HEADER HYDROLASE 10-NOV-02 1N6E
TITLE TRICORN PROTEASE IN COMPLEX WITH A TRIDECAPEPTIDE CHLOROMETHYL KETONE
TITLE 2 DERIVATIVE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRICORN PROTEASE;
COMPND 3 CHAIN: A, C, E, G, I, K;
COMPND 4 EC: 3.4.21.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: DQTQKAAAELTFF;
COMPND 8 CHAIN: B, D, F, H, J, L;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOPLASMA ACIDOPHILUM;
SOURCE 3 ORGANISM_TAXID: 2303;
SOURCE 4 GENE: TRI, TA1490;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PRSET6C;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 13 ORGANISM_TAXID: 32630;
SOURCE 14 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN THERMOPLASMA
SOURCE 15 ACIDOPHILUM
KEYWDS TRICORN PROTEASE, HYDROLASE, PROPELLER
EXPDTA X-RAY DIFFRACTION
AUTHOR J.-S.KIM,M.GROLL,R.HUBER,H.BRANDSTETTER
REVDAT 4 31-JAN-24 1N6E 1 COMPND SOURCE REMARK DBREF
REVDAT 4 2 1 SEQRES HET HETNAM HETSYN
REVDAT 4 3 1 FORMUL LINK ATOM
REVDAT 3 25-OCT-23 1N6E 1 REMARK LINK
REVDAT 2 24-FEB-09 1N6E 1 VERSN
REVDAT 1 30-DEC-02 1N6E 0
JRNL AUTH J.-S.KIM,M.GROLL,H.-J.MUSIOL,R.BEHRENDT,M.KAISER,L.MORODER,
JRNL AUTH 2 R.HUBER,H.BRANDSTETTER
JRNL TITL NAVIGATION INSIDE A PROTEASE: SUBSTRATE SELECTION AND
JRNL TITL 2 PRODUCT EXIT IN THE TRICORN PROTEASE FROM THERMOPLASMA
JRNL TITL 3 ACIDOPHILUM
JRNL REF J.MOL.BIOL. V. 324 1041 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 12470958
JRNL DOI 10.1016/S0022-2836(02)01153-1
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 86.6
REMARK 3 NUMBER OF REFLECTIONS : 167003
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.254
REMARK 3 FREE R VALUE : 0.288
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 18487
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 49584
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 960
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.014
REMARK 3 BOND ANGLES (DEGREES) : 1.490
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1N6E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-NOV-02.
REMARK 100 THE DEPOSITION ID IS D_1000017575.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-DEC-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9794
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 209855
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 3.070
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.30500
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIRECT REFINEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 1K32
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: ISOPROPANOL, MES, PH 6.4, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 122.55000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: DODECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 62660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 205760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -160.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K, L
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 PRO A 2
REMARK 465 SER A 3
REMARK 465 LEU A 4
REMARK 465 MET A 5
REMARK 465 SER A 6
REMARK 465 PHE A 7
REMARK 465 GLY A 8
REMARK 465 SER A 9
REMARK 465 CYS A 10
REMARK 465 GLN A 11
REMARK 465 TRP A 12
REMARK 465 ILE A 13
REMARK 465 ASP A 14
REMARK 465 GLN A 15
REMARK 465 GLY A 16
REMARK 465 ARG A 17
REMARK 465 PHE A 18
REMARK 465 SER A 19
REMARK 465 ARG A 20
REMARK 465 SER A 21
REMARK 465 LEU A 22
REMARK 465 TYR A 23
REMARK 465 ARG A 24
REMARK 465 ASN A 25
REMARK 465 PHE A 26
REMARK 465 LYS A 27
REMARK 465 THR A 28
REMARK 465 PHE A 29
REMARK 465 LYS A 30
REMARK 465 LEU A 31
REMARK 465 HIS A 32
REMARK 465 GLU A 33
REMARK 465 MET A 34
REMARK 465 HIS A 35
REMARK 465 GLY A 36
REMARK 465 LEU A 37
REMARK 465 CYS A 38
REMARK 465 TRP A 1062
REMARK 465 ASN A 1063
REMARK 465 GLU A 1064
REMARK 465 GLU A 1065
REMARK 465 LEU A 1066
REMARK 465 PRO A 1067
REMARK 465 GLN A 1068
REMARK 465 ARG A 1069
REMARK 465 PRO A 1070
REMARK 465 SER A 1071
REMARK 465 ASP B 1201
REMARK 465 GLN B 1202
REMARK 465 MET C 1
REMARK 465 PRO C 2
REMARK 465 SER C 3
REMARK 465 LEU C 4
REMARK 465 MET C 5
REMARK 465 SER C 6
REMARK 465 PHE C 7
REMARK 465 GLY C 8
REMARK 465 SER C 9
REMARK 465 CYS C 10
REMARK 465 GLN C 11
REMARK 465 TRP C 12
REMARK 465 ILE C 13
REMARK 465 ASP C 14
REMARK 465 GLN C 15
REMARK 465 GLY C 16
REMARK 465 ARG C 17
REMARK 465 PHE C 18
REMARK 465 SER C 19
REMARK 465 ARG C 20
REMARK 465 SER C 21
REMARK 465 LEU C 22
REMARK 465 TYR C 23
REMARK 465 ARG C 24
REMARK 465 ASN C 25
REMARK 465 PHE C 26
REMARK 465 LYS C 27
REMARK 465 THR C 28
REMARK 465 PHE C 29
REMARK 465 LYS C 30
REMARK 465 LEU C 31
REMARK 465 HIS C 32
REMARK 465 GLU C 33
REMARK 465 MET C 34
REMARK 465 HIS C 35
REMARK 465 GLY C 36
REMARK 465 LEU C 37
REMARK 465 CYS C 38
REMARK 465 TRP C 1062
REMARK 465 ASN C 1063
REMARK 465 GLU C 1064
REMARK 465 GLU C 1065
REMARK 465 LEU C 1066
REMARK 465 PRO C 1067
REMARK 465 GLN C 1068
REMARK 465 ARG C 1069
REMARK 465 PRO C 1070
REMARK 465 SER C 1071
REMARK 465 ASP D 1201
REMARK 465 GLN D 1202
REMARK 465 MET E 1
REMARK 465 PRO E 2
REMARK 465 SER E 3
REMARK 465 LEU E 4
REMARK 465 MET E 5
REMARK 465 SER E 6
REMARK 465 PHE E 7
REMARK 465 GLY E 8
REMARK 465 SER E 9
REMARK 465 CYS E 10
REMARK 465 GLN E 11
REMARK 465 TRP E 12
REMARK 465 ILE E 13
REMARK 465 ASP E 14
REMARK 465 GLN E 15
REMARK 465 GLY E 16
REMARK 465 ARG E 17
REMARK 465 PHE E 18
REMARK 465 SER E 19
REMARK 465 ARG E 20
REMARK 465 SER E 21
REMARK 465 LEU E 22
REMARK 465 TYR E 23
REMARK 465 ARG E 24
REMARK 465 ASN E 25
REMARK 465 PHE E 26
REMARK 465 LYS E 27
REMARK 465 THR E 28
REMARK 465 PHE E 29
REMARK 465 LYS E 30
REMARK 465 LEU E 31
REMARK 465 HIS E 32
REMARK 465 GLU E 33
REMARK 465 MET E 34
REMARK 465 HIS E 35
REMARK 465 GLY E 36
REMARK 465 LEU E 37
REMARK 465 CYS E 38
REMARK 465 TRP E 1062
REMARK 465 ASN E 1063
REMARK 465 GLU E 1064
REMARK 465 GLU E 1065
REMARK 465 LEU E 1066
REMARK 465 PRO E 1067
REMARK 465 GLN E 1068
REMARK 465 ARG E 1069
REMARK 465 PRO E 1070
REMARK 465 SER E 1071
REMARK 465 ASP F 1201
REMARK 465 GLN F 1202
REMARK 465 MET G 1
REMARK 465 PRO G 2
REMARK 465 SER G 3
REMARK 465 LEU G 4
REMARK 465 MET G 5
REMARK 465 SER G 6
REMARK 465 PHE G 7
REMARK 465 GLY G 8
REMARK 465 SER G 9
REMARK 465 CYS G 10
REMARK 465 GLN G 11
REMARK 465 TRP G 12
REMARK 465 ILE G 13
REMARK 465 ASP G 14
REMARK 465 GLN G 15
REMARK 465 GLY G 16
REMARK 465 ARG G 17
REMARK 465 PHE G 18
REMARK 465 SER G 19
REMARK 465 ARG G 20
REMARK 465 SER G 21
REMARK 465 LEU G 22
REMARK 465 TYR G 23
REMARK 465 ARG G 24
REMARK 465 ASN G 25
REMARK 465 PHE G 26
REMARK 465 LYS G 27
REMARK 465 THR G 28
REMARK 465 PHE G 29
REMARK 465 LYS G 30
REMARK 465 LEU G 31
REMARK 465 HIS G 32
REMARK 465 GLU G 33
REMARK 465 MET G 34
REMARK 465 HIS G 35
REMARK 465 GLY G 36
REMARK 465 LEU G 37
REMARK 465 CYS G 38
REMARK 465 TRP G 1062
REMARK 465 ASN G 1063
REMARK 465 GLU G 1064
REMARK 465 GLU G 1065
REMARK 465 LEU G 1066
REMARK 465 PRO G 1067
REMARK 465 GLN G 1068
REMARK 465 ARG G 1069
REMARK 465 PRO G 1070
REMARK 465 SER G 1071
REMARK 465 ASP H 1201
REMARK 465 GLN H 1202
REMARK 465 MET I 1
REMARK 465 PRO I 2
REMARK 465 SER I 3
REMARK 465 LEU I 4
REMARK 465 MET I 5
REMARK 465 SER I 6
REMARK 465 PHE I 7
REMARK 465 GLY I 8
REMARK 465 SER I 9
REMARK 465 CYS I 10
REMARK 465 GLN I 11
REMARK 465 TRP I 12
REMARK 465 ILE I 13
REMARK 465 ASP I 14
REMARK 465 GLN I 15
REMARK 465 GLY I 16
REMARK 465 ARG I 17
REMARK 465 PHE I 18
REMARK 465 SER I 19
REMARK 465 ARG I 20
REMARK 465 SER I 21
REMARK 465 LEU I 22
REMARK 465 TYR I 23
REMARK 465 ARG I 24
REMARK 465 ASN I 25
REMARK 465 PHE I 26
REMARK 465 LYS I 27
REMARK 465 THR I 28
REMARK 465 PHE I 29
REMARK 465 LYS I 30
REMARK 465 LEU I 31
REMARK 465 HIS I 32
REMARK 465 GLU I 33
REMARK 465 MET I 34
REMARK 465 HIS I 35
REMARK 465 GLY I 36
REMARK 465 LEU I 37
REMARK 465 CYS I 38
REMARK 465 TRP I 1062
REMARK 465 ASN I 1063
REMARK 465 GLU I 1064
REMARK 465 GLU I 1065
REMARK 465 LEU I 1066
REMARK 465 PRO I 1067
REMARK 465 GLN I 1068
REMARK 465 ARG I 1069
REMARK 465 PRO I 1070
REMARK 465 SER I 1071
REMARK 465 ASP J 1201
REMARK 465 GLN J 1202
REMARK 465 MET K 1
REMARK 465 PRO K 2
REMARK 465 SER K 3
REMARK 465 LEU K 4
REMARK 465 MET K 5
REMARK 465 SER K 6
REMARK 465 PHE K 7
REMARK 465 GLY K 8
REMARK 465 SER K 9
REMARK 465 CYS K 10
REMARK 465 GLN K 11
REMARK 465 TRP K 12
REMARK 465 ILE K 13
REMARK 465 ASP K 14
REMARK 465 GLN K 15
REMARK 465 GLY K 16
REMARK 465 ARG K 17
REMARK 465 PHE K 18
REMARK 465 SER K 19
REMARK 465 ARG K 20
REMARK 465 SER K 21
REMARK 465 LEU K 22
REMARK 465 TYR K 23
REMARK 465 ARG K 24
REMARK 465 ASN K 25
REMARK 465 PHE K 26
REMARK 465 LYS K 27
REMARK 465 THR K 28
REMARK 465 PHE K 29
REMARK 465 LYS K 30
REMARK 465 LEU K 31
REMARK 465 HIS K 32
REMARK 465 GLU K 33
REMARK 465 MET K 34
REMARK 465 HIS K 35
REMARK 465 GLY K 36
REMARK 465 LEU K 37
REMARK 465 CYS K 38
REMARK 465 TRP K 1062
REMARK 465 ASN K 1063
REMARK 465 GLU K 1064
REMARK 465 GLU K 1065
REMARK 465 LEU K 1066
REMARK 465 PRO K 1067
REMARK 465 GLN K 1068
REMARK 465 ARG K 1069
REMARK 465 PRO K 1070
REMARK 465 SER K 1071
REMARK 465 ASP L 1201
REMARK 465 GLN L 1202
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 MET A 39 CB CG SD CE
REMARK 480 ARG A 283 CG CD NE CZ NH1 NH2
REMARK 480 GLU A 301 CG CD OE1 OE2
REMARK 480 LYS A 302 CG CD CE NZ
REMARK 480 LYS A 396 CB CG CD CE NZ
REMARK 480 GLU A 398 CB CG CD OE1 OE2
REMARK 480 GLU A 562 CG CD OE1 OE2
REMARK 480 LYS A 646 CG CD CE NZ
REMARK 480 GLU A 663 CG CD OE1 OE2
REMARK 480 LYS A 664 CG CD CE NZ
REMARK 480 GLU A 666 CG CD OE1 OE2
REMARK 480 LYS A 675 CB CG CD CE NZ
REMARK 480 LYS A 708 CB CG CD CE NZ
REMARK 480 ARG A 836 CB CG CD NE CZ NH1 NH2
REMARK 480 LYS A 876 CG CD CE NZ
REMARK 480 LYS A 931 CG CD CE NZ
REMARK 480 LYS A 1044 CG CD CE NZ
REMARK 480 GLU A 1057 CG CD OE1 OE2
REMARK 480 ARG A 1060 CG CD NE CZ NH1 NH2
REMARK 480 ASN A 1061 N CA C CB CG OD1 ND2
REMARK 480 MET C 39 CB CG SD CE
REMARK 480 ARG C 283 CG CD NE CZ NH1 NH2
REMARK 480 GLU C 301 CG CD OE1 OE2
REMARK 480 LYS C 302 CG CD CE NZ
REMARK 480 LYS C 396 CB CG CD CE NZ
REMARK 480 GLU C 398 CB CG CD OE1 OE2
REMARK 480 GLU C 562 CG CD OE1 OE2
REMARK 480 LYS C 646 CG CD CE NZ
REMARK 480 GLU C 663 CG CD OE1 OE2
