HEADER HYDROLASE/HYDROLASE INHIBITOR 09-JUN-15 5BXN
TITLE YEAST 20S PROTEASOME BETA2-G170A MUTANT IN COMPLEX WITH BORTEZOMIB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-2;
COMPND 3 CHAIN: A, O;
COMPND 4 SYNONYM: MACROPAIN SUBUNIT Y7,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 5 SUBUNIT Y7,PROTEASOME COMPONENT Y7,PROTEINASE YSCE SUBUNIT 7;
COMPND 6 EC: 3.4.25.1;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-3;
COMPND 9 CHAIN: B, P;
COMPND 10 SYNONYM: MACROPAIN SUBUNIT Y13,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 11 SUBUNIT Y13,PROTEASOME COMPONENT Y13,PROTEINASE YSCE SUBUNIT 13;
COMPND 12 EC: 3.4.25.1;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-4;
COMPND 15 CHAIN: C, Q;
COMPND 16 SYNONYM: MACROPAIN SUBUNIT PRE6,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 17 SUBUNIT PRE6,PROTEASOME COMPONENT PRE6,PROTEINASE YSCE SUBUNIT PRE6;
COMPND 18 EC: 3.4.25.1;
COMPND 19 MOL_ID: 4;
COMPND 20 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-5;
COMPND 21 CHAIN: D, R;
COMPND 22 SYNONYM: MACROPAIN SUBUNIT PUP2,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 23 SUBUNIT PUP2,PROTEASOME COMPONENT PUP2,PROTEINASE YSCE SUBUNIT PUP2;
COMPND 24 EC: 3.4.25.1;
COMPND 25 MOL_ID: 5;
COMPND 26 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-6;
COMPND 27 CHAIN: E, S;
COMPND 28 SYNONYM: MACROPAIN SUBUNIT PRE5,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 29 SUBUNIT PRE5,PROTEASOME COMPONENT PRE5,PROTEINASE YSCE SUBUNIT PRE5;
COMPND 30 EC: 3.4.25.1;
COMPND 31 MOL_ID: 6;
COMPND 32 MOLECULE: PROBABLE PROTEASOME SUBUNIT ALPHA TYPE-7;
COMPND 33 CHAIN: F, T;
COMPND 34 SYNONYM: MACROPAIN SUBUNIT C1,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 35 SUBUNIT C1,PROTEASOME COMPONENT C1,PROTEINASE YSCE SUBUNIT 1;
COMPND 36 EC: 3.4.25.1;
COMPND 37 MOL_ID: 7;
COMPND 38 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-1;
COMPND 39 CHAIN: G, U;
COMPND 40 SYNONYM: MACROPAIN SUBUNIT C7-ALPHA,MULTICATALYTIC ENDOPEPTIDASE
COMPND 41 COMPLEX C7,PROTEASOME COMPONENT C7-ALPHA,PROTEASOME COMPONENT Y8,
COMPND 42 PROTEINASE YSCE SUBUNIT 7,SCL1 SUPPRESSOR PROTEIN;
COMPND 43 EC: 3.4.25.1;
COMPND 44 MOL_ID: 8;
COMPND 45 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-2;
COMPND 46 CHAIN: H, V;
COMPND 47 SYNONYM: MACROPAIN SUBUNIT PUP1,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 48 SUBUNIT PUP1,PROTEASOME COMPONENT PUP1,PROTEINASE YSCE SUBUNIT PUP1;
COMPND 49 EC: 3.4.25.1;
COMPND 50 ENGINEERED: YES;
COMPND 51 MUTATION: YES;
COMPND 52 MOL_ID: 9;
COMPND 53 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-3;
COMPND 54 CHAIN: I, W;
COMPND 55 SYNONYM: MACROPAIN SUBUNIT PUP3,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 56 SUBUNIT PUP3,PROTEASOME COMPONENT PUP3;
COMPND 57 EC: 3.4.25.1;
COMPND 58 MOL_ID: 10;
COMPND 59 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-4;
COMPND 60 CHAIN: J, X;
COMPND 61 SYNONYM: MACROPAIN SUBUNIT C11,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 62 SUBUNIT C11,PROTEASOME COMPONENT C11,PROTEINASE YSCE SUBUNIT 11;
COMPND 63 EC: 3.4.25.1;
COMPND 64 MOL_ID: 11;
COMPND 65 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-5;
COMPND 66 CHAIN: K, Y;
COMPND 67 SYNONYM: MACROPAIN SUBUNIT PRE2,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 68 SUBUNIT PRE2,PROTEASOME COMPONENT PRE2,PROTEINASE YSCE SUBUNIT PRE2;
COMPND 69 EC: 3.4.25.1;
COMPND 70 MOL_ID: 12;
COMPND 71 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-6;
COMPND 72 CHAIN: L, Z;
COMPND 73 SYNONYM: MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C5,PROTEASOME
COMPND 74 COMPONENT C5;
COMPND 75 EC: 3.4.25.1;
COMPND 76 MOL_ID: 13;
COMPND 77 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-7;
COMPND 78 CHAIN: M, a;
COMPND 79 SYNONYM: MACROPAIN SUBUNIT PRE4,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 80 SUBUNIT PRE4,PROTEASOME COMPONENT PRE4,PROTEINASE YSCE SUBUNIT PRE4;
COMPND 81 EC: 3.4.25.1;
COMPND 82 MOL_ID: 14;
COMPND 83 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-1;
COMPND 84 CHAIN: N, b;
COMPND 85 SYNONYM: MACROPAIN SUBUNIT PRE3,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 86 SUBUNIT PRE3,PROTEASOME COMPONENT PRE3,PROTEINASE YSCE SUBUNIT PRE3;
COMPND 87 EC: 3.4.25.1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 3 S288C);
SOURCE 4 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 5 ORGANISM_TAXID: 559292;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 8 S288C);
SOURCE 9 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 10 ORGANISM_TAXID: 559292;
SOURCE 11 MOL_ID: 3;
SOURCE 12 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 13 S288C);
SOURCE 14 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 15 ORGANISM_TAXID: 559292;
SOURCE 16 MOL_ID: 4;
SOURCE 17 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 18 S288C);
SOURCE 19 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 20 ORGANISM_TAXID: 559292;
SOURCE 21 MOL_ID: 5;
SOURCE 22 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 23 S288C);
SOURCE 24 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 25 ORGANISM_TAXID: 559292;
SOURCE 26 MOL_ID: 6;
SOURCE 27 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 28 S288C);
SOURCE 29 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 30 ORGANISM_TAXID: 559292;
SOURCE 31 MOL_ID: 7;
SOURCE 32 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 33 S288C);
SOURCE 34 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 35 ORGANISM_TAXID: 559292;
SOURCE 36 MOL_ID: 8;
SOURCE 37 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 38 S288C);
SOURCE 39 ORGANISM_TAXID: 559292;
SOURCE 40 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 41 S288C);
SOURCE 42 EXPRESSION_SYSTEM_TAXID: 559292;
SOURCE 43 MOL_ID: 9;
SOURCE 44 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 45 S288C);
SOURCE 46 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 47 ORGANISM_TAXID: 559292;
SOURCE 48 MOL_ID: 10;
SOURCE 49 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 50 S288C);
SOURCE 51 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 52 ORGANISM_TAXID: 559292;
SOURCE 53 MOL_ID: 11;
SOURCE 54 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 55 S288C);
SOURCE 56 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 57 ORGANISM_TAXID: 559292;
SOURCE 58 MOL_ID: 12;
SOURCE 59 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 60 S288C);
SOURCE 61 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 62 ORGANISM_TAXID: 559292;
SOURCE 63 MOL_ID: 13;
SOURCE 64 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 65 S288C);
SOURCE 66 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 67 ORGANISM_TAXID: 559292;
SOURCE 68 MOL_ID: 14;
SOURCE 69 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 70 S288C);
SOURCE 71 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 72 ORGANISM_TAXID: 559292
KEYWDS HYDROLASE-HYDROLASE INHIBITOR COMPLEX, IMMUNODEFICIENCY, PROTEASOME,
KEYWDS 2 MUTANT, ASSEMBLY DEFECT
EXPDTA X-RAY DIFFRACTION
AUTHOR E.M.HUBER,M.GROLL
REVDAT 4 10-JAN-24 5BXN 1 LINK
REVDAT 3 31-OCT-18 5BXN 1 COMPND SOURCE
REVDAT 2 11-JUL-18 5BXN 1 JRNL REMARK LINK ATOM
REVDAT 1 15-JUN-16 5BXN 0
JRNL AUTH I.TREISE,E.M.HUBER,T.KLEIN-RODEWALD,W.HEINEMEYER,
JRNL AUTH 2 S.A.GRASSMANN,M.BASLER,T.ADLER,B.RATHKOLB,L.HELMING,
JRNL AUTH 3 C.ANDRES,M.KLAFTEN,C.LANDBRECHT,T.WIELAND,T.M.STROM,
JRNL AUTH 4 K.D.MCCOY,A.J.MACPHERSON,E.WOLF,M.GROETTRUP,M.OLLERT,F.NEFF,
JRNL AUTH 5 V.GAILUS-DURNER,H.FUCHS,M.HRABE DE ANGELIS,M.GROLL,D.H.BUSCH
JRNL TITL DEFECTIVE IMMUNO- AND THYMOPROTEASOME ASSEMBLY CAUSES SEVERE
JRNL TITL 2 IMMUNODEFICIENCY.
