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HEADER LYASE 20-FEB-17 5UW5
TITLE PCY1 H695A VARIANT 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 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 5UW5 1 JRNL
REVDAT 2 21-JUN-17 5UW5 1 JRNL
REVDAT 1 31-MAY-17 5UW5 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. 2.94 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) : 2.94
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 58051
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3094
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.94
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.02
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4238
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.49
REMARK 3 BIN R VALUE (WORKING SET) : 0.2750
REMARK 3 BIN FREE R VALUE SET COUNT : 205
REMARK 3 BIN FREE R VALUE : 0.2990
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 22634
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 26
REMARK 3 SOLVENT ATOMS : 64
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.91
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.33000
REMARK 3 B22 (A**2) : 0.09000
REMARK 3 B33 (A**2) : -0.91000
REMARK 3 B12 (A**2) : 0.66000
REMARK 3 B13 (A**2) : 1.00000
REMARK 3 B23 (A**2) : 0.13000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.428
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.328
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.074
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.923
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.883
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 23313 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 21763 ; 0.005 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 31592 ; 1.407 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): 50155 ; 1.132 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2826 ; 6.237 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1154 ;34.004 ;23.995
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3897 ;15.904 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 146 ;16.734 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3350 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 26499 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 5547 ; 0.004 ; 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): 11325 ; 2.079 ; 3.175
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 11324 ; 2.079 ; 3.175
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14144 ; 3.519 ; 4.759
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 14145 ; 3.519 ; 4.759
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 11988 ; 2.095 ; 3.407
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 11989 ; 2.095 ; 3.407
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 17449 ; 3.617 ; 5.023
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 25149 ; 5.712 ;24.944
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 25150 ; 5.712 ;24.944
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 9 1031 B 9 1031 42760 0.08 0.05
REMARK 3 2 A 9 1031 C 9 1031 42356 0.10 0.05
REMARK 3 3 A 9 1031 D 9 1031 42372 0.09 0.05
REMARK 3 4 B 5 1032 C 5 1032 42787 0.09 0.05
REMARK 3 5 B 4 1032 D 4 1032 42939 0.08 0.05
REMARK 3 6 C 5 1032 D 5 1032 42845 0.09 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 5UW5 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_1000226249.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-FEB-14
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-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97857
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 : 61150
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.940
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 (%) : 98.8
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.12700
REMARK 200 FOR THE DATA SET : 11.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.94
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.50600
REMARK 200 FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
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 (%): 42.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16 % PEG 8,000, 50 MM CALCIUM ACETATE,
REMARK 280 0.1 M SODIUM CACODYLATE, 8 MG/ML PROTEIN, PROTEIN WAS
