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HEADER HYDROLASE 04-MAR-23 8ILT
TITLE CRYSTAL STRUCTURE OF EST30
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLESTERASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I;
COMPND 4 SYNONYM: EST30;
COMPND 5 EC: 3.1.1.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GEOBACILLUS STEAROTHERMOPHILUS;
SOURCE 3 ORGANISM_COMMON: BACILLUS STEAROTHERMOPHILUS;
SOURCE 4 ORGANISM_TAXID: 1422;
SOURCE 5 GENE: EST, EST30;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CARBOXYLESTERASE, ENZYME, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.FENG,Z.LUO
REVDAT 1 06-MAR-24 8ILT 0
JRNL AUTH Y.FENG,Z.LUO
JRNL TITL CRYSTAL STRUCTURE OF EST30
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.42 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1-4487
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.42
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.54
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 106615
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.217
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.273
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5611
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 2.4820 - 2.4200 0.99 7752 386 0.3710 0.3610
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.42000
REMARK 3 B22 (A**2) : 4.36000
REMARK 3 B33 (A**2) : -4.20000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.11000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 8ILT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 10-MAR-23.
REMARK 100 THE DEPOSITION ID IS D_1300036000.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JAN-23
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 112238
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.420
REMARK 200 RESOLUTION RANGE LOW (A) : 49.540
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.730
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.7800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.42
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.48
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: ZINC ACETATE TETRAHYDRATE, PEG3350,
REMARK 280 VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 29.99400
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9
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 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 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 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 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 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 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 8
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 9
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 HIS A 252
REMARK 465 HIS A 253
REMARK 465 HIS A 254
REMARK 465 HIS A 255
REMARK 465 HIS B 251
REMARK 465 HIS B 252
REMARK 465 HIS B 253
REMARK 465 HIS B 254
REMARK 465 HIS B 255
REMARK 465 HIS C 254
REMARK 465 HIS C 255
REMARK 465 GLU D 249
REMARK 465 HIS D 250
REMARK 465 HIS D 251
REMARK 465 HIS D 252
REMARK 465 HIS D 253
REMARK 465 HIS D 254
REMARK 465 HIS D 255
REMARK 465 HIS E 255
REMARK 465 GLU F 249
REMARK 465 HIS F 250
REMARK 465 HIS F 251
REMARK 465 HIS F 252
REMARK 465 HIS F 253
REMARK 465 HIS F 254
REMARK 465 HIS F 255
REMARK 465 LEU G 248
REMARK 465 GLU G 249
REMARK 465 HIS G 250
REMARK 465 HIS G 251
REMARK 465 HIS G 252
REMARK 465 HIS G 253
REMARK 465 HIS G 254
REMARK 465 HIS G 255
REMARK 465 GLU H 249
REMARK 465 HIS H 250
REMARK 465 HIS H 251
REMARK 465 HIS H 252
REMARK 465 HIS H 253
REMARK 465 HIS H 254
REMARK 465 HIS H 255
REMARK 465 GLU I 249
REMARK 465 HIS I 250
REMARK 465 HIS I 251
REMARK 465 HIS I 252
REMARK 465 HIS I 253
REMARK 465 HIS I 254
REMARK 465 HIS I 255
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 THR F 64 CG2 THR F 163 2.01
REMARK 500 N GLY E 15 O HOH E 301 2.01
REMARK 500 O THR D 64 CG2 THR D 163 2.04
REMARK 500 O ALA I 240 O HOH I 301 2.07
REMARK 500 O HOH A 340 O HOH A 362 2.08
REMARK 500 OH TYR E 239 O HOH E 302 2.18
