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HEADER LYASE 20-FEB-17 5UW3
TITLE PCY1 IN COMPLEX WITH FOLLOWER PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEPTIDE CYCLASE 1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: PRESEGETALIN A1;
COMPND 7 CHAIN: E, F, G, H;
COMPND 8 FRAGMENT: UNP RESIDUES 14-32;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VACCARIA HISPANICA;
SOURCE 3 ORGANISM_TAXID: 39387;
SOURCE 4 GENE: PCY1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 SYNTHETIC: YES;
SOURCE 9 ORGANISM_SCIENTIFIC: VACCARIA HISPANICA;
SOURCE 10 ORGANISM_TAXID: 39387
KEYWDS NATURAL PRODUCT, ORBITIDE, CYCLASE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.R.CHEKAN,S.K.NAIR
REVDAT 3 05-JUL-17 5UW3 1 JRNL
REVDAT 2 21-JUN-17 5UW3 1 JRNL
REVDAT 1 31-MAY-17 5UW3 0
JRNL AUTH J.R.CHEKAN,P.ESTRADA,P.S.COVELLO,S.K.NAIR
JRNL TITL CHARACTERIZATION OF THE MACROCYCLASE INVOLVED IN THE
JRNL TITL 2 BIOSYNTHESIS OF RIPP CYCLIC PEPTIDES IN PLANTS.
JRNL REF PROC. NATL. ACAD. SCI. V. 114 6551 2017
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 28584123
JRNL DOI 10.1073/PNAS.1620499114
REMARK 2
REMARK 2 RESOLUTION. 1.96 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.96
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 3 NUMBER OF REFLECTIONS : 191296
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) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 9945
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) : 1.96
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.01
REMARK 3 REFLECTION IN BIN (WORKING SET) : 14335
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.66
REMARK 3 BIN R VALUE (WORKING SET) : 0.2170
REMARK 3 BIN FREE R VALUE SET COUNT : 678
REMARK 3 BIN FREE R VALUE : 0.2600
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 22650
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 2061
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.96
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.51000
REMARK 3 B22 (A**2) : -0.45000
REMARK 3 B33 (A**2) : 0.04000
REMARK 3 B12 (A**2) : 0.55000
REMARK 3 B13 (A**2) : 0.26000
REMARK 3 B23 (A**2) : -0.19000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.198
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.163
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.118
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.122
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.936
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.912
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 23248 ; 0.017 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 21696 ; 0.009 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 31491 ; 1.684 ; 1.952
REMARK 3 BOND ANGLES OTHERS (DEGREES): 49991 ; 1.461 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2808 ; 6.545 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1153 ;33.297 ;23.981
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3884 ;14.469 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 145 ;16.257 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3340 ; 0.108 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 26372 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 5535 ; 0.008 ; 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): 11280 ; 1.825 ; 1.781
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 11279 ; 1.825 ; 1.781
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14072 ; 2.710 ; 2.661
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 14073 ; 2.710 ; 2.661
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 11968 ; 2.391 ; 2.086
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 11969 ; 2.391 ; 2.086
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 17420 ; 3.729 ; 3.023
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 27947 ; 6.081 ;15.363
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 27186 ; 5.952 ;15.164
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 6
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 12 1031 B 12 1031 42209 0.10 0.05
REMARK 3 2 A 12 1031 C 12 1031 42052 0.11 0.05
REMARK 3 3 A 12 1031 D 12 1031 41917 0.10 0.05
REMARK 3 4 B 5 1031 C 5 1031 42313 0.11 0.05
REMARK 3 5 B 3 1032 D 3 1032 42586 0.10 0.05
REMARK 3 6 C 5 1032 D 5 1032 42377 0.11 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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
REMARK 4
REMARK 4 5UW3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1000226243.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-DEC-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97856
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AUTOPROC
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 201248
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.960
REMARK 200 RESOLUTION RANGE LOW (A) : 44.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.12900
REMARK 200 FOR THE DATA SET : 8.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.96
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.52500
REMARK 200 FOR SHELL : 3.300
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: 1QFS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG 8,000, 0.2 M CALCIUM ACETATE,
REMARK 280 0.1 M SODIUM CACODYLATE (PH 6.5), 14 MG/ML PROTEIN, PROTEIN WAS
REMARK 280 PREINCUBATED WITH 5 MM BORIC ACID AND 1 MM PSA1 [14-32], VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 282K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, G
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -25
REMARK 465 SER A -24
REMARK 465 TYR A -23
REMARK 465 TYR A -22
REMARK 465 HIS A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 LEU A -15
REMARK 465 GLU A -14
REMARK 465 SER A -13
REMARK 465 THR A -12
REMARK 465 SER A -11
REMARK 465 LEU A -10
REMARK 465 TYR A -9
REMARK 465 LYS A -8
REMARK 465 LYS A -7
REMARK 465 ALA A -6
REMARK 465 GLY A -5
REMARK 465 SER A -4
REMARK 465 GLU A -3
REMARK 465 PHE A -2
REMARK 465 ALA A -1
REMARK 465 LEU A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 THR A 3
REMARK 465 SER A 4
REMARK 465 GLY A 5
REMARK 465 PHE A 6
REMARK 465 SER A 7
REMARK 465 LYS A 8
REMARK 465 PRO A 9
REMARK 465 LEU A 10
REMARK 465 HIS A 11
REMARK 465 LEU A 198
REMARK 465 LYS A 199
REMARK 465 GLU A 200
REMARK 465 GLY A 201
REMARK 465 GLU A 202
REMARK 465 ASP A 203
REMARK 465 HIS A 204
REMARK 465 MET A 205
REMARK 465 THR A 206
REMARK 465 ARG A 207
REMARK 465 SER A 208
REMARK 465 ALA A 209
REMARK 465 VAL A 210
REMARK 465 ARG A 281
REMARK 465 GLY A 282
REMARK 465 ARG A 283
REMARK 465 GLU A 284
REMARK 465 ASP A 285
REMARK 465 SER A 286
REMARK 465 ASP A 724
REMARK 465 GLY E 1014
REMARK 465 VAL E 1015
REMARK 465 PRO E 1016