REMARK 480 LYS C 664 CG CD CE NZ
REMARK 480 GLU C 666 CG CD OE1 OE2
REMARK 480 LYS C 675 CB CG CD CE NZ
REMARK 480 LYS C 708 CB CG CD CE NZ
REMARK 480 ARG C 836 CB CG CD NE CZ NH1 NH2
REMARK 480 LYS C 876 CG CD CE NZ
REMARK 480 LYS C 931 CG CD CE NZ
REMARK 480 LYS C 1044 CG CD CE NZ
REMARK 480 GLU C 1057 CG CD OE1 OE2
REMARK 480 ARG C 1060 CG CD NE CZ NH1 NH2
REMARK 480 ASN C 1061 N CA C CB CG OD1 ND2
REMARK 480 MET E 39 CB CG SD CE
REMARK 480 ARG E 283 CG CD NE CZ NH1 NH2
REMARK 480 GLU E 301 CG CD OE1 OE2
REMARK 480 LYS E 302 CG CD CE NZ
REMARK 480 LYS E 396 CB CG CD CE NZ
REMARK 480 GLU E 398 CB CG CD OE1 OE2
REMARK 480 GLU E 562 CG CD OE1 OE2
REMARK 480 LYS E 646 CG CD CE NZ
REMARK 480 GLU E 663 CG CD OE1 OE2
REMARK 480 LYS E 664 CG CD CE NZ
REMARK 480 GLU E 666 CG CD OE1 OE2
REMARK 480 LYS E 675 CB CG CD CE NZ
REMARK 480 LYS E 708 CB CG CD CE NZ
REMARK 480 ARG E 836 CB CG CD NE CZ NH1 NH2
REMARK 480 LYS E 876 CG CD CE NZ
REMARK 480 LYS E 931 CG CD CE NZ
REMARK 480 LYS E 1044 CG CD CE NZ
REMARK 480 GLU E 1057 CG CD OE1 OE2
REMARK 480 ARG E 1060 CG CD NE CZ NH1 NH2
REMARK 480 ASN E 1061 N CA C CB CG OD1 ND2
REMARK 480 MET G 39 CB CG SD CE
REMARK 480 ARG G 283 CG CD NE CZ NH1 NH2
REMARK 480 GLU G 301 CG CD OE1 OE2
REMARK 480 LYS G 302 CG CD CE NZ
REMARK 480 LYS G 396 CB CG CD CE NZ
REMARK 480 GLU G 398 CB CG CD OE1 OE2
REMARK 480 GLU G 562 CG CD OE1 OE2
REMARK 480 LYS G 646 CG CD CE NZ
REMARK 480 GLU G 663 CG CD OE1 OE2
REMARK 480 LYS G 664 CG CD CE NZ
REMARK 480 GLU G 666 CG CD OE1 OE2
REMARK 480 LYS G 675 CB CG CD CE NZ
REMARK 480 LYS G 708 CB CG CD CE NZ
REMARK 480 ARG G 836 CB CG CD NE CZ NH1 NH2
REMARK 480 LYS G 876 CG CD CE NZ
REMARK 480 LYS G 931 CG CD CE NZ
REMARK 480 LYS G 1044 CG CD CE NZ
REMARK 480 GLU G 1057 CG CD OE1 OE2
REMARK 480 ARG G 1060 CG CD NE CZ NH1 NH2
REMARK 480 ASN G 1061 N CA C CB CG OD1 ND2
REMARK 480 MET I 39 CB CG SD CE
REMARK 480 ARG I 283 CG CD NE CZ NH1 NH2
REMARK 480 GLU I 301 CG CD OE1 OE2
REMARK 480 LYS I 302 CG CD CE NZ
REMARK 480 LYS I 396 CB CG CD CE NZ
REMARK 480 GLU I 398 CB CG CD OE1 OE2
REMARK 480 GLU I 562 CG CD OE1 OE2
REMARK 480 LYS I 646 CG CD CE NZ
REMARK 480 GLU I 663 CG CD OE1 OE2
REMARK 480 LYS I 664 CG CD CE NZ
REMARK 480 GLU I 666 CG CD OE1 OE2
REMARK 480 LYS I 675 CB CG CD CE NZ
REMARK 480 LYS I 708 CB CG CD CE NZ
REMARK 480 ARG I 836 CB CG CD NE CZ NH1 NH2
REMARK 480 LYS I 876 CG CD CE NZ
REMARK 480 LYS I 931 CG CD CE NZ
REMARK 480 LYS I 1044 CG CD CE NZ
REMARK 480 GLU I 1057 CG CD OE1 OE2
REMARK 480 ARG I 1060 CG CD NE CZ NH1 NH2
REMARK 480 ASN I 1061 N CA C CB CG OD1 ND2
REMARK 480 MET K 39 CB CG SD CE
REMARK 480 ARG K 283 CG CD NE CZ NH1 NH2
REMARK 480 GLU K 301 CG CD OE1 OE2
REMARK 480 LYS K 302 CG CD CE NZ
REMARK 480 LYS K 396 CB CG CD CE NZ
REMARK 480 GLU K 398 CB CG CD OE1 OE2
REMARK 480 GLU K 562 CG CD OE1 OE2
REMARK 480 LYS K 646 CG CD CE NZ
REMARK 480 GLU K 663 CG CD OE1 OE2
REMARK 480 LYS K 664 CG CD CE NZ
REMARK 480 GLU K 666 CG CD OE1 OE2
REMARK 480 LYS K 675 CB CG CD CE NZ
REMARK 480 LYS K 708 CB CG CD CE NZ
REMARK 480 ARG K 836 CB CG CD NE CZ NH1 NH2
REMARK 480 LYS K 876 CG CD CE NZ
REMARK 480 LYS K 931 CG CD CE NZ
REMARK 480 LYS K 1044 CG CD CE NZ
REMARK 480 GLU K 1057 CG CD OE1 OE2
REMARK 480 ARG K 1060 CG CD NE CZ NH1 NH2
REMARK 480 ASN K 1061 N CA C CB CG OD1 ND2
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 OG SER C 965 C1 0QE D 1214 1.27
REMARK 500 OG SER A 965 C1 0QE B 1214 1.27
REMARK 500 OG SER E 965 C1 0QE F 1214 1.31
REMARK 500 OG SER I 965 C1 0QE J 1214 1.33
REMARK 500 OG SER K 965 C1 0QE L 1214 1.34
REMARK 500 OG SER G 965 C1 0QE H 1214 1.38
REMARK 500 O PHE F 1213 O HOH F 239 1.73
REMARK 500 CB SER C 965 C1 0QE D 1214 1.87
REMARK 500 CB SER G 965 C1 0QE H 1214 1.87
REMARK 500 CB SER I 965 C1 0QE J 1214 1.88
REMARK 500 CB SER A 965 C1 0QE B 1214 1.88
REMARK 500 CB SER E 965 C1 0QE F 1214 1.88
REMARK 500 CB SER K 965 C1 0QE L 1214 1.88
REMARK 500 OE1 GLU K 1010 O HOH K 1079 2.06
REMARK 500 OE1 GLU C 789 O HOH C 1119 2.06
REMARK 500 OG SER K 519 O HOH K 1125 2.10
REMARK 500 N PHE E 533 O HOH E 1181 2.11
REMARK 500 ND2 ASN C 720 O HOH C 1186 2.12
REMARK 500 O GLU F 1209 O HOH F 525 2.14
REMARK 500 O SER I 548 O HOH I 1178 2.15
REMARK 500 OD2 ASP K 107 O HOH K 1131 2.16
REMARK 500 N TYR E 1035 O HOH E 1104 2.17
REMARK 500 O ARG A 743 O HOH A 1151 2.18
REMARK 500 ND2 ASN C 279 O HOH C 1184 2.18
REMARK 500 OG1 THR K 439 O HOH K 1089 2.19
REMARK 500 O PRO C 601 O HOH C 1096 2.19
REMARK 500 N PHE K 533 O HOH K 1090 2.19
REMARK 500 OG SER C 965 C PHE D 1213 2.19
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 N ASN A 167 OD2 ASP I 143 2545 2.06
REMARK 500 N ASN C 167 OD2 ASP G 143 2455 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 PHE B1213 C PHE B1213 O 0.198
REMARK 500 CYS C 161 CB CYS C 161 SG 0.103
REMARK 500 PHE D1213 C PHE D1213 O 0.209
REMARK 500 PHE F1213 C PHE F1213 O 0.183
REMARK 500 PHE H1213 C PHE H1213 O 0.214
REMARK 500 CYS I 161 CB CYS I 161 SG 0.107
REMARK 500 PHE J1213 C PHE J1213 O 0.197
REMARK 500 PHE L1213 C PHE L1213 O 0.156
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 45 65.24 35.52
REMARK 500 ASP A 59 -2.83 63.03
REMARK 500 THR A 135 81.03 69.57
REMARK 500 ASP A 143 1.06 -66.00
REMARK 500 ASN A 218 86.21 -154.48
REMARK 500 SER A 219 47.01 12.43
REMARK 500 ASP A 227 77.94 -150.08
REMARK 500 LEU A 259 17.42 -69.63
REMARK 500 THR A 271 -11.08 -147.82
REMARK 500 ASP A 328 109.69 58.82
REMARK 500 PRO A 361 172.36 -53.01
REMARK 500 ARG A 363 72.37 80.58
REMARK 500 ALA A 397 84.09 -164.28
REMARK 500 ILE A 449 66.43 -100.26
REMARK 500 GLU A 496 40.77 -106.34
REMARK 500 SER A 498 -144.42 -158.75
REMARK 500 TYR A 517 47.03 -108.03
REMARK 500 ASP A 521 119.13 -164.00
REMARK 500 LEU A 529 96.39 -65.92
REMARK 500 SER A 561 75.80 -101.85
REMARK 500 GLU A 562 -135.14 -81.26
REMARK 500 ALA A 563 44.64 70.67
REMARK 500 ASN A 579 75.09 -68.36
REMARK 500 MET A 587 146.08 -171.84
REMARK 500 PRO A 665 -7.25 -57.16
REMARK 500 ASP A 667 64.03 -100.07
REMARK 500 TYR A 715 -70.55 -48.14
REMARK 500 ASN A 820 107.20 -54.76
REMARK 500 ASP A 855 20.83 -151.14
REMARK 500 PHE A 919 3.79 -162.92
REMARK 500 ASN A 949 51.90 -90.91
REMARK 500 SER A 965 -116.67 60.19
REMARK 500 THR A 995 77.96 -151.45
REMARK 500 PRO A1009 99.79 -68.93
REMARK 500 ASP A1017 39.41 74.93
REMARK 500 ALA A1018 -14.96 -176.13
REMARK 500 TYR A1025 -47.98 -150.21
REMARK 500 ARG A1060 44.06 -149.13
REMARK 500 GLN B1204 176.36 59.88
REMARK 500 ALA B1206 15.22 -142.86
REMARK 500 ALA B1208 136.56 -39.11
REMARK 500 ASN C 45 64.83 34.65
REMARK 500 ASP C 59 -3.28 63.57
REMARK 500 SER C 101 -35.92 -38.80
REMARK 500 THR C 135 80.26 69.92
REMARK 500 ASP C 143 2.16 -66.00
REMARK 500 ASN C 218 86.67 -156.11
REMARK 500 SER C 219 47.16 13.28
REMARK 500 LEU C 259 18.21 -67.85
REMARK 500 ASP C 263 61.88 60.13
REMARK 500
REMARK 500 THIS ENTRY HAS 232 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR E 776 0.07 SIDE CHAIN
REMARK 500 TYR E 822 0.07 SIDE CHAIN
REMARK 500 TYR K 822 0.07 SIDE CHAIN
REMARK 500 TYR K1025 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0QE B 1214
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0QE D 1214
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0QE F 1214
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0QE H 1214
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0QE J 1214
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0QE L 1214
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1K32 RELATED DB: PDB
REMARK 900 RELATED ID: 1N6D RELATED DB: PDB
REMARK 900 1N6D CONTAINS TETRAPEPTIDE CHLOROMETHYL KETONE DERIVATIVE
REMARK 900 RELATED ID: 1N6F RELATED DB: PDB
REMARK 900 1N6F CONTAINS Z-PHE-DIKETO-ARG-GLU-PHE
DBREF 1N6E A 1 1071 UNP P96086 TRI_THEAC 1 1071
DBREF 1N6E B 1201 1214 PDB 1N6E 1N6E 1201 1214
DBREF 1N6E C 1 1071 UNP P96086 TRI_THEAC 1 1071
DBREF 1N6E D 1201 1214 PDB 1N6E 1N6E 1201 1214
DBREF 1N6E E 1 1071 UNP P96086 TRI_THEAC 1 1071
DBREF 1N6E F 1201 1214 PDB 1N6E 1N6E 1201 1214
DBREF 1N6E G 1 1071 UNP P96086 TRI_THEAC 1 1071
DBREF 1N6E H 1201 1214 PDB 1N6E 1N6E 1201 1214
DBREF 1N6E I 1 1071 UNP P96086 TRI_THEAC 1 1071
DBREF 1N6E J 1201 1214 PDB 1N6E 1N6E 1201 1214
DBREF 1N6E K 1 1071 UNP P96086 TRI_THEAC 1 1071
DBREF 1N6E L 1201 1214 PDB 1N6E 1N6E 1201 1214
SEQRES 1 A 1071 MET PRO SER LEU MET SER PHE GLY SER CYS GLN TRP ILE
SEQRES 2 A 1071 ASP GLN GLY ARG PHE SER ARG SER LEU TYR ARG ASN PHE
SEQRES 3 A 1071 LYS THR PHE LYS LEU HIS GLU MET HIS GLY LEU CYS MET
SEQRES 4 A 1071 PRO ASN LEU LEU LEU ASN PRO ASP ILE HIS GLY ASP ARG
SEQRES 5 A 1071 ILE ILE PHE VAL CYS CYS ASP ASP LEU TRP GLU HIS ASP
SEQRES 6 A 1071 LEU LYS SER GLY SER THR ARG LYS ILE VAL SER ASN LEU
SEQRES 7 A 1071 GLY VAL ILE ASN ASN ALA ARG PHE PHE PRO ASP GLY ARG
SEQRES 8 A 1071 LYS ILE ALA ILE ARG VAL MET ARG GLY SER SER LEU ASN
SEQRES 9 A 1071 THR ALA ASP LEU TYR PHE TYR ASN GLY GLU ASN GLY GLU
SEQRES 10 A 1071 ILE LYS ARG ILE THR TYR PHE SER GLY LYS SER THR GLY
SEQRES 11 A 1071 ARG ARG MET PHE THR ASP VAL ALA GLY PHE ASP PRO ASP
SEQRES 12 A 1071 GLY ASN LEU ILE ILE SER THR ASP ALA MET GLN PRO PHE
SEQRES 13 A 1071 SER SER MET THR CYS LEU TYR ARG VAL GLU ASN ASP GLY
SEQRES 14 A 1071 ILE ASN PHE VAL PRO LEU ASN LEU GLY PRO ALA THR HIS
SEQRES 15 A 1071 ILE LEU PHE ALA ASP GLY ARG ARG VAL ILE GLY ARG ASN
SEQRES 16 A 1071 THR PHE GLU LEU PRO HIS TRP LYS GLY TYR ARG GLY GLY
SEQRES 17 A 1071 THR ARG GLY LYS ILE TRP ILE GLU VAL ASN SER GLY ALA
SEQRES 18 A 1071 PHE LYS LYS ILE VAL ASP MET SER THR HIS VAL SER SER
SEQRES 19 A 1071 PRO VAL ILE VAL GLY HIS ARG ILE TYR PHE ILE THR ASP
SEQRES 20 A 1071 ILE ASP GLY PHE GLY GLN ILE TYR SER THR ASP LEU ASP
SEQRES 21 A 1071 GLY LYS ASP LEU ARG LYS HIS THR SER PHE THR ASP TYR
SEQRES 22 A 1071 TYR PRO ARG HIS LEU ASN THR ASP GLY ARG ARG ILE LEU
SEQRES 23 A 1071 PHE SER LYS GLY GLY SER ILE TYR ILE PHE ASN PRO ASP
SEQRES 24 A 1071 THR GLU LYS ILE GLU LYS ILE GLU ILE GLY ASP LEU GLU
SEQRES 25 A 1071 SER PRO GLU ASP ARG ILE ILE SER ILE PRO SER LYS PHE
SEQRES 26 A 1071 ALA GLU ASP PHE SER PRO LEU ASP GLY ASP LEU ILE ALA
SEQRES 27 A 1071 PHE VAL SER ARG GLY GLN ALA PHE ILE GLN ASP VAL SER
SEQRES 28 A 1071 GLY THR TYR VAL LEU LYS VAL PRO GLU PRO LEU ARG ILE
