HEADER HYDROLASE 15-NOV-07 2ZCY
TITLE YEAST 20S PROTEASOME:SYRINGOLIN A-COMPLEX
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 MOL_ID: 2;
COMPND 8 MOLECULE: PROTEASOME COMPONENT Y13;
COMPND 9 CHAIN: B, P;
COMPND 10 SYNONYM: MACROPAIN SUBUNIT Y13, PROTEINASE YSCE SUBUNIT 13,
COMPND 11 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT Y13;
COMPND 12 EC: 3.4.25.1;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: PROTEASOME COMPONENT PRE6;
COMPND 15 CHAIN: C, Q;
COMPND 16 SYNONYM: MACROPAIN SUBUNIT PRE6, PROTEINASE YSCE SUBUNIT PRE6,
COMPND 17 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT PRE6;
COMPND 18 EC: 3.4.25.1;
COMPND 19 MOL_ID: 4;
COMPND 20 MOLECULE: PROTEASOME COMPONENT PUP2;
COMPND 21 CHAIN: D, R;
COMPND 22 SYNONYM: MACROPAIN SUBUNIT PUP2, PROTEINASE YSCE SUBUNIT PUP2,
COMPND 23 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT PUP2;
COMPND 24 EC: 3.4.25.1;
COMPND 25 MOL_ID: 5;
COMPND 26 MOLECULE: PROTEASOME COMPONENT PRE5;
COMPND 27 CHAIN: E, S;
COMPND 28 SYNONYM: MACROPAIN SUBUNIT PRE5, PROTEINASE YSCE SUBUNIT PRE5,
COMPND 29 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT PRE5;
COMPND 30 EC: 3.4.25.1;
COMPND 31 MOL_ID: 6;
COMPND 32 MOLECULE: PROTEASOME COMPONENT C1;
COMPND 33 CHAIN: F, T;
COMPND 34 SYNONYM: MACROPAIN SUBUNIT C1, PROTEINASE YSCE SUBUNIT 1,
COMPND 35 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C1;
COMPND 36 EC: 3.4.25.1;
COMPND 37 MOL_ID: 7;
COMPND 38 MOLECULE: PROTEASOME COMPONENT C7-ALPHA;
COMPND 39 CHAIN: G, U;
COMPND 40 SYNONYM: MACROPAIN SUBUNIT C7- ALPHA, PROTEINASE YSCE SUBUNIT 7,
COMPND 41 MULTICATALYTIC ENDOPEPTIDASE COMPLEX C7, PROTEASOME COMPONENT Y8,
COMPND 42 SCL1 SUPPRESSOR PROTEIN;
COMPND 43 EC: 3.4.25.1;
COMPND 44 MOL_ID: 8;
COMPND 45 MOLECULE: PROTEASOME COMPONENT PUP1;
COMPND 46 CHAIN: H, V;
COMPND 47 SYNONYM: MACROPAIN SUBUNIT PUP1, PROTEINASE YSCE SUBUNIT PUP1,
COMPND 48 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT PUP1;
COMPND 49 EC: 3.4.25.1;
COMPND 50 MOL_ID: 9;
COMPND 51 MOLECULE: PROTEASOME COMPONENT PUP3;
COMPND 52 CHAIN: I, W;
COMPND 53 SYNONYM: MACROPAIN SUBUNIT PUP3, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 54 SUBUNIT PUP3;
COMPND 55 EC: 3.4.25.1;
COMPND 56 MOL_ID: 10;
COMPND 57 MOLECULE: PROTEASOME COMPONENT C11;
COMPND 58 CHAIN: J, X;
COMPND 59 SYNONYM: MACROPAIN SUBUNIT C11, PROTEINASE YSCE SUBUNIT 11,
COMPND 60 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C11;
COMPND 61 EC: 3.4.25.1;
COMPND 62 MOL_ID: 11;
COMPND 63 MOLECULE: PROTEASOME COMPONENT PRE2;
COMPND 64 CHAIN: K, Y;
COMPND 65 SYNONYM: MACROPAIN SUBUNIT PRE2, PROTEINASE YSCE SUBUNIT PRE2,
COMPND 66 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT PRE2;
COMPND 67 EC: 3.4.25.1;
COMPND 68 MOL_ID: 12;
COMPND 69 MOLECULE: PROTEASOME COMPONENT C5;
COMPND 70 CHAIN: L, Z;
COMPND 71 SYNONYM: MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C5;
COMPND 72 EC: 3.4.25.1;
COMPND 73 MOL_ID: 13;
COMPND 74 MOLECULE: PROTEASOME COMPONENT PRE4;
COMPND 75 CHAIN: M, 0;
COMPND 76 SYNONYM: MACROPAIN SUBUNIT PRE4, PROTEINASE YSCE SUBUNIT PRE4,
COMPND 77 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT PRE4;
COMPND 78 EC: 3.4.25.1;
COMPND 79 MOL_ID: 14;
COMPND 80 MOLECULE: PROTEASOME COMPONENT PRE3;
COMPND 81 CHAIN: N, 1;
COMPND 82 SYNONYM: MACROPAIN SUBUNIT PRE3, PROTEINASE YSCE SUBUNIT PRE3,
COMPND 83 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT PRE3;
COMPND 84 EC: 3.4.25.1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 STRAIN: W303;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 8 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 9 ORGANISM_TAXID: 4932;
SOURCE 10 STRAIN: W303;
SOURCE 11 MOL_ID: 3;
SOURCE 12 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 13 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 14 ORGANISM_TAXID: 4932;
SOURCE 15 STRAIN: W303;
SOURCE 16 MOL_ID: 4;
SOURCE 17 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 18 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 19 ORGANISM_TAXID: 4932;
SOURCE 20 STRAIN: W303;
SOURCE 21 MOL_ID: 5;
SOURCE 22 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 23 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 24 ORGANISM_TAXID: 4932;
SOURCE 25 STRAIN: W303;
SOURCE 26 MOL_ID: 6;
SOURCE 27 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 28 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 29 ORGANISM_TAXID: 4932;
SOURCE 30 STRAIN: W303;
SOURCE 31 MOL_ID: 7;
SOURCE 32 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 33 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 34 ORGANISM_TAXID: 4932;
SOURCE 35 STRAIN: W303;
SOURCE 36 MOL_ID: 8;
SOURCE 37 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 38 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 39 ORGANISM_TAXID: 4932;
SOURCE 40 STRAIN: W303;
SOURCE 41 MOL_ID: 9;
SOURCE 42 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 43 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 44 ORGANISM_TAXID: 4932;
SOURCE 45 STRAIN: W303;
SOURCE 46 MOL_ID: 10;
SOURCE 47 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 48 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 49 ORGANISM_TAXID: 4932;
SOURCE 50 STRAIN: W303;
SOURCE 51 MOL_ID: 11;
SOURCE 52 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 53 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 54 ORGANISM_TAXID: 4932;
SOURCE 55 STRAIN: W303;
SOURCE 56 MOL_ID: 12;
SOURCE 57 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 58 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 59 ORGANISM_TAXID: 4932;
SOURCE 60 STRAIN: W303;
SOURCE 61 MOL_ID: 13;
SOURCE 62 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 63 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 64 ORGANISM_TAXID: 4932;
SOURCE 65 STRAIN: W303;
SOURCE 66 MOL_ID: 14;
SOURCE 67 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 68 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 69 ORGANISM_TAXID: 4932;
SOURCE 70 STRAIN: W303
KEYWDS ALPHA/BETA SANDWICH, CYTOPLASM, HYDROLASE, NUCLEUS, PROTEASE,
KEYWDS 2 PROTEASOME, THREONINE PROTEASE, UBL CONJUGATION, PHOSPHOPROTEIN,
KEYWDS 3 ZYMOGEN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.GROLL,R.DUDLER,M.KAISER
REVDAT 4 01-NOV-23 2ZCY 1 REMARK LINK
REVDAT 3 24-FEB-09 2ZCY 1 VERSN
REVDAT 2 15-APR-08 2ZCY 1 JRNL
REVDAT 1 08-APR-08 2ZCY 0
JRNL AUTH M.GROLL,B.SCHELLENBERG,A.S.BACHMANN,C.R.ARCHER,R.HUBER,
JRNL AUTH 2 T.K.POWELL,S.LINDOW,M.KAISER,R.DUDLER
JRNL TITL A PLANT PATHOGEN VIRULENCE FACTOR INHIBITS THE EUKARYOTIC
JRNL TITL 2 PROTEASOME BY A NOVEL MECHANISM
JRNL REF NATURE V. 452 755 2008
JRNL REFN ISSN 0028-0836
JRNL PMID 18401409
JRNL DOI 10.1038/NATURE06782
REMARK 2
REMARK 2 RESOLUTION. 2.90 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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 3370702.060
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 230972
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) : 0.215
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 11532
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) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 36483
REMARK 3 BIN R VALUE (WORKING SET) : 0.3180
REMARK 3 BIN FREE R VALUE : 0.3400
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1976
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 : 49538
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 210
REMARK 3 SOLVENT ATOMS : 1018
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 8.83000
REMARK 3 B22 (A**2) : -24.71000
REMARK 3 B33 (A**2) : 15.88000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.22000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.36
REMARK 3 ESD FROM SIGMAA (A) : 0.49
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) : 0.42
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.54
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) : 23.20
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 : 0.35
REMARK 3 BSOL : 34.77
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 : SYR.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
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 2ZCY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-NOV-07.