REMARK 465 VAL E 1017
REMARK 465 TRP E 1018
REMARK 465 ALA E 1019
REMARK 465 PHE E 1020
REMARK 465 GLN E 1021
REMARK 465 ALA E 1022
REMARK 465 LYS E 1023
REMARK 465 ASP E 1024
REMARK 465 VAL E 1025
REMARK 465 GLU E 1026
REMARK 465 MET B -25
REMARK 465 SER B -24
REMARK 465 TYR B -23
REMARK 465 TYR B -22
REMARK 465 HIS B -21
REMARK 465 HIS B -20
REMARK 465 HIS B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 LEU B -15
REMARK 465 GLU B -14
REMARK 465 SER B -13
REMARK 465 THR B -12
REMARK 465 SER B -11
REMARK 465 LEU B -10
REMARK 465 TYR B -9
REMARK 465 LYS B -8
REMARK 465 LYS B -7
REMARK 465 ALA B -6
REMARK 465 GLY B -5
REMARK 465 SER B -4
REMARK 465 GLU B -3
REMARK 465 PHE B -2
REMARK 465 ALA B -1
REMARK 465 LEU B 0
REMARK 465 LEU B 198
REMARK 465 LYS B 199
REMARK 465 GLU B 200
REMARK 465 GLY B 201
REMARK 465 GLU B 202
REMARK 465 ASP B 203
REMARK 465 HIS B 204
REMARK 465 MET B 205
REMARK 465 THR B 206
REMARK 465 ARG B 207
REMARK 465 SER B 208
REMARK 465 PHE B 280
REMARK 465 ARG B 281
REMARK 465 GLY B 282
REMARK 465 ARG B 283
REMARK 465 GLU B 284
REMARK 465 ASP B 285
REMARK 465 GLY F 1014
REMARK 465 VAL F 1015
REMARK 465 PRO F 1016
REMARK 465 VAL F 1017
REMARK 465 TRP F 1018
REMARK 465 ALA F 1019
REMARK 465 PHE F 1020
REMARK 465 GLN F 1021
REMARK 465 ALA F 1022
REMARK 465 LYS F 1023
REMARK 465 ASP F 1024
REMARK 465 VAL F 1025
REMARK 465 GLU F 1026
REMARK 465 MET C -25
REMARK 465 SER C -24
REMARK 465 TYR C -23
REMARK 465 TYR C -22
REMARK 465 HIS C -21
REMARK 465 HIS C -20
REMARK 465 HIS C -19
REMARK 465 HIS C -18
REMARK 465 HIS C -17
REMARK 465 HIS C -16
REMARK 465 LEU C -15
REMARK 465 GLU C -14
REMARK 465 SER C -13
REMARK 465 THR C -12
REMARK 465 SER C -11
REMARK 465 LEU C -10
REMARK 465 TYR C -9
REMARK 465 LYS C -8
REMARK 465 LYS C -7
REMARK 465 ALA C -6
REMARK 465 GLY C -5
REMARK 465 SER C -4
REMARK 465 GLU C -3
REMARK 465 PHE C -2
REMARK 465 ALA C -1
REMARK 465 LEU C 0
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 THR C 3
REMARK 465 SER C 4
REMARK 465 LEU C 198
REMARK 465 LYS C 199
REMARK 465 GLU C 200
REMARK 465 GLY C 201
REMARK 465 GLU C 202
REMARK 465 ASP C 203
REMARK 465 HIS C 204
REMARK 465 MET C 205
REMARK 465 THR C 206
REMARK 465 ARG C 207
REMARK 465 SER C 208
REMARK 465 ALA C 209
REMARK 465 GLY C 282
REMARK 465 ARG C 283
REMARK 465 GLU C 284
REMARK 465 ASP C 285
REMARK 465 SER C 286
REMARK 465 ASP C 724
REMARK 465 GLY G 1014
REMARK 465 VAL G 1015
REMARK 465 PRO G 1016
REMARK 465 VAL G 1017
REMARK 465 TRP G 1018
REMARK 465 ALA G 1019
REMARK 465 PHE G 1020
REMARK 465 GLN G 1021
REMARK 465 ALA G 1022
REMARK 465 LYS G 1023
REMARK 465 ASP G 1024
REMARK 465 VAL G 1025
REMARK 465 GLU G 1026
REMARK 465 MET D -25
REMARK 465 SER D -24
REMARK 465 TYR D -23
REMARK 465 TYR D -22
REMARK 465 HIS D -21
REMARK 465 HIS D -20
REMARK 465 HIS D -19
REMARK 465 HIS D -18
REMARK 465 HIS D -17
REMARK 465 HIS D -16
REMARK 465 LEU D -15
REMARK 465 GLU D -14
REMARK 465 SER D -13
REMARK 465 THR D -12
REMARK 465 SER D -11
REMARK 465 LEU D -10
REMARK 465 TYR D -9
REMARK 465 LYS D -8
REMARK 465 LYS D -7
REMARK 465 ALA D -6
REMARK 465 GLY D -5
REMARK 465 SER D -4
REMARK 465 GLU D -3
REMARK 465 PHE D -2
REMARK 465 ALA D -1
REMARK 465 LEU D 0
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 PRO D 197
REMARK 465 LEU D 198
REMARK 465 LYS D 199
REMARK 465 GLU D 200
REMARK 465 GLY D 201
REMARK 465 GLU D 202
REMARK 465 ASP D 203
REMARK 465 HIS D 204
REMARK 465 MET D 205
REMARK 465 THR D 206
REMARK 465 ARG D 207
REMARK 465 SER D 208
REMARK 465 ALA D 209
REMARK 465 VAL D 210
REMARK 465 GLU D 278
REMARK 465 SER D 279
REMARK 465 PHE D 280
REMARK 465 ARG D 281
REMARK 465 GLY D 282
REMARK 465 ARG D 283
REMARK 465 GLU D 284
REMARK 465 ASP D 285
REMARK 465 SER D 286
REMARK 465 ASP D 724
REMARK 465 GLY H 1014
REMARK 465 VAL H 1015
REMARK 465 PRO H 1016
REMARK 465 VAL H 1017
REMARK 465 TRP H 1018
REMARK 465 ALA H 1019
REMARK 465 PHE H 1020
REMARK 465 GLN H 1021
REMARK 465 ALA H 1022
REMARK 465 LYS H 1023
REMARK 465 ASP H 1024
REMARK 465 VAL H 1025
REMARK 465 GLU H 1026
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 HOH C 1357 O HOH C 1371 1.77
REMARK 500 O HOH D 902 O HOH D 904 1.79
REMARK 500 CG ASN C 422 O HOH C 902 1.81
REMARK 500 O HOH D 1367 O HOH D 1376 1.83
REMARK 500 O ARG B 231 O HOH B 901 1.85
REMARK 500 CE LYS A 321 O HOH A 905 1.89
REMARK 500 O HOH A 903 O HOH A 941 1.89
REMARK 500 OD1 ASP C 246 O HOH C 901 1.89
REMARK 500 O HOH B 1041 O HOH B 1337 1.91
REMARK 500 O HOH A 1301 O HOH A 1332 1.91
REMARK 500 O HOH C 916 O HOH C 1236 1.92
REMARK 500 O HOH C 1304 O HOH C 1352 1.93
REMARK 500 O HOH B 1279 O HOH B 1295 1.93
REMARK 500 O HOH D 1346 O HOH D 1370 1.94
REMARK 500 SD MET D 714 O HOH D 1365 1.95
REMARK 500 NE ARG A 710 O HOH A 901 1.96
REMARK 500 NE ARG B 710 O HOH B 902 1.99
REMARK 500 SD MET B 714 O HOH B 1318 1.99
REMARK 500 ND2 ASN C 422 O HOH C 902 2.00
REMARK 500 CB LEU B 161 O HOH B 1326 2.00
REMARK 500 O ALA B 553 O LEU B 578 2.00
REMARK 500 O HOH D 1279 O HOH D 1369 2.01
REMARK 500 O HOH A 915 O HOH A 1077 2.02
REMARK 500 O HOH B 1041 O HOH B 1242 2.03
REMARK 500 O2 CAC D 801 O HOH D 901 2.04
REMARK 500 NH1 ARG C 320 O SER C 341 2.05
REMARK 500 N ASN D 211 O HOH D 902 2.05
REMARK 500 SG CYS A 673 O HOH A 929 2.05
REMARK 500 C TYR D 135 O HOH D 908 2.06
REMARK 500 O HOH A 1245 O HOH A 1301 2.07
REMARK 500 OH TYR D 195 O HOH D 903 2.07
REMARK 500 O ALA D 553 O LEU D 578 2.08
REMARK 500 N ASN F 1027 O HOH F 1101 2.09
REMARK 500 SD MET A 714 O HOH A 1291 2.09
REMARK 500 C ILE C 723 O HOH C 1063 2.09
REMARK 500 O HOH A 919 O HOH A 1124 2.10
REMARK 500 O MET B 589 ND1 HIS B 660 2.10
REMARK 500 O MET D 589 ND1 HIS D 660 2.11
REMARK 500 O HOH A 1280 O HOH A 1318 2.11
REMARK 500 NH2 ARG C 440 O HOH C 903 2.11
REMARK 500 OH TYR A 622 O HOH A 902 2.11
REMARK 500 O HOH A 937 O HOH A 1187 2.12
REMARK 500 O HOH C 909 O HOH C 1050 2.12
REMARK 500 O HOH A 1175 O HOH A 1299 2.12
REMARK 500 O VAL A 30 O HOH A 903 2.12
REMARK 500 OE1 GLU A 719 O HOH A 904 2.13
REMARK 500 N ALA C 287 O HOH C 904 2.14
REMARK 500 CG LYS A 663 O HOH A 1227 2.14
REMARK 500 O SER A 58 OE1 GLU A 61 2.14
REMARK 500 NZ LYS A 321 O HOH A 905 2.14
REMARK 500
REMARK 500 THIS ENTRY HAS 60 CLOSE CONTACTS
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH2 ARG A 554 OE1 GLU D 638 1456 2.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 TRP B 618 CB TRP B 618 CG -0.128
REMARK 500 GLY C 608 N GLY C 608 CA 0.160
REMARK 500 ARG D 496 CD ARG D 496 NE -0.107
REMARK 500 GLY D 608 N GLY D 608 CA 0.163
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 161 CA - CB - CG ANGL. DEV. = 16.8 DEGREES
REMARK 500 LEU A 161 CB - CG - CD1 ANGL. DEV. = -11.4 DEGREES