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 ALA A 14 -92.64 -137.54
REMARK 500 THR A 26 -9.30 73.00
REMARK 500 ASN A 28 -167.42 -161.26
REMARK 500 SER A 94 -111.10 66.36
REMARK 500 TYR A 120 -132.00 -132.54
REMARK 500 SER A 200 -38.59 -37.74
REMARK 500 ASP A 246 -76.11 -72.90
REMARK 500 PRO B 9 -179.06 -60.86
REMARK 500 ALA B 14 -42.46 -154.61
REMARK 500 SER B 94 -107.32 63.54
REMARK 500 TYR B 120 -126.79 -132.30
REMARK 500 MET B 161 55.66 -141.02
REMARK 500 MET C 2 142.48 -172.60
REMARK 500 ALA C 14 -118.94 -145.19
REMARK 500 SER C 94 -111.28 49.48
REMARK 500 THR C 106 -43.79 -137.99
REMARK 500 TYR C 120 -141.29 -137.51
REMARK 500 PRO D 9 170.41 -59.65
REMARK 500 ALA D 14 -13.04 -157.14
REMARK 500 THR D 26 -7.51 76.46
REMARK 500 SER D 94 -111.39 63.47
REMARK 500 TYR D 120 -148.97 -133.72
REMARK 500 HIS D 192 64.10 -102.18
REMARK 500 TRP D 247 16.29 59.97
REMARK 500 ALA E 14 -6.17 -153.28
REMARK 500 SER E 94 -101.83 67.52
REMARK 500 TYR E 120 -130.49 -125.77
REMARK 500 ALA F 14 -115.92 -145.66
REMARK 500 THR F 26 -11.41 69.97
REMARK 500 SER F 94 -113.16 60.79
REMARK 500 TYR F 120 -125.66 -134.51
REMARK 500 SER F 200 -37.80 -37.06
REMARK 500 ALA G 14 -68.21 -131.49
REMARK 500 THR G 26 -5.44 65.75
REMARK 500 SER G 94 -120.32 59.98
REMARK 500 TYR G 120 -129.99 -128.65
REMARK 500 GLU G 124 -73.68 -57.44
REMARK 500 PRO G 160 55.04 -92.71
REMARK 500 MET H 2 114.98 -173.30
REMARK 500 ALA H 14 -112.55 -145.80
REMARK 500 THR H 26 -10.33 79.88
REMARK 500 SER H 94 -127.10 54.11
REMARK 500 TYR H 120 -144.88 -140.01
REMARK 500 ALA H 135 -70.52 -54.28
REMARK 500 GLU H 142 37.55 -91.50
REMARK 500 MET H 161 -48.53 -135.98
REMARK 500 SER H 200 -36.93 -35.96
REMARK 500 GLN H 214 144.01 -176.72
REMARK 500 TRP H 247 -45.59 80.71
REMARK 500 MET I 2 114.47 -166.28
REMARK 500
REMARK 500 THIS ENTRY HAS 60 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 8ILT A 2 247 UNP Q06174 EST_GEOSE 1 246
DBREF 8ILT B 2 247 UNP Q06174 EST_GEOSE 1 246
DBREF 8ILT C 2 247 UNP Q06174 EST_GEOSE 1 246
DBREF 8ILT D 2 247 UNP Q06174 EST_GEOSE 1 246
DBREF 8ILT E 2 247 UNP Q06174 EST_GEOSE 1 246
DBREF 8ILT F 2 247 UNP Q06174 EST_GEOSE 1 246
DBREF 8ILT G 2 247 UNP Q06174 EST_GEOSE 1 246
DBREF 8ILT H 2 247 UNP Q06174 EST_GEOSE 1 246
DBREF 8ILT I 2 247 UNP Q06174 EST_GEOSE 1 246
SEQADV 8ILT MET A 1 UNP Q06174 INITIATING METHIONINE
SEQADV 8ILT SER A 127 UNP Q06174 MET 126 ENGINEERED MUTATION
SEQADV 8ILT LEU A 130 UNP Q06174 GLY 129 ENGINEERED MUTATION
SEQADV 8ILT LYS A 171 UNP Q06174 ILE 170 ENGINEERED MUTATION
SEQADV 8ILT LEU A 248 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT GLU A 249 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS A 250 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS A 251 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS A 252 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS A 253 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS A 254 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS A 255 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT MET B 1 UNP Q06174 INITIATING METHIONINE
SEQADV 8ILT SER B 127 UNP Q06174 MET 126 ENGINEERED MUTATION
SEQADV 8ILT LEU B 130 UNP Q06174 GLY 129 ENGINEERED MUTATION
SEQADV 8ILT LYS B 171 UNP Q06174 ILE 170 ENGINEERED MUTATION
SEQADV 8ILT LEU B 248 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT GLU B 249 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS B 250 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS B 251 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS B 252 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS B 253 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS B 254 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS B 255 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT MET C 1 UNP Q06174 INITIATING METHIONINE
SEQADV 8ILT SER C 127 UNP Q06174 MET 126 ENGINEERED MUTATION
SEQADV 8ILT LEU C 130 UNP Q06174 GLY 129 ENGINEERED MUTATION
SEQADV 8ILT LYS C 171 UNP Q06174 ILE 170 ENGINEERED MUTATION