REMARK 100 THE DEPOSITION ID IS D_1000027814.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JUN-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 252555
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 99.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.13500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.89
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.94
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 1.80
REMARK 200 R MERGE FOR SHELL (I) : 0.52500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 1RYP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES, 12% MPD, 30MM MGAC2, PH 6.8,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K
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 150.98200
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: 28-MERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 28-MERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 116230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 213210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -338.9 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, 0, 1
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 B 3
REMARK 465 LYS B 240
REMARK 465 LYS B 241
REMARK 465 ASP B 242
REMARK 465 GLU B 243
REMARK 465 ASP B 244
REMARK 465 GLU B 245
REMARK 465 GLU B 246
REMARK 465 ALA B 247
REMARK 465 ASP B 248
REMARK 465 GLU B 249
REMARK 465 ASP B 250
REMARK 465 MET B 251
REMARK 465 LYS B 252
REMARK 465 MET C 5
REMARK 465 SER C 6
REMARK 465 GLN C 244
REMARK 465 GLU C 245
REMARK 465 GLN C 246
REMARK 465 ASP C 247
REMARK 465 LYS C 248
REMARK 465 LYS C 249
REMARK 465 LYS C 250
REMARK 465 LYS C 251
REMARK 465 SER C 252
REMARK 465 ASN C 253
REMARK 465 HIS C 254
REMARK 465 MET D 1
REMARK 465 PHE D 2
REMARK 465 LEU D 3
REMARK 465 THR D 4
REMARK 465 ARG D 5
REMARK 465 SER D 6
REMARK 465 GLU D 7
REMARK 465 TYR D 8
REMARK 465 SER D 245
REMARK 465 PRO D 246
REMARK 465 GLU D 247
REMARK 465 GLU D 248
REMARK 465 ALA D 249
REMARK 465 ASP D 250
REMARK 465 VAL D 251
REMARK 465 GLU D 252
REMARK 465 MET D 253
REMARK 465 SER D 254
REMARK 465 MET E 3
REMARK 465 THR F 2
REMARK 465 SER F 3
REMARK 465 ILE F 4
REMARK 465 GLY F 242
REMARK 465 ASP F 243
REMARK 465 ASP F 244
REMARK 465 ASP F 245
REMARK 465 GLU F 246
REMARK 465 ASP F 247
REMARK 465 GLU F 248
REMARK 465 ASP F 249
REMARK 465 ASP F 250
REMARK 465 SER F 251
REMARK 465 ASP F 252
REMARK 465 ASN F 253
REMARK 465 VAL F 254
REMARK 465 MET F 255
REMARK 465 SER F 256
REMARK 465 SER F 257
REMARK 465 ASP F 258
REMARK 465 ASP F 259
REMARK 465 GLU F 260
REMARK 465 ASN F 261
REMARK 465 ALA F 262
REMARK 465 PRO F 263
REMARK 465 VAL F 264
REMARK 465 ALA F 265
REMARK 465 THR F 266
REMARK 465 ASN F 267
REMARK 465 ALA F 268
REMARK 465 ASN F 269
REMARK 465 ALA F 270
REMARK 465 THR F 271
REMARK 465 THR F 272
REMARK 465 ASP F 273
REMARK 465 GLN F 274
REMARK 465 GLU F 275
REMARK 465 GLY F 276
REMARK 465 ASP F 277
REMARK 465 ILE F 278
REMARK 465 HIS F 279
REMARK 465 LEU F 280
REMARK 465 GLU F 281
REMARK 465 MET G -3
REMARK 465 SER G -2
REMARK 465 GLY G -1
REMARK 465 ALA G 0
REMARK 465 ALA G 1
REMARK 465 ALA G 2
REMARK 465 ALA G 3
REMARK 465 SER G 4
REMARK 465 ALA G 5
REMARK 465 ILE H 224
REMARK 465 GLN H 225
REMARK 465 GLU H 226
REMARK 465 GLU H 227
REMARK 465 GLN H 228
REMARK 465 VAL H 229
REMARK 465 ASP H 230
REMARK 465 ILE H 231
REMARK 465 THR H 232
REMARK 465 ALA H 233
REMARK 465 MET I -9
REMARK 465 MET L -28
REMARK 465 ALA L -27
REMARK 465 THR L -26
REMARK 465 ILE L -25
REMARK 465 ALA L -24
REMARK 465 SER L -23
REMARK 465 GLU L -22
REMARK 465 TYR L -21
REMARK 465 SER L -20
REMARK 465 SER L -19
REMARK 465 GLU L -18
REMARK 465 ALA L -17
REMARK 465 SER L -16
REMARK 465 ASN L -15
REMARK 465 THR L -14
REMARK 465 PRO L -13
REMARK 465 ILE L -12
REMARK 465 GLU L -11
REMARK 465 HIS L -10
REMARK 465 MET M -41
REMARK 465 ASN M -40
REMARK 465 HIS M -39
REMARK 465 ASP M -38
REMARK 465 PRO M -37
REMARK 465 PHE M -36
REMARK 465 SER M -35
REMARK 465 TRP M -34
REMARK 465 GLY M -33
REMARK 465 ARG M -32
REMARK 465 PRO M -31
REMARK 465 ALA M -30
REMARK 465 ASP M -29
REMARK 465 SER M -28
REMARK 465 THR M -27
REMARK 465 TYR M -26
REMARK 465 GLY M -25
REMARK 465 ALA M -24
REMARK 465 TYR M -23
REMARK 465 ASN M -22
REMARK 465 THR M -21
REMARK 465 GLN M -20
REMARK 465 ILE M -19
REMARK 465 ALA M -18
REMARK 465 ASN M -17
REMARK 465 ALA M -16
REMARK 465 GLY M -15
REMARK 465 ALA M -14
REMARK 465 SER M -13
REMARK 465 PRO M -12
REMARK 465 MET M -11
REMARK 465 VAL M -10
REMARK 465 ASN M -9
REMARK 465 MET P 3
REMARK 465 LYS P 240
REMARK 465 LYS P 241
REMARK 465 ASP P 242
REMARK 465 GLU P 243
REMARK 465 ASP P 244
REMARK 465 GLU P 245
REMARK 465 GLU P 246
REMARK 465 ALA P 247
REMARK 465 ASP P 248
REMARK 465 GLU P 249
REMARK 465 ASP P 250
REMARK 465 MET P 251
REMARK 465 LYS P 252
REMARK 465 MET Q 5
REMARK 465 SER Q 6
REMARK 465 GLN Q 244
REMARK 465 GLU Q 245
REMARK 465 GLN Q 246
REMARK 465 ASP Q 247
REMARK 465 LYS Q 248
REMARK 465 LYS Q 249
REMARK 465 LYS Q 250
REMARK 465 LYS Q 251
REMARK 465 SER Q 252
REMARK 465 ASN Q 253
REMARK 465 HIS Q 254
REMARK 465 MET R 1
REMARK 465 PHE R 2
REMARK 465 LEU R 3
REMARK 465 THR R 4
REMARK 465 ARG R 5
REMARK 465 SER R 6
REMARK 465 GLU R 7
REMARK 465 TYR R 8
REMARK 465 SER R 245
REMARK 465 PRO R 246
REMARK 465 GLU R 247
REMARK 465 GLU R 248
REMARK 465 ALA R 249
REMARK 465 ASP R 250
REMARK 465 VAL R 251
REMARK 465 GLU R 252
REMARK 465 MET R 253
REMARK 465 SER R 254
REMARK 465 MET S 3
REMARK 465 THR T 2
REMARK 465 SER T 3
REMARK 465 ILE T 4
REMARK 465 GLY T 242
REMARK 465 ASP T 243
REMARK 465 ASP T 244
REMARK 465 ASP T 245
REMARK 465 GLU T 246
REMARK 465 ASP T 247
REMARK 465 GLU T 248
REMARK 465 ASP T 249
REMARK 465 ASP T 250
REMARK 465 SER T 251
REMARK 465 ASP T 252
REMARK 465 ASN T 253
REMARK 465 VAL T 254
REMARK 465 MET T 255
REMARK 465 SER T 256
REMARK 465 SER T 257
REMARK 465 ASP T 258
REMARK 465 ASP T 259
REMARK 465 GLU T 260
REMARK 465 ASN T 261
REMARK 465 ALA T 262
REMARK 465 PRO T 263
REMARK 465 VAL T 264
REMARK 465 ALA T 265
REMARK 465 THR T 266
REMARK 465 ASN T 267
REMARK 465 ALA T 268
REMARK 465 ASN T 269
REMARK 465 ALA T 270
REMARK 465 THR T 271
REMARK 465 THR T 272
REMARK 465 ASP T 273
REMARK 465 GLN T 274
REMARK 465 GLU T 275
REMARK 465 GLY T 276
REMARK 465 ASP T 277
REMARK 465 ILE T 278
REMARK 465 HIS T 279
REMARK 465 LEU T 280
REMARK 465 GLU T 281
REMARK 465 MET U -3
REMARK 465 SER U -2
REMARK 465 GLY U -1
REMARK 465 ALA U 0
REMARK 465 ALA U 1
REMARK 465 ALA U 2
REMARK 465 ALA U 3
REMARK 465 SER U 4
REMARK 465 ALA U 5
REMARK 465 ILE V 224
REMARK 465 GLN V 225
REMARK 465 GLU V 226
REMARK 465 GLU V 227
REMARK 465 GLN V 228
REMARK 465 VAL V 229
REMARK 465 ASP V 230
REMARK 465 ILE V 231
REMARK 465 THR V 232
REMARK 465 ALA V 233
REMARK 465 MET W -9
REMARK 465 MET Z -28
REMARK 465 ALA Z -27
REMARK 465 THR Z -26
REMARK 465 ILE Z -25
REMARK 465 ALA Z -24
REMARK 465 SER Z -23
REMARK 465 GLU Z -22
REMARK 465 TYR Z -21
REMARK 465 SER Z -20
REMARK 465 SER Z -19
REMARK 465 GLU Z -18
REMARK 465 ALA Z -17
REMARK 465 SER Z -16
REMARK 465 ASN Z -15
REMARK 465 THR Z -14
REMARK 465 PRO Z -13
REMARK 465 ILE Z -12
REMARK 465 GLU Z -11
REMARK 465 HIS Z -10
REMARK 465 MET 0 -41
REMARK 465 ASN 0 -40
REMARK 465 HIS 0 -39
REMARK 465 ASP 0 -38
REMARK 465 PRO 0 -37
REMARK 465 PHE 0 -36
REMARK 465 SER 0 -35
REMARK 465 TRP 0 -34
REMARK 465 GLY 0 -33
REMARK 465 ARG 0 -32
REMARK 465 PRO 0 -31
REMARK 465 ALA 0 -30
REMARK 465 ASP 0 -29
REMARK 465 SER 0 -28
REMARK 465 THR 0 -27
REMARK 465 TYR 0 -26
REMARK 465 GLY 0 -25
REMARK 465 ALA 0 -24
REMARK 465 TYR 0 -23
REMARK 465 ASN 0 -22
REMARK 465 THR 0 -21
REMARK 465 GLN 0 -20
REMARK 465 ILE 0 -19
REMARK 465 ALA 0 -18
REMARK 465 ASN 0 -17
REMARK 465 ALA 0 -16
REMARK 465 GLY 0 -15
REMARK 465 ALA 0 -14
REMARK 465 SER 0 -13
REMARK 465 PRO 0 -12
REMARK 465 MET 0 -11
REMARK 465 VAL 0 -10
REMARK 465 ASN 0 -9
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 ND2 ASN K 208 O HOH K 7727 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO L 94 C - N - CA ANGL. DEV. = 10.0 DEGREES