REMARK 500 ASP A 269 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 336 CB - CG - OD1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ARG A 360 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 382 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 LEU B 161 CA - CB - CG ANGL. DEV. = 15.7 DEGREES
REMARK 500 ASP B 336 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP B 590 N - CA - CB ANGL. DEV. = 11.0 DEGREES
REMARK 500 THR B 598 CB - CA - C ANGL. DEV. = -17.5 DEGREES
REMARK 500 LEU B 599 CA - CB - CG ANGL. DEV. = 14.4 DEGREES
REMARK 500 ARG B 710 CD - NE - CZ ANGL. DEV. = 9.3 DEGREES
REMARK 500 LEU C 134 CA - CB - CG ANGL. DEV. = 14.5 DEGREES
REMARK 500 ARG C 360 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG C 396 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 TYR C 607 O - C - N ANGL. DEV. = -12.1 DEGREES
REMARK 500 GLY C 608 C - N - CA ANGL. DEV. = -25.3 DEGREES
REMARK 500 ASP D 336 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ARG D 496 CD - NE - CZ ANGL. DEV. = 9.1 DEGREES
REMARK 500 ARG D 496 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG D 496 NE - CZ - NH2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 MET D 589 O - C - N ANGL. DEV. = -10.4 DEGREES
REMARK 500 ASP D 590 N - CA - CB ANGL. DEV. = 13.0 DEGREES
REMARK 500 TYR D 607 O - C - N ANGL. DEV. = -12.1 DEGREES
REMARK 500 GLY D 608 C - N - CA ANGL. DEV. = -26.3 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 ALA A 89 -126.53 50.05
REMARK 500 LYS A 177 -87.54 -121.30
REMARK 500 ALA A 318 79.86 -156.07
REMARK 500 LYS A 321 159.43 65.61
REMARK 500 GLU A 354 -47.29 71.36
REMARK 500 ASP A 423 64.69 -153.77
REMARK 500 TYR A 481 -76.70 -135.41
REMARK 500 ARG A 528 -119.89 55.88
REMARK 500 ARG A 554 -2.93 80.72
REMARK 500 SER A 562 -119.10 63.19
REMARK 500 CYS A 586 57.46 33.86
REMARK 500 THR A 598 -107.98 31.39
REMARK 500 CYS A 673 -65.45 -127.64
REMARK 500 ALA B 89 -123.40 55.54
REMARK 500 TRP B 175 37.04 71.24
REMARK 500 LYS B 177 -88.46 -120.56
REMARK 500 ARG B 231 -39.35 -141.74
REMARK 500 ASP B 232 71.89 50.61
REMARK 500 ALA B 318 78.86 -154.52
REMARK 500 LYS B 321 160.04 68.51
REMARK 500 GLU B 354 -48.44 70.19
REMARK 500 ASP B 423 62.44 -154.43
REMARK 500 TYR B 481 -75.84 -134.85
REMARK 500 ARG B 528 -118.29 54.06
REMARK 500 SER B 562 -116.79 63.02
REMARK 500 CYS B 586 55.38 36.79
REMARK 500 ASP B 590 65.50 73.22
REMARK 500 THR B 598 77.73 8.01
REMARK 500 LEU B 599 -9.36 86.24
REMARK 500 CYS B 673 -65.51 -128.94
REMARK 500 ALA C 89 -123.57 52.56
REMARK 500 LYS C 177 -86.77 -120.92
REMARK 500 ARG C 231 -39.47 -143.82
REMARK 500 ASP C 232 73.81 51.13
REMARK 500 SER C 279 -28.31 -38.85
REMARK 500 ALA C 318 83.16 -154.29
REMARK 500 LYS C 321 155.14 72.16
REMARK 500 GLU C 354 -53.59 66.11
REMARK 500 ASP C 423 67.26 -152.05
REMARK 500 TYR C 481 -77.12 -135.71
REMARK 500 ARG C 528 -119.10 56.14
REMARK 500 SER C 562 -117.32 62.16
REMARK 500 CYS C 586 56.85 35.71
REMARK 500 THR C 598 -105.74 31.74
REMARK 500 CYS C 673 -63.49 -128.89
REMARK 500 ALA D 89 -121.13 50.07
REMARK 500 LYS D 177 -86.11 -120.85
REMARK 500 ASP D 257 -75.49 -96.00
REMARK 500 ALA D 318 81.06 -156.48
REMARK 500 LYS D 321 157.11 68.25
REMARK 500
REMARK 500 THIS ENTRY HAS 59 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1351 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH C1462 DISTANCE = 6.01 ANGSTROMS
REMARK 525 HOH C1463 DISTANCE = 6.42 ANGSTROMS
REMARK 525 HOH D1435 DISTANCE = 6.90 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CAC A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CAC B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CAC C 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CAC D 801
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5UW5 RELATED DB: PDB
REMARK 900 RELATED ID: 5UW6 RELATED DB: PDB
REMARK 900 RELATED ID: 5UW7 RELATED DB: PDB
REMARK 900 RELATED ID: 5UZW RELATED DB: PDB
DBREF 5UW3 A 1 724 UNP R4P353 R4P353_9CARY 1 724
DBREF 5UW3 E 1014 1032 UNP F6LNL5 F6LNL5_9CARY 14 32
DBREF 5UW3 B 1 724 UNP R4P353 R4P353_9CARY 1 724
DBREF 5UW3 F 1014 1032 UNP F6LNL5 F6LNL5_9CARY 14 32
DBREF 5UW3 C 1 724 UNP R4P353 R4P353_9CARY 1 724
DBREF 5UW3 G 1014 1032 UNP F6LNL5 F6LNL5_9CARY 14 32
DBREF 5UW3 D 1 724 UNP R4P353 R4P353_9CARY 1 724
DBREF 5UW3 H 1014 1032 UNP F6LNL5 F6LNL5_9CARY 14 32
SEQADV 5UW3 MET A -25 UNP R4P353 INITIATING METHIONINE
SEQADV 5UW3 SER A -24 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 TYR A -23 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 TYR A -22 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 HIS A -21 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 HIS A -20 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 HIS A -19 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 HIS A -18 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 HIS A -17 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 HIS A -16 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 LEU A -15 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 GLU A -14 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 SER A -13 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 THR A -12 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 SER A -11 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 LEU A -10 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 TYR A -9 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 LYS A -8 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 LYS A -7 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 ALA A -6 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 GLY A -5 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 SER A -4 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 GLU A -3 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 PHE A -2 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 ALA A -1 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 LEU A 0 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 MET B -25 UNP R4P353 INITIATING METHIONINE