REMARK 280 PREINCUBATED WITH 1 MM PRESEGETALIN A1 [14-32], PH 6.5, 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: 1270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27950 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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: 1500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 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: 1180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28550 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: 1180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28300 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 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 14
REMARK 465 VAL E 15
REMARK 465 PRO E 16
REMARK 465 VAL E 17
REMARK 465 TRP E 18
REMARK 465 ALA E 19
REMARK 465 PHE E 20
REMARK 465 GLN E 21
REMARK 465 ALA E 22
REMARK 465 LYS E 23
REMARK 465 ASP E 24
REMARK 465 VAL E 25
REMARK 465 GLU E 26
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 MET B 1
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 SER B 286
REMARK 465 GLY F 14
REMARK 465 VAL F 15
REMARK 465 PRO F 16
REMARK 465 VAL F 17
REMARK 465 TRP F 18
REMARK 465 ALA F 19
REMARK 465 PHE F 20
REMARK 465 GLN F 21
REMARK 465 ALA F 22
REMARK 465 LYS F 23
REMARK 465 ASP F 24
REMARK 465 VAL F 25
REMARK 465 GLU F 26
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 14
REMARK 465 VAL G 15
REMARK 465 PRO G 16
REMARK 465 VAL G 17
REMARK 465 TRP G 18
REMARK 465 ALA G 19
REMARK 465 PHE G 20
REMARK 465 GLN G 21
REMARK 465 ALA G 22
REMARK 465 LYS G 23
REMARK 465 ASP G 24
REMARK 465 VAL G 25
REMARK 465 GLU G 26
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 THR D 3
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 14
REMARK 465 VAL H 15
REMARK 465 PRO H 16
REMARK 465 VAL H 17
REMARK 465 TRP H 18
REMARK 465 ALA H 19
REMARK 465 PHE H 20
REMARK 465 GLN H 21
REMARK 465 ALA H 22
REMARK 465 LYS H 23
REMARK 465 ASP H 24
REMARK 465 VAL H 25
REMARK 465 GLU H 26
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 GLU A 639 O HOH A 901 1.79
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 CA CA A 802 CA CA C 802 1545 1.68
REMARK 500 NZ LYS C 188 OD1 ASP D 111 1465 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 161 CB - CG - CD1 ANGL. DEV. = -10.9 DEGREES
REMARK 500 LEU A 602 CA - CB - CG ANGL. DEV. = 15.1 DEGREES
REMARK 500 CYS A 609 CA - CB - SG ANGL. DEV. = 9.9 DEGREES
REMARK 500 THR B 598 CB - CA - C ANGL. DEV. = -17.6 DEGREES
REMARK 500 LEU B 599 CA - CB - CG ANGL. DEV. = 14.7 DEGREES
REMARK 500 ILE B 704 CA - CB - CG1 ANGL. DEV. = 11.8 DEGREES
REMARK 500 LEU C 134 CA - CB - CG ANGL. DEV. = 22.2 DEGREES
REMARK 500 ARG C 554 CA - CB - CG ANGL. DEV. = 14.5 DEGREES
REMARK 500 LEU C 599 CA - CB - CG ANGL. DEV. = 16.4 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 -121.17 53.40
REMARK 500 ALA A 89 -122.17 53.40
REMARK 500 LYS A 177 -78.89 -119.57
REMARK 500 ALA A 318 79.01 -161.65
REMARK 500 LYS A 321 163.77 69.59
REMARK 500 GLU A 354 -49.51 63.40
REMARK 500 ASP A 423 62.49 -151.77
REMARK 500 TYR A 481 -75.22 -138.43
REMARK 500 ARG A 528 -112.07 50.97
REMARK 500 ARG A 554 -9.32 81.29
REMARK 500 SER A 562 -118.66 60.61
REMARK 500 ARG A 575 58.67 -141.12
REMARK 500 CYS A 586 56.68 27.06
REMARK 500 THR A 598 -108.69 32.15
REMARK 500 SER A 623 108.96 -48.24
REMARK 500 ASN A 627 31.44 -140.89
REMARK 500 ARG A 655 -72.66 -86.87
REMARK 500 CYS A 673 -64.64 -130.65
REMARK 500 GLN A 681 98.20 -65.65
REMARK 500 ARG A 698 78.79 37.86
REMARK 500 THR A 700 158.51 -45.18
REMARK 500 MET A 701 -60.11 81.15
REMARK 500 SER B 7 -62.33 -124.94
REMARK 500 ALA B 89 -121.20 54.18
REMARK 500 LYS B 177 -80.05 -120.39
REMARK 500 ARG B 231 -45.61 -138.66
REMARK 500 ASP B 232 77.65 55.16
REMARK 500 ALA B 318 79.03 -161.00
REMARK 500 LYS B 321 163.57 69.28
REMARK 500 GLU B 354 -50.38 64.03
REMARK 500 ASP B 423 62.21 -151.81
REMARK 500 TYR B 481 -76.04 -138.66
REMARK 500 ARG B 528 -112.84 51.44
REMARK 500 SER B 562 -118.04 59.89
REMARK 500 ARG B 575 58.24 -141.20
REMARK 500 CYS B 586 56.40 26.08
REMARK 500 ASP B 590 68.72 73.78
REMARK 500 THR B 598 84.12 6.24
REMARK 500 LEU B 599 -1.53 73.31
REMARK 500 SER B 623 109.35 -47.04
REMARK 500 ARG B 655 -73.16 -86.08
REMARK 500 CYS B 673 -64.30 -130.96
REMARK 500 GLN B 681 97.98 -66.01
REMARK 500 THR B 700 -52.97 -28.54