REMARK 500 PRO Z 94 C - N - CA ANGL. DEV. = 10.0 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 5 113.88 33.80
REMARK 500 ASP A 6 106.46 -44.31
REMARK 500 SER A 56 137.22 -179.48
REMARK 500 THR A 63 3.85 -67.86
REMARK 500 TYR A 100 -66.24 -153.46
REMARK 500 GLN A 125 -30.39 -132.46
REMARK 500 LYS A 167 -72.43 -37.44
REMARK 500 ASP A 182 28.03 -78.97
REMARK 500 GLU A 203 -70.84 -71.26
REMARK 500 ASN A 21B 78.74 -109.94
REMARK 500 ARG B 6 -38.62 -30.14
REMARK 500 ARG B 11 61.41 64.17
REMARK 500 THR B 13 63.30 -119.14
REMARK 500 VAL B 54 109.96 59.99
REMARK 500 GLU B 65 -1.92 -149.47
REMARK 500 LYS B 66 -22.94 -140.44
REMARK 500 PRO B 153 -31.06 -38.38
REMARK 500 ASP B 21C -60.89 169.26
REMARK 500 ASP C 9 21.50 -141.44
REMARK 500 ASN C 44 30.03 -152.78
REMARK 500 LEU C 58 21.77 170.81
REMARK 500 ASP C 105 133.47 -176.89
REMARK 500 GLN C 125 40.36 -144.99
REMARK 500 ASN C 179 -6.98 -159.86
REMARK 500 PRO C 183 88.84 -46.62
REMARK 500 GLN C 202 79.96 49.74
REMARK 500 THR C 203 104.03 38.39
REMARK 500 GLU C 242 61.93 -67.96
REMARK 500 ARG D 10 133.35 -178.93
REMARK 500 LYS D 43 -2.88 -59.71
REMARK 500 ARG D 53 63.89 71.84
REMARK 500 SER D 56 149.25 178.89
REMARK 500 GLU D 60 93.67 -62.97
REMARK 500 SER D 12E 81.65 -60.84
REMARK 500 GLU D 12G -114.52 177.79
REMARK 500 GLU D 125 58.96 -149.83
REMARK 500 ARG D 126 96.35 -63.94
REMARK 500 MET D 128 119.23 171.38
REMARK 500 SER D 18D 10.48 -58.04
REMARK 500 ARG E 5 -45.17 -28.65
REMARK 500 SER E 42 -148.88 -99.12
REMARK 500 ALA E 55 -68.00 -92.82
REMARK 500 ASP E 56 -157.26 -106.66
REMARK 500 ASP E 142 -156.88 -127.20
REMARK 500 LEU E 180 -77.97 -18.34
REMARK 500 ASN E 185 81.12 -154.85
REMARK 500 ARG E 202 -66.12 -169.78
REMARK 500 ASP E 203 -74.71 -50.27
REMARK 500 GLU E 204 -157.59 -123.94
REMARK 500 LYS E 217 -70.92 -23.85
REMARK 500
REMARK 500 THIS ENTRY HAS 220 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 L 145 0.10 SIDE CHAIN
REMARK 500 TYR Z 145 0.10 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 SRG H 7710
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SRG K 7710
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SRG N 7710
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SRG V 7710
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SRG Y 7710
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SRG 1 7710
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PMA RELATED DB: PDB
REMARK 900 T. ACIDOPHILUM 20S PROTEASOME (WILD TYPE)
REMARK 900 RELATED ID: 1RYP RELATED DB: PDB
REMARK 900 YEAST 20S PROTEASOME (WILD TYPE)
REMARK 900 RELATED ID: 1IRU RELATED DB: PDB
REMARK 900 BOVINE 20S PROTEASOME (WILD TYPE)
REMARK 900 RELATED ID: 3BDM RELATED DB: PDB
REMARK 900 YEAST 20S PROTEASOME COMPLEX WITH GLIDOBACTIN A
DBREF 2ZCY A 4 236 UNP P23639 PSA2_YEAST 1 250
DBREF 2ZCY B 3 252 UNP P23638 PSA4_YEAST 1 258
DBREF 2ZCY C 5 254 UNP P40303 PSA7_YEAST 1 254
DBREF 2ZCY D 1 254 UNP P32379 PSA5_YEAST 1 260
DBREF 2ZCY E 3 233 UNP P40302 PSA1_YEAST 1 234
DBREF 2ZCY F 2 281 UNP P21242 PSA3_YEAST 2 288
DBREF 2ZCY G -3 240 UNP P21243 PSA6_YEAST 1 252
DBREF 2ZCY H 1 233 UNP P25043 PSB7_YEAST 30 261
DBREF 2ZCY I -9 194 UNP P25451 PSB3_YEAST 1 205
DBREF 2ZCY J -1 193 UNP P22141 PSB2_YEAST 1 198
DBREF 2ZCY K 1 211 UNP P30656 PSB5_YEAST 76 287
DBREF 2ZCY L -28 194 UNP P23724 PSB1_YEAST 1 241
DBREF 2ZCY M -41 211 UNP P30657 PSB4_YEAST 1 266
DBREF 2ZCY N 1 18J UNP P38624 PSB6_YEAST 20 215
DBREF 2ZCY O 4 236 UNP P23639 PSA2_YEAST 1 250
DBREF 2ZCY P 3 252 UNP P23638 PSA4_YEAST 1 258
DBREF 2ZCY Q 5 254 UNP P40303 PSA7_YEAST 1 254
DBREF 2ZCY R 1 254 UNP P32379 PSA5_YEAST 1 260
DBREF 2ZCY S 3 233 UNP P40302 PSA1_YEAST 1 234
DBREF 2ZCY T 2 281 UNP P21242 PSA3_YEAST 2 288
DBREF 2ZCY U -3 240 UNP P21243 PSA6_YEAST 1 252
DBREF 2ZCY V 1 233 UNP P25043 PSB7_YEAST 30 261
DBREF 2ZCY W -9 194 UNP P25451 PSB3_YEAST 1 205
DBREF 2ZCY X -1 193 UNP P22141 PSB2_YEAST 1 198
DBREF 2ZCY Y 1 211 UNP P30656 PSB5_YEAST 76 287
DBREF 2ZCY Z -28 194 UNP P23724 PSB1_YEAST 1 241
DBREF 2ZCY 0 -41 211 UNP P30657 PSB4_YEAST 1 266
DBREF 2ZCY 1 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 258 MET GLY SER ARG ARG TYR ASP SER ARG THR THR ILE PHE
SEQRES 2 B 258 SER PRO GLU GLY ARG LEU TYR GLN VAL GLU TYR ALA LEU
SEQRES 3 B 258 GLU SER ILE SER HIS ALA GLY THR ALA ILE GLY ILE MET
SEQRES 4 B 258 ALA SER ASP GLY ILE VAL LEU ALA ALA GLU ARG LYS VAL
SEQRES 5 B 258 THR SER THR LEU LEU GLU GLN ASP THR SER THR GLU LYS
SEQRES 6 B 258 LEU TYR LYS LEU ASN ASP LYS ILE ALA VAL ALA VAL ALA
SEQRES 7 B 258 GLY LEU THR ALA ASP ALA GLU ILE LEU ILE ASN THR ALA
SEQRES 8 B 258 ARG ILE HIS ALA GLN ASN TYR LEU LYS THR TYR ASN GLU
SEQRES 9 B 258 ASP ILE PRO VAL GLU ILE LEU VAL ARG ARG LEU SER ASP
SEQRES 10 B 258 ILE LYS GLN GLY TYR THR GLN HIS GLY GLY LEU ARG PRO
SEQRES 11 B 258 PHE GLY VAL SER PHE ILE TYR ALA GLY TYR ASP ASP ARG
SEQRES 12 B 258 TYR GLY TYR GLN LEU TYR THR SER ASN PRO SER GLY ASN
SEQRES 13 B 258 TYR THR GLY TRP LYS ALA ILE SER VAL GLY ALA ASN THR
SEQRES 14 B 258 SER ALA ALA GLN THR LEU LEU GLN MET ASP TYR LYS ASP
SEQRES 15 B 258 ASP MET LYS VAL ASP ASP ALA ILE GLU LEU ALA LEU LYS
SEQRES 16 B 258 THR LEU SER LYS THR THR ASP SER SER ALA LEU THR TYR
SEQRES 17 B 258 ASP ARG LEU GLU PHE ALA THR ILE ARG LYS GLY ALA ASN
SEQRES 18 B 258 ASP GLY GLU VAL TYR GLN LYS ILE PHE LYS PRO GLN GLU
SEQRES 19 B 258 ILE LYS ASP ILE LEU VAL LYS THR GLY ILE THR LYS LYS
SEQRES 20 B 258 ASP GLU ASP GLU GLU ALA ASP GLU ASP MET LYS
SEQRES 1 C 254 MET SER GLY TYR ASP ARG ALA LEU SER ILE PHE SER PRO
SEQRES 2 C 254 ASP GLY HIS ILE PHE GLN VAL GLU TYR ALA LEU GLU ALA
SEQRES 3 C 254 VAL LYS ARG GLY THR CYS ALA VAL GLY VAL LYS GLY LYS
SEQRES 4 C 254 ASN CYS VAL VAL LEU GLY CYS GLU ARG ARG SER THR LEU
SEQRES 5 C 254 LYS LEU GLN ASP THR ARG ILE THR PRO SER LYS VAL SER
SEQRES 6 C 254 LYS ILE ASP SER HIS VAL VAL LEU SER PHE SER GLY LEU
SEQRES 7 C 254 ASN ALA ASP SER ARG ILE LEU ILE GLU LYS ALA ARG VAL
SEQRES 8 C 254 GLU ALA GLN SER HIS ARG LEU THR LEU GLU ASP PRO VAL
SEQRES 9 C 254 THR VAL GLU TYR LEU THR ARG TYR VAL ALA GLY VAL GLN
SEQRES 10 C 254 GLN ARG TYR THR GLN SER GLY GLY VAL ARG PRO PHE GLY
SEQRES 11 C 254 VAL SER THR LEU ILE ALA GLY PHE ASP PRO ARG ASP ASP
SEQRES 12 C 254 GLU PRO LYS LEU TYR GLN THR GLU PRO SER GLY ILE TYR
SEQRES 13 C 254 SER SER TRP SER ALA GLN THR ILE GLY ARG ASN SER LYS
SEQRES 14 C 254 THR VAL ARG GLU PHE LEU GLU LYS ASN TYR ASP ARG LYS
SEQRES 15 C 254 GLU PRO PRO ALA THR VAL GLU GLU CYS VAL LYS LEU THR
SEQRES 16 C 254 VAL ARG SER LEU LEU GLU VAL VAL GLN THR GLY ALA LYS
SEQRES 17 C 254 ASN ILE GLU ILE THR VAL VAL LYS PRO ASP SER ASP ILE
SEQRES 18 C 254 VAL ALA LEU SER SER GLU GLU ILE ASN GLN TYR VAL THR
SEQRES 19 C 254 GLN ILE GLU GLN GLU LYS GLN GLU GLN GLN GLU GLN ASP
SEQRES 20 C 254 LYS LYS LYS LYS SER ASN HIS
SEQRES 1 D 260 MET PHE LEU THR ARG SER GLU TYR ASP ARG GLY VAL SER
SEQRES 2 D 260 THR PHE SER PRO GLU GLY ARG LEU PHE GLN VAL GLU TYR
SEQRES 3 D 260 SER LEU GLU ALA ILE LYS LEU GLY SER THR ALA ILE GLY
SEQRES 4 D 260 ILE ALA THR LYS GLU GLY VAL VAL LEU GLY VAL GLU LYS
SEQRES 5 D 260 ARG ALA THR SER PRO LEU LEU GLU SER ASP SER ILE GLU
SEQRES 6 D 260 LYS ILE VAL GLU ILE ASP ARG HIS ILE GLY CYS ALA MET
SEQRES 7 D 260 SER GLY LEU THR ALA ASP ALA ARG SER MET ILE GLU HIS
SEQRES 8 D 260 ALA ARG THR ALA ALA VAL THR HIS ASN LEU TYR TYR ASP
SEQRES 9 D 260 GLU ASP ILE ASN VAL GLU SER LEU THR GLN SER VAL CYS
SEQRES 10 D 260 ASP LEU ALA LEU ARG PHE GLY GLU GLY ALA SER GLY GLU
SEQRES 11 D 260 GLU ARG LEU MET SER ARG PRO PHE GLY VAL ALA LEU LEU
SEQRES 12 D 260 ILE ALA GLY HIS ASP ALA ASP ASP GLY TYR GLN LEU PHE
SEQRES 13 D 260 HIS ALA GLU PRO SER GLY THR PHE TYR ARG TYR ASN ALA
SEQRES 14 D 260 LYS ALA ILE GLY SER GLY SER GLU GLY ALA GLN ALA GLU
SEQRES 15 D 260 LEU LEU ASN GLU TRP HIS SER SER LEU THR LEU LYS GLU
SEQRES 16 D 260 ALA GLU LEU LEU VAL LEU LYS ILE LEU LYS GLN VAL MET
SEQRES 17 D 260 GLU GLU LYS LEU ASP GLU ASN ASN ALA GLN LEU SER CYS
SEQRES 18 D 260 ILE THR LYS GLN ASP GLY PHE LYS ILE TYR ASP ASN GLU
SEQRES 19 D 260 LYS THR ALA GLU LEU ILE LYS GLU LEU LYS GLU LYS GLU