JRNL REF SCI REP V. 8 5975 2018
JRNL REFN ESSN 2045-2322
JRNL PMID 29654304
JRNL DOI 10.1038/S41598-018-24199-0
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 3 NUMBER OF REFLECTIONS : 237314
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 12491
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 17184
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.11
REMARK 3 BIN R VALUE (WORKING SET) : 0.3190
REMARK 3 BIN FREE R VALUE SET COUNT : 905
REMARK 3 BIN FREE R VALUE : 0.3450
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 49298
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 181
REMARK 3 SOLVENT ATOMS : 374
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 70.02
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.12000
REMARK 3 B22 (A**2) : -7.93000
REMARK 3 B33 (A**2) : 3.74000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.90000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.288
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.235
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 28.150
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 50384 ; 0.005 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 48138 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 68168 ; 1.034 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES):110828 ; 0.768 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 6306 ; 4.894 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 2246 ;34.424 ;24.408
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 8736 ;14.682 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 284 ;14.377 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 7678 ; 0.058 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 57160 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 11310 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 25314 ; 2.086 ; 4.607
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 25313 ; 2.086 ; 4.607
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 31590 ; 2.681 ; 6.898
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 31591 ; 2.681 ; 6.899
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 25070 ; 2.031 ; 4.977
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 25070 ; 2.031 ; 4.977
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 36578 ; 2.390 ; 7.315
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 54499 ; 3.070 ;36.141
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 54464 ; 3.050 ;36.134
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 98522 ; 1.097 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 264 ;34.405 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 97735 ; 5.718 ; 5.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 14
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A O
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 300 1
REMARK 3 1 O 1 O 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 3099 ; 0.010 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 A (A): 3253 ; 0.000 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 A (A): 3439 ; 0.010 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 A (A): 3618 ; 0.010 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 A (A): 3001 ; 0.010 ; 0.050
REMARK 3 TIGHT THERMAL 1 A (A**2): 3795 ; 4.840 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : B P
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 1 B 300 1
REMARK 3 1 P 1 P 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 2 B (A**2): 3756 ; 3.750 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : C Q
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C 1 C 300 1
REMARK 3 1 Q 1 Q 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 3 C (A**2): 3729 ;10.010 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : D R
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 D 1 D 300 1
REMARK 3 1 R 1 R 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 4 D (A**2): 3578 ; 6.390 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 5
REMARK 3 CHAIN NAMES : E S
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 E 1 E 300 1
REMARK 3 1 S 1 S 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 5 E (A**2): 3509 ; 6.460 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 6
REMARK 3 CHAIN NAMES : F T
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 F 1 F 300 1
REMARK 3 1 T 1 T 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 6 F (A**2): 3749 ; 5.530 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 7
REMARK 3 CHAIN NAMES : G U
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 G 1 G 300 1
REMARK 3 1 U 1 U 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 7 G (A**2): 3770 ; 3.000 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 8
REMARK 3 CHAIN NAMES : H V
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 H 1 H 300 1
REMARK 3 1 V 1 V 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 8 H (A**2): 3391 ; 4.280 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 9
REMARK 3 CHAIN NAMES : I W
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 I 1 I 300 1
REMARK 3 1 W 1 W 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 9 I (A**2): 3119 ; 2.950 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 10
REMARK 3 CHAIN NAMES : J X
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 J 1 J 300 1
REMARK 3 1 X 1 X 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 10 J (A**2): 3099 ; 2.890 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 11
REMARK 3 CHAIN NAMES : K Y
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 K 1 K 300 1
REMARK 3 1 Y 1 Y 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 11 K (A**2): 3253 ; 2.500 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 12
REMARK 3 CHAIN NAMES : L Z
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 L 1 L 300 1
REMARK 3 1 Z 1 Z 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 12 L (A**2): 3439 ; 2.460 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 13
REMARK 3 CHAIN NAMES : M a
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 M 1 M 300 1
REMARK 3 1 a 1 a 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 13 M (A**2): 3618 ; 2.160 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 14
REMARK 3 CHAIN NAMES : N b
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 N 1 N 300 1
REMARK 3 1 b 1 b 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 14 N (A**2): 3001 ; 2.150 ; 0.500
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 28
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 250
REMARK 3 ORIGIN FOR THE GROUP (A): 67.1202 -92.0694 46.1411
REMARK 3 T TENSOR
REMARK 3 T11: 0.2525 T22: 0.2506
REMARK 3 T33: 0.3428 T12: -0.0588
REMARK 3 T13: 0.0146 T23: -0.0350
REMARK 3 L TENSOR
REMARK 3 L11: 0.2032 L22: 0.2072
REMARK 3 L33: 0.0252 L12: -0.1413
REMARK 3 L13: 0.0013 L23: 0.0111
REMARK 3 S TENSOR
REMARK 3 S11: -0.0422 S12: 0.0030 S13: -0.0133
REMARK 3 S21: 0.0642 S22: 0.0347 S23: -0.1243
REMARK 3 S31: -0.0532 S32: -0.0161 S33: 0.0074
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 244
REMARK 3 ORIGIN FOR THE GROUP (A): 59.4170 -87.6941 16.5953
REMARK 3 T TENSOR
REMARK 3 T11: 0.2812 T22: 0.2960
REMARK 3 T33: 0.2919 T12: -0.0620
REMARK 3 T13: 0.1040 T23: 0.0664
REMARK 3 L TENSOR
REMARK 3 L11: 0.0869 L22: 0.1586
REMARK 3 L33: 0.2976 L12: -0.0506