SEQADV 5UW3 SER B -24 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 TYR B -23 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 TYR B -22 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 HIS B -21 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 HIS B -20 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 HIS B -19 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 HIS B -18 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 HIS B -17 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 HIS B -16 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 LEU B -15 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 GLU B -14 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 SER B -13 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 THR B -12 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 SER B -11 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 LEU B -10 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 TYR B -9 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 LYS B -8 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 LYS B -7 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 ALA B -6 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 GLY B -5 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 SER B -4 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 GLU B -3 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 PHE B -2 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 ALA B -1 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 LEU B 0 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 MET C -25 UNP R4P353 INITIATING METHIONINE
SEQADV 5UW3 SER C -24 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 TYR C -23 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 TYR C -22 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 HIS C -21 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 HIS C -20 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 HIS C -19 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 HIS C -18 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 HIS C -17 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 HIS C -16 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 LEU C -15 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 GLU C -14 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 SER C -13 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 THR C -12 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 SER C -11 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 LEU C -10 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 TYR C -9 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 LYS C -8 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 LYS C -7 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 ALA C -6 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 GLY C -5 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 SER C -4 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 GLU C -3 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 PHE C -2 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 ALA C -1 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 LEU C 0 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 MET D -25 UNP R4P353 INITIATING METHIONINE
SEQADV 5UW3 SER D -24 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 TYR D -23 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 TYR D -22 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 HIS D -21 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 HIS D -20 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 HIS D -19 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 HIS D -18 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 HIS D -17 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 HIS D -16 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 LEU D -15 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 GLU D -14 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 SER D -13 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 THR D -12 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 SER D -11 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 LEU D -10 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 TYR D -9 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 LYS D -8 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 LYS D -7 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 ALA D -6 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 GLY D -5 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 SER D -4 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 GLU D -3 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 PHE D -2 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 ALA D -1 UNP R4P353 EXPRESSION TAG
SEQADV 5UW3 LEU D 0 UNP R4P353 EXPRESSION TAG
SEQRES 1 A 750 MET SER TYR TYR HIS HIS HIS HIS HIS HIS LEU GLU SER
SEQRES 2 A 750 THR SER LEU TYR LYS LYS ALA GLY SER GLU PHE ALA LEU
SEQRES 3 A 750 MET ALA THR SER GLY PHE SER LYS PRO LEU HIS TYR PRO
SEQRES 4 A 750 PRO VAL ARG ARG ASP GLU THR VAL VAL ASP ASP TYR PHE
SEQRES 5 A 750 GLY VAL LYS VAL ALA ASP PRO TYR ARG TRP LEU GLU ASP
SEQRES 6 A 750 PRO ASN SER GLU GLU THR LYS GLU PHE VAL ASP ASN GLN
SEQRES 7 A 750 GLU LYS LEU ALA ASN SER VAL LEU GLU GLU CYS GLU LEU
SEQRES 8 A 750 ILE ASP LYS PHE LYS GLN LYS ILE ILE ASP PHE VAL ASN
SEQRES 9 A 750 PHE PRO ARG CYS GLY VAL PRO PHE ARG ARG ALA ASN LYS
SEQRES 10 A 750 TYR PHE HIS PHE TYR ASN SER GLY LEU GLN ALA GLN ASN
SEQRES 11 A 750 VAL PHE GLN MET GLN ASP ASP LEU ASP GLY LYS PRO GLU
SEQRES 12 A 750 VAL LEU TYR ASP PRO ASN LEU ARG GLU GLY GLY ARG SER
SEQRES 13 A 750 GLY LEU SER LEU TYR SER VAL SER GLU ASP ALA LYS TYR
SEQRES 14 A 750 PHE ALA PHE GLY ILE HIS SER GLY LEU THR GLU TRP VAL
SEQRES 15 A 750 THR ILE LYS ILE LEU LYS THR GLU ASP ARG SER TYR LEU
SEQRES 16 A 750 PRO ASP THR LEU GLU TRP VAL LYS PHE SER PRO ALA ILE
SEQRES 17 A 750 TRP THR HIS ASP ASN LYS GLY PHE PHE TYR CYS PRO TYR
SEQRES 18 A 750 PRO PRO LEU LYS GLU GLY GLU ASP HIS MET THR ARG SER
SEQRES 19 A 750 ALA VAL ASN GLN GLU ALA ARG TYR HIS PHE LEU GLY THR
SEQRES 20 A 750 ASP GLN SER GLU ASP ILE LEU LEU TRP ARG ASP LEU GLU
SEQRES 21 A 750 ASN PRO ALA HIS HIS LEU LYS CYS GLN ILE THR ASP ASP
SEQRES 22 A 750 GLY LYS TYR PHE LEU LEU TYR ILE LEU ASP GLY CYS ASP
SEQRES 23 A 750 ASP ALA ASN LYS VAL TYR CYS LEU ASP LEU THR LYS LEU
SEQRES 24 A 750 PRO ASN GLY LEU GLU SER PHE ARG GLY ARG GLU ASP SER
SEQRES 25 A 750 ALA PRO PHE MET LYS LEU ILE ASP SER PHE ASP ALA SER
SEQRES 26 A 750 TYR THR ALA ILE ALA ASN ASP GLY SER VAL PHE THR PHE
SEQRES 27 A 750 GLN THR ASN LYS ASP ALA PRO ARG LYS LYS LEU VAL ARG
SEQRES 28 A 750 VAL ASP LEU ASN ASN PRO SER VAL TRP THR ASP LEU VAL
SEQRES 29 A 750 PRO GLU SER LYS LYS ASP LEU LEU GLU SER ALA HIS ALA
SEQRES 30 A 750 VAL ASN GLU ASN GLN LEU ILE LEU ARG TYR LEU SER ASP
SEQRES 31 A 750 VAL LYS HIS VAL LEU GLU ILE ARG ASP LEU GLU SER GLY
SEQRES 32 A 750 ALA LEU GLN HIS ARG LEU PRO ILE ASP ILE GLY SER VAL
SEQRES 33 A 750 ASP GLY ILE THR ALA ARG ARG ARG ASP SER VAL VAL PHE
SEQRES 34 A 750 PHE LYS PHE THR SER ILE LEU THR PRO GLY ILE VAL TYR
SEQRES 35 A 750 GLN CYS ASP LEU LYS ASN ASP PRO THR GLN LEU LYS ILE
SEQRES 36 A 750 PHE ARG GLU SER VAL VAL PRO ASP PHE ASP ARG SER GLU