REMARK 500 SER C 7 -64.68 -120.97
REMARK 500 ALA C 89 -120.95 54.32
REMARK 500 LYS C 177 -80.03 -120.54
REMARK 500 ARG C 231 -44.29 -140.61
REMARK 500 ASP C 232 77.53 53.99
REMARK 500 PHE C 280 18.21 83.47
REMARK 500
REMARK 500 THIS ENTRY HAS 84 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PRO A 9 LEU A 10 -146.79
REMARK 500 GLY A 697 ARG A 698 146.26
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 802 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 64 OE2
REMARK 620 2 GLU C 61 O 52.6
REMARK 620 3 GLU C 64 OE2 54.8 2.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 803 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 717 O
REMARK 620 2 GLU A 719 OE2 68.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 803 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 639 O
REMARK 620 2 GLU C 639 OE1 94.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 802 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA B 717 O
REMARK 620 2 GLU B 719 OE1 71.7
REMARK 620 3 GLU B 719 OE2 75.6 46.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 802 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 64 OE2
REMARK 620 2 GLU A 64 OE2 61.6
REMARK 620 N 1
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 CA A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CAC B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CAC C 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
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: 5UW3 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 5UW5 A 1 724 UNP R4P353 R4P353_9CARY 1 724
DBREF 5UW5 E 14 32 UNP F6LNL5 F6LNL5_9CARY 14 32
DBREF 5UW5 B 1 724 UNP R4P353 R4P353_9CARY 1 724
DBREF 5UW5 F 14 32 UNP F6LNL5 F6LNL5_9CARY 14 32
DBREF 5UW5 C 1 724 UNP R4P353 R4P353_9CARY 1 724
DBREF 5UW5 G 14 32 UNP F6LNL5 F6LNL5_9CARY 14 32
DBREF 5UW5 D 1 724 UNP R4P353 R4P353_9CARY 1 724
DBREF 5UW5 H 14 32 UNP F6LNL5 F6LNL5_9CARY 14 32
SEQADV 5UW5 MET A -25 UNP R4P353 INITIATING METHIONINE
SEQADV 5UW5 SER A -24 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 TYR A -23 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 TYR A -22 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 HIS A -21 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 HIS A -20 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 HIS A -19 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 HIS A -18 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 HIS A -17 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 HIS A -16 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 LEU A -15 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 GLU A -14 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 SER A -13 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 THR A -12 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 SER A -11 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 LEU A -10 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 TYR A -9 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 LYS A -8 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 LYS A -7 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 ALA A -6 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 GLY A -5 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 SER A -4 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 GLU A -3 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 PHE A -2 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 ALA A -1 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 LEU A 0 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 ALA A 695 UNP R4P353 HIS 695 CONFLICT
SEQADV 5UW5 MET B -25 UNP R4P353 INITIATING METHIONINE
SEQADV 5UW5 SER B -24 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 TYR B -23 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 TYR B -22 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 HIS B -21 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 HIS B -20 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 HIS B -19 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 HIS B -18 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 HIS B -17 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 HIS B -16 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 LEU B -15 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 