SEQRES 29 A 1071 ARG TYR VAL ARG ARG GLY GLY ASP THR LYS VAL ALA PHE
SEQRES 30 A 1071 ILE HIS GLY THR ARG GLU GLY ASP PHE LEU GLY ILE TYR
SEQRES 31 A 1071 ASP TYR ARG THR GLY LYS ALA GLU LYS PHE GLU GLU ASN
SEQRES 32 A 1071 LEU GLY ASN VAL PHE ALA MET GLY VAL ASP ARG ASN GLY
SEQRES 33 A 1071 LYS PHE ALA VAL VAL ALA ASN ASP ARG PHE GLU ILE MET
SEQRES 34 A 1071 THR VAL ASP LEU GLU THR GLY LYS PRO THR VAL ILE GLU
SEQRES 35 A 1071 ARG SER ARG GLU ALA MET ILE THR ASP PHE THR ILE SER
SEQRES 36 A 1071 ASP ASN SER ARG PHE ILE ALA TYR GLY PHE PRO LEU LYS
SEQRES 37 A 1071 HIS GLY GLU THR ASP GLY TYR VAL MET GLN ALA ILE HIS
SEQRES 38 A 1071 VAL TYR ASP MET GLU GLY ARG LYS ILE PHE ALA ALA THR
SEQRES 39 A 1071 THR GLU ASN SER HIS ASP TYR ALA PRO ALA PHE ASP ALA
SEQRES 40 A 1071 ASP SER LYS ASN LEU TYR TYR LEU SER TYR ARG SER LEU
SEQRES 41 A 1071 ASP PRO SER PRO ASP ARG VAL VAL LEU ASN PHE SER PHE
SEQRES 42 A 1071 GLU VAL VAL SER LYS PRO PHE VAL ILE PRO LEU ILE PRO
SEQRES 43 A 1071 GLY SER PRO ASN PRO THR LYS LEU VAL PRO ARG SER MET
SEQRES 44 A 1071 THR SER GLU ALA GLY GLU TYR ASP LEU ASN ASP MET TYR
SEQRES 45 A 1071 LYS ARG SER SER PRO ILE ASN VAL ASP PRO GLY ASP TYR
SEQRES 46 A 1071 ARG MET ILE ILE PRO LEU GLU SER SER ILE LEU ILE TYR
SEQRES 47 A 1071 SER VAL PRO VAL HIS GLY GLU PHE ALA ALA TYR TYR GLN
SEQRES 48 A 1071 GLY ALA PRO GLU LYS GLY VAL LEU LEU LYS TYR ASP VAL
SEQRES 49 A 1071 LYS THR ARG LYS VAL THR GLU VAL LYS ASN ASN LEU THR
SEQRES 50 A 1071 ASP LEU ARG LEU SER ALA ASP ARG LYS THR VAL MET VAL
SEQRES 51 A 1071 ARG LYS ASP ASP GLY LYS ILE TYR THR PHE PRO LEU GLU
SEQRES 52 A 1071 LYS PRO GLU ASP GLU ARG THR VAL GLU THR ASP LYS ARG
SEQRES 53 A 1071 PRO LEU VAL SER SER ILE HIS GLU GLU PHE LEU GLN MET
SEQRES 54 A 1071 TYR ASP GLU ALA TRP LYS LEU ALA ARG ASP ASN TYR TRP
SEQRES 55 A 1071 ASN GLU ALA VAL ALA LYS GLU ILE SER GLU ARG ILE TYR
SEQRES 56 A 1071 GLU LYS TYR ARG ASN LEU VAL PRO LEU CYS LYS THR ARG
SEQRES 57 A 1071 TYR ASP LEU SER ASN VAL ILE VAL GLU MET GLN GLY GLU
SEQRES 58 A 1071 TYR ARG THR SER HIS SER TYR GLU MET GLY GLY THR PHE
SEQRES 59 A 1071 THR ASP LYS ASP PRO PHE ARG SER GLY ARG ILE ALA CYS
SEQRES 60 A 1071 ASP PHE LYS LEU ASP GLY ASP HIS TYR VAL VAL ALA LYS
SEQRES 61 A 1071 ALA TYR ALA GLY ASP TYR SER ASN GLU GLY GLU LYS SER
SEQRES 62 A 1071 PRO ILE PHE GLU TYR GLY ILE ASP PRO THR GLY TYR LEU
SEQRES 63 A 1071 ILE GLU ASP ILE ASP GLY GLU THR VAL GLY ALA GLY SER
SEQRES 64 A 1071 ASN ILE TYR ARG VAL LEU SER GLU LYS ALA GLY THR SER
SEQRES 65 A 1071 ALA ARG ILE ARG LEU SER GLY LYS GLY GLY ASP LYS ARG
SEQRES 66 A 1071 ASP LEU MET ILE ASP ILE LEU ASP ASP ASP ARG PHE ILE
SEQRES 67 A 1071 ARG TYR ARG SER TRP VAL GLU ALA ASN ARG ARG TYR VAL
SEQRES 68 A 1071 HIS GLU ARG SER LYS GLY THR ILE GLY TYR ILE HIS ILE
SEQRES 69 A 1071 PRO ASP MET GLY MET MET GLY LEU ASN GLU PHE TYR ARG
SEQRES 70 A 1071 LEU PHE ILE ASN GLU SER SER TYR GLN GLY LEU ILE VAL
SEQRES 71 A 1071 ASP VAL ARG PHE ASN GLY GLY GLY PHE VAL SER GLN LEU
SEQRES 72 A 1071 ILE ILE GLU LYS LEU MET ASN LYS ARG ILE GLY TYR ASP
SEQRES 73 A 1071 ASN PRO ARG ARG GLY THR LEU SER PRO TYR PRO THR ASN
SEQRES 74 A 1071 SER VAL ARG GLY LYS ILE ILE ALA ILE THR ASN GLU TYR
SEQRES 75 A 1071 ALA GLY SER ASP GLY ASP ILE PHE SER PHE SER PHE LYS
SEQRES 76 A 1071 LYS LEU GLY LEU GLY LYS LEU ILE GLY THR ARG THR TRP
SEQRES 77 A 1071 GLY GLY VAL VAL GLY ILE THR PRO LYS ARG ARG LEU ILE
SEQRES 78 A 1071 ASP GLY THR VAL LEU THR GLN PRO GLU PHE ALA PHE TRP
SEQRES 79 A 1071 PHE ARG ASP ALA GLY PHE GLY VAL GLU ASN TYR GLY VAL
SEQRES 80 A 1071 ASP PRO ASP VAL GLU ILE GLU TYR ALA PRO HIS ASP TYR
SEQRES 81 A 1071 LEU SER GLY LYS ASP PRO GLN ILE ASP TYR ALA ILE ASP
SEQRES 82 A 1071 ALA LEU ILE GLU GLU LEU ARG ASN TRP ASN GLU GLU LEU
SEQRES 83 A 1071 PRO GLN ARG PRO SER
SEQRES 1 B 14 ASP GLN THR GLN LYS ALA ALA ALA GLU LEU THR PHE PHE
SEQRES 2 B 14 0QE
SEQRES 1 C 1071 MET PRO SER LEU MET SER PHE GLY SER CYS GLN TRP ILE
SEQRES 2 C 1071 ASP GLN GLY ARG PHE SER ARG SER LEU TYR ARG ASN PHE
SEQRES 3 C 1071 LYS THR PHE LYS LEU HIS GLU MET HIS GLY LEU CYS MET
SEQRES 4 C 1071 PRO ASN LEU LEU LEU ASN PRO ASP ILE HIS GLY ASP ARG
SEQRES 5 C 1071 ILE ILE PHE VAL CYS CYS ASP ASP LEU TRP GLU HIS ASP
SEQRES 6 C 1071 LEU LYS SER GLY SER THR ARG LYS ILE VAL SER ASN LEU
SEQRES 7 C 1071 GLY VAL ILE ASN ASN ALA ARG PHE PHE PRO ASP GLY ARG
SEQRES 8 C 1071 LYS ILE ALA ILE ARG VAL MET ARG GLY SER SER LEU ASN
SEQRES 9 C 1071 THR ALA ASP LEU TYR PHE TYR ASN GLY GLU ASN GLY GLU
SEQRES 10 C 1071 ILE LYS ARG ILE THR TYR PHE SER GLY LYS SER THR GLY
SEQRES 11 C 1071 ARG ARG MET PHE THR ASP VAL ALA GLY PHE ASP PRO ASP
SEQRES 12 C 1071 GLY ASN LEU ILE ILE SER THR ASP ALA MET GLN PRO PHE
SEQRES 13 C 1071 SER SER MET THR CYS LEU TYR ARG VAL GLU ASN ASP GLY
SEQRES 14 C 1071 ILE ASN PHE VAL PRO LEU ASN LEU GLY PRO ALA THR HIS
SEQRES 15 C 1071 ILE LEU PHE ALA ASP GLY ARG ARG VAL ILE GLY ARG ASN
SEQRES 16 C 1071 THR PHE GLU LEU PRO HIS TRP LYS GLY TYR ARG GLY GLY
SEQRES 17 C 1071 THR ARG GLY LYS ILE TRP ILE GLU VAL ASN SER GLY ALA
SEQRES 18 C 1071 PHE LYS LYS ILE VAL ASP MET SER THR HIS VAL SER SER
SEQRES 19 C 1071 PRO VAL ILE VAL GLY HIS ARG ILE TYR PHE ILE THR ASP
SEQRES 20 C 1071 ILE ASP GLY PHE GLY GLN ILE TYR SER THR ASP LEU ASP
SEQRES 21 C 1071 GLY LYS ASP LEU ARG LYS HIS THR SER PHE THR ASP TYR
SEQRES 22 C 1071 TYR PRO ARG HIS LEU ASN THR ASP GLY ARG ARG ILE LEU
SEQRES 23 C 1071 PHE SER LYS GLY GLY SER ILE TYR ILE PHE ASN PRO ASP
SEQRES 24 C 1071 THR GLU LYS ILE GLU LYS ILE GLU ILE GLY ASP LEU GLU
SEQRES 25 C 1071 SER PRO GLU ASP ARG ILE ILE SER ILE PRO SER LYS PHE
SEQRES 26 C 1071 ALA GLU ASP PHE SER PRO LEU ASP GLY ASP LEU ILE ALA
SEQRES 27 C 1071 PHE VAL SER ARG GLY GLN ALA PHE ILE GLN ASP VAL SER
SEQRES 28 C 1071 GLY THR TYR VAL LEU LYS VAL PRO GLU PRO LEU ARG ILE
SEQRES 29 C 1071 ARG TYR VAL ARG ARG GLY GLY ASP THR LYS VAL ALA PHE
SEQRES 30 C 1071 ILE HIS GLY THR ARG GLU GLY ASP PHE LEU GLY ILE TYR
SEQRES 31 C 1071 ASP TYR ARG THR GLY LYS ALA GLU LYS PHE GLU GLU ASN
SEQRES 32 C 1071 LEU GLY ASN VAL PHE ALA MET GLY VAL ASP ARG ASN GLY
SEQRES 33 C 1071 LYS PHE ALA VAL VAL ALA ASN ASP ARG PHE GLU ILE MET
SEQRES 34 C 1071 THR VAL ASP LEU GLU THR GLY LYS PRO THR VAL ILE GLU
SEQRES 35 C 1071 ARG SER ARG GLU ALA MET ILE THR ASP PHE THR ILE SER
SEQRES 36 C 1071 ASP ASN SER ARG PHE ILE ALA TYR GLY PHE PRO LEU LYS
SEQRES 37 C 1071 HIS GLY GLU THR ASP GLY TYR VAL MET GLN ALA ILE HIS
SEQRES 38 C 1071 VAL TYR ASP MET GLU GLY ARG LYS ILE PHE ALA ALA THR
SEQRES 39 C 1071 THR GLU ASN SER HIS ASP TYR ALA PRO ALA PHE ASP ALA
SEQRES 40 C 1071 ASP SER LYS ASN LEU TYR TYR LEU SER TYR ARG SER LEU
SEQRES 41 C 1071 ASP PRO SER PRO ASP ARG VAL VAL LEU ASN PHE SER PHE
SEQRES 42 C 1071 GLU VAL VAL SER LYS PRO PHE VAL ILE PRO LEU ILE PRO
SEQRES 43 C 1071 GLY SER PRO ASN PRO THR LYS LEU VAL PRO ARG SER MET
SEQRES 44 C 1071 THR SER GLU ALA GLY GLU TYR ASP LEU ASN ASP MET TYR
SEQRES 45 C 1071 LYS ARG SER SER PRO ILE ASN VAL ASP PRO GLY ASP TYR
SEQRES 46 C 1071 ARG MET ILE ILE PRO LEU GLU SER SER ILE LEU ILE TYR
SEQRES 47 C 1071 SER VAL PRO VAL HIS GLY GLU PHE ALA ALA TYR TYR GLN
SEQRES 48 C 1071 GLY ALA PRO GLU LYS GLY VAL LEU LEU LYS TYR ASP VAL
SEQRES 49 C 1071 LYS THR ARG LYS VAL THR GLU VAL LYS ASN ASN LEU THR
SEQRES 50 C 1071 ASP LEU ARG LEU SER ALA ASP ARG LYS THR VAL MET VAL
SEQRES 51 C 1071 ARG LYS ASP ASP GLY LYS ILE TYR THR PHE PRO LEU GLU
SEQRES 52 C 1071 LYS PRO GLU ASP GLU ARG THR VAL GLU THR ASP LYS ARG
SEQRES 53 C 1071 PRO LEU VAL SER SER ILE HIS GLU GLU PHE LEU GLN MET
SEQRES 54 C 1071 TYR ASP GLU ALA TRP LYS LEU ALA ARG ASP ASN TYR TRP
SEQRES 55 C 1071 ASN GLU ALA VAL ALA LYS GLU ILE SER GLU ARG ILE TYR
SEQRES 56 C 1071 GLU LYS TYR ARG ASN LEU VAL PRO LEU CYS LYS THR ARG
SEQRES 57 C 1071 TYR ASP LEU SER ASN VAL ILE VAL GLU MET GLN GLY GLU
SEQRES 58 C 1071 TYR ARG THR SER HIS SER TYR GLU MET GLY GLY THR PHE
SEQRES 59 C 1071 THR ASP LYS ASP PRO PHE ARG SER GLY ARG ILE ALA CYS
SEQRES 60 C 1071 ASP PHE LYS LEU ASP GLY ASP HIS TYR VAL VAL ALA LYS
SEQRES 61 C 1071 ALA TYR ALA GLY ASP TYR SER ASN GLU GLY GLU LYS SER
SEQRES 62 C 1071 PRO ILE PHE GLU TYR GLY ILE ASP PRO THR GLY TYR LEU
SEQRES 63 C 1071 ILE GLU ASP ILE ASP GLY GLU THR VAL GLY ALA GLY SER
SEQRES 64 C 1071 ASN ILE TYR ARG VAL LEU SER GLU LYS ALA GLY THR SER
SEQRES 65 C 1071 ALA ARG ILE ARG LEU SER GLY LYS GLY GLY ASP LYS ARG
SEQRES 66 C 1071 ASP LEU MET ILE ASP ILE LEU ASP ASP ASP ARG PHE ILE
SEQRES 67 C 1071 ARG TYR ARG SER TRP VAL GLU ALA ASN ARG ARG TYR VAL
SEQRES 68 C 1071 HIS GLU ARG SER LYS GLY THR ILE GLY TYR ILE HIS ILE
SEQRES 69 C 1071 PRO ASP MET GLY MET MET GLY LEU ASN GLU PHE TYR ARG
SEQRES 70 C 1071 LEU PHE ILE ASN GLU SER SER TYR GLN GLY LEU ILE VAL
SEQRES 71 C 1071 ASP VAL ARG PHE ASN GLY GLY GLY PHE VAL SER GLN LEU
SEQRES 72 C 1071 ILE ILE GLU LYS LEU MET ASN LYS ARG ILE GLY TYR ASP
SEQRES 73 C 1071 ASN PRO ARG ARG GLY THR LEU SER PRO TYR PRO THR ASN
SEQRES 74 C 1071 SER VAL ARG GLY LYS ILE ILE ALA ILE THR ASN GLU TYR
SEQRES 75 C 1071 ALA GLY SER ASP GLY ASP ILE PHE SER PHE SER PHE LYS
SEQRES 76 C 1071 LYS LEU GLY LEU GLY LYS LEU ILE GLY THR ARG THR TRP
SEQRES 77 C 1071 GLY GLY VAL VAL GLY ILE THR PRO LYS ARG ARG LEU ILE
SEQRES 78 C 1071 ASP GLY THR VAL LEU THR GLN PRO GLU PHE ALA PHE TRP
SEQRES 79 C 1071 PHE ARG ASP ALA GLY PHE GLY VAL GLU ASN TYR GLY VAL
SEQRES 80 C 1071 ASP PRO ASP VAL GLU ILE GLU TYR ALA PRO HIS ASP TYR
SEQRES 81 C 1071 LEU SER GLY LYS ASP PRO GLN ILE ASP TYR ALA ILE ASP
SEQRES 82 C 1071 ALA LEU ILE GLU GLU LEU ARG ASN TRP ASN GLU GLU LEU
SEQRES 83 C 1071 PRO GLN ARG PRO SER
SEQRES 1 D 14 ASP GLN THR GLN LYS ALA ALA ALA GLU LEU THR PHE PHE
SEQRES 2 D 14 0QE
SEQRES 1 E 1071 MET PRO SER LEU MET SER PHE GLY SER CYS GLN TRP ILE
SEQRES 2 E 1071 ASP GLN GLY ARG PHE SER ARG SER LEU TYR ARG ASN PHE
SEQRES 3 E 1071 LYS THR PHE LYS LEU HIS GLU MET HIS GLY LEU CYS MET
SEQRES 4 E 1071 PRO ASN LEU LEU LEU ASN PRO ASP ILE HIS GLY ASP ARG
SEQRES 5 E 1071 ILE ILE PHE VAL CYS CYS ASP ASP LEU TRP GLU HIS ASP
SEQRES 6 E 1071 LEU LYS SER GLY SER THR ARG LYS ILE VAL SER ASN LEU
SEQRES 7 E 1071 GLY VAL ILE ASN ASN ALA ARG PHE PHE PRO ASP GLY ARG