SEQRES 37 A 750 PHE GLU VAL LYS GLN VAL PHE VAL PRO SER LYS ASP GLY
SEQRES 38 A 750 THR LYS ILE PRO ILE PHE ILE ALA ALA ARG LYS GLY ILE
SEQRES 39 A 750 SER LEU ASP GLY SER HIS PRO CYS GLU MET HIS GLY TYR
SEQRES 40 A 750 GLY GLY PHE GLY ILE ASN MET MET PRO THR PHE SER ALA
SEQRES 41 A 750 SER ARG ILE VAL PHE LEU LYS HIS LEU GLY GLY VAL PHE
SEQRES 42 A 750 CYS LEU ALA ASN ILE ARG GLY GLY GLY GLU TYR GLY GLU
SEQRES 43 A 750 GLU TRP HIS LYS ALA GLY PHE ARG ASP LYS LYS GLN ASN
SEQRES 44 A 750 VAL PHE ASP ASP PHE ILE SER ALA ALA GLU TYR LEU ILE
SEQRES 45 A 750 SER SER GLY TYR THR LYS ALA ARG ARG VAL ALA ILE GLU
SEQRES 46 A 750 GLY GLY SER ASN GLY GLY LEU LEU VAL ALA ALA CYS ILE
SEQRES 47 A 750 ASN GLN ARG PRO ASP LEU PHE GLY CYS ALA GLU ALA ASN
SEQRES 48 A 750 CYS GLY VAL MET ASP MET LEU ARG PHE HIS LYS PHE THR
SEQRES 49 A 750 LEU GLY TYR LEU TRP THR GLY ASP TYR GLY CYS SER ASP
SEQRES 50 A 750 LYS GLU GLU GLU PHE LYS TRP LEU ILE LYS TYR SER PRO
SEQRES 51 A 750 ILE HIS ASN VAL ARG ARG PRO TRP GLU GLN PRO GLY ASN
SEQRES 52 A 750 GLU GLU THR GLN TYR PRO ALA THR MET ILE LEU THR ALA
SEQRES 53 A 750 ASP HIS ASP ASP ARG VAL VAL PRO LEU HIS SER PHE LYS
SEQRES 54 A 750 LEU LEU ALA THR MET GLN HIS VAL LEU CYS THR SER LEU
SEQRES 55 A 750 GLU ASP SER PRO GLN LYS ASN PRO ILE ILE ALA ARG ILE
SEQRES 56 A 750 GLN ARG LYS ALA ALA HIS TYR GLY ARG ALA THR MET THR
SEQRES 57 A 750 GLN ILE ALA GLU VAL ALA ASP ARG TYR GLY PHE MET ALA
SEQRES 58 A 750 LYS ALA LEU GLU ALA PRO TRP ILE ASP
SEQRES 1 E 19 GLY VAL PRO VAL TRP ALA PHE GLN ALA LYS ASP VAL GLU
SEQRES 2 E 19 ASN ALA SER ALA PRO VAL
SEQRES 1 B 750 MET SER TYR TYR HIS HIS HIS HIS HIS HIS LEU GLU SER
SEQRES 2 B 750 THR SER LEU TYR LYS LYS ALA GLY SER GLU PHE ALA LEU
SEQRES 3 B 750 MET ALA THR SER GLY PHE SER LYS PRO LEU HIS TYR PRO
SEQRES 4 B 750 PRO VAL ARG ARG ASP GLU THR VAL VAL ASP ASP TYR PHE
SEQRES 5 B 750 GLY VAL LYS VAL ALA ASP PRO TYR ARG TRP LEU GLU ASP
SEQRES 6 B 750 PRO ASN SER GLU GLU THR LYS GLU PHE VAL ASP ASN GLN
SEQRES 7 B 750 GLU LYS LEU ALA ASN SER VAL LEU GLU GLU CYS GLU LEU
SEQRES 8 B 750 ILE ASP LYS PHE LYS GLN LYS ILE ILE ASP PHE VAL ASN
SEQRES 9 B 750 PHE PRO ARG CYS GLY VAL PRO PHE ARG ARG ALA ASN LYS
SEQRES 10 B 750 TYR PHE HIS PHE TYR ASN SER GLY LEU GLN ALA GLN ASN
SEQRES 11 B 750 VAL PHE GLN MET GLN ASP ASP LEU ASP GLY LYS PRO GLU
SEQRES 12 B 750 VAL LEU TYR ASP PRO ASN LEU ARG GLU GLY GLY ARG SER
SEQRES 13 B 750 GLY LEU SER LEU TYR SER VAL SER GLU ASP ALA LYS TYR
SEQRES 14 B 750 PHE ALA PHE GLY ILE HIS SER GLY LEU THR GLU TRP VAL
SEQRES 15 B 750 THR ILE LYS ILE LEU LYS THR GLU ASP ARG SER TYR LEU
SEQRES 16 B 750 PRO ASP THR LEU GLU TRP VAL LYS PHE SER PRO ALA ILE
SEQRES 17 B 750 TRP THR HIS ASP ASN LYS GLY PHE PHE TYR CYS PRO TYR
SEQRES 18 B 750 PRO PRO LEU LYS GLU GLY GLU ASP HIS MET THR ARG SER
SEQRES 19 B 750 ALA VAL ASN GLN GLU ALA ARG TYR HIS PHE LEU GLY THR
SEQRES 20 B 750 ASP GLN SER GLU ASP ILE LEU LEU TRP ARG ASP LEU GLU
SEQRES 21 B 750 ASN PRO ALA HIS HIS LEU LYS CYS GLN ILE THR ASP ASP
SEQRES 22 B 750 GLY LYS TYR PHE LEU LEU TYR ILE LEU ASP GLY CYS ASP
SEQRES 23 B 750 ASP ALA ASN LYS VAL TYR CYS LEU ASP LEU THR LYS LEU
SEQRES 24 B 750 PRO ASN GLY LEU GLU SER PHE ARG GLY ARG GLU ASP SER
SEQRES 25 B 750 ALA PRO PHE MET LYS LEU ILE ASP SER PHE ASP ALA SER
SEQRES 26 B 750 TYR THR ALA ILE ALA ASN ASP GLY SER VAL PHE THR PHE
SEQRES 27 B 750 GLN THR ASN LYS ASP ALA PRO ARG LYS LYS LEU VAL ARG
SEQRES 28 B 750 VAL ASP LEU ASN ASN PRO SER VAL TRP THR ASP LEU VAL
SEQRES 29 B 750 PRO GLU SER LYS LYS ASP LEU LEU GLU SER ALA HIS ALA
SEQRES 30 B 750 VAL ASN GLU ASN GLN LEU ILE LEU ARG TYR LEU SER ASP
SEQRES 31 B 750 VAL LYS HIS VAL LEU GLU ILE ARG ASP LEU GLU SER GLY
SEQRES 32 B 750 ALA LEU GLN HIS ARG LEU PRO ILE ASP ILE GLY SER VAL
SEQRES 33 B 750 ASP GLY ILE THR ALA ARG ARG ARG ASP SER VAL VAL PHE
SEQRES 34 B 750 PHE LYS PHE THR SER ILE LEU THR PRO GLY ILE VAL TYR
SEQRES 35 B 750 GLN CYS ASP LEU LYS ASN ASP PRO THR GLN LEU LYS ILE
SEQRES 36 B 750 PHE ARG GLU SER VAL VAL PRO ASP PHE ASP ARG SER GLU
SEQRES 37 B 750 PHE GLU VAL LYS GLN VAL PHE VAL PRO SER LYS ASP GLY
SEQRES 38 B 750 THR LYS ILE PRO ILE PHE ILE ALA ALA ARG LYS GLY ILE
SEQRES 39 B 750 SER LEU ASP GLY SER HIS PRO CYS GLU MET HIS GLY TYR
SEQRES 40 B 750 GLY GLY PHE GLY ILE ASN MET MET PRO THR PHE SER ALA
SEQRES 41 B 750 SER ARG ILE VAL PHE LEU LYS HIS LEU GLY GLY VAL PHE
SEQRES 42 B 750 CYS LEU ALA ASN ILE ARG GLY GLY GLY GLU TYR GLY GLU
SEQRES 43 B 750 GLU TRP HIS LYS ALA GLY PHE ARG ASP LYS LYS GLN ASN
SEQRES 44 B 750 VAL PHE ASP ASP PHE ILE SER ALA ALA GLU TYR LEU ILE
SEQRES 45 B 750 SER SER GLY TYR THR LYS ALA ARG ARG VAL ALA ILE GLU
SEQRES 46 B 750 GLY GLY SER ASN GLY GLY LEU LEU VAL ALA ALA CYS ILE
SEQRES 47 B 750 ASN GLN ARG PRO ASP LEU PHE GLY CYS ALA GLU ALA ASN
SEQRES 48 B 750 CYS GLY VAL MET ASP MET LEU ARG PHE HIS LYS PHE THR
SEQRES 49 B 750 LEU GLY TYR LEU TRP THR GLY ASP TYR GLY CYS SER ASP
SEQRES 50 B 750 LYS GLU GLU GLU PHE LYS TRP LEU ILE LYS TYR SER PRO
SEQRES 51 B 750 ILE HIS ASN VAL ARG ARG PRO TRP GLU GLN PRO GLY ASN
SEQRES 52 B 750 GLU GLU THR GLN TYR PRO ALA THR MET ILE LEU THR ALA
SEQRES 53 B 750 ASP HIS ASP ASP ARG VAL VAL PRO LEU HIS SER PHE LYS
SEQRES 54 B 750 LEU LEU ALA THR MET GLN HIS VAL LEU CYS THR SER LEU
SEQRES 55 B 750 GLU ASP SER PRO GLN LYS ASN PRO ILE ILE ALA ARG ILE
SEQRES 56 B 750 GLN ARG LYS ALA ALA HIS TYR GLY ARG ALA THR MET THR
SEQRES 57 B 750 GLN ILE ALA GLU VAL ALA ASP ARG TYR GLY PHE MET ALA
SEQRES 58 B 750 LYS ALA LEU GLU ALA PRO TRP ILE ASP
SEQRES 1 F 19 GLY VAL PRO VAL TRP ALA PHE GLN ALA LYS ASP VAL GLU
SEQRES 2 F 19 ASN ALA SER ALA PRO VAL
SEQRES 1 C 750 MET SER TYR TYR HIS HIS HIS HIS HIS HIS LEU GLU SER
SEQRES 2 C 750 THR SER LEU TYR LYS LYS ALA GLY SER GLU PHE ALA LEU
SEQRES 3 C 750 MET ALA THR SER GLY PHE SER LYS PRO LEU HIS TYR PRO
SEQRES 4 C 750 PRO VAL ARG ARG ASP GLU THR VAL VAL ASP ASP TYR PHE
SEQRES 5 C 750 GLY VAL LYS VAL ALA ASP PRO TYR ARG TRP LEU GLU ASP
SEQRES 6 C 750 PRO ASN SER GLU GLU THR LYS GLU PHE VAL ASP ASN GLN
SEQRES 7 C 750 GLU LYS LEU ALA ASN SER VAL LEU GLU GLU CYS GLU LEU
SEQRES 8 C 750 ILE ASP LYS PHE LYS GLN LYS ILE ILE ASP PHE VAL ASN
SEQRES 9 C 750 PHE PRO ARG CYS GLY VAL PRO PHE ARG ARG ALA ASN LYS
SEQRES 10 C 750 TYR PHE HIS PHE TYR ASN SER GLY LEU GLN ALA GLN ASN
SEQRES 11 C 750 VAL PHE GLN MET GLN ASP ASP LEU ASP GLY LYS PRO GLU
SEQRES 12 C 750 VAL LEU TYR ASP PRO ASN LEU ARG GLU GLY GLY ARG SER
SEQRES 13 C 750 GLY LEU SER LEU TYR SER VAL SER GLU ASP ALA LYS TYR
SEQRES 14 C 750 PHE ALA PHE GLY ILE HIS SER GLY LEU THR GLU TRP VAL
SEQRES 15 C 750 THR ILE LYS ILE LEU LYS THR GLU ASP ARG SER TYR LEU
SEQRES 16 C 750 PRO ASP THR LEU GLU TRP VAL LYS PHE SER PRO ALA ILE
