE SER ASP ASN HIS GLU GLU ALA MET
SEQRES 24 B 459 THR LYS ILE LEU GLY LYS ASP TYR ASN THR PHE GLU ASN
SEQRES 25 B 459 ALA GLN ALA GLN ARG VAL PRO LEU MET ILE HIS VAL PRO
SEQRES 26 B 459 GLY VAL GLN GLY GLY VAL GLN GLU GLN TYR GLY GLY GLN
SEQRES 27 B 459 VAL ASP LEU LEU PRO THR LEU LEU HIS LEU LEU GLY VAL
SEQRES 28 B 459 ASP ASN LYS GLU TYR LEU GLN PHE GLY THR ASP LEU LEU
SEQRES 29 B 459 SER LYS ASP HIS LYS GLN LEU VAL PRO PHE ARG ASN GLY
SEQRES 30 B 459 ASP TYR ILE THR PRO THR TYR SER MET ILE GLY GLY ASN
SEQRES 31 B 459 MET TYR ASN GLN GLN THR GLY GLU PRO ILE ALA THR GLU
SEQRES 32 B 459 THR LYS GLU MET LYS GLU THR LYS GLU LYS VAL ALA LYS
SEQRES 33 B 459 GLU LEU GLU LEU SER ASP SER VAL LEU GLN GLY ASP LEU
SEQRES 34 B 459 LEU ARG PHE TYR ALA PRO ASP GLY PHE LYS LYS VAL ASP
SEQRES 35 B 459 PRO SER LYS TYR ASN TYR ASN LYS LYS LYS SER THR ASP
SEQRES 36 B 459 SER SER ASP LYS
SEQRES 1 C 459 MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP
SEQRES 2 C 459 ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET
SEQRES 3 C 459 GLY SER GLY ILE GLN ASP SER SER ASP VAL THR GLU VAL
SEQRES 4 C 459 LEU ASN TYR THR LYS SER LYS TYR ALA ALA PRO ASN PRO
SEQRES 5 C 459 GLU TYR PHE GLY LYS ALA LYS GLY LYS ASN VAL ILE TYR
SEQRES 6 C 459 ILE HIS LEU GLU SER PHE GLN GLN PHE LEU VAL ASN TYR
SEQRES 7 C 459 LYS LEU ASN GLY GLU GLU VAL THR PRO PHE ILE ASN SER
SEQRES 8 C 459 PHE PHE LYS ASP GLN ASN THR LEU SER PHE THR ASN PHE
SEQRES 9 C 459 PHE HIS GLN THR GLY GLN GLY LYS TPO ALA ASP SER GLU
SEQRES 10 C 459 MET LEU LEU GLU ASN SER LEU TYR GLY LEU PRO GLN GLY
SEQRES 11 C 459 SER ALA PHE THR THR LYS GLY GLN ASN THR TYR GLU SER
SEQRES 12 C 459 ALA SER ALA ILE LEU GLY GLN GLN GLY TYR THR SER ALA
SEQRES 13 C 459 VAL PHE HIS GLY ASN TYR LYS SER PHE TRP ASN ARG ASP
SEQRES 14 C 459 GLU ILE TYR LYS GLN PHE GLY TYR ASP ASN PHE PHE ASP
SEQRES 15 C 459 ALA SER TYR TYR ASP MET ASN GLU ALA ASP VAL SER ASN
SEQRES 16 C 459 TYR GLY LEU LYS ASP LYS PRO PHE PHE LYS GLU SER GLU
SEQRES 17 C 459 GLU TYR LEU SER SER LEU GLN GLN PRO PHE TYR THR LYS
SEQRES 18 C 459 PHE ILE THR LEU THR ASN HIS PHE PRO TYR PRO ILE ASP
SEQRES 19 C 459 GLU LYS ASP ALA SER ILE ALA PRO ALA THR THR GLY ASP
SEQRES 20 C 459 SER SER VAL ASP THR TYR PHE GLN THR ALA ARG TYR LEU
SEQRES 21 C 459 ASP GLU SER VAL LYS SER PHE VAL ASP TYR LEU LYS LYS
SEQRES 22 C 459 SER GLY LEU TYR ASP ASN SER VAL ILE ILE MET TYR GLY
SEQRES 23 C 459 ASP HIS TYR GLY ILE SER ASP ASN HIS GLU GLU ALA MET
SEQRES 24 C 459 THR LYS ILE LEU GLY LYS ASP TYR ASN THR PHE GLU ASN
SEQRES 25 C 459 ALA GLN ALA GLN ARG VAL PRO LEU MET ILE HIS VAL PRO
SEQRES 26 C 459 GLY VAL GLN GLY GLY VAL GLN GLU GLN TYR GLY GLY GLN
