HEADER HYDROLASE 18-APR-06 2GPL
TITLE TMC-95 BASED BIPHENYL-ETHER MACROCYCLES: SPECIFIC PROTEASOME
TITLE 2 INHIBITORS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEASOME COMPONENT Y7;
COMPND 3 CHAIN: A, O;
COMPND 4 SYNONYM: MACROPAIN SUBUNIT Y7, PROTEINASE YSCE SUBUNIT 7,
COMPND 5 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT Y7;
COMPND 6 EC: 3.4.25.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: PROTEASOME COMPONENT Y13;
COMPND 10 CHAIN: B, P;
COMPND 11 SYNONYM: MACROPAIN SUBUNIT Y13, PROTEINASE YSCE SUBUNIT 13,
COMPND 12 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT Y13;
COMPND 13 EC: 3.4.25.1;
COMPND 14 ENGINEERED: YES;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: PROTEASOME COMPONENT PRE6;
COMPND 17 CHAIN: C, Q;
COMPND 18 SYNONYM: MACROPAIN SUBUNIT PRE6, PROTEINASE YSCE SUBUNIT PRE6,
COMPND 19 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT PRE6;
COMPND 20 EC: 3.4.25.1;
COMPND 21 ENGINEERED: YES;
COMPND 22 MOL_ID: 4;
COMPND 23 MOLECULE: PROTEASOME COMPONENT PUP2;
COMPND 24 CHAIN: D, R;
COMPND 25 SYNONYM: MACROPAIN SUBUNIT PUP2, PROTEINASE YSCE SUBUNIT PUP2,
COMPND 26 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT PUP2;
COMPND 27 EC: 3.4.25.1;
COMPND 28 ENGINEERED: YES;
COMPND 29 MOL_ID: 5;
COMPND 30 MOLECULE: PROTEASOME COMPONENT PRE5;
COMPND 31 CHAIN: E, S;
COMPND 32 SYNONYM: MACROPAIN SUBUNIT PRE5, PROTEINASE YSCE SUBUNIT PRE5,
COMPND 33 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT PRE5;
COMPND 34 EC: 3.4.25.1;
COMPND 35 ENGINEERED: YES;
COMPND 36 MOL_ID: 6;
COMPND 37 MOLECULE: PROTEASOME COMPONENT C1;
COMPND 38 CHAIN: F, T;
COMPND 39 SYNONYM: MACROPAIN SUBUNIT C1, PROTEINASE YSCE SUBUNIT 1,
COMPND 40 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C1;
COMPND 41 EC: 3.4.25.1;
COMPND 42 ENGINEERED: YES;
COMPND 43 MOL_ID: 7;
COMPND 44 MOLECULE: PROTEASOME COMPONENT C7-ALPHA;
COMPND 45 CHAIN: G, U;
COMPND 46 SYNONYM: MACROPAIN SUBUNIT C7- ALPHA, PROTEINASE YSCE SUBUNIT 7,
COMPND 47 MULTICATALYTIC ENDOPEPTIDASE COMPLEX C7, COMPONENT Y8, SCL1
COMPND 48 SUPPRESSOR PROTEIN;
COMPND 49 EC: 3.4.25.1;
COMPND 50 ENGINEERED: YES;
COMPND 51 MOL_ID: 8;
COMPND 52 MOLECULE: PROTEASOME COMPONENT PUP1;
COMPND 53 CHAIN: H, V;
COMPND 54 SYNONYM: MACROPAIN SUBUNIT PUP1, PROTEINASE YSCE SUBUNIT PUP1,
COMPND 55 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT PUP1;
COMPND 56 EC: 3.4.25.1;
COMPND 57 ENGINEERED: YES;
COMPND 58 MOL_ID: 9;
COMPND 59 MOLECULE: PROTEASOME COMPONENT PUP3;
COMPND 60 CHAIN: I, W;
COMPND 61 SYNONYM: MACROPAIN SUBUNIT PUP3, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 62 SUBUNIT PUP3;
COMPND 63 EC: 3.4.25.1;
COMPND 64 ENGINEERED: YES;
COMPND 65 MOL_ID: 10;
COMPND 66 MOLECULE: PROTEASOME COMPONENT C11;
COMPND 67 CHAIN: J, X;
COMPND 68 SYNONYM: MACROPAIN SUBUNIT C11, PROTEINASE YSCE SUBUNIT 11,
COMPND 69 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C11;
COMPND 70 EC: 3.4.25.1;
COMPND 71 ENGINEERED: YES;
COMPND 72 MOL_ID: 11;
COMPND 73 MOLECULE: PROTEASOME COMPONENT PRE2;
COMPND 74 CHAIN: K, Y;
COMPND 75 SYNONYM: MACROPAIN SUBUNIT PRE2, PROTEINASE YSCE SUBUNIT PRE2,
COMPND 76 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT PRE2;
COMPND 77 EC: 3.4.25.1;
COMPND 78 ENGINEERED: YES;
COMPND 79 MOL_ID: 12;
COMPND 80 MOLECULE: PROTEASOME COMPONENT C5;
COMPND 81 CHAIN: L, Z;
COMPND 82 SYNONYM: MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C5;
COMPND 83 EC: 3.4.25.1;
COMPND 84 ENGINEERED: YES;
COMPND 85 MOL_ID: 13;
COMPND 86 MOLECULE: PROTEASOME COMPONENT PRE4;
COMPND 87 CHAIN: M, 1;
COMPND 88 SYNONYM: MACROPAIN SUBUNIT PRE4, PROTEINASE YSCE SUBUNIT PRE4,
COMPND 89 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT PRE4;
COMPND 90 EC: 3.4.25.1;
COMPND 91 ENGINEERED: YES;
COMPND 92 MOL_ID: 14;
COMPND 93 MOLECULE: PROTEASOME COMPONENT PRE3;
COMPND 94 CHAIN: N, 2;
COMPND 95 SYNONYM: MACROPAIN SUBUNIT PRE3, PROTEINASE YSCE SUBUNIT PRE3,
COMPND 96 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT PRE3;
COMPND 97 EC: 3.4.25.1;
COMPND 98 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: PRS4, PRE8;
SOURCE 6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 11 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 12 ORGANISM_TAXID: 4932;
SOURCE 13 GENE: PRS5, PRE9;
SOURCE 14 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 15 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 17 MOL_ID: 3;
SOURCE 18 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 19 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 20 ORGANISM_TAXID: 4932;
SOURCE 21 GENE: PRE6;
SOURCE 22 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 23 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 24 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 25 MOL_ID: 4;
SOURCE 26 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 27 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 28 ORGANISM_TAXID: 4932;
SOURCE 29 GENE: PUP2, DOA5;
SOURCE 30 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 31 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 32 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 33 MOL_ID: 5;
SOURCE 34 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 35 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 36 ORGANISM_TAXID: 4932;
SOURCE 37 GENE: PRE5;
SOURCE 38 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 39 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 40 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 41 MOL_ID: 6;
SOURCE 42 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 43 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 44 ORGANISM_TAXID: 4932;
SOURCE 45 GENE: PRS1, PRC1, PRE10;
SOURCE 46 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 47 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 48 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 49 MOL_ID: 7;
SOURCE 50 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 51 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 52 ORGANISM_TAXID: 4932;
SOURCE 53 GENE: PRS2, PRC2, SCL1;
SOURCE 54 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 55 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 56 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 57 MOL_ID: 8;
SOURCE 58 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 59 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 60 ORGANISM_TAXID: 4932;
SOURCE 61 GENE: PUP1;
SOURCE 62 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 63 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 64 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 65 MOL_ID: 9;
SOURCE 66 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 67 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 68 ORGANISM_TAXID: 4932;
SOURCE 69 GENE: PUP3;
SOURCE 70 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 71 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 72 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 73 MOL_ID: 10;
SOURCE 74 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 75 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 76 ORGANISM_TAXID: 4932;
SOURCE 77 GENE: PRE1;
SOURCE 78 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 79 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 80 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 81 MOL_ID: 11;
SOURCE 82 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 83 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 84 ORGANISM_TAXID: 4932;
SOURCE 85 GENE: PRE2, DOA3, PRG1;
SOURCE 86 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 87 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 88 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 89 MOL_ID: 12;
SOURCE 90 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 91 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 92 ORGANISM_TAXID: 4932;
SOURCE 93 GENE: PRS3, PRE7, PTS1;
SOURCE 94 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 95 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 96 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 97 MOL_ID: 13;
SOURCE 98 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 99 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 100 ORGANISM_TAXID: 4932;
SOURCE 101 GENE: PRE4;
SOURCE 102 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 103 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 104 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 105 MOL_ID: 14;
SOURCE 106 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 107 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 108 ORGANISM_TAXID: 4932;
SOURCE 109 GENE: PRE3;
SOURCE 110 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 111 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 112 EXPRESSION_SYSTEM_TAXID: 4932
KEYWDS PROTEASOMAL SUBUNIT FOLD REPRESENTS AN ANTIPARALLEL BETA-SHEET
KEYWDS 2 FLANKED BY HELICES; NTN-HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.GROLL,M.GOETZ,M.KAISER,E.WEYHER,M.MORODER
REVDAT 3 30-AUG-23 2GPL 1 REMARK
REVDAT 2 24-FEB-09 2GPL 1 VERSN
REVDAT 1 11-JUL-06 2GPL 0
JRNL AUTH M.GROLL,M.GOETZ,M.KAISER,E.WEYHER,L.MORODER
JRNL TITL TMC-95-BASED INHIBITOR DESIGN PROVIDES EVIDENCE FOR THE
JRNL TITL 2 CATALYTIC VERSATILITY OF THE PROTEASOME.
JRNL REF CHEM.BIOL. V. 13 607 2006
JRNL REFN ISSN 1074-5521
JRNL PMID 16793518
JRNL DOI 10.1016/J.CHEMBIOL.2006.04.005
REMARK 2
REMARK 2 RESOLUTION. 2.81 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 2.81
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 3454667.770
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 250974
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 SET) : 0.217
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 12489
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.002
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.97
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 35777
REMARK 3 BIN R VALUE (WORKING SET) : 0.3270
REMARK 3 BIN FREE R VALUE : 0.3620
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1874
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.008
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 49548
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 96
REMARK 3 SOLVENT ATOMS : 1070
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 41.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 11.33000
REMARK 3 B22 (A**2) : -23.55000
REMARK 3 B33 (A**2) : 12.22000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.96000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.37
REMARK 3 ESD FROM SIGMAA (A) : 0.45
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.41
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.50
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.770
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
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 : FLAT MODEL
REMARK 3 KSOL : 0.33
REMARK 3 BSOL : 37.06
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : BIA.PAR
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : BIA.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2GPL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-APR-06.
REMARK 100 THE DEPOSITION ID IS D_1000037399.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JUN-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MPG/DESY, HAMBURG
REMARK 200 BEAMLINE : BW6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.05
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 252489
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 15.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
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) : 2.81
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.33100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS 1.1
REMARK 200 STARTING MODEL: YEAST 20S PROTEASOME (1RYP)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20MM MGAC2; 0.1M MES, 12% MPD;
REMARK 280 CRYSTALS APPEARED WITHIN 7 DAYS; CRYSTAL SIZE 0.2 X 0.2 X 0.6
REMARK 280 MM3, PH 6.7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 150.48100
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS THE WHOLE CONTENT OF THE
REMARK 300 ASYMMETRIC UNIT CELL.