REMARK 3 L13: 0.0865 L23: 0.0107
REMARK 3 S TENSOR
REMARK 3 S11: -0.0762 S12: -0.0118 S13: -0.0736
REMARK 3 S21: -0.1044 S22: -0.0392 S23: 0.0333
REMARK 3 S31: -0.1300 S32: 0.0628 S33: 0.1154
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1 C 240
REMARK 3 ORIGIN FOR THE GROUP (A): 32.0816 -87.2846 1.3795
REMARK 3 T TENSOR
REMARK 3 T11: 0.2833 T22: 0.2452
REMARK 3 T33: 0.2220 T12: -0.0278
REMARK 3 T13: 0.0510 T23: 0.0606
REMARK 3 L TENSOR
REMARK 3 L11: 0.0866 L22: 0.2802
REMARK 3 L33: 0.2576 L12: 0.0683
REMARK 3 L13: 0.0598 L23: -0.1292
REMARK 3 S TENSOR
REMARK 3 S11: -0.0605 S12: -0.0404 S13: 0.0199
REMARK 3 S21: -0.1018 S22: 0.0395 S23: 0.0246
REMARK 3 S31: -0.0207 S32: 0.0409 S33: 0.0210
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 1 D 242
REMARK 3 ORIGIN FOR THE GROUP (A): 2.9333 -90.0765 14.1383
REMARK 3 T TENSOR
REMARK 3 T11: 0.2021 T22: 0.1871
REMARK 3 T33: 0.3688 T12: 0.0503
REMARK 3 T13: -0.0691 T23: 0.0995
REMARK 3 L TENSOR
REMARK 3 L11: 0.2666 L22: 0.5077
REMARK 3 L33: 0.2790 L12: -0.0560
REMARK 3 L13: 0.0356 L23: -0.3298
REMARK 3 S TENSOR
REMARK 3 S11: -0.0117 S12: -0.0996 S13: -0.0034
REMARK 3 S21: -0.1160 S22: -0.0112 S23: 0.1801
REMARK 3 S31: 0.0269 S32: 0.0769 S33: 0.0229
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 3 E 233
REMARK 3 ORIGIN FOR THE GROUP (A): -3.1233 -94.5436 46.1178
REMARK 3 T TENSOR
REMARK 3 T11: 0.1610 T22: 0.2468
REMARK 3 T33: 0.5221 T12: 0.0743
REMARK 3 T13: 0.1363 T23: 0.0205
REMARK 3 L TENSOR
REMARK 3 L11: 0.1973 L22: 0.4180
REMARK 3 L33: 0.3135 L12: 0.2398
REMARK 3 L13: -0.0302 L23: -0.1732
REMARK 3 S TENSOR
REMARK 3 S11: -0.0583 S12: 0.0232 S13: 0.0951
REMARK 3 S21: 0.0586 S22: 0.0452 S23: 0.2786
REMARK 3 S31: -0.1211 S32: -0.0033 S33: 0.0131
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 2 F 244
REMARK 3 ORIGIN FOR THE GROUP (A): 15.5025 -95.2406 70.2402
REMARK 3 T TENSOR
REMARK 3 T11: 0.3344 T22: 0.2451
REMARK 3 T33: 0.2360 T12: 0.0485
REMARK 3 T13: 0.2200 T23: -0.0741
REMARK 3 L TENSOR
REMARK 3 L11: 0.3843 L22: 0.0579
REMARK 3 L33: 0.1693 L12: 0.1404
REMARK 3 L13: 0.2483 L23: 0.0915
REMARK 3 S TENSOR
REMARK 3 S11: -0.0261 S12: -0.0192 S13: 0.0831
REMARK 3 S21: 0.0074 S22: -0.0402 S23: 0.0577
REMARK 3 S31: -0.0251 S32: -0.0219 S33: 0.0663
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 2 G 242
REMARK 3 ORIGIN FOR THE GROUP (A): 47.9919 -93.5238 71.3901
REMARK 3 T TENSOR
REMARK 3 T11: 0.4823 T22: 0.2250
REMARK 3 T33: 0.1958 T12: -0.0367
REMARK 3 T13: -0.0237 T23: -0.0619
REMARK 3 L TENSOR
REMARK 3 L11: 0.0226 L22: 0.0452
REMARK 3 L33: 0.0034 L12: 0.0106
REMARK 3 L13: -0.0057 L23: 0.0015
REMARK 3 S TENSOR
REMARK 3 S11: 0.0491 S12: 0.0551 S13: -0.0192
REMARK 3 S21: 0.1164 S22: -0.0275 S23: -0.0567
REMARK 3 S31: -0.0195 S32: -0.0111 S33: -0.0215
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 1 H 222
REMARK 3 ORIGIN FOR THE GROUP (A): 67.8208-130.1536 48.2668
REMARK 3 T TENSOR
REMARK 3 T11: 0.1210 T22: 0.2955
REMARK 3 T33: 0.2877 T12: -0.0137
REMARK 3 T13: -0.0176 T23: -0.0108
REMARK 3 L TENSOR
REMARK 3 L11: 0.0521 L22: 0.2113
REMARK 3 L33: 0.0183 L12: 0.0309
REMARK 3 L13: -0.0299 L23: -0.0243
REMARK 3 S TENSOR
REMARK 3 S11: 0.0287 S12: 0.0601 S13: 0.0324
REMARK 3 S21: 0.0842 S22: -0.0176 S23: -0.1859
REMARK 3 S31: -0.0234 S32: -0.0451 S33: -0.0111
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 1 I 204
REMARK 3 ORIGIN FOR THE GROUP (A): 68.3234-127.3406 20.8140
REMARK 3 T TENSOR
REMARK 3 T11: 0.0985 T22: 0.3361
REMARK 3 T33: 0.3545 T12: -0.0104
REMARK 3 T13: 0.1586 T23: -0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 0.0308 L22: 0.2009
REMARK 3 L33: 0.0512 L12: -0.0296
REMARK 3 L13: 0.0071 L23: -0.0838
REMARK 3 S TENSOR
REMARK 3 S11: 0.0214 S12: 0.0429 S13: 0.0080
REMARK 3 S21: -0.0623 S22: -0.0362 S23: -0.1563
REMARK 3 S31: 0.0015 S32: -0.0272 S33: 0.0148
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 1 J 195
REMARK 3 ORIGIN FOR THE GROUP (A): 44.6099-126.4632 -0.5675
REMARK 3 T TENSOR
REMARK 3 T11: 0.3047 T22: 0.2879
REMARK 3 T33: 0.1250 T12: -0.0206
REMARK 3 T13: 0.1271 T23: 0.0163
REMARK 3 L TENSOR
REMARK 3 L11: 0.4481 L22: 0.4465
REMARK 3 L33: 0.0909 L12: 0.1430
REMARK 3 L13: 0.0812 L23: -0.1208
REMARK 3 S TENSOR
REMARK 3 S11: 0.0273 S12: -0.0193 S13: 0.0470
REMARK 3 S21: -0.2346 S22: -0.0000 S23: 0.0320
REMARK 3 S31: 0.0363 S32: 0.0404 S33: -0.0273
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K 1 K 212
REMARK 3 ORIGIN FOR THE GROUP (A): 10.7660-130.8901 2.6463
REMARK 3 T TENSOR
REMARK 3 T11: 0.2105 T22: 0.2785
REMARK 3 T33: 0.2400 T12: 0.0129
REMARK 3 T13: -0.0885 T23: 0.0428
REMARK 3 L TENSOR
REMARK 3 L11: 0.0584 L22: 0.1085
REMARK 3 L33: 0.0179 L12: 0.0706
REMARK 3 L13: 0.0034 L23: 0.0214
REMARK 3 S TENSOR
REMARK 3 S11: -0.0035 S12: -0.0349 S13: 0.0412
REMARK 3 S21: -0.0176 S22: 0.0193 S23: 0.0714
REMARK 3 S31: 0.0060 S32: 0.0574 S33: -0.0157
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 1 L 222
REMARK 3 ORIGIN FOR THE GROUP (A): -4.5293-134.5133 28.8959
REMARK 3 T TENSOR
REMARK 3 T11: 0.0268 T22: 0.2983
REMARK 3 T33: 0.4474 T12: 0.0283
REMARK 3 T13: 0.0719 T23: 0.0614
REMARK 3 L TENSOR
REMARK 3 L11: 0.0097 L22: 0.1843
REMARK 3 L33: 0.3354 L12: -0.0006
REMARK 3 L13: 0.0272 L23: 0.1651
REMARK 3 S TENSOR
REMARK 3 S11: -0.0067 S12: -0.0224 S13: -0.0385
REMARK 3 S21: 0.0028 S22: -0.0080 S23: 0.2016
REMARK 3 S31: -0.0384 S32: 0.0658 S33: 0.0147
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : M 1 M 233
REMARK 3 ORIGIN FOR THE GROUP (A): 8.0872-138.1698 60.6861
REMARK 3 T TENSOR
REMARK 3 T11: 0.2330 T22: 0.3168
REMARK 3 T33: 0.2687 T12: -0.0088
REMARK 3 T13: 0.1810 T23: 0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 0.1242 L22: 0.4221
REMARK 3 L33: 0.0326 L12: -0.1278
REMARK 3 L13: 0.0522 L23: -0.0637
REMARK 3 S TENSOR
REMARK 3 S11: 0.0442 S12: 0.0077 S13: 0.0341
REMARK 3 S21: 0.1952 S22: -0.0186 S23: 0.0917
REMARK 3 S31: -0.0021 S32: 0.0371 S33: -0.0256
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : N 1 N 196
REMARK 3 ORIGIN FOR THE GROUP (A): 40.2263-134.3607 70.8072
REMARK 3 T TENSOR
REMARK 3 T11: 0.3752 T22: 0.2808
REMARK 3 T33: 0.1102 T12: -0.0246
REMARK 3 T13: -0.0161 T23: -0.0272
REMARK 3 L TENSOR
REMARK 3 L11: 0.2417 L22: 0.5295
REMARK 3 L33: 0.1608 L12: 0.1346
REMARK 3 L13: -0.1865 L23: -0.1716
REMARK 3 S TENSOR
REMARK 3 S11: 0.0618 S12: 0.1023 S13: 0.0427
REMARK 3 S21: 0.2515 S22: -0.0551 S23: -0.1300
REMARK 3 S31: -0.0394 S32: -0.0521 S33: -0.0067
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : O 1 O 250
REMARK 3 ORIGIN FOR THE GROUP (A): 2.0218-206.8972 36.5508
REMARK 3 T TENSOR
REMARK 3 T11: 0.1922 T22: 0.1930
REMARK 3 T33: 0.3427 T12: -0.0606
REMARK 3 T13: -0.0361 T23: 0.0626
REMARK 3 L TENSOR
REMARK 3 L11: 0.3740 L22: 0.2897
REMARK 3 L33: 0.0941 L12: -0.0363
REMARK 3 L13: -0.0266 L23: 0.0167
REMARK 3 S TENSOR
REMARK 3 S11: 0.0122 S12: 0.0428 S13: -0.0010
REMARK 3 S21: 0.0725 S22: 0.0265 S23: 0.0258
REMARK 3 S31: 0.1104 S32: 0.0132 S33: -0.0387
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : P 1 P 244
REMARK 3 ORIGIN FOR THE GROUP (A): 8.4857-205.6574 6.4149
REMARK 3 T TENSOR
REMARK 3 T11: 0.2717 T22: 0.1983
REMARK 3 T33: 0.3018 T12: -0.0199
REMARK 3 T13: -0.1068 T23: -0.0737
REMARK 3 L TENSOR
REMARK 3 L11: 0.2651 L22: 0.2898
REMARK 3 L33: 0.1101 L12: 0.2163
REMARK 3 L13: 0.0372 L23: 0.1181
REMARK 3 S TENSOR