SEQRES 27 C 459 VAL ASP LEU LEU PRO THR LEU LEU HIS LEU LEU GLY VAL
SEQRES 28 C 459 ASP ASN LYS GLU TYR LEU GLN PHE GLY THR ASP LEU LEU
SEQRES 29 C 459 SER LYS ASP HIS LYS GLN LEU VAL PRO PHE ARG ASN GLY
SEQRES 30 C 459 ASP TYR ILE THR PRO THR TYR SER MET ILE GLY GLY ASN
SEQRES 31 C 459 MET TYR ASN GLN GLN THR GLY GLU PRO ILE ALA THR GLU
SEQRES 32 C 459 THR LYS GLU MET LYS GLU THR LYS GLU LYS VAL ALA LYS
SEQRES 33 C 459 GLU LEU GLU LEU SER ASP SER VAL LEU GLN GLY ASP LEU
SEQRES 34 C 459 LEU ARG PHE TYR ALA PRO ASP GLY PHE LYS LYS VAL ASP
SEQRES 35 C 459 PRO SER LYS TYR ASN TYR ASN LYS LYS LYS SER THR ASP
SEQRES 36 C 459 SER SER ASP LYS
SEQRES 1 D 459 MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP
SEQRES 2 D 459 ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET
SEQRES 3 D 459 GLY SER GLY ILE GLN ASP SER SER ASP VAL THR GLU VAL
SEQRES 4 D 459 LEU ASN TYR THR LYS SER LYS TYR ALA ALA PRO ASN PRO
SEQRES 5 D 459 GLU TYR PHE GLY LYS ALA LYS GLY LYS ASN VAL ILE TYR
SEQRES 6 D 459 ILE HIS LEU GLU SER PHE GLN GLN PHE LEU VAL ASN TYR
SEQRES 7 D 459 LYS LEU ASN GLY GLU GLU VAL THR PRO PHE ILE ASN SER
SEQRES 8 D 459 PHE PHE LYS ASP GLN ASN THR LEU SER PHE THR ASN PHE
SEQRES 9 D 459 PHE HIS GLN THR GLY GLN GLY LYS TPO ALA ASP SER GLU
SEQRES 10 D 459 MET LEU LEU GLU ASN SER LEU TYR GLY LEU PRO GLN GLY
SEQRES 11 D 459 SER ALA PHE THR THR LYS GLY GLN ASN THR TYR GLU SER
SEQRES 12 D 459 ALA SER ALA ILE LEU GLY GLN GLN GLY TYR THR SER ALA
SEQRES 13 D 459 VAL PHE HIS GLY ASN TYR LYS SER PHE TRP ASN ARG ASP
SEQRES 14 D 459 GLU ILE TYR LYS GLN PHE GLY TYR ASP ASN PHE PHE ASP
SEQRES 15 D 459 ALA SER TYR TYR ASP MET ASN GLU ALA ASP VAL SER ASN
SEQRES 16 D 459 TYR GLY LEU LYS ASP LYS PRO PHE PHE LYS GLU SER GLU
SEQRES 17 D 459 GLU TYR LEU SER SER LEU GLN GLN PRO PHE TYR THR LYS
SEQRES 18 D 459 PHE ILE THR LEU THR ASN HIS PHE PRO TYR PRO ILE ASP
SEQRES 19 D 459 GLU LYS ASP ALA SER ILE ALA PRO ALA THR THR GLY ASP
SEQRES 20 D 459 SER SER VAL ASP THR TYR PHE GLN THR ALA ARG TYR LEU
SEQRES 21 D 459 ASP GLU SER VAL LYS SER PHE VAL ASP TYR LEU LYS LYS
SEQRES 22 D 459 SER GLY LEU TYR ASP ASN SER VAL ILE ILE MET TYR GLY
SEQRES 23 D 459 ASP HIS TYR GLY ILE SER ASP ASN HIS GLU GLU ALA MET
SEQRES 24 D 459 THR LYS ILE LEU GLY LYS ASP TYR ASN THR PHE GLU ASN
SEQRES 25 D 459 ALA GLN ALA GLN ARG VAL PRO LEU MET ILE HIS VAL PRO
SEQRES 26 D 459 GLY VAL GLN GLY GLY VAL GLN GLU GLN TYR GLY GLY GLN
SEQRES 27 D 459 VAL ASP LEU LEU PRO THR LEU LEU HIS LEU LEU GLY VAL
SEQRES 28 D 459 ASP ASN LYS GLU TYR LEU GLN PHE GLY THR ASP LEU LEU
SEQRES 29 D 459 SER LYS ASP HIS LYS GLN LEU VAL PRO PHE ARG ASN GLY
SEQRES 30 D 459 ASP TYR ILE THR PRO THR TYR SER MET ILE GLY GLY ASN