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: 28-MERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 28-MERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 117910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 214550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -350.0 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, M, N, O, P, Q, R, S,
REMARK 350 AND CHAINS: T, U, V, W, X, Y, Z, 1, 2
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 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 PRO Z 94 C - N - CA ANGL. DEV. = 9.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR A 5 118.33 60.23
REMARK 500 LYS A 53 71.25 -66.79
REMARK 500 SER A 56 140.91 164.17
REMARK 500 THR A 63 11.90 -65.31
REMARK 500 PRO A 72 -5.18 -59.31
REMARK 500 TYR A 100 -62.68 -152.73
REMARK 500 LYS A 167 -76.02 -34.05
REMARK 500 ASN A 21B 78.28 -108.13
REMARK 500 ALA A 235 23.14 -75.38
REMARK 500 ARG B 6 -38.38 -33.51
REMARK 500 ARG B 11 69.80 63.13
REMARK 500 THR B 13 51.41 -118.78
REMARK 500 VAL B 54 128.67 56.39
REMARK 500 THR B 64 98.61 -163.85
REMARK 500 MET B 184 167.22 -48.01
REMARK 500 SER B 20A -83.31 -54.58
REMARK 500 ASP B 208 -3.80 -58.70
REMARK 500 LYS B 21A 60.54 -114.76
REMARK 500 ASP B 21C -63.31 171.14
REMARK 500 THR B 236 10.20 -65.67
REMARK 500 ASN C 44 38.73 -145.25
REMARK 500 ARG C 53 174.65 -56.39
REMARK 500 SER C 54 38.85 -153.59
REMARK 500 LEU C 58 24.64 169.35
REMARK 500 THR C 63 122.06 -37.16
REMARK 500 ASP C 105 131.74 -175.05
REMARK 500 GLN C 125 43.81 -142.64
REMARK 500 ASN C 179 3.90 -156.12
REMARK 500 PRO C 183 86.41 -36.55
REMARK 500 ALA C 184 0.45 -55.43
REMARK 500 GLN C 202 81.43 55.61
REMARK 500 THR C 203 87.18 41.07
REMARK 500 GLU C 242 35.36 -69.91
REMARK 500 ALA D 120 -71.61 -28.75
REMARK 500 SER D 12E 81.50 -66.21
REMARK 500 GLU D 12G -134.46 169.68
REMARK 500 MET D 128 112.68 -178.14
REMARK 500 ARG E 5 -57.04 -11.07
REMARK 500 SER E 42 -134.56 -99.58
REMARK 500 TYR E 63 78.50 -101.58
REMARK 500 GLN E 64 129.29 -17.54
REMARK 500 ASP E 142 -157.49 -119.63
REMARK 500 LYS E 143 2.24 -69.97
REMARK 500 THR E 163 174.63 176.46
REMARK 500 LEU E 180 -75.56 -35.94
REMARK 500 ARG E 202 -55.79 165.43
REMARK 500 ASP E 203 -80.18 -56.32
REMARK 500 GLU E 204 -145.12 -118.04
REMARK 500 LYS E 217 -65.52 -15.44
REMARK 500 PHE E 221 117.31 -39.88
REMARK 500
REMARK 500 THIS ENTRY HAS 191 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 BIQ H 1000
REMARK 615 BIQ V 1001
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BIQ H 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BIQ V 1001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1RYP RELATED DB: PDB
REMARK 900 RELATED ID: 1JD2 RELATED DB: PDB
DBREF 2GPL A 4 236 UNP P23639 PSA2_YEAST 1 250
DBREF 2GPL O 4 236 UNP P23639 PSA2_YEAST 1 250
DBREF 2GPL B 4 239 UNP P23638 PSA4_YEAST 2 245
DBREF 2GPL P 4 239 UNP P23638 PSA4_YEAST 2 245
DBREF 2GPL C 7 243 UNP P40303 PSA7_YEAST 3 243
DBREF 2GPL Q 7 243 UNP P40303 PSA7_YEAST 3 243
DBREF 2GPL D 9 244 UNP P32379 PSA5_YEAST 9 250
DBREF 2GPL R 9 244 UNP P32379 PSA5_YEAST 9 250
DBREF 2GPL E 4 233 UNP P40302 PSA1_YEAST 2 234
DBREF 2GPL S 4 233 UNP P40302 PSA1_YEAST 2 234
DBREF 2GPL F 5 241 UNP P21242 PSA3_YEAST 4 247
DBREF 2GPL T 5 241 UNP P21242 PSA3_YEAST 4 247
DBREF 2GPL G 6 240 UNP P21243 PSA6_YEAST 10 252
DBREF 2GPL U 6 240 UNP P21243 PSA6_YEAST 10 252
DBREF 2GPL H 1 223 UNP P25043 PSB7_YEAST 30 251
DBREF 2GPL V 1 223 UNP P25043 PSB7_YEAST 30 251
DBREF 2GPL I -8 194 UNP P25451 PSB3_YEAST 2 205
DBREF 2GPL W -8 194 UNP P25451 PSB3_YEAST 2 205
DBREF 2GPL J -1 193 UNP P22141 PSB2_YEAST 1 198
DBREF 2GPL X -1 193 UNP P22141 PSB2_YEAST 1 198
DBREF 2GPL K 1 211 UNP P30656 PSB5_YEAST 76 287
DBREF 2GPL Y 1 211 UNP P30656 PSB5_YEAST 76 287
DBREF 2GPL L -9 194 UNP P23724 PSB1_YEAST 20 241
DBREF 2GPL Z -9 194 UNP P23724 PSB1_YEAST 20 241
DBREF 2GPL M -8 211 UNP P30657 PSB4_YEAST 34 266
DBREF 2GPL 1 -8 211 UNP P30657 PSB4_YEAST 34 266
DBREF 2GPL N 1 18J UNP P38624 PSB6_YEAST 20 215
DBREF 2GPL 2 1 18J UNP P38624 PSB6_YEAST 20 215
SEQRES 1 A 250 MET THR ASP ARG TYR SER PHE SER LEU THR THR PHE SER
SEQRES 2 A 250 PRO SER GLY LYS LEU GLY GLN ILE ASP TYR ALA LEU THR
SEQRES 3 A 250 ALA VAL LYS GLN GLY VAL THR SER LEU GLY ILE LYS ALA
SEQRES 4 A 250 THR ASN GLY VAL VAL ILE ALA THR GLU LYS LYS SER SER
SEQRES 5 A 250 SER PRO LEU ALA MET SER GLU THR LEU SER LYS VAL SER
SEQRES 6 A 250 LEU LEU THR PRO ASP ILE GLY ALA VAL TYR SER GLY MET
SEQRES 7 A 250 GLY PRO ASP TYR ARG VAL LEU VAL ASP LYS SER ARG LYS
SEQRES 8 A 250 VAL ALA HIS THR SER TYR LYS ARG ILE TYR GLY GLU TYR
SEQRES 9 A 250 PRO PRO THR LYS LEU LEU VAL SER GLU VAL ALA LYS ILE
SEQRES 10 A 250 MET GLN GLU ALA THR GLN SER GLY GLY VAL ARG PRO PHE
SEQRES 11 A 250 GLY VAL SER LEU LEU ILE ALA GLY HIS ASP GLU PHE ASN
SEQRES 12 A 250 GLY PHE SER LEU TYR GLN VAL ASP PRO SER GLY SER TYR
SEQRES 13 A 250 PHE PRO TRP LYS ALA THR ALA ILE GLY LYS GLY SER VAL
SEQRES 14 A 250 ALA ALA LYS THR PHE LEU GLU LYS ARG TRP ASN ASP GLU
SEQRES 15 A 250 LEU GLU LEU GLU ASP ALA ILE HIS ILE ALA LEU LEU THR
SEQRES 16 A 250 LEU LYS GLU SER VAL GLU GLY GLU PHE ASN GLY ASP THR
SEQRES 17 A 250 ILE GLU LEU ALA ILE ILE GLY ASP GLU ASN PRO ASP LEU
SEQRES 18 A 250 LEU GLY TYR THR GLY ILE PRO THR ASP LYS GLY PRO ARG
SEQRES 19 A 250 PHE ARG LYS LEU THR SER GLN GLU ILE ASN ASP ARG LEU
SEQRES 20 A 250 GLU ALA LEU
SEQRES 1 B 244 GLY SER ARG ARG TYR ASP SER ARG THR THR ILE PHE SER
SEQRES 2 B 244 PRO GLU GLY ARG LEU TYR GLN VAL GLU TYR ALA LEU GLU
SEQRES 3 B 244 SER ILE SER HIS ALA GLY THR ALA ILE GLY ILE MET ALA
SEQRES 4 B 244 SER ASP GLY ILE VAL LEU ALA ALA GLU ARG LYS VAL THR
SEQRES 5 B 244 SER THR LEU LEU GLU GLN ASP THR SER THR GLU LYS LEU
SEQRES 6 B 244 TYR LYS LEU ASN ASP LYS ILE ALA VAL ALA VAL ALA GLY
SEQRES 7 B 244 LEU THR ALA ASP ALA GLU ILE LEU ILE ASN THR ALA ARG
SEQRES 8 B 244 ILE HIS ALA GLN ASN TYR LEU LYS THR TYR ASN GLU ASP
SEQRES 9 B 244 ILE PRO VAL GLU ILE LEU VAL ARG ARG LEU SER ASP ILE
SEQRES 10 B 244 LYS GLN GLY TYR THR GLN HIS GLY GLY LEU ARG PRO PHE
SEQRES 11 B 244 GLY VAL SER PHE ILE TYR ALA GLY TYR ASP ASP ARG TYR
SEQRES 12 B 244 GLY TYR GLN LEU TYR THR SER ASN PRO SER GLY ASN TYR
SEQRES 13 B 244 THR GLY TRP LYS ALA ILE SER VAL GLY ALA ASN THR SER
SEQRES 14 B 244 ALA ALA GLN THR LEU LEU GLN MET ASP TYR LYS ASP ASP
SEQRES 15 B 244 MET LYS VAL ASP ASP ALA ILE GLU LEU ALA LEU LYS THR
SEQRES 16 B 244 LEU SER LYS THR THR ASP SER SER ALA LEU THR TYR ASP
SEQRES 17 B 244 ARG LEU GLU PHE ALA THR ILE ARG LYS GLY ALA ASN ASP
SEQRES 18 B 244 GLY GLU VAL TYR GLN LYS ILE PHE LYS PRO GLN GLU ILE
SEQRES 19 B 244 LYS ASP ILE LEU VAL LYS THR GLY ILE THR
SEQRES 1 C 241 GLY TYR ASP ARG ALA LEU SER ILE PHE SER PRO ASP GLY
SEQRES 2 C 241 HIS ILE PHE GLN VAL GLU TYR ALA LEU GLU ALA VAL LYS
SEQRES 3 C 241 ARG GLY THR CYS ALA VAL GLY VAL LYS GLY LYS ASN CYS
SEQRES 4 C 241 VAL VAL LEU GLY CYS GLU ARG ARG SER THR LEU LYS LEU
SEQRES 5 C 241 GLN ASP THR ARG ILE THR PRO SER LYS VAL SER LYS ILE
SEQRES 6 C 241 ASP SER HIS VAL VAL LEU SER PHE SER GLY LEU ASN ALA
SEQRES 7 C 241 ASP SER ARG ILE LEU ILE GLU LYS ALA ARG VAL GLU ALA
SEQRES 8 C 241 GLN SER HIS ARG LEU THR LEU GLU ASP PRO VAL THR VAL
SEQRES 9 C 241 GLU TYR LEU THR ARG TYR VAL ALA GLY VAL GLN GLN ARG
SEQRES 10 C 241 TYR THR GLN SER GLY GLY VAL ARG PRO PHE GLY VAL SER
SEQRES 11 C 241 THR LEU ILE ALA GLY PHE ASP PRO ARG ASP ASP GLU PRO
SEQRES 12 C 241 LYS LEU TYR GLN THR GLU PRO SER GLY ILE TYR SER SER
SEQRES 13 C 241 TRP SER ALA GLN THR ILE GLY ARG ASN SER LYS THR VAL
SEQRES 14 C 241 ARG GLU PHE LEU GLU LYS ASN TYR ASP ARG LYS GLU PRO
SEQRES 15 C 241 PRO ALA THR VAL GLU GLU CYS VAL LYS LEU THR VAL ARG
SEQRES 16 C 241 SER LEU LEU GLU VAL VAL GLN THR GLY ALA LYS ASN ILE
SEQRES 17 C 241 GLU ILE THR VAL VAL LYS PRO ASP SER ASP ILE VAL ALA
SEQRES 18 C 241 LEU SER SER GLU GLU ILE ASN GLN TYR VAL THR GLN ILE
SEQRES 19 C 241 GLU GLN GLU LYS GLN GLU GLN
SEQRES 1 D 242 ASP ARG GLY VAL SER THR PHE SER PRO GLU GLY ARG LEU
SEQRES 2 D 242 PHE GLN VAL GLU TYR SER LEU GLU ALA ILE LYS LEU GLY
SEQRES 3 D 242 SER THR ALA ILE GLY ILE ALA THR LYS GLU GLY VAL VAL
SEQRES 4 D 242 LEU GLY VAL GLU LYS ARG ALA THR SER PRO LEU LEU GLU
SEQRES 5 D 242 SER ASP SER ILE GLU LYS ILE VAL GLU ILE ASP ARG HIS
SEQRES 6 D 242 ILE GLY CYS ALA MET SER GLY LEU THR ALA ASP ALA ARG
SEQRES 7 D 242 SER MET ILE GLU HIS ALA ARG THR ALA ALA VAL THR HIS
SEQRES 8 D 242 ASN LEU TYR TYR ASP GLU ASP ILE ASN VAL GLU SER LEU
SEQRES 9 D 242 THR GLN SER VAL CYS ASP LEU ALA LEU ARG PHE GLY GLU
SEQRES 10 D 242 GLY ALA SER GLY GLU GLU ARG LEU MET SER ARG PRO PHE
SEQRES 11 D 242 GLY VAL ALA LEU LEU ILE ALA GLY HIS ASP ALA ASP ASP
SEQRES 12 D 242 GLY TYR GLN LEU PHE HIS ALA GLU PRO SER GLY THR PHE
SEQRES 13 D 242 TYR ARG TYR ASN ALA LYS ALA ILE GLY SER GLY SER GLU
SEQRES 14 D 242 GLY ALA GLN ALA GLU LEU LEU ASN GLU TRP HIS SER SER