SEQRES 20 D 260 ALA ALA GLU SER PRO GLU GLU ALA ASP VAL GLU MET SER
SEQRES 1 E 234 MET PHE ARG ASN ASN TYR ASP GLY ASP THR VAL THR PHE
SEQRES 2 E 234 SER PRO THR GLY ARG LEU PHE GLN VAL GLU TYR ALA LEU
SEQRES 3 E 234 GLU ALA ILE LYS GLN GLY SER VAL THR VAL GLY LEU ARG
SEQRES 4 E 234 SER ASN THR HIS ALA VAL LEU VAL ALA LEU LYS ARG ASN
SEQRES 5 E 234 ALA ASP GLU LEU SER SER TYR GLN LYS LYS ILE ILE LYS
SEQRES 6 E 234 CYS ASP GLU HIS MET GLY LEU SER LEU ALA GLY LEU ALA
SEQRES 7 E 234 PRO ASP ALA ARG VAL LEU SER ASN TYR LEU ARG GLN GLN
SEQRES 8 E 234 CYS ASN TYR SER SER LEU VAL PHE ASN ARG LYS LEU ALA
SEQRES 9 E 234 VAL GLU ARG ALA GLY HIS LEU LEU CYS ASP LYS ALA GLN
SEQRES 10 E 234 LYS ASN THR GLN SER TYR GLY GLY ARG PRO TYR GLY VAL
SEQRES 11 E 234 GLY LEU LEU ILE ILE GLY TYR ASP LYS SER GLY ALA HIS
SEQRES 12 E 234 LEU LEU GLU PHE GLN PRO SER GLY ASN VAL THR GLU LEU
SEQRES 13 E 234 TYR GLY THR ALA ILE GLY ALA ARG SER GLN GLY ALA LYS
SEQRES 14 E 234 THR TYR LEU GLU ARG THR LEU ASP THR PHE ILE LYS ILE
SEQRES 15 E 234 ASP GLY ASN PRO ASP GLU LEU ILE LYS ALA GLY VAL GLU
SEQRES 16 E 234 ALA ILE SER GLN SER LEU ARG ASP GLU SER LEU THR VAL
SEQRES 17 E 234 ASP ASN LEU SER ILE ALA ILE VAL GLY LYS ASP THR PRO
SEQRES 18 E 234 PHE THR ILE TYR ASP GLY GLU ALA VAL ALA LYS TYR ILE
SEQRES 1 F 287 THR SER ILE GLY THR GLY TYR ASP LEU SER ASN SER VAL
SEQRES 2 F 287 PHE SER PRO ASP GLY ARG ASN PHE GLN VAL GLU TYR ALA
SEQRES 3 F 287 VAL LYS ALA VAL GLU ASN GLY THR THR SER ILE GLY ILE
SEQRES 4 F 287 LYS CYS ASN ASP GLY VAL VAL PHE ALA VAL GLU LYS LEU
SEQRES 5 F 287 ILE THR SER LYS LEU LEU VAL PRO GLN LYS ASN VAL LYS
SEQRES 6 F 287 ILE GLN VAL VAL ASP ARG HIS ILE GLY CYS VAL TYR SER
SEQRES 7 F 287 GLY LEU ILE PRO ASP GLY ARG HIS LEU VAL ASN ARG GLY
SEQRES 8 F 287 ARG GLU GLU ALA ALA SER PHE LYS LYS LEU TYR LYS THR
SEQRES 9 F 287 PRO ILE PRO ILE PRO ALA PHE ALA ASP ARG LEU GLY GLN
SEQRES 10 F 287 TYR VAL GLN ALA HIS THR LEU TYR ASN SER VAL ARG PRO
SEQRES 11 F 287 PHE GLY VAL SER THR ILE PHE GLY GLY VAL ASP LYS ASN
SEQRES 12 F 287 GLY ALA HIS LEU TYR MET LEU GLU PRO SER GLY SER TYR
SEQRES 13 F 287 TRP GLY TYR LYS GLY ALA ALA THR GLY LYS GLY ARG GLN
SEQRES 14 F 287 SER ALA LYS ALA GLU LEU GLU LYS LEU VAL ASP HIS HIS
SEQRES 15 F 287 PRO GLU GLY LEU SER ALA ARG GLU ALA VAL LYS GLN ALA
SEQRES 16 F 287 ALA LYS ILE ILE TYR LEU ALA HIS GLU ASP ASN LYS GLU
SEQRES 17 F 287 LYS ASP PHE GLU LEU GLU ILE SER TRP CYS SER LEU SER
SEQRES 18 F 287 GLU THR ASN GLY LEU HIS LYS PHE VAL LYS GLY ASP LEU
SEQRES 19 F 287 LEU GLN GLU ALA ILE ASP PHE ALA GLN LYS GLU ILE ASN
SEQRES 20 F 287 GLY ASP ASP ASP GLU ASP GLU ASP ASP SER ASP ASN VAL
SEQRES 21 F 287 MET SER SER ASP ASP GLU ASN ALA PRO VAL ALA THR ASN
SEQRES 22 F 287 ALA ASN ALA THR THR ASP GLN GLU GLY ASP ILE HIS LEU
SEQRES 23 F 287 GLU
SEQRES 1 G 252 MET SER GLY ALA ALA ALA ALA SER ALA ALA GLY TYR ASP
SEQRES 2 G 252 ARG HIS ILE THR ILE PHE SER PRO GLU GLY ARG LEU TYR
SEQRES 3 G 252 GLN VAL GLU TYR ALA PHE LYS ALA THR ASN GLN THR ASN
SEQRES 4 G 252 ILE ASN SER LEU ALA VAL ARG GLY LYS ASP CYS THR VAL
SEQRES 5 G 252 VAL ILE SER GLN LYS LYS VAL PRO ASP LYS LEU LEU ASP
SEQRES 6 G 252 PRO THR THR VAL SER TYR ILE PHE CYS ILE SER ARG THR
SEQRES 7 G 252 ILE GLY MET VAL VAL ASN GLY PRO ILE PRO ASP ALA ARG
SEQRES 8 G 252 ASN ALA ALA LEU ARG ALA LYS ALA GLU ALA ALA GLU PHE
SEQRES 9 G 252 ARG TYR LYS TYR GLY TYR ASP MET PRO CYS ASP VAL LEU
SEQRES 10 G 252 ALA LYS ARG MET ALA ASN LEU SER GLN ILE TYR THR GLN
SEQRES 11 G 252 ARG ALA TYR MET ARG PRO LEU GLY VAL ILE LEU THR PHE
SEQRES 12 G 252 VAL SER VAL ASP GLU GLU LEU GLY PRO SER ILE TYR LYS
SEQRES 13 G 252 THR ASP PRO ALA GLY TYR TYR VAL GLY TYR LYS ALA THR
SEQRES 14 G 252 ALA THR GLY PRO LYS GLN GLN GLU ILE THR THR ASN LEU
SEQRES 15 G 252 GLU ASN HIS PHE LYS LYS SER LYS ILE ASP HIS ILE ASN
SEQRES 16 G 252 GLU GLU SER TRP GLU LYS VAL VAL GLU PHE ALA ILE THR
SEQRES 17 G 252 HIS MET ILE ASP ALA LEU GLY THR GLU PHE SER LYS ASN
SEQRES 18 G 252 ASP LEU GLU VAL GLY VAL ALA THR LYS ASP LYS PHE PHE
SEQRES 19 G 252 THR LEU SER ALA GLU ASN ILE GLU GLU ARG LEU VAL ALA
SEQRES 20 G 252 ILE ALA GLU GLN ASP
SEQRES 1 H 232 THR THR ILE VAL GLY VAL LYS PHE ASN ASN GLY VAL VAL
SEQRES 2 H 232 ILE ALA ALA ASP THR ARG SER THR GLN GLY PRO ILE VAL
SEQRES 3 H 232 ALA ASP LYS ASN CYS ALA LYS LEU HIS ARG ILE SER PRO
SEQRES 4 H 232 LYS ILE TRP CYS ALA GLY ALA GLY THR ALA ALA ASP THR
SEQRES 5 H 232 GLU ALA VAL THR GLN LEU ILE GLY SER ASN ILE GLU LEU
SEQRES 6 H 232 HIS SER LEU TYR THR SER ARG GLU PRO ARG VAL VAL SER
SEQRES 7 H 232 ALA LEU GLN MET LEU LYS GLN HIS LEU PHE LYS TYR GLN
SEQRES 8 H 232 GLY HIS ILE GLY ALA TYR LEU ILE VAL ALA GLY VAL ASP
SEQRES 9 H 232 PRO THR GLY SER HIS LEU PHE SER ILE HIS ALA HIS GLY
SEQRES 10 H 232 SER THR ASP VAL GLY TYR TYR LEU SER LEU GLY SER GLY
SEQRES 11 H 232 SER LEU ALA ALA MET ALA VAL LEU GLU SER HIS TRP LYS
SEQRES 12 H 232 GLN ASP LEU THR LYS GLU GLU ALA ILE LYS LEU ALA SER
SEQRES 13 H 232 ASP ALA ILE GLN ALA GLY ILE TRP ASN ASP LEU GLY SER
SEQRES 14 H 232 GLY SER ASN VAL ASP VAL CYS VAL MET GLU ILE GLY LYS
SEQRES 15 H 232 ASP ALA GLU TYR LEU ARG ASN TYR LEU THR PRO ASN VAL
SEQRES 16 H 232 ARG GLU GLU LYS GLN LYS SER TYR LYS PHE PRO ARG GLY
SEQRES 17 H 232 THR THR ALA VAL LEU LYS GLU SER ILE VAL ASN ILE CYS
SEQRES 18 H 232 ASP ILE GLN GLU GLU GLN VAL ASP ILE THR ALA
SEQRES 1 I 205 MET SER ASP PRO SER SER ILE ASN GLY GLY ILE VAL VAL
SEQRES 2 I 205 ALA MET THR GLY LYS ASP CYS VAL ALA ILE ALA CYS ASP
SEQRES 3 I 205 LEU ARG LEU GLY SER GLN SER LEU GLY VAL SER ASN LYS
SEQRES 4 I 205 PHE GLU LYS ILE PHE HIS TYR GLY HIS VAL PHE LEU GLY
SEQRES 5 I 205 ILE THR GLY LEU ALA THR ASP VAL THR THR LEU ASN GLU
SEQRES 6 I 205 MET PHE ARG TYR LYS THR ASN LEU TYR LYS LEU LYS GLU
SEQRES 7 I 205 GLU ARG ALA ILE GLU PRO GLU THR PHE THR GLN LEU VAL
SEQRES 8 I 205 SER SER SER LEU TYR GLU ARG ARG PHE GLY PRO TYR PHE
SEQRES 9 I 205 VAL GLY PRO VAL VAL ALA GLY ILE ASN SER LYS SER GLY
SEQRES 10 I 205 LYS PRO PHE ILE ALA GLY PHE ASP LEU ILE GLY CYS ILE
SEQRES 11 I 205 ASP GLU ALA LYS ASP PHE ILE VAL SER GLY THR ALA SER
SEQRES 12 I 205 ASP GLN LEU PHE GLY MET CYS GLU SER LEU TYR GLU PRO
SEQRES 13 I 205 ASN LEU GLU PRO GLU ASP LEU PHE GLU THR ILE SER GLN
SEQRES 14 I 205 ALA LEU LEU ASN ALA ALA ASP ARG ASP ALA LEU SER GLY
SEQRES 15 I 205 TRP GLY ALA VAL VAL TYR ILE ILE LYS LYS ASP GLU VAL
SEQRES 16 I 205 VAL 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 241 MET ALA THR ILE ALA SER GLU TYR SER SER GLU ALA SER
SEQRES 2 L 241 ASN THR PRO ILE GLU HIS GLN PHE ASN PRO TYR GLY ASP
SEQRES 3 L 241 ASN GLY GLY THR ILE LEU GLY ILE ALA GLY GLU ASP PHE
SEQRES 4 L 241 ALA VAL LEU ALA GLY ASP THR ARG ASN ILE THR ASP TYR
SEQRES 5 L 241 SER ILE ASN SER ARG TYR GLU PRO LYS VAL PHE ASP CYS
SEQRES 6 L 241 GLY ASP ASN ILE VAL MET SER ALA ASN GLY PHE ALA ALA
SEQRES 7 L 241 ASP GLY ASP ALA LEU VAL LYS ARG PHE LYS ASN SER VAL
SEQRES 8 L 241 LYS TRP TYR HIS PHE ASP HIS ASN ASP LYS LYS LEU SER
SEQRES 9 L 241 ILE ASN SER ALA ALA ARG ASN ILE GLN HIS LEU LEU TYR
SEQRES 10 L 241 GLY LYS ARG PHE PHE PRO TYR TYR VAL HIS THR ILE ILE
SEQRES 11 L 241 ALA GLY LEU ASP GLU ASP GLY LYS GLY ALA VAL TYR SER
SEQRES 12 L 241 PHE ASP PRO VAL GLY SER TYR GLU ARG GLU GLN CYS ARG
SEQRES 13 L 241 ALA GLY GLY ALA ALA ALA SER LEU ILE MET PRO PHE LEU
SEQRES 14 L 241 ASP ASN GLN VAL ASN PHE LYS ASN GLN TYR GLU PRO GLY
SEQRES 15 L 241 THR ASN GLY LYS VAL LYS LYS PRO LEU LYS TYR LEU SER
SEQRES 16 L 241 VAL GLU GLU VAL ILE LYS LEU VAL ARG ASP SER PHE THR
SEQRES 17 L 241 SER ALA THR GLU ARG HIS ILE GLN VAL GLY ASP GLY LEU
SEQRES 18 L 241 GLU ILE LEU ILE VAL THR LYS ASP GLY VAL ARG LYS GLU
SEQRES 19 L 241 PHE TYR GLU LEU LYS ARG ASP
SEQRES 1 M 266 MET ASN HIS ASP PRO PHE SER TRP GLY ARG PRO ALA ASP
SEQRES 2 M 266 SER THR TYR GLY ALA TYR ASN THR GLN ILE ALA ASN ALA
SEQRES 3 M 266 GLY ALA SER PRO MET VAL ASN THR GLN GLN PRO ILE VAL
SEQRES 4 M 266 THR GLY THR SER VAL ILE SER MET LYS TYR ASP ASN GLY
SEQRES 5 M 266 VAL ILE ILE ALA ALA ASP ASN LEU GLY SER TYR GLY SER