SEQRES 31 D 459 MET TYR ASN GLN GLN THR GLY GLU PRO ILE ALA THR GLU
SEQRES 32 D 459 THR LYS GLU MET LYS GLU THR LYS GLU LYS VAL ALA LYS
SEQRES 33 D 459 GLU LEU GLU LEU SER ASP SER VAL LEU GLN GLY ASP LEU
SEQRES 34 D 459 LEU ARG PHE TYR ALA PRO ASP GLY PHE LYS LYS VAL ASP
SEQRES 35 D 459 PRO SER LYS TYR ASN TYR ASN LYS LYS LYS SER THR ASP
SEQRES 36 D 459 SER SER ASP LYS
SEQRES 1 E 459 MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP
SEQRES 2 E 459 ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET
SEQRES 3 E 459 GLY SER GLY ILE GLN ASP SER SER ASP VAL THR GLU VAL
SEQRES 4 E 459 LEU ASN TYR THR LYS SER LYS TYR ALA ALA PRO ASN PRO
SEQRES 5 E 459 GLU TYR PHE GLY LYS ALA LYS GLY LYS ASN VAL ILE TYR
SEQRES 6 E 459 ILE HIS LEU GLU SER PHE GLN GLN PHE LEU VAL ASN TYR
SEQRES 7 E 459 LYS LEU ASN GLY GLU GLU VAL THR PRO PHE ILE ASN SER
SEQRES 8 E 459 PHE PHE LYS ASP GLN ASN THR LEU SER PHE THR ASN PHE
SEQRES 9 E 459 PHE HIS GLN THR GLY GLN GLY LYS TPO ALA ASP SER GLU
SEQRES 10 E 459 MET LEU LEU GLU ASN SER LEU TYR GLY LEU PRO GLN GLY
SEQRES 11 E 459 SER ALA PHE THR THR LYS GLY GLN ASN THR TYR GLU SER
SEQRES 12 E 459 ALA SER ALA ILE LEU GLY GLN GLN GLY TYR THR SER ALA
SEQRES 13 E 459 VAL PHE HIS GLY ASN TYR LYS SER PHE TRP ASN ARG ASP
SEQRES 14 E 459 GLU ILE TYR LYS GLN PHE GLY TYR ASP ASN PHE PHE ASP
SEQRES 15 E 459 ALA SER TYR TYR ASP MET ASN GLU ALA ASP VAL SER ASN
SEQRES 16 E 459 TYR GLY LEU LYS ASP LYS PRO PHE PHE LYS GLU SER GLU
SEQRES 17 E 459 GLU TYR LEU SER SER LEU GLN GLN PRO PHE TYR THR LYS
SEQRES 18 E 459 PHE ILE THR LEU THR ASN HIS PHE PRO TYR PRO ILE ASP
SEQRES 19 E 459 GLU LYS ASP ALA SER ILE ALA PRO ALA THR THR GLY ASP
SEQRES 20 E 459 SER SER VAL ASP THR TYR PHE GLN THR ALA ARG TYR LEU
SEQRES 21 E 459 ASP GLU SER VAL LYS SER PHE VAL ASP TYR LEU LYS LYS
SEQRES 22 E 459 SER GLY LEU TYR ASP ASN SER VAL ILE ILE MET TYR GLY
SEQRES 23 E 459 ASP HIS TYR GLY ILE SER ASP ASN HIS GLU GLU ALA MET
SEQRES 24 E 459 THR LYS ILE LEU GLY LYS ASP TYR ASN THR PHE GLU ASN
SEQRES 25 E 459 ALA GLN ALA GLN ARG VAL PRO LEU MET ILE HIS VAL PRO
SEQRES 26 E 459 GLY VAL GLN GLY GLY VAL GLN GLU GLN TYR GLY GLY GLN
SEQRES 27 E 459 VAL ASP LEU LEU PRO THR LEU LEU HIS LEU LEU GLY VAL
SEQRES 28 E 459 ASP ASN LYS GLU TYR LEU GLN PHE GLY THR ASP LEU LEU
SEQRES 29 E 459 SER LYS ASP HIS LYS GLN LEU VAL PRO PHE ARG ASN GLY
SEQRES 30 E 459 ASP TYR ILE THR PRO THR TYR SER MET ILE GLY GLY ASN
SEQRES 31 E 459 MET TYR ASN GLN GLN THR GLY GLU PRO ILE ALA THR GLU
SEQRES 32 E 459 THR LYS GLU MET LYS GLU THR LYS GLU LYS VAL ALA LYS
SEQRES 33 E 459 GLU LEU GLU LEU SER ASP SER VAL LEU GLN GLY ASP LEU