SEQRES 15 D 242 LEU THR LEU LYS GLU ALA GLU LEU LEU VAL LEU LYS ILE
SEQRES 16 D 242 LEU LYS GLN VAL MET GLU GLU LYS LEU ASP GLU ASN ASN
SEQRES 17 D 242 ALA GLN LEU SER CYS ILE THR LYS GLN ASP GLY PHE LYS
SEQRES 18 D 242 ILE TYR ASP ASN GLU LYS THR ALA GLU LEU ILE LYS GLU
SEQRES 19 D 242 LEU LYS GLU LYS GLU ALA ALA GLU
SEQRES 1 E 233 PHE ARG ASN ASN TYR ASP GLY ASP THR VAL THR PHE SER
SEQRES 2 E 233 PRO THR GLY ARG LEU PHE GLN VAL GLU TYR ALA LEU GLU
SEQRES 3 E 233 ALA ILE LYS GLN GLY SER VAL THR VAL GLY LEU ARG SER
SEQRES 4 E 233 ASN THR HIS ALA VAL LEU VAL ALA LEU LYS ARG ASN ALA
SEQRES 5 E 233 ASP GLU LEU SER SER TYR GLN LYS LYS ILE ILE LYS CYS
SEQRES 6 E 233 ASP GLU HIS MET GLY LEU SER LEU ALA GLY LEU ALA PRO
SEQRES 7 E 233 ASP ALA ARG VAL LEU SER ASN TYR LEU ARG GLN GLN CYS
SEQRES 8 E 233 ASN TYR SER SER LEU VAL PHE ASN ARG LYS LEU ALA VAL
SEQRES 9 E 233 GLU ARG ALA GLY HIS LEU LEU CYS ASP LYS ALA GLN LYS
SEQRES 10 E 233 ASN THR GLN SER TYR GLY GLY ARG PRO TYR GLY VAL GLY
SEQRES 11 E 233 LEU LEU ILE ILE GLY TYR ASP LYS SER GLY ALA HIS LEU
SEQRES 12 E 233 LEU GLU PHE GLN PRO SER GLY ASN VAL THR GLU LEU TYR
SEQRES 13 E 233 GLY THR ALA ILE GLY ALA ARG SER GLN GLY ALA LYS THR
SEQRES 14 E 233 TYR LEU GLU ARG THR LEU ASP THR PHE ILE LYS ILE ASP
SEQRES 15 E 233 GLY ASN PRO ASP GLU LEU ILE LYS ALA GLY VAL GLU ALA
SEQRES 16 E 233 ILE SER GLN SER LEU ARG ASP GLU SER LEU THR VAL ASP
SEQRES 17 E 233 ASN LEU SER ILE ALA ILE VAL GLY LYS ASP THR PRO PHE
SEQRES 18 E 233 THR ILE TYR ASP GLY GLU ALA VAL ALA LYS TYR ILE
SEQRES 1 F 244 GLY THR GLY TYR ASP LEU SER ASN SER VAL PHE SER PRO
SEQRES 2 F 244 ASP GLY ARG ASN PHE GLN VAL GLU TYR ALA VAL LYS ALA
SEQRES 3 F 244 VAL GLU ASN GLY THR THR SER ILE GLY ILE LYS CYS ASN
SEQRES 4 F 244 ASP GLY VAL VAL PHE ALA VAL GLU LYS LEU ILE THR SER
SEQRES 5 F 244 LYS LEU LEU VAL PRO GLN LYS ASN VAL LYS ILE GLN VAL
SEQRES 6 F 244 VAL ASP ARG HIS ILE GLY CYS VAL TYR SER GLY LEU ILE
SEQRES 7 F 244 PRO ASP GLY ARG HIS LEU VAL ASN ARG GLY ARG GLU GLU
SEQRES 8 F 244 ALA ALA SER PHE LYS LYS LEU TYR LYS THR PRO ILE PRO
SEQRES 9 F 244 ILE PRO ALA PHE ALA ASP ARG LEU GLY GLN TYR VAL GLN
SEQRES 10 F 244 ALA HIS THR LEU TYR ASN SER VAL ARG PRO PHE GLY VAL
SEQRES 11 F 244 SER THR ILE PHE GLY GLY VAL ASP LYS ASN GLY ALA HIS
SEQRES 12 F 244 LEU TYR MET LEU GLU PRO SER GLY SER TYR TRP GLY TYR
SEQRES 13 F 244 LYS GLY ALA ALA THR GLY LYS GLY ARG GLN SER ALA LYS
SEQRES 14 F 244 ALA GLU LEU GLU LYS LEU VAL ASP HIS HIS PRO GLU GLY
SEQRES 15 F 244 LEU SER ALA ARG GLU ALA VAL LYS GLN ALA ALA LYS ILE
SEQRES 16 F 244 ILE TYR LEU ALA HIS GLU ASP ASN LYS GLU LYS ASP PHE
SEQRES 17 F 244 GLU LEU GLU ILE SER TRP CYS SER LEU SER GLU THR ASN
SEQRES 18 F 244 GLY LEU HIS LYS PHE VAL LYS GLY ASP LEU LEU GLN GLU
SEQRES 19 F 244 ALA ILE ASP PHE ALA GLN LYS GLU ILE ASN
SEQRES 1 G 243 ALA GLY TYR ASP ARG HIS ILE THR ILE PHE SER PRO GLU
SEQRES 2 G 243 GLY ARG LEU TYR GLN VAL GLU TYR ALA PHE LYS ALA THR
SEQRES 3 G 243 ASN GLN THR ASN ILE ASN SER LEU ALA VAL ARG GLY LYS
SEQRES 4 G 243 ASP CYS THR VAL VAL ILE SER GLN LYS LYS VAL PRO ASP
SEQRES 5 G 243 LYS LEU LEU ASP PRO THR THR VAL SER TYR ILE PHE CYS
SEQRES 6 G 243 ILE SER ARG THR ILE GLY MET VAL VAL ASN GLY PRO ILE
SEQRES 7 G 243 PRO ASP ALA ARG ASN ALA ALA LEU ARG ALA LYS ALA GLU
SEQRES 8 G 243 ALA ALA GLU PHE ARG TYR LYS TYR GLY TYR ASP MET PRO
SEQRES 9 G 243 CYS ASP VAL LEU ALA LYS ARG MET ALA ASN LEU SER GLN
SEQRES 10 G 243 ILE TYR THR GLN ARG ALA TYR MET ARG PRO LEU GLY VAL
SEQRES 11 G 243 ILE LEU THR PHE VAL SER VAL ASP GLU GLU LEU GLY PRO
SEQRES 12 G 243 SER ILE TYR LYS THR ASP PRO ALA GLY TYR TYR VAL GLY
SEQRES 13 G 243 TYR LYS ALA THR ALA THR GLY PRO LYS GLN GLN GLU ILE
SEQRES 14 G 243 THR THR ASN LEU GLU ASN HIS PHE LYS LYS SER LYS ILE
SEQRES 15 G 243 ASP HIS ILE ASN GLU GLU SER TRP GLU LYS VAL VAL GLU
SEQRES 16 G 243 PHE ALA ILE THR HIS MET ILE ASP ALA LEU GLY THR GLU
SEQRES 17 G 243 PHE SER LYS ASN ASP LEU GLU VAL GLY VAL ALA THR LYS
SEQRES 18 G 243 ASP LYS PHE PHE THR LEU SER ALA GLU ASN ILE GLU GLU
SEQRES 19 G 243 ARG LEU VAL ALA ILE ALA GLU GLN ASP
SEQRES 1 H 222 THR THR ILE VAL GLY VAL LYS PHE ASN ASN GLY VAL VAL
SEQRES 2 H 222 ILE ALA ALA ASP THR ARG SER THR GLN GLY PRO ILE VAL
SEQRES 3 H 222 ALA ASP LYS ASN CYS ALA LYS LEU HIS ARG ILE SER PRO
SEQRES 4 H 222 LYS ILE TRP CYS ALA GLY ALA GLY THR ALA ALA ASP THR
SEQRES 5 H 222 GLU ALA VAL THR GLN LEU ILE GLY SER ASN ILE GLU LEU
SEQRES 6 H 222 HIS SER LEU TYR THR SER ARG GLU PRO ARG VAL VAL SER
SEQRES 7 H 222 ALA LEU GLN MET LEU LYS GLN HIS LEU PHE LYS TYR GLN
SEQRES 8 H 222 GLY HIS ILE GLY ALA TYR LEU ILE VAL ALA GLY VAL ASP
SEQRES 9 H 222 PRO THR GLY SER HIS LEU PHE SER ILE HIS ALA HIS GLY
SEQRES 10 H 222 SER THR ASP VAL GLY TYR TYR LEU SER LEU GLY SER GLY
SEQRES 11 H 222 SER LEU ALA ALA MET ALA VAL LEU GLU SER HIS TRP LYS
SEQRES 12 H 222 GLN ASP LEU THR LYS GLU GLU ALA ILE LYS LEU ALA SER
SEQRES 13 H 222 ASP ALA ILE GLN ALA GLY ILE TRP ASN ASP LEU GLY SER
SEQRES 14 H 222 GLY SER ASN VAL ASP VAL CYS VAL MET GLU ILE GLY LYS
SEQRES 15 H 222 ASP ALA GLU TYR LEU ARG ASN TYR LEU THR PRO ASN VAL
SEQRES 16 H 222 ARG GLU GLU LYS GLN LYS SER TYR LYS PHE PRO ARG GLY
SEQRES 17 H 222 THR THR ALA VAL LEU LYS GLU SER ILE VAL ASN ILE CYS
SEQRES 18 H 222 ASP
SEQRES 1 I 204 SER ASP PRO SER SER ILE ASN GLY GLY ILE VAL VAL ALA
SEQRES 2 I 204 MET THR GLY LYS ASP CYS VAL ALA ILE ALA CYS ASP LEU
SEQRES 3 I 204 ARG LEU GLY SER GLN SER LEU GLY VAL SER ASN LYS PHE
SEQRES 4 I 204 GLU LYS ILE PHE HIS TYR GLY HIS VAL PHE LEU GLY ILE
SEQRES 5 I 204 THR GLY LEU ALA THR ASP VAL THR THR LEU ASN GLU MET
SEQRES 6 I 204 PHE ARG TYR LYS THR ASN LEU TYR LYS LEU LYS GLU GLU
SEQRES 7 I 204 ARG ALA ILE GLU PRO GLU THR PHE THR GLN LEU VAL SER
SEQRES 8 I 204 SER SER LEU TYR GLU ARG ARG PHE GLY PRO TYR PHE VAL
SEQRES 9 I 204 GLY PRO VAL VAL ALA GLY ILE ASN SER LYS SER GLY LYS
SEQRES 10 I 204 PRO PHE ILE ALA GLY PHE ASP LEU ILE GLY CYS ILE ASP
SEQRES 11 I 204 GLU ALA LYS ASP PHE ILE VAL SER GLY THR ALA SER ASP
SEQRES 12 I 204 GLN LEU PHE GLY MET CYS GLU SER LEU TYR GLU PRO ASN
SEQRES 13 I 204 LEU GLU PRO GLU ASP LEU PHE GLU THR ILE SER GLN ALA
SEQRES 14 I 204 LEU LEU ASN ALA ALA ASP ARG ASP ALA LEU SER GLY TRP
SEQRES 15 I 204 GLY ALA VAL VAL TYR ILE ILE LYS LYS ASP GLU VAL VAL
SEQRES 16 I 204 LYS ARG TYR LEU LYS MET ARG GLN ASP
SEQRES 1 J 198 MET ASP ILE ILE LEU GLY ILE ARG VAL GLN ASP SER VAL
SEQRES 2 J 198 ILE LEU ALA SER SER LYS ALA VAL THR ARG GLY ILE SER
SEQRES 3 J 198 VAL LEU LYS ASP SER ASP ASP LYS THR ARG GLN LEU SER
SEQRES 4 J 198 PRO HIS THR LEU MET SER PHE ALA GLY GLU ALA GLY ASP
SEQRES 5 J 198 THR VAL GLN PHE ALA GLU TYR ILE GLN ALA ASN ILE GLN
SEQRES 6 J 198 LEU TYR SER ILE ARG GLU ASP TYR GLU LEU SER PRO GLN
SEQRES 7 J 198 ALA VAL SER SER PHE VAL ARG GLN GLU LEU ALA LYS SER
SEQRES 8 J 198 ILE ARG SER ARG ARG PRO TYR GLN VAL ASN VAL LEU ILE
SEQRES 9 J 198 GLY GLY TYR ASP LYS LYS LYS ASN LYS PRO GLU LEU TYR
SEQRES 10 J 198 GLN ILE ASP TYR LEU GLY THR LYS VAL GLU LEU PRO TYR
SEQRES 11 J 198 GLY ALA HIS GLY TYR SER GLY PHE TYR THR PHE SER LEU
SEQRES 12 J 198 LEU ASP HIS HIS TYR ARG PRO ASP MET THR THR GLU GLU
SEQRES 13 J 198 GLY LEU ASP LEU LEU LYS LEU CYS VAL GLN GLU LEU GLU
SEQRES 14 J 198 LYS ARG MET PRO MET ASP PHE LYS GLY VAL ILE VAL LYS
SEQRES 15 J 198 ILE VAL ASP LYS ASP GLY ILE ARG GLN VAL ASP ASP PHE
SEQRES 16 J 198 GLN ALA GLN
SEQRES 1 K 212 THR THR THR LEU ALA PHE ARG PHE GLN GLY GLY ILE ILE
SEQRES 2 K 212 VAL ALA VAL ASP SER ARG ALA THR ALA GLY ASN TRP VAL
SEQRES 3 K 212 ALA SER GLN THR VAL LYS LYS VAL ILE GLU ILE ASN PRO
SEQRES 4 K 212 PHE LEU LEU GLY THR MET ALA GLY GLY ALA ALA ASP CYS
SEQRES 5 K 212 GLN PHE TRP GLU THR TRP LEU GLY SER GLN CYS ARG LEU
SEQRES 6 K 212 HIS GLU LEU ARG GLU LYS GLU ARG ILE SER VAL ALA ALA
SEQRES 7 K 212 ALA SER LYS ILE LEU SER ASN LEU VAL TYR GLN TYR LYS
SEQRES 8 K 212 GLY ALA GLY LEU SER MET GLY THR MET ILE CYS GLY TYR
SEQRES 9 K 212 THR ARG LYS GLU GLY PRO THR ILE TYR TYR VAL ASP SER
SEQRES 10 K 212 ASP GLY THR ARG LEU LYS GLY ASP ILE PHE CYS VAL GLY
SEQRES 11 K 212 SER GLY GLN THR PHE ALA TYR GLY VAL LEU ASP SER ASN
SEQRES 12 K 212 TYR LYS TRP ASP LEU SER VAL GLU ASP ALA LEU TYR LEU
SEQRES 13 K 212 GLY LYS ARG SER ILE LEU ALA ALA ALA HIS ARG ASP ALA
SEQRES 14 K 212 TYR SER GLY GLY SER VAL ASN LEU TYR HIS VAL THR GLU
SEQRES 15 K 212 ASP GLY TRP ILE TYR HIS GLY ASN HIS ASP VAL GLY GLU
SEQRES 16 K 212 LEU PHE TRP LYS VAL LYS GLU GLU GLU GLY SER PHE ASN
SEQRES 17 K 212 ASN VAL ILE GLY
SEQRES 1 L 222 GLN PHE ASN PRO TYR GLY ASP ASN GLY GLY THR ILE LEU
SEQRES 2 L 222 GLY ILE ALA GLY GLU ASP PHE ALA VAL LEU ALA GLY ASP
SEQRES 3 L 222 THR ARG ASN ILE THR ASP TYR SER ILE ASN SER ARG TYR
SEQRES 4 L 222 GLU PRO LYS VAL PHE ASP CYS GLY ASP ASN ILE VAL MET
SEQRES 5 L 222 SER ALA ASN GLY PHE ALA ALA ASP GLY ASP ALA LEU VAL