SEQRES 17 C 750 TRP THR HIS ASP ASN LYS GLY PHE PHE TYR CYS PRO TYR
SEQRES 18 C 750 PRO PRO LEU LYS GLU GLY GLU ASP HIS MET THR ARG SER
SEQRES 19 C 750 ALA VAL ASN GLN GLU ALA ARG TYR HIS PHE LEU GLY THR
SEQRES 20 C 750 ASP GLN SER GLU ASP ILE LEU LEU TRP ARG ASP LEU GLU
SEQRES 21 C 750 ASN PRO ALA HIS HIS LEU LYS CYS GLN ILE THR ASP ASP
SEQRES 22 C 750 GLY LYS TYR PHE LEU LEU TYR ILE LEU ASP GLY CYS ASP
SEQRES 23 C 750 ASP ALA ASN LYS VAL TYR CYS LEU ASP LEU THR LYS LEU
SEQRES 24 C 750 PRO ASN GLY LEU GLU SER PHE ARG GLY ARG GLU ASP SER
SEQRES 25 C 750 ALA PRO PHE MET LYS LEU ILE ASP SER PHE ASP ALA SER
SEQRES 26 C 750 TYR THR ALA ILE ALA ASN ASP GLY SER VAL PHE THR PHE
SEQRES 27 C 750 GLN THR ASN LYS ASP ALA PRO ARG LYS LYS LEU VAL ARG
SEQRES 28 C 750 VAL ASP LEU ASN ASN PRO SER VAL TRP THR ASP LEU VAL
SEQRES 29 C 750 PRO GLU SER LYS LYS ASP LEU LEU GLU SER ALA HIS ALA
SEQRES 30 C 750 VAL ASN GLU ASN GLN LEU ILE LEU ARG TYR LEU SER ASP
SEQRES 31 C 750 VAL LYS HIS VAL LEU GLU ILE ARG ASP LEU GLU SER GLY
SEQRES 32 C 750 ALA LEU GLN HIS ARG LEU PRO ILE ASP ILE GLY SER VAL
SEQRES 33 C 750 ASP GLY ILE THR ALA ARG ARG ARG ASP SER VAL VAL PHE
SEQRES 34 C 750 PHE LYS PHE THR SER ILE LEU THR PRO GLY ILE VAL TYR
SEQRES 35 C 750 GLN CYS ASP LEU LYS ASN ASP PRO THR GLN LEU LYS ILE
SEQRES 36 C 750 PHE ARG GLU SER VAL VAL PRO ASP PHE ASP ARG SER GLU
SEQRES 37 C 750 PHE GLU VAL LYS GLN VAL PHE VAL PRO SER LYS ASP GLY
SEQRES 38 C 750 THR LYS ILE PRO ILE PHE ILE ALA ALA ARG LYS GLY ILE
SEQRES 39 C 750 SER LEU ASP GLY SER HIS PRO CYS GLU MET HIS GLY TYR
SEQRES 40 C 750 GLY GLY PHE GLY ILE ASN MET MET PRO THR PHE SER ALA
SEQRES 41 C 750 SER ARG ILE VAL PHE LEU LYS HIS LEU GLY GLY VAL PHE
SEQRES 42 C 750 CYS LEU ALA ASN ILE ARG GLY GLY GLY GLU TYR GLY GLU
SEQRES 43 C 750 GLU TRP HIS LYS ALA GLY PHE ARG ASP LYS LYS GLN ASN
SEQRES 44 C 750 VAL PHE ASP ASP PHE ILE SER ALA ALA GLU TYR LEU ILE
SEQRES 45 C 750 SER SER GLY TYR THR LYS ALA ARG ARG VAL ALA ILE GLU
SEQRES 46 C 750 GLY GLY SER ASN GLY GLY LEU LEU VAL ALA ALA CYS ILE
SEQRES 47 C 750 ASN GLN ARG PRO ASP LEU PHE GLY CYS ALA GLU ALA ASN
SEQRES 48 C 750 CYS GLY VAL MET ASP MET LEU ARG PHE HIS LYS PHE THR
SEQRES 49 C 750 LEU GLY TYR LEU TRP THR GLY ASP TYR GLY CYS SER ASP
SEQRES 50 C 750 LYS GLU GLU GLU PHE LYS TRP LEU ILE LYS TYR SER PRO
SEQRES 51 C 750 ILE HIS ASN VAL ARG ARG PRO TRP GLU GLN PRO GLY ASN
SEQRES 52 C 750 GLU GLU THR GLN TYR PRO ALA THR MET ILE LEU THR ALA
SEQRES 53 C 750 ASP HIS ASP ASP ARG VAL VAL PRO LEU HIS SER PHE LYS
SEQRES 54 C 750 LEU LEU ALA THR MET GLN HIS VAL LEU CYS THR SER LEU
SEQRES 55 C 750 GLU ASP SER PRO GLN LYS ASN PRO ILE ILE ALA ARG ILE
SEQRES 56 C 750 GLN ARG LYS ALA ALA HIS TYR GLY ARG ALA THR MET THR
SEQRES 57 C 750 GLN ILE ALA GLU VAL ALA ASP ARG TYR GLY PHE MET ALA
SEQRES 58 C 750 LYS ALA LEU GLU ALA PRO TRP ILE ASP
SEQRES 1 G 19 GLY VAL PRO VAL TRP ALA PHE GLN ALA LYS ASP VAL GLU
SEQRES 2 G 19 ASN ALA SER ALA PRO VAL
SEQRES 1 D 750 MET SER TYR TYR HIS HIS HIS HIS HIS HIS LEU GLU SER
SEQRES 2 D 750 THR SER LEU TYR LYS LYS ALA GLY SER GLU PHE ALA LEU
SEQRES 3 D 750 MET ALA THR SER GLY PHE SER LYS PRO LEU HIS TYR PRO
SEQRES 4 D 750 PRO VAL ARG ARG ASP GLU THR VAL VAL ASP ASP TYR PHE
SEQRES 5 D 750 GLY VAL LYS VAL ALA ASP PRO TYR ARG TRP LEU GLU ASP
SEQRES 6 D 750 PRO ASN SER GLU GLU THR LYS GLU PHE VAL ASP ASN GLN
SEQRES 7 D 750 GLU LYS LEU ALA ASN SER VAL LEU GLU GLU CYS GLU LEU
SEQRES 8 D 750 ILE ASP LYS PHE LYS GLN LYS ILE ILE ASP PHE VAL ASN
SEQRES 9 D 750 PHE PRO ARG CYS GLY VAL PRO PHE ARG ARG ALA ASN LYS
SEQRES 10 D 750 TYR PHE HIS PHE TYR ASN SER GLY LEU GLN ALA GLN ASN
SEQRES 11 D 750 VAL PHE GLN MET GLN ASP ASP LEU ASP GLY LYS PRO GLU
SEQRES 12 D 750 VAL LEU TYR ASP PRO ASN LEU ARG GLU GLY GLY ARG SER
SEQRES 13 D 750 GLY LEU SER LEU TYR SER VAL SER GLU ASP ALA LYS TYR
SEQRES 14 D 750 PHE ALA PHE GLY ILE HIS SER GLY LEU THR GLU TRP VAL
SEQRES 15 D 750 THR ILE LYS ILE LEU LYS THR GLU ASP ARG SER TYR LEU
SEQRES 16 D 750 PRO ASP THR LEU GLU TRP VAL LYS PHE SER PRO ALA ILE
SEQRES 17 D 750 TRP THR HIS ASP ASN LYS GLY PHE PHE TYR CYS PRO TYR
SEQRES 18 D 750 PRO PRO LEU LYS GLU GLY GLU ASP HIS MET THR ARG SER
SEQRES 19 D 750 ALA VAL ASN GLN GLU ALA ARG TYR HIS PHE LEU GLY THR
SEQRES 20 D 750 ASP GLN SER GLU ASP ILE LEU LEU TRP ARG ASP LEU GLU
SEQRES 21 D 750 ASN PRO ALA HIS HIS LEU LYS CYS GLN ILE THR ASP ASP
SEQRES 22 D 750 GLY LYS TYR PHE LEU LEU TYR ILE LEU ASP GLY CYS ASP
SEQRES 23 D 750 ASP ALA ASN LYS VAL TYR CYS LEU ASP LEU THR LYS LEU
SEQRES 24 D 750 PRO ASN GLY LEU GLU SER PHE ARG GLY ARG GLU ASP SER
SEQRES 25 D 750 ALA PRO PHE MET LYS LEU ILE ASP SER PHE ASP ALA SER
SEQRES 26 D 750 TYR THR ALA ILE ALA ASN ASP GLY SER VAL PHE THR PHE
SEQRES 27 D 750 GLN THR ASN LYS ASP ALA PRO ARG LYS LYS LEU VAL ARG
SEQRES 28 D 750 VAL ASP LEU ASN ASN PRO SER VAL TRP THR ASP LEU VAL
SEQRES 29 D 750 PRO GLU SER LYS LYS ASP LEU LEU GLU SER ALA HIS ALA
SEQRES 30 D 750 VAL ASN GLU ASN GLN LEU ILE LEU ARG TYR LEU SER ASP
SEQRES 31 D 750 VAL LYS HIS VAL LEU GLU ILE ARG ASP LEU GLU SER GLY
SEQRES 32 D 750 ALA LEU GLN HIS ARG LEU PRO ILE ASP ILE GLY SER VAL
SEQRES 33 D 750 ASP GLY ILE THR ALA ARG ARG ARG ASP SER VAL VAL PHE
SEQRES 34 D 750 PHE LYS PHE THR SER ILE LEU THR PRO GLY ILE VAL TYR
SEQRES 35 D 750 GLN CYS ASP LEU LYS ASN ASP PRO THR GLN LEU LYS ILE
SEQRES 36 D 750 PHE ARG GLU SER VAL VAL PRO ASP PHE ASP ARG SER GLU
SEQRES 37 D 750 PHE GLU VAL LYS GLN VAL PHE VAL PRO SER LYS ASP GLY
SEQRES 38 D 750 THR LYS ILE PRO ILE PHE ILE ALA ALA ARG LYS GLY ILE
SEQRES 39 D 750 SER LEU ASP GLY SER HIS PRO CYS GLU MET HIS GLY TYR
SEQRES 40 D 750 GLY GLY PHE GLY ILE ASN MET MET PRO THR PHE SER ALA
SEQRES 41 D 750 SER ARG ILE VAL PHE LEU LYS HIS LEU GLY GLY VAL PHE
SEQRES 42 D 750 CYS LEU ALA ASN ILE ARG GLY GLY GLY GLU TYR GLY GLU
SEQRES 43 D 750 GLU TRP HIS LYS ALA GLY PHE ARG ASP LYS LYS GLN ASN
SEQRES 44 D 750 VAL PHE ASP ASP PHE ILE SER ALA ALA GLU TYR LEU ILE
SEQRES 45 D 750 SER SER GLY TYR THR LYS ALA ARG ARG VAL ALA ILE GLU
SEQRES 46 D 750 GLY GLY SER ASN GLY GLY LEU LEU VAL ALA ALA CYS ILE
SEQRES 47 D 750 ASN GLN ARG PRO ASP LEU PHE GLY CYS ALA GLU ALA ASN
SEQRES 48 D 750 CYS GLY VAL MET ASP MET LEU ARG PHE HIS LYS PHE THR
SEQRES 49 D 750 LEU GLY TYR LEU TRP THR GLY ASP TYR GLY CYS SER ASP
SEQRES 50 D 750 LYS GLU GLU GLU PHE LYS TRP LEU ILE LYS TYR SER PRO
SEQRES 51 D 750 ILE HIS ASN VAL ARG ARG PRO TRP GLU GLN PRO GLY ASN
SEQRES 52 D 750 GLU GLU THR GLN TYR PRO ALA THR MET ILE LEU THR ALA
SEQRES 53 D 750 ASP HIS ASP ASP ARG VAL VAL PRO LEU HIS SER PHE LYS
SEQRES 54 D 750 LEU LEU ALA THR MET GLN HIS VAL LEU CYS THR SER LEU