REMARK 3 S11: -0.0099 S12: -0.0273 S13: -0.0097
REMARK 3 S21: -0.0741 S22: -0.0043 S23: -0.0230
REMARK 3 S31: 0.0206 S32: 0.0054 S33: 0.0142
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Q 1 Q 240
REMARK 3 ORIGIN FOR THE GROUP (A): 35.5043-203.4101 -9.5078
REMARK 3 T TENSOR
REMARK 3 T11: 0.4765 T22: 0.1420
REMARK 3 T33: 0.2843 T12: 0.0861
REMARK 3 T13: -0.1093 T23: -0.1432
REMARK 3 L TENSOR
REMARK 3 L11: 0.2736 L22: 0.2666
REMARK 3 L33: 0.2447 L12: 0.2502
REMARK 3 L13: 0.1878 L23: 0.1734
REMARK 3 S TENSOR
REMARK 3 S11: 0.0803 S12: -0.0271 S13: -0.0068
REMARK 3 S21: -0.0928 S22: -0.0020 S23: 0.0398
REMARK 3 S31: 0.0389 S32: 0.1025 S33: -0.0784
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : R 1 R 242
REMARK 3 ORIGIN FOR THE GROUP (A): 65.0259-202.8732 2.8610
REMARK 3 T TENSOR
REMARK 3 T11: 0.2954 T22: 0.2148
REMARK 3 T33: 0.3632 T12: 0.0996
REMARK 3 T13: 0.1670 T23: -0.0651
REMARK 3 L TENSOR
REMARK 3 L11: 0.5194 L22: 0.4378
REMARK 3 L33: 0.1742 L12: -0.0443
REMARK 3 L13: 0.2974 L23: -0.0305
REMARK 3 S TENSOR
REMARK 3 S11: 0.1387 S12: -0.1353 S13: -0.0237
REMARK 3 S21: -0.2321 S22: -0.1204 S23: -0.1361
REMARK 3 S31: 0.1012 S32: -0.0546 S33: -0.0182
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : S 3 S 233
REMARK 3 ORIGIN FOR THE GROUP (A): 72.1696-204.1855 34.7310
REMARK 3 T TENSOR
REMARK 3 T11: 0.1009 T22: 0.2035
REMARK 3 T33: 0.7392 T12: 0.1207
REMARK 3 T13: -0.1002 T23: -0.1162
REMARK 3 L TENSOR
REMARK 3 L11: 0.2472 L22: 0.6474
REMARK 3 L33: 0.3022 L12: 0.3379
REMARK 3 L13: 0.0793 L23: -0.0942
REMARK 3 S TENSOR
REMARK 3 S11: 0.0862 S12: 0.0936 S13: -0.1734
REMARK 3 S21: 0.0624 S22: 0.0711 S23: -0.3083
REMARK 3 S31: 0.1163 S32: 0.0555 S33: -0.1573
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : T 2 T 244
REMARK 3 ORIGIN FOR THE GROUP (A): 54.4155-207.9261 59.0891
REMARK 3 T TENSOR
REMARK 3 T11: 0.3498 T22: 0.1362
REMARK 3 T33: 0.4464 T12: 0.0313
REMARK 3 T13: -0.2994 T23: 0.1273
REMARK 3 L TENSOR
REMARK 3 L11: 0.1080 L22: 0.0936
REMARK 3 L33: 0.0420 L12: 0.0946
REMARK 3 L13: -0.0352 L23: -0.0127
REMARK 3 S TENSOR
REMARK 3 S11: 0.1171 S12: 0.0047 S13: -0.1497
REMARK 3 S21: 0.1236 S22: -0.0673 S23: -0.1682
REMARK 3 S31: -0.0598 S32: -0.0659 S33: -0.0498
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : U 2 U 242
REMARK 3 ORIGIN FOR THE GROUP (A): 22.0799-210.0866 60.8479
REMARK 3 T TENSOR
REMARK 3 T11: 0.4289 T22: 0.1633
REMARK 3 T33: 0.2583 T12: -0.0249
REMARK 3 T13: -0.1140 T23: 0.1058
REMARK 3 L TENSOR
REMARK 3 L11: 0.0358 L22: 0.0411
REMARK 3 L33: 0.0240 L12: -0.0032
REMARK 3 L13: 0.0225 L23: -0.0009
REMARK 3 S TENSOR
REMARK 3 S11: 0.0680 S12: 0.0502 S13: -0.0207
REMARK 3 S21: 0.1004 S22: -0.0147 S23: 0.0080
REMARK 3 S31: 0.0622 S32: 0.0021 S33: -0.0533
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : V 1 V 222
REMARK 3 ORIGIN FOR THE GROUP (A): 1.5147-169.8331 45.6013
REMARK 3 T TENSOR
REMARK 3 T11: 0.0717 T22: 0.3087
REMARK 3 T33: 0.2769 T12: -0.0242
REMARK 3 T13: 0.0776 T23: 0.0701
REMARK 3 L TENSOR
REMARK 3 L11: 0.1723 L22: 0.2274
REMARK 3 L33: 0.3627 L12: -0.0595
REMARK 3 L13: 0.2475 L23: -0.0927
REMARK 3 S TENSOR
REMARK 3 S11: 0.0400 S12: 0.0451 S13: -0.0138
REMARK 3 S21: -0.0028 S22: 0.0099 S23: 0.1882
REMARK 3 S31: 0.0349 S32: 0.0451 S33: -0.0499
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : W 1 W 204
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0395-167.5645 18.1594
REMARK 3 T TENSOR
REMARK 3 T11: 0.0846 T22: 0.2305
REMARK 3 T33: 0.2905 T12: -0.0140
REMARK 3 T13: -0.0756 T23: 0.0259
REMARK 3 L TENSOR
REMARK 3 L11: 0.4034 L22: 0.6567
REMARK 3 L33: 0.1001 L12: -0.0774
REMARK 3 L13: 0.1111 L23: -0.0768
REMARK 3 S TENSOR
REMARK 3 S11: 0.0381 S12: -0.0131 S13: 0.0280
REMARK 3 S21: -0.1604 S22: 0.0139 S23: 0.1561
REMARK 3 S31: 0.0631 S32: 0.0685 S33: -0.0521
REMARK 3
REMARK 3 TLS GROUP : 24
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : X 1 X 195
REMARK 3 ORIGIN FOR THE GROUP (A): 23.0194-164.4471 -3.8209
REMARK 3 T TENSOR
REMARK 3 T11: 0.3164 T22: 0.2420
REMARK 3 T33: 0.1425 T12: -0.0019
REMARK 3 T13: -0.0465 T23: -0.0380
REMARK 3 L TENSOR
REMARK 3 L11: 0.0813 L22: 0.2011
REMARK 3 L33: 0.0070 L12: 0.0854
REMARK 3 L13: -0.0117 L23: -0.0070
REMARK 3 S TENSOR
REMARK 3 S11: 0.0097 S12: -0.0307 S13: -0.0286
REMARK 3 S21: -0.1572 S22: 0.0063 S23: 0.0268
REMARK 3 S31: -0.0159 S32: 0.0263 S33: -0.0160
REMARK 3
REMARK 3 TLS GROUP : 25
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Y 1 Y 212
REMARK 3 ORIGIN FOR THE GROUP (A): 56.9808-160.6357 -0.8475
REMARK 3 T TENSOR
REMARK 3 T11: 0.2034 T22: 0.3245
REMARK 3 T33: 0.2523 T12: 0.0318
REMARK 3 T13: 0.1551 T23: -0.0622
REMARK 3 L TENSOR
REMARK 3 L11: 0.3492 L22: 0.8471
REMARK 3 L33: 0.1571 L12: 0.3936
REMARK 3 L13: 0.1757 L23: 0.0767
REMARK 3 S TENSOR
REMARK 3 S11: 0.0280 S12: 0.0018 S13: -0.0713
REMARK 3 S21: -0.1262 S22: 0.0449 S23: -0.1200
REMARK 3 S31: 0.0625 S32: 0.0037 S33: -0.0729
REMARK 3
REMARK 3 TLS GROUP : 26
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Z 1 Z 222
REMARK 3 ORIGIN FOR THE GROUP (A): 73.1141-161.7967 25.1364
REMARK 3 T TENSOR
REMARK 3 T11: 0.0745 T22: 0.3324
REMARK 3 T33: 0.4973 T12: 0.0311
REMARK 3 T13: 0.0142 T23: -0.0427
REMARK 3 L TENSOR
REMARK 3 L11: 0.0296 L22: 0.4992
REMARK 3 L33: 0.3468 L12: 0.0959
REMARK 3 L13: -0.0993 L23: -0.3328
REMARK 3 S TENSOR
REMARK 3 S11: -0.0090 S12: 0.0135 S13: -0.0288
REMARK 3 S21: 0.0697 S22: -0.0444 S23: -0.2384
REMARK 3 S31: -0.0189 S32: -0.0731 S33: 0.0534
REMARK 3
REMARK 3 TLS GROUP : 27
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : a 1 a 233
REMARK 3 ORIGIN FOR THE GROUP (A): 61.6293-164.0009 57.4107
REMARK 3 T TENSOR
REMARK 3 T11: 0.2863 T22: 0.2603
REMARK 3 T33: 0.3328 T12: 0.0068
REMARK 3 T13: -0.1596 T23: 0.0167
REMARK 3 L TENSOR
REMARK 3 L11: 0.1669 L22: 0.2107
REMARK 3 L33: 0.0239 L12: 0.0321
REMARK 3 L13: -0.0148 L23: 0.0528
REMARK 3 S TENSOR
REMARK 3 S11: 0.0339 S12: 0.0817 S13: -0.1008
REMARK 3 S21: 0.1896 S22: -0.0003 S23: -0.1633
REMARK 3 S31: 0.0245 S32: -0.0392 S33: -0.0336
REMARK 3
REMARK 3 TLS GROUP : 28
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : b 1 b 196
REMARK 3 ORIGIN FOR THE GROUP (A): 29.8464-169.7123 67.6837
REMARK 3 T TENSOR
REMARK 3 T11: 0.3600 T22: 0.2635
REMARK 3 T33: 0.1557 T12: -0.0253
REMARK 3 T13: 0.0044 T23: 0.0583
REMARK 3 L TENSOR
REMARK 3 L11: 0.0526 L22: 0.3635
REMARK 3 L33: 0.0127 L12: 0.0866
REMARK 3 L13: -0.0025 L23: 0.0429
REMARK 3 S TENSOR
REMARK 3 S11: 0.0728 S12: 0.0758 S13: -0.0043
REMARK 3 S21: 0.2370 S22: -0.0491 S23: -0.0497
REMARK 3 S31: 0.0329 S32: -0.0472 S33: -0.0238
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5BXN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-JUN-15.
REMARK 100 THE DEPOSITION ID IS D_1000210730.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-FEB-14
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 : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : LN2 COOLED FIXED-EXIT. SI(111)
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 249805
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.45300
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: REFMAC
REMARK 200 STARTING MODEL: 1RYP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 MM MGAC2, 13% MPD, 0.1 M MES, PH
REMARK 280 6.8, 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 150.43000