GLU B -14 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 SER B -13 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 THR B -12 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 SER B -11 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 LEU B -10 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 TYR B -9 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 LYS B -8 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 LYS B -7 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 ALA B -6 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 GLY B -5 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 SER B -4 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 GLU B -3 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 PHE B -2 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 ALA B -1 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 LEU B 0 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 ALA B 695 UNP R4P353 HIS 695 CONFLICT
SEQADV 5UW5 MET C -25 UNP R4P353 INITIATING METHIONINE
SEQADV 5UW5 SER C -24 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 TYR C -23 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 TYR C -22 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 HIS C -21 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 HIS C -20 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 HIS C -19 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 HIS C -18 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 HIS C -17 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 HIS C -16 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 LEU C -15 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 GLU C -14 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 SER C -13 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 THR C -12 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 SER C -11 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 LEU C -10 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 TYR C -9 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 LYS C -8 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 LYS C -7 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 ALA C -6 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 GLY C -5 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 SER C -4 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 GLU C -3 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 PHE C -2 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 ALA C -1 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 LEU C 0 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 ALA C 695 UNP R4P353 HIS 695 CONFLICT
SEQADV 5UW5 MET D -25 UNP R4P353 INITIATING METHIONINE
SEQADV 5UW5 SER D -24 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 TYR D -23 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 TYR D -22 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 HIS D -21 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 HIS D -20 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 HIS D -19 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 HIS D -18 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 HIS D -17 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 HIS D -16 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 LEU D -15 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 GLU D -14 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 SER D -13 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 THR D -12 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 SER D -11 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 LEU D -10 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 TYR D -9 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 LYS D -8 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 LYS D -7 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 ALA D -6 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 GLY D -5 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 SER D -4 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 GLU D -3 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 PHE D -2 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 ALA D -1 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 LEU D 0 UNP R4P353 EXPRESSION TAG