SEQRES 34 E 459 LEU ARG PHE TYR ALA PRO ASP GLY PHE LYS LYS VAL ASP
SEQRES 35 E 459 PRO SER LYS TYR ASN TYR ASN LYS LYS LYS SER THR ASP
SEQRES 36 E 459 SER SER ASP LYS
MODRES 4UOO TPO A 307 THR PHOSPHOTHREONINE
MODRES 4UOO TPO B 307 THR PHOSPHOTHREONINE
MODRES 4UOO TPO C 307 THR PHOSPHOTHREONINE
MODRES 4UOO TPO D 307 THR PHOSPHOTHREONINE
MODRES 4UOO TPO E 307 THR PHOSPHOTHREONINE
HET TPO A 307 11
HET TPO B 307 11
HET TPO C 307 11
HET TPO D 307 11
HET TPO E 307 11
HET MG A1645 1
HET MG B1645 1
HET MG C1645 1
HET MG D1645 1
HET MG E1645 1
HETNAM TPO PHOSPHOTHREONINE
HETNAM MG MAGNESIUM ION
HETSYN TPO PHOSPHONOTHREONINE
FORMUL 1 TPO 5(C4 H10 N O6 P)
FORMUL 6 MG 5(MG 2+)
HELIX 1 1 THR A 231 TYR A 241 1 11
HELIX 2 2 GLN A 266 VAL A 270 5 5
HELIX 3 3 THR A 280 ASP A 289 1 10
HELIX 4 4 LYS A 306 SER A 317 1 12
HELIX 5 5 SER A 325 LYS A 330 1 6
HELIX 6 6 SER A 337 GLN A 344 1 8
HELIX 7 7 SER A 358 TRP A 360 5 3
HELIX 8 8 ASN A 361 GLY A 370 1 10
HELIX 9 9 ASP A 376 TYR A 380 5 5
HELIX 10 10 ASN A 383 ASP A 386 5 4
HELIX 11 11 LYS A 393 SER A 407 1 15
HELIX 12 12 ASP A 441 THR A 446 1 6
HELIX 13 13 THR A 446 SER A 468 1 23
HELIX 14 14 GLY A 469 ASN A 473 1 5
HELIX 15 15 HIS A 489 GLY A 498 1 10
HELIX 16 16 ASN A 502 ALA A 509 1 8
HELIX 17 17 ASP A 534 LEU A 543 1 10
HELIX 18 18 THR A 598 ASP A 622 1 25
HELIX 19 19 LEU A 623 PHE A 626 5 4
HELIX 20 20 ASP A 636 TYR A 640 5 5
HELIX 21 21 THR B 231 TYR B 241 1 11
HELIX 22 22 GLN B 266 VAL B 270 5 5
HELIX 23 23 THR B 280 ASP B 289 1 10
HELIX 24 24 LYS B 306 SER B 317 1 12
HELIX 25 25 SER B 325 LYS B 330 1 6
HELIX 26 26 SER B 337 LEU B 342 1 6
HELIX 27 27 SER B 358 TRP B 360 5 3
HELIX 28 28 ASN B 361 GLY B 370 1 10
HELIX 29 29 ASP B 376 TYR B 380 5 5
HELIX 30 30 LYS B 393 SER B 401 1 9
HELIX 31 31 SER B 401 SER B 407 1 7
HELIX 32 32 ASP B 441 THR B 446 1 6
HELIX 33 33 THR B 446 SER B 468 1 23
HELIX 34 34 GLY B 469 ASP B 472 5 4
HELIX 35 35 HIS B 489 GLY B 498 1 10
HELIX 36 36 ASN B 502 ALA B 509 1 8
HELIX 37 37 ASP B 534 LEU B 543 1 10
HELIX 38 38 THR B 598 ASP B 622 1 25
HELIX 39 39 LEU B 623 PHE B 626 5 4
HELIX 40 40 ASP B 636 TYR B 640 5 5
HELIX 41 41 THR C 231 TYR C 241 1 11
HELIX 42 42 GLN C 266 VAL C 270 5 5
HELIX 43 43 THR C 280 ASP C 289 1 10
HELIX 44 44 LYS C 306 SER C 317 1 12
HELIX 45 45 SER C 325 LYS C 330 1 6
HELIX 46 46 SER C 337 GLN C 344 1 8
HELIX 47 47 SER C 358 TRP C 360 5 3
HELIX 48 48 ASN C 361 GLY C 370 1 10
HELIX 49 49 ASP C 376 TYR C 380 5 5
HELIX 50 50 ASN C 383 ALA C 385 5 3
HELIX 51 51 LYS C 393 SER C 401 1 9
HELIX 52 52 SER C 401 SER C 407 1 7
HELIX 53 53 ASP C 441 THR C 446 1 6
HELIX 54 54 THR C 446 GLY C 469 1 24
HELIX 55 55 GLY C 469 ASN C 473 1 5
HELIX 56 56 HIS C 489 GLY C 498 1 10