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 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, a, b
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 0
REMARK 465 LYS B 245
REMARK 465 LYS B 246
REMARK 465 ASP B 247
REMARK 465 GLU B 248
REMARK 465 ASP B 249
REMARK 465 GLU B 250
REMARK 465 GLU B 251
REMARK 465 ALA B 252
REMARK 465 ASP B 253
REMARK 465 GLU B 254
REMARK 465 ASP B 255
REMARK 465 MET B 256
REMARK 465 LYS B 257
REMARK 465 MET C -1
REMARK 465 SER C 0
REMARK 465 GLN C 241
REMARK 465 GLN C 242
REMARK 465 GLU C 243
REMARK 465 GLN C 244
REMARK 465 ASP C 245
REMARK 465 LYS C 246
REMARK 465 LYS C 247
REMARK 465 LYS C 248
REMARK 465 LYS C 249
REMARK 465 SER C 250
REMARK 465 ASN C 251
REMARK 465 HIS C 252
REMARK 465 MET D -7
REMARK 465 PHE D -6
REMARK 465 LEU D -5
REMARK 465 THR D -4
REMARK 465 ARG D -3
REMARK 465 SER D -2
REMARK 465 GLU D -1
REMARK 465 TYR D 0
REMARK 465 GLY D 118
REMARK 465 ALA D 119
REMARK 465 SER D 120
REMARK 465 GLY D 121
REMARK 465 GLU D 122
REMARK 465 GLU D 123
REMARK 465 ARG D 124
REMARK 465 SER D 243
REMARK 465 PRO D 244
REMARK 465 GLU D 245
REMARK 465 GLU D 246
REMARK 465 ALA D 247
REMARK 465 ASP D 248
REMARK 465 VAL D 249
REMARK 465 GLU D 250
REMARK 465 MET D 251
REMARK 465 SER D 252
REMARK 465 MET E 0
REMARK 465 PHE E 1
REMARK 465 ARG E 2
REMARK 465 MET F -3
REMARK 465 THR F -2
REMARK 465 SER F -1
REMARK 465 ILE F 0
REMARK 465 GLY F 1
REMARK 465 GLY F 245
REMARK 465 ASP F 246
REMARK 465 ASP F 247
REMARK 465 ASP F 248
REMARK 465 GLU F 249
REMARK 465 ASP F 250
REMARK 465 GLU F 251
REMARK 465 ASP F 252
REMARK 465 ASP F 253
REMARK 465 SER F 254
REMARK 465 ASP F 255
REMARK 465 ASN F 256
REMARK 465 VAL F 257
REMARK 465 MET F 258
REMARK 465 SER F 259
REMARK 465 SER F 260
REMARK 465 ASP F 261
REMARK 465 ASP F 262
REMARK 465 GLU F 263
REMARK 465 ASN F 264
REMARK 465 ALA F 265
REMARK 465 PRO F 266
REMARK 465 VAL F 267
REMARK 465 ALA F 268
REMARK 465 THR F 269
REMARK 465 ASN F 270
REMARK 465 ALA F 271
REMARK 465 ASN F 272
REMARK 465 ALA F 273
REMARK 465 THR F 274
REMARK 465 THR F 275
REMARK 465 ASP F 276
REMARK 465 GLN F 277
REMARK 465 GLU F 278
REMARK 465 GLY F 279
REMARK 465 ASP F 280
REMARK 465 ILE F 281
REMARK 465 HIS F 282
REMARK 465 LEU F 283
REMARK 465 GLU F 284
REMARK 465 MET G -8
REMARK 465 SER G -7
REMARK 465 GLY G -6
REMARK 465 ALA G -5
REMARK 465 ALA G -4
REMARK 465 ALA G -3
REMARK 465 ALA G -2
REMARK 465 SER G -1
REMARK 465 ALA G 0
REMARK 465 ALA G 1
REMARK 465 ASP G 243
REMARK 465 ILE H 223
REMARK 465 GLN H 224
REMARK 465 GLU H 225
REMARK 465 GLU H 226
REMARK 465 GLN H 227
REMARK 465 VAL H 228
REMARK 465 ASP H 229
REMARK 465 ILE H 230
REMARK 465 THR H 231
REMARK 465 ALA H 232
REMARK 465 MET I 0
REMARK 465 GLN J 196
REMARK 465 ALA J 197
REMARK 465 GLN J 198
REMARK 465 THR M -12
REMARK 465 GLN M -11
REMARK 465 ILE M -10
REMARK 465 ALA M -9
REMARK 465 ASN M -8
REMARK 465 ALA M -7
REMARK 465 GLY M -6
REMARK 465 ALA M -5
REMARK 465 SER M -4
REMARK 465 PRO M -3
REMARK 465 MET M -2
REMARK 465 VAL M -1
REMARK 465 ASN M 0
REMARK 465 MET P 0
REMARK 465 LYS P 245
REMARK 465 LYS P 246
REMARK 465 ASP P 247
REMARK 465 GLU P 248
REMARK 465 ASP P 249
REMARK 465 GLU P 250
REMARK 465 GLU P 251
REMARK 465 ALA P 252
REMARK 465 ASP P 253
REMARK 465 GLU P 254
REMARK 465 ASP P 255
REMARK 465 MET P 256
REMARK 465 LYS P 257
REMARK 465 MET Q -1
REMARK 465 SER Q 0
REMARK 465 GLN Q 241
REMARK 465 GLN Q 242
REMARK 465 GLU Q 243
REMARK 465 GLN Q 244
REMARK 465 ASP Q 245
REMARK 465 LYS Q 246
REMARK 465 LYS Q 247
REMARK 465 LYS Q 248
REMARK 465 LYS Q 249
REMARK 465 SER Q 250
REMARK 465 ASN Q 251
REMARK 465 HIS Q 252
REMARK 465 MET R -7
REMARK 465 PHE R -6
REMARK 465 LEU R -5
REMARK 465 THR R -4
REMARK 465 ARG R -3
REMARK 465 SER R -2
REMARK 465 GLU R -1
REMARK 465 TYR R 0
REMARK 465 GLY R 118
REMARK 465 ALA R 119
REMARK 465 SER R 120
REMARK 465 GLY R 121
REMARK 465 GLU R 122
REMARK 465 GLU R 123
REMARK 465 ARG R 124
REMARK 465 SER R 243
REMARK 465 PRO R 244
REMARK 465 GLU R 245
REMARK 465 GLU R 246
REMARK 465 ALA R 247
REMARK 465 ASP R 248
REMARK 465 VAL R 249
REMARK 465 GLU R 250
REMARK 465 MET R 251
REMARK 465 SER R 252
REMARK 465 MET S 0
REMARK 465 PHE S 1
REMARK 465 ARG S 2
REMARK 465 MET T -3
REMARK 465 THR T -2
REMARK 465 SER T -1
REMARK 465 ILE T 0
REMARK 465 GLY T 1
REMARK 465 GLY T 245
REMARK 465 ASP T 246
REMARK 465 ASP T 247
REMARK 465 ASP T 248
REMARK 465 GLU T 249
REMARK 465 ASP T 250
REMARK 465 GLU T 251
REMARK 465 ASP T 252
REMARK 465 ASP T 253
REMARK 465 SER T 254
REMARK 465 ASP T 255
REMARK 465 ASN T 256
REMARK 465 VAL T 257
REMARK 465 MET T 258
REMARK 465 SER T 259
REMARK 465 SER T 260
REMARK 465 ASP T 261
REMARK 465 ASP T 262
REMARK 465 GLU T 263
REMARK 465 ASN T 264
REMARK 465 ALA T 265
REMARK 465 PRO T 266
REMARK 465 VAL T 267
REMARK 465 ALA T 268
REMARK 465 THR T 269
REMARK 465 ASN T 270
REMARK 465 ALA T 271
REMARK 465 ASN T 272
REMARK 465 ALA T 273
REMARK 465 THR T 274
REMARK 465 THR T 275
REMARK 465 ASP T 276
REMARK 465 GLN T 277
REMARK 465 GLU T 278
REMARK 465 GLY T 279
REMARK 465 ASP T 280
REMARK 465 ILE T 281
REMARK 465 HIS T 282
REMARK 465 LEU T 283
REMARK 465 GLU T 284
REMARK 465 MET U -8
REMARK 465 SER U -7
REMARK 465 GLY U -6
REMARK 465 ALA U -5
REMARK 465 ALA U -4
REMARK 465 ALA U -3
REMARK 465 ALA U -2
REMARK 465 SER U -1
REMARK 465 ALA U 0
REMARK 465 ALA U 1
REMARK 465 ASP U 243
REMARK 465 ILE V 223
REMARK 465 GLN V 224
REMARK 465 GLU V 225
REMARK 465 GLU V 226
REMARK 465 GLN V 227
REMARK 465 VAL V 228
REMARK 465 ASP V 229
REMARK 465 ILE V 230
REMARK 465 THR V 231
REMARK 465 ALA V 232
REMARK 465 MET W 0
REMARK 465 GLN X 196
REMARK 465 ALA X 197
REMARK 465 GLN X 198
REMARK 465 THR a -12
REMARK 465 GLN a -11
REMARK 465 ILE a -10
REMARK 465 ALA a -9
REMARK 465 ASN a -8
REMARK 465 ALA a -7
REMARK 465 GLY a -6
REMARK 465 ALA a -5
REMARK 465 SER a -4
REMARK 465 PRO a -3
REMARK 465 MET a -2
REMARK 465 VAL a -1
REMARK 465 ASN a 0
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 OXT ASP Z 222 MG MG H 302 1.58
REMARK 500 OH TYR J 139 O ILE X 25 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 VAL H 4 CB VAL H 4 CG1 -0.139
REMARK 500 VAL H 4 CB VAL H 4 CG2 -0.138
REMARK 500 VAL V 4 CB VAL V 4 CG1 -0.132
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 VAL H 4 CG1 - CB - CG2 ANGL. DEV. = -26.1 DEGREES
REMARK 500 PRO H 193 C - N - CD ANGL. DEV. = 12.7 DEGREES
REMARK 500 ARG J 149 CD - NE - CZ ANGL. DEV. = 10.6 DEGREES
REMARK 500 ARG J 149 NE - CZ - NH1 ANGL. DEV. = -8.0 DEGREES
REMARK 500 ARG J 149 NE - CZ - NH2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 VAL V 4 CG1 - CB - CG2 ANGL. DEV. = -26.2 DEGREES
REMARK 500 ARG X 23 CG - CD - NE ANGL. DEV. = 12.7 DEGREES
REMARK 500 ARG X 149 CD - NE - CZ ANGL. DEV. = 17.1 DEGREES
REMARK 500 ARG X 149 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG X 149 NE - CZ - NH2 ANGL. DEV. = -10.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR A 2 139.85 58.51
REMARK 500 TYR A 97 -67.11 -148.86
REMARK 500 ALA A 249 46.07 -95.74
REMARK 500 ARG B 8 74.96 61.32
REMARK 500 THR B 10 56.93 -114.35
REMARK 500 VAL B 51 88.96 -6.40
REMARK 500 LYS B 64 -51.03 -122.28
REMARK 500 ASN B 220 100.53 -53.26
REMARK 500 ASP B 221 -179.12 72.33
REMARK 500 PRO C 183 105.48 -43.75
REMARK 500 GLN C 202 -96.65 111.03
REMARK 500 ALA C 205 -105.27 -82.76
REMARK 500 SER D 5 33.92 -99.75
REMARK 500 ARG D 45 71.64 55.98