SEQRES 6 M 266 LEU LEU ARG PHE ASN GLY VAL GLU ARG LEU ILE PRO VAL
SEQRES 7 M 266 GLY ASP ASN THR VAL VAL GLY ILE SER GLY ASP ILE SER
SEQRES 8 M 266 ASP MET GLN HIS ILE GLU ARG LEU LEU LYS ASP LEU VAL
SEQRES 9 M 266 THR GLU ASN ALA TYR ASP ASN PRO LEU ALA ASP ALA GLU
SEQRES 10 M 266 GLU ALA LEU GLU PRO SER TYR ILE PHE GLU TYR LEU ALA
SEQRES 11 M 266 THR VAL MET TYR GLN ARG ARG SER LYS MET ASN PRO LEU
SEQRES 12 M 266 TRP ASN ALA ILE ILE VAL ALA GLY VAL GLN SER ASN GLY
SEQRES 13 M 266 ASP GLN PHE LEU ARG TYR VAL ASN LEU LEU GLY VAL THR
SEQRES 14 M 266 TYR SER SER PRO THR LEU ALA THR GLY PHE GLY ALA HIS
SEQRES 15 M 266 MET ALA ASN PRO LEU LEU ARG LYS VAL VAL ASP ARG GLU
SEQRES 16 M 266 SER ASP ILE PRO LYS THR THR VAL GLN VAL ALA GLU GLU
SEQRES 17 M 266 ALA ILE VAL ASN ALA MET ARG VAL LEU TYR TYR ARG ASP
SEQRES 18 M 266 ALA ARG SER SER ARG ASN PHE SER LEU ALA ILE ILE ASP
SEQRES 19 M 266 LYS ASN THR GLY LEU THR PHE LYS LYS ASN LEU GLN VAL
SEQRES 20 M 266 GLU ASN MET LYS TRP ASP PHE ALA LYS ASP ILE LYS GLY
SEQRES 21 M 266 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 258 MET GLY SER ARG ARG TYR ASP SER ARG THR THR ILE PHE
SEQRES 2 P 258 SER PRO GLU GLY ARG LEU TYR GLN VAL GLU TYR ALA LEU
SEQRES 3 P 258 GLU SER ILE SER HIS ALA GLY THR ALA ILE GLY ILE MET
SEQRES 4 P 258 ALA SER ASP GLY ILE VAL LEU ALA ALA GLU ARG LYS VAL
SEQRES 5 P 258 THR SER THR LEU LEU GLU GLN ASP THR SER THR GLU LYS
SEQRES 6 P 258 LEU TYR LYS LEU ASN ASP LYS ILE ALA VAL ALA VAL ALA
SEQRES 7 P 258 GLY LEU THR ALA ASP ALA GLU ILE LEU ILE ASN THR ALA
SEQRES 8 P 258 ARG ILE HIS ALA GLN ASN TYR LEU LYS THR TYR ASN GLU
SEQRES 9 P 258 ASP ILE PRO VAL GLU ILE LEU VAL ARG ARG LEU SER ASP
SEQRES 10 P 258 ILE LYS GLN GLY TYR THR GLN HIS GLY GLY LEU ARG PRO
SEQRES 11 P 258 PHE GLY VAL SER PHE ILE TYR ALA GLY TYR ASP ASP ARG
SEQRES 12 P 258 TYR GLY TYR GLN LEU TYR THR SER ASN PRO SER GLY ASN
SEQRES 13 P 258 TYR THR GLY TRP LYS ALA ILE SER VAL GLY ALA ASN THR
SEQRES 14 P 258 SER ALA ALA GLN THR LEU LEU GLN MET ASP TYR LYS ASP
SEQRES 15 P 258 ASP MET LYS VAL ASP ASP ALA ILE GLU LEU ALA LEU LYS
SEQRES 16 P 258 THR LEU SER LYS THR THR ASP SER SER ALA LEU THR TYR
SEQRES 17 P 258 ASP ARG LEU GLU PHE ALA THR ILE ARG LYS GLY ALA ASN
SEQRES 18 P 258 ASP GLY GLU VAL TYR GLN LYS ILE PHE LYS PRO GLN GLU
SEQRES 19 P 258 ILE LYS ASP ILE LEU VAL LYS THR GLY ILE THR LYS LYS
SEQRES 20 P 258 ASP GLU ASP GLU GLU ALA ASP GLU ASP MET LYS
SEQRES 1 Q 254 MET SER GLY TYR ASP ARG ALA LEU SER ILE PHE SER PRO
SEQRES 2 Q 254 ASP GLY HIS ILE PHE GLN VAL GLU TYR ALA LEU GLU ALA
SEQRES 3 Q 254 VAL LYS ARG GLY THR CYS ALA VAL GLY VAL LYS GLY LYS
SEQRES 4 Q 254 ASN CYS VAL VAL LEU GLY CYS GLU ARG ARG SER THR LEU
SEQRES 5 Q 254 LYS LEU GLN ASP THR ARG ILE THR PRO SER LYS VAL SER
SEQRES 6 Q 254 LYS ILE ASP SER HIS VAL VAL LEU SER PHE SER GLY LEU
SEQRES 7 Q 254 ASN ALA ASP SER ARG ILE LEU ILE GLU LYS ALA ARG VAL
SEQRES 8 Q 254 GLU ALA GLN SER HIS ARG LEU THR LEU GLU ASP PRO VAL
SEQRES 9 Q 254 THR VAL GLU TYR LEU THR ARG TYR VAL ALA GLY VAL GLN
SEQRES 10 Q 254 GLN ARG TYR THR GLN SER GLY GLY VAL ARG PRO PHE GLY
SEQRES 11 Q 254 VAL SER THR LEU ILE ALA GLY PHE ASP PRO ARG ASP ASP
SEQRES 12 Q 254 GLU PRO LYS LEU TYR GLN THR GLU PRO SER GLY ILE TYR
SEQRES 13 Q 254 SER SER TRP SER ALA GLN THR ILE GLY ARG ASN SER LYS
SEQRES 14 Q 254 THR VAL ARG GLU PHE LEU GLU LYS ASN TYR ASP ARG LYS
SEQRES 15 Q 254 GLU PRO PRO ALA THR VAL GLU GLU CYS VAL LYS LEU THR
SEQRES 16 Q 254 VAL ARG SER LEU LEU GLU VAL VAL GLN THR GLY ALA LYS
SEQRES 17 Q 254 ASN ILE GLU ILE THR VAL VAL LYS PRO ASP SER ASP ILE
SEQRES 18 Q 254 VAL ALA LEU SER SER GLU GLU ILE ASN GLN TYR VAL THR
SEQRES 19 Q 254 GLN ILE GLU GLN GLU LYS GLN GLU GLN GLN GLU GLN ASP
SEQRES 20 Q 254 LYS LYS LYS LYS SER ASN HIS
SEQRES 1 R 260 MET PHE LEU THR ARG SER GLU TYR ASP ARG GLY VAL SER
SEQRES 2 R 260 THR PHE SER PRO GLU GLY ARG LEU PHE GLN VAL GLU TYR
SEQRES 3 R 260 SER LEU GLU ALA ILE LYS LEU GLY SER THR ALA ILE GLY
SEQRES 4 R 260 ILE ALA THR LYS GLU GLY VAL VAL LEU GLY VAL GLU LYS
SEQRES 5 R 260 ARG ALA THR SER PRO LEU LEU GLU SER ASP SER ILE GLU
SEQRES 6 R 260 LYS ILE VAL GLU ILE ASP ARG HIS ILE GLY CYS ALA MET
SEQRES 7 R 260 SER GLY LEU THR ALA ASP ALA ARG SER MET ILE GLU HIS
SEQRES 8 R 260 ALA ARG THR ALA ALA VAL THR HIS ASN LEU TYR TYR ASP
SEQRES 9 R 260 GLU ASP ILE ASN VAL GLU SER LEU THR GLN SER VAL CYS
SEQRES 10 R 260 ASP LEU ALA LEU ARG PHE GLY GLU GLY ALA SER GLY GLU
SEQRES 11 R 260 GLU ARG LEU MET SER ARG PRO PHE GLY VAL ALA LEU LEU
SEQRES 12 R 260 ILE ALA GLY HIS ASP ALA ASP ASP GLY TYR GLN LEU PHE
SEQRES 13 R 260 HIS ALA GLU PRO SER GLY THR PHE TYR ARG TYR ASN ALA
SEQRES 14 R 260 LYS ALA ILE GLY SER GLY SER GLU GLY ALA GLN ALA GLU
SEQRES 15 R 260 LEU LEU ASN GLU TRP HIS SER SER LEU THR LEU LYS GLU
SEQRES 16 R 260 ALA GLU LEU LEU VAL LEU LYS ILE LEU LYS GLN VAL MET
SEQRES 17 R 260 GLU GLU LYS LEU ASP GLU ASN ASN ALA GLN LEU SER CYS
SEQRES 18 R 260 ILE THR LYS GLN ASP GLY PHE LYS ILE TYR ASP ASN GLU
SEQRES 19 R 260 LYS THR ALA GLU LEU ILE LYS GLU LEU LYS GLU LYS GLU
SEQRES 20 R 260 ALA ALA GLU SER PRO GLU GLU ALA ASP VAL GLU MET SER
SEQRES 1 S 234 MET PHE ARG ASN ASN TYR ASP GLY ASP THR VAL THR PHE
SEQRES 2 S 234 SER PRO THR GLY ARG LEU PHE GLN VAL GLU TYR ALA LEU
SEQRES 3 S 234 GLU ALA ILE LYS GLN GLY SER VAL THR VAL GLY LEU ARG
SEQRES 4 S 234 SER ASN THR HIS ALA VAL LEU VAL ALA LEU LYS ARG ASN
SEQRES 5 S 234 ALA ASP GLU LEU SER SER TYR GLN LYS LYS ILE ILE LYS
SEQRES 6 S 234 CYS ASP GLU HIS MET GLY LEU SER LEU ALA GLY LEU ALA
SEQRES 7 S 234 PRO ASP ALA ARG VAL LEU SER ASN TYR LEU ARG GLN GLN
SEQRES 8 S 234 CYS ASN TYR SER SER LEU VAL PHE ASN ARG LYS LEU ALA
SEQRES 9 S 234 VAL GLU ARG ALA GLY HIS LEU LEU CYS ASP LYS ALA GLN
SEQRES 10 S 234 LYS ASN THR GLN SER TYR GLY GLY ARG PRO TYR GLY VAL
SEQRES 11 S 234 GLY LEU LEU ILE ILE GLY TYR ASP LYS SER GLY ALA HIS
SEQRES 12 S 234 LEU LEU GLU PHE GLN PRO SER GLY ASN VAL THR GLU LEU
SEQRES 13 S 234 TYR GLY THR ALA ILE GLY ALA ARG SER GLN GLY ALA LYS
SEQRES 14 S 234 THR TYR LEU GLU ARG THR LEU ASP THR PHE ILE LYS ILE
SEQRES 15 S 234 ASP GLY ASN PRO ASP GLU LEU ILE LYS ALA GLY VAL GLU
SEQRES 16 S 234 ALA ILE SER GLN SER LEU ARG ASP GLU SER LEU THR VAL
SEQRES 17 S 234 ASP ASN LEU SER ILE ALA ILE VAL GLY LYS ASP THR PRO
SEQRES 18 S 234 PHE THR ILE TYR ASP GLY GLU ALA VAL ALA LYS TYR ILE
SEQRES 1 T 287 THR SER ILE GLY THR GLY TYR ASP LEU SER ASN SER VAL
SEQRES 2 T 287 PHE SER PRO ASP GLY ARG ASN PHE GLN VAL GLU TYR ALA
SEQRES 3 T 287 VAL LYS ALA VAL GLU ASN GLY THR THR SER ILE GLY ILE
SEQRES 4 T 287 LYS CYS ASN ASP GLY VAL VAL PHE ALA VAL GLU LYS LEU
SEQRES 5 T 287 ILE THR SER LYS LEU LEU VAL PRO GLN LYS ASN VAL LYS
SEQRES 6 T 287 ILE GLN VAL VAL ASP ARG HIS ILE GLY CYS VAL TYR SER
SEQRES 7 T 287 GLY LEU ILE PRO ASP GLY ARG HIS LEU VAL ASN ARG GLY
SEQRES 8 T 287 ARG GLU GLU ALA ALA SER PHE LYS LYS LEU TYR LYS THR
SEQRES 9 T 287 PRO ILE PRO ILE PRO ALA PHE ALA ASP ARG LEU GLY GLN
SEQRES 10 T 287 TYR VAL GLN ALA HIS THR LEU TYR ASN SER VAL ARG PRO
SEQRES 11 T 287 PHE GLY VAL SER THR ILE PHE GLY GLY VAL ASP LYS ASN
SEQRES 12 T 287 GLY ALA HIS LEU TYR MET LEU GLU PRO SER GLY SER TYR
SEQRES 13 T 287 TRP GLY TYR LYS GLY ALA ALA THR GLY LYS GLY ARG GLN
SEQRES 14 T 287 SER ALA LYS ALA GLU LEU GLU LYS LEU VAL ASP HIS HIS
SEQRES 15 T 287 PRO GLU GLY LEU SER ALA ARG GLU ALA VAL LYS GLN ALA
SEQRES 16 T 287 ALA LYS ILE ILE TYR LEU ALA HIS GLU ASP ASN LYS GLU
SEQRES 17 T 287 LYS ASP PHE GLU LEU GLU ILE SER TRP CYS SER LEU SER
SEQRES 18 T 287 GLU THR ASN GLY LEU HIS LYS PHE VAL LYS GLY ASP LEU
SEQRES 19 T 287 LEU GLN GLU ALA ILE ASP PHE ALA GLN LYS GLU ILE ASN
SEQRES 20 T 287 GLY ASP ASP ASP GLU ASP GLU ASP ASP SER ASP ASN VAL
SEQRES 21 T 287 MET SER SER ASP ASP GLU ASN ALA PRO VAL ALA THR ASN
SEQRES 22 T 287 ALA ASN ALA THR THR ASP GLN GLU GLY ASP ILE HIS LEU
SEQRES 23 T 287 GLU
SEQRES 1 U 252 MET SER GLY ALA ALA ALA ALA SER ALA ALA GLY TYR ASP
SEQRES 2 U 252 ARG HIS ILE THR ILE PHE SER PRO GLU GLY ARG LEU TYR
SEQRES 3 U 252 GLN VAL GLU TYR ALA PHE LYS ALA THR ASN GLN THR ASN