SEQRES 8 E 1071 LYS ILE ALA ILE ARG VAL MET ARG GLY SER SER LEU ASN
SEQRES 9 E 1071 THR ALA ASP LEU TYR PHE TYR ASN GLY GLU ASN GLY GLU
SEQRES 10 E 1071 ILE LYS ARG ILE THR TYR PHE SER GLY LYS SER THR GLY
SEQRES 11 E 1071 ARG ARG MET PHE THR ASP VAL ALA GLY PHE ASP PRO ASP
SEQRES 12 E 1071 GLY ASN LEU ILE ILE SER THR ASP ALA MET GLN PRO PHE
SEQRES 13 E 1071 SER SER MET THR CYS LEU TYR ARG VAL GLU ASN ASP GLY
SEQRES 14 E 1071 ILE ASN PHE VAL PRO LEU ASN LEU GLY PRO ALA THR HIS
SEQRES 15 E 1071 ILE LEU PHE ALA ASP GLY ARG ARG VAL ILE GLY ARG ASN
SEQRES 16 E 1071 THR PHE GLU LEU PRO HIS TRP LYS GLY TYR ARG GLY GLY
SEQRES 17 E 1071 THR ARG GLY LYS ILE TRP ILE GLU VAL ASN SER GLY ALA
SEQRES 18 E 1071 PHE LYS LYS ILE VAL ASP MET SER THR HIS VAL SER SER
SEQRES 19 E 1071 PRO VAL ILE VAL GLY HIS ARG ILE TYR PHE ILE THR ASP
SEQRES 20 E 1071 ILE ASP GLY PHE GLY GLN ILE TYR SER THR ASP LEU ASP
SEQRES 21 E 1071 GLY LYS ASP LEU ARG LYS HIS THR SER PHE THR ASP TYR
SEQRES 22 E 1071 TYR PRO ARG HIS LEU ASN THR ASP GLY ARG ARG ILE LEU
SEQRES 23 E 1071 PHE SER LYS GLY GLY SER ILE TYR ILE PHE ASN PRO ASP
SEQRES 24 E 1071 THR GLU LYS ILE GLU LYS ILE GLU ILE GLY ASP LEU GLU
SEQRES 25 E 1071 SER PRO GLU ASP ARG ILE ILE SER ILE PRO SER LYS PHE
SEQRES 26 E 1071 ALA GLU ASP PHE SER PRO LEU ASP GLY ASP LEU ILE ALA
SEQRES 27 E 1071 PHE VAL SER ARG GLY GLN ALA PHE ILE GLN ASP VAL SER
SEQRES 28 E 1071 GLY THR TYR VAL LEU LYS VAL PRO GLU PRO LEU ARG ILE
SEQRES 29 E 1071 ARG TYR VAL ARG ARG GLY GLY ASP THR LYS VAL ALA PHE
SEQRES 30 E 1071 ILE HIS GLY THR ARG GLU GLY ASP PHE LEU GLY ILE TYR
SEQRES 31 E 1071 ASP TYR ARG THR GLY LYS ALA GLU LYS PHE GLU GLU ASN
SEQRES 32 E 1071 LEU GLY ASN VAL PHE ALA MET GLY VAL ASP ARG ASN GLY
SEQRES 33 E 1071 LYS PHE ALA VAL VAL ALA ASN ASP ARG PHE GLU ILE MET
SEQRES 34 E 1071 THR VAL ASP LEU GLU THR GLY LYS PRO THR VAL ILE GLU
SEQRES 35 E 1071 ARG SER ARG GLU ALA MET ILE THR ASP PHE THR ILE SER
SEQRES 36 E 1071 ASP ASN SER ARG PHE ILE ALA TYR GLY PHE PRO LEU LYS
SEQRES 37 E 1071 HIS GLY GLU THR ASP GLY TYR VAL MET GLN ALA ILE HIS
SEQRES 38 E 1071 VAL TYR ASP MET GLU GLY ARG LYS ILE PHE ALA ALA THR
SEQRES 39 E 1071 THR GLU ASN SER HIS ASP TYR ALA PRO ALA PHE ASP ALA
SEQRES 40 E 1071 ASP SER LYS ASN LEU TYR TYR LEU SER TYR ARG SER LEU
SEQRES 41 E 1071 ASP PRO SER PRO ASP ARG VAL VAL LEU ASN PHE SER PHE
SEQRES 42 E 1071 GLU VAL VAL SER LYS PRO PHE VAL ILE PRO LEU ILE PRO
SEQRES 43 E 1071 GLY SER PRO ASN PRO THR LYS LEU VAL PRO ARG SER MET
SEQRES 44 E 1071 THR SER GLU ALA GLY GLU TYR ASP LEU ASN ASP MET TYR
SEQRES 45 E 1071 LYS ARG SER SER PRO ILE ASN VAL ASP PRO GLY ASP TYR
SEQRES 46 E 1071 ARG MET ILE ILE PRO LEU GLU SER SER ILE LEU ILE TYR
SEQRES 47 E 1071 SER VAL PRO VAL HIS GLY GLU PHE ALA ALA TYR TYR GLN
SEQRES 48 E 1071 GLY ALA PRO GLU LYS GLY VAL LEU LEU LYS TYR ASP VAL
SEQRES 49 E 1071 LYS THR ARG LYS VAL THR GLU VAL LYS ASN ASN LEU THR
SEQRES 50 E 1071 ASP LEU ARG LEU SER ALA ASP ARG LYS THR VAL MET VAL
SEQRES 51 E 1071 ARG LYS ASP ASP GLY LYS ILE TYR THR PHE PRO LEU GLU
SEQRES 52 E 1071 LYS PRO GLU ASP GLU ARG THR VAL GLU THR ASP LYS ARG
SEQRES 53 E 1071 PRO LEU VAL SER SER ILE HIS GLU GLU PHE LEU GLN MET
SEQRES 54 E 1071 TYR ASP GLU ALA TRP LYS LEU ALA ARG ASP ASN TYR TRP
SEQRES 55 E 1071 ASN GLU ALA VAL ALA LYS GLU ILE SER GLU ARG ILE TYR
SEQRES 56 E 1071 GLU LYS TYR ARG ASN LEU VAL PRO LEU CYS LYS THR ARG
SEQRES 57 E 1071 TYR ASP LEU SER ASN VAL ILE VAL GLU MET GLN GLY GLU
SEQRES 58 E 1071 TYR ARG THR SER HIS SER TYR GLU MET GLY GLY THR PHE
SEQRES 59 E 1071 THR ASP LYS ASP PRO PHE ARG SER GLY ARG ILE ALA CYS
SEQRES 60 E 1071 ASP PHE LYS LEU ASP GLY ASP HIS TYR VAL VAL ALA LYS
SEQRES 61 E 1071 ALA TYR ALA GLY ASP TYR SER ASN GLU GLY GLU LYS SER
SEQRES 62 E 1071 PRO ILE PHE GLU TYR GLY ILE ASP PRO THR GLY TYR LEU
SEQRES 63 E 1071 ILE GLU ASP ILE ASP GLY GLU THR VAL GLY ALA GLY SER
SEQRES 64 E 1071 ASN ILE TYR ARG VAL LEU SER GLU LYS ALA GLY THR SER
SEQRES 65 E 1071 ALA ARG ILE ARG LEU SER GLY LYS GLY GLY ASP LYS ARG
SEQRES 66 E 1071 ASP LEU MET ILE ASP ILE LEU ASP ASP ASP ARG PHE ILE
SEQRES 67 E 1071 ARG TYR ARG SER TRP VAL GLU ALA ASN ARG ARG TYR VAL
SEQRES 68 E 1071 HIS GLU ARG SER LYS GLY THR ILE GLY TYR ILE HIS ILE
SEQRES 69 E 1071 PRO ASP MET GLY MET MET GLY LEU ASN GLU PHE TYR ARG
SEQRES 70 E 1071 LEU PHE ILE ASN GLU SER SER TYR GLN GLY LEU ILE VAL
SEQRES 71 E 1071 ASP VAL ARG PHE ASN GLY GLY GLY PHE VAL SER GLN LEU
SEQRES 72 E 1071 ILE ILE GLU LYS LEU MET ASN LYS ARG ILE GLY TYR ASP
SEQRES 73 E 1071 ASN PRO ARG ARG GLY THR LEU SER PRO TYR PRO THR ASN
SEQRES 74 E 1071 SER VAL ARG GLY LYS ILE ILE ALA ILE THR ASN GLU TYR
SEQRES 75 E 1071 ALA GLY SER ASP GLY ASP ILE PHE SER PHE SER PHE LYS
SEQRES 76 E 1071 LYS LEU GLY LEU GLY LYS LEU ILE GLY THR ARG THR TRP
SEQRES 77 E 1071 GLY GLY VAL VAL GLY ILE THR PRO LYS ARG ARG LEU ILE
SEQRES 78 E 1071 ASP GLY THR VAL LEU THR GLN PRO GLU PHE ALA PHE TRP
SEQRES 79 E 1071 PHE ARG ASP ALA GLY PHE GLY VAL GLU ASN TYR GLY VAL
SEQRES 80 E 1071 ASP PRO ASP VAL GLU ILE GLU TYR ALA PRO HIS ASP TYR
SEQRES 81 E 1071 LEU SER GLY LYS ASP PRO GLN ILE ASP TYR ALA ILE ASP
SEQRES 82 E 1071 ALA LEU ILE GLU GLU LEU ARG ASN TRP ASN GLU GLU LEU
SEQRES 83 E 1071 PRO GLN ARG PRO SER
SEQRES 1 F 14 ASP GLN THR GLN LYS ALA ALA ALA GLU LEU THR PHE PHE
SEQRES 2 F 14 0QE
SEQRES 1 G 1071 MET PRO SER LEU MET SER PHE GLY SER CYS GLN TRP ILE
SEQRES 2 G 1071 ASP GLN GLY ARG PHE SER ARG SER LEU TYR ARG ASN PHE
SEQRES 3 G 1071 LYS THR PHE LYS LEU HIS GLU MET HIS GLY LEU CYS MET
SEQRES 4 G 1071 PRO ASN LEU LEU LEU ASN PRO ASP ILE HIS GLY ASP ARG
SEQRES 5 G 1071 ILE ILE PHE VAL CYS CYS ASP ASP LEU TRP GLU HIS ASP
SEQRES 6 G 1071 LEU LYS SER GLY SER THR ARG LYS ILE VAL SER ASN LEU
SEQRES 7 G 1071 GLY VAL ILE ASN ASN ALA ARG PHE PHE PRO ASP GLY ARG
SEQRES 8 G 1071 LYS ILE ALA ILE ARG VAL MET ARG GLY SER SER LEU ASN
SEQRES 9 G 1071 THR ALA ASP LEU TYR PHE TYR ASN GLY GLU ASN GLY GLU
SEQRES 10 G 1071 ILE LYS ARG ILE THR TYR PHE SER GLY LYS SER THR GLY
SEQRES 11 G 1071 ARG ARG MET PHE THR ASP VAL ALA GLY PHE ASP PRO ASP
SEQRES 12 G 1071 GLY ASN LEU ILE ILE SER THR ASP ALA MET GLN PRO PHE
SEQRES 13 G 1071 SER SER MET THR CYS LEU TYR ARG VAL GLU ASN ASP GLY
SEQRES 14 G 1071 ILE ASN PHE VAL PRO LEU ASN LEU GLY PRO ALA THR HIS
SEQRES 15 G 1071 ILE LEU PHE ALA ASP GLY ARG ARG VAL ILE GLY ARG ASN
SEQRES 16 G 1071 THR PHE GLU LEU PRO HIS TRP LYS GLY TYR ARG GLY GLY
SEQRES 17 G 1071 THR ARG GLY LYS ILE TRP ILE GLU VAL ASN SER GLY ALA
SEQRES 18 G 1071 PHE LYS LYS ILE VAL ASP MET SER THR HIS VAL SER SER
SEQRES 19 G 1071 PRO VAL ILE VAL GLY HIS ARG ILE TYR PHE ILE THR ASP
SEQRES 20 G 1071 ILE ASP GLY PHE GLY GLN ILE TYR SER THR ASP LEU ASP
SEQRES 21 G 1071 GLY LYS ASP LEU ARG LYS HIS THR SER PHE THR ASP TYR
SEQRES 22 G 1071 TYR PRO ARG HIS LEU ASN THR ASP GLY ARG ARG ILE LEU
SEQRES 23 G 1071 PHE SER LYS GLY GLY SER ILE TYR ILE PHE ASN PRO ASP
SEQRES 24 G 1071 THR GLU LYS ILE GLU LYS ILE GLU ILE GLY ASP LEU GLU
SEQRES 25 G 1071 SER PRO GLU ASP ARG ILE ILE SER ILE PRO SER LYS PHE
SEQRES 26 G 1071 ALA GLU ASP PHE SER PRO LEU ASP GLY ASP LEU ILE ALA
SEQRES 27 G 1071 PHE VAL SER ARG GLY GLN ALA PHE ILE GLN ASP VAL SER
SEQRES 28 G 1071 GLY THR TYR VAL LEU LYS VAL PRO GLU PRO LEU ARG ILE
SEQRES 29 G 1071 ARG TYR VAL ARG ARG GLY GLY ASP THR LYS VAL ALA PHE
SEQRES 30 G 1071 ILE HIS GLY THR ARG GLU GLY ASP PHE LEU GLY ILE TYR
SEQRES 31 G 1071 ASP TYR ARG THR GLY LYS ALA GLU LYS PHE GLU GLU ASN
SEQRES 32 G 1071 LEU GLY ASN VAL PHE ALA MET GLY VAL ASP ARG ASN GLY
SEQRES 33 G 1071 LYS PHE ALA VAL VAL ALA ASN ASP ARG PHE GLU ILE MET
SEQRES 34 G 1071 THR VAL ASP LEU GLU THR GLY LYS PRO THR VAL ILE GLU
SEQRES 35 G 1071 ARG SER ARG GLU ALA MET ILE THR ASP PHE THR ILE SER
SEQRES 36 G 1071 ASP ASN SER ARG PHE ILE ALA TYR GLY PHE PRO LEU LYS
SEQRES 37 G 1071 HIS GLY GLU THR ASP GLY TYR VAL MET GLN ALA ILE HIS
SEQRES 38 G 1071 VAL TYR ASP MET GLU GLY ARG LYS ILE PHE ALA ALA THR
SEQRES 39 G 1071 THR GLU ASN SER HIS ASP TYR ALA PRO ALA PHE ASP ALA
SEQRES 40 G 1071 ASP SER LYS ASN LEU TYR TYR LEU SER TYR ARG SER LEU
SEQRES 41 G 1071 ASP PRO SER PRO ASP ARG VAL VAL LEU ASN PHE SER PHE
SEQRES 42 G 1071 GLU VAL VAL SER LYS PRO PHE VAL ILE PRO LEU ILE PRO
SEQRES 43 G 1071 GLY SER PRO ASN PRO THR LYS LEU VAL PRO ARG SER MET
SEQRES 44 G 1071 THR SER GLU ALA GLY GLU TYR ASP LEU ASN ASP MET TYR
SEQRES 45 G 1071 LYS ARG SER SER PRO ILE ASN VAL ASP PRO GLY ASP TYR
SEQRES 46 G 1071 ARG MET ILE ILE PRO LEU GLU SER SER ILE LEU ILE TYR
SEQRES 47 G 1071 SER VAL PRO VAL HIS GLY GLU PHE ALA ALA TYR TYR GLN
SEQRES 48 G 1071 GLY ALA PRO GLU LYS GLY VAL LEU LEU LYS TYR ASP VAL
SEQRES 49 G 1071 LYS THR ARG LYS VAL THR GLU VAL LYS ASN ASN LEU THR
SEQRES 50 G 1071 ASP LEU ARG LEU SER ALA ASP ARG LYS THR VAL MET VAL
SEQRES 51 G 1071 ARG LYS ASP ASP GLY LYS ILE TYR THR PHE PRO LEU GLU
SEQRES 52 G 1071 LYS PRO GLU ASP GLU ARG THR VAL GLU THR ASP LYS ARG
SEQRES 53 G 1071 PRO LEU VAL SER SER ILE HIS GLU GLU PHE LEU GLN MET
SEQRES 54 G 1071 TYR ASP GLU ALA TRP LYS LEU ALA ARG ASP ASN TYR TRP
SEQRES 55 G 1071 ASN GLU ALA VAL ALA LYS GLU ILE SER GLU ARG ILE TYR
SEQRES 56 G 1071 GLU LYS TYR ARG ASN LEU VAL PRO LEU CYS LYS THR ARG
SEQRES 57 G 1071 TYR ASP LEU SER ASN VAL ILE VAL GLU MET GLN GLY GLU
SEQRES 58 G 1071 TYR ARG THR SER HIS SER TYR GLU MET GLY GLY THR PHE
SEQRES 59 G 1071 THR ASP LYS ASP PRO PHE ARG SER GLY ARG ILE ALA CYS
SEQRES 60 G 1071 ASP PHE LYS LEU ASP GLY ASP HIS TYR VAL VAL ALA LYS
SEQRES 61 G 1071 ALA TYR ALA GLY ASP TYR SER ASN GLU GLY GLU LYS SER
SEQRES 62 G 1071 PRO ILE PHE GLU TYR GLY ILE ASP PRO THR GLY TYR LEU
SEQRES 63 G 1071 ILE GLU ASP ILE ASP GLY GLU THR VAL GLY ALA GLY SER
SEQRES 64 G 1071 ASN ILE TYR ARG VAL LEU SER GLU LYS ALA GLY THR SER
SEQRES 65 G 1071 ALA ARG ILE ARG LEU SER GLY LYS GLY GLY ASP LYS ARG
SEQRES 66 G 1071 ASP LEU MET ILE ASP ILE LEU ASP ASP ASP ARG PHE ILE
SEQRES 67 G 1071 ARG TYR ARG SER TRP VAL GLU ALA ASN ARG ARG TYR VAL
SEQRES 68 G 1071 HIS GLU ARG SER LYS GLY THR ILE GLY TYR ILE HIS ILE
SEQRES 69 G 1071 PRO ASP MET GLY MET MET GLY LEU ASN GLU PHE TYR ARG
SEQRES 70 G 1071 LEU PHE ILE ASN GLU SER SER TYR GLN GLY LEU ILE VAL
SEQRES 71 G 1071 ASP VAL ARG PHE ASN GLY GLY GLY PHE VAL SER GLN LEU