REMARK 500 SER E 39 -155.85 -112.46
REMARK 500 ASP E 137 -160.00 -122.97
REMARK 500 ASP E 202 -58.36 66.33
REMARK 500 ASP F 67 -132.87 56.48
REMARK 500 LYS F 100 -54.23 76.28
REMARK 500 ASP F 138 -169.15 -126.75
REMARK 500 ASN H 30 57.48 -147.61
REMARK 500 ASP H 145 59.34 70.77
REMARK 500 SER H 171 -125.22 68.23
REMARK 500 LEU H 187 78.31 -104.85
REMARK 500 VAL H 195 -104.60 62.14
REMARK 500 ARG H 196 150.57 89.70
REMARK 500 GLN I 31 -109.58 61.00
REMARK 500 ASP I 192 33.57 -148.09
REMARK 500 GLN I 203 49.96 -103.39
REMARK 500 ASP J 2 -93.29 -105.76
REMARK 500 VAL J 9 -167.07 -104.49
REMARK 500 SER J 31 34.60 -150.13
REMARK 500 ASP L 32 -116.28 54.07
REMARK 500 PHE L 103 67.35 -162.50
REMARK 500 ASN L 165 73.97 50.49
REMARK 500 ASP L 200 -66.20 67.98
REMARK 500 ILE M 5 -78.83 -108.37
REMARK 500 THR M 9 -151.97 -88.28
REMARK 500 ALA M 83 -113.35 -145.31
REMARK 500 LYS N 107 -147.65 66.00
REMARK 500 THR O 2 139.91 58.65
REMARK 500 TYR O 97 -67.36 -148.03
REMARK 500 ALA O 249 46.05 -95.60
REMARK 500 ARG P 8 75.06 61.69
REMARK 500 THR P 10 56.69 -113.74
REMARK 500 VAL P 51 89.08 -6.66
REMARK 500 LYS P 64 -50.97 -122.37
REMARK 500 ASN P 220 100.46 -53.42
REMARK 500 ASP P 221 -179.03 72.53
REMARK 500 PRO Q 183 105.42 -43.83
REMARK 500
REMARK 500 THIS ENTRY HAS 81 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PRO V 193 ASN V 194 -132.26
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 ARG X 149 0.15 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG G 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR G 8 OG1
REMARK 620 2 TYR G 119 O 73.7
REMARK 620 3 ARG G 122 O 75.7 67.7
REMARK 620 4 MET G 125 O 145.8 73.6 83.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG H 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE H 163 O
REMARK 620 2 ASP H 166 O 115.8
REMARK 620 3 SER H 169 O 97.2 84.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG I 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA I 174 O
REMARK 620 2 ASP I 177 O 66.1
REMARK 620 3 SER I 180 O 80.8 84.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG I 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP I 204 O
REMARK 620 2 ALA Y 165 O 107.0
REMARK 620 3 ASP Y 168 O 161.2 91.0
REMARK 620 4 SER Y 171 O 95.6 85.1 80.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG K 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA K 165 O
REMARK 620 2 ASP K 168 O 100.4
REMARK 620 3 ASP W 204 O 96.7 148.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG L 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP L 222 OXT
REMARK 620 2 ILE V 163 O 93.0
REMARK 620 3 ASP V 166 O 142.2 123.3
REMARK 620 4 SER V 169 O 106.4 88.6 86.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG N 202 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE N 163 O
REMARK 620 2 ASP N 166 O 71.9
REMARK 620 3 SER N 169 O 100.1 70.8
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG G 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL G 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BO2 H 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG I 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG J 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BO2 K 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG K 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BO2 N 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG N 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL N 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL U 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG L 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG I 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG Z 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG H 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL b 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide BO2 V 301 and THR V
REMARK 800 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide BO2 Y 301 and THR Y
REMARK 800 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide BO2 b 201 and THR b
REMARK 800 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1RYP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE 20S PROTEASOME FROM YEAST AT 2.4 ANGSTROMS
REMARK 900 RESOLUTION
DBREF 5BXN A 1 250 UNP P23639 PSA2_YEAST 1 250
DBREF 5BXN B 0 257 UNP P23638 PSA3_YEAST 1 258
DBREF 5BXN C -1 252 UNP P40303 PSA4_YEAST 1 254
DBREF 5BXN D -7 252 UNP P32379 PSA5_YEAST 1 260
DBREF 5BXN E 0 233 UNP P40302 PSA6_YEAST 1 234
DBREF 5BXN F -3 284 UNP P21242 PSA7_YEAST 1 288
DBREF 5BXN G -8 243 UNP P21243 PSA1_YEAST 1 252
DBREF 5BXN H 1 232 UNP P25043 PSB2_YEAST 30 261
DBREF 5BXN I 0 204 UNP P25451 PSB3_YEAST 1 205
DBREF 5BXN J 1 198 UNP P22141 PSB4_YEAST 1 198
DBREF 5BXN K 1 212 UNP P30656 PSB5_YEAST 76 287
DBREF 5BXN L 1 222 UNP P23724 PSB6_YEAST 20 241
DBREF 5BXN M -12 233 UNP P30657 PSB7_YEAST 21 266
DBREF 5BXN N 1 196 UNP P38624 PSB1_YEAST 20 215
DBREF 5BXN O 1 250 UNP P23639 PSA2_YEAST 1 250
DBREF 5BXN P 0 257 UNP P23638 PSA3_YEAST 1 258
DBREF 5BXN Q -1 252 UNP P40303 PSA4_YEAST 1 254
DBREF 5BXN R -7 252 UNP P32379 PSA5_YEAST 1 260
DBREF 5BXN S 0 233 UNP P40302 PSA6_YEAST 1 234
DBREF 5BXN T -3 284 UNP P21242 PSA7_YEAST 1 288
DBREF 5BXN U -8 243 UNP P21243 PSA1_YEAST 1 252
DBREF 5BXN V 1 232 UNP P25043 PSB2_YEAST 30 261
DBREF 5BXN W 0 204 UNP P25451 PSB3_YEAST 1 205
DBREF 5BXN X 1 198 UNP P22141 PSB4_YEAST 1 198
DBREF 5BXN Y 1 212 UNP P30656 PSB5_YEAST 76 287
DBREF 5BXN Z 1 222 UNP P23724 PSB6_YEAST 20 241
DBREF 5BXN a -12 233 UNP P30657 PSB7_YEAST 21 266
DBREF 5BXN b 1 196 UNP P38624 PSB1_YEAST 20 215
SEQADV 5BXN ALA H 170 UNP P25043 GLY 199 ENGINEERED MUTATION
SEQADV 5BXN ALA V 170 UNP P25043 GLY 199 ENGINEERED MUTATION
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 288 MET THR SER ILE GLY THR GLY TYR ASP LEU SER ASN SER
SEQRES 2 F 288 VAL PHE SER PRO ASP GLY ARG ASN PHE GLN VAL GLU TYR
SEQRES 3 F 288 ALA VAL LYS ALA VAL GLU ASN GLY THR THR SER ILE GLY
SEQRES 4 F 288 ILE LYS CYS ASN ASP GLY VAL VAL PHE ALA VAL GLU LYS
SEQRES 5 F 288 LEU ILE THR SER LYS LEU LEU VAL PRO GLN LYS ASN VAL
SEQRES 6 F 288 LYS ILE GLN VAL VAL ASP ARG HIS ILE GLY CYS VAL TYR
SEQRES 7 F 288 SER GLY LEU ILE PRO ASP GLY ARG HIS LEU VAL ASN ARG
SEQRES 8 F 288 GLY ARG GLU GLU ALA ALA SER PHE LYS LYS LEU TYR LYS
SEQRES 9 F 288 THR PRO ILE PRO ILE PRO ALA PHE ALA ASP ARG LEU GLY
SEQRES 10 F 288 GLN TYR VAL GLN ALA HIS THR LEU TYR ASN SER VAL ARG
SEQRES 11 F 288 PRO PHE GLY VAL SER THR ILE PHE GLY GLY VAL ASP LYS
SEQRES 12 F 288 ASN GLY ALA HIS LEU TYR MET LEU GLU PRO SER GLY SER
SEQRES 13 F 288 TYR TRP GLY TYR LYS GLY ALA ALA THR GLY LYS GLY ARG
SEQRES 14 F 288 GLN SER ALA LYS ALA GLU LEU GLU LYS LEU VAL ASP HIS
SEQRES 15 F 288 HIS PRO GLU GLY LEU SER ALA ARG GLU ALA VAL LYS GLN
SEQRES 16 F 288 ALA ALA LYS ILE ILE TYR LEU ALA HIS GLU ASP ASN LYS
SEQRES 17 F 288 GLU LYS ASP PHE GLU LEU GLU ILE SER TRP CYS SER LEU
SEQRES 18 F 288 SER GLU THR ASN GLY LEU HIS LYS PHE VAL LYS GLY ASP
SEQRES 19 F 288 LEU LEU GLN GLU ALA ILE ASP PHE ALA GLN LYS GLU ILE
SEQRES 20 F 288 ASN GLY ASP ASP ASP GLU ASP GLU ASP ASP SER ASP ASN
SEQRES 21 F 288 VAL MET SER SER ASP ASP GLU ASN ALA PRO VAL ALA THR
SEQRES 22 F 288 ASN ALA ASN ALA THR THR ASP GLN GLU GLY ASP ILE HIS