SEQRES 55 D 750 GLU ASP SER PRO GLN LYS ASN PRO ILE ILE ALA ARG ILE
SEQRES 56 D 750 GLN ARG LYS ALA ALA HIS TYR GLY ARG ALA THR MET THR
SEQRES 57 D 750 GLN ILE ALA GLU VAL ALA ASP ARG TYR GLY PHE MET ALA
SEQRES 58 D 750 LYS ALA LEU GLU ALA PRO TRP ILE ASP
SEQRES 1 H 19 GLY VAL PRO VAL TRP ALA PHE GLN ALA LYS ASP VAL GLU
SEQRES 2 H 19 ASN ALA SER ALA PRO VAL
HET CAC A 801 5
HET CAC B 801 5
HET CAC C 801 5
HET CAC D 801 5
HETNAM CAC CACODYLATE ION
HETSYN CAC DIMETHYLARSINATE
FORMUL 9 CAC 4(C2 H6 AS O2 1-)
FORMUL 13 HOH *2061(H2 O)
HELIX 1 AA1 TYR A 34 ASP A 39 5 6
HELIX 2 AA2 SER A 42 GLU A 62 1 21
HELIX 3 AA3 LEU A 65 ASN A 78 1 14
HELIX 4 AA4 ASP A 121 ARG A 129 5 9
HELIX 5 AA5 ASP A 222 ASP A 226 5 5
HELIX 6 AA6 THR A 271 LEU A 273 5 3
HELIX 7 AA7 GLY A 276 PHE A 280 5 5
HELIX 8 AA8 ASP A 439 SER A 441 5 3
HELIX 9 AA9 SER A 493 LEU A 503 1 11
HELIX 10 AB1 GLY A 519 ALA A 525 1 7
HELIX 11 AB2 GLY A 526 ASP A 529 5 4
HELIX 12 AB3 LYS A 530 SER A 548 1 19
HELIX 13 AB4 SER A 562 ARG A 575 1 14
HELIX 14 AB5 PRO A 576 PHE A 579 5 4
HELIX 15 AB6 ARG A 593 PHE A 597 5 5
HELIX 16 AB7 LEU A 599 LEU A 602 5 4
HELIX 17 AB8 TRP A 603 GLY A 608 1 6
HELIX 18 AB9 LYS A 612 SER A 623 1 12
HELIX 19 AC1 PRO A 624 ASN A 627 5 4
HELIX 20 AC2 ARG A 630 GLN A 634 5 5
HELIX 21 AC3 PRO A 658 CYS A 673 1 16
HELIX 22 AC4 ALA A 699 LEU A 718 1 20
HELIX 23 AC5 TYR B 34 ASP B 39 5 6
HELIX 24 AC6 SER B 42 GLU B 62 1 21
HELIX 25 AC7 LEU B 65 ASN B 78 1 14
HELIX 26 AC8 ASP B 121 ARG B 129 5 9
HELIX 27 AC9 ASP B 222 ASP B 226 5 5
HELIX 28 AD1 THR B 271 LEU B 273 5 3
HELIX 29 AD2 ASP B 439 SER B 441 5 3
HELIX 30 AD3 SER B 493 LEU B 503 1 11
HELIX 31 AD4 GLY B 519 ALA B 525 1 7
HELIX 32 AD5 GLY B 526 LYS B 530 5 5
HELIX 33 AD6 LYS B 531 SER B 548 1 18
HELIX 34 AD7 LYS B 552 ARG B 554 5 3
HELIX 35 AD8 SER B 562 ARG B 575 1 14
HELIX 36 AD9 ARG B 593 PHE B 597 5 5
HELIX 37 AE1 LEU B 599 LEU B 602 5 4
HELIX 38 AE2 TRP B 603 GLY B 608 1 6
HELIX 39 AE3 LYS B 612 SER B 623 1 12
HELIX 40 AE4 PRO B 624 ASN B 627 5 4
HELIX 41 AE5 ARG B 630 GLN B 634 5 5
HELIX 42 AE6 PRO B 658 CYS B 673 1 16
HELIX 43 AE7 ALA B 699 LEU B 718 1 20
HELIX 44 AE8 TYR C 34 ASP C 39 5 6
HELIX 45 AE9 SER C 42 GLU C 62 1 21
HELIX 46 AF1 LEU C 65 ASN C 78 1 14
HELIX 47 AF2 ASP C 121 ARG C 129 5 9
HELIX 48 AF3 ASP C 222 ASP C 226 5 5
HELIX 49 AF4 THR C 271 LEU C 273 5 3
HELIX 50 AF5 GLY C 276 ARG C 281 5 6
HELIX 51 AF6 ASP C 439 SER C 441 5 3
HELIX 52 AF7 SER C 493 LEU C 503 1 11
HELIX 53 AF8 GLY C 519 ALA C 525 1 7
HELIX 54 AF9 GLY C 526 ASP C 529 5 4
HELIX 55 AG1 LYS C 530 SER C 548 1 19
HELIX 56 AG2 LYS C 552 ARG C 554 5 3
HELIX 57 AG3 SER C 562 ARG C 575 1 14
HELIX 58 AG4 PRO C 576 PHE C 579 5 4
HELIX 59 AG5 ARG C 593 PHE C 597 5 5
HELIX 60 AG6 LEU C 599 THR C 604 5 6
HELIX 61 AG7 LYS C 612 SER C 623 1 12
HELIX 62 AG8 PRO C 624 ASN C 627 5 4
HELIX 63 AG9 ARG C 630 GLN C 634 5 5
HELIX 64 AH1 PRO C 658 CYS C 673 1 16
HELIX 65 AH2 ALA C 699 LEU C 718 1 20
HELIX 66 AH3 TYR D 34 ASP D 39 5 6
HELIX 67 AH4 SER D 42 GLU D 62 1 21
HELIX 68 AH5 LEU D 65 ASN D 78 1 14
HELIX 69 AH6 ASP D 121 ARG D 129 5 9
HELIX 70 AH7 ASP D 222 ASP D 226 5 5
HELIX 71 AH8 THR D 271 LEU D 273 5 3
HELIX 72 AH9 ASP D 439 SER D 441 5 3
HELIX 73 AI1 SER D 493 LEU D 503 1 11
HELIX 74 AI2 GLY D 519 ALA D 525 1 7
HELIX 75 AI3 GLY D 526 ASP D 529 5 4
HELIX 76 AI4 LYS D 530 SER D 548 1 19
HELIX 77 AI5 LYS D 552 ARG D 554 5 3
HELIX 78 AI6 SER D 562 ARG D 575 1 14
HELIX 79 AI7 PRO D 576 PHE D 579 5 4
HELIX 80 AI8 ARG D 593 PHE D 597 5 5
HELIX 81 AI9 LEU D 599 THR D 604 5 6
HELIX 82 AJ1 LYS D 612 SER D 623 1 12
HELIX 83 AJ2 PRO D 624 ASN D 627 5 4
HELIX 84 AJ3 ARG D 630 GLN D 634 5 5
HELIX 85 AJ4 PRO D 658 CYS D 673 1 16
HELIX 86 AJ5 ALA D 699 LEU D 718 1 20
SHEET 1 AA1 2 VAL A 22 TYR A 25 0
SHEET 2 AA1 2 VAL A 28 ALA A 31 -1 O VAL A 28 N TYR A 25
SHEET 1 AA2 3 ARG A 81 CYS A 82 0
SHEET 2 AA2 3 LYS A 91 ASN A 97 -1 O ASN A 97 N ARG A 81
SHEET 3 AA2 3 PHE A 86 ARG A 88 -1 N PHE A 86 O PHE A 93
SHEET 1 AA3 4 ARG A 81 CYS A 82 0
SHEET 2 AA3 4 LYS A 91 ASN A 97 -1 O ASN A 97 N ARG A 81
SHEET 3 AA3 4 VAL A 105 GLN A 109 -1 O VAL A 105 N TYR A 96
SHEET 4 AA3 4 GLU A 117 TYR A 120 -1 O GLU A 117 N MET A 108
SHEET 1 AA4 4 TYR A 135 VAL A 137 0
SHEET 2 AA4 4 TYR A 143 HIS A 149 -1 O ALA A 145 N SER A 136
SHEET 3 AA4 4 VAL A 156 LYS A 162 -1 O LEU A 161 N PHE A 144
SHEET 4 AA4 4 LEU A 173 VAL A 176 -1 O VAL A 176 N VAL A 156
SHEET 1 AA5 4 ILE A 182 TRP A 183 0
SHEET 2 AA5 4 GLY A 189 TYR A 192 -1 O PHE A 191 N ILE A 182
SHEET 3 AA5 4 ALA A 214 PHE A 218 -1 O ARG A 215 N TYR A 192
SHEET 4 AA5 4 ILE A 227 TRP A 230 -1 O LEU A 229 N ALA A 214
SHEET 1 AA6 4 HIS A 239 ILE A 244 0
SHEET 2 AA6 4 TYR A 250 LEU A 256 -1 O LEU A 252 N GLN A 243
SHEET 3 AA6 4 LYS A 264 ASP A 269 -1 O LEU A 268 N PHE A 251
SHEET 4 AA6 4 MET A 290 ILE A 293 -1 O MET A 290 N CYS A 267
SHEET 1 AA7 4 TYR A 300 ASP A 306 0
SHEET 2 AA7 4 VAL A 309 THR A 314 -1 O THR A 311 N ILE A 303
SHEET 3 AA7 4 LYS A 322 ASP A 327 -1 O VAL A 326 N PHE A 310
SHEET 4 AA7 4 ASN A 330 VAL A 338 -1 O LEU A 337 N LEU A 323
SHEET 1 AA8 4 LEU A 345 VAL A 352 0
SHEET 2 AA8 4 GLN A 356 SER A 363 -1 O ARG A 360 N SER A 348
SHEET 3 AA8 4 LYS A 366 ASP A 373 -1 O VAL A 368 N TYR A 361
SHEET 4 AA8 4 LEU A 379 PRO A 384 -1 O LEU A 383 N LEU A 369
SHEET 1 AA9 4 SER A 389 ASP A 391 0
SHEET 2 AA9 4 VAL A 401 SER A 408 -1 O LYS A 405 N ASP A 391
SHEET 3 AA9 4 THR A 411 ASP A 419 -1 O ILE A 414 N PHE A 406
SHEET 4 AA9 4 LYS A 428 GLU A 432 -1 O LYS A 428 N GLN A 417
SHEET 1 AB1 8 PHE A 443 PRO A 451 0
SHEET 2 AB1 8 LYS A 457 ARG A 465 -1 O ILE A 458 N VAL A 450
SHEET 3 AB1 8 VAL A 506 ALA A 510 -1 O PHE A 507 N ALA A 463
SHEET 4 AB1 8 CYS A 476 HIS A 479 1 N HIS A 479 O CYS A 508
SHEET 5 AB1 8 VAL A 556 GLY A 561 1 O ALA A 557 N CYS A 476
SHEET 6 AB1 8 CYS A 581 ASN A 585 1 O ASN A 585 N GLY A 560
SHEET 7 AB1 8 ALA A 644 HIS A 652 1 O MET A 646 N ALA A 582
SHEET 8 AB1 8 ILE A 685 ALA A 694 1 O GLN A 690 N ASP A 651
SHEET 1 AB2 2 VAL B 22 TYR B 25 0
SHEET 2 AB2 2 VAL B 28 ALA B 31 -1 O VAL B 28 N TYR B 25
SHEET 1 AB3 3 ARG B 81 CYS B 82 0
SHEET 2 AB3 3 LYS B 91 ASN B 97 -1 O ASN B 97 N ARG B 81
SHEET 3 AB3 3 PHE B 86 ARG B 88 -1 N PHE B 86 O PHE B 93
SHEET 1 AB4 4 ARG B 81 CYS B 82 0
SHEET 2 AB4 4 LYS B 91 ASN B 97 -1 O ASN B 97 N ARG B 81
SHEET 3 AB4 4 VAL B 105 GLN B 109 -1 O VAL B 105 N TYR B 96
SHEET 4 AB4 4 GLU B 117 TYR B 120 -1 O LEU B 119 N PHE B 106
SHEET 1 AB5 4 TYR B 135 VAL B 137 0
SHEET 2 AB5 4 TYR B 143 HIS B 149 -1 O ALA B 145 N SER B 136
SHEET 3 AB5 4 VAL B 156 LYS B 162 -1 O LYS B 159 N PHE B 146
SHEET 4 AB5 4 LEU B 173 VAL B 176 -1 O VAL B 176 N VAL B 156
SHEET 1 AB6 4 ILE B 182 TRP B 183 0