SEQRES 72 G 1071 ILE ILE GLU LYS LEU MET ASN LYS ARG ILE GLY TYR ASP
SEQRES 73 G 1071 ASN PRO ARG ARG GLY THR LEU SER PRO TYR PRO THR ASN
SEQRES 74 G 1071 SER VAL ARG GLY LYS ILE ILE ALA ILE THR ASN GLU TYR
SEQRES 75 G 1071 ALA GLY SER ASP GLY ASP ILE PHE SER PHE SER PHE LYS
SEQRES 76 G 1071 LYS LEU GLY LEU GLY LYS LEU ILE GLY THR ARG THR TRP
SEQRES 77 G 1071 GLY GLY VAL VAL GLY ILE THR PRO LYS ARG ARG LEU ILE
SEQRES 78 G 1071 ASP GLY THR VAL LEU THR GLN PRO GLU PHE ALA PHE TRP
SEQRES 79 G 1071 PHE ARG ASP ALA GLY PHE GLY VAL GLU ASN TYR GLY VAL
SEQRES 80 G 1071 ASP PRO ASP VAL GLU ILE GLU TYR ALA PRO HIS ASP TYR
SEQRES 81 G 1071 LEU SER GLY LYS ASP PRO GLN ILE ASP TYR ALA ILE ASP
SEQRES 82 G 1071 ALA LEU ILE GLU GLU LEU ARG ASN TRP ASN GLU GLU LEU
SEQRES 83 G 1071 PRO GLN ARG PRO SER
SEQRES 1 H 14 ASP GLN THR GLN LYS ALA ALA ALA GLU LEU THR PHE PHE
SEQRES 2 H 14 0QE
SEQRES 1 I 1071 MET PRO SER LEU MET SER PHE GLY SER CYS GLN TRP ILE
SEQRES 2 I 1071 ASP GLN GLY ARG PHE SER ARG SER LEU TYR ARG ASN PHE
SEQRES 3 I 1071 LYS THR PHE LYS LEU HIS GLU MET HIS GLY LEU CYS MET
SEQRES 4 I 1071 PRO ASN LEU LEU LEU ASN PRO ASP ILE HIS GLY ASP ARG
SEQRES 5 I 1071 ILE ILE PHE VAL CYS CYS ASP ASP LEU TRP GLU HIS ASP
SEQRES 6 I 1071 LEU LYS SER GLY SER THR ARG LYS ILE VAL SER ASN LEU
SEQRES 7 I 1071 GLY VAL ILE ASN ASN ALA ARG PHE PHE PRO ASP GLY ARG
SEQRES 8 I 1071 LYS ILE ALA ILE ARG VAL MET ARG GLY SER SER LEU ASN
SEQRES 9 I 1071 THR ALA ASP LEU TYR PHE TYR ASN GLY GLU ASN GLY GLU
SEQRES 10 I 1071 ILE LYS ARG ILE THR TYR PHE SER GLY LYS SER THR GLY
SEQRES 11 I 1071 ARG ARG MET PHE THR ASP VAL ALA GLY PHE ASP PRO ASP
SEQRES 12 I 1071 GLY ASN LEU ILE ILE SER THR ASP ALA MET GLN PRO PHE
SEQRES 13 I 1071 SER SER MET THR CYS LEU TYR ARG VAL GLU ASN ASP GLY
SEQRES 14 I 1071 ILE ASN PHE VAL PRO LEU ASN LEU GLY PRO ALA THR HIS
SEQRES 15 I 1071 ILE LEU PHE ALA ASP GLY ARG ARG VAL ILE GLY ARG ASN
SEQRES 16 I 1071 THR PHE GLU LEU PRO HIS TRP LYS GLY TYR ARG GLY GLY
SEQRES 17 I 1071 THR ARG GLY LYS ILE TRP ILE GLU VAL ASN SER GLY ALA
SEQRES 18 I 1071 PHE LYS LYS ILE VAL ASP MET SER THR HIS VAL SER SER
SEQRES 19 I 1071 PRO VAL ILE VAL GLY HIS ARG ILE TYR PHE ILE THR ASP
SEQRES 20 I 1071 ILE ASP GLY PHE GLY GLN ILE TYR SER THR ASP LEU ASP
SEQRES 21 I 1071 GLY LYS ASP LEU ARG LYS HIS THR SER PHE THR ASP TYR
SEQRES 22 I 1071 TYR PRO ARG HIS LEU ASN THR ASP GLY ARG ARG ILE LEU
SEQRES 23 I 1071 PHE SER LYS GLY GLY SER ILE TYR ILE PHE ASN PRO ASP
SEQRES 24 I 1071 THR GLU LYS ILE GLU LYS ILE GLU ILE GLY ASP LEU GLU
SEQRES 25 I 1071 SER PRO GLU ASP ARG ILE ILE SER ILE PRO SER LYS PHE
SEQRES 26 I 1071 ALA GLU ASP PHE SER PRO LEU ASP GLY ASP LEU ILE ALA
SEQRES 27 I 1071 PHE VAL SER ARG GLY GLN ALA PHE ILE GLN ASP VAL SER
SEQRES 28 I 1071 GLY THR TYR VAL LEU LYS VAL PRO GLU PRO LEU ARG ILE
SEQRES 29 I 1071 ARG TYR VAL ARG ARG GLY GLY ASP THR LYS VAL ALA PHE
SEQRES 30 I 1071 ILE HIS GLY THR ARG GLU GLY ASP PHE LEU GLY ILE TYR
SEQRES 31 I 1071 ASP TYR ARG THR GLY LYS ALA GLU LYS PHE GLU GLU ASN
SEQRES 32 I 1071 LEU GLY ASN VAL PHE ALA MET GLY VAL ASP ARG ASN GLY
SEQRES 33 I 1071 LYS PHE ALA VAL VAL ALA ASN ASP ARG PHE GLU ILE MET
SEQRES 34 I 1071 THR VAL ASP LEU GLU THR GLY LYS PRO THR VAL ILE GLU
SEQRES 35 I 1071 ARG SER ARG GLU ALA MET ILE THR ASP PHE THR ILE SER
SEQRES 36 I 1071 ASP ASN SER ARG PHE ILE ALA TYR GLY PHE PRO LEU LYS
SEQRES 37 I 1071 HIS GLY GLU THR ASP GLY TYR VAL MET GLN ALA ILE HIS
SEQRES 38 I 1071 VAL TYR ASP MET GLU GLY ARG LYS ILE PHE ALA ALA THR
SEQRES 39 I 1071 THR GLU ASN SER HIS ASP TYR ALA PRO ALA PHE ASP ALA
SEQRES 40 I 1071 ASP SER LYS ASN LEU TYR TYR LEU SER TYR ARG SER LEU
SEQRES 41 I 1071 ASP PRO SER PRO ASP ARG VAL VAL LEU ASN PHE SER PHE
SEQRES 42 I 1071 GLU VAL VAL SER LYS PRO PHE VAL ILE PRO LEU ILE PRO
SEQRES 43 I 1071 GLY SER PRO ASN PRO THR LYS LEU VAL PRO ARG SER MET
SEQRES 44 I 1071 THR SER GLU ALA GLY GLU TYR ASP LEU ASN ASP MET TYR
SEQRES 45 I 1071 LYS ARG SER SER PRO ILE ASN VAL ASP PRO GLY ASP TYR
SEQRES 46 I 1071 ARG MET ILE ILE PRO LEU GLU SER SER ILE LEU ILE TYR
SEQRES 47 I 1071 SER VAL PRO VAL HIS GLY GLU PHE ALA ALA TYR TYR GLN
SEQRES 48 I 1071 GLY ALA PRO GLU LYS GLY VAL LEU LEU LYS TYR ASP VAL
SEQRES 49 I 1071 LYS THR ARG LYS VAL THR GLU VAL LYS ASN ASN LEU THR
SEQRES 50 I 1071 ASP LEU ARG LEU SER ALA ASP ARG LYS THR VAL MET VAL
SEQRES 51 I 1071 ARG LYS ASP ASP GLY LYS ILE TYR THR PHE PRO LEU GLU
SEQRES 52 I 1071 LYS PRO GLU ASP GLU ARG THR VAL GLU THR ASP LYS ARG
SEQRES 53 I 1071 PRO LEU VAL SER SER ILE HIS GLU GLU PHE LEU GLN MET
SEQRES 54 I 1071 TYR ASP GLU ALA TRP LYS LEU ALA ARG ASP ASN TYR TRP
SEQRES 55 I 1071 ASN GLU ALA VAL ALA LYS GLU ILE SER GLU ARG ILE TYR
SEQRES 56 I 1071 GLU LYS TYR ARG ASN LEU VAL PRO LEU CYS LYS THR ARG
SEQRES 57 I 1071 TYR ASP LEU SER ASN VAL ILE VAL GLU MET GLN GLY GLU
SEQRES 58 I 1071 TYR ARG THR SER HIS SER TYR GLU MET GLY GLY THR PHE
SEQRES 59 I 1071 THR ASP LYS ASP PRO PHE ARG SER GLY ARG ILE ALA CYS
SEQRES 60 I 1071 ASP PHE LYS LEU ASP GLY ASP HIS TYR VAL VAL ALA LYS
SEQRES 61 I 1071 ALA TYR ALA GLY ASP TYR SER ASN GLU GLY GLU LYS SER
SEQRES 62 I 1071 PRO ILE PHE GLU TYR GLY ILE ASP PRO THR GLY TYR LEU
SEQRES 63 I 1071 ILE GLU ASP ILE ASP GLY GLU THR VAL GLY ALA GLY SER
SEQRES 64 I 1071 ASN ILE TYR ARG VAL LEU SER GLU LYS ALA GLY THR SER
SEQRES 65 I 1071 ALA ARG ILE ARG LEU SER GLY LYS GLY GLY ASP LYS ARG
SEQRES 66 I 1071 ASP LEU MET ILE ASP ILE LEU ASP ASP ASP ARG PHE ILE
SEQRES 67 I 1071 ARG TYR ARG SER TRP VAL GLU ALA ASN ARG ARG TYR VAL
SEQRES 68 I 1071 HIS GLU ARG SER LYS GLY THR ILE GLY TYR ILE HIS ILE
SEQRES 69 I 1071 PRO ASP MET GLY MET MET GLY LEU ASN GLU PHE TYR ARG
SEQRES 70 I 1071 LEU PHE ILE ASN GLU SER SER TYR GLN GLY LEU ILE VAL
SEQRES 71 I 1071 ASP VAL ARG PHE ASN GLY GLY GLY PHE VAL SER GLN LEU
SEQRES 72 I 1071 ILE ILE GLU LYS LEU MET ASN LYS ARG ILE GLY TYR ASP
SEQRES 73 I 1071 ASN PRO ARG ARG GLY THR LEU SER PRO TYR PRO THR ASN
SEQRES 74 I 1071 SER VAL ARG GLY LYS ILE ILE ALA ILE THR ASN GLU TYR
SEQRES 75 I 1071 ALA GLY SER ASP GLY ASP ILE PHE SER PHE SER PHE LYS
SEQRES 76 I 1071 LYS LEU GLY LEU GLY LYS LEU ILE GLY THR ARG THR TRP
SEQRES 77 I 1071 GLY GLY VAL VAL GLY ILE THR PRO LYS ARG ARG LEU ILE
SEQRES 78 I 1071 ASP GLY THR VAL LEU THR GLN PRO GLU PHE ALA PHE TRP
SEQRES 79 I 1071 PHE ARG ASP ALA GLY PHE GLY VAL GLU ASN TYR GLY VAL
SEQRES 80 I 1071 ASP PRO ASP VAL GLU ILE GLU TYR ALA PRO HIS ASP TYR
SEQRES 81 I 1071 LEU SER GLY LYS ASP PRO GLN ILE ASP TYR ALA ILE ASP
SEQRES 82 I 1071 ALA LEU ILE GLU GLU LEU ARG ASN TRP ASN GLU GLU LEU
SEQRES 83 I 1071 PRO GLN ARG PRO SER
SEQRES 1 J 14 ASP GLN THR GLN LYS ALA ALA ALA GLU LEU THR PHE PHE
SEQRES 2 J 14 0QE
SEQRES 1 K 1071 MET PRO SER LEU MET SER PHE GLY SER CYS GLN TRP ILE
SEQRES 2 K 1071 ASP GLN GLY ARG PHE SER ARG SER LEU TYR ARG ASN PHE
SEQRES 3 K 1071 LYS THR PHE LYS LEU HIS GLU MET HIS GLY LEU CYS MET
SEQRES 4 K 1071 PRO ASN LEU LEU LEU ASN PRO ASP ILE HIS GLY ASP ARG
SEQRES 5 K 1071 ILE ILE PHE VAL CYS CYS ASP ASP LEU TRP GLU HIS ASP
SEQRES 6 K 1071 LEU LYS SER GLY SER THR ARG LYS ILE VAL SER ASN LEU
SEQRES 7 K 1071 GLY VAL ILE ASN ASN ALA ARG PHE PHE PRO ASP GLY ARG
SEQRES 8 K 1071 LYS ILE ALA ILE ARG VAL MET ARG GLY SER SER LEU ASN
SEQRES 9 K 1071 THR ALA ASP LEU TYR PHE TYR ASN GLY GLU ASN GLY GLU
SEQRES 10 K 1071 ILE LYS ARG ILE THR TYR PHE SER GLY LYS SER THR GLY
SEQRES 11 K 1071 ARG ARG MET PHE THR ASP VAL ALA GLY PHE ASP PRO ASP
SEQRES 12 K 1071 GLY ASN LEU ILE ILE SER THR ASP ALA MET GLN PRO PHE
SEQRES 13 K 1071 SER SER MET THR CYS LEU TYR ARG VAL GLU ASN ASP GLY
SEQRES 14 K 1071 ILE ASN PHE VAL PRO LEU ASN LEU GLY PRO ALA THR HIS
SEQRES 15 K 1071 ILE LEU PHE ALA ASP GLY ARG ARG VAL ILE GLY ARG ASN
SEQRES 16 K 1071 THR PHE GLU LEU PRO HIS TRP LYS GLY TYR ARG GLY GLY
SEQRES 17 K 1071 THR ARG GLY LYS ILE TRP ILE GLU VAL ASN SER GLY ALA
SEQRES 18 K 1071 PHE LYS LYS ILE VAL ASP MET SER THR HIS VAL SER SER
SEQRES 19 K 1071 PRO VAL ILE VAL GLY HIS ARG ILE TYR PHE ILE THR ASP
SEQRES 20 K 1071 ILE ASP GLY PHE GLY GLN ILE TYR SER THR ASP LEU ASP
SEQRES 21 K 1071 GLY LYS ASP LEU ARG LYS HIS THR SER PHE THR ASP TYR
SEQRES 22 K 1071 TYR PRO ARG HIS LEU ASN THR ASP GLY ARG ARG ILE LEU
SEQRES 23 K 1071 PHE SER LYS GLY GLY SER ILE TYR ILE PHE ASN PRO ASP
SEQRES 24 K 1071 THR GLU LYS ILE GLU LYS ILE GLU ILE GLY ASP LEU GLU
SEQRES 25 K 1071 SER PRO GLU ASP ARG ILE ILE SER ILE PRO SER LYS PHE
SEQRES 26 K 1071 ALA GLU ASP PHE SER PRO LEU ASP GLY ASP LEU ILE ALA
SEQRES 27 K 1071 PHE VAL SER ARG GLY GLN ALA PHE ILE GLN ASP VAL SER
SEQRES 28 K 1071 GLY THR TYR VAL LEU LYS VAL PRO GLU PRO LEU ARG ILE
SEQRES 29 K 1071 ARG TYR VAL ARG ARG GLY GLY ASP THR LYS VAL ALA PHE
SEQRES 30 K 1071 ILE HIS GLY THR ARG GLU GLY ASP PHE LEU GLY ILE TYR
SEQRES 31 K 1071 ASP TYR ARG THR GLY LYS ALA GLU LYS PHE GLU GLU ASN
SEQRES 32 K 1071 LEU GLY ASN VAL PHE ALA MET GLY VAL ASP ARG ASN GLY
SEQRES 33 K 1071 LYS PHE ALA VAL VAL ALA ASN ASP ARG PHE GLU ILE MET
SEQRES 34 K 1071 THR VAL ASP LEU GLU THR GLY LYS PRO THR VAL ILE GLU
SEQRES 35 K 1071 ARG SER ARG GLU ALA MET ILE THR ASP PHE THR ILE SER
SEQRES 36 K 1071 ASP ASN SER ARG PHE ILE ALA TYR GLY PHE PRO LEU LYS
SEQRES 37 K 1071 HIS GLY GLU THR ASP GLY TYR VAL MET GLN ALA ILE HIS
SEQRES 38 K 1071 VAL TYR ASP MET GLU GLY ARG LYS ILE PHE ALA ALA THR
SEQRES 39 K 1071 THR GLU ASN SER HIS ASP TYR ALA PRO ALA PHE ASP ALA
SEQRES 40 K 1071 ASP SER LYS ASN LEU TYR TYR LEU SER TYR ARG SER LEU
SEQRES 41 K 1071 ASP PRO SER PRO ASP ARG VAL VAL LEU ASN PHE SER PHE
SEQRES 42 K 1071 GLU VAL VAL SER LYS PRO PHE VAL ILE PRO LEU ILE PRO
SEQRES 43 K 1071 GLY SER PRO ASN PRO THR LYS LEU VAL PRO ARG SER MET
SEQRES 44 K 1071 THR SER GLU ALA GLY GLU TYR ASP LEU ASN ASP MET TYR
SEQRES 45 K 1071 LYS ARG SER SER PRO ILE ASN VAL ASP PRO GLY ASP TYR
SEQRES 46 K 1071 ARG MET ILE ILE PRO LEU GLU SER SER ILE LEU ILE TYR
SEQRES 47 K 1071 SER VAL PRO VAL HIS GLY GLU PHE ALA ALA TYR TYR GLN
SEQRES 48 K 1071 GLY ALA PRO GLU LYS GLY VAL LEU LEU LYS TYR ASP VAL
SEQRES 49 K 1071 LYS THR ARG LYS VAL THR GLU VAL LYS ASN ASN LEU THR
SEQRES 50 K 1071 ASP LEU ARG LEU SER ALA ASP ARG LYS THR VAL MET VAL