SEQRES 6 L 222 LYS ARG PHE LYS ASN SER VAL LYS TRP TYR HIS PHE ASP
SEQRES 7 L 222 HIS ASN ASP LYS LYS LEU SER ILE ASN SER ALA ALA ARG
SEQRES 8 L 222 ASN ILE GLN HIS LEU LEU TYR GLY LYS ARG PHE PHE PRO
SEQRES 9 L 222 TYR TYR VAL HIS THR ILE ILE ALA GLY LEU ASP GLU ASP
SEQRES 10 L 222 GLY LYS GLY ALA VAL TYR SER PHE ASP PRO VAL GLY SER
SEQRES 11 L 222 TYR GLU ARG GLU GLN CYS ARG ALA GLY GLY ALA ALA ALA
SEQRES 12 L 222 SER LEU ILE MET PRO PHE LEU ASP ASN GLN VAL ASN PHE
SEQRES 13 L 222 LYS ASN GLN TYR GLU PRO GLY THR ASN GLY LYS VAL LYS
SEQRES 14 L 222 LYS PRO LEU LYS TYR LEU SER VAL GLU GLU VAL ILE LYS
SEQRES 15 L 222 LEU VAL ARG ASP SER PHE THR SER ALA THR GLU ARG HIS
SEQRES 16 L 222 ILE GLN VAL GLY ASP GLY LEU GLU ILE LEU ILE VAL THR
SEQRES 17 L 222 LYS ASP GLY VAL ARG LYS GLU PHE TYR GLU LEU LYS ARG
SEQRES 18 L 222 ASP
SEQRES 1 M 233 THR GLN GLN PRO ILE VAL THR GLY THR SER VAL ILE SER
SEQRES 2 M 233 MET LYS TYR ASP ASN GLY VAL ILE ILE ALA ALA ASP ASN
SEQRES 3 M 233 LEU GLY SER TYR GLY SER LEU LEU ARG PHE ASN GLY VAL
SEQRES 4 M 233 GLU ARG LEU ILE PRO VAL GLY ASP ASN THR VAL VAL GLY
SEQRES 5 M 233 ILE SER GLY ASP ILE SER ASP MET GLN HIS ILE GLU ARG
SEQRES 6 M 233 LEU LEU LYS ASP LEU VAL THR GLU ASN ALA TYR ASP ASN
SEQRES 7 M 233 PRO LEU ALA ASP ALA GLU GLU ALA LEU GLU PRO SER TYR
SEQRES 8 M 233 ILE PHE GLU TYR LEU ALA THR VAL MET TYR GLN ARG ARG
SEQRES 9 M 233 SER LYS MET ASN PRO LEU TRP ASN ALA ILE ILE VAL ALA
SEQRES 10 M 233 GLY VAL GLN SER ASN GLY ASP GLN PHE LEU ARG TYR VAL
SEQRES 11 M 233 ASN LEU LEU GLY VAL THR TYR SER SER PRO THR LEU ALA
SEQRES 12 M 233 THR GLY PHE GLY ALA HIS MET ALA ASN PRO LEU LEU ARG
SEQRES 13 M 233 LYS VAL VAL ASP ARG GLU SER ASP ILE PRO LYS THR THR
SEQRES 14 M 233 VAL GLN VAL ALA GLU GLU ALA ILE VAL ASN ALA MET ARG
SEQRES 15 M 233 VAL LEU TYR TYR ARG ASP ALA ARG SER SER ARG ASN PHE
SEQRES 16 M 233 SER LEU ALA ILE ILE ASP LYS ASN THR GLY LEU THR PHE
SEQRES 17 M 233 LYS LYS ASN LEU GLN VAL GLU ASN MET LYS TRP ASP PHE
SEQRES 18 M 233 ALA LYS ASP ILE LYS GLY TYR GLY THR GLN LYS ILE
SEQRES 1 N 196 THR SER ILE MET ALA VAL THR PHE LYS ASP GLY VAL ILE
SEQRES 2 N 196 LEU GLY ALA ASP SER ARG THR THR THR GLY ALA TYR ILE
SEQRES 3 N 196 ALA ASN ARG VAL THR ASP LYS LEU THR ARG VAL HIS ASP
SEQRES 4 N 196 LYS ILE TRP CYS CYS ARG SER GLY SER ALA ALA ASP THR
SEQRES 5 N 196 GLN ALA ILE ALA ASP ILE VAL GLN TYR HIS LEU GLU LEU
SEQRES 6 N 196 TYR THR SER GLN TYR GLY THR PRO SER THR GLU THR ALA
SEQRES 7 N 196 ALA SER VAL PHE LYS GLU LEU CYS TYR GLU ASN LYS ASP
SEQRES 8 N 196 ASN LEU THR ALA GLY ILE ILE VAL ALA GLY TYR ASP ASP
SEQRES 9 N 196 LYS ASN LYS GLY GLU VAL TYR THR ILE PRO LEU GLY GLY
SEQRES 10 N 196 SER VAL HIS LYS LEU PRO TYR ALA ILE ALA GLY SER GLY
SEQRES 11 N 196 SER THR PHE ILE TYR GLY TYR CYS ASP LYS ASN PHE ARG
SEQRES 12 N 196 GLU ASN MET SER LYS GLU GLU THR VAL ASP PHE ILE LYS
SEQRES 13 N 196 HIS SER LEU SER GLN ALA ILE LYS TRP ASP GLY SER SER
SEQRES 14 N 196 GLY GLY VAL ILE ARG MET VAL VAL LEU THR ALA ALA GLY
SEQRES 15 N 196 VAL GLU ARG LEU ILE PHE TYR PRO ASP GLU TYR GLU GLN
SEQRES 16 N 196 LEU
SEQRES 1 O 250 MET THR ASP ARG TYR SER PHE SER LEU THR THR PHE SER
SEQRES 2 O 250 PRO SER GLY LYS LEU GLY GLN ILE ASP TYR ALA LEU THR
SEQRES 3 O 250 ALA VAL LYS GLN GLY VAL THR SER LEU GLY ILE LYS ALA
SEQRES 4 O 250 THR ASN GLY VAL VAL ILE ALA THR GLU LYS LYS SER SER
SEQRES 5 O 250 SER PRO LEU ALA MET SER GLU THR LEU SER LYS VAL SER
SEQRES 6 O 250 LEU LEU THR PRO ASP ILE GLY ALA VAL TYR SER GLY MET
SEQRES 7 O 250 GLY PRO ASP TYR ARG VAL LEU VAL ASP LYS SER ARG LYS
SEQRES 8 O 250 VAL ALA HIS THR SER TYR LYS ARG ILE TYR GLY GLU TYR
SEQRES 9 O 250 PRO PRO THR LYS LEU LEU VAL SER GLU VAL ALA LYS ILE
SEQRES 10 O 250 MET GLN GLU ALA THR GLN SER GLY GLY VAL ARG PRO PHE
SEQRES 11 O 250 GLY VAL SER LEU LEU ILE ALA GLY HIS ASP GLU PHE ASN
SEQRES 12 O 250 GLY PHE SER LEU TYR GLN VAL ASP PRO SER GLY SER TYR
SEQRES 13 O 250 PHE PRO TRP LYS ALA THR ALA ILE GLY LYS GLY SER VAL
SEQRES 14 O 250 ALA ALA LYS THR PHE LEU GLU LYS ARG TRP ASN ASP GLU
SEQRES 15 O 250 LEU GLU LEU GLU ASP ALA ILE HIS ILE ALA LEU LEU THR
SEQRES 16 O 250 LEU LYS GLU SER VAL GLU GLY GLU PHE ASN GLY ASP THR
SEQRES 17 O 250 ILE GLU LEU ALA ILE ILE GLY ASP GLU ASN PRO ASP LEU
SEQRES 18 O 250 LEU GLY TYR THR GLY ILE PRO THR ASP LYS GLY PRO ARG
SEQRES 19 O 250 PHE ARG LYS LEU THR SER GLN GLU ILE ASN ASP ARG LEU
SEQRES 20 O 250 GLU ALA LEU
SEQRES 1 P 244 GLY SER ARG ARG TYR ASP SER ARG THR THR ILE PHE SER
SEQRES 2 P 244 PRO GLU GLY ARG LEU TYR GLN VAL GLU TYR ALA LEU GLU
SEQRES 3 P 244 SER ILE SER HIS ALA GLY THR ALA ILE GLY ILE MET ALA
SEQRES 4 P 244 SER ASP GLY ILE VAL LEU ALA ALA GLU ARG LYS VAL THR
SEQRES 5 P 244 SER THR LEU LEU GLU GLN ASP THR SER THR GLU LYS LEU
SEQRES 6 P 244 TYR LYS LEU ASN ASP LYS ILE ALA VAL ALA VAL ALA GLY
SEQRES 7 P 244 LEU THR ALA ASP ALA GLU ILE LEU ILE ASN THR ALA ARG
SEQRES 8 P 244 ILE HIS ALA GLN ASN TYR LEU LYS THR TYR ASN GLU ASP
SEQRES 9 P 244 ILE PRO VAL GLU ILE LEU VAL ARG ARG LEU SER ASP ILE
SEQRES 10 P 244 LYS GLN GLY TYR THR GLN HIS GLY GLY LEU ARG PRO PHE
SEQRES 11 P 244 GLY VAL SER PHE ILE TYR ALA GLY TYR ASP ASP ARG TYR
SEQRES 12 P 244 GLY TYR GLN LEU TYR THR SER ASN PRO SER GLY ASN TYR
SEQRES 13 P 244 THR GLY TRP LYS ALA ILE SER VAL GLY ALA ASN THR SER
SEQRES 14 P 244 ALA ALA GLN THR LEU LEU GLN MET ASP TYR LYS ASP ASP
SEQRES 15 P 244 MET LYS VAL ASP ASP ALA ILE GLU LEU ALA LEU LYS THR
SEQRES 16 P 244 LEU SER LYS THR THR ASP SER SER ALA LEU THR TYR ASP
SEQRES 17 P 244 ARG LEU GLU PHE ALA THR ILE ARG LYS GLY ALA ASN ASP
SEQRES 18 P 244 GLY GLU VAL TYR GLN LYS ILE PHE LYS PRO GLN GLU ILE
SEQRES 19 P 244 LYS ASP ILE LEU VAL LYS THR GLY ILE THR
SEQRES 1 Q 241 GLY TYR ASP ARG ALA LEU SER ILE PHE SER PRO ASP GLY
SEQRES 2 Q 241 HIS ILE PHE GLN VAL GLU TYR ALA LEU GLU ALA VAL LYS
SEQRES 3 Q 241 ARG GLY THR CYS ALA VAL GLY VAL LYS GLY LYS ASN CYS
SEQRES 4 Q 241 VAL VAL LEU GLY CYS GLU ARG ARG SER THR LEU LYS LEU
SEQRES 5 Q 241 GLN ASP THR ARG ILE THR PRO SER LYS VAL SER LYS ILE
SEQRES 6 Q 241 ASP SER HIS VAL VAL LEU SER PHE SER GLY LEU ASN ALA
SEQRES 7 Q 241 ASP SER ARG ILE LEU ILE GLU LYS ALA ARG VAL GLU ALA
SEQRES 8 Q 241 GLN SER HIS ARG LEU THR LEU GLU ASP PRO VAL THR VAL
SEQRES 9 Q 241 GLU TYR LEU THR ARG TYR VAL ALA GLY VAL GLN GLN ARG
SEQRES 10 Q 241 TYR THR GLN SER GLY GLY VAL ARG PRO PHE GLY VAL SER
SEQRES 11 Q 241 THR LEU ILE ALA GLY PHE ASP PRO ARG ASP ASP GLU PRO
SEQRES 12 Q 241 LYS LEU TYR GLN THR GLU PRO SER GLY ILE TYR SER SER
SEQRES 13 Q 241 TRP SER ALA GLN THR ILE GLY ARG ASN SER LYS THR VAL
SEQRES 14 Q 241 ARG GLU PHE LEU GLU LYS ASN TYR ASP ARG LYS GLU PRO
SEQRES 15 Q 241 PRO ALA THR VAL GLU GLU CYS VAL LYS LEU THR VAL ARG
SEQRES 16 Q 241 SER LEU LEU GLU VAL VAL GLN THR GLY ALA LYS ASN ILE
SEQRES 17 Q 241 GLU ILE THR VAL VAL LYS PRO ASP SER ASP ILE VAL ALA
SEQRES 18 Q 241 LEU SER SER GLU GLU ILE ASN GLN TYR VAL THR GLN ILE
SEQRES 19 Q 241 GLU GLN GLU LYS GLN GLU GLN
SEQRES 1 R 242 ASP ARG GLY VAL SER THR PHE SER PRO GLU GLY ARG LEU
SEQRES 2 R 242 PHE GLN VAL GLU TYR SER LEU GLU ALA ILE LYS LEU GLY
SEQRES 3 R 242 SER THR ALA ILE GLY ILE ALA THR LYS GLU GLY VAL VAL
SEQRES 4 R 242 LEU GLY VAL GLU LYS ARG ALA THR SER PRO LEU LEU GLU
SEQRES 5 R 242 SER ASP SER ILE GLU LYS ILE VAL GLU ILE ASP ARG HIS
SEQRES 6 R 242 ILE GLY CYS ALA MET SER GLY LEU THR ALA ASP ALA ARG
SEQRES 7 R 242 SER MET ILE GLU HIS ALA ARG THR ALA ALA VAL THR HIS
SEQRES 8 R 242 ASN LEU TYR TYR ASP GLU ASP ILE ASN VAL GLU SER LEU
SEQRES 9 R 242 THR GLN SER VAL CYS ASP LEU ALA LEU ARG PHE GLY GLU
SEQRES 10 R 242 GLY ALA SER GLY GLU GLU ARG LEU MET SER ARG PRO PHE
SEQRES 11 R 242 GLY VAL ALA LEU LEU ILE ALA GLY HIS ASP ALA ASP ASP
SEQRES 12 R 242 GLY TYR GLN LEU PHE HIS ALA GLU PRO SER GLY THR PHE
SEQRES 13 R 242 TYR ARG TYR ASN ALA LYS ALA ILE GLY SER GLY SER GLU
SEQRES 14 R 242 GLY ALA GLN ALA GLU LEU LEU ASN GLU TRP HIS SER SER
SEQRES 15 R 242 LEU THR LEU LYS GLU ALA GLU LEU LEU VAL LEU LYS ILE
SEQRES 16 R 242 LEU LYS GLN VAL MET GLU GLU LYS LEU ASP GLU ASN ASN
SEQRES 17 R 242 ALA GLN LEU SER CYS ILE THR LYS GLN ASP GLY PHE LYS
SEQRES 18 R 242 ILE TYR ASP ASN GLU LYS THR ALA GLU LEU ILE LYS GLU
SEQRES 19 R 242 LEU LYS GLU LYS GLU ALA ALA GLU
SEQRES 1 S 233 PHE ARG ASN ASN TYR ASP GLY ASP THR VAL THR PHE SER
SEQRES 2 S 233 PRO THR GLY ARG LEU PHE GLN VAL GLU TYR ALA LEU GLU
SEQRES 3 S 233 ALA ILE LYS GLN GLY SER VAL THR VAL GLY LEU ARG SER
SEQRES 4 S 233 ASN THR HIS ALA VAL LEU VAL ALA LEU LYS ARG ASN ALA
SEQRES 5 S 233 ASP GLU LEU SER SER TYR GLN LYS LYS ILE ILE LYS CYS
SEQRES 6 S 233 ASP GLU HIS MET GLY LEU SER LEU ALA GLY LEU ALA PRO
SEQRES 7 S 233 ASP ALA ARG VAL LEU SER ASN TYR LEU ARG GLN GLN CYS
SEQRES 8 S 233 ASN TYR SER SER LEU VAL PHE ASN ARG LYS LEU ALA VAL
SEQRES 9 S 233 GLU ARG ALA GLY HIS LEU LEU CYS ASP LYS ALA GLN LYS