SEQRES 23 F 288 LEU 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 ALA 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 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 246 THR GLN ILE ALA ASN ALA GLY ALA SER PRO MET VAL ASN
SEQRES 2 M 246 THR GLN GLN PRO ILE VAL THR GLY THR SER VAL ILE SER
SEQRES 3 M 246 MET LYS TYR ASP ASN GLY VAL ILE ILE ALA ALA ASP ASN
SEQRES 4 M 246 LEU GLY SER TYR GLY SER LEU LEU ARG PHE ASN GLY VAL
SEQRES 5 M 246 GLU ARG LEU ILE PRO VAL GLY ASP ASN THR VAL VAL GLY
SEQRES 6 M 246 ILE SER GLY ASP ILE SER ASP MET GLN HIS ILE GLU ARG
SEQRES 7 M 246 LEU LEU LYS ASP LEU VAL THR GLU ASN ALA TYR ASP ASN
SEQRES 8 M 246 PRO LEU ALA ASP ALA GLU GLU ALA LEU GLU PRO SER TYR
SEQRES 9 M 246 ILE PHE GLU TYR LEU ALA THR VAL MET TYR GLN ARG ARG
SEQRES 10 M 246 SER LYS MET ASN PRO LEU TRP ASN ALA ILE ILE VAL ALA
SEQRES 11 M 246 GLY VAL GLN SER ASN GLY ASP GLN PHE LEU ARG TYR VAL
SEQRES 12 M 246 ASN LEU LEU GLY VAL THR TYR SER SER PRO THR LEU ALA
SEQRES 13 M 246 THR GLY PHE GLY ALA HIS MET ALA ASN PRO LEU LEU ARG
SEQRES 14 M 246 LYS VAL VAL ASP ARG GLU SER ASP ILE PRO LYS THR THR
SEQRES 15 M 246 VAL GLN VAL ALA GLU GLU ALA ILE VAL ASN ALA MET ARG
SEQRES 16 M 246 VAL LEU TYR TYR ARG ASP ALA ARG SER SER ARG ASN PHE
SEQRES 17 M 246 SER LEU ALA ILE ILE ASP LYS ASN THR GLY LEU THR PHE
SEQRES 18 M 246 LYS LYS ASN LEU GLN VAL GLU ASN MET LYS TRP ASP PHE
SEQRES 19 M 246 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 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 288 MET THR SER ILE GLY THR GLY TYR ASP LEU SER ASN SER
SEQRES 2 T 288 VAL PHE SER PRO ASP GLY ARG ASN PHE GLN VAL GLU TYR
SEQRES 3 T 288 ALA VAL LYS ALA VAL GLU ASN GLY THR THR SER ILE GLY
SEQRES 4 T 288 ILE LYS CYS ASN ASP GLY VAL VAL PHE ALA VAL GLU LYS
SEQRES 5 T 288 LEU ILE THR SER LYS LEU LEU VAL PRO GLN LYS ASN VAL
SEQRES 6 T 288 LYS ILE GLN VAL VAL ASP ARG HIS ILE GLY CYS VAL TYR
SEQRES 7 T 288 SER GLY LEU ILE PRO ASP GLY ARG HIS LEU VAL ASN ARG
SEQRES 8 T 288 GLY ARG GLU GLU ALA ALA SER PHE LYS LYS LEU TYR LYS
SEQRES 9 T 288 THR PRO ILE PRO ILE PRO ALA PHE ALA ASP ARG LEU GLY
SEQRES 10 T 288 GLN TYR VAL GLN ALA HIS THR LEU TYR ASN SER VAL ARG
SEQRES 11 T 288 PRO PHE GLY VAL SER THR ILE PHE GLY GLY VAL ASP LYS
SEQRES 12 T 288 ASN GLY ALA HIS LEU TYR MET LEU GLU PRO SER GLY SER
SEQRES 13 T 288 TYR TRP GLY TYR LYS GLY ALA ALA THR GLY LYS GLY ARG
SEQRES 14 T 288 GLN SER ALA LYS ALA GLU LEU GLU LYS LEU VAL ASP HIS
SEQRES 15 T 288 HIS PRO GLU GLY LEU SER ALA ARG GLU ALA VAL LYS GLN
SEQRES 16 T 288 ALA ALA LYS ILE ILE TYR LEU ALA HIS GLU ASP ASN LYS
SEQRES 17 T 288 GLU LYS ASP PHE GLU LEU GLU ILE SER TRP CYS SER LEU
SEQRES 18 T 288 SER GLU THR ASN GLY LEU HIS LYS PHE VAL LYS GLY ASP
SEQRES 19 T 288 LEU LEU GLN GLU ALA ILE ASP PHE ALA GLN LYS GLU ILE
SEQRES 20 T 288 ASN GLY ASP ASP ASP GLU ASP GLU ASP ASP SER ASP ASN
SEQRES 21 T 288 VAL MET SER SER ASP ASP GLU ASN ALA PRO VAL ALA THR
SEQRES 22 T 288 ASN ALA ASN ALA THR THR ASP GLN GLU GLY ASP ILE HIS
SEQRES 23 T 288 LEU 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 ALA 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 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 a 246 THR GLN ILE ALA ASN ALA GLY ALA SER PRO MET VAL ASN
SEQRES 2 a 246 THR GLN GLN PRO ILE VAL THR GLY THR SER VAL ILE SER
SEQRES 3 a 246 MET LYS TYR ASP ASN GLY VAL ILE ILE ALA ALA ASP ASN
SEQRES 4 a 246 LEU GLY SER TYR GLY SER LEU LEU ARG PHE ASN GLY VAL
SEQRES 5 a 246 GLU ARG LEU ILE PRO VAL GLY ASP ASN THR VAL VAL GLY
SEQRES 6 a 246 ILE SER GLY ASP ILE SER ASP MET GLN HIS ILE GLU ARG
SEQRES 7 a 246 LEU LEU LYS ASP LEU VAL THR GLU ASN ALA TYR ASP ASN
SEQRES 8 a 246 PRO LEU ALA ASP ALA GLU GLU ALA LEU GLU PRO SER TYR
SEQRES 9 a 246 ILE PHE GLU TYR LEU ALA THR VAL MET TYR GLN ARG ARG
SEQRES 10 a 246 SER LYS MET ASN PRO LEU TRP ASN ALA ILE ILE VAL ALA
SEQRES 11 a 246 GLY VAL GLN SER ASN GLY ASP GLN PHE LEU ARG TYR VAL
SEQRES 12 a 246 ASN LEU LEU GLY VAL THR TYR SER SER PRO THR LEU ALA
SEQRES 13 a 246 THR GLY PHE GLY ALA HIS MET ALA ASN PRO LEU LEU ARG
SEQRES 14 a 246 LYS VAL VAL ASP ARG GLU SER ASP ILE PRO LYS THR THR
SEQRES 15 a 246 VAL GLN VAL ALA GLU GLU ALA ILE VAL ASN ALA MET ARG
SEQRES 16 a 246 VAL LEU TYR TYR ARG ASP ALA ARG SER SER ARG ASN PHE
SEQRES 17 a 246 SER LEU ALA ILE ILE ASP LYS ASN THR GLY LEU THR PHE
SEQRES 18 a 246 LYS LYS ASN LEU GLN VAL GLU ASN MET LYS TRP ASP PHE
SEQRES 19 a 246 ALA LYS ASP ILE LYS GLY TYR GLY THR GLN LYS ILE
SEQRES 1 b 196 THR SER ILE MET ALA VAL THR PHE LYS ASP GLY VAL ILE
SEQRES 2 b 196 LEU GLY ALA ASP SER ARG THR THR THR GLY ALA TYR ILE
SEQRES 3 b 196 ALA ASN ARG VAL THR ASP LYS LEU THR ARG VAL HIS ASP
SEQRES 4 b 196 LYS ILE TRP CYS CYS ARG SER GLY SER ALA ALA ASP THR
SEQRES 5 b 196 GLN ALA ILE ALA ASP ILE VAL GLN TYR HIS LEU GLU LEU
SEQRES 6 b 196 TYR THR SER GLN TYR GLY THR PRO SER THR GLU THR ALA
SEQRES 7 b 196 ALA SER VAL PHE LYS GLU LEU CYS TYR GLU ASN LYS ASP
SEQRES 8 b 196 ASN LEU THR ALA GLY ILE ILE VAL ALA GLY TYR ASP ASP
SEQRES 9 b 196 LYS ASN LYS GLY GLU VAL TYR THR ILE PRO LEU GLY GLY
SEQRES 10 b 196 SER VAL HIS LYS LEU PRO TYR ALA ILE ALA GLY SER GLY
SEQRES 11 b 196 SER THR PHE ILE TYR GLY TYR CYS ASP LYS ASN PHE ARG
SEQRES 12 b 196 GLU ASN MET SER LYS GLU GLU THR VAL ASP PHE ILE LYS
SEQRES 13 b 196 HIS SER LEU SER GLN ALA ILE LYS TRP ASP GLY SER SER
SEQRES 14 b 196 GLY GLY VAL ILE ARG MET VAL VAL LEU THR ALA ALA GLY
SEQRES 15 b 196 VAL GLU ARG LEU ILE PHE TYR PRO ASP GLU TYR GLU GLN
SEQRES 16 b 196 LEU
HET MG G 301 1
HET CL G 302 1
HET BO2 H 301 28
HET MG H 302 1
HET MG I 301 1
HET MG I 302 1
HET MG J 201 1
HET BO2 K 301 28
HET MG K 302 1
HET MG L 301 1
HET BO2 N 201 28
HET MG N 202 1
HET CL N 203 1
HET CL U 301 1
HET BO2 V 301 28
HET BO2 Y 301 28
HET MG Z 301 1
HET BO2 b 201 28
HET CL b 202 1
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
HETNAM BO2 N-[(1R)-1-(DIHYDROXYBORYL)-3-METHYLBUTYL]-N-(PYRAZIN-2-
HETNAM 2 BO2 YLCARBONYL)-L-PHENYLALANINAMIDE
HETSYN BO2 BORTEZOMIB
FORMUL 29 MG 9(MG 2+)
FORMUL 30 CL 4(CL 1-)
FORMUL 31 BO2 6(C19 H25 B N4 O4)
FORMUL 48 HOH *374(H2 O)
HELIX 1 AA1 LEU A 18 GLY A 31 1 14
HELIX 2 AA2 MET A 78 SER A 96 1 19
HELIX 3 AA3 TYR A 97 GLY A 102 1 6
HELIX 4 AA4 PRO A 106 ALA A 121 1 16
HELIX 5 AA5 GLY A 167 TRP A 179 1 13
HELIX 6 AA6 GLU A 184 VAL A 200 1 17
HELIX 7 AA7 ASN A 218 LEU A 222 5 5
HELIX 8 AA8 THR A 239 ALA A 249 1 11
HELIX 9 AA9 GLY B 1 ASP B 6 5 6
HELIX 10 AB1 LEU B 18 SER B 29 1 12
HELIX 11 AB2 GLU B 57 SER B 61 5 5
HELIX 12 AB3 LEU B 79 ASN B 102 1 24
HELIX 13 AB4 PRO B 106 HIS B 124 1 19
HELIX 14 AB5 ASN B 167 TYR B 179 1 13
HELIX 15 AB6 LYS B 184 THR B 200 1 17
HELIX 16 AB7 THR B 206 ASP B 208 5 3
HELIX 17 AB8 LYS B 230 THR B 241 1 12
HELIX 18 AB9 ILE C 15 GLY C 28 1 14
HELIX 19 AC1 LEU C 76 GLU C 99 1 24
HELIX 20 AC2 THR C 103 TYR C 118 1 16
HELIX 21 AC3 ASN C 165 TYR C 177 1 13
HELIX 22 AC4 THR C 185 GLU C 199 1 15
HELIX 23 AC5 SER C 223 GLN C 239 1 17
HELIX 24 AC6 LEU D 13 LEU D 25 1 13
HELIX 25 AC7 GLU D 52 ILE D 56 5 5
HELIX 26 AC8 ASP D 76 ASP D 96 1 21
HELIX 27 AC9 ASN D 100 LEU D 113 1 14
HELIX 28 AD1 GLY D 167 TRP D 179 1 13
HELIX 29 AD2 THR D 184 MET D 200 1 17
HELIX 30 AD3 ASP D 224 ALA D 241 1 18
HELIX 31 AD4 LEU E 18 GLY E 31 1 14
HELIX 32 AD5 LEU E 76 ASN E 99 1 24
HELIX 33 AD6 ALA E 103 SER E 121 1 19
HELIX 34 AD7 ARG E 163 ILE E 179 1 17
HELIX 35 AD8 ASN E 184 SER E 197 1 14
HELIX 36 AD9 GLN E 198 LEU E 200 5 3
HELIX 37 AE1 ASP E 225 ILE E 233 5 9