SEQRES 51 K 1071 ARG LYS ASP ASP GLY LYS ILE TYR THR PHE PRO LEU GLU
SEQRES 52 K 1071 LYS PRO GLU ASP GLU ARG THR VAL GLU THR ASP LYS ARG
SEQRES 53 K 1071 PRO LEU VAL SER SER ILE HIS GLU GLU PHE LEU GLN MET
SEQRES 54 K 1071 TYR ASP GLU ALA TRP LYS LEU ALA ARG ASP ASN TYR TRP
SEQRES 55 K 1071 ASN GLU ALA VAL ALA LYS GLU ILE SER GLU ARG ILE TYR
SEQRES 56 K 1071 GLU LYS TYR ARG ASN LEU VAL PRO LEU CYS LYS THR ARG
SEQRES 57 K 1071 TYR ASP LEU SER ASN VAL ILE VAL GLU MET GLN GLY GLU
SEQRES 58 K 1071 TYR ARG THR SER HIS SER TYR GLU MET GLY GLY THR PHE
SEQRES 59 K 1071 THR ASP LYS ASP PRO PHE ARG SER GLY ARG ILE ALA CYS
SEQRES 60 K 1071 ASP PHE LYS LEU ASP GLY ASP HIS TYR VAL VAL ALA LYS
SEQRES 61 K 1071 ALA TYR ALA GLY ASP TYR SER ASN GLU GLY GLU LYS SER
SEQRES 62 K 1071 PRO ILE PHE GLU TYR GLY ILE ASP PRO THR GLY TYR LEU
SEQRES 63 K 1071 ILE GLU ASP ILE ASP GLY GLU THR VAL GLY ALA GLY SER
SEQRES 64 K 1071 ASN ILE TYR ARG VAL LEU SER GLU LYS ALA GLY THR SER
SEQRES 65 K 1071 ALA ARG ILE ARG LEU SER GLY LYS GLY GLY ASP LYS ARG
SEQRES 66 K 1071 ASP LEU MET ILE ASP ILE LEU ASP ASP ASP ARG PHE ILE
SEQRES 67 K 1071 ARG TYR ARG SER TRP VAL GLU ALA ASN ARG ARG TYR VAL
SEQRES 68 K 1071 HIS GLU ARG SER LYS GLY THR ILE GLY TYR ILE HIS ILE
SEQRES 69 K 1071 PRO ASP MET GLY MET MET GLY LEU ASN GLU PHE TYR ARG
SEQRES 70 K 1071 LEU PHE ILE ASN GLU SER SER TYR GLN GLY LEU ILE VAL
SEQRES 71 K 1071 ASP VAL ARG PHE ASN GLY GLY GLY PHE VAL SER GLN LEU
SEQRES 72 K 1071 ILE ILE GLU LYS LEU MET ASN LYS ARG ILE GLY TYR ASP
SEQRES 73 K 1071 ASN PRO ARG ARG GLY THR LEU SER PRO TYR PRO THR ASN
SEQRES 74 K 1071 SER VAL ARG GLY LYS ILE ILE ALA ILE THR ASN GLU TYR
SEQRES 75 K 1071 ALA GLY SER ASP GLY ASP ILE PHE SER PHE SER PHE LYS
SEQRES 76 K 1071 LYS LEU GLY LEU GLY LYS LEU ILE GLY THR ARG THR TRP
SEQRES 77 K 1071 GLY GLY VAL VAL GLY ILE THR PRO LYS ARG ARG LEU ILE
SEQRES 78 K 1071 ASP GLY THR VAL LEU THR GLN PRO GLU PHE ALA PHE TRP
SEQRES 79 K 1071 PHE ARG ASP ALA GLY PHE GLY VAL GLU ASN TYR GLY VAL
SEQRES 80 K 1071 ASP PRO ASP VAL GLU ILE GLU TYR ALA PRO HIS ASP TYR
SEQRES 81 K 1071 LEU SER GLY LYS ASP PRO GLN ILE ASP TYR ALA ILE ASP
SEQRES 82 K 1071 ALA LEU ILE GLU GLU LEU ARG ASN TRP ASN GLU GLU LEU
SEQRES 83 K 1071 PRO GLN ARG PRO SER
SEQRES 1 L 14 ASP GLN THR GLN LYS ALA ALA ALA GLU LEU THR PHE PHE
SEQRES 2 L 14 0QE
HET 0QE B1214 1
HET 0QE D1214 1
HET 0QE F1214 1
HET 0QE H1214 1
HET 0QE J1214 1
HET 0QE L1214 1
HETNAM 0QE CHLOROMETHANE
HETSYN 0QE CHLORO METHYL GROUP
FORMUL 2 0QE 6(C H3 CL)
FORMUL 13 HOH *960(H2 O)
HELIX 1 1 ILE A 321 LYS A 324 5 4
HELIX 2 2 ASN A 550 LEU A 554 5 5
HELIX 3 3 PRO A 556 THR A 560 5 5
HELIX 4 4 ASP A 570 ARG A 574 5 5
HELIX 5 5 GLU A 605 GLN A 611 1 7
HELIX 6 6 ILE A 682 TYR A 701 1 20
HELIX 7 7 ASN A 703 ASN A 720 1 18
HELIX 8 8 LEU A 721 CYS A 725 5 5
HELIX 9 9 THR A 727 GLU A 741 1 15
HELIX 10 10 SER A 793 GLY A 799 5 7
HELIX 11 11 ASN A 820 GLU A 827 1 8
HELIX 12 12 ASP A 855 SER A 875 1 21
HELIX 13 13 GLY A 888 SER A 903 1 16
HELIX 14 14 VAL A 920 ASN A 930 1 11
HELIX 15 15 SER A 965 LEU A 977 1 13
HELIX 16 16 ALA A 1036 SER A 1042 1 7
HELIX 17 17 ASP A 1045 LEU A 1059 1 15
HELIX 18 18 ILE C 321 LYS C 324 5 4
HELIX 19 19 ASN C 550 LEU C 554 5 5
HELIX 20 20 PRO C 556 THR C 560 5 5
HELIX 21 21 ASP C 570 ARG C 574 5 5
HELIX 22 22 GLU C 605 GLN C 611 1 7
HELIX 23 23 ILE C 682 TYR C 701 1 20
HELIX 24 24 ASN C 703 ASN C 720 1 18
HELIX 25 25 LEU C 721 CYS C 725 5 5
HELIX 26 26 THR C 727 GLU C 741 1 15
HELIX 27 27 SER C 793 GLY C 799 5 7
HELIX 28 28 ASN C 820 GLU C 827 1 8
HELIX 29 29 ASP C 855 SER C 875 1 21
HELIX 30 30 GLY C 888 SER C 903 1 16
HELIX 31 31 VAL C 920 ASN C 930 1 11
HELIX 32 32 SER C 965 LEU C 977 1 13
HELIX 33 33 ALA C 1036 SER C 1042 1 7
HELIX 34 34 ASP C 1045 LEU C 1059 1 15
HELIX 35 35 ILE E 321 LYS E 324 5 4
HELIX 36 36 ASN E 550 LEU E 554 5 5
HELIX 37 37 PRO E 556 THR E 560 5 5
HELIX 38 38 ASP E 570 ARG E 574 5 5
HELIX 39 39 GLU E 605 GLN E 611 1 7
HELIX 40 40 ILE E 682 TYR E 701 1 20
HELIX 41 41 ASN E 703 ASN E 720 1 18
HELIX 42 42 LEU E 721 CYS E 725 5 5
HELIX 43 43 THR E 727 GLU E 741 1 15
HELIX 44 44 SER E 793 GLY E 799 5 7
HELIX 45 45 ASN E 820 GLU E 827 1 8
HELIX 46 46 ASP E 855 SER E 875 1 21
HELIX 47 47 GLY E 888 SER E 903 1 16
HELIX 48 48 VAL E 920 ASN E 930 1 11
HELIX 49 49 SER E 965 LEU E 977 1 13
HELIX 50 50 ALA E 1036 SER E 1042 1 7
HELIX 51 51 ASP E 1045 LEU E 1059 1 15
HELIX 52 52 ILE G 321 LYS G 324 5 4
HELIX 53 53 ASN G 550 LEU G 554 5 5
HELIX 54 54 PRO G 556 THR G 560 5 5
HELIX 55 55 ASP G 570 ARG G 574 5 5
HELIX 56 56 GLU G 605 GLN G 611 1 7
HELIX 57 57 ILE G 682 TYR G 701 1 20
HELIX 58 58 ASN G 703 ASN G 720 1 18
HELIX 59 59 LEU G 721 CYS G 725 5 5
HELIX 60 60 THR G 727 GLU G 741 1 15
HELIX 61 61 SER G 793 GLY G 799 5 7
HELIX 62 62 ASN G 820 GLU G 827 1 8
HELIX 63 63 ASP G 855 SER G 875 1 21
HELIX 64 64 GLY G 888 SER G 903 1 16
HELIX 65 65 VAL G 920 ASN G 930 1 11
HELIX 66 66 SER G 965 LEU G 977 1 13
HELIX 67 67 ALA G 1036 SER G 1042 1 7
HELIX 68 68 ASP G 1045 LEU G 1059 1 15
HELIX 69 69 ILE I 321 LYS I 324 5 4
HELIX 70 70 ASN I 550 LEU I 554 5 5
HELIX 71 71 PRO I 556 THR I 560 5 5
HELIX 72 72 ASP I 570 ARG I 574 5 5
HELIX 73 73 GLU I 605 GLN I 611 1 7
HELIX 74 74 ILE I 682 TYR I 701 1 20
HELIX 75 75 ASN I 703 ASN I 720 1 18
HELIX 76 76 LEU I 721 CYS I 725 5 5
HELIX 77 77 THR I 727 GLU I 741 1 15
HELIX 78 78 SER I 793 GLY I 799 5 7
HELIX 79 79 ASN I 820 GLU I 827 1 8
HELIX 80 80 ASP I 855 SER I 875 1 21
HELIX 81 81 GLY I 888 SER I 903 1 16
HELIX 82 82 VAL I 920 ASN I 930 1 11
HELIX 83 83 SER I 965 LEU I 977 1 13
HELIX 84 84 ALA I 1036 SER I 1042 1 7
HELIX 85 85 ASP I 1045 LEU I 1059 1 15
HELIX 86 86 ILE K 321 LYS K 324 5 4
HELIX 87 87 ASN K 550 LEU K 554 5 5
HELIX 88 88 PRO K 556 THR K 560 5 5
HELIX 89 89 ASP K 570 ARG K 574 5 5
HELIX 90 90 GLU K 605 GLN K 611 1 7
HELIX 91 91 ILE K 682 TYR K 701 1 20
HELIX 92 92 ASN K 703 ASN K 720 1 18
HELIX 93 93 LEU K 721 CYS K 725 5 5
HELIX 94 94 THR K 727 GLU K 741 1 15
HELIX 95 95 SER K 793 GLY K 799 5 7
HELIX 96 96 ASN K 820 GLU K 827 1 8
HELIX 97 97 ASP K 855 SER K 875 1 21
HELIX 98 98 GLY K 888 SER K 903 1 16
HELIX 99 99 VAL K 920 ASN K 930 1 11
HELIX 100 100 SER K 965 LEU K 977 1 13
HELIX 101 101 ALA K 1036 SER K 1042 1 7
HELIX 102 102 ASP K 1045 LEU K 1059 1 15
SHEET 1 A 4 LEU A 44 HIS A 49 0
SHEET 2 A 4 ARG A 52 CYS A 57 -1 O ARG A 52 N HIS A 49
SHEET 3 A 4 ASP A 60 ASP A 65 -1 O ASP A 60 N CYS A 57
SHEET 4 A 4 THR A 71 VAL A 75 -1 O ARG A 72 N GLU A 63
SHEET 1 B 6 VAL A 80 PHE A 86 0
SHEET 2 B 6 LYS A 92 ARG A 99 -1 O ALA A 94 N ARG A 85
SHEET 3 B 6 THR A 105 ASN A 112 -1 N THR A 105 O ARG A 99
SHEET 4 B 6 GLY A 126 LYS A 127 -1 N GLY A 126 O ALA A 106
SHEET 5 B 6 THR A 105 ASN A 112 -1 O ALA A 106 N GLY A 126
SHEET 6 B 6 GLU A 117 ARG A 120 -1 O GLU A 117 N ASN A 112
SHEET 1 C 4 ASP A 136 PHE A 140 0
SHEET 2 C 4 LEU A 146 THR A 150 -1 O ILE A 147 N ALA A 138
SHEET 3 C 4 CYS A 161 GLU A 166 -1 O CYS A 161 N THR A 150
SHEET 4 C 4 ASN A 171 PRO A 179 -1 O ASN A 171 N GLU A 166
SHEET 1 D 4 HIS A 182 ALA A 186 0
SHEET 2 D 4 ARG A 189 ARG A 194 -1 O ARG A 189 N ALA A 186
SHEET 3 D 4 LYS A 212 ASN A 218 -1 O LYS A 212 N ARG A 194
SHEET 4 D 4 ALA A 221 VAL A 226 -1 O ALA A 221 N VAL A 217
SHEET 1 E 4 SER A 233 VAL A 238 0
SHEET 2 E 4 ARG A 241 THR A 246 -1 O ARG A 241 N VAL A 238
SHEET 3 E 4 GLN A 253 ASP A 258 -1 N GLN A 253 O THR A 246
SHEET 4 E 4 ARG A 265 LYS A 266 -1 N ARG A 265 O SER A 256
SHEET 1 F 4 ARG A 276 THR A 280 0
SHEET 2 F 4 ILE A 285 LYS A 289 -1 N LEU A 286 O ASN A 279
SHEET 3 F 4 SER A 292 PHE A 296 -1 N SER A 292 O LYS A 289
SHEET 4 F 4 ILE A 303 LYS A 305 -1 N GLU A 304 O ILE A 295
SHEET 1 G 4 ALA A 326 LEU A 332 0
SHEET 2 G 4 LEU A 336 SER A 341 -1 O LEU A 336 N LEU A 332
SHEET 3 G 4 GLN A 344 ASP A 349 -1 O GLN A 344 N SER A 341
SHEET 4 G 4 VAL A 355 LYS A 357 -1 O LEU A 356 N ILE A 347
SHEET 1 H 4 ILE A 364 ARG A 369 0
SHEET 2 H 4 LYS A 374 GLY A 380 -1 N ALA A 376 O ARG A 368
SHEET 3 H 4 ASP A 385 ASP A 391 -1 O PHE A 386 N HIS A 379
SHEET 4 H 4 LYS A 399 GLY A 405 -1 N PHE A 400 O LEU A 387
SHEET 1 I 4 VAL A 407 VAL A 412 0
SHEET 2 I 4 PHE A 418 ASN A 423 -1 N VAL A 420 O GLY A 411
SHEET 3 I 4 GLU A 427 ASP A 432 -1 O GLU A 427 N ASN A 423
SHEET 4 I 4 PRO A 438 ARG A 443 -1 O THR A 439 N THR A 430
SHEET 1 J 4 PHE A 452 ILE A 454 0
SHEET 2 J 4 PHE A 460 LEU A 467 -1 O ALA A 462 N THR A 453
SHEET 3 J 4 MET A 477 ASP A 484 -1 N MET A 477 O LEU A 467
SHEET 4 J 4 LYS A 489 ALA A 492 -1 O LYS A 489 N ASP A 484
SHEET 1 K 2 ASP A 500 PHE A 505 0
SHEET 2 K 2 LEU A 512 SER A 516 -1 N TYR A 513 O ALA A 504
SHEET 1 L 2 PHE A 540 VAL A 541 0
SHEET 2 L 2 SER A 576 PRO A 577 -1 O SER A 576 N VAL A 541
SHEET 1 M 7 TYR A 585 PRO A 590 0
SHEET 2 M 7 SER A 594 SER A 599 -1 O LEU A 596 N ILE A 589
SHEET 3 M 7 GLY A 617 ASP A 623 -1 O VAL A 618 N SER A 599
SHEET 4 M 7 VAL A 629 LEU A 641 -1 O THR A 630 N LYS A 621
SHEET 5 M 7 THR A 647 LYS A 652 -1 O MET A 649 N ARG A 640
SHEET 6 M 7 ILE A 657 PRO A 661 -1 O TYR A 658 N VAL A 650
SHEET 7 M 7 ARG A 669 THR A 670 -1 N ARG A 669 O THR A 659
SHEET 1 N 2 GLU A 749 MET A 750 0
SHEET 2 N 2 VAL A1005 LEU A1006 -1 N VAL A1005 O MET A 750
SHEET 1 O 7 CYS A 767 ASP A 772 0
SHEET 2 O 7 HIS A 775 ALA A 781 -1 O HIS A 775 N ASP A 772
SHEET 3 O 7 LEU A 806 ILE A 810 -1 N ILE A 807 O TYR A 776
SHEET 4 O 7 GLU A 813 THR A 814 -1 O GLU A 813 N ILE A 810
SHEET 5 O 7 LEU A 806 ILE A 810 -1 N ILE A 810 O GLU A 813
SHEET 6 O 7 SER A 832 SER A 838 -1 N ARG A 836 O ASP A 809
SHEET 7 O 7 LYS A 844 ASP A 850 -1 O ARG A 845 N LEU A 837
SHEET 1 P 5 ILE A 879 HIS A 883 0
SHEET 2 P 5 GLY A 907 ASP A 911 1 O GLY A 907 N GLY A 880
SHEET 3 P 5 LYS A 954 THR A 959 1 O LYS A 954 N LEU A 908
SHEET 4 P 5 GLY A 980 GLY A 984 1 O LYS A 981 N ALA A 957
SHEET 5 P 5 VAL A1031 GLU A1032 1 N VAL A1031 O LEU A 982
SHEET 1 Q 2 GLY A 934 ASP A 936 0
SHEET 2 Q 2 SER A 944 TYR A 946 -1 O SER A 944 N ASP A 936
SHEET 1 R 2 VAL A 992 GLY A 993 0
SHEET 2 R 2 PHE A1011 ALA A1012 -1 N PHE A1011 O GLY A 993
SHEET 1 S 4 LEU C 44 HIS C 49 0
SHEET 2 S 4 ARG C 52 CYS C 57 -1 O ARG C 52 N HIS C 49
SHEET 3 S 4 ASP C 60 ASP C 65 -1 O ASP C 60 N CYS C 57
SHEET 4 S 4 THR C 71 VAL C 75 -1 O ARG C 72 N GLU C 63