HELIX 57 57 ASN C 502 ALA C 509 1 8
HELIX 58 58 ASP C 534 LEU C 543 1 10
HELIX 59 59 THR C 598 ASP C 622 1 25
HELIX 60 60 LEU C 623 PHE C 626 5 4
HELIX 61 61 ASP C 636 TYR C 640 5 5
HELIX 62 62 THR D 231 TYR D 241 1 11
HELIX 63 63 GLN D 266 VAL D 270 5 5
HELIX 64 64 THR D 280 LYS D 288 1 9
HELIX 65 65 LYS D 306 SER D 317 1 12
HELIX 66 66 SER D 325 LYS D 330 1 6
HELIX 67 67 SER D 337 GLN D 344 1 8
HELIX 68 68 SER D 358 TRP D 360 5 3
HELIX 69 69 ASN D 361 GLY D 370 1 10
HELIX 70 70 ASP D 376 TYR D 380 5 5
HELIX 71 71 ASN D 383 ALA D 385 5 3
HELIX 72 72 LYS D 393 SER D 401 1 9
HELIX 73 73 SER D 401 SER D 407 1 7
HELIX 74 74 ASP D 441 THR D 446 1 6
HELIX 75 75 THR D 446 SER D 468 1 23
HELIX 76 76 GLY D 469 ASN D 473 1 5
HELIX 77 77 HIS D 489 GLY D 498 1 10
HELIX 78 78 ASN D 502 ALA D 509 1 8
HELIX 79 79 ASP D 534 LEU D 543 1 10
HELIX 80 80 THR D 598 ASP D 622 1 25
HELIX 81 81 LEU D 623 PHE D 626 5 4
HELIX 82 82 ASP D 636 TYR D 640 5 5
HELIX 83 83 THR E 231 TYR E 241 1 11
HELIX 84 84 GLN E 266 VAL E 270 5 5
HELIX 85 85 THR E 280 ASP E 289 1 10
HELIX 86 86 LYS E 306 SER E 317 1 12
HELIX 87 87 SER E 325 LYS E 330 1 6
HELIX 88 88 SER E 337 GLN E 344 1 8
HELIX 89 89 SER E 358 TRP E 360 5 3
HELIX 90 90 ASN E 361 GLY E 370 1 10
HELIX 91 91 ASP E 376 TYR E 380 5 5
HELIX 92 92 ASN E 383 ASP E 386 5 4
HELIX 93 93 LYS E 393 SER E 401 1 9
HELIX 94 94 SER E 401 SER E 407 1 7
HELIX 95 95 ASP E 441 THR E 446 1 6
HELIX 96 96 THR E 446 SER E 468 1 23
HELIX 97 97 GLY E 469 ASN E 473 1 5
HELIX 98 98 HIS E 489 GLY E 498 1 10
HELIX 99 99 ASN E 502 ALA E 509 1 8
HELIX 100 100 ASP E 534 LEU E 543 1 10
HELIX 101 101 THR E 598 ASP E 622 1 25
HELIX 102 102 LEU E 623 PHE E 626 5 4
HELIX 103 103 ASP E 636 TYR E 640 5 5
SHEET 1 AA 8 ASN A 373 PHE A 375 0
SHEET 2 AA 8 THR A 348 HIS A 353 1 O SER A 349 N ASN A 373
SHEET 3 AA 8 PHE A 412 ILE A 417 1 O TYR A 413 N ALA A 350
SHEET 4 AA 8 ASN A 256 LEU A 262 1 O VAL A 257 N THR A 414
SHEET 5 AA 8 SER A 474 GLY A 480 1 O VAL A 475 N ILE A 258
SHEET 6 AA 8 LEU A 514 HIS A 517 -1 O MET A 515 N MET A 478
SHEET 7 AA 8 THR A 292 PHE A 295 -1 O LEU A 293 N ILE A 516
SHEET 8 AA 8 GLY A 524 GLN A 526 1 O GLY A 524 N SER A 294
SHEET 1 AB 2 LYS A 273 LEU A 274 0
SHEET 2 AB 2 GLU A 277 GLU A 278 -1 O GLU A 277 N LEU A 274
SHEET 1 AC 2 PHE A 298 PHE A 299 0
SHEET 2 AC 2 GLY A 530 GLY A 531 1 O GLY A 530 N PHE A 299
SHEET 1 AD 5 VAL A 566 PRO A 567 0
SHEET 2 AD 5 TYR A 573 ILE A 574 -1 O ILE A 574 N VAL A 566
SHEET 3 AD 5 TYR A 578 ILE A 581 -1 O MET A 580 N TYR A 573
SHEET 4 AD 5 ASN A 584 ASN A 587 -1 O ASN A 584 N ILE A 581
SHEET 5 AD 5 PRO A 593 ILE A 594 -1 O ILE A 594 N MET A 585
SHEET 1 BA 8 ASN B 373 PHE B 375 0