SEQADV 5UW5 ALA D 695 UNP R4P353 HIS 695 CONFLICT
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 ALA 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 ALA 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 ALA 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 ALA 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 CA A 802 1
HET CA A 803 1
HET CAC B 801 5
HET CA B 802 1
HET CA B 803 1
HET CAC C 801 5
HET CA C 802 1
HET CA C 803 1
HET CAC D 801 5
HETNAM CAC CACODYLATE ION
HETNAM CA CALCIUM ION
HETSYN CAC DIMETHYLARSINATE
FORMUL 9 CAC 4(C2 H6 AS O2 1-)
FORMUL 10 CA 6(CA 2+)
FORMUL 19 HOH *64(H2 O)
HELIX 1 AA1 TYR A 34 ASP A 39 5 6
HELIX 2 AA2 SER A 42 CYS A 63 1 22
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 ASN A 275 SER A 279 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 MET A 701 LEU A 718 1 18
HELIX 23 AC5 TYR B 34 ASP B 39 5 6
HELIX 24 AC6 SER B 42 CYS B 63 1 22
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 ASN B 275 SER B 279 5 5
HELIX 30 AD3 ASP B 439 SER B 441 5 3
HELIX 31 AD4 SER B 493 LEU B 503 1 11
HELIX 32 AD5 GLY B 519 ALA B 525 1 7
HELIX 33 AD6 GLY B 526 ASP B 529 5 4
HELIX 34 AD7 LYS B 530 SER B 548 1 19
HELIX 35 AD8 LYS B 552 ARG B 554 5 3
HELIX 36 AD9 SER B 562 ARG B 575 1 14
HELIX 37 AE1 PRO B 576 PHE B 579 5 4
HELIX 38 AE2 ARG B 593 PHE B 597 5 5
HELIX 39 AE3 LEU B 599 LEU B 602 5 4
HELIX 40 AE4 TRP B 603 GLY B 608 1 6
HELIX 41 AE5 LYS B 612 SER B 623 1 12
HELIX 42 AE6 PRO B 624 ASN B 627 5 4
HELIX 43 AE7 ARG B 630 GLN B 634 5 5
HELIX 44 AE8 PRO B 658 CYS B 673 1 16
HELIX 45 AE9 ALA B 699 LEU B 718 1 20
HELIX 46 AF1 TYR C 34 ASP C 39 5 6
HELIX 47 AF2 SER C 42 GLU C 62 1 21
HELIX 48 AF3 LEU C 65 ASN C 78 1 14
HELIX 49 AF4 ASP C 121 ARG C 129 5 9
HELIX 50 AF5 ASP C 222 ASP C 226 5 5
HELIX 51 AF6 THR C 271 LEU C 273 5 3
HELIX 52 AF7 ASN C 275 SER C 279 5 5
HELIX 53 AF8 ASP C 439 SER C 441 5 3
HELIX 54 AF9 SER C 493 LEU C 503 1 11
HELIX 55 AG1 GLY C 519 ALA C 525 1 7
HELIX 56 AG2 GLY C 526 ASP C 529 5 4
HELIX 57 AG3 LYS C 530 SER C 548 1 19
HELIX 58 AG4 LYS C 552 ARG C 554 5 3
HELIX 59 AG5 SER C 562 ARG C 575 1 14
HELIX 60 AG6 PRO C 576 PHE C 579 5 4
HELIX 61 AG7 ARG C 593 PHE C 597 5 5
HELIX 62 AG8 LEU C 599 THR C 604 5 6
HELIX 63 AG9 LYS C 612 SER C 623 1 12
HELIX 64 AH1 PRO C 624 ASN C 627 5 4
HELIX 65 AH2 ARG C 630 GLN C 634 5 5
HELIX 66 AH3 PRO C 658 CYS C 673 1 16
HELIX 67 AH4 ALA C 699 LEU C 718 1 20
HELIX 68 AH5 TYR D 34 ASP D 39 5 6
HELIX 69 AH6 SER D 42 CYS D 63 1 22
HELIX 70 AH7 LEU D 65 ASN D 78 1 14
HELIX 71 AH8 ASP D 121 ARG D 129 5 9
HELIX 72 AH9 ASP D 222 ASP D 226 5 5
HELIX 73 AI1 THR D 271 LEU D 273 5 3
HELIX 74 AI2 ASP D 439 SER D 441 5 3
HELIX 75 AI3 SER D 493 LEU D 503 1 11
HELIX 76 AI4 GLY D 519 ALA D 525 1 7
HELIX 77 AI5 GLY D 526 ASP D 529 5 4
HELIX 78 AI6 LYS D 530 SER D 548 1 19
HELIX 79 AI7 LYS D 552 ARG D 554 5 3
HELIX 80 AI8 SER D 562 ARG D 575 1 14
HELIX 81 AI9 PRO D 576 PHE D 579 5 4
HELIX 82 AJ1 ARG D 593 PHE D 597 5 5
HELIX 83 AJ2 LEU D 599 THR D 604 5 6
HELIX 84 AJ3 LYS D 612 SER D 623 1 12
HELIX 85 AJ4 PRO D 624 ASN D 627 5 4
HELIX 86 AJ5 ARG D 630 GLN D 634 5 5
HELIX 87 AJ6 PRO D 658 CYS D 673 1 16
HELIX 88 AJ7 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 30 N ASP A 23
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 LEU A 119 N PHE A 106
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 ASN A 263 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 324 N PHE A 312
SHEET 4 AA7 4 TRP A 334 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 LEU A 362 -1 O LEU A 362 N LEU A 345
SHEET 3 AA8 4 HIS A 367 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 THR A 407 -1 O LYS A 405 N ASP A 391
SHEET 3 AA9 4 ILE A 414 ASP A 419 -1 O CYS A 418 N VAL A 402
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 460 N VAL A 448
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 GLU A 477 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 ALA A 650 1 O LEU A 648 N ALA A 584
SHEET 8 AB1 8 ILE A 685 GLN A 690 1 O ILE A 686 N THR A 645
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 30 N ASP B 23
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 LEU B 161 N PHE B 144
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 ASN B 263 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 324 N PHE B 312