SEQRES 4 U 252 ILE ASN SER LEU ALA VAL ARG GLY LYS ASP CYS THR VAL
SEQRES 5 U 252 VAL ILE SER GLN LYS LYS VAL PRO ASP LYS LEU LEU ASP
SEQRES 6 U 252 PRO THR THR VAL SER TYR ILE PHE CYS ILE SER ARG THR
SEQRES 7 U 252 ILE GLY MET VAL VAL ASN GLY PRO ILE PRO ASP ALA ARG
SEQRES 8 U 252 ASN ALA ALA LEU ARG ALA LYS ALA GLU ALA ALA GLU PHE
SEQRES 9 U 252 ARG TYR LYS TYR GLY TYR ASP MET PRO CYS ASP VAL LEU
SEQRES 10 U 252 ALA LYS ARG MET ALA ASN LEU SER GLN ILE TYR THR GLN
SEQRES 11 U 252 ARG ALA TYR MET ARG PRO LEU GLY VAL ILE LEU THR PHE
SEQRES 12 U 252 VAL SER VAL ASP GLU GLU LEU GLY PRO SER ILE TYR LYS
SEQRES 13 U 252 THR ASP PRO ALA GLY TYR TYR VAL GLY TYR LYS ALA THR
SEQRES 14 U 252 ALA THR GLY PRO LYS GLN GLN GLU ILE THR THR ASN LEU
SEQRES 15 U 252 GLU ASN HIS PHE LYS LYS SER LYS ILE ASP HIS ILE ASN
SEQRES 16 U 252 GLU GLU SER TRP GLU LYS VAL VAL GLU PHE ALA ILE THR
SEQRES 17 U 252 HIS MET ILE ASP ALA LEU GLY THR GLU PHE SER LYS ASN
SEQRES 18 U 252 ASP LEU GLU VAL GLY VAL ALA THR LYS ASP LYS PHE PHE
SEQRES 19 U 252 THR LEU SER ALA GLU ASN ILE GLU GLU ARG LEU VAL ALA
SEQRES 20 U 252 ILE ALA GLU GLN ASP
SEQRES 1 V 232 THR THR ILE VAL GLY VAL LYS PHE ASN ASN GLY VAL VAL
SEQRES 2 V 232 ILE ALA ALA ASP THR ARG SER THR GLN GLY PRO ILE VAL
SEQRES 3 V 232 ALA ASP LYS ASN CYS ALA LYS LEU HIS ARG ILE SER PRO
SEQRES 4 V 232 LYS ILE TRP CYS ALA GLY ALA GLY THR ALA ALA ASP THR
SEQRES 5 V 232 GLU ALA VAL THR GLN LEU ILE GLY SER ASN ILE GLU LEU
SEQRES 6 V 232 HIS SER LEU TYR THR SER ARG GLU PRO ARG VAL VAL SER
SEQRES 7 V 232 ALA LEU GLN MET LEU LYS GLN HIS LEU PHE LYS TYR GLN
SEQRES 8 V 232 GLY HIS ILE GLY ALA TYR LEU ILE VAL ALA GLY VAL ASP
SEQRES 9 V 232 PRO THR GLY SER HIS LEU PHE SER ILE HIS ALA HIS GLY
SEQRES 10 V 232 SER THR ASP VAL GLY TYR TYR LEU SER LEU GLY SER GLY
SEQRES 11 V 232 SER LEU ALA ALA MET ALA VAL LEU GLU SER HIS TRP LYS
SEQRES 12 V 232 GLN ASP LEU THR LYS GLU GLU ALA ILE LYS LEU ALA SER
SEQRES 13 V 232 ASP ALA ILE GLN ALA GLY ILE TRP ASN ASP LEU GLY SER
SEQRES 14 V 232 GLY SER ASN VAL ASP VAL CYS VAL MET GLU ILE GLY LYS
SEQRES 15 V 232 ASP ALA GLU TYR LEU ARG ASN TYR LEU THR PRO ASN VAL
SEQRES 16 V 232 ARG GLU GLU LYS GLN LYS SER TYR LYS PHE PRO ARG GLY
SEQRES 17 V 232 THR THR ALA VAL LEU LYS GLU SER ILE VAL ASN ILE CYS
SEQRES 18 V 232 ASP ILE GLN GLU GLU GLN VAL ASP ILE THR ALA
SEQRES 1 W 205 MET SER ASP PRO SER SER ILE ASN GLY GLY ILE VAL VAL
SEQRES 2 W 205 ALA MET THR GLY LYS ASP CYS VAL ALA ILE ALA CYS ASP
SEQRES 3 W 205 LEU ARG LEU GLY SER GLN SER LEU GLY VAL SER ASN LYS
SEQRES 4 W 205 PHE GLU LYS ILE PHE HIS TYR GLY HIS VAL PHE LEU GLY
SEQRES 5 W 205 ILE THR GLY LEU ALA THR ASP VAL THR THR LEU ASN GLU
SEQRES 6 W 205 MET PHE ARG TYR LYS THR ASN LEU TYR LYS LEU LYS GLU
SEQRES 7 W 205 GLU ARG ALA ILE GLU PRO GLU THR PHE THR GLN LEU VAL
SEQRES 8 W 205 SER SER SER LEU TYR GLU ARG ARG PHE GLY PRO TYR PHE
SEQRES 9 W 205 VAL GLY PRO VAL VAL ALA GLY ILE ASN SER LYS SER GLY
SEQRES 10 W 205 LYS PRO PHE ILE ALA GLY PHE ASP LEU ILE GLY CYS ILE
SEQRES 11 W 205 ASP GLU ALA LYS ASP PHE ILE VAL SER GLY THR ALA SER
SEQRES 12 W 205 ASP GLN LEU PHE GLY MET CYS GLU SER LEU TYR GLU PRO
SEQRES 13 W 205 ASN LEU GLU PRO GLU ASP LEU PHE GLU THR ILE SER GLN
SEQRES 14 W 205 ALA LEU LEU ASN ALA ALA ASP ARG ASP ALA LEU SER GLY
SEQRES 15 W 205 TRP GLY ALA VAL VAL TYR ILE ILE LYS LYS ASP GLU VAL
SEQRES 16 W 205 VAL 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 241 MET ALA THR ILE ALA SER GLU TYR SER SER GLU ALA SER
SEQRES 2 Z 241 ASN THR PRO ILE GLU HIS GLN PHE ASN PRO TYR GLY ASP
SEQRES 3 Z 241 ASN GLY GLY THR ILE LEU GLY ILE ALA GLY GLU ASP PHE
SEQRES 4 Z 241 ALA VAL LEU ALA GLY ASP THR ARG ASN ILE THR ASP TYR
SEQRES 5 Z 241 SER ILE ASN SER ARG TYR GLU PRO LYS VAL PHE ASP CYS
SEQRES 6 Z 241 GLY ASP ASN ILE VAL MET SER ALA ASN GLY PHE ALA ALA
SEQRES 7 Z 241 ASP GLY ASP ALA LEU VAL LYS ARG PHE LYS ASN SER VAL
SEQRES 8 Z 241 LYS TRP TYR HIS PHE ASP HIS ASN ASP LYS LYS LEU SER
SEQRES 9 Z 241 ILE ASN SER ALA ALA ARG ASN ILE GLN HIS LEU LEU TYR
SEQRES 10 Z 241 GLY LYS ARG PHE PHE PRO TYR TYR VAL HIS THR ILE ILE
SEQRES 11 Z 241 ALA GLY LEU ASP GLU ASP GLY LYS GLY ALA VAL TYR SER
SEQRES 12 Z 241 PHE ASP PRO VAL GLY SER TYR GLU ARG GLU GLN CYS ARG
SEQRES 13 Z 241 ALA GLY GLY ALA ALA ALA SER LEU ILE MET PRO PHE LEU
SEQRES 14 Z 241 ASP ASN GLN VAL ASN PHE LYS ASN GLN TYR GLU PRO GLY
SEQRES 15 Z 241 THR ASN GLY LYS VAL LYS LYS PRO LEU LYS TYR LEU SER
SEQRES 16 Z 241 VAL GLU GLU VAL ILE LYS LEU VAL ARG ASP SER PHE THR
SEQRES 17 Z 241 SER ALA THR GLU ARG HIS ILE GLN VAL GLY ASP GLY LEU
SEQRES 18 Z 241 GLU ILE LEU ILE VAL THR LYS ASP GLY VAL ARG LYS GLU
SEQRES 19 Z 241 PHE TYR GLU LEU LYS ARG ASP
SEQRES 1 0 266 MET ASN HIS ASP PRO PHE SER TRP GLY ARG PRO ALA ASP
SEQRES 2 0 266 SER THR TYR GLY ALA TYR ASN THR GLN ILE ALA ASN ALA
SEQRES 3 0 266 GLY ALA SER PRO MET VAL ASN THR GLN GLN PRO ILE VAL
SEQRES 4 0 266 THR GLY THR SER VAL ILE SER MET LYS TYR ASP ASN GLY
SEQRES 5 0 266 VAL ILE ILE ALA ALA ASP ASN LEU GLY SER TYR GLY SER
SEQRES 6 0 266 LEU LEU ARG PHE ASN GLY VAL GLU ARG LEU ILE PRO VAL
SEQRES 7 0 266 GLY ASP ASN THR VAL VAL GLY ILE SER GLY ASP ILE SER
SEQRES 8 0 266 ASP MET GLN HIS ILE GLU ARG LEU LEU LYS ASP LEU VAL
SEQRES 9 0 266 THR GLU ASN ALA TYR ASP ASN PRO LEU ALA ASP ALA GLU
SEQRES 10 0 266 GLU ALA LEU GLU PRO SER TYR ILE PHE GLU TYR LEU ALA
SEQRES 11 0 266 THR VAL MET TYR GLN ARG ARG SER LYS MET ASN PRO LEU
SEQRES 12 0 266 TRP ASN ALA ILE ILE VAL ALA GLY VAL GLN SER ASN GLY
SEQRES 13 0 266 ASP GLN PHE LEU ARG TYR VAL ASN LEU LEU GLY VAL THR
SEQRES 14 0 266 TYR SER SER PRO THR LEU ALA THR GLY PHE GLY ALA HIS
SEQRES 15 0 266 MET ALA ASN PRO LEU LEU ARG LYS VAL VAL ASP ARG GLU
SEQRES 16 0 266 SER ASP ILE PRO LYS THR THR VAL GLN VAL ALA GLU GLU
SEQRES 17 0 266 ALA ILE VAL ASN ALA MET ARG VAL LEU TYR TYR ARG ASP
SEQRES 18 0 266 ALA ARG SER SER ARG ASN PHE SER LEU ALA ILE ILE ASP
SEQRES 19 0 266 LYS ASN THR GLY LEU THR PHE LYS LYS ASN LEU GLN VAL
SEQRES 20 0 266 GLU ASN MET LYS TRP ASP PHE ALA LYS ASP ILE LYS GLY
SEQRES 21 0 266 TYR GLY THR GLN LYS ILE
SEQRES 1 1 196 THR SER ILE MET ALA VAL THR PHE LYS ASP GLY VAL ILE
SEQRES 2 1 196 LEU GLY ALA ASP SER ARG THR THR THR GLY ALA TYR ILE
SEQRES 3 1 196 ALA ASN ARG VAL THR ASP LYS LEU THR ARG VAL HIS ASP
SEQRES 4 1 196 LYS ILE TRP CYS CYS ARG SER GLY SER ALA ALA ASP THR
SEQRES 5 1 196 GLN ALA ILE ALA ASP ILE VAL GLN TYR HIS LEU GLU LEU
SEQRES 6 1 196 TYR THR SER GLN TYR GLY THR PRO SER THR GLU THR ALA
SEQRES 7 1 196 ALA SER VAL PHE LYS GLU LEU CYS TYR GLU ASN LYS ASP
SEQRES 8 1 196 ASN LEU THR ALA GLY ILE ILE VAL ALA GLY TYR ASP ASP
SEQRES 9 1 196 LYS ASN LYS GLY GLU VAL TYR THR ILE PRO LEU GLY GLY
SEQRES 10 1 196 SER VAL HIS LYS LEU PRO TYR ALA ILE ALA GLY SER GLY
SEQRES 11 1 196 SER THR PHE ILE TYR GLY TYR CYS ASP LYS ASN PHE ARG
SEQRES 12 1 196 GLU ASN MET SER LYS GLU GLU THR VAL ASP PHE ILE LYS
SEQRES 13 1 196 HIS SER LEU SER GLN ALA ILE LYS TRP ASP GLY SER SER
SEQRES 14 1 196 GLY GLY VAL ILE ARG MET VAL VAL LEU THR ALA ALA GLY
SEQRES 15 1 196 VAL GLU ARG LEU ILE PHE TYR PRO ASP GLU TYR GLU GLN
SEQRES 16 1 196 LEU
HET SRG H7710 35
HET SRG K7710 35
HET SRG N7710 35
HET SRG V7710 35
HET SRG Y7710 35
HET SRG 17710 35
HETNAM SRG (2S)-2-[[(2S)-1-[[(5S,8S,9E)-2,7-DIOXO-5-PROPAN-2-YL-1,
HETNAM 2 SRG 6-DIAZACYCLODODECA-3,9-DIEN-8-YL]AMINO]-3-METHYL-1-
HETNAM 3 SRG OXO-BUTAN-2-YL]CARBAMOYLAMINO]-3-METHYL-BUTANOIC ACID
HETSYN SRG SYRINGOLIN A
FORMUL 29 SRG 6(C24 H39 N5 O6)
FORMUL 35 HOH *1018(H2 O)
HELIX 1 1 LEU A 21 GLY A 34 1 14
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 GLU A 234 1 10
HELIX 10 10 ALA A 235 LEU A 236 5 2
HELIX 11 11 GLY B 4 ASP B 9 5 6
HELIX 12 12 LEU B 21 SER B 32 1 12
HELIX 13 13 LEU B 81 ASN B 104 1 24
HELIX 14 14 PRO B 108 HIS B 126 1 19
HELIX 15 15 ASN B 168 TYR B 180 1 13
HELIX 16 16 LYS B 185 THR B 202 1 17
HELIX 17 17 THR B 206 ASP B 208 5 3
HELIX 18 18 LYS B 225 THR B 236 1 12
HELIX 19 19 ILE C 21 ARG C 33 1 13
HELIX 20 20 LEU C 81 GLU C 104 1 24
HELIX 21 21 THR C 108 TYR C 123 1 16
HELIX 22 22 ASN C 168 LYS C 178 1 11