SHEET 2 BA 8 THR B 348 HIS B 353 1 O SER B 349 N ASN B 373
SHEET 3 BA 8 PHE B 412 ILE B 417 1 O TYR B 413 N ALA B 350
SHEET 4 BA 8 ASN B 256 LEU B 262 1 O VAL B 257 N THR B 414
SHEET 5 BA 8 SER B 474 GLY B 480 1 O VAL B 475 N ILE B 258
SHEET 6 BA 8 LEU B 514 HIS B 517 -1 O MET B 515 N MET B 478
SHEET 7 BA 8 THR B 292 PHE B 295 -1 O LEU B 293 N ILE B 516
SHEET 8 BA 8 GLY B 524 GLN B 526 1 O GLY B 524 N SER B 294
SHEET 1 BB 2 LYS B 273 LEU B 274 0
SHEET 2 BB 2 GLU B 277 GLU B 278 -1 O GLU B 277 N LEU B 274
SHEET 1 BC 2 PHE B 298 PHE B 299 0
SHEET 2 BC 2 GLY B 530 GLY B 531 1 O GLY B 530 N PHE B 299
SHEET 1 BD 4 VAL B 566 PRO B 567 0
SHEET 2 BD 4 TYR B 573 ILE B 574 -1 O ILE B 574 N VAL B 566
SHEET 3 BD 4 TYR B 578 ILE B 581 -1 O MET B 580 N TYR B 573
SHEET 4 BD 4 ASN B 584 ASN B 587 -1 O ASN B 584 N ILE B 581
SHEET 1 CA 8 ASN C 373 PHE C 375 0
SHEET 2 CA 8 THR C 348 HIS C 353 1 O SER C 349 N ASN C 373
SHEET 3 CA 8 PHE C 412 ILE C 417 1 O TYR C 413 N ALA C 350
SHEET 4 CA 8 ASN C 256 LEU C 262 1 O VAL C 257 N THR C 414
SHEET 5 CA 8 SER C 474 GLY C 480 1 O VAL C 475 N ILE C 258
SHEET 6 CA 8 LEU C 514 HIS C 517 -1 O MET C 515 N MET C 478
SHEET 7 CA 8 THR C 292 PHE C 295 -1 O LEU C 293 N ILE C 516
SHEET 8 CA 8 GLY C 524 GLN C 526 1 O GLY C 524 N SER C 294
SHEET 1 CB 2 LYS C 273 LEU C 274 0
SHEET 2 CB 2 GLU C 277 GLU C 278 -1 O GLU C 277 N LEU C 274
SHEET 1 CC 2 PHE C 298 PHE C 299 0
SHEET 2 CC 2 GLY C 530 GLY C 531 1 O GLY C 530 N PHE C 299
SHEET 1 CD 2 VAL C 387 SER C 388 0
SHEET 2 CD 2 GLY C 391 LEU C 392 -1 O GLY C 391 N SER C 388
SHEET 1 CE 4 VAL C 566 PRO C 567 0
SHEET 2 CE 4 TYR C 573 ILE C 574 -1 O ILE C 574 N VAL C 566
SHEET 3 CE 4 TYR C 578 ILE C 581 -1 O MET C 580 N TYR C 573
SHEET 4 CE 4 ASN C 584 ASN C 587 -1 O ASN C 584 N ILE C 581
SHEET 1 DA 8 ASN D 373 PHE D 375 0
SHEET 2 DA 8 THR D 348 HIS D 353 1 O SER D 349 N ASN D 373
SHEET 3 DA 8 PHE D 412 ILE D 417 1 O TYR D 413 N ALA D 350
SHEET 4 DA 8 ASN D 256 LEU D 262 1 O VAL D 257 N THR D 414
SHEET 5 DA 8 SER D 474 GLY D 480 1 O VAL D 475 N ILE D 258
SHEET 6 DA 8 LEU D 514 HIS D 517 -1 O MET D 515 N MET D 478
SHEET 7 DA 8 THR D 292 PHE D 295 -1 O LEU D 293 N ILE D 516
SHEET 8 DA 8 GLY D 524 GLN D 526 1 O GLY D 524 N SER D 294
SHEET 1 DB 2 LYS D 273 LEU D 274 0
SHEET 2 DB 2 GLU D 277 GLU D 278 -1 O GLU D 277 N LEU D 274
SHEET 1 DC 2 PHE D 298 PHE D 299 0
SHEET 2 DC 2 GLY D 530 GLY D 531 1 O GLY D 530 N PHE D 299
SHEET 1 DD 2 VAL D 387 SER D 388 0
SHEET 2 DD 2 GLY D 391 LEU D 392 -1 O GLY D 391 N SER D 388
SHEET 1 DE 4 VAL D 566 PRO D 567 0
SHEET 2 DE 4 TYR D 573 ILE D 574 -1 O ILE D 574 N VAL D 566
SHEET 3 DE 4 TYR D 578 ILE D 581 -1 O MET D 580 N TYR D 573