SEQADV 8ILT LEU C 248 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT GLU C 249 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS C 250 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS C 251 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS C 252 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS C 253 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS C 254 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS C 255 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT MET D 1 UNP Q06174 INITIATING METHIONINE
SEQADV 8ILT SER D 127 UNP Q06174 MET 126 ENGINEERED MUTATION
SEQADV 8ILT LEU D 130 UNP Q06174 GLY 129 ENGINEERED MUTATION
SEQADV 8ILT LYS D 171 UNP Q06174 ILE 170 ENGINEERED MUTATION
SEQADV 8ILT LEU D 248 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT GLU D 249 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS D 250 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS D 251 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS D 252 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS D 253 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS D 254 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS D 255 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT MET E 1 UNP Q06174 INITIATING METHIONINE
SEQADV 8ILT SER E 127 UNP Q06174 MET 126 ENGINEERED MUTATION
SEQADV 8ILT LEU E 130 UNP Q06174 GLY 129 ENGINEERED MUTATION
SEQADV 8ILT LYS E 171 UNP Q06174 ILE 170 ENGINEERED MUTATION
SEQADV 8ILT LEU E 248 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT GLU E 249 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS E 250 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS E 251 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS E 252 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS E 253 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS E 254 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS E 255 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT MET F 1 UNP Q06174 INITIATING METHIONINE
SEQADV 8ILT SER F 127 UNP Q06174 MET 126 ENGINEERED MUTATION
SEQADV 8ILT LEU F 130 UNP Q06174 GLY 129 ENGINEERED MUTATION
SEQADV 8ILT LYS F 171 UNP Q06174 ILE 170 ENGINEERED MUTATION
SEQADV 8ILT LEU F 248 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT GLU F 249 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS F 250 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS F 251 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS F 252 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS F 253 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS F 254 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS F 255 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT MET G 1 UNP Q06174 INITIATING METHIONINE
SEQADV 8ILT SER G 127 UNP Q06174 MET 126 ENGINEERED MUTATION
SEQADV 8ILT LEU G 130 UNP Q06174 GLY 129 ENGINEERED MUTATION
SEQADV 8ILT LYS G 171 UNP Q06174 ILE 170 ENGINEERED MUTATION
SEQADV 8ILT LEU G 248 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT GLU G 249 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS G 250 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS G 251 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS G 252 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS G 253 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS G 254 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS G 255 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT MET H 1 UNP Q06174 INITIATING METHIONINE
SEQADV 8ILT SER H 127 UNP Q06174 MET 126 ENGINEERED MUTATION
SEQADV 8ILT LEU H 130 UNP Q06174 GLY 129 ENGINEERED MUTATION
SEQADV 8ILT LYS H 171 UNP Q06174 ILE 170 ENGINEERED MUTATION
SEQADV 8ILT LEU H 248 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT GLU H 249 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS H 250 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS H 251 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS H 252 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS H 253 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS H 254 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS H 255 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT MET I 1 UNP Q06174 INITIATING METHIONINE