SEQRES 10 S 233 ASN THR GLN SER TYR GLY GLY ARG PRO TYR GLY VAL GLY
SEQRES 11 S 233 LEU LEU ILE ILE GLY TYR ASP LYS SER GLY ALA HIS LEU
SEQRES 12 S 233 LEU GLU PHE GLN PRO SER GLY ASN VAL THR GLU LEU TYR
SEQRES 13 S 233 GLY THR ALA ILE GLY ALA ARG SER GLN GLY ALA LYS THR
SEQRES 14 S 233 TYR LEU GLU ARG THR LEU ASP THR PHE ILE LYS ILE ASP
SEQRES 15 S 233 GLY ASN PRO ASP GLU LEU ILE LYS ALA GLY VAL GLU ALA
SEQRES 16 S 233 ILE SER GLN SER LEU ARG ASP GLU SER LEU THR VAL ASP
SEQRES 17 S 233 ASN LEU SER ILE ALA ILE VAL GLY LYS ASP THR PRO PHE
SEQRES 18 S 233 THR ILE TYR ASP GLY GLU ALA VAL ALA LYS TYR ILE
SEQRES 1 T 244 GLY THR GLY TYR ASP LEU SER ASN SER VAL PHE SER PRO
SEQRES 2 T 244 ASP GLY ARG ASN PHE GLN VAL GLU TYR ALA VAL LYS ALA
SEQRES 3 T 244 VAL GLU ASN GLY THR THR SER ILE GLY ILE LYS CYS ASN
SEQRES 4 T 244 ASP GLY VAL VAL PHE ALA VAL GLU LYS LEU ILE THR SER
SEQRES 5 T 244 LYS LEU LEU VAL PRO GLN LYS ASN VAL LYS ILE GLN VAL
SEQRES 6 T 244 VAL ASP ARG HIS ILE GLY CYS VAL TYR SER GLY LEU ILE
SEQRES 7 T 244 PRO ASP GLY ARG HIS LEU VAL ASN ARG GLY ARG GLU GLU
SEQRES 8 T 244 ALA ALA SER PHE LYS LYS LEU TYR LYS THR PRO ILE PRO
SEQRES 9 T 244 ILE PRO ALA PHE ALA ASP ARG LEU GLY GLN TYR VAL GLN
SEQRES 10 T 244 ALA HIS THR LEU TYR ASN SER VAL ARG PRO PHE GLY VAL
SEQRES 11 T 244 SER THR ILE PHE GLY GLY VAL ASP LYS ASN GLY ALA HIS
SEQRES 12 T 244 LEU TYR MET LEU GLU PRO SER GLY SER TYR TRP GLY TYR
SEQRES 13 T 244 LYS GLY ALA ALA THR GLY LYS GLY ARG GLN SER ALA LYS
SEQRES 14 T 244 ALA GLU LEU GLU LYS LEU VAL ASP HIS HIS PRO GLU GLY
SEQRES 15 T 244 LEU SER ALA ARG GLU ALA VAL LYS GLN ALA ALA LYS ILE
SEQRES 16 T 244 ILE TYR LEU ALA HIS GLU ASP ASN LYS GLU LYS ASP PHE
SEQRES 17 T 244 GLU LEU GLU ILE SER TRP CYS SER LEU SER GLU THR ASN
SEQRES 18 T 244 GLY LEU HIS LYS PHE VAL LYS GLY ASP LEU LEU GLN GLU
SEQRES 19 T 244 ALA ILE ASP PHE ALA GLN LYS GLU ILE ASN
SEQRES 1 U 243 ALA GLY TYR ASP ARG HIS ILE THR ILE PHE SER PRO GLU
SEQRES 2 U 243 GLY ARG LEU TYR GLN VAL GLU TYR ALA PHE LYS ALA THR
SEQRES 3 U 243 ASN GLN THR ASN ILE ASN SER LEU ALA VAL ARG GLY LYS
SEQRES 4 U 243 ASP CYS THR VAL VAL ILE SER GLN LYS LYS VAL PRO ASP
SEQRES 5 U 243 LYS LEU LEU ASP PRO THR THR VAL SER TYR ILE PHE CYS
SEQRES 6 U 243 ILE SER ARG THR ILE GLY MET VAL VAL ASN GLY PRO ILE
SEQRES 7 U 243 PRO ASP ALA ARG ASN ALA ALA LEU ARG ALA LYS ALA GLU
SEQRES 8 U 243 ALA ALA GLU PHE ARG TYR LYS TYR GLY TYR ASP MET PRO
SEQRES 9 U 243 CYS ASP VAL LEU ALA LYS ARG MET ALA ASN LEU SER GLN
SEQRES 10 U 243 ILE TYR THR GLN ARG ALA TYR MET ARG PRO LEU GLY VAL
SEQRES 11 U 243 ILE LEU THR PHE VAL SER VAL ASP GLU GLU LEU GLY PRO
SEQRES 12 U 243 SER ILE TYR LYS THR ASP PRO ALA GLY TYR TYR VAL GLY
SEQRES 13 U 243 TYR LYS ALA THR ALA THR GLY PRO LYS GLN GLN GLU ILE
SEQRES 14 U 243 THR THR ASN LEU GLU ASN HIS PHE LYS LYS SER LYS ILE
SEQRES 15 U 243 ASP HIS ILE ASN GLU GLU SER TRP GLU LYS VAL VAL GLU
SEQRES 16 U 243 PHE ALA ILE THR HIS MET ILE ASP ALA LEU GLY THR GLU
SEQRES 17 U 243 PHE SER LYS ASN ASP LEU GLU VAL GLY VAL ALA THR LYS
SEQRES 18 U 243 ASP LYS PHE PHE THR LEU SER ALA GLU ASN ILE GLU GLU
SEQRES 19 U 243 ARG LEU VAL ALA ILE ALA GLU GLN ASP
SEQRES 1 V 222 THR THR ILE VAL GLY VAL LYS PHE ASN ASN GLY VAL VAL
SEQRES 2 V 222 ILE ALA ALA ASP THR ARG SER THR GLN GLY PRO ILE VAL
SEQRES 3 V 222 ALA ASP LYS ASN CYS ALA LYS LEU HIS ARG ILE SER PRO
SEQRES 4 V 222 LYS ILE TRP CYS ALA GLY ALA GLY THR ALA ALA ASP THR
SEQRES 5 V 222 GLU ALA VAL THR GLN LEU ILE GLY SER ASN ILE GLU LEU
SEQRES 6 V 222 HIS SER LEU TYR THR SER ARG GLU PRO ARG VAL VAL SER
SEQRES 7 V 222 ALA LEU GLN MET LEU LYS GLN HIS LEU PHE LYS TYR GLN
SEQRES 8 V 222 GLY HIS ILE GLY ALA TYR LEU ILE VAL ALA GLY VAL ASP
SEQRES 9 V 222 PRO THR GLY SER HIS LEU PHE SER ILE HIS ALA HIS GLY
SEQRES 10 V 222 SER THR ASP VAL GLY TYR TYR LEU SER LEU GLY SER GLY
SEQRES 11 V 222 SER LEU ALA ALA MET ALA VAL LEU GLU SER HIS TRP LYS
SEQRES 12 V 222 GLN ASP LEU THR LYS GLU GLU ALA ILE LYS LEU ALA SER
SEQRES 13 V 222 ASP ALA ILE GLN ALA GLY ILE TRP ASN ASP LEU GLY SER
SEQRES 14 V 222 GLY SER ASN VAL ASP VAL CYS VAL MET GLU ILE GLY LYS
SEQRES 15 V 222 ASP ALA GLU TYR LEU ARG ASN TYR LEU THR PRO ASN VAL
SEQRES 16 V 222 ARG GLU GLU LYS GLN LYS SER TYR LYS PHE PRO ARG GLY
SEQRES 17 V 222 THR THR ALA VAL LEU LYS GLU SER ILE VAL ASN ILE CYS
SEQRES 18 V 222 ASP
SEQRES 1 W 204 SER ASP PRO SER SER ILE ASN GLY GLY ILE VAL VAL ALA
SEQRES 2 W 204 MET THR GLY LYS ASP CYS VAL ALA ILE ALA CYS ASP LEU
SEQRES 3 W 204 ARG LEU GLY SER GLN SER LEU GLY VAL SER ASN LYS PHE
SEQRES 4 W 204 GLU LYS ILE PHE HIS TYR GLY HIS VAL PHE LEU GLY ILE
SEQRES 5 W 204 THR GLY LEU ALA THR ASP VAL THR THR LEU ASN GLU MET
SEQRES 6 W 204 PHE ARG TYR LYS THR ASN LEU TYR LYS LEU LYS GLU GLU
SEQRES 7 W 204 ARG ALA ILE GLU PRO GLU THR PHE THR GLN LEU VAL SER
SEQRES 8 W 204 SER SER LEU TYR GLU ARG ARG PHE GLY PRO TYR PHE VAL
SEQRES 9 W 204 GLY PRO VAL VAL ALA GLY ILE ASN SER LYS SER GLY LYS
SEQRES 10 W 204 PRO PHE ILE ALA GLY PHE ASP LEU ILE GLY CYS ILE ASP
SEQRES 11 W 204 GLU ALA LYS ASP PHE ILE VAL SER GLY THR ALA SER ASP
SEQRES 12 W 204 GLN LEU PHE GLY MET CYS GLU SER LEU TYR GLU PRO ASN
SEQRES 13 W 204 LEU GLU PRO GLU ASP LEU PHE GLU THR ILE SER GLN ALA
SEQRES 14 W 204 LEU LEU ASN ALA ALA ASP ARG ASP ALA LEU SER GLY TRP
SEQRES 15 W 204 GLY ALA VAL VAL TYR ILE ILE LYS LYS ASP GLU VAL VAL
SEQRES 16 W 204 LYS ARG TYR LEU LYS MET ARG GLN ASP
SEQRES 1 X 198 MET ASP ILE ILE LEU GLY ILE ARG VAL GLN ASP SER VAL
SEQRES 2 X 198 ILE LEU ALA SER SER LYS ALA VAL THR ARG GLY ILE SER
SEQRES 3 X 198 VAL LEU LYS ASP SER ASP ASP LYS THR ARG GLN LEU SER
SEQRES 4 X 198 PRO HIS THR LEU MET SER PHE ALA GLY GLU ALA GLY ASP
SEQRES 5 X 198 THR VAL GLN PHE ALA GLU TYR ILE GLN ALA ASN ILE GLN
SEQRES 6 X 198 LEU TYR SER ILE ARG GLU ASP TYR GLU LEU SER PRO GLN
SEQRES 7 X 198 ALA VAL SER SER PHE VAL ARG GLN GLU LEU ALA LYS SER
SEQRES 8 X 198 ILE ARG SER ARG ARG PRO TYR GLN VAL ASN VAL LEU ILE
SEQRES 9 X 198 GLY GLY TYR ASP LYS LYS LYS ASN LYS PRO GLU LEU TYR
SEQRES 10 X 198 GLN ILE ASP TYR LEU GLY THR LYS VAL GLU LEU PRO TYR
SEQRES 11 X 198 GLY ALA HIS GLY TYR SER GLY PHE TYR THR PHE SER LEU
SEQRES 12 X 198 LEU ASP HIS HIS TYR ARG PRO ASP MET THR THR GLU GLU
SEQRES 13 X 198 GLY LEU ASP LEU LEU LYS LEU CYS VAL GLN GLU LEU GLU
SEQRES 14 X 198 LYS ARG MET PRO MET ASP PHE LYS GLY VAL ILE VAL LYS
SEQRES 15 X 198 ILE VAL ASP LYS ASP GLY ILE ARG GLN VAL ASP ASP PHE
SEQRES 16 X 198 GLN ALA GLN
SEQRES 1 Y 212 THR THR THR LEU ALA PHE ARG PHE GLN GLY GLY ILE ILE
SEQRES 2 Y 212 VAL ALA VAL ASP SER ARG ALA THR ALA GLY ASN TRP VAL
SEQRES 3 Y 212 ALA SER GLN THR VAL LYS LYS VAL ILE GLU ILE ASN PRO
SEQRES 4 Y 212 PHE LEU LEU GLY THR MET ALA GLY GLY ALA ALA ASP CYS
SEQRES 5 Y 212 GLN PHE TRP GLU THR TRP LEU GLY SER GLN CYS ARG LEU
SEQRES 6 Y 212 HIS GLU LEU ARG GLU LYS GLU ARG ILE SER VAL ALA ALA
SEQRES 7 Y 212 ALA SER LYS ILE LEU SER ASN LEU VAL TYR GLN TYR LYS
SEQRES 8 Y 212 GLY ALA GLY LEU SER MET GLY THR MET ILE CYS GLY TYR
SEQRES 9 Y 212 THR ARG LYS GLU GLY PRO THR ILE TYR TYR VAL ASP SER
SEQRES 10 Y 212 ASP GLY THR ARG LEU LYS GLY ASP ILE PHE CYS VAL GLY
SEQRES 11 Y 212 SER GLY GLN THR PHE ALA TYR GLY VAL LEU ASP SER ASN
SEQRES 12 Y 212 TYR LYS TRP ASP LEU SER VAL GLU ASP ALA LEU TYR LEU
SEQRES 13 Y 212 GLY LYS ARG SER ILE LEU ALA ALA ALA HIS ARG ASP ALA
SEQRES 14 Y 212 TYR SER GLY GLY SER VAL ASN LEU TYR HIS VAL THR GLU
SEQRES 15 Y 212 ASP GLY TRP ILE TYR HIS GLY ASN HIS ASP VAL GLY GLU
SEQRES 16 Y 212 LEU PHE TRP LYS VAL LYS GLU GLU GLU GLY SER PHE ASN
SEQRES 17 Y 212 ASN VAL ILE GLY
SEQRES 1 Z 222 GLN PHE ASN PRO TYR GLY ASP ASN GLY GLY THR ILE LEU
SEQRES 2 Z 222 GLY ILE ALA GLY GLU ASP PHE ALA VAL LEU ALA GLY ASP
SEQRES 3 Z 222 THR ARG ASN ILE THR ASP TYR SER ILE ASN SER ARG TYR
SEQRES 4 Z 222 GLU PRO LYS VAL PHE ASP CYS GLY ASP ASN ILE VAL MET
SEQRES 5 Z 222 SER ALA ASN GLY PHE ALA ALA ASP GLY ASP ALA LEU VAL
SEQRES 6 Z 222 LYS ARG PHE LYS ASN SER VAL LYS TRP TYR HIS PHE ASP
SEQRES 7 Z 222 HIS ASN ASP LYS LYS LEU SER ILE ASN SER ALA ALA ARG
SEQRES 8 Z 222 ASN ILE GLN HIS LEU LEU TYR GLY LYS ARG PHE PHE PRO
SEQRES 9 Z 222 TYR TYR VAL HIS THR ILE ILE ALA GLY LEU ASP GLU ASP
SEQRES 10 Z 222 GLY LYS GLY ALA VAL TYR SER PHE ASP PRO VAL GLY SER
SEQRES 11 Z 222 TYR GLU ARG GLU GLN CYS ARG ALA GLY GLY ALA ALA ALA
SEQRES 12 Z 222 SER LEU ILE MET PRO PHE LEU ASP ASN GLN VAL ASN PHE
SEQRES 13 Z 222 LYS ASN GLN TYR GLU PRO GLY THR ASN GLY LYS VAL LYS
SEQRES 14 Z 222 LYS PRO LEU LYS TYR LEU SER VAL GLU GLU VAL ILE LYS
SEQRES 15 Z 222 LEU VAL ARG ASP SER PHE THR SER ALA THR GLU ARG HIS
SEQRES 16 Z 222 ILE GLN VAL GLY ASP GLY LEU GLU ILE LEU ILE VAL THR
SEQRES 17 Z 222 LYS ASP GLY VAL ARG LYS GLU PHE TYR GLU LEU LYS ARG
SEQRES 18 Z 222 ASP
SEQRES 1 1 233 THR GLN GLN PRO ILE VAL THR GLY THR SER VAL ILE SER