SHEET 4 DE 4 ASN D 584 ASN D 587 -1 O ASN D 584 N ILE D 581
SHEET 1 EA 8 ASN E 373 PHE E 375 0
SHEET 2 EA 8 THR E 348 HIS E 353 1 O SER E 349 N ASN E 373
SHEET 3 EA 8 PHE E 412 ILE E 417 1 O TYR E 413 N ALA E 350
SHEET 4 EA 8 ASN E 256 LEU E 262 1 O VAL E 257 N THR E 414
SHEET 5 EA 8 SER E 474 GLY E 480 1 O VAL E 475 N ILE E 258
SHEET 6 EA 8 LEU E 514 HIS E 517 -1 O MET E 515 N MET E 478
SHEET 7 EA 8 THR E 292 PHE E 295 -1 O LEU E 293 N ILE E 516
SHEET 8 EA 8 GLY E 524 GLN E 526 1 O GLY E 524 N SER E 294
SHEET 1 EB 2 LYS E 273 LEU E 274 0
SHEET 2 EB 2 GLU E 277 GLU E 278 -1 O GLU E 277 N LEU E 274
SHEET 1 EC 2 PHE E 298 PHE E 299 0
SHEET 2 EC 2 GLY E 530 GLY E 531 1 O GLY E 530 N PHE E 299
SHEET 1 ED 4 VAL E 566 PRO E 567 0
SHEET 2 ED 4 TYR E 573 ILE E 574 -1 O ILE E 574 N VAL E 566
SHEET 3 ED 4 TYR E 578 ILE E 581 -1 O MET E 580 N TYR E 573
SHEET 4 ED 4 ASN E 584 ASN E 587 -1 O ASN E 584 N ILE E 581
LINK C LYS A 306 N TPO A 307 1555 1555 1.33
LINK C TPO A 307 N ALA A 308 1555 1555 1.33
LINK C LYS B 306 N TPO B 307 1555 1555 1.33
LINK C TPO B 307 N ALA B 308 1555 1555 1.33
LINK C LYS C 306 N TPO C 307 1555 1555 1.33
LINK C TPO C 307 N ALA C 308 1555 1555 1.33
LINK C LYS D 306 N TPO D 307 1555 1555 1.33
LINK C TPO D 307 N ALA D 308 1555 1555 1.33
LINK C LYS E 306 N TPO E 307 1555 1555 1.33
LINK C TPO E 307 N ALA E 308 1555 1555 1.33
LINK OE1 GLU A 263 MG MG A1645 1555 1555 2.95
LINK OE2 GLU A 263 MG MG A1645 1555 1555 1.99
LINK OG1 TPO A 307 MG MG A1645 1555 1555 2.20
LINK O3P TPO A 307 MG MG A1645 1555 1555 2.77
LINK OD2 ASP A 481 MG MG A1645 1555 1555 2.04
LINK NE2 HIS A 482 MG MG A1645 1555 1555 2.17
LINK OE2 GLU B 263 MG MG B1645 1555 1555 1.99
LINK OE1 GLU B 263 MG MG B1645 1555 1555 2.93
LINK OG1 TPO B 307 MG MG B1645 1555 1555 2.08
LINK O3P TPO B 307 MG MG B1645 1555 1555 2.75
LINK OD2 ASP B 481 MG MG B1645 1555 1555 2.04
LINK NE2 HIS B 482 MG MG B1645 1555 1555 2.14
LINK OE2 GLU C 263 MG MG C1645 1555 1555 1.98
LINK OE1 GLU C 263 MG MG C1645 1555 1555 2.65
LINK O3P TPO C 307 MG MG C1645 1555 1555 2.40
LINK P TPO C 307 MG MG C1645 1555 1555 2.71
LINK OG1 TPO C 307 MG MG C1645 1555 1555 2.06
LINK OD2 ASP C 481 MG MG C1645 1555 1555 2.08
LINK NE2 HIS C 482 MG MG C1645 1555 1555 2.23
LINK OE2 GLU D 263 MG MG D1645 1555 1555 1.99
LINK O3P TPO D 307 MG MG D1645 1555 1555 2.66
LINK OG1 TPO D 307 MG MG D1645 1555 1555 2.15
LINK OD2 ASP D 481 MG MG D1645 1555 1555 2.02
LINK NE2 HIS D 482 MG MG D1645 1555 1555 2.14
LINK OE2 GLU E 263 MG MG E1645 1555 1555 2.02
LINK O3P TPO E 307 MG MG E1645 1555 1555 2.65
LINK OG1 TPO E 307 MG MG E1645 1555 1555 2.03
LINK OD2 ASP E 481 MG MG E1645 1555 1555 2.08