HELIX 23 23 THR C 185 GLN C 202 1 18
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 LYS E 122 1 15
HELIX 37 37 ASN E 123 GLN E 125 5 3
HELIX 38 38 SER E 169 ILE E 18D 1 16
HELIX 39 39 ASN E 185 SER E 198 1 14
HELIX 40 40 GLN E 199 LEU E 201 5 3
HELIX 41 41 GLY E 226 LYS E 231 1 6
HELIX 42 42 ASN F 21 ASN F 33 1 13
HELIX 43 43 LEU F 81 LYS F 104 1 24
HELIX 44 44 PRO F 108 HIS F 123 1 16
HELIX 45 45 GLY F 168 HIS F 18C 1 16
HELIX 46 46 SER F 185 ALA F 201 1 16
HELIX 47 47 HIS F 202 LYS F 206 5 5
HELIX 48 48 LYS F 225 ILE F 240 1 16
HELIX 49 49 LEU G 21 THR G 31 1 11
HELIX 50 50 ASP G 60 VAL G 64 5 5
HELIX 51 51 PRO G 81 GLY G 104 1 24
HELIX 52 52 PRO G 108 ARG G 126 1 19
HELIX 53 53 LYS G 168 LYS G 17E 1 17
HELIX 54 54 SER G 18M GLY G 202 1 18
HELIX 55 55 SER G 225 GLU G 238 1 14
HELIX 56 56 THR H 48 SER H 71 1 24
HELIX 57 57 ARG H 75 TYR H 90 1 16
HELIX 58 58 GLY H 130 TRP H 142 1 13
HELIX 59 59 THR H 147 ASP H 166 1 20
HELIX 60 60 ASP I -7 ILE I -3 5 5
HELIX 61 61 LEU I 48 GLU I 71 1 24
HELIX 62 62 GLU I 75 GLU I 89 1 15
HELIX 63 63 ALA I 130 TYR I 142 1 13
HELIX 64 64 GLU I 147 ASP I 164 1 18
HELIX 65 65 GLY J 50 ASP J 71 1 22
HELIX 66 66 SER J 75 ILE J 90A 1 17
HELIX 67 67 SER J 130 HIS J 141 1 12
HELIX 68 68 THR J 147 MET J 166 1 20
HELIX 69 69 GLY K 48 LYS K 71 1 24
HELIX 70 70 SER K 75 TYR K 90 1 16
HELIX 71 71 GLY K 130 SER K 140 1 11
HELIX 72 72 SER K 147 ASP K 166 1 20
HELIX 73 73 VAL K 192 GLY K 204 1 13
HELIX 74 74 PHE L 48 HIS L 70 1 23
HELIX 75 75 SER L 75 GLY L 89 1 15
HELIX 76 76 ALA L 130 VAL L 142 1 13
HELIX 77 77 SER L 147 HIS L 166 1 20
HELIX 78 78 ILE M 49 TYR M 68 1 20
HELIX 79 79 GLU M 75 LYS M 92A 1 19
HELIX 80 80 GLY M 128 VAL M 14A 1 15
HELIX 81 81 ARG M 14C ILE M 14G 5 5
HELIX 82 82 THR M 147 ASP M 166 1 20
HELIX 83 83 TRP M 197 ILE M 203 5 7
HELIX 84 84 SER N 48 GLY N 72 1 24
HELIX 85 85 SER N 75 ASN N 90 1 16
HELIX 86 86 LYS N 91 LEU N 95 5 4
HELIX 87 87 GLY N 128 PHE N 133 5 6
HELIX 88 88 ILE N 134 LYS N 140 1 7
HELIX 89 89 SER N 147 ASP N 166 1 20
HELIX 90 90 TYR N 18C GLN N 18I 1 7
HELIX 91 91 LEU O 21 GLY O 34 1 14
HELIX 92 92 SER O 61 LEU O 64 5 4
HELIX 93 93 MET O 81 SER O 99 1 19
HELIX 94 94 TYR O 100 GLY O 104 1 6
HELIX 95 95 PRO O 108 ALA O 123 1 16
HELIX 96 96 GLY O 168 TRP O 180 1 13
HELIX 97 97 GLU O 185 VAL O 202 1 17
HELIX 98 98 ASN O 21B LEU O 21G 5 5
HELIX 99 99 THR O 225 GLU O 234 1 10
HELIX 100 100 ALA O 235 LEU O 236 5 2
HELIX 101 101 GLY P 4 ASP P 9 5 6
HELIX 102 102 LEU P 21 SER P 32 1 12
HELIX 103 103 LEU P 81 ASN P 104 1 24
HELIX 104 104 PRO P 108 HIS P 126 1 19
HELIX 105 105 ASN P 168 TYR P 180 1 13
HELIX 106 106 LYS P 185 THR P 202 1 17
HELIX 107 107 THR P 206 ASP P 208 5 3
HELIX 108 108 LYS P 225 THR P 236 1 12
HELIX 109 109 ILE Q 21 ARG Q 33 1 13
HELIX 110 110 LEU Q 81 GLU Q 104 1 24
HELIX 111 111 THR Q 108 TYR Q 123 1 16
HELIX 112 112 ASN Q 168 LYS Q 178 1 11
HELIX 113 113 THR Q 185 GLN Q 202 1 18
HELIX 114 114 SER Q 225 GLU Q 242 1 18
HELIX 115 115 LEU R 21 LEU R 33 1 13
HELIX 116 116 GLU R 60 ILE R 64 5 5
HELIX 117 117 THR R 82 ASP R 84 5 3
HELIX 118 118 ALA R 85 ASP R 104 1 20
HELIX 119 119 ASN R 108 LEU R 121 1 14
HELIX 120 120 GLY R 168 TRP R 180 1 13
HELIX 121 121 THR R 185 MET R 201 1 17
HELIX 122 122 ASP R 225 ALA R 243 1 18
HELIX 123 123 PHE S 4 TYR S 8 5 5
HELIX 124 124 LEU S 21 GLN S 33 1 13
HELIX 125 125 LEU S 81 ASN S 104 1 24
HELIX 126 126 ALA S 108 LYS S 122 1 15
HELIX 127 127 ASN S 123 GLN S 125 5 3
HELIX 128 128 SER S 169 ILE S 18D 1 16
HELIX 129 129 ASN S 185 SER S 198 1 14
HELIX 130 130 GLN S 199 LEU S 201 5 3
HELIX 131 131 GLY S 226 LYS S 231 1 6
HELIX 132 132 ASN T 21 ASN T 33 1 13
HELIX 133 133 LEU T 81 LYS T 104 1 24
HELIX 134 134 PRO T 108 HIS T 123 1 16
HELIX 135 135 GLY T 168 HIS T 18C 1 16
HELIX 136 136 SER T 185 ALA T 201 1 16
HELIX 137 137 HIS T 202 LYS T 206 5 5
HELIX 138 138 LYS T 225 ILE T 240 1 16
HELIX 139 139 LEU U 21 THR U 31 1 11
HELIX 140 140 ASP U 60 VAL U 64 5 5
HELIX 141 141 PRO U 81 GLY U 104 1 24
HELIX 142 142 PRO U 108 ARG U 126 1 19
HELIX 143 143 LYS U 168 LYS U 17E 1 17
HELIX 144 144 SER U 18M GLY U 202 1 18
HELIX 145 145 SER U 225 GLU U 238 1 14
HELIX 146 146 THR V 48 SER V 71 1 24
HELIX 147 147 ARG V 75 TYR V 90 1 16
HELIX 148 148 GLY V 130 TRP V 142 1 13
HELIX 149 149 THR V 147 ASP V 166 1 20
HELIX 150 150 ASP W -7 ILE W -3 5 5
HELIX 151 151 LEU W 48 GLU W 71 1 24
HELIX 152 152 GLU W 75 GLU W 89 1 15
HELIX 153 153 ALA W 130 TYR W 142 1 13
HELIX 154 154 GLU W 147 ASP W 164 1 18
HELIX 155 155 GLY X 50 ASP X 71 1 22
HELIX 156 156 SER X 75 ILE X 90A 1 17
HELIX 157 157 SER X 130 HIS X 141 1 12
HELIX 158 158 THR X 147 MET X 166 1 20
HELIX 159 159 GLY Y 48 LYS Y 71 1 24
HELIX 160 160 SER Y 75 TYR Y 90 1 16
HELIX 161 161 GLY Y 130 SER Y 140 1 11
HELIX 162 162 SER Y 147 ASP Y 166 1 20
HELIX 163 163 VAL Y 192 GLY Y 204 1 13
HELIX 164 164 PHE Z 48 HIS Z 70 1 23
HELIX 165 165 SER Z 75 GLY Z 89 1 15
HELIX 166 166 ALA Z 130 VAL Z 142 1 13
HELIX 167 167 SER Z 147 HIS Z 166 1 20
HELIX 168 168 ILE 0 49 TYR 0 68 1 20
HELIX 169 169 GLU 0 75 LYS 0 92A 1 19
HELIX 170 170 GLY 0 128 VAL 0 14A 1 15
HELIX 171 171 ARG 0 14C ILE 0 14G 5 5
HELIX 172 172 THR 0 147 ASP 0 166 1 20
HELIX 173 173 TRP 0 197 ILE 0 203 5 7
HELIX 174 174 SER 1 48 GLY 1 72 1 24
HELIX 175 175 SER 1 75 ASN 1 90 1 16
HELIX 176 176 LYS 1 91 LEU 1 95 5 4
HELIX 177 177 GLY 1 128 PHE 1 133 5 6
HELIX 178 178 ILE 1 134 LYS 1 140 1 7
HELIX 179 179 SER 1 147 ASP 1 166 1 20
HELIX 180 180 TYR 1 18C GLN 1 18I 1 7
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 ASP H 17 -1 N VAL H 12 O MET H 178
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 127 N ILE H 3
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 TYR B 149 N TYR B 138
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 GLY C 39 O GLN C 163
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 VAL C 215 N VAL C 46
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 ASP C 71 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 VAL D 47 N ILE D 40
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 ALA D 139 N GLY D 75
SHEET 4 I 5 GLY D 145 ALA D 151 -1 O PHE D 149 N ILE D 138
SHEET 5 I 5 PHE D 157 ARG D 159 -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 SER E 211 N ALA E 50
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 ILE F 54 -1 O VAL F 47 N ILE F 40
SHEET 4 L 5 ASP F 207 SER F 216 -1 O ASP F 207 N ILE F 54
SHEET 5 L 5 HIS F 221 VAL F 224 -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 TYR F 149 N PHE F 138
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 ALA G 39 O THR G 163
SHEET 3 N 5 THR G 46 GLN G 51 -1 O ILE G 49 N LEU G 38
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 THR G 137 N VAL G 77
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 ILE H 25 N GLN H 22
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 TYR I 188 N LEU H 214
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 GLY I 8 O CYS I 11
SHEET 6 R 6 PHE I 124 GLY I 128 -1 O SER I 127 N VAL I 3
SHEET 1 S 2 LEU I 20 SER I 22 0
SHEET 2 S 2 LEU I 25 SER I 28 -1 O LEU I 25 N SER I 22
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 ALA I 102 N PHE I 42
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 HIS J 127 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 ALA J 15 N LEU J 4
SHEET 4 U 5 VAL J 173 ASP J 179 -1 O VAL J 178 N VAL J 12
SHEET 5 U 5 GLY J 183 GLN J 186 -1 O GLY J 183 N ASP J 179
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 SER K 28 N ALA K 20
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 ARG L 185 N ILE L 177
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 GLY L 38 0
SHEET 2 AC 5 ILE L 41 GLY L 47 -1 O ILE L 41 N CYS L 37
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 ALA M 102 N VAL M 42
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 TYR M 120 -1 O TYR M 120 N TYR M 112
SHEET 1 AF 5 THR M 124 ALA M 126 0
SHEET 2 AF 5 ILE M 4 LYS M 7 -1 N SER M 5 O LEU M 125
SHEET 3 AF 5 GLY M 11 ASP M 17 -1 O ALA M 15 N ILE M 4