SEQRES 2 1 233 MET LYS TYR ASP ASN GLY VAL ILE ILE ALA ALA ASP ASN
SEQRES 3 1 233 LEU GLY SER TYR GLY SER LEU LEU ARG PHE ASN GLY VAL
SEQRES 4 1 233 GLU ARG LEU ILE PRO VAL GLY ASP ASN THR VAL VAL GLY
SEQRES 5 1 233 ILE SER GLY ASP ILE SER ASP MET GLN HIS ILE GLU ARG
SEQRES 6 1 233 LEU LEU LYS ASP LEU VAL THR GLU ASN ALA TYR ASP ASN
SEQRES 7 1 233 PRO LEU ALA ASP ALA GLU GLU ALA LEU GLU PRO SER TYR
SEQRES 8 1 233 ILE PHE GLU TYR LEU ALA THR VAL MET TYR GLN ARG ARG
SEQRES 9 1 233 SER LYS MET ASN PRO LEU TRP ASN ALA ILE ILE VAL ALA
SEQRES 10 1 233 GLY VAL GLN SER ASN GLY ASP GLN PHE LEU ARG TYR VAL
SEQRES 11 1 233 ASN LEU LEU GLY VAL THR TYR SER SER PRO THR LEU ALA
SEQRES 12 1 233 THR GLY PHE GLY ALA HIS MET ALA ASN PRO LEU LEU ARG
SEQRES 13 1 233 LYS VAL VAL ASP ARG GLU SER ASP ILE PRO LYS THR THR
SEQRES 14 1 233 VAL GLN VAL ALA GLU GLU ALA ILE VAL ASN ALA MET ARG
SEQRES 15 1 233 VAL LEU TYR TYR ARG ASP ALA ARG SER SER ARG ASN PHE
SEQRES 16 1 233 SER LEU ALA ILE ILE ASP LYS ASN THR GLY LEU THR PHE
SEQRES 17 1 233 LYS LYS ASN LEU GLN VAL GLU ASN MET LYS TRP ASP PHE
SEQRES 18 1 233 ALA LYS ASP ILE LYS GLY TYR GLY THR GLN LYS ILE
SEQRES 1 2 196 THR SER ILE MET ALA VAL THR PHE LYS ASP GLY VAL ILE
SEQRES 2 2 196 LEU GLY ALA ASP SER ARG THR THR THR GLY ALA TYR ILE
SEQRES 3 2 196 ALA ASN ARG VAL THR ASP LYS LEU THR ARG VAL HIS ASP
SEQRES 4 2 196 LYS ILE TRP CYS CYS ARG SER GLY SER ALA ALA ASP THR
SEQRES 5 2 196 GLN ALA ILE ALA ASP ILE VAL GLN TYR HIS LEU GLU LEU
SEQRES 6 2 196 TYR THR SER GLN TYR GLY THR PRO SER THR GLU THR ALA
SEQRES 7 2 196 ALA SER VAL PHE LYS GLU LEU CYS TYR GLU ASN LYS ASP
SEQRES 8 2 196 ASN LEU THR ALA GLY ILE ILE VAL ALA GLY TYR ASP ASP
SEQRES 9 2 196 LYS ASN LYS GLY GLU VAL TYR THR ILE PRO LEU GLY GLY
SEQRES 10 2 196 SER VAL HIS LYS LEU PRO TYR ALA ILE ALA GLY SER GLY
SEQRES 11 2 196 SER THR PHE ILE TYR GLY TYR CYS ASP LYS ASN PHE ARG
SEQRES 12 2 196 GLU ASN MET SER LYS GLU GLU THR VAL ASP PHE ILE LYS
SEQRES 13 2 196 HIS SER LEU SER GLN ALA ILE LYS TRP ASP GLY SER SER
SEQRES 14 2 196 GLY GLY VAL ILE ARG MET VAL VAL LEU THR ALA ALA GLY
SEQRES 15 2 196 VAL GLU ARG LEU ILE PHE TYR PRO ASP GLU TYR GLU GLN
SEQRES 16 2 196 LEU
HET BIQ H1000 48
HET BIQ V1001 48
HETNAM BIQ BENZYL [12-(2-AMINO-2-OXOETHYL)-4-NITRO-10,13-DIOXO-15-
HETNAM 2 BIQ [(PROPYLAMINO)CARBONYL]-2-OXA-11,14-DIAZATRICYCLO[15
HETNAM 3 BIQ .2.2.1~3,7~]DOCOSA-1(19),3(22),4,6,17,20-HEXAEN-9-
HETNAM 4 BIQ YL]CARBAMATE
FORMUL 29 BIQ 2(C33 H36 N6 O9)
FORMUL 31 HOH *1070(H2 O)
HELIX 1 1 LEU A 21 GLN A 33 1 13
HELIX 2 2 MET A 60 LEU A 64 5 5
HELIX 3 3 MET A 81 SER A 99 1 19
HELIX 4 4 TYR A 100 GLY A 104 1 6
HELIX 5 5 PRO A 108 ALA A 123 1 16
HELIX 6 6 GLY A 168 TRP A 180 1 13
HELIX 7 7 GLU A 185 VAL A 202 1 17
HELIX 8 8 ASN A 21B LEU A 21G 5 5
HELIX 9 9 THR A 225 ALA A 235 1 11
HELIX 10 10 SER B 5 ASP B 9 5 5
HELIX 11 11 LEU B 21 SER B 32 1 12
HELIX 12 12 LEU B 81 ASN B 104 1 24
HELIX 13 13 PRO B 108 HIS B 126 1 19
HELIX 14 14 ASN B 168 TYR B 180 1 13
HELIX 15 15 LYS B 185 THR B 202 1 17
HELIX 16 16 THR B 206 ASP B 208 5 3
HELIX 17 17 LYS B 225 THR B 236 1 12
HELIX 18 18 ILE C 21 ARG C 33 1 13
HELIX 19 19 LEU C 81 GLU C 104 1 24
HELIX 20 20 THR C 108 TYR C 123 1 16
HELIX 21 21 ASN C 168 LYS C 178 1 11
HELIX 22 22 THR C 185 GLN C 202 1 18
HELIX 23 23 GLY C 206 LYS C 208 5 3
HELIX 24 24 SER C 225 GLU C 242 1 18
HELIX 25 25 LEU D 21 LEU D 33 1 13
HELIX 26 26 GLU D 60 ILE D 64 5 5
HELIX 27 27 THR D 82 ASP D 84 5 3
HELIX 28 28 ALA D 85 ASP D 104 1 20
HELIX 29 29 ASN D 108 LEU D 121 1 14
HELIX 30 30 GLY D 168 TRP D 180 1 13
HELIX 31 31 THR D 185 MET D 201 1 17
HELIX 32 32 ASP D 225 ALA D 243 1 18
HELIX 33 33 PHE E 4 TYR E 8 5 5
HELIX 34 34 LEU E 21 GLN E 33 1 13
HELIX 35 35 LEU E 81 ASN E 104 1 24
HELIX 36 36 ALA E 108 ASN E 123 1 16
HELIX 37 37 SER E 169 ILE E 18D 1 16
HELIX 38 38 ASN E 185 SER E 198 1 14
HELIX 39 39 GLN E 199 LEU E 201 5 3
HELIX 40 40 GLY E 226 LYS E 231 1 6
HELIX 41 41 ASN F 21 ASN F 33 1 13
HELIX 42 42 LEU F 81 LYS F 104 1 24
HELIX 43 43 PRO F 108 HIS F 123 1 16
HELIX 44 44 GLY F 168 HIS F 18B 1 15
HELIX 45 45 SER F 185 HIS F 202 1 17
HELIX 46 46 GLU F 203 LYS F 206 5 4
HELIX 47 47 LYS F 225 ILE F 240 1 16
HELIX 48 48 LEU G 21 THR G 31 1 11
HELIX 49 49 ASP G 60 VAL G 64 5 5
HELIX 50 50 PRO G 81 GLY G 104 1 24
HELIX 51 51 PRO G 108 ARG G 126 1 19
HELIX 52 52 LYS G 168 LYS G 17E 1 17
HELIX 53 53 SER G 18M GLY G 202 1 18
HELIX 54 54 SER G 225 GLU G 238 1 14
HELIX 55 55 THR H 48 SER H 71 1 24
HELIX 56 56 ARG H 75 TYR H 90 1 16
HELIX 57 57 GLY H 130 TRP H 142 1 13
HELIX 58 58 THR H 147 ASP H 166 1 20
HELIX 59 59 ASP I -7 ILE I -3 5 5
HELIX 60 60 LEU I 48 GLU I 71 1 24
HELIX 61 61 GLU I 75 GLU I 89 1 15
HELIX 62 62 ALA I 130 TYR I 142 1 13
HELIX 63 63 GLU I 147 ASP I 164 1 18
HELIX 64 64 GLY J 50 ASP J 71 1 22
HELIX 65 65 SER J 75 ARG J 90B 1 18
HELIX 66 66 TYR J 129 TYR J 142 1 14
HELIX 67 67 THR J 147 MET J 166 1 20
HELIX 68 68 GLY K 48 LYS K 71 1 24
HELIX 69 69 SER K 75 TYR K 90 1 16
HELIX 70 70 GLY K 130 TYR K 142 1 13
HELIX 71 71 SER K 147 ASP K 166 1 20
HELIX 72 72 VAL K 192 GLY K 204 1 13
HELIX 73 73 PHE L 48 HIS L 70 1 23
HELIX 74 74 SER L 75 GLY L 89 1 15
HELIX 75 75 ALA L 130 VAL L 142 1 13
HELIX 76 76 SER L 147 HIS L 166 1 20
HELIX 77 77 ILE M 49 TYR M 68 1 20
HELIX 78 78 GLU M 75 LYS M 92A 1 19
HELIX 79 79 GLY M 128 ARG M 139 1 12
HELIX 80 80 ARG M 14C ILE M 14G 5 5
HELIX 81 81 THR M 147 ASP M 166 1 20
HELIX 82 82 TRP M 197 ASP M 202 5 6
HELIX 83 83 SER N 48 GLY N 72 1 24
HELIX 84 84 SER N 75 ASN N 90 1 16
HELIX 85 85 GLY N 128 PHE N 133 5 6
HELIX 86 86 ILE N 134 PHE N 142 1 9
HELIX 87 87 SER N 147 ASP N 166 1 20
HELIX 88 88 TYR N 18C GLU N 18H 1 6
HELIX 89 89 LEU O 21 GLY O 34 1 14
HELIX 90 90 MET O 60 LEU O 64 5 5
HELIX 91 91 MET O 81 SER O 99 1 19
HELIX 92 92 TYR O 100 GLY O 104 1 6
HELIX 93 93 PRO O 108 ALA O 123 1 16
HELIX 94 94 GLY O 168 TRP O 180 1 13
HELIX 95 95 GLU O 185 VAL O 202 1 17
HELIX 96 96 ASN O 21B LEU O 21G 5 5
HELIX 97 97 THR O 225 ALA O 235 1 11
HELIX 98 98 SER P 5 ASP P 9 5 5
HELIX 99 99 LEU P 21 SER P 32 1 12
HELIX 100 100 LEU P 81 ASN P 104 1 24
HELIX 101 101 PRO P 108 HIS P 126 1 19
HELIX 102 102 ASN P 168 TYR P 180 1 13
HELIX 103 103 LYS P 185 THR P 202 1 17
HELIX 104 104 THR P 206 ASP P 208 5 3
HELIX 105 105 LYS P 225 THR P 236 1 12
HELIX 106 106 ILE Q 21 ARG Q 33 1 13
HELIX 107 107 LEU Q 81 GLU Q 104 1 24
HELIX 108 108 THR Q 108 TYR Q 123 1 16
HELIX 109 109 ASN Q 168 LYS Q 178 1 11
HELIX 110 110 THR Q 185 GLN Q 202 1 18
HELIX 111 111 GLY Q 206 LYS Q 208 5 3
HELIX 112 112 SER Q 225 GLU Q 242 1 18
HELIX 113 113 LEU R 21 LEU R 33 1 13
HELIX 114 114 GLU R 60 ILE R 64 5 5
HELIX 115 115 THR R 82 ASP R 84 5 3
HELIX 116 116 ALA R 85 ASP R 104 1 20
HELIX 117 117 ASN R 108 LEU R 121 1 14
HELIX 118 118 GLY R 168 TRP R 180 1 13
HELIX 119 119 THR R 185 MET R 201 1 17
HELIX 120 120 ASP R 225 ALA R 243 1 18
HELIX 121 121 PHE S 4 TYR S 8 5 5
HELIX 122 122 LEU S 21 GLN S 33 1 13
HELIX 123 123 LEU S 81 ASN S 104 1 24
HELIX 124 124 ALA S 108 ASN S 123 1 16
HELIX 125 125 SER S 169 ILE S 18D 1 16
HELIX 126 126 ASN S 185 GLN S 199 1 15
HELIX 127 127 GLY S 226 LYS S 231 1 6
HELIX 128 128 ASN T 21 ASN T 33 1 13
HELIX 129 129 LEU T 81 LYS T 104 1 24
HELIX 130 130 PRO T 108 HIS T 123 1 16
HELIX 131 131 GLY T 168 HIS T 18B 1 15
HELIX 132 132 SER T 185 HIS T 202 1 17
HELIX 133 133 GLU T 203 LYS T 206 5 4
HELIX 134 134 LYS T 225 ILE T 240 1 16
HELIX 135 135 LEU U 21 THR U 31 1 11
HELIX 136 136 ASP U 60 VAL U 64 5 5
HELIX 137 137 PRO U 81 GLY U 104 1 24
HELIX 138 138 PRO U 108 ARG U 126 1 19
HELIX 139 139 LYS U 168 LYS U 17E 1 17
HELIX 140 140 SER U 18M GLY U 202 1 18
HELIX 141 141 SER U 225 GLU U 238 1 14
HELIX 142 142 THR V 48 SER V 71 1 24
HELIX 143 143 ARG V 75 TYR V 90 1 16
HELIX 144 144 GLY V 130 TRP V 142 1 13
HELIX 145 145 THR V 147 ASP V 166 1 20
HELIX 146 146 ASP W -7 ILE W -3 5 5
HELIX 147 147 LEU W 48 GLU W 71 1 24
HELIX 148 148 GLU W 75 GLU W 89 1 15
HELIX 149 149 ALA W 130 TYR W 142 1 13
HELIX 150 150 GLU W 147 ASP W 164 1 18
HELIX 151 151 GLY X 50 ASP X 71 1 22
HELIX 152 152 SER X 75 ARG X 90B 1 18
HELIX 153 153 TYR X 129 TYR X 142 1 14
HELIX 154 154 THR X 147 MET X 166 1 20
HELIX 155 155 GLY Y 48 LYS Y 71 1 24
HELIX 156 156 SER Y 75 TYR Y 90 1 16
HELIX 157 157 GLY Y 130 TYR Y 142 1 13
HELIX 158 158 SER Y 147 ASP Y 166 1 20
HELIX 159 159 VAL Y 192 GLY Y 204 1 13
HELIX 160 160 PHE Z 48 HIS Z 70 1 23
HELIX 161 161 SER Z 75 GLY Z 89 1 15
HELIX 162 162 ALA Z 130 VAL Z 142 1 13
HELIX 163 163 SER Z 147 HIS Z 166 1 20
HELIX 164 164 ILE 1 49 TYR 1 68 1 20
HELIX 165 165 GLU 1 75 LYS 1 92A 1 19
HELIX 166 166 GLY 1 128 ARG 1 139 1 12
HELIX 167 167 ARG 1 14C ILE 1 14G 5 5
HELIX 168 168 THR 1 147 ASP 1 166 1 20
HELIX 169 169 TRP 1 197 ASP 1 202 5 6
HELIX 170 170 SER 2 48 GLY 2 72 1 24
HELIX 171 171 SER 2 75 ASN 2 90 1 16
HELIX 172 172 GLY 2 128 PHE 2 133 5 6