SEQADV 8ILT SER I 127 UNP Q06174 MET 126 ENGINEERED MUTATION
SEQADV 8ILT LEU I 130 UNP Q06174 GLY 129 ENGINEERED MUTATION
SEQADV 8ILT LYS I 171 UNP Q06174 ILE 170 ENGINEERED MUTATION
SEQADV 8ILT LEU I 248 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT GLU I 249 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS I 250 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS I 251 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS I 252 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS I 253 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS I 254 UNP Q06174 EXPRESSION TAG
SEQADV 8ILT HIS I 255 UNP Q06174 EXPRESSION TAG
SEQRES 1 A 255 MET MET LYS ILE VAL PRO PRO LYS PRO PHE PHE PHE GLU
SEQRES 2 A 255 ALA GLY GLU ARG ALA VAL LEU LEU LEU HIS GLY PHE THR
SEQRES 3 A 255 GLY ASN SER ALA ASP VAL ARG MET LEU GLY ARG PHE LEU
SEQRES 4 A 255 GLU SER LYS GLY TYR THR CYS HIS ALA PRO ILE TYR LYS
SEQRES 5 A 255 GLY HIS GLY VAL PRO PRO GLU GLU LEU VAL HIS THR GLY
SEQRES 6 A 255 PRO ASP ASP TRP TRP GLN ASP VAL MET ASN GLY TYR GLU
SEQRES 7 A 255 PHE LEU LYS ASN LYS GLY TYR GLU LYS ILE ALA VAL ALA
SEQRES 8 A 255 GLY LEU SER LEU GLY GLY VAL PHE SER LEU LYS LEU GLY
SEQRES 9 A 255 TYR THR VAL PRO ILE GLU GLY ILE VAL THR MET CYS ALA
SEQRES 10 A 255 PRO MET TYR ILE LYS SER GLU GLU THR SER TYR GLU LEU
SEQRES 11 A 255 VAL LEU GLU TYR ALA ARG GLU TYR LYS LYS ARG GLU GLY
SEQRES 12 A 255 LYS SER GLU GLU GLN ILE GLU GLN GLU MET GLU LYS PHE
SEQRES 13 A 255 LYS GLN THR PRO MET LYS THR LEU LYS ALA LEU GLN GLU
SEQRES 14 A 255 LEU LYS ALA ASP VAL ARG ASP HIS LEU ASP LEU ILE TYR
SEQRES 15 A 255 ALA PRO THR PHE VAL VAL GLN ALA ARG HIS ASP GLU MET
SEQRES 16 A 255 ILE ASN PRO ASP SER ALA ASN ILE ILE TYR ASN GLU ILE
SEQRES 17 A 255 GLU SER PRO VAL LYS GLN ILE LYS TRP TYR GLU GLN SER
SEQRES 18 A 255 GLY HIS VAL ILE THR LEU ASP GLN GLU LYS ASP GLN LEU
SEQRES 19 A 255 HIS GLU ASP ILE TYR ALA PHE LEU GLU SER LEU ASP TRP
SEQRES 20 A 255 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 255 MET MET LYS ILE VAL PRO PRO LYS PRO PHE PHE PHE GLU
SEQRES 2 B 255 ALA GLY GLU ARG ALA VAL LEU LEU LEU HIS GLY PHE THR
SEQRES 3 B 255 GLY ASN SER ALA ASP VAL ARG MET LEU GLY ARG PHE LEU
SEQRES 4 B 255 GLU SER LYS GLY TYR THR CYS HIS ALA PRO ILE TYR LYS
SEQRES 5 B 255 GLY HIS GLY VAL PRO PRO GLU GLU LEU VAL HIS THR GLY
SEQRES 6 B 255 PRO ASP ASP TRP TRP GLN ASP VAL MET ASN GLY TYR GLU
SEQRES 7 B 255 PHE LEU LYS ASN LYS GLY TYR GLU LYS ILE ALA VAL ALA
SEQRES 8 B 255 GLY LEU SER LEU GLY GLY VAL PHE SER LEU LYS LEU GLY
SEQRES 9 B 255 TYR THR VAL PRO ILE GLU GLY ILE VAL THR MET CYS ALA
SEQRES 10 B 255 PRO MET TYR ILE LYS SER GLU GLU THR SER TYR GLU LEU
SEQRES 11 B 255 VAL LEU GLU TYR ALA ARG GLU TYR LYS LYS ARG GLU GLY
SEQRES 12 B 255 LYS SER GLU GLU GLN ILE GLU GLN GLU MET GLU LYS PHE
SEQRES 13 B 255 LYS GLN THR PRO MET LYS THR LEU LYS ALA LEU GLN GLU
SEQRES 14 B 255 LEU LYS ALA ASP VAL ARG ASP HIS LEU ASP LEU ILE TYR
SEQRES 15 B 255 ALA PRO THR PHE VAL VAL GLN ALA ARG HIS ASP GLU MET
SEQRES 16 B 255 ILE ASN PRO ASP SER ALA ASN ILE ILE TYR ASN GLU ILE
SEQRES 17 B 255 GLU SER PRO VAL LYS GLN ILE LYS TRP TYR GLU GLN SER
SEQRES 18 B 255 GLY HIS VAL ILE THR LEU ASP GLN GLU LYS ASP GLN LEU
SEQRES 19 B 255 HIS GLU ASP ILE TYR ALA PHE LEU GLU SER LEU ASP TRP
SEQRES 20 B 255 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 255 MET MET LYS ILE VAL PRO PRO LYS PRO PHE PHE PHE GLU
SEQRES 2 C 255 ALA GLY GLU ARG ALA VAL LEU LEU LEU HIS GLY PHE THR
SEQRES 3 C 255 GLY ASN SER ALA ASP VAL ARG MET LEU GLY ARG PHE LEU
SEQRES 4 C 255 GLU SER LYS GLY TYR THR CYS HIS ALA PRO ILE TYR LYS
SEQRES 5 C 255 GLY HIS GLY VAL PRO PRO GLU GLU LEU VAL HIS THR GLY
SEQRES 6 C 255 PRO ASP ASP TRP TRP GLN ASP VAL MET ASN GLY TYR GLU
SEQRES 7 C 255 PHE LEU LYS ASN LYS GLY TYR GLU LYS ILE ALA VAL ALA
SEQRES 8 C 255 GLY LEU SER LEU GLY GLY VAL PHE SER LEU LYS LEU GLY
SEQRES 9 C 255 TYR THR VAL PRO ILE GLU GLY ILE VAL THR MET CYS ALA
SEQRES 10 C 255 PRO MET TYR ILE LYS SER GLU GLU THR SER TYR GLU LEU
SEQRES 11 C 255 VAL LEU GLU TYR ALA ARG GLU TYR LYS LYS ARG GLU GLY
SEQRES 12 C 255 LYS SER GLU GLU GLN ILE GLU GLN GLU MET GLU LYS PHE