HELIX 38 AE2 ASN F 17 GLY F 30 1 14
HELIX 39 AE3 LEU F 77 LYS F 100 1 24
HELIX 40 AE4 PRO F 104 HIS F 119 1 16
HELIX 41 AE5 GLY F 164 HIS F 179 1 16
HELIX 42 AE6 SER F 184 HIS F 200 1 17
HELIX 43 AE7 GLU F 201 LYS F 204 5 4
HELIX 44 AE8 LYS F 228 ASN F 244 1 17
HELIX 45 AE9 GLY G 2 HIS G 6 5 5
HELIX 46 AF1 LEU G 16 THR G 26 1 11
HELIX 47 AF2 ASP G 56 VAL G 60 5 5
HELIX 48 AF3 PRO G 77 GLY G 100 1 24
HELIX 49 AF4 PRO G 104 ARG G 122 1 19
HELIX 50 AF5 LYS G 165 LYS G 181 1 17
HELIX 51 AF6 SER G 189 GLY G 206 1 18
HELIX 52 AF7 SER G 228 GLU G 241 1 14
HELIX 53 AF8 THR H 48 SER H 71 1 24
HELIX 54 AF9 ARG H 75 TYR H 90 1 16
HELIX 55 AG1 GLY H 130 TRP H 142 1 13
HELIX 56 AG2 THR H 147 ASP H 166 1 20
HELIX 57 AG3 ASP I 2 ILE I 6 5 5
HELIX 58 AG4 LEU I 55 GLU I 78 1 24
HELIX 59 AG5 GLU I 82 GLU I 96 1 15
HELIX 60 AG6 ALA I 141 TYR I 153 1 13
HELIX 61 AG7 GLU I 158 ASP I 175 1 18
HELIX 62 AG8 GLY J 51 ASP J 72 1 22
HELIX 63 AG9 SER J 76 ILE J 92 1 17
HELIX 64 AH1 TYR J 135 TYR J 148 1 14
HELIX 65 AH2 THR J 153 MET J 172 1 20
HELIX 66 AH3 GLY K 48 LYS K 71 1 24
HELIX 67 AH4 SER K 75 TYR K 90 1 16
HELIX 68 AH5 GLY K 132 TYR K 144 1 13
HELIX 69 AH6 SER K 149 ASP K 168 1 20
HELIX 70 AH7 VAL K 193 GLY K 205 1 13
HELIX 71 AH8 PHE L 57 HIS L 79 1 23
HELIX 72 AH9 SER L 85 GLY L 99 1 15
HELIX 73 AI1 ALA L 142 VAL L 154 1 13
HELIX 74 AI2 SER L 176 HIS L 195 1 20
HELIX 75 AI3 ILE M 57 TYR M 76 1 20
HELIX 76 AI4 GLU M 88 LYS M 106 1 19
HELIX 77 AI5 GLY M 145 ARG M 156 1 12
HELIX 78 AI6 ARG M 161 ILE M 165 5 5
HELIX 79 AI7 THR M 169 ASP M 188 1 20
HELIX 80 AI8 TRP M 219 ILE M 225 5 7
HELIX 81 AI9 SER N 48 GLY N 71 1 24
HELIX 82 AJ1 SER N 74 ASN N 89 1 16
HELIX 83 AJ2 GLY N 128 PHE N 133 5 6
HELIX 84 AJ3 ILE N 134 PHE N 142 1 9
HELIX 85 AJ4 SER N 147 ASP N 166 1 20
HELIX 86 AJ5 TYR N 189 GLU N 194 1 6
HELIX 87 AJ6 LEU O 18 GLY O 31 1 14
HELIX 88 AJ7 MET O 78 SER O 96 1 19
HELIX 89 AJ8 TYR O 97 GLY O 102 1 6
HELIX 90 AJ9 PRO O 106 ALA O 121 1 16
HELIX 91 AK1 GLY O 167 TRP O 179 1 13
HELIX 92 AK2 GLU O 184 VAL O 200 1 17
HELIX 93 AK3 ASN O 218 LEU O 222 5 5
HELIX 94 AK4 THR O 239 ALA O 249 1 11
HELIX 95 AK5 GLY P 1 ASP P 6 5 6
HELIX 96 AK6 LEU P 18 SER P 29 1 12
HELIX 97 AK7 GLU P 57 SER P 61 5 5
HELIX 98 AK8 LEU P 79 ASN P 102 1 24
HELIX 99 AK9 PRO P 106 HIS P 124 1 19
HELIX 100 AL1 ASN P 167 TYR P 179 1 13
HELIX 101 AL2 LYS P 184 THR P 200 1 17
HELIX 102 AL3 THR P 206 ASP P 208 5 3
HELIX 103 AL4 LYS P 230 THR P 241 1 12
HELIX 104 AL5 ILE Q 15 GLY Q 28 1 14
HELIX 105 AL6 LEU Q 76 GLU Q 99 1 24
HELIX 106 AL7 THR Q 103 TYR Q 118 1 16
HELIX 107 AL8 ASN Q 165 TYR Q 177 1 13
HELIX 108 AL9 THR Q 185 GLU Q 199 1 15
HELIX 109 AM1 SER Q 223 GLN Q 239 1 17
HELIX 110 AM2 LEU R 13 LEU R 25 1 13
HELIX 111 AM3 GLU R 52 ILE R 56 5 5
HELIX 112 AM4 ASP R 76 ASP R 96 1 21
HELIX 113 AM5 ASN R 100 LEU R 113 1 14
HELIX 114 AM6 GLY R 167 TRP R 179 1 13
HELIX 115 AM7 THR R 184 MET R 200 1 17
HELIX 116 AM8 ASP R 224 ALA R 241 1 18
HELIX 117 AM9 LEU S 18 GLY S 31 1 14
HELIX 118 AN1 LEU S 76 ASN S 99 1 24
HELIX 119 AN2 ALA S 103 SER S 121 1 19
HELIX 120 AN3 ARG S 163 ILE S 179 1 17
HELIX 121 AN4 ASN S 184 SER S 197 1 14
HELIX 122 AN5 GLN S 198 LEU S 200 5 3
HELIX 123 AN6 ASP S 225 ILE S 233 5 9
HELIX 124 AN7 ASN T 17 GLY T 30 1 14
HELIX 125 AN8 LEU T 77 LYS T 100 1 24
HELIX 126 AN9 PRO T 104 HIS T 119 1 16
HELIX 127 AO1 GLY T 164 HIS T 179 1 16
HELIX 128 AO2 SER T 184 HIS T 200 1 17
HELIX 129 AO3 GLU T 201 LYS T 204 5 4
HELIX 130 AO4 LYS T 228 ASN T 244 1 17
HELIX 131 AO5 GLY U 2 HIS U 6 5 5
HELIX 132 AO6 LEU U 16 THR U 26 1 11
HELIX 133 AO7 ASP U 56 VAL U 60 5 5
HELIX 134 AO8 PRO U 77 GLY U 100 1 24
HELIX 135 AO9 PRO U 104 ARG U 122 1 19
HELIX 136 AP1 LYS U 165 LYS U 181 1 17
HELIX 137 AP2 SER U 189 GLY U 206 1 18
HELIX 138 AP3 SER U 228 GLU U 241 1 14
HELIX 139 AP4 THR V 48 SER V 71 1 24
HELIX 140 AP5 ARG V 75 TYR V 90 1 16
HELIX 141 AP6 GLY V 130 TRP V 142 1 13
HELIX 142 AP7 THR V 147 ASP V 166 1 20
HELIX 143 AP8 ASP W 2 ILE W 6 5 5
HELIX 144 AP9 LEU W 55 GLU W 78 1 24
HELIX 145 AQ1 GLU W 82 GLU W 96 1 15
HELIX 146 AQ2 ALA W 141 TYR W 153 1 13
HELIX 147 AQ3 GLU W 158 ASP W 175 1 18
HELIX 148 AQ4 GLY X 51 ASP X 72 1 22
HELIX 149 AQ5 SER X 76 ILE X 92 1 17
HELIX 150 AQ6 TYR X 135 TYR X 148 1 14
HELIX 151 AQ7 THR X 153 MET X 172 1 20
HELIX 152 AQ8 GLY Y 48 LYS Y 71 1 24
HELIX 153 AQ9 SER Y 75 TYR Y 90 1 16
HELIX 154 AR1 GLY Y 132 TYR Y 144 1 13
HELIX 155 AR2 SER Y 149 ASP Y 168 1 20
HELIX 156 AR3 VAL Y 193 GLY Y 205 1 13
HELIX 157 AR4 PHE Z 57 HIS Z 79 1 23
HELIX 158 AR5 SER Z 85 GLY Z 99 1 15
HELIX 159 AR6 ALA Z 142 VAL Z 154 1 13
HELIX 160 AR7 SER Z 176 HIS Z 195 1 20
HELIX 161 AR8 ILE a 57 TYR a 76 1 20
HELIX 162 AR9 GLU a 88 LYS a 106 1 19
HELIX 163 AS1 GLY a 145 ARG a 156 1 12
HELIX 164 AS2 ARG a 161 ILE a 165 5 5
HELIX 165 AS3 THR a 169 ASP a 188 1 20
HELIX 166 AS4 TRP a 219 ILE a 225 5 7
HELIX 167 AS5 SER b 48 GLY b 71 1 24
HELIX 168 AS6 SER b 74 ASN b 89 1 16
HELIX 169 AS7 GLY b 128 PHE b 133 5 6
HELIX 170 AS8 ILE b 134 PHE b 142 1 9
HELIX 171 AS9 SER b 147 ASP b 166 1 20
HELIX 172 AT1 TYR b 189 GLU b 194 1 6
SHEET 1 AA1 5 ALA A 161 ILE A 164 0
SHEET 2 AA1 5 SER A 34 LYS A 38 -1 N SER A 34 O ILE A 164
SHEET 3 AA1 5 VAL A 43 GLU A 48 -1 O VAL A 44 N ILE A 37
SHEET 4 AA1 5 ILE A 209 ILE A 214 -1 O ILE A 214 N VAL A 43
SHEET 5 AA1 5 PHE A 235 LYS A 237 -1 O ARG A 236 N ILE A 213
SHEET 1 AA2 5 SER A 65 THR A 68 0
SHEET 2 AA2 5 ILE A 71 GLY A 77 -1 O ALA A 73 N SER A 65
SHEET 3 AA2 5 VAL A 132 ASP A 140 -1 O ALA A 137 N GLY A 72
SHEET 4 AA2 5 GLY A 144 VAL A 150 -1 O TYR A 148 N ILE A 136
SHEET 5 AA2 5 TYR A 156 PRO A 158 -1 O PHE A 157 N GLN A 149
SHEET 1 AA3 6 TYR A 224 THR A 225 0
SHEET 2 AA3 6 ALA H 184 LEU H 191 1 O TYR H 186 N THR A 225
SHEET 3 AA3 6 VAL H 173 GLU H 179 -1 N VAL H 175 O LEU H 187
SHEET 4 AA3 6 GLY H 11 ALA H 16 -1 N VAL H 12 O MET H 178
SHEET 5 AA3 6 ILE H 3 PHE H 8 -1 N VAL H 6 O VAL H 13
SHEET 6 AA3 6 TYR H 124 LEU H 127 -1 O LEU H 125 N GLY H 5
SHEET 1 AA4 5 ALA B 161 VAL B 164 0
SHEET 2 AA4 5 ALA B 34 ALA B 39 -1 N GLY B 36 O ILE B 162
SHEET 3 AA4 5 GLY B 42 GLU B 48 -1 O ALA B 46 N ILE B 35
SHEET 4 AA4 5 LEU B 210 ARG B 216 -1 O ALA B 213 N LEU B 45
SHEET 5 AA4 5 TYR B 225 ILE B 228 -1 O TYR B 225 N ARG B 216
SHEET 1 AA5 5 LEU B 65 LYS B 67 0
SHEET 2 AA5 5 ILE B 72 GLY B 78 -1 O VAL B 74 N TYR B 66
SHEET 3 AA5 5 VAL B 132 ASP B 140 -1 O ALA B 137 N ALA B 73
SHEET 4 AA5 5 GLY B 144 SER B 150 -1 O TYR B 148 N TYR B 136
SHEET 5 AA5 5 TYR B 156 TRP B 159 -1 O TRP B 159 N LEU B 147
SHEET 1 AA6 5 ALA C 159 ILE C 162 0
SHEET 2 AA6 5 ALA C 31 LYS C 35 -1 N GLY C 33 O GLN C 160
SHEET 3 AA6 5 VAL C 40 GLU C 45 -1 O GLY C 43 N VAL C 32
SHEET 4 AA6 5 ILE C 208 LYS C 214 -1 O VAL C 213 N VAL C 40
SHEET 5 AA6 5 ASP C 218 ALA C 221 -1 O ASP C 218 N LYS C 214
SHEET 1 AA7 5 SER C 63 LYS C 64 0
SHEET 2 AA7 5 VAL C 69 GLY C 75 -1 O LEU C 71 N SER C 63
SHEET 3 AA7 5 VAL C 129 GLY C 135 -1 O ALA C 134 N VAL C 70
SHEET 4 AA7 5 LYS C 144 THR C 148 -1 O TYR C 146 N ILE C 133
SHEET 5 AA7 5 TYR C 154 SER C 156 -1 O SER C 155 N GLN C 147
SHEET 1 AA8 5 ALA D 161 ILE D 164 0
SHEET 2 AA8 5 ALA D 29 ALA D 33 -1 N GLY D 31 O LYS D 162
SHEET 3 AA8 5 VAL D 38 GLU D 43 -1 O GLY D 41 N ILE D 30
SHEET 4 AA8 5 ALA D 209 THR D 215 -1 O SER D 212 N LEU D 40
SHEET 5 AA8 5 GLY D 219 ILE D 222 -1 O LYS D 221 N CYS D 213
SHEET 1 AA9 5 