HELIX 173 173 ILE 2 134 PHE 2 142 1 9
HELIX 174 174 SER 2 147 ASP 2 166 1 20
HELIX 175 175 TYR 2 18C GLU 2 18H 1 6
SHEET 1 A 5 ALA A 162 ILE A 165 0
SHEET 2 A 5 SER A 37 ALA A 42 -1 N SER A 37 O ILE A 165
SHEET 3 A 5 GLY A 45 GLU A 51 -1 O GLY A 45 N ALA A 42
SHEET 4 A 5 ILE A 210 ILE A 215 -1 O ALA A 213 N ILE A 48
SHEET 5 A 5 PHE A 221 LYS A 223 -1 O ARG A 222 N ILE A 214
SHEET 1 B 5 SER A 68 THR A 71 0
SHEET 2 B 5 ILE A 74 GLY A 80 -1 O ILE A 74 N LEU A 70
SHEET 3 B 5 VAL A 134 ASP A 142 -1 O ALA A 139 N GLY A 75
SHEET 4 B 5 GLY A 146 VAL A 151 -1 O TYR A 149 N ILE A 138
SHEET 5 B 5 TYR A 157 PRO A 159 -1 O PHE A 158 N GLN A 150
SHEET 1 C 6 TYR A 21I THR A 21J 0
SHEET 2 C 6 ALA H 184 LEU H 192 1 O TYR H 186 N THR A 21J
SHEET 3 C 6 VAL H 173 GLU H 179 -1 N VAL H 175 O LEU H 187
SHEET 4 C 6 GLY H 11 ALA H 16 -1 N ALA H 16 O ASP H 174
SHEET 5 C 6 ILE H 3 PHE H 8 -1 N VAL H 6 O VAL H 13
SHEET 6 C 6 TYR H 124 LEU H 127 -1 O LEU H 125 N GLY H 5
SHEET 1 D 5 ALA B 162 VAL B 165 0
SHEET 2 D 5 ALA B 37 ALA B 42 -1 N GLY B 39 O ILE B 163
SHEET 3 D 5 GLY B 45 GLU B 51 -1 O ALA B 49 N ILE B 38
SHEET 4 D 5 LEU B 210 ARG B 216 -1 O ALA B 213 N LEU B 48
SHEET 5 D 5 TYR B 220 ILE B 223 -1 O TYR B 220 N ARG B 216
SHEET 1 E 5 LEU B 67 LYS B 69 0
SHEET 2 E 5 ILE B 74 GLY B 80 -1 O VAL B 76 N TYR B 68
SHEET 3 E 5 VAL B 134 ASP B 142 -1 O ALA B 139 N ALA B 75
SHEET 4 E 5 GLY B 145 SER B 151 -1 O GLN B 147 N GLY B 140
SHEET 5 E 5 TYR B 157 GLY B 159 -1 O THR B 158 N THR B 150
SHEET 1 F 5 ALA C 162 ILE C 165 0
SHEET 2 F 5 ALA C 37 LYS C 41 -1 N ALA C 37 O ILE C 165
SHEET 3 F 5 VAL C 46 GLU C 51 -1 O GLY C 49 N VAL C 38
SHEET 4 F 5 ILE C 210 LYS C 216 -1 O THR C 213 N LEU C 48
SHEET 5 F 5 ASP C 220 ALA C 223 -1 O ASP C 220 N LYS C 216
SHEET 1 G 5 SER C 68 LYS C 69 0
SHEET 2 G 5 VAL C 74 GLY C 80 -1 O LEU C 76 N SER C 68
SHEET 3 G 5 VAL C 134 GLY C 140 -1 O ALA C 139 N VAL C 75
SHEET 4 G 5 LYS C 147 THR C 151 -1 O TYR C 149 N ILE C 138
SHEET 5 G 5 TYR C 157 SER C 159 -1 O SER C 158 N GLN C 150
SHEET 1 H 5 ALA D 162 ILE D 165 0
SHEET 2 H 5 ALA D 37 THR D 42 -1 N GLY D 39 O LYS D 163
SHEET 3 H 5 GLY D 45 GLU D 51 -1 O GLY D 49 N ILE D 38
SHEET 4 H 5 ALA D 210 THR D 216 -1 O SER D 213 N LEU D 48
SHEET 5 H 5 GLY D 220 ILE D 223 -1 O GLY D 220 N THR D 216
SHEET 1 I 5 ILE D 67 ASP D 71 0
SHEET 2 I 5 ILE D 74 GLY D 80 -1 O CYS D 76 N VAL D 68
SHEET 3 I 5 VAL D 134 ASP D 142 -1 O LEU D 137 N ALA D 77
SHEET 4 I 5 GLY D 145 ALA D 151 -1 O GLN D 147 N GLY D 140
SHEET 5 I 5 PHE D 157 TYR D 160 -1 O TYR D 158 N HIS D 150
SHEET 1 J 5 GLY E 162 ILE E 165 0
SHEET 2 J 5 THR E 37 ARG E 41 -1 N GLY E 39 O THR E 163
SHEET 3 J 5 HIS E 45 LEU E 51 -1 O VAL E 49 N VAL E 38
SHEET 4 J 5 LEU E 210 GLY E 216 -1 O ALA E 213 N LEU E 48
SHEET 5 J 5 THR E 219 ASP E 225 -1 O TYR E 224 N ILE E 212
SHEET 1 K 5 ILE E 67 ASP E 71 0
SHEET 2 K 5 MET E 74 GLY E 80 -1 O LEU E 76 N ILE E 68
SHEET 3 K 5 VAL E 134 ASP E 142 -1 O GLY E 135 N ALA E 79
SHEET 4 K 5 GLY E 145 PHE E 151 -1 O PHE E 151 N LEU E 136
SHEET 5 K 5 VAL E 157 GLU E 159 -1 O THR E 158 N GLU E 150
SHEET 1 L 5 GLY F 162 THR F 165 0
SHEET 2 L 5 SER F 37 CYS F 42 -1 N GLY F 39 O ALA F 163
SHEET 3 L 5 GLY F 45 LEU F 53 -1 O ALA F 49 N ILE F 38
SHEET 4 L 5 PHE F 208 SER F 216 -1 O SER F 213 N PHE F 48
SHEET 5 L 5 LYS F 222 PHE F 223 -1 O LYS F 222 N TRP F 214
SHEET 1 M 5 GLN F 68 VAL F 70 0
SHEET 2 M 5 ILE F 74 GLY F 80 -1 O CYS F 76 N GLN F 68
SHEET 3 M 5 VAL F 134 ASP F 142 -1 O ILE F 137 N VAL F 77
SHEET 4 M 5 GLY F 145 LEU F 151 -1 O GLY F 145 N ASP F 142
SHEET 5 M 5 TYR F 157 GLY F 159 -1 O TRP F 158 N MET F 150
SHEET 1 N 5 ALA G 162 THR G 165 0
SHEET 2 N 5 SER G 37 ARG G 41 -1 N SER G 37 O THR G 165
SHEET 3 N 5 CYS G 45 GLN G 51 -1 O VAL G 47 N VAL G 40
SHEET 4 N 5 LEU G 210 THR G 216 -1 O ALA G 215 N THR G 46
SHEET 5 N 5 LYS G 220 THR G 223 -1 O LYS G 220 N THR G 216
SHEET 1 O 5 ILE G 67 CYS G 69 0
SHEET 2 O 5 GLY G 75 ASN G 79 -1 O MET G 76 N PHE G 68
SHEET 3 O 5 ILE G 135 ASP G 142 -1 O VAL G 139 N GLY G 75
SHEET 4 O 5 GLY G 145 THR G 151 -1 O TYR G 149 N PHE G 138
SHEET 5 O 5 TYR G 157 GLY G 159 -1 O VAL G 158 N LYS G 150
SHEET 1 P 2 SER H 20 GLN H 22 0
SHEET 2 P 2 ILE H 25 ASP H 28 -1 O ASP H 28 N SER H 20
SHEET 1 Q 5 LEU H 34 SER H 38 0
SHEET 2 Q 5 ILE H 41 GLY H 47 -1 O CYS H 43 N HIS H 35
SHEET 3 Q 5 ALA H 97 ASP H 105 -1 O TYR H 98 N ALA H 46
SHEET 4 Q 5 GLY H 107 ILE H 113 -1 O ILE H 113 N LEU H 99
SHEET 5 Q 5 THR H 119 VAL H 121 -1 O ASP H 120 N SER H 112
SHEET 1 R 6 VAL H 213 ILE H 218 0
SHEET 2 R 6 VAL I 184 LEU I 189 -1 O LYS I 186 N SER H 217
SHEET 3 R 6 ALA I 173 LYS I 179 -1 N VAL I 175 O ARG I 187
SHEET 4 R 6 CYS I 11 ASP I 17 -1 N VAL I 12 O ILE I 178
SHEET 5 R 6 ILE I 2 GLY I 8 -1 N MET I 6 O ALA I 13
SHEET 6 R 6 PHE I 124 GLY I 128 -1 O ILE I 125 N ALA I 5
SHEET 1 S 2 LEU I 20 SER I 22 0
SHEET 2 S 2 LEU I 25 SER I 28 -1 O VAL I 27 N LEU I 20
SHEET 1 T 5 ILE I 34 TYR I 38 0
SHEET 2 T 5 VAL I 41 GLY I 47 -1 O LEU I 43 N PHE I 35
SHEET 3 T 5 VAL I 97 ILE I 104 -1 O VAL I 100 N GLY I 44
SHEET 4 T 5 PRO I 108 PHE I 113 -1 O ALA I 111 N VAL I 101
SHEET 5 T 5 ILE I 119 ASP I 120 -1 O ASP I 120 N GLY I 112
SHEET 1 U 5 TYR J 124 ALA J 126 0
SHEET 2 U 5 ILE J 3 ARG J 7 -1 N GLY J 5 O GLY J 125
SHEET 3 U 5 SER J 11 SER J 17 -1 O ILE J 13 N ILE J 6
SHEET 4 U 5 VAL J 173 ASP J 179 -1 O ILE J 174 N SER J 16
SHEET 5 U 5 GLY J 183 VAL J 187 -1 O ARG J 185 N ILE J 177
SHEET 1 V 2 VAL J 20 ARG J 22 0
SHEET 2 V 2 SER J 25 LYS J 28 -1 O SER J 25 N ARG J 22
SHEET 1 W 5 THR J 34 SER J 38 0
SHEET 2 W 5 THR J 41 GLY J 47 -1 O MET J 43 N ARG J 35
SHEET 3 W 5 VAL J 97 ASP J 105 -1 O GLY J 102 N LEU J 42
SHEET 4 W 5 LYS J 107 ILE J 113 -1 O ILE J 113 N VAL J 99
SHEET 5 W 5 LYS J 119 GLU J 121 -1 O VAL J 120 N GLN J 112
SHEET 1 X 5 ILE K 124 VAL K 127 0
SHEET 2 X 5 THR K 3 PHE K 8 -1 N THR K 3 O VAL K 127
SHEET 3 X 5 GLY K 11 VAL K 16 -1 O GLY K 11 N PHE K 8
SHEET 4 X 5 SER K 172 THR K 179 -1 O VAL K 178 N ILE K 12
SHEET 5 X 5 GLY K 183 ASP K 191 -1 O ILE K 185 N HIS K 177
SHEET 1 Y 2 ALA K 20 ALA K 22 0
SHEET 2 Y 2 TRP K 25 SER K 28 -1 O TRP K 25 N ALA K 22
SHEET 1 Z 5 VAL K 34 ASN K 38 0
SHEET 2 Z 5 LEU K 41 THR K 44 -1 O GLY K 43 N ILE K 35
SHEET 3 Z 5 GLY K 98 THR K 105 -1 O CYS K 102 N LEU K 42
SHEET 4 Z 5 GLY K 107 ASP K 114 -1 O GLY K 107 N THR K 105
SHEET 5 Z 5 ARG K 119 LYS K 121 -1 O LEU K 120 N TYR K 112
SHEET 1 AA 5 CYS L 124 GLY L 128 0
SHEET 2 AA 5 THR L 2 ALA L 7 -1 N ILE L 3 O GLY L 127
SHEET 3 AA 5 ALA L 12 ASP L 17 -1 O ALA L 15 N LEU L 4
SHEET 4 AA 5 GLY L 172 THR L 179 -1 O VAL L 178 N ALA L 12
SHEET 5 AA 5 GLY L 183 GLU L 190 -1 O TYR L 189 N LEU L 173
SHEET 1 AB 2 ASN L 20 THR L 22 0
SHEET 2 AB 2 SER L 25 SER L 28 -1 O ASN L 27 N ASN L 20
SHEET 1 AC 5 PHE L 35 ASP L 36 0
SHEET 2 AC 5 VAL L 42 GLY L 47 -1 O MET L 43 N PHE L 35
SHEET 3 AC 5 VAL L 97 LEU L 104 -1 O HIS L 98 N ASN L 46
SHEET 4 AC 5 GLY L 108 PHE L 113 -1 O PHE L 113 N THR L 99
SHEET 5 AC 5 TYR L 119 GLU L 122 -1 O GLU L 122 N VAL L 110
SHEET 1 AD 5 LEU M 25 PHE M 28 0
SHEET 2 AD 5 GLY M 20 TYR M 22 -1 N GLY M 20 O PHE M 28
SHEET 3 AD 5 VAL M -3 GLY M -1 -1 N THR M -2 O SER M 21
SHEET 4 AD 5 THR M 41 ASP M 48 -1 O GLY M 47 N GLY M -1
SHEET 5 AD 5 LEU M 34 VAL M 37 -1 N ILE M 35 O VAL M 43
SHEET 1 AE 7 LEU M 25 PHE M 28 0
SHEET 2 AE 7 GLY M 20 TYR M 22 -1 N GLY M 20 O PHE M 28
SHEET 3 AE 7 VAL M -3 GLY M -1 -1 N THR M -2 O SER M 21
SHEET 4 AE 7 THR M 41 ASP M 48 -1 O GLY M 47 N GLY M -1
SHEET 5 AE 7 ASN M 97 VAL M 104 -1 O ILE M 100 N GLY M 44
SHEET 6 AE 7 GLN M 108 ASN M 114 -1 O PHE M 109 N GLY M 103
SHEET 7 AE 7 THR M 119 SER M 121 -1 O TYR M 120 N TYR M 112
SHEET 1 AF 5 THR M 124 ALA M 126 0
SHEET 2 AF 5 VAL M 3 LYS M 7 -1 N SER M 5 O LEU M 125
SHEET 3 AF 5 GLY M 11 ASP M 17 -1 O ILE M 13 N MET M 6
SHEET 4 AF 5 ASN M 172 ASP M 179 -1 O ALA M 176 N ILE M 14
SHEET 5 AF 5 GLY M 183 GLN M 191 -1 O GLY M 183 N ASP M 179
SHEET 1 AG 5 TYR N 124 ALA N 127 0
SHEET 2 AG 5 ILE N 3 PHE N 8 -1 N ILE N 3 O ALA N 127
SHEET 3 AG 5 GLY N 11 ALA N 16 -1 O GLY N 15 N MET N 4
SHEET 4 AG 5 ILE N 173 THR N 179 -1 O LEU N 178 N VAL N 12
SHEET 5 AG 5 GLY N 183 PHE N 18B-1 O LEU N 187 N MET N 175
SHEET 1 AH 2 THR N 20 THR N 22 0
SHEET 2 AH 2 TYR N 25 ASN N 28 -1 O ASN N 28 N THR N 20
SHEET 1 AI 5 LEU N 34 HIS N 38 0
SHEET 2 AI 5 ILE N 41 GLY N 47 -1 O CYS N 43 N THR N 35
SHEET 3 AI 5 ALA N 97 ASP N 105 -1 O GLY N 98 N SER N 46
SHEET 4 AI 5 LYS N 107 ILE N 113 -1 O TYR N 111 N VAL N 101
SHEET 5 AI 5 HIS N 120 LEU N 122 -1 O HIS N 120 N THR N 112
SHEET 1 AJ 5 ALA O 162 ILE O 165 0
SHEET 2 AJ 5 SER O 37 ALA O 42 -1 N SER O 37 O ILE O 165
SHEET 3 AJ 5 GLY O 45 GLU O 51 -1 O GLY O 45 N ALA O 42
SHEET 4 AJ 5 ILE O 210 ILE O 215 -1 O ALA O 213 N ILE O 48
SHEET 5 AJ 5 PHE O 221 LYS O 223 -1 O ARG O 222 N ILE O 214
SHEET 1 AK 5 SER O 68 THR O 71 0