SEQRES 13 C 255 LYS GLN THR PRO MET LYS THR LEU LYS ALA LEU GLN GLU
SEQRES 14 C 255 LEU LYS ALA ASP VAL ARG ASP HIS LEU ASP LEU ILE TYR
SEQRES 15 C 255 ALA PRO THR PHE VAL VAL GLN ALA ARG HIS ASP GLU MET
SEQRES 16 C 255 ILE ASN PRO ASP SER ALA ASN ILE ILE TYR ASN GLU ILE
SEQRES 17 C 255 GLU SER PRO VAL LYS GLN ILE LYS TRP TYR GLU GLN SER
SEQRES 18 C 255 GLY HIS VAL ILE THR LEU ASP GLN GLU LYS ASP GLN LEU
SEQRES 19 C 255 HIS GLU ASP ILE TYR ALA PHE LEU GLU SER LEU ASP TRP
SEQRES 20 C 255 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 D 255 MET MET LYS ILE VAL PRO PRO LYS PRO PHE PHE PHE GLU
SEQRES 2 D 255 ALA GLY GLU ARG ALA VAL LEU LEU LEU HIS GLY PHE THR
SEQRES 3 D 255 GLY ASN SER ALA ASP VAL ARG MET LEU GLY ARG PHE LEU
SEQRES 4 D 255 GLU SER LYS GLY TYR THR CYS HIS ALA PRO ILE TYR LYS
SEQRES 5 D 255 GLY HIS GLY VAL PRO PRO GLU GLU LEU VAL HIS THR GLY
SEQRES 6 D 255 PRO ASP ASP TRP TRP GLN ASP VAL MET ASN GLY TYR GLU
SEQRES 7 D 255 PHE LEU LYS ASN LYS GLY TYR GLU LYS ILE ALA VAL ALA
SEQRES 8 D 255 GLY LEU SER LEU GLY GLY VAL PHE SER LEU LYS LEU GLY
SEQRES 9 D 255 TYR THR VAL PRO ILE GLU GLY ILE VAL THR MET CYS ALA
SEQRES 10 D 255 PRO MET TYR ILE LYS SER GLU GLU THR SER TYR GLU LEU
SEQRES 11 D 255 VAL LEU GLU TYR ALA ARG GLU TYR LYS LYS ARG GLU GLY
SEQRES 12 D 255 LYS SER GLU GLU GLN ILE GLU GLN GLU MET GLU LYS PHE
SEQRES 13 D 255 LYS GLN THR PRO MET LYS THR LEU LYS ALA LEU GLN GLU
SEQRES 14 D 255 LEU LYS ALA ASP VAL ARG ASP HIS LEU ASP LEU ILE TYR
SEQRES 15 D 255 ALA PRO THR PHE VAL VAL GLN ALA ARG HIS ASP GLU MET
SEQRES 16 D 255 ILE ASN PRO ASP SER ALA ASN ILE ILE TYR ASN GLU ILE
SEQRES 17 D 255 GLU SER PRO VAL LYS GLN ILE LYS TRP TYR GLU GLN SER
SEQRES 18 D 255 GLY HIS VAL ILE THR LEU ASP GLN GLU LYS ASP GLN LEU
SEQRES 19 D 255 HIS GLU ASP ILE TYR ALA PHE LEU GLU SER LEU ASP TRP
SEQRES 20 D 255 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 E 255 MET MET LYS ILE VAL PRO PRO LYS PRO PHE PHE PHE GLU
SEQRES 2 E 255 ALA GLY GLU ARG ALA VAL LEU LEU LEU HIS GLY PHE THR
SEQRES 3 E 255 GLY ASN SER ALA ASP VAL ARG MET LEU GLY ARG PHE LEU
SEQRES 4 E 255 GLU SER LYS GLY TYR THR CYS HIS ALA PRO ILE TYR LYS
SEQRES 5 E 255 GLY HIS GLY VAL PRO PRO GLU GLU LEU VAL HIS THR GLY
SEQRES 6 E 255 PRO ASP ASP TRP TRP GLN ASP VAL MET ASN GLY TYR GLU
SEQRES 7 E 255 PHE LEU LYS ASN LYS GLY TYR GLU LYS ILE ALA VAL ALA
SEQRES 8 E 255 GLY LEU SER LEU GLY GLY VAL PHE SER LEU LYS LEU GLY
SEQRES 9 E 255 TYR THR VAL PRO ILE GLU GLY ILE VAL THR MET CYS ALA
SEQRES 10 E 255 PRO MET TYR ILE LYS SER GLU GLU THR SER TYR GLU LEU
SEQRES 11 E 255 VAL LEU GLU TYR ALA ARG GLU TYR LYS LYS ARG GLU GLY
SEQRES 12 E 255 LYS SER GLU GLU GLN ILE GLU GLN GLU MET GLU LYS PHE
SEQRES 13 E 255 LYS GLN THR PRO MET LYS THR LEU LYS ALA LEU GLN GLU
SEQRES 14 E 255 LEU LYS ALA ASP VAL ARG ASP HIS LEU ASP LEU ILE TYR
SEQRES 15 E 255 ALA PRO THR PHE VAL VAL GLN ALA ARG HIS ASP GLU MET
SEQRES 16 E 255 ILE ASN PRO ASP SER ALA ASN ILE ILE TYR ASN GLU ILE
SEQRES 17 E 255 GLU SER PRO VAL LYS GLN ILE LYS TRP TYR GLU GLN SER
SEQRES 18 E 255 GLY HIS VAL ILE THR LEU ASP GLN GLU LYS ASP GLN LEU
SEQRES 19 E 255 HIS GLU ASP ILE TYR ALA PHE LEU GLU SER LEU ASP TRP
SEQRES 20 E 255 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 F 255 MET MET LYS ILE VAL PRO PRO LYS PRO PHE PHE PHE GLU
SEQRES 2 F 255 ALA GLY GLU ARG ALA VAL LEU LEU LEU HIS GLY PHE THR
SEQRES 3 F 255 GLY ASN SER ALA ASP VAL ARG MET LEU GLY ARG PHE LEU
SEQRES 4 F 255 GLU SER LYS GLY TYR THR CYS HIS ALA PRO ILE TYR LYS
SEQRES 5 F 255 GLY HIS GLY VAL PRO PRO GLU GLU LEU VAL HIS THR GLY
SEQRES 6 F 255 PRO ASP ASP TRP TRP GLN ASP VAL MET ASN GLY TYR GLU
SEQRES 7 F 255 PHE LEU LYS ASN LYS GLY TYR GLU LYS ILE ALA VAL ALA
SEQRES 8 F 255 GLY LEU SER LEU GLY GLY VAL PHE SER LEU LYS LEU GLY
SEQRES 9 F 255 TYR THR VAL PRO ILE GLU GLY ILE VAL THR MET CYS ALA
SEQRES 10 F 255 PRO MET TYR ILE LYS SER GLU GLU THR SER TYR GLU LEU
SEQRES 11 F 255 VAL LEU GLU TYR ALA ARG GLU TYR LYS LYS ARG GLU GLY
SEQRES 12 F 255 LYS SER GLU GLU GLN ILE GLU GLN GLU MET GLU LYS PHE
SEQRES 13 F 255 LYS GLN THR PRO MET LYS THR LEU LYS ALA LEU GLN GLU