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 ARG N 174 N ALA N 16
SHEET 5 AG 5 GLY N 183 PHE N 18B-1 O GLU N 185 N VAL N 177
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 6 ALA O 59 MET O 60 0
SHEET 2 AK 6 TYR U 157 TYR U 160 -1 O GLY U 159 N MET O 60
SHEET 3 AK 6 GLY U 145 THR U 151 -1 N ILE U 148 O TYR U 160
SHEET 4 AK 6 ILE U 135 ASP U 142 -1 N PHE U 138 O TYR U 149
SHEET 5 AK 6 GLY U 75 ASN U 79 -1 N VAL U 77 O THR U 137
SHEET 6 AK 6 ILE U 67 CYS U 69 -1 N PHE U 68 O MET U 76
SHEET 1 AL 5 SER O 68 THR O 71 0
SHEET 2 AL 5 ILE O 74 GLY O 80 -1 O ILE O 74 N LEU O 70
SHEET 3 AL 5 VAL O 134 ASP O 142 -1 O ALA O 139 N GLY O 75
SHEET 4 AL 5 GLY O 146 VAL O 151 -1 O TYR O 149 N ILE O 138
SHEET 5 AL 5 TYR O 157 PRO O 159 -1 O PHE O 158 N GLN O 150
SHEET 1 AM 6 TYR O 21I THR O 21J 0
SHEET 2 AM 6 ALA V 184 LEU V 192 1 O TYR V 186 N THR O 21J
SHEET 3 AM 6 VAL V 173 GLU V 179 -1 N VAL V 175 O LEU V 187
SHEET 4 AM 6 GLY V 11 ALA V 16 -1 N VAL V 12 O MET V 178
SHEET 5 AM 6 ILE V 3 PHE V 8 -1 N VAL V 6 O VAL V 13
SHEET 6 AM 6 TYR V 124 LEU V 127 -1 O LEU V 127 N ILE V 3
SHEET 1 AN 5 ALA P 162 VAL P 165 0
SHEET 2 AN 5 ALA P 37 ALA P 42 -1 N GLY P 39 O ILE P 163
SHEET 3 AN 5 GLY P 45 GLU P 51 -1 O ALA P 49 N ILE P 38
SHEET 4 AN 5 LEU P 210 ARG P 216 -1 O ALA P 213 N LEU P 48
SHEET 5 AN 5 TYR P 220 ILE P 223 -1 O TYR P 220 N ARG P 216
SHEET 1 AO 5 LEU P 67 LYS P 69 0
SHEET 2 AO 5 ILE P 74 GLY P 80 -1 O VAL P 76 N TYR P 68
SHEET 3 AO 5 VAL P 134 ASP P 142 -1 O ALA P 139 N ALA P 75
SHEET 4 AO 5 GLY P 145 SER P 151 -1 O TYR P 149 N TYR P 138
SHEET 5 AO 5 TYR P 157 GLY P 159 -1 O THR P 158 N THR P 150
SHEET 1 AP 5 ALA Q 162 ILE Q 165 0
SHEET 2 AP 5 ALA Q 37 LYS Q 41 -1 N GLY Q 39 O GLN Q 163
SHEET 3 AP 5 VAL Q 46 GLU Q 51 -1 O GLY Q 49 N VAL Q 38
SHEET 4 AP 5 ILE Q 210 LYS Q 216 -1 O VAL Q 215 N VAL Q 46
SHEET 5 AP 5 ASP Q 220 ALA Q 223 -1 O ASP Q 220 N LYS Q 216
SHEET 1 AQ 5 SER Q 68 ASP Q 71 0
SHEET 2 AQ 5 VAL Q 74 GLY Q 80 -1 O LEU Q 76 N SER Q 68
SHEET 3 AQ 5 VAL Q 134 GLY Q 140 -1 O LEU Q 137 N SER Q 77
SHEET 4 AQ 5 LYS Q 147 THR Q 151 -1 O TYR Q 149 N ILE Q 138
SHEET 5 AQ 5 TYR Q 157 SER Q 159 -1 O SER Q 158 N GLN Q 150
SHEET 1 AR 5 ALA R 162 ILE R 165 0
SHEET 2 AR 5 ALA R 37 THR R 42 -1 N ALA R 37 O ILE R 165
SHEET 3 AR 5 GLY R 45 GLU R 51 -1 O VAL R 47 N ILE R 40
SHEET 4 AR 5 ALA R 210 THR R 216 -1 O SER R 213 N LEU R 48
SHEET 5 AR 5 GLY R 220 ILE R 223 -1 O GLY R 220 N THR R 216
SHEET 1 AS 5 ILE R 67 ASP R 71 0
SHEET 2 AS 5 ILE R 74 GLY R 80 -1 O ILE R 74 N ILE R 70
SHEET 3 AS 5 VAL R 134 ASP R 142 -1 O ALA R 139 N GLY R 75
SHEET 4 AS 5 GLY R 145 ALA R 151 -1 O PHE R 149 N ILE R 138
SHEET 5 AS 5 PHE R 157 ARG R 159 -1 O TYR R 158 N HIS R 150
SHEET 1 AT 5 GLY S 162 ILE S 165 0
SHEET 2 AT 5 THR S 37 ARG S 41 -1 N GLY S 39 O THR S 163
SHEET 3 AT 5 HIS S 45 LEU S 51 -1 O VAL S 49 N VAL S 38
SHEET 4 AT 5 LEU S 210 GLY S 216 -1 O SER S 211 N ALA S 50
SHEET 5 AT 5 THR S 219 ASP S 225 -1 O TYR S 224 N ILE S 212
SHEET 1 AU 5 ILE S 67 ASP S 71 0
SHEET 2 AU 5 MET S 74 GLY S 80 -1 O LEU S 76 N ILE S 68
SHEET 3 AU 5 VAL S 134 ASP S 142 -1 O GLY S 135 N ALA S 79
SHEET 4 AU 5 GLY S 145 PHE S 151 -1 O PHE S 151 N LEU S 136
SHEET 5 AU 5 VAL S 157 GLU S 159 -1 O THR S 158 N GLU S 150
SHEET 1 AV 5 GLY T 162 THR T 165 0
SHEET 2 AV 5 SER T 37 CYS T 42 -1 N GLY T 39 O ALA T 163
SHEET 3 AV 5 GLY T 45 ILE T 54 -1 O VAL T 47 N ILE T 40
SHEET 4 AV 5 ASP T 207 SER T 216 -1 O ASP T 207 N ILE T 54
SHEET 5 AV 5 HIS T 221 PHE T 223 -1 O LYS T 222 N TRP T 214
SHEET 1 AW 5 GLN T 68 VAL T 70 0
SHEET 2 AW 5 ILE T 74 GLY T 80 -1 O CYS T 76 N GLN T 68
SHEET 3 AW 5 VAL T 134 ASP T 142 -1 O ILE T 137 N VAL T 77
SHEET 4 AW 5 GLY T 145 LEU T 151 -1 O TYR T 149 N PHE T 138
SHEET 5 AW 5 TYR T 157 GLY T 159 -1 O TRP T 158 N MET T 150
SHEET 1 AX 5 ALA U 162 THR U 165 0
SHEET 2 AX 5 SER U 37 ARG U 41 -1 N ALA U 39 O THR U 163
SHEET 3 AX 5 THR U 46 GLN U 51 -1 O ILE U 49 N LEU U 38
SHEET 4 AX 5 LEU U 210 THR U 216 -1 O ALA U 215 N THR U 46
SHEET 5 AX 5 LYS U 220 THR U 223 -1 O LYS U 220 N THR U 216
SHEET 1 AY 2 SER V 20 GLN V 22 0
SHEET 2 AY 2 ILE V 25 ASP V 28 -1 O ILE V 25 N GLN V 22
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 VAL W 4 O ALA W 15
SHEET 6 BA 6 PHE W 124 GLY W 128 -1 O SER W 127 N VAL W 3
SHEET 1 BB 2 LEU W 20 SER W 22 0
SHEET 2 BB 2 LEU W 25 SER W 28 -1 O LEU W 25 N SER W 22
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 HIS X 127 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 ALA X 15 N LEU X 4
SHEET 4 BD 5 VAL X 173 ASP X 179 -1 O VAL X 178 N VAL X 12
SHEET 5 BD 5 GLY X 183 GLN X 186 -1 O GLY X 183 N ASP X 179
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 ASN X 98 N ALA X 46
SHEET 4 BF 5 LYS X 107 ILE X 113 -1 O TYR X 111 N ILE X 101
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 SER Y 28 N ALA Y 20
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 VAL Y 113 N THR Y 99
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 ARG Z 185 N ILE Z 177
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 GLY Z 38 0
SHEET 2 BL 5 ILE Z 41 GLY Z 47 -1 O ILE Z 41 N CYS Z 37
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 0 25 PHE 0 28 0
SHEET 2 BM 5 GLY 0 20 TYR 0 22 -1 N GLY 0 20 O PHE 0 28
SHEET 3 BM 5 VAL 0 -3 GLY 0 -1 -1 N THR 0 -2 O SER 0 21
SHEET 4 BM 5 THR 0 41 ASP 0 48 -1 O GLY 0 47 N GLY 0 -1
SHEET 5 BM 5 LEU 0 34 VAL 0 37 -1 N ILE 0 35 O VAL 0 43
SHEET 1 BN 7 LEU 0 25 PHE 0 28 0
SHEET 2 BN 7 GLY 0 20 TYR 0 22 -1 N GLY 0 20 O PHE 0 28
SHEET 3 BN 7 VAL 0 -3 GLY 0 -1 -1 N THR 0 -2 O SER 0 21
SHEET 4 BN 7 THR 0 41 ASP 0 48 -1 O GLY 0 47 N GLY 0 -1
SHEET 5 BN 7 ASN 0 97 VAL 0 104 -1 O ALA 0 102 N VAL 0 42
SHEET 6 BN 7 GLN 0 108 ASN 0 114 -1 O PHE 0 109 N GLY 0 103
SHEET 7 BN 7 THR 0 119 TYR 0 120 -1 O TYR 0 120 N TYR 0 112
SHEET 1 BO 5 THR 0 124 ALA 0 126 0
SHEET 2 BO 5 ILE 0 4 LYS 0 7 -1 N SER 0 5 O LEU 0 125
SHEET 3 BO 5 GLY 0 11 ASP 0 17 -1 O ILE 0 13 N MET 0 6
SHEET 4 BO 5 ASN 0 172 ASP 0 179 -1 O ALA 0 176 N ILE 0 14
SHEET 5 BO 5 GLY 0 183 GLN 0 191 -1 O GLY 0 183 N ASP 0 179
SHEET 1 BP 5 TYR 1 124 ALA 1 127 0
SHEET 2 BP 5 ILE 1 3 PHE 1 8 -1 N ILE 1 3 O ALA 1 127
SHEET 3 BP 5 GLY 1 11 ALA 1 16 -1 O GLY 1 15 N MET 1 4
SHEET 4 BP 5 ILE 1 173 THR 1 179 -1 O LEU 1 178 N VAL 1 12
SHEET 5 BP 5 GLY 1 183 PHE 1 18B-1 O GLU 1 185 N VAL 1 177
SHEET 1 BQ 2 THR 1 20 THR 1 22 0
SHEET 2 BQ 2 TYR 1 25 ASN 1 28 -1 O ASN 1 28 N THR 1 20
SHEET 1 BR 5 LEU 1 34 HIS 1 38 0
SHEET 2 BR 5 ILE 1 41 GLY 1 47 -1 O CYS 1 43 N THR 1 35
SHEET 3 BR 5 ALA 1 97 ASP 1 105 -1 O GLY 1 98 N SER 1 46
SHEET 4 BR 5 LYS 1 107 ILE 1 113 -1 O TYR 1 111 N VAL 1 101
SHEET 5 BR 5 HIS 1 120 LEU 1 122 -1 O HIS 1 120 N THR 1 112
LINK OG1 THR H 1 C26 SRG H7710 1555 1555 1.53
LINK OG1 THR K 1 C26 SRG K7710 1555 1555 1.53
LINK OG1 THR N 1 C26 SRG N7710 1555 1555 1.54
LINK OG1 THR V 1 C26 SRG V7710 1555 1555 1.52
LINK OG1 THR Y 1 C26 SRG Y7710 1555 1555 1.52
LINK OG1 THR 1 1 C26 SRG 17710 1555 1555 1.54
SITE 1 AC1 13 THR H 1 SER H 20 THR H 21 GLN H 22
SITE 2 AC1 13 ALA H 27 LYS H 33 GLY H 45 GLY H 47
SITE 3 AC1 13 ALA H 49 HOH H7748 ASP I 114 ILE I 116
SITE 4 AC1 13 CYS I 118
SITE 1 AC2 9 THR K 1 ALA K 20 THR K 21 LYS K 33
SITE 2 AC2 9 GLY K 47 ALA K 49 HOH K7722 ASP L 114
SITE 3 AC2 9 PRO L 115
SITE 1 AC3 12 SER H 118 HOH H7721 THR N 1 THR N 20
SITE 2 AC3 12 THR N 21 THR N 22 LYS N 33 ARG N 45
SITE 3 AC3 12 SER N 46 GLY N 47 HOH N7715 HOH N7750
SITE 1 AC4 13 THR V 1 SER V 20 THR V 21 GLN V 22
SITE 2 AC4 13 ALA V 27 LYS V 33 GLY V 45 GLY V 47
SITE 3 AC4 13 ALA V 49 HOH V7742 ASP W 114 ILE W 116
SITE 4 AC4 13 CYS W 118
SITE 1 AC5 9 THR Y 1 ALA Y 20 THR Y 21 LYS Y 33
SITE 2 AC5 9 GLY Y 47 ALA Y 49 HOH Y7718 ASP Z 114
SITE 3 AC5 9 PRO Z 115
SITE 1 AC6 10 THR 1 1 THR 1 20 THR 1 21 THR 1 22
SITE 2 AC6 10 LYS 1 33 ARG 1 45 SER 1 46 GLY 1 47
SITE 3 AC6 10 HOH 17755 SER V 118
CRYST1 135.051 301.964 143.835 90.00 112.87 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 0.007405 0.000000 0.003123 0.00000
SCALE2 0.000000 0.003312 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007545 0.00000
(ATOM LINES ARE NOT SHOWN.)
END