SHEET 2 AK 5 ILE O 74 GLY O 80 -1 O ILE O 74 N LEU O 70
SHEET 3 AK 5 VAL O 134 ASP O 142 -1 O ALA O 139 N GLY O 75
SHEET 4 AK 5 GLY O 146 VAL O 151 -1 O TYR O 149 N ILE O 138
SHEET 5 AK 5 TYR O 157 PRO O 159 -1 O PHE O 158 N GLN O 150
SHEET 1 AL 6 TYR O 21I THR O 21J 0
SHEET 2 AL 6 ALA V 184 LEU V 192 1 O TYR V 186 N THR O 21J
SHEET 3 AL 6 VAL V 173 GLU V 179 -1 N VAL V 175 O LEU V 187
SHEET 4 AL 6 GLY V 11 ALA V 16 -1 N ALA V 16 O ASP V 174
SHEET 5 AL 6 ILE V 3 PHE V 8 -1 N VAL V 6 O VAL V 13
SHEET 6 AL 6 TYR V 124 LEU V 127 -1 O LEU V 125 N GLY V 5
SHEET 1 AM 5 ALA P 162 VAL P 165 0
SHEET 2 AM 5 ALA P 37 ALA P 42 -1 N GLY P 39 O ILE P 163
SHEET 3 AM 5 GLY P 45 GLU P 51 -1 O ALA P 49 N ILE P 38
SHEET 4 AM 5 LEU P 210 ARG P 216 -1 O ALA P 213 N LEU P 48
SHEET 5 AM 5 TYR P 220 ILE P 223 -1 O TYR P 220 N ARG P 216
SHEET 1 AN 5 LEU P 67 LYS P 69 0
SHEET 2 AN 5 ILE P 74 GLY P 80 -1 O VAL P 76 N TYR P 68
SHEET 3 AN 5 VAL P 134 ASP P 142 -1 O ALA P 139 N ALA P 75
SHEET 4 AN 5 GLY P 145 SER P 151 -1 O GLN P 147 N GLY P 140
SHEET 5 AN 5 TYR P 157 GLY P 159 -1 O THR P 158 N THR P 150
SHEET 1 AO 5 ALA Q 162 ILE Q 165 0
SHEET 2 AO 5 ALA Q 37 LYS Q 41 -1 N ALA Q 37 O ILE Q 165
SHEET 3 AO 5 VAL Q 46 GLU Q 51 -1 O GLY Q 49 N VAL Q 38
SHEET 4 AO 5 ILE Q 210 LYS Q 216 -1 O THR Q 213 N LEU Q 48
SHEET 5 AO 5 ASP Q 220 ALA Q 223 -1 O ASP Q 220 N LYS Q 216
SHEET 1 AP 5 SER Q 68 LYS Q 69 0
SHEET 2 AP 5 VAL Q 74 GLY Q 80 -1 O LEU Q 76 N SER Q 68
SHEET 3 AP 5 VAL Q 134 GLY Q 140 -1 O ALA Q 139 N VAL Q 75
SHEET 4 AP 5 LYS Q 147 THR Q 151 -1 O TYR Q 149 N ILE Q 138
SHEET 5 AP 5 TYR Q 157 SER Q 159 -1 O SER Q 158 N GLN Q 150
SHEET 1 AQ 5 ALA R 162 ILE R 165 0
SHEET 2 AQ 5 ALA R 37 THR R 42 -1 N GLY R 39 O LYS R 163
SHEET 3 AQ 5 GLY R 45 GLU R 51 -1 O GLY R 49 N ILE R 38
SHEET 4 AQ 5 ALA R 210 THR R 216 -1 O SER R 213 N LEU R 48
SHEET 5 AQ 5 GLY R 220 ILE R 223 -1 O GLY R 220 N THR R 216
SHEET 1 AR 5 ILE R 67 ASP R 71 0
SHEET 2 AR 5 ILE R 74 GLY R 80 -1 O ILE R 74 N ILE R 70
SHEET 3 AR 5 VAL R 134 ASP R 142 -1 O LEU R 137 N ALA R 77
SHEET 4 AR 5 GLY R 145 ALA R 151 -1 O GLN R 147 N GLY R 140
SHEET 5 AR 5 PHE R 157 TYR R 160 -1 O TYR R 158 N HIS R 150
SHEET 1 AS 5 GLY S 162 ILE S 165 0
SHEET 2 AS 5 THR S 37 ARG S 41 -1 N GLY S 39 O THR S 163
SHEET 3 AS 5 HIS S 45 LEU S 51 -1 O VAL S 49 N VAL S 38
SHEET 4 AS 5 LEU S 210 GLY S 216 -1 O ALA S 213 N LEU S 48
SHEET 5 AS 5 THR S 219 ASP S 225 -1 O TYR S 224 N ILE S 212
SHEET 1 AT 5 ILE S 67 ASP S 71 0
SHEET 2 AT 5 MET S 74 GLY S 80 -1 O LEU S 76 N ILE S 68
SHEET 3 AT 5 VAL S 134 ASP S 142 -1 O GLY S 135 N ALA S 79
SHEET 4 AT 5 GLY S 145 PHE S 151 -1 O PHE S 151 N LEU S 136
SHEET 5 AT 5 VAL S 157 GLU S 159 -1 O THR S 158 N GLU S 150
SHEET 1 AU 5 GLY T 162 THR T 165 0
SHEET 2 AU 5 SER T 37 CYS T 42 -1 N GLY T 39 O ALA T 163
SHEET 3 AU 5 GLY T 45 LEU T 53 -1 O ALA T 49 N ILE T 38
SHEET 4 AU 5 PHE T 208 SER T 216 -1 O SER T 213 N PHE T 48
SHEET 5 AU 5 LYS T 222 PHE T 223 -1 O LYS T 222 N TRP T 214
SHEET 1 AV 5 GLN T 68 VAL T 70 0
SHEET 2 AV 5 ILE T 74 GLY T 80 -1 O CYS T 76 N GLN T 68
SHEET 3 AV 5 VAL T 134 ASP T 142 -1 O ILE T 137 N VAL T 77
SHEET 4 AV 5 GLY T 145 LEU T 151 -1 O TYR T 149 N PHE T 138
SHEET 5 AV 5 TYR T 157 GLY T 159 -1 O TRP T 158 N MET T 150
SHEET 1 AW 5 ALA U 162 THR U 165 0
SHEET 2 AW 5 SER U 37 ARG U 41 -1 N SER U 37 O THR U 165
SHEET 3 AW 5 CYS U 45 GLN U 51 -1 O VAL U 47 N VAL U 40
SHEET 4 AW 5 LEU U 210 THR U 216 -1 O ALA U 215 N THR U 46
SHEET 5 AW 5 LYS U 220 THR U 223 -1 O LYS U 220 N THR U 216
SHEET 1 AX 5 ILE U 67 CYS U 69 0
SHEET 2 AX 5 GLY U 75 ASN U 79 -1 O MET U 76 N PHE U 68
SHEET 3 AX 5 ILE U 135 ASP U 142 -1 O VAL U 139 N GLY U 75
SHEET 4 AX 5 GLY U 145 THR U 151 -1 O TYR U 149 N PHE U 138
SHEET 5 AX 5 TYR U 157 GLY U 159 -1 O VAL U 158 N LYS U 150
SHEET 1 AY 2 SER V 20 GLN V 22 0
SHEET 2 AY 2 ILE V 25 ASP V 28 -1 O ASP V 28 N SER V 20
SHEET 1 AZ 5 LEU V 34 SER V 38 0
SHEET 2 AZ 5 ILE V 41 GLY V 47 -1 O CYS V 43 N HIS V 35
SHEET 3 AZ 5 ALA V 97 ASP V 105 -1 O TYR V 98 N ALA V 46
SHEET 4 AZ 5 GLY V 107 ILE V 113 -1 O ILE V 113 N LEU V 99
SHEET 5 AZ 5 THR V 119 VAL V 121 -1 O ASP V 120 N SER V 112
SHEET 1 BA 6 VAL V 213 ILE V 218 0
SHEET 2 BA 6 VAL W 184 LEU W 189 -1 O LYS W 186 N SER V 217
SHEET 3 BA 6 ALA W 173 LYS W 179 -1 N VAL W 175 O ARG W 187
SHEET 4 BA 6 CYS W 11 ASP W 17 -1 N VAL W 12 O ILE W 178
SHEET 5 BA 6 ILE W 2 GLY W 8 -1 N MET W 6 O ALA W 13
SHEET 6 BA 6 PHE W 124 GLY W 128 -1 O ILE W 125 N ALA W 5
SHEET 1 BB 2 LEU W 20 SER W 22 0
SHEET 2 BB 2 LEU W 25 SER W 28 -1 O VAL W 27 N LEU W 20
SHEET 1 BC 5 ILE W 34 TYR W 38 0
SHEET 2 BC 5 VAL W 41 GLY W 47 -1 O LEU W 43 N PHE W 35
SHEET 3 BC 5 VAL W 97 ILE W 104 -1 O ALA W 102 N PHE W 42
SHEET 4 BC 5 PRO W 108 PHE W 113 -1 O ALA W 111 N VAL W 101
SHEET 5 BC 5 ILE W 119 ASP W 120 -1 O ASP W 120 N GLY W 112
SHEET 1 BD 5 TYR X 124 ALA X 126 0
SHEET 2 BD 5 ILE X 3 ARG X 7 -1 N GLY X 5 O GLY X 125
SHEET 3 BD 5 SER X 11 SER X 17 -1 O ILE X 13 N ILE X 6
SHEET 4 BD 5 VAL X 173 ASP X 179 -1 O LYS X 176 N LEU X 14
SHEET 5 BD 5 GLY X 183 VAL X 187 -1 O ARG X 185 N ILE X 177
SHEET 1 BE 2 VAL X 20 ARG X 22 0
SHEET 2 BE 2 SER X 25 LYS X 28 -1 O SER X 25 N ARG X 22
SHEET 1 BF 5 THR X 34 SER X 38 0
SHEET 2 BF 5 THR X 41 GLY X 47 -1 O MET X 43 N ARG X 35
SHEET 3 BF 5 VAL X 97 ASP X 105 -1 O GLY X 102 N LEU X 42
SHEET 4 BF 5 LYS X 107 ILE X 113 -1 O ILE X 113 N VAL X 99
SHEET 5 BF 5 LYS X 119 GLU X 121 -1 O VAL X 120 N GLN X 112
SHEET 1 BG 5 ILE Y 124 VAL Y 127 0
SHEET 2 BG 5 THR Y 3 PHE Y 8 -1 N THR Y 3 O VAL Y 127
SHEET 3 BG 5 GLY Y 11 VAL Y 16 -1 O GLY Y 11 N PHE Y 8
SHEET 4 BG 5 SER Y 172 THR Y 179 -1 O VAL Y 178 N ILE Y 12
SHEET 5 BG 5 GLY Y 183 ASP Y 191 -1 O ILE Y 185 N HIS Y 177
SHEET 1 BH 2 ALA Y 20 ALA Y 22 0
SHEET 2 BH 2 TRP Y 25 SER Y 28 -1 O TRP Y 25 N ALA Y 22
SHEET 1 BI 5 VAL Y 34 ASN Y 38 0
SHEET 2 BI 5 LEU Y 41 THR Y 44 -1 O GLY Y 43 N ILE Y 35
SHEET 3 BI 5 GLY Y 98 THR Y 105 -1 O CYS Y 102 N LEU Y 42
SHEET 4 BI 5 GLY Y 107 ASP Y 114 -1 O GLY Y 107 N THR Y 105
SHEET 5 BI 5 ARG Y 119 LYS Y 121 -1 O LEU Y 120 N TYR Y 112
SHEET 1 BJ 5 CYS Z 124 GLY Z 128 0
SHEET 2 BJ 5 THR Z 2 ALA Z 7 -1 N ILE Z 3 O GLY Z 127
SHEET 3 BJ 5 ALA Z 12 ASP Z 17 -1 O ALA Z 15 N LEU Z 4
SHEET 4 BJ 5 GLY Z 172 THR Z 179 -1 O VAL Z 178 N ALA Z 12
SHEET 5 BJ 5 GLY Z 183 GLU Z 190 -1 O TYR Z 189 N LEU Z 173
SHEET 1 BK 2 ASN Z 20 THR Z 22 0
SHEET 2 BK 2 SER Z 25 SER Z 28 -1 O ASN Z 27 N ASN Z 20
SHEET 1 BL 5 PHE Z 35 ASP Z 36 0
SHEET 2 BL 5 VAL Z 42 GLY Z 47 -1 O MET Z 43 N PHE Z 35
SHEET 3 BL 5 VAL Z 97 LEU Z 104 -1 O HIS Z 98 N ASN Z 46
SHEET 4 BL 5 GLY Z 108 PHE Z 113 -1 O PHE Z 113 N THR Z 99
SHEET 5 BL 5 TYR Z 119 GLU Z 122 -1 O GLU Z 122 N VAL Z 110
SHEET 1 BM 5 LEU 1 25 PHE 1 28 0
SHEET 2 BM 5 GLY 1 20 TYR 1 22 -1 N GLY 1 20 O PHE 1 28
SHEET 3 BM 5 VAL 1 -3 GLY 1 -1 -1 N THR 1 -2 O SER 1 21
SHEET 4 BM 5 THR 1 41 ASP 1 48 -1 O GLY 1 47 N GLY 1 -1
SHEET 5 BM 5 LEU 1 34 VAL 1 37 -1 N ILE 1 35 O VAL 1 43
SHEET 1 BN 7 LEU 1 25 PHE 1 28 0
SHEET 2 BN 7 GLY 1 20 TYR 1 22 -1 N GLY 1 20 O PHE 1 28
SHEET 3 BN 7 VAL 1 -3 GLY 1 -1 -1 N THR 1 -2 O SER 1 21
SHEET 4 BN 7 THR 1 41 ASP 1 48 -1 O GLY 1 47 N GLY 1 -1
SHEET 5 BN 7 ASN 1 97 VAL 1 104 -1 O ALA 1 102 N VAL 1 42
SHEET 6 BN 7 GLN 1 108 ASN 1 114 -1 O PHE 1 109 N GLY 1 103
SHEET 7 BN 7 THR 1 119 SER 1 121 -1 O TYR 1 120 N TYR 1 112
SHEET 1 BO 5 THR 1 124 ALA 1 126 0
SHEET 2 BO 5 VAL 1 3 LYS 1 7 -1 N SER 1 5 O LEU 1 125
SHEET 3 BO 5 GLY 1 11 ASP 1 17 -1 O ILE 1 13 N MET 1 6
SHEET 4 BO 5 ASN 1 172 ASP 1 179 -1 O ALA 1 176 N ILE 1 14
SHEET 5 BO 5 GLY 1 183 GLN 1 191 -1 O GLY 1 183 N ASP 1 179
SHEET 1 BP 5 TYR 2 124 ALA 2 127 0
SHEET 2 BP 5 ILE 2 3 PHE 2 8 -1 N ILE 2 3 O ALA 2 127
SHEET 3 BP 5 GLY 2 11 ALA 2 16 -1 O GLY 2 15 N MET 2 4
SHEET 4 BP 5 ILE 2 173 THR 2 179 -1 O LEU 2 178 N VAL 2 12
SHEET 5 BP 5 GLY 2 183 PHE 2 18B-1 O LEU 2 187 N MET 2 175
SHEET 1 BQ 2 THR 2 20 THR 2 22 0
SHEET 2 BQ 2 TYR 2 25 ASN 2 28 -1 O ASN 2 28 N THR 2 20
SHEET 1 BR 5 LEU 2 34 HIS 2 38 0
SHEET 2 BR 5 ILE 2 41 GLY 2 47 -1 O CYS 2 43 N THR 2 35
SHEET 3 BR 5 ALA 2 97 ASP 2 105 -1 O GLY 2 98 N SER 2 46
SHEET 4 BR 5 LYS 2 107 ILE 2 113 -1 O TYR 2 111 N VAL 2 101
SHEET 5 BR 5 HIS 2 120 LEU 2 122 -1 O HIS 2 120 N THR 2 112
SITE 1 AC1 14 THR H 1 SER H 20 THR H 21 GLN H 22
SITE 2 AC1 14 ALA H 27 LYS H 33 GLY H 45 GLY H 47
SITE 3 AC1 14 THR H 48 ALA H 49 HOH H1028 ASP I 114
SITE 4 AC1 14 LEU I 115 HOH I 237
SITE 1 AC2 13 THR V 1 SER V 20 THR V 21 GLN V 22
SITE 2 AC2 13 ALA V 27 LYS V 33 GLY V 45 GLY V 47
SITE 3 AC2 13 THR V 48 ALA V 49 HOH V1034 ASP W 114
SITE 4 AC2 13 LEU W 115
CRYST1 136.425 300.962 144.762 90.00 113.17 90.00 P 1 21 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 0.007330 0.000000 0.003137 0.00000
SCALE2 0.000000 0.003323 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007514 0.00000
(ATOM LINES ARE NOT SHOWN.)
END