SEQRES 14 F 255 LEU LYS ALA ASP VAL ARG ASP HIS LEU ASP LEU ILE TYR
SEQRES 15 F 255 ALA PRO THR PHE VAL VAL GLN ALA ARG HIS ASP GLU MET
SEQRES 16 F 255 ILE ASN PRO ASP SER ALA ASN ILE ILE TYR ASN GLU ILE
SEQRES 17 F 255 GLU SER PRO VAL LYS GLN ILE LYS TRP TYR GLU GLN SER
SEQRES 18 F 255 GLY HIS VAL ILE THR LEU ASP GLN GLU LYS ASP GLN LEU
SEQRES 19 F 255 HIS GLU ASP ILE TYR ALA PHE LEU GLU SER LEU ASP TRP
SEQRES 20 F 255 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 G 255 MET MET LYS ILE VAL PRO PRO LYS PRO PHE PHE PHE GLU
SEQRES 2 G 255 ALA GLY GLU ARG ALA VAL LEU LEU LEU HIS GLY PHE THR
SEQRES 3 G 255 GLY ASN SER ALA ASP VAL ARG MET LEU GLY ARG PHE LEU
SEQRES 4 G 255 GLU SER LYS GLY TYR THR CYS HIS ALA PRO ILE TYR LYS
SEQRES 5 G 255 GLY HIS GLY VAL PRO PRO GLU GLU LEU VAL HIS THR GLY
SEQRES 6 G 255 PRO ASP ASP TRP TRP GLN ASP VAL MET ASN GLY TYR GLU
SEQRES 7 G 255 PHE LEU LYS ASN LYS GLY TYR GLU LYS ILE ALA VAL ALA
SEQRES 8 G 255 GLY LEU SER LEU GLY GLY VAL PHE SER LEU LYS LEU GLY
SEQRES 9 G 255 TYR THR VAL PRO ILE GLU GLY ILE VAL THR MET CYS ALA
SEQRES 10 G 255 PRO MET TYR ILE LYS SER GLU GLU THR SER TYR GLU LEU
SEQRES 11 G 255 VAL LEU GLU TYR ALA ARG GLU TYR LYS LYS ARG GLU GLY
SEQRES 12 G 255 LYS SER GLU GLU GLN ILE GLU GLN GLU MET GLU LYS PHE
SEQRES 13 G 255 LYS GLN THR PRO MET LYS THR LEU LYS ALA LEU GLN GLU
SEQRES 14 G 255 LEU LYS ALA ASP VAL ARG ASP HIS LEU ASP LEU ILE TYR
SEQRES 15 G 255 ALA PRO THR PHE VAL VAL GLN ALA ARG HIS ASP GLU MET
SEQRES 16 G 255 ILE ASN PRO ASP SER ALA ASN ILE ILE TYR ASN GLU ILE
SEQRES 17 G 255 GLU SER PRO VAL LYS GLN ILE LYS TRP TYR GLU GLN SER
SEQRES 18 G 255 GLY HIS VAL ILE THR LEU ASP GLN GLU LYS ASP GLN LEU
SEQRES 19 G 255 HIS GLU ASP ILE TYR ALA PHE LEU GLU SER LEU ASP TRP
SEQRES 20 G 255 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 H 255 MET MET LYS ILE VAL PRO PRO LYS PRO PHE PHE PHE GLU
SEQRES 2 H 255 ALA GLY GLU ARG ALA VAL LEU LEU LEU HIS GLY PHE THR
SEQRES 3 H 255 GLY ASN SER ALA ASP VAL ARG MET LEU GLY ARG PHE LEU
SEQRES 4 H 255 GLU SER LYS GLY TYR THR CYS HIS ALA PRO ILE TYR LYS
SEQRES 5 H 255 GLY HIS GLY VAL PRO PRO GLU GLU LEU VAL HIS THR GLY
SEQRES 6 H 255 PRO ASP ASP TRP TRP GLN ASP VAL MET ASN GLY TYR GLU
SEQRES 7 H 255 PHE LEU LYS ASN LYS GLY TYR GLU LYS ILE ALA VAL ALA
SEQRES 8 H 255 GLY LEU SER LEU GLY GLY VAL PHE SER LEU LYS LEU GLY
SEQRES 9 H 255 TYR THR VAL PRO ILE GLU GLY ILE VAL THR MET CYS ALA
SEQRES 10 H 255 PRO MET TYR ILE LYS SER GLU GLU THR SER TYR GLU LEU
SEQRES 11 H 255 VAL LEU GLU TYR ALA ARG GLU TYR LYS LYS ARG GLU GLY
SEQRES 12 H 255 LYS SER GLU GLU GLN ILE GLU GLN GLU MET GLU LYS PHE
SEQRES 13 H 255 LYS GLN THR PRO MET LYS THR LEU LYS ALA LEU GLN GLU
SEQRES 14 H 255 LEU LYS ALA ASP VAL ARG ASP HIS LEU ASP LEU ILE TYR
SEQRES 15 H 255 ALA PRO THR PHE VAL VAL GLN ALA ARG HIS ASP GLU MET
SEQRES 16 H 255 ILE ASN PRO ASP SER ALA ASN ILE ILE TYR ASN GLU ILE
SEQRES 17 H 255 GLU SER PRO VAL LYS GLN ILE LYS TRP TYR GLU GLN SER
SEQRES 18 H 255 GLY HIS VAL ILE THR LEU ASP GLN GLU LYS ASP GLN LEU
SEQRES 19 H 255 HIS GLU ASP ILE TYR ALA PHE LEU GLU SER LEU ASP TRP
SEQRES 20 H 255 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 I 255 MET MET LYS ILE VAL PRO PRO LYS PRO PHE PHE PHE GLU
SEQRES 2 I 255 ALA GLY GLU ARG ALA VAL LEU LEU LEU HIS GLY PHE THR
SEQRES 3 I 255 GLY ASN SER ALA ASP VAL ARG MET LEU GLY ARG PHE LEU
SEQRES 4 I 255 GLU SER LYS GLY TYR THR CYS HIS ALA PRO ILE TYR LYS
SEQRES 5 I 255 GLY HIS GLY VAL PRO PRO GLU GLU LEU VAL HIS THR GLY
SEQRES 6 I 255 PRO ASP ASP TRP TRP GLN ASP VAL MET ASN GLY TYR GLU
SEQRES 7 I 255 PHE LEU LYS ASN LYS GLY TYR GLU LYS ILE ALA VAL ALA
SEQRES 8 I 255 GLY LEU SER LEU GLY GLY VAL PHE SER LEU LYS LEU GLY
SEQRES 9 I 255 TYR THR VAL PRO ILE GLU GLY ILE VAL THR MET CYS ALA
SEQRES 10 I 255 PRO MET TYR ILE LYS SER GLU GLU THR SER TYR GLU LEU
SEQRES 11 I 255 VAL LEU GLU TYR ALA ARG GLU TYR LYS LYS ARG GLU GLY
SEQRES 12 I 255 LYS SER GLU GLU GLN ILE GLU GLN GLU MET GLU LYS PHE
SEQRES 13 I 255 LYS GLN THR PRO MET LYS THR LEU LYS ALA LEU GLN GLU