SHEET 4 AB8 4 TRP B 334 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 LEU B 362 -1 O LEU B 362 N LEU B 345
SHEET 3 AB9 4 HIS B 367 ASP B 373 -1 O VAL B 368 N TYR B 361
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 THR B 407 -1 O LYS B 405 N ASP B 391
SHEET 3 AC1 4 ILE B 414 ASP B 419 -1 O CYS B 418 N VAL B 402
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 460 N VAL B 448
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 GLU B 477 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 CYS B 581 ASN B 585 1 O ASN B 585 N GLY B 560
SHEET 7 AC2 8 ALA B 644 ALA B 650 1 O LEU B 648 N ALA B 584
SHEET 8 AC2 8 ILE B 685 GLN B 690 1 O ILE B 686 N THR B 645
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 30 N ASP C 23
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 LEU C 161 N PHE C 144
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 ASN C 263 ASP C 269 -1 O LEU C 268 N PHE C 251
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 324 N PHE C 312
SHEET 4 AC9 4 TRP C 334 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 LEU C 362 -1 O LEU C 362 N LEU C 345
SHEET 3 AD1 4 HIS C 367 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 THR C 407 -1 O LYS C 405 N ASP C 391
SHEET 3 AD2 4 ILE C 414 ASP C 419 -1 O CYS C 418 N VAL C 402
SHEET 4 AD2 4 LYS C 428 GLU C 432 -1 O PHE C 430 N VAL C 415
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 462 N LYS C 446
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 GLU C 477 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 ALA C 650 1 O LEU C 648 N ALA C 584
SHEET 8 AD3 8 ILE C 685 GLN C 690 1 O ILE C 686 N THR C 645
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 30 N ASP D 23
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 GLU D 117 N MET D 108
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 ARG D 215 N TYR D 192
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 ASN D 263 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 324 N PHE D 312
SHEET 4 AE1 4 TRP D 334 VAL D 338 -1 O THR D 335 N ARG D 325
SHEET 1 AE2 4 LEU D 345 VAL D 352 0
SHEET 2 AE2 4 GLN D 356 LEU D 362 -1 O LEU D 362 N LEU D 345
SHEET 3 AE2 4 HIS D 367 ASP D 373 -1 O VAL D 368 N TYR D 361
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 THR D 407 -1 O LYS D 405 N ASP D 391
SHEET 3 AE3 4 ILE D 414 ASP D 419 -1 O CYS D 418 N VAL D 402
SHEET 4 AE3 4 LYS D 428 GLU D 432 -1 O LYS D 428 N GLN D 417
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 462 N LYS D 446
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 GLU D 477 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 ALA D 650 1 O LEU D 648 N ALA D 584
SHEET 8 AE4 8 ILE D 685 GLN D 690 1 O ILE D 686 N THR D 645
LINK OE2 GLU A 64 CA CA A 802 1555 1555 2.97
LINK O ALA A 717 CA CA A 803 1555 1555 2.79
LINK OE2 GLU A 719 CA CA A 803 1555 1555 2.69
LINK O GLU B 639 CA CA B 803 1555 1555 2.11
LINK O ALA B 717 CA CA B 802 1555 1555 2.56
LINK OE1 GLU B 719 CA CA B 802 1555 1555 2.86
LINK OE2 GLU B 719 CA CA B 802 1555 1555 2.53
LINK OE2 GLU C 64 CA CA C 802 1555 1555 3.17
LINK OE2 GLU A 64 CA CA C 802 1555 1545 2.80
LINK O GLU B 639 CA CA C 803 1555 1554 2.68
LINK O GLU C 61 CA CA A 802 1555 1565 3.03
LINK OE2 GLU C 64 CA CA A 802 1555 1565 2.41
LINK OE1 GLU C 639 CA CA B 803 1555 1556 2.98
SITE 1 AC1 6 TYR A 481 PHE A 484 SER A 562 ASN A 563
SITE 2 AC1 6 VAL A 588 TRP A 603
SITE 1 AC2 5 GLU A 61 GLU A 64 GLU C 61 GLU C 64
SITE 2 AC2 5 CA C 802
SITE 1 AC3 2 ALA A 717 GLU A 719
SITE 1 AC4 7 TYR B 481 PHE B 484 SER B 562 ASN B 563
SITE 2 AC4 7 VAL B 588 TRP B 603 ARG B 655
SITE 1 AC5 2 ALA B 717 GLU B 719
SITE 1 AC6 3 GLU B 639 GLU C 639 CA C 803
SITE 1 AC7 5 TYR C 481 PHE C 484 SER C 562 ASN C 563
SITE 2 AC7 5 VAL C 588
SITE 1 AC8 4 GLU A 64 CA A 802 GLU C 61 GLU C 64
SITE 1 AC9 3 GLU B 639 CA B 803 GLU C 639
SITE 1 AD1 4 TYR D 481 SER D 562 ASN D 563 TRP D 603
CRYST1 65.020 85.614 137.870 87.49 78.51 89.44 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 0.015380 -0.000151 -0.003123 0.00000
SCALE2 0.000000 0.011681 -0.000500 0.00000
SCALE3 0.000000 0.000000 0.007408 0.00000
TER 5640 ILE A 723
TER 5679 VAL E 32
TER 11339 ASP B 724
TER 11379 VAL F 32
TER 17040 ILE C 723
TER 17079 VAL G 32
TER 22676 ILE D 723
TER 22716 VAL H 32
MASTER 758 0 10 88 164 0 14 622724 8 33 240
END |