SHEET 2 AB6 4 GLY B 189 TYR B 192 -1 O PHE B 191 N ILE B 182
SHEET 3 AB6 4 ALA B 214 PHE B 218 -1 O HIS B 217 N PHE B 190
SHEET 4 AB6 4 ILE B 227 TRP B 230 -1 O LEU B 229 N ALA B 214
SHEET 1 AB7 4 HIS B 239 ILE B 244 0
SHEET 2 AB7 4 TYR B 250 LEU B 256 -1 O LEU B 252 N GLN B 243
SHEET 3 AB7 4 LYS B 264 ASP B 269 -1 O LEU B 268 N PHE B 251
SHEET 4 AB7 4 MET B 290 ILE B 293 -1 O MET B 290 N CYS B 267
SHEET 1 AB8 4 TYR B 300 ASP B 306 0
SHEET 2 AB8 4 VAL B 309 THR B 314 -1 O THR B 311 N ILE B 303
SHEET 3 AB8 4 LYS B 322 ASP B 327 -1 O VAL B 326 N PHE B 310
SHEET 4 AB8 4 ASN B 330 VAL B 338 -1 O LEU B 337 N LEU B 323
SHEET 1 AB9 4 LEU B 345 VAL B 352 0
SHEET 2 AB9 4 GLN B 356 SER B 363 -1 O ARG B 360 N SER B 348
SHEET 3 AB9 4 LYS B 366 ASP B 373 -1 O LYS B 366 N SER B 363
SHEET 4 AB9 4 LEU B 379 PRO B 384 -1 O LEU B 383 N LEU B 369
SHEET 1 AC1 4 SER B 389 ASP B 391 0
SHEET 2 AC1 4 VAL B 401 SER B 408 -1 O LYS B 405 N ASP B 391
SHEET 3 AC1 4 THR B 411 ASP B 419 -1 O ILE B 414 N PHE B 406
SHEET 4 AC1 4 LYS B 428 GLU B 432 -1 O LYS B 428 N GLN B 417
SHEET 1 AC2 8 PHE B 443 PRO B 451 0
SHEET 2 AC2 8 LYS B 457 ARG B 465 -1 O ILE B 458 N VAL B 450
SHEET 3 AC2 8 VAL B 506 ALA B 510 -1 O PHE B 507 N ALA B 463
SHEET 4 AC2 8 CYS B 476 HIS B 479 1 N HIS B 479 O CYS B 508
SHEET 5 AC2 8 VAL B 556 GLY B 561 1 O ALA B 557 N CYS B 476
SHEET 6 AC2 8 PHE B 579 ASN B 585 1 O ASN B 585 N GLY B 560
SHEET 7 AC2 8 ALA B 644 ALA B 650 1 O MET B 646 N ALA B 582
SHEET 8 AC2 8 ILE B 685 GLN B 690 1 O GLN B 690 N THR B 649
SHEET 1 AC3 2 VAL C 22 TYR C 25 0
SHEET 2 AC3 2 VAL C 28 ALA C 31 -1 O VAL C 28 N TYR C 25
SHEET 1 AC4 3 ARG C 81 CYS C 82 0
SHEET 2 AC4 3 LYS C 91 ASN C 97 -1 O ASN C 97 N ARG C 81
SHEET 3 AC4 3 PHE C 86 ARG C 88 -1 N PHE C 86 O PHE C 93
SHEET 1 AC5 4 ARG C 81 CYS C 82 0
SHEET 2 AC5 4 LYS C 91 ASN C 97 -1 O ASN C 97 N ARG C 81
SHEET 3 AC5 4 VAL C 105 GLN C 109 -1 O VAL C 105 N TYR C 96
SHEET 4 AC5 4 GLU C 117 TYR C 120 -1 O LEU C 119 N PHE C 106
SHEET 1 AC6 4 TYR C 135 VAL C 137 0
SHEET 2 AC6 4 TYR C 143 HIS C 149 -1 O ALA C 145 N SER C 136
SHEET 3 AC6 4 VAL C 156 LYS C 162 -1 O THR C 157 N ILE C 148
SHEET 4 AC6 4 LEU C 173 VAL C 176 -1 O VAL C 176 N VAL C 156
SHEET 1 AC7 4 ILE C 182 TRP C 183 0
SHEET 2 AC7 4 GLY C 189 TYR C 192 -1 O PHE C 191 N ILE C 182
SHEET 3 AC7 4 ALA C 214 PHE C 218 -1 O ARG C 215 N TYR C 192
SHEET 4 AC7 4 ILE C 227 TRP C 230 -1 O LEU C 229 N ALA C 214
SHEET 1 AC8 4 HIS C 239 ILE C 244 0
SHEET 2 AC8 4 TYR C 250 LEU C 256 -1 O LEU C 252 N GLN C 243
SHEET 3 AC8 4 LYS C 264 ASP C 269 -1 O TYR C 266 N LEU C 253
SHEET 4 AC8 4 MET C 290 ILE C 293 -1 O MET C 290 N CYS C 267
SHEET 1 AC9 4 TYR C 300 ASP C 306 0
SHEET 2 AC9 4 VAL C 309 THR C 314 -1 O THR C 311 N ILE C 303
SHEET 3 AC9 4 LYS C 322 ASP C 327 -1 O VAL C 326 N PHE C 310
SHEET 4 AC9 4 ASN C 330 VAL C 338 -1 O LEU C 337 N LEU C 323
SHEET 1 AD1 4 LEU C 345 VAL C 352 0
SHEET 2 AD1 4 GLN C 356 SER C 363 -1 O ARG C 360 N SER C 348
SHEET 3 AD1 4 LYS C 366 ASP C 373 -1 O VAL C 368 N TYR C 361
SHEET 4 AD1 4 LEU C 379 PRO C 384 -1 O LEU C 383 N LEU C 369
SHEET 1 AD2 4 SER C 389 ASP C 391 0
SHEET 2 AD2 4 VAL C 401 SER C 408 -1 O LYS C 405 N ASP C 391
SHEET 3 AD2 4 THR C 411 ASP C 419 -1 O TYR C 416 N PHE C 404
SHEET 4 AD2 4 LYS C 428 GLU C 432 -1 O LYS C 428 N GLN C 417
SHEET 1 AD3 8 PHE C 443 PRO C 451 0
SHEET 2 AD3 8 LYS C 457 ARG C 465 -1 O ILE C 458 N VAL C 450
SHEET 3 AD3 8 VAL C 506 ALA C 510 -1 O PHE C 507 N ALA C 463
SHEET 4 AD3 8 CYS C 476 HIS C 479 1 N HIS C 479 O CYS C 508
SHEET 5 AD3 8 VAL C 556 GLY C 561 1 O ALA C 557 N CYS C 476
SHEET 6 AD3 8 CYS C 581 ASN C 585 1 O ASN C 585 N GLY C 560
SHEET 7 AD3 8 ALA C 644 HIS C 652 1 O LEU C 648 N ALA C 584
SHEET 8 AD3 8 ILE C 685 ALA C 694 1 O GLN C 690 N ASP C 651
SHEET 1 AD4 2 VAL D 22 TYR D 25 0
SHEET 2 AD4 2 VAL D 28 ALA D 31 -1 O VAL D 28 N TYR D 25
SHEET 1 AD5 3 ARG D 81 CYS D 82 0
SHEET 2 AD5 3 LYS D 91 ASN D 97 -1 O ASN D 97 N ARG D 81
SHEET 3 AD5 3 PHE D 86 ARG D 88 -1 N PHE D 86 O PHE D 93
SHEET 1 AD6 4 ARG D 81 CYS D 82 0
SHEET 2 AD6 4 LYS D 91 ASN D 97 -1 O ASN D 97 N ARG D 81
SHEET 3 AD6 4 VAL D 105 GLN D 109 -1 O VAL D 105 N TYR D 96
SHEET 4 AD6 4 GLU D 117 TYR D 120 -1 O LEU D 119 N PHE D 106
SHEET 1 AD7 4 TYR D 135 VAL D 137 0
SHEET 2 AD7 4 TYR D 143 HIS D 149 -1 O ALA D 145 N SER D 136
SHEET 3 AD7 4 VAL D 156 LYS D 162 -1 O THR D 157 N ILE D 148
SHEET 4 AD7 4 LEU D 173 VAL D 176 -1 O VAL D 176 N VAL D 156
SHEET 1 AD8 4 ILE D 182 TRP D 183 0
SHEET 2 AD8 4 GLY D 189 TYR D 192 -1 O PHE D 191 N ILE D 182
SHEET 3 AD8 4 ALA D 214 PHE D 218 -1 O HIS D 217 N PHE D 190
SHEET 4 AD8 4 ILE D 227 TRP D 230 -1 O LEU D 229 N ALA D 214
SHEET 1 AD9 4 HIS D 239 ILE D 244 0
SHEET 2 AD9 4 TYR D 250 LEU D 256 -1 O LEU D 252 N GLN D 243
SHEET 3 AD9 4 LYS D 264 ASP D 269 -1 O LEU D 268 N PHE D 251
SHEET 4 AD9 4 MET D 290 ILE D 293 -1 O MET D 290 N CYS D 267
SHEET 1 AE1 4 TYR D 300 ASP D 306 0
SHEET 2 AE1 4 VAL D 309 THR D 314 -1 O THR D 311 N ILE D 303
SHEET 3 AE1 4 LYS D 322 ASP D 327 -1 O VAL D 326 N PHE D 310
SHEET 4 AE1 4 ASN D 330 VAL D 338 -1 O LEU D 337 N LEU D 323
SHEET 1 AE2 4 LEU D 345 VAL D 352 0
SHEET 2 AE2 4 GLN D 356 SER D 363 -1 O ARG D 360 N SER D 348
SHEET 3 AE2 4 LYS D 366 ASP D 373 -1 O LYS D 366 N SER D 363
SHEET 4 AE2 4 LEU D 379 PRO D 384 -1 O LEU D 383 N LEU D 369
SHEET 1 AE3 4 SER D 389 ASP D 391 0
SHEET 2 AE3 4 VAL D 401 SER D 408 -1 O LYS D 405 N ASP D 391
SHEET 3 AE3 4 THR D 411 ASP D 419 -1 O ILE D 414 N PHE D 406
SHEET 4 AE3 4 LYS D 428 GLU D 432 -1 O PHE D 430 N VAL D 415
SHEET 1 AE4 8 PHE D 443 PRO D 451 0
SHEET 2 AE4 8 LYS D 457 ARG D 465 -1 O ILE D 458 N VAL D 450
SHEET 3 AE4 8 VAL D 506 ALA D 510 -1 O PHE D 507 N ALA D 463
SHEET 4 AE4 8 CYS D 476 HIS D 479 1 N HIS D 479 O CYS D 508
SHEET 5 AE4 8 VAL D 556 GLY D 561 1 O ALA D 557 N CYS D 476
SHEET 6 AE4 8 CYS D 581 ASN D 585 1 O ASN D 585 N GLY D 560
SHEET 7 AE4 8 ALA D 644 HIS D 652 1 O MET D 646 N ALA D 582
SHEET 8 AE4 8 ILE D 685 ALA D 694 1 O GLN D 690 N ASP D 651
SITE 1 AC1 5 TYR A 481 PHE A 484 SER A 562 ASN A 563
SITE 2 AC1 5 TRP A 603
SITE 1 AC2 5 TYR B 481 PHE B 484 SER B 562 ASN B 563
SITE 2 AC2 5 TRP B 603
SITE 1 AC3 4 TYR C 481 SER C 562 ASN C 563 TRP C 603
SITE 1 AC4 5 TYR D 481 SER D 562 ASN D 563 TRP D 603
SITE 2 AC4 5 HOH D 901
CRYST1 65.495 85.591 137.720 87.41 78.28 89.33 P 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.015268 -0.000178 -0.003164 0.00000
SCALE2 0.000000 0.011684 -0.000512 0.00000
SCALE3 0.000000 0.000000 0.007423 0.00000
TER 5574 ILE A 723
TER 5613 VAL E1032
TER 11283 ASP B 724
TER 11323 VAL F1032
TER 16970 ILE C 723
TER 17009 VAL G1032
TER 22618 ILE D 723
TER 22658 VAL H1032
MASTER 784 0 4 86 164 0 7 624731 8 20 240
END |