SEQRES 14 I 255 LEU LYS ALA ASP VAL ARG ASP HIS LEU ASP LEU ILE TYR
SEQRES 15 I 255 ALA PRO THR PHE VAL VAL GLN ALA ARG HIS ASP GLU MET
SEQRES 16 I 255 ILE ASN PRO ASP SER ALA ASN ILE ILE TYR ASN GLU ILE
SEQRES 17 I 255 GLU SER PRO VAL LYS GLN ILE LYS TRP TYR GLU GLN SER
SEQRES 18 I 255 GLY HIS VAL ILE THR LEU ASP GLN GLU LYS ASP GLN LEU
SEQRES 19 I 255 HIS GLU ASP ILE TYR ALA PHE LEU GLU SER LEU ASP TRP
SEQRES 20 I 255 LEU GLU HIS HIS HIS HIS HIS HIS
FORMUL 10 HOH *415(H2 O)
HELIX 1 AA1 ASN A 28 ASP A 31 5 4
HELIX 2 AA2 VAL A 32 LYS A 42 1 11
HELIX 3 AA3 PRO A 57 VAL A 62 1 6
HELIX 4 AA4 GLY A 65 LYS A 83 1 19
HELIX 5 AA5 SER A 94 TYR A 105 1 12
HELIX 6 AA6 ILE A 121 GLU A 142 1 22
HELIX 7 AA7 SER A 145 GLN A 158 1 14
HELIX 8 AA8 LYS A 162 HIS A 177 1 16
HELIX 9 AA9 LEU A 178 ILE A 181 5 4
HELIX 10 AB1 ASP A 199 ILE A 208 1 10
HELIX 11 AB2 VAL A 224 ASP A 228 5 5
HELIX 12 AB3 GLU A 230 SER A 244 1 15
HELIX 13 AB4 SER B 29 LYS B 42 1 14
HELIX 14 AB5 PRO B 57 VAL B 62 1 6
HELIX 15 AB6 GLY B 65 LYS B 83 1 19
HELIX 16 AB7 SER B 94 TYR B 105 1 12
HELIX 17 AB8 ILE B 121 GLU B 142 1 22
HELIX 18 AB9 SER B 145 GLN B 158 1 14
HELIX 19 AC1 MET B 161 HIS B 177 1 17
HELIX 20 AC2 LEU B 178 ILE B 181 5 4
HELIX 21 AC3 ASP B 199 ILE B 208 1 10
HELIX 22 AC4 VAL B 224 ASP B 228 5 5
HELIX 23 AC5 GLU B 230 SER B 244 1 15
HELIX 24 AC6 ASN C 28 ASP C 31 5 4
HELIX 25 AC7 VAL C 32 LYS C 42 1 11
HELIX 26 AC8 PRO C 57 VAL C 62 1 6
HELIX 27 AC9 GLY C 65 LYS C 83 1 19
HELIX 28 AD1 SER C 94 TYR C 105 1 12
HELIX 29 AD2 ILE C 121 GLU C 142 1 22
HELIX 30 AD3 SER C 145 LYS C 157 1 13
HELIX 31 AD4 PRO C 160 ASP C 176 1 17
HELIX 32 AD5 HIS C 177 ILE C 181 5 5
HELIX 33 AD6 ASP C 199 ILE C 208 1 10
HELIX 34 AD7 VAL C 224 ASP C 228 5 5
HELIX 35 AD8 GLU C 230 SER C 244 1 15
HELIX 36 AD9 ASN D 28 ASP D 31 5 4
HELIX 37 AE1 VAL D 32 LYS D 42 1 11
HELIX 38 AE2 PRO D 57 VAL D 62 1 6
HELIX 39 AE3 GLY D 65 LYS D 83 1 19
HELIX 40 AE4 SER D 94 TYR D 105 1 12
HELIX 41 AE5 ILE D 121 GLU D 142 1 22
HELIX 42 AE6 SER D 145 LYS D 157 1 13
HELIX 43 AE7 PRO D 160 ASP D 176 1 17
HELIX 44 AE8 HIS D 177 ILE D 181 5 5
HELIX 45 AE9 ASP D 199 ILE D 208 1 10
HELIX 46 AF1 VAL D 224 ASP D 228 5 5
HELIX 47 AF2 GLU D 230 SER D 244 1 15
HELIX 48 AF3 ASN E 28 ASP E 31 5 4
HELIX 49 AF4 VAL E 32 LYS E 42 1 11
HELIX 50 AF5 PRO E 57 VAL E 62 1 6
HELIX 51 AF6 GLY E 65 LYS E 83 1 19
HELIX 52 AF7 SER E 94 TYR E 105 1 12
HELIX 53 AF8 ILE E 121 GLU E 142 1 22
HELIX 54 AF9 SER E 145 LYS E 157 1 13
HELIX 55 AG1 PRO E 160 LEU E 178 1 19
HELIX 56 AG2 ASP E 179 ILE E 181 5 3
HELIX 57 AG3 ASP E 199 ILE E 208 1 10
HELIX 58 AG4 VAL E 224 ASP E 228 5 5
HELIX 59 AG5 GLU E 230 LEU E 245 1 16
HELIX 60 AG6 ASN F 28 ASP F 31 5 4
HELIX 61 AG7 VAL F 32 SER F 41 1 10
HELIX 62 AG8 PRO F 57 VAL F 62 1 6
HELIX 63 AG9 GLY F 65 ASN F 82 1 18
HELIX 64 AH1 SER F 94 GLY F 104 1 11
HELIX 65 AH2 ILE F 121 GLY F 143 1 23
HELIX 66 AH3 SER F 145 LYS F 157 1 13
HELIX 67 AH4 PRO F 160 LEU F 178 1 19
HELIX 68 AH5 ASP F 179 ILE F 181 5 3
HELIX 69 AH6 ASP F 199 ILE F 208 1 10
HELIX 70 AH7 VAL F 224 ASP F 228 5 5
HELIX 71 AH8 GLU F 230 SER F 244 1 15
HELIX 72 AH9 ASN G 28 ASP G 31 5 4
HELIX 73 AI1 VAL G 32 LYS G 42 1 11
HELIX 74 AI2 PRO G 57 VAL G 62 1 6
HELIX 75 AI3 GLY G 65 LYS G 83 1 19
HELIX 76 AI4 SER G 94 TYR G 105 1 12
HELIX 77 AI5 ILE G 121 GLU G 142 1 22
HELIX 78 AI6 SER G 145 LYS G 157 1 13
HELIX 79 AI7 MET G 161 HIS G 177 1 17
HELIX 80 AI8 LEU G 178 ILE G 181 5 4
HELIX 81 AI9 ASP G 199 ILE G 208 1 10
HELIX 82 AJ1 GLU G 230 SER G 244 1 15
HELIX 83 AJ2 ASN H 28 ASP H 31 5 4
HELIX 84 AJ3 VAL H 32 LYS H 42 1 11
HELIX 85 AJ4 PRO H 57 VAL H 62 1 6
HELIX 86 AJ5 GLY H 65 LYS H 83 1 19
HELIX 87 AJ6 SER H 94 LEU H 103 1 10
HELIX 88 AJ7 GLY H 104 THR H 106 5 3
HELIX 89 AJ8 ILE H 121 GLU H 142 1 22
HELIX 90 AJ9 SER H 145 LYS H 157 1 13
HELIX 91 AK1 MET H 161 ASP H 176 1 16
HELIX 92 AK2 HIS H 177 ILE H 181 5 5
HELIX 93 AK3 ASP H 199 ILE H 208 1 10
HELIX 94 AK4 GLU H 230 LEU H 245 1 16
HELIX 95 AK5 SER I 29 SER I 41 1 13
HELIX 96 AK6 PRO I 57 VAL I 62 1 6
HELIX 97 AK7 GLY I 65 LYS I 83 1 19
HELIX 98 AK8 SER I 94 GLY I 104 1 11
HELIX 99 AK9 ILE I 121 GLU I 142 1 22