LINK NE2 HIS E 482 MG MG E1645 1555 1555 2.14
CISPEP 1 GLN A 410 PRO A 411 0 -0.45
CISPEP 2 PHE A 423 PRO A 424 0 4.79
CISPEP 3 GLU A 429 LYS A 430 0 1.24
CISPEP 4 GLN B 410 PRO B 411 0 1.27
CISPEP 5 PHE B 423 PRO B 424 0 4.47
CISPEP 6 GLU B 429 LYS B 430 0 -2.84
CISPEP 7 GLN C 410 PRO C 411 0 -0.49
CISPEP 8 PHE C 423 PRO C 424 0 2.42
CISPEP 9 GLU C 429 LYS C 430 0 1.78
CISPEP 10 GLN D 410 PRO D 411 0 -0.88
CISPEP 11 PHE D 423 PRO D 424 0 4.33
CISPEP 12 GLU D 429 LYS D 430 0 1.37
CISPEP 13 GLN E 410 PRO E 411 0 -0.50
CISPEP 14 PHE E 423 PRO E 424 0 4.99
CISPEP 15 GLU E 429 LYS E 430 0 -4.66
SITE 1 AC1 4 GLU A 263 TPO A 307 ASP A 481 HIS A 482
SITE 1 AC2 4 GLU B 263 TPO B 307 ASP B 481 HIS B 482
SITE 1 AC3 4 GLU C 263 TPO C 307 ASP C 481 HIS C 482
SITE 1 AC4 4 GLU D 263 TPO D 307 ASP D 481 HIS D 482
SITE 1 AC5 4 GLU E 263 TPO E 307 ASP E 481 HIS E 482
CRYST1 119.760 119.760 473.910 90.00 90.00 90.00 P 41 21 2 40
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 0.008350 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008350 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002110 0.00000
MTRIX1 1 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 1 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 1 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 2 -0.860700 0.509000 0.012800 -90.34060 1
MTRIX2 2 -0.509000 -0.860800 0.005600 51.76350 1
MTRIX3 2 0.013900 -0.001700 0.999900 -39.06780 1
MTRIX1 3 0.878100 0.478400 -0.002400 -5.79690 1
MTRIX2 3 0.478400 -0.878100 -0.002900 149.89610 1
MTRIX3 3 -0.003500 0.001400 -1.000000 79.03670 1
MTRIX1 4 0.503100 -0.864100 -0.015500 32.12680 1
MTRIX2 4 0.864200 0.503100 0.008300 111.12950 1
MTRIX3 4 0.000700 -0.017600 0.999800 -78.25850 1
MTRIX1 5 -0.515100 -0.857100 -0.006500 -67.98310 1
MTRIX2 5 -0.856900 0.514800 0.025000 28.91460 1
MTRIX3 5 -0.018000 0.018500 -0.999700 38.86650 1
MTRIX1 6 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 6 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 6 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 7 -0.514628 -0.857401 -0.004655 -68.01523 1
MTRIX2 7 -0.857164 0.514340 0.026905 28.81536 1
MTRIX3 7 -0.020674 0.017836 -0.999627 38.74216 1
MTRIX1 8 0.502595 -0.864356 -0.016952 32.22073 1
MTRIX2 8 0.864521 0.502522 0.008658 111.13499 1
MTRIX3 8 0.001036 -0.019007 0.999819 -78.15736 1
MTRIX1 9 0.878512 0.477721 -0.000283 -5.87117 1
MTRIX2 9 0.477715 -0.878505 -0.004218 149.96748 1
MTRIX3 9 -0.002263 0.003571 -0.999991 78.94776 1
MTRIX1 10 -0.860344 0.509584 0.011492 -90.27109 1
MTRIX2 10 -0.509547 -0.860421 0.006176 51.69691 1
MTRIX3 10 0.013035 -0.000542 0.999915 -39.13647 1
(ATOM LINES ARE NOT SHOWN.)
END