SHEET 1 T 6 VAL C 80 PHE C 86 0
SHEET 2 T 6 LYS C 92 ARG C 99 -1 O ALA C 94 N ARG C 85
SHEET 3 T 6 THR C 105 ASN C 112 -1 N THR C 105 O ARG C 99
SHEET 4 T 6 GLY C 126 LYS C 127 -1 N GLY C 126 O ALA C 106
SHEET 5 T 6 THR C 105 ASN C 112 -1 O ALA C 106 N GLY C 126
SHEET 6 T 6 GLU C 117 ARG C 120 -1 O GLU C 117 N ASN C 112
SHEET 1 U 4 ASP C 136 PHE C 140 0
SHEET 2 U 4 LEU C 146 THR C 150 -1 O ILE C 147 N ALA C 138
SHEET 3 U 4 CYS C 161 GLU C 166 -1 O CYS C 161 N THR C 150
SHEET 4 U 4 ASN C 171 PRO C 179 -1 O ASN C 171 N GLU C 166
SHEET 1 V 4 HIS C 182 ALA C 186 0
SHEET 2 V 4 ARG C 189 ARG C 194 -1 O ARG C 189 N ALA C 186
SHEET 3 V 4 LYS C 212 ASN C 218 -1 O LYS C 212 N ARG C 194
SHEET 4 V 4 ALA C 221 VAL C 226 -1 O ALA C 221 N VAL C 217
SHEET 1 W 4 SER C 233 VAL C 238 0
SHEET 2 W 4 ARG C 241 THR C 246 -1 O ARG C 241 N VAL C 238
SHEET 3 W 4 GLN C 253 ASP C 258 -1 N GLN C 253 O THR C 246
SHEET 4 W 4 ARG C 265 LYS C 266 -1 N ARG C 265 O SER C 256
SHEET 1 X 4 PRO C 275 THR C 280 0
SHEET 2 X 4 ILE C 285 LYS C 289 -1 N LEU C 286 O ASN C 279
SHEET 3 X 4 SER C 292 PHE C 296 -1 N SER C 292 O LYS C 289
SHEET 4 X 4 ILE C 303 LYS C 305 -1 N GLU C 304 O ILE C 295
SHEET 1 Y 4 ALA C 326 LEU C 332 0
SHEET 2 Y 4 LEU C 336 SER C 341 -1 O LEU C 336 N LEU C 332
SHEET 3 Y 4 GLN C 344 ASP C 349 -1 O GLN C 344 N SER C 341
SHEET 4 Y 4 VAL C 355 LYS C 357 -1 O LEU C 356 N ILE C 347
SHEET 1 Z 4 ILE C 364 ARG C 369 0
SHEET 2 Z 4 LYS C 374 GLY C 380 -1 N ALA C 376 O ARG C 368
SHEET 3 Z 4 ASP C 385 ASP C 391 -1 O PHE C 386 N HIS C 379
SHEET 4 Z 4 LYS C 399 GLY C 405 -1 N PHE C 400 O LEU C 387
SHEET 1 AA 4 VAL C 407 VAL C 412 0
SHEET 2 AA 4 PHE C 418 ASN C 423 -1 N VAL C 420 O GLY C 411
SHEET 3 AA 4 GLU C 427 ASP C 432 -1 O GLU C 427 N ASN C 423
SHEET 4 AA 4 PRO C 438 ARG C 443 -1 O THR C 439 N THR C 430
SHEET 1 AB 4 PHE C 452 ILE C 454 0
SHEET 2 AB 4 PHE C 460 LEU C 467 -1 O ALA C 462 N THR C 453
SHEET 3 AB 4 MET C 477 ASP C 484 -1 N MET C 477 O LEU C 467
SHEET 4 AB 4 LYS C 489 ALA C 492 -1 O LYS C 489 N ASP C 484
SHEET 1 AC 4 ASP C 500 PHE C 505 0
SHEET 2 AC 4 ASN C 511 SER C 516 -1 N TYR C 513 O ALA C 504
SHEET 3 AC 4 LYS C 538 PRO C 543 -1 N LYS C 538 O SER C 516
SHEET 4 AC 4 SER C 576 PRO C 577 -1 O SER C 576 N VAL C 541
SHEET 1 AD 2 SER C 523 PRO C 524 0
SHEET 2 AD 2 PHE C 531 SER C 532 -1 O SER C 532 N SER C 523
SHEET 1 AE 2 TYR C 585 PRO C 590 0
SHEET 2 AE 2 ILE C 595 SER C 599 -1 O LEU C 596 N ILE C 589
SHEET 1 AF 5 GLY C 617 TYR C 622 0
SHEET 2 AF 5 VAL C 629 LEU C 641 -1 O THR C 630 N LYS C 621
SHEET 3 AF 5 THR C 647 LYS C 652 -1 O MET C 649 N ARG C 640
SHEET 4 AF 5 ILE C 657 PRO C 661 -1 O TYR C 658 N VAL C 650
SHEET 5 AF 5 ARG C 669 THR C 670 -1 N ARG C 669 O THR C 659
SHEET 1 AG 2 GLU C 749 MET C 750 0
SHEET 2 AG 2 VAL C1005 LEU C1006 -1 N VAL C1005 O MET C 750
SHEET 1 AH 7 CYS C 767 ASP C 772 0
SHEET 2 AH 7 HIS C 775 ALA C 781 -1 O HIS C 775 N ASP C 772
SHEET 3 AH 7 LEU C 806 ILE C 810 -1 N ILE C 807 O TYR C 776
SHEET 4 AH 7 GLU C 813 THR C 814 -1 O GLU C 813 N ILE C 810
SHEET 5 AH 7 LEU C 806 ILE C 810 -1 N ILE C 810 O GLU C 813
SHEET 6 AH 7 SER C 832 SER C 838 -1 N ARG C 836 O ASP C 809
SHEET 7 AH 7 LYS C 844 ASP C 850 -1 O ARG C 845 N LEU C 837
SHEET 1 AI 5 ILE C 879 HIS C 883 0
SHEET 2 AI 5 GLY C 907 ASP C 911 1 O GLY C 907 N GLY C 880
SHEET 3 AI 5 LYS C 954 THR C 959 1 O LYS C 954 N LEU C 908
SHEET 4 AI 5 GLY C 980 GLY C 984 1 O LYS C 981 N ALA C 957
SHEET 5 AI 5 VAL C1031 GLU C1032 1 N VAL C1031 O LEU C 982
SHEET 1 AJ 2 GLY C 934 ASP C 936 0
SHEET 2 AJ 2 SER C 944 TYR C 946 -1 O SER C 944 N ASP C 936
SHEET 1 AK 2 VAL C 992 GLY C 993 0
SHEET 2 AK 2 PHE C1011 ALA C1012 -1 N PHE C1011 O GLY C 993
SHEET 1 AL 4 LEU E 44 HIS E 49 0
SHEET 2 AL 4 ARG E 52 CYS E 57 -1 O ARG E 52 N HIS E 49
SHEET 3 AL 4 ASP E 60 ASP E 65 -1 O ASP E 60 N CYS E 57
SHEET 4 AL 4 THR E 71 VAL E 75 -1 O ARG E 72 N GLU E 63
SHEET 1 AM 6 VAL E 80 PHE E 86 0
SHEET 2 AM 6 LYS E 92 ARG E 99 -1 O ALA E 94 N ARG E 85
SHEET 3 AM 6 THR E 105 ASN E 112 -1 N THR E 105 O ARG E 99
SHEET 4 AM 6 GLY E 126 LYS E 127 -1 N GLY E 126 O ALA E 106
SHEET 5 AM 6 THR E 105 ASN E 112 -1 O ALA E 106 N GLY E 126
SHEET 6 AM 6 GLU E 117 ARG E 120 -1 O GLU E 117 N ASN E 112
SHEET 1 AN 4 ASP E 136 PHE E 140 0
SHEET 2 AN 4 LEU E 146 THR E 150 -1 O ILE E 147 N ALA E 138
SHEET 3 AN 4 CYS E 161 GLU E 166 -1 O CYS E 161 N THR E 150
SHEET 4 AN 4 ASN E 171 PRO E 179 -1 O ASN E 171 N GLU E 166
SHEET 1 AO 4 HIS E 182 ALA E 186 0
SHEET 2 AO 4 ARG E 189 ARG E 194 -1 O ARG E 189 N ALA E 186
SHEET 3 AO 4 LYS E 212 ASN E 218 -1 O LYS E 212 N ARG E 194
SHEET 4 AO 4 ALA E 221 VAL E 226 -1 O ALA E 221 N VAL E 217
SHEET 1 AP 4 SER E 233 VAL E 238 0
SHEET 2 AP 4 ARG E 241 THR E 246 -1 O ARG E 241 N VAL E 238
SHEET 3 AP 4 GLN E 253 ASP E 258 -1 N GLN E 253 O THR E 246
SHEET 4 AP 4 ARG E 265 LYS E 266 -1 N ARG E 265 O SER E 256
SHEET 1 AQ 4 ARG E 276 THR E 280 0
SHEET 2 AQ 4 ILE E 285 LYS E 289 -1 N LEU E 286 O ASN E 279
SHEET 3 AQ 4 SER E 292 PHE E 296 -1 O SER E 292 N LYS E 289
SHEET 4 AQ 4 ILE E 303 LYS E 305 -1 N GLU E 304 O ILE E 295
SHEET 1 AR 4 ALA E 326 LEU E 332 0
SHEET 2 AR 4 LEU E 336 SER E 341 -1 O LEU E 336 N LEU E 332
SHEET 3 AR 4 GLN E 344 ASP E 349 -1 O GLN E 344 N SER E 341
SHEET 4 AR 4 VAL E 355 LYS E 357 -1 O LEU E 356 N ILE E 347
SHEET 1 AS 4 ILE E 364 ARG E 369 0
SHEET 2 AS 4 LYS E 374 GLY E 380 -1 N ALA E 376 O ARG E 368
SHEET 3 AS 4 ASP E 385 ASP E 391 -1 O PHE E 386 N HIS E 379
SHEET 4 AS 4 LYS E 399 GLY E 405 -1 N PHE E 400 O LEU E 387
SHEET 1 AT 4 VAL E 407 VAL E 412 0
SHEET 2 AT 4 PHE E 418 ASN E 423 -1 N VAL E 420 O GLY E 411
SHEET 3 AT 4 GLU E 427 ASP E 432 -1 O GLU E 427 N ASN E 423
SHEET 4 AT 4 PRO E 438 ARG E 443 -1 O THR E 439 N THR E 430
SHEET 1 AU 4 PHE E 452 ILE E 454 0
SHEET 2 AU 4 PHE E 460 LEU E 467 -1 O ALA E 462 N THR E 453
SHEET 3 AU 4 MET E 477 ASP E 484 -1 N MET E 477 O LEU E 467
SHEET 4 AU 4 LYS E 489 ALA E 492 -1 O LYS E 489 N ASP E 484
SHEET 1 AV 4 ASP E 500 PHE E 505 0
SHEET 2 AV 4 ASN E 511 SER E 516 -1 N TYR E 513 O ALA E 504
SHEET 3 AV 4 LYS E 538 PRO E 543 -1 N LYS E 538 O SER E 516
SHEET 4 AV 4 SER E 576 PRO E 577 -1 O SER E 576 N VAL E 541
SHEET 1 AW 2 SER E 523 PRO E 524 0
SHEET 2 AW 2 PHE E 531 SER E 532 -1 O SER E 532 N SER E 523
SHEET 1 AX 2 TYR E 585 PRO E 590 0
SHEET 2 AX 2 ILE E 595 SER E 599 -1 N LEU E 596 O ILE E 589
SHEET 1 AY 5 GLY E 617 TYR E 622 0
SHEET 2 AY 5 VAL E 629 LEU E 641 -1 O THR E 630 N LYS E 621
SHEET 3 AY 5 THR E 647 LYS E 652 -1 O MET E 649 N ARG E 640
SHEET 4 AY 5 ILE E 657 PRO E 661 -1 N TYR E 658 O VAL E 650
SHEET 5 AY 5 ARG E 669 THR E 670 -1 N ARG E 669 O THR E 659
SHEET 1 AZ 2 GLU E 749 MET E 750 0
SHEET 2 AZ 2 VAL E1005 LEU E1006 -1 N VAL E1005 O MET E 750
SHEET 1 BA 7 CYS E 767 ASP E 772 0
SHEET 2 BA 7 HIS E 775 ALA E 781 -1 O HIS E 775 N ASP E 772
SHEET 3 BA 7 LEU E 806 ILE E 810 -1 N ILE E 807 O TYR E 776
SHEET 4 BA 7 GLU E 813 THR E 814 -1 O GLU E 813 N ILE E 810
SHEET 5 BA 7 LEU E 806 ILE E 810 -1 N ILE E 810 O GLU E 813
SHEET 6 BA 7 SER E 832 SER E 838 -1 N ARG E 836 O ASP E 809
SHEET 7 BA 7 LYS E 844 ASP E 850 -1 N ARG E 845 O LEU E 837
SHEET 1 BB 5 ILE E 879 HIS E 883 0
SHEET 2 BB 5 GLY E 907 ASP E 911 1 O GLY E 907 N GLY E 880
SHEET 3 BB 5 LYS E 954 THR E 959 1 O LYS E 954 N LEU E 908
SHEET 4 BB 5 GLY E 980 GLY E 984 1 O LYS E 981 N ALA E 957
SHEET 5 BB 5 VAL E1031 GLU E1032 1 N VAL E1031 O LEU E 982
SHEET 1 BC 2 GLY E 934 ASP E 936 0
SHEET 2 BC 2 SER E 944 TYR E 946 -1 O SER E 944 N ASP E 936
SHEET 1 BD 2 VAL E 992 GLY E 993 0
SHEET 2 BD 2 PHE E1011 ALA E1012 -1 N PHE E1011 O GLY E 993
SHEET 1 BE 4 LEU G 44 HIS G 49 0
SHEET 2 BE 4 ARG G 52 CYS G 57 -1 O ARG G 52 N HIS G 49
SHEET 3 BE 4 ASP G 60 ASP G 65 -1 O ASP G 60 N CYS G 57
SHEET 4 BE 4 THR G 71 VAL G 75 -1 O ARG G 72 N GLU G 63
SHEET 1 BF 6 VAL G 80 PHE G 86 0
SHEET 2 BF 6 LYS G 92 ARG G 99 -1 O ALA G 94 N ARG G 85
SHEET 3 BF 6 THR G 105 ASN G 112 -1 N THR G 105 O ARG G 99
SHEET 4 BF 6 GLY G 126 LYS G 127 -1 O GLY G 126 N ALA G 106
SHEET 5 BF 6 THR G 105 ASN G 112 -1 N ALA G 106 O GLY G 126
SHEET 6 BF 6 GLU G 117 ARG G 120 -1 O GLU G 117 N ASN G 112
SHEET 1 BG 4 ASP G 136 PHE G 140 0
SHEET 2 BG 4 LEU G 146 THR G 150 -1 O ILE G 147 N ALA G 138
SHEET 3 BG 4 CYS G 161 GLU G 166 -1 O CYS G 161 N THR G 150
SHEET 4 BG 4 ASN G 171 PRO G 179 -1 O ASN G 171 N GLU G 166
SHEET 1 BH 4 HIS G 182 ALA G 186 0
SHEET 2 BH 4 ARG G 189 ARG G 194 -1 O ARG G 189 N ALA G 186
SHEET 3 BH 4 LYS G 212 ASN G 218 -1 O LYS G 212 N ARG G 194
SHEET 4 BH 4 ALA G 221 VAL G 226 -1 O ALA G 221 N VAL G 217
SHEET 1 BI 4 SER G 233 VAL G 238 0
SHEET 2 BI 4 ARG G 241 THR G 246 -1 O ARG G 241 N VAL G 238
SHEET 3 BI 4 GLN G 253 ASP G 258 -1 N GLN G 253 O THR G 246
SHEET 4 BI 4 ARG G 265 LYS G 266 -1 N ARG G 265 O SER G 256
SHEET 1 BJ 4 ARG G 276 THR G 280 0
SHEET 2 BJ 4 ILE G 285 LYS G 289 -1 N LEU G 286 O ASN G 279
SHEET 3 BJ 4 SER G 292 PHE G 296 -1 O SER G 292 N LYS G 289
SHEET 4 BJ 4 ILE G 303 LYS G 305 -1 N GLU G 304 O ILE G 295
SHEET 1 BK 4 ALA G 326 LEU G 332 0
SHEET 2 BK 4 LEU G 336 SER G 341 -1 O LEU G 336 N LEU G 332
SHEET 3 BK 4 GLN G 344 ASP G 349 -1 O GLN G 344 N SER G 341
SHEET 4 BK 4 VAL G 355 LYS G 357 -1 N LEU G 356 O ILE G 347
SHEET 1 BL 4 ILE G 364 ARG G 369 0
SHEET 2 BL 4 LYS G 374 GLY G 380 -1 N ALA G 376 O ARG G 368
SHEET 3 BL 4 ASP G 385 ASP G 391 -1 O PHE G 386 N HIS G 379
SHEET 4 BL 4 LYS G 399 GLY G 405 -1 N PHE G 400 O LEU G 387
SHEET 1 BM 4 VAL G 407 VAL G 412 0
SHEET 2 BM 4 PHE G 418 ASN G 423 -1 N VAL G 420 O GLY G 411
SHEET 3 BM 4 GLU G 427 ASP G 432 -1 O GLU G 427 N ASN G 423
SHEET 4 BM 4 PRO G 438 ARG G 443 -1 O THR G 439 N THR G 430
SHEET 1 BN 4 PHE G 452 ILE G 454 0
SHEET 2 BN 4 PHE G 460 LEU G 467 -1 O ALA G 462 N THR G 453
SHEET 3 BN 4 MET G 477 ASP G 484 -1 N MET G 477 O LEU G 467
SHEET 4 BN 4 LYS G 489 ALA G 492 -1 O LYS G 489 N ASP G 484
SHEET 1 BO 4 ASP G 500 PHE G 505 0
SHEET 2 BO 4 ASN G 511 SER G 516 -1 N TYR G 513 O ALA G 504
SHEET 3 BO 4 LYS G 538 PRO G 543 -1 N LYS G 538 O SER G 516
SHEET 4 BO 4 SER G 576 PRO G 577 -1 O SER G 576 N VAL G 541
SHEET 1 BP 2 SER G 523 PRO G 524 0
SHEET 2 BP 2 PHE G 531 SER G 532 -1 N SER G 532 O SER G 523
SHEET 1 BQ 2 TYR G 585 PRO G 590 0