HELIX 100 AL1 SER I 145 LYS I 157 1 13
HELIX 101 AL2 THR I 163 HIS I 177 1 15
HELIX 102 AL3 LEU I 178 ILE I 181 5 4
HELIX 103 AL4 ASP I 199 ILE I 208 1 10
HELIX 104 AL5 VAL I 224 ASP I 228 5 5
HELIX 105 AL6 GLU I 230 LEU I 245 1 16
SHEET 1 AA1 7 PHE A 10 PHE A 12 0
SHEET 2 AA1 7 THR A 45 ALA A 48 -1 O CYS A 46 N PHE A 12
SHEET 3 AA1 7 ALA A 18 LEU A 22 1 N LEU A 21 O HIS A 47
SHEET 4 AA1 7 ILE A 88 LEU A 93 1 O LEU A 93 N LEU A 22
SHEET 5 AA1 7 ILE A 112 MET A 115 1 O VAL A 113 N GLY A 92
SHEET 6 AA1 7 THR A 185 ALA A 190 1 O VAL A 188 N THR A 114
SHEET 7 AA1 7 LYS A 213 TYR A 218 1 O GLN A 214 N VAL A 187
SHEET 1 AA2 7 PHE B 10 PHE B 12 0
SHEET 2 AA2 7 THR B 45 ALA B 48 -1 O CYS B 46 N PHE B 12
SHEET 3 AA2 7 ALA B 18 LEU B 22 1 N LEU B 21 O HIS B 47
SHEET 4 AA2 7 ILE B 88 LEU B 93 1 O ALA B 89 N LEU B 20
SHEET 5 AA2 7 ILE B 112 MET B 115 1 O MET B 115 N GLY B 92
SHEET 6 AA2 7 THR B 185 ALA B 190 1 O PHE B 186 N ILE B 112
SHEET 7 AA2 7 LYS B 213 TYR B 218 1 O GLN B 214 N VAL B 187
SHEET 1 AA3 7 PHE C 10 PHE C 12 0
SHEET 2 AA3 7 THR C 45 ALA C 48 -1 O CYS C 46 N PHE C 12
SHEET 3 AA3 7 ALA C 18 LEU C 22 1 N LEU C 21 O HIS C 47
SHEET 4 AA3 7 ILE C 88 LEU C 93 1 O ALA C 91 N LEU C 20
SHEET 5 AA3 7 ILE C 112 MET C 115 1 O MET C 115 N GLY C 92
SHEET 6 AA3 7 THR C 185 ALA C 190 1 O VAL C 188 N THR C 114
SHEET 7 AA3 7 LYS C 213 TYR C 218 1 O GLN C 214 N VAL C 187
SHEET 1 AA4 7 PHE D 10 PHE D 12 0
SHEET 2 AA4 7 THR D 45 ALA D 48 -1 O CYS D 46 N PHE D 12
SHEET 3 AA4 7 ALA D 18 LEU D 22 1 N LEU D 21 O HIS D 47
SHEET 4 AA4 7 ILE D 88 LEU D 93 1 O ALA D 91 N LEU D 20
SHEET 5 AA4 7 ILE D 112 MET D 115 1 O MET D 115 N GLY D 92
SHEET 6 AA4 7 THR D 185 ALA D 190 1 O PHE D 186 N ILE D 112
SHEET 7 AA4 7 LYS D 213 TYR D 218 1 O GLN D 214 N VAL D 187
SHEET 1 AA5 7 PHE E 10 PHE E 12 0
SHEET 2 AA5 7 THR E 45 ALA E 48 -1 O CYS E 46 N PHE E 12
SHEET 3 AA5 7 ALA E 18 LEU E 22 1 N LEU E 21 O HIS E 47
SHEET 4 AA5 7 ILE E 88 LEU E 93 1 O ALA E 91 N LEU E 20
SHEET 5 AA5 7 ILE E 112 MET E 115 1 O VAL E 113 N GLY E 92
SHEET 6 AA5 7 THR E 185 ALA E 190 1 O PHE E 186 N ILE E 112
SHEET 7 AA5 7 LYS E 213 TYR E 218 1 O GLN E 214 N VAL E 187
SHEET 1 AA6 7 PHE F 10 PHE F 12 0
SHEET 2 AA6 7 THR F 45 ALA F 48 -1 O CYS F 46 N PHE F 12
SHEET 3 AA6 7 ALA F 18 LEU F 22 1 N LEU F 21 O HIS F 47
SHEET 4 AA6 7 ILE F 88 LEU F 93 1 O ALA F 89 N ALA F 18
SHEET 5 AA6 7 ILE F 112 MET F 115 1 O MET F 115 N GLY F 92
SHEET 6 AA6 7 THR F 185 ALA F 190 1 O PHE F 186 N ILE F 112
SHEET 7 AA6 7 LYS F 213 TYR F 218 1 O GLN F 214 N VAL F 187
SHEET 1 AA7 7 PHE G 10 PHE G 12 0
SHEET 2 AA7 7 THR G 45 ALA G 48 -1 O CYS G 46 N PHE G 12
SHEET 3 AA7 7 ALA G 18 LEU G 22 1 N LEU G 21 O HIS G 47
SHEET 4 AA7 7 ILE G 88 LEU G 93 1 O ALA G 91 N LEU G 22
SHEET 5 AA7 7 ILE G 112 MET G 115 1 O MET G 115 N GLY G 92
SHEET 6 AA7 7 THR G 185 ALA G 190 1 O PHE G 186 N THR G 114
SHEET 7 AA7 7 LYS G 213 TYR G 218 1 O TYR G 218 N GLN G 189
SHEET 1 AA8 2 PHE H 10 PHE H 12 0
SHEET 2 AA8 2 CYS H 46 ALA H 48 -1 O CYS H 46 N PHE H 12
SHEET 1 AA9 5 ALA H 18 LEU H 22 0
SHEET 2 AA9 5 ILE H 88 LEU H 93 1 O ALA H 89 N LEU H 20
SHEET 3 AA9 5 ILE H 112 MET H 115 1 O MET H 115 N GLY H 92
SHEET 4 AA9 5 THR H 185 ALA H 190 1 O VAL H 188 N THR H 114
SHEET 5 AA9 5 ILE H 215 TYR H 218 1 O LYS H 216 N VAL H 187
SHEET 1 AB1 2 PHE I 10 PHE I 12 0
SHEET 2 AB1 2 CYS I 46 ALA I 48 -1 O CYS I 46 N PHE I 12
SHEET 1 AB2 5 ALA I 18 LEU I 22 0
SHEET 2 AB2 5 ILE I 88 LEU I 93 1 O ALA I 91 N LEU I 20
SHEET 3 AB2 5 ILE I 112 MET I 115 1 O MET I 115 N GLY I 92
SHEET 4 AB2 5 THR I 185 ALA I 190 1 O PHE I 186 N ILE I 112
SHEET 5 AB2 5 LYS I 213 TYR I 218 1 O TYR I 218 N GLN I 189
CRYST1 149.964 59.988 166.039 90.00 99.24 90.00 P 1 21 1 18
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 0.006668 0.000000 0.001085 0.00000
SCALE2 0.000000 0.016670 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006102 0.00000
TER 2044 HIS A 251
TER 4085 HIS B 250
TER 6144 HIS C 253
TER 8154 LEU D 248
TER 10231 HIS E 254
TER 12241 LEU F 248
TER 14246 TRP G 247
TER 16256 LEU H 248
TER 18266 LEU I 248
MASTER 375 0 0 105 63 0 0 618644 9 0 180
END |