SHEET 2 BQ 2 ILE G 595 SER G 599 -1 O LEU G 596 N ILE G 589
SHEET 1 BR 5 GLY G 617 TYR G 622 0
SHEET 2 BR 5 VAL G 629 LEU G 641 -1 O THR G 630 N LYS G 621
SHEET 3 BR 5 THR G 647 LYS G 652 -1 O MET G 649 N ARG G 640
SHEET 4 BR 5 ILE G 657 PRO G 661 -1 O TYR G 658 N VAL G 650
SHEET 5 BR 5 ARG G 669 THR G 670 -1 N ARG G 669 O THR G 659
SHEET 1 BS 2 GLU G 749 MET G 750 0
SHEET 2 BS 2 VAL G1005 LEU G1006 -1 N VAL G1005 O MET G 750
SHEET 1 BT 7 CYS G 767 ASP G 772 0
SHEET 2 BT 7 HIS G 775 ALA G 781 -1 O HIS G 775 N ASP G 772
SHEET 3 BT 7 LEU G 806 ILE G 810 -1 N ILE G 807 O TYR G 776
SHEET 4 BT 7 GLU G 813 THR G 814 -1 O GLU G 813 N ILE G 810
SHEET 5 BT 7 LEU G 806 ILE G 810 -1 N ILE G 810 O GLU G 813
SHEET 6 BT 7 SER G 832 SER G 838 -1 N ARG G 836 O ASP G 809
SHEET 7 BT 7 LYS G 844 ASP G 850 -1 N ARG G 845 O LEU G 837
SHEET 1 BU 5 ILE G 879 HIS G 883 0
SHEET 2 BU 5 GLY G 907 ASP G 911 1 O GLY G 907 N GLY G 880
SHEET 3 BU 5 LYS G 954 THR G 959 1 O LYS G 954 N LEU G 908
SHEET 4 BU 5 GLY G 980 GLY G 984 1 O LYS G 981 N ALA G 957
SHEET 5 BU 5 VAL G1031 GLU G1032 1 N VAL G1031 O LEU G 982
SHEET 1 BV 2 GLY G 934 ASP G 936 0
SHEET 2 BV 2 SER G 944 TYR G 946 -1 O SER G 944 N ASP G 936
SHEET 1 BW 2 VAL G 992 GLY G 993 0
SHEET 2 BW 2 PHE G1011 ALA G1012 -1 N PHE G1011 O GLY G 993
SHEET 1 BX 4 LEU I 44 HIS I 49 0
SHEET 2 BX 4 ARG I 52 CYS I 57 -1 O ARG I 52 N HIS I 49
SHEET 3 BX 4 ASP I 60 ASP I 65 -1 O ASP I 60 N CYS I 57
SHEET 4 BX 4 THR I 71 VAL I 75 -1 O ARG I 72 N GLU I 63
SHEET 1 BY 6 VAL I 80 PHE I 86 0
SHEET 2 BY 6 LYS I 92 ARG I 99 -1 O ALA I 94 N ARG I 85
SHEET 3 BY 6 THR I 105 ASN I 112 -1 N THR I 105 O ARG I 99
SHEET 4 BY 6 GLY I 126 LYS I 127 -1 N GLY I 126 O ALA I 106
SHEET 5 BY 6 THR I 105 ASN I 112 -1 O ALA I 106 N GLY I 126
SHEET 6 BY 6 GLU I 117 ARG I 120 -1 O GLU I 117 N ASN I 112
SHEET 1 BZ 4 ASP I 136 PHE I 140 0
SHEET 2 BZ 4 LEU I 146 THR I 150 -1 O ILE I 147 N ALA I 138
SHEET 3 BZ 4 CYS I 161 GLU I 166 -1 O CYS I 161 N THR I 150
SHEET 4 BZ 4 ASN I 171 PRO I 179 -1 O ASN I 171 N GLU I 166
SHEET 1 CA 4 HIS I 182 ALA I 186 0
SHEET 2 CA 4 ARG I 189 ARG I 194 -1 O ARG I 189 N ALA I 186
SHEET 3 CA 4 LYS I 212 ASN I 218 -1 O LYS I 212 N ARG I 194
SHEET 4 CA 4 ALA I 221 VAL I 226 -1 O ALA I 221 N VAL I 217
SHEET 1 CB 4 SER I 233 VAL I 238 0
SHEET 2 CB 4 ARG I 241 THR I 246 -1 O ARG I 241 N VAL I 238
SHEET 3 CB 4 GLN I 253 ASP I 258 -1 N GLN I 253 O THR I 246
SHEET 4 CB 4 ARG I 265 LYS I 266 -1 N ARG I 265 O SER I 256
SHEET 1 CC 4 ARG I 276 THR I 280 0
SHEET 2 CC 4 ILE I 285 LYS I 289 -1 N LEU I 286 O ASN I 279
SHEET 3 CC 4 SER I 292 PHE I 296 -1 O SER I 292 N LYS I 289
SHEET 4 CC 4 ILE I 303 LYS I 305 -1 N GLU I 304 O ILE I 295
SHEET 1 CD 4 ALA I 326 LEU I 332 0
SHEET 2 CD 4 LEU I 336 SER I 341 -1 O LEU I 336 N LEU I 332
SHEET 3 CD 4 GLN I 344 ASP I 349 -1 O GLN I 344 N SER I 341
SHEET 4 CD 4 VAL I 355 LYS I 357 -1 N LEU I 356 O ILE I 347
SHEET 1 CE 4 ILE I 364 ARG I 369 0
SHEET 2 CE 4 LYS I 374 GLY I 380 -1 N ALA I 376 O ARG I 368
SHEET 3 CE 4 ASP I 385 ASP I 391 -1 O PHE I 386 N HIS I 379
SHEET 4 CE 4 LYS I 399 GLY I 405 -1 N PHE I 400 O LEU I 387
SHEET 1 CF 4 VAL I 407 VAL I 412 0
SHEET 2 CF 4 PHE I 418 ASN I 423 -1 N VAL I 420 O GLY I 411
SHEET 3 CF 4 GLU I 427 ASP I 432 -1 O GLU I 427 N ASN I 423
SHEET 4 CF 4 PRO I 438 ARG I 443 -1 O THR I 439 N THR I 430
SHEET 1 CG 4 PHE I 452 ILE I 454 0
SHEET 2 CG 4 PHE I 460 LEU I 467 -1 O ALA I 462 N THR I 453
SHEET 3 CG 4 MET I 477 ASP I 484 -1 N MET I 477 O LEU I 467
SHEET 4 CG 4 LYS I 489 ALA I 492 -1 O LYS I 489 N ASP I 484
SHEET 1 CH 4 ASP I 500 PHE I 505 0
SHEET 2 CH 4 ASN I 511 SER I 516 -1 N TYR I 513 O ALA I 504
SHEET 3 CH 4 LYS I 538 PRO I 543 -1 N LYS I 538 O SER I 516
SHEET 4 CH 4 SER I 576 PRO I 577 -1 O SER I 576 N VAL I 541
SHEET 1 CI 2 SER I 523 PRO I 524 0
SHEET 2 CI 2 PHE I 531 SER I 532 -1 O SER I 532 N SER I 523
SHEET 1 CJ 2 TYR I 585 PRO I 590 0
SHEET 2 CJ 2 ILE I 595 SER I 599 -1 O LEU I 596 N ILE I 589
SHEET 1 CK 5 GLY I 617 TYR I 622 0
SHEET 2 CK 5 VAL I 629 LEU I 641 -1 O THR I 630 N LYS I 621
SHEET 3 CK 5 THR I 647 LYS I 652 -1 O MET I 649 N ARG I 640
SHEET 4 CK 5 ILE I 657 PRO I 661 -1 N TYR I 658 O VAL I 650
SHEET 5 CK 5 ARG I 669 THR I 670 -1 N ARG I 669 O THR I 659
SHEET 1 CL 2 GLU I 749 MET I 750 0
SHEET 2 CL 2 VAL I1005 LEU I1006 -1 N VAL I1005 O MET I 750
SHEET 1 CM 7 CYS I 767 ASP I 772 0
SHEET 2 CM 7 HIS I 775 ALA I 781 -1 O HIS I 775 N ASP I 772
SHEET 3 CM 7 LEU I 806 ILE I 810 -1 N ILE I 807 O TYR I 776
SHEET 4 CM 7 GLU I 813 THR I 814 -1 O GLU I 813 N ILE I 810
SHEET 5 CM 7 LEU I 806 ILE I 810 -1 N ILE I 810 O GLU I 813
SHEET 6 CM 7 SER I 832 SER I 838 -1 N ARG I 836 O ASP I 809
SHEET 7 CM 7 LYS I 844 ASP I 850 -1 O ARG I 845 N LEU I 837
SHEET 1 CN 5 ILE I 879 HIS I 883 0
SHEET 2 CN 5 GLY I 907 ASP I 911 1 O GLY I 907 N GLY I 880
SHEET 3 CN 5 LYS I 954 THR I 959 1 O LYS I 954 N LEU I 908
SHEET 4 CN 5 GLY I 980 GLY I 984 1 O LYS I 981 N ALA I 957
SHEET 5 CN 5 VAL I1031 GLU I1032 1 N VAL I1031 O LEU I 982
SHEET 1 CO 2 GLY I 934 ASP I 936 0
SHEET 2 CO 2 SER I 944 TYR I 946 -1 O SER I 944 N ASP I 936
SHEET 1 CP 2 VAL I 992 GLY I 993 0
SHEET 2 CP 2 PHE I1011 ALA I1012 -1 N PHE I1011 O GLY I 993
SHEET 1 CQ 4 LEU K 44 HIS K 49 0
SHEET 2 CQ 4 ARG K 52 CYS K 57 -1 O ARG K 52 N HIS K 49
SHEET 3 CQ 4 ASP K 60 ASP K 65 -1 O ASP K 60 N CYS K 57
SHEET 4 CQ 4 THR K 71 VAL K 75 -1 O ARG K 72 N GLU K 63
SHEET 1 CR 6 VAL K 80 PHE K 86 0
SHEET 2 CR 6 LYS K 92 ARG K 99 -1 O ALA K 94 N ARG K 85
SHEET 3 CR 6 THR K 105 ASN K 112 -1 N THR K 105 O ARG K 99
SHEET 4 CR 6 GLY K 126 LYS K 127 -1 N GLY K 126 O ALA K 106
SHEET 5 CR 6 THR K 105 ASN K 112 -1 O ALA K 106 N GLY K 126
SHEET 6 CR 6 GLU K 117 ARG K 120 -1 O GLU K 117 N ASN K 112
SHEET 1 CS 4 ASP K 136 PHE K 140 0
SHEET 2 CS 4 LEU K 146 THR K 150 -1 O ILE K 147 N ALA K 138
SHEET 3 CS 4 CYS K 161 GLU K 166 -1 O CYS K 161 N THR K 150
SHEET 4 CS 4 ASN K 171 PRO K 179 -1 O ASN K 171 N GLU K 166
SHEET 1 CT 4 HIS K 182 ALA K 186 0
SHEET 2 CT 4 ARG K 189 ARG K 194 -1 O ARG K 189 N ALA K 186
SHEET 3 CT 4 LYS K 212 ASN K 218 -1 O LYS K 212 N ARG K 194
SHEET 4 CT 4 ALA K 221 VAL K 226 -1 O ALA K 221 N VAL K 217
SHEET 1 CU 4 SER K 233 VAL K 238 0
SHEET 2 CU 4 ARG K 241 THR K 246 -1 O ARG K 241 N VAL K 238
SHEET 3 CU 4 GLN K 253 ASP K 258 -1 N GLN K 253 O THR K 246
SHEET 4 CU 4 ARG K 265 LYS K 266 -1 N ARG K 265 O SER K 256
SHEET 1 CV 4 PRO K 275 THR K 280 0
SHEET 2 CV 4 ILE K 285 LYS K 289 -1 N LEU K 286 O ASN K 279
SHEET 3 CV 4 SER K 292 PHE K 296 -1 O SER K 292 N LYS K 289
SHEET 4 CV 4 ILE K 303 LYS K 305 -1 N GLU K 304 O ILE K 295
SHEET 1 CW 4 ALA K 326 LEU K 332 0
SHEET 2 CW 4 LEU K 336 SER K 341 -1 O LEU K 336 N LEU K 332
SHEET 3 CW 4 GLN K 344 ASP K 349 -1 N GLN K 344 O SER K 341
SHEET 4 CW 4 VAL K 355 LYS K 357 -1 O LEU K 356 N ILE K 347
SHEET 1 CX 4 ILE K 364 ARG K 369 0
SHEET 2 CX 4 LYS K 374 GLY K 380 -1 N ALA K 376 O ARG K 368
SHEET 3 CX 4 ASP K 385 ASP K 391 -1 O PHE K 386 N HIS K 379
SHEET 4 CX 4 LYS K 399 GLY K 405 -1 N PHE K 400 O LEU K 387
SHEET 1 CY 4 VAL K 407 VAL K 412 0
SHEET 2 CY 4 PHE K 418 ASN K 423 -1 N VAL K 420 O GLY K 411
SHEET 3 CY 4 GLU K 427 ASP K 432 -1 O GLU K 427 N ASN K 423
SHEET 4 CY 4 PRO K 438 ARG K 443 -1 O THR K 439 N THR K 430
SHEET 1 CZ 4 PHE K 452 ILE K 454 0
SHEET 2 CZ 4 PHE K 460 LEU K 467 -1 O ALA K 462 N THR K 453
SHEET 3 CZ 4 MET K 477 ASP K 484 -1 N MET K 477 O LEU K 467
SHEET 4 CZ 4 LYS K 489 ALA K 492 -1 O LYS K 489 N ASP K 484
SHEET 1 DA 4 ASP K 500 PHE K 505 0
SHEET 2 DA 4 ASN K 511 SER K 516 -1 N TYR K 513 O ALA K 504
SHEET 3 DA 4 LYS K 538 PRO K 543 -1 N LYS K 538 O SER K 516
SHEET 4 DA 4 SER K 576 PRO K 577 -1 O SER K 576 N VAL K 541
SHEET 1 DB 2 SER K 523 PRO K 524 0
SHEET 2 DB 2 PHE K 531 SER K 532 -1 O SER K 532 N SER K 523
SHEET 1 DC 2 TYR K 585 PRO K 590 0
SHEET 2 DC 2 ILE K 595 SER K 599 -1 O LEU K 596 N ILE K 589
SHEET 1 DD 5 GLY K 617 TYR K 622 0
SHEET 2 DD 5 VAL K 629 LEU K 641 -1 O THR K 630 N LYS K 621
SHEET 3 DD 5 THR K 647 LYS K 652 -1 O MET K 649 N ARG K 640
SHEET 4 DD 5 ILE K 657 PRO K 661 -1 N TYR K 658 O VAL K 650
SHEET 5 DD 5 ARG K 669 THR K 670 -1 N ARG K 669 O THR K 659
SHEET 1 DE 2 GLU K 749 MET K 750 0
SHEET 2 DE 2 VAL K1005 LEU K1006 -1 N VAL K1005 O MET K 750
SHEET 1 DF 7 CYS K 767 ASP K 772 0
SHEET 2 DF 7 HIS K 775 ALA K 781 -1 O HIS K 775 N ASP K 772
SHEET 3 DF 7 LEU K 806 ILE K 810 -1 N ILE K 807 O TYR K 776
SHEET 4 DF 7 GLU K 813 THR K 814 -1 O GLU K 813 N ILE K 810
SHEET 5 DF 7 LEU K 806 ILE K 810 -1 N ILE K 810 O GLU K 813
SHEET 6 DF 7 SER K 832 SER K 838 -1 N ARG K 836 O ASP K 809
SHEET 7 DF 7 LYS K 844 ASP K 850 -1 O ARG K 845 N LEU K 837
SHEET 1 DG 5 ILE K 879 HIS K 883 0
SHEET 2 DG 5 GLY K 907 ASP K 911 1 O GLY K 907 N GLY K 880
SHEET 3 DG 5 LYS K 954 THR K 959 1 O LYS K 954 N LEU K 908
SHEET 4 DG 5 GLY K 980 GLY K 984 1 O LYS K 981 N ALA K 957
SHEET 5 DG 5 VAL K1031 GLU K1032 1 N VAL K1031 O LEU K 982
SHEET 1 DH 2 GLY K 934 ASP K 936 0
SHEET 2 DH 2 SER K 944 TYR K 946 -1 O SER K 944 N ASP K 936
SHEET 1 DI 2 VAL K 992 GLY K 993 0
SHEET 2 DI 2 PHE K1011 ALA K1012 -1 N PHE K1011 O GLY K 993
LINK C PHE B1213 C1 0QE B1214 1555 1555 1.15
LINK C PHE D1213 C1 0QE D1214 1555 1555 1.22
LINK C PHE F1213 C1 0QE F1214 1555 1555 1.21
LINK C PHE H1213 C1 0QE H1214 1555 1555 1.19
LINK C PHE J1213 C1 0QE J1214 1555 1555 1.21
LINK C PHE L1213 C1 0QE L1214 1555 1555 1.23
CISPEP 1 TYR A 946 PRO A 947 0 2.00
CISPEP 2 TYR C 946 PRO C 947 0 2.07
CISPEP 3 TYR E 946 PRO E 947 0 15.83
CISPEP 4 TYR G 946 PRO G 947 0 1.01
CISPEP 5 TYR I 946 PRO I 947 0 8.19
CISPEP 6 TYR K 946 PRO K 947 0 6.13
SITE 1 AC1 4 HIS A 746 SER A 965 ASP A 966 PHE B1213
SITE 1 AC2 4 HIS C 746 SER C 965 ASP C 966 PHE D1213
SITE 1 AC3 4 HIS E 746 SER E 965 ASP E 966 PHE F1213
SITE 1 AC4 4 HIS G 746 SER G 965 ASP G 966 PHE H1213
SITE 1 AC5 4 HIS I 746 SER I 965 ASP I 966 PHE J1213
SITE 1 AC6 4 HIS K 746 SER K 965 ASP K 966 PHE L1213
CRYST1 95.470 245.100 157.890 90.00 105.19 90.00 P 1 21 1 12
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 0.010474 0.000000 0.002844 0.00000
SCALE2 0.000000 0.004080 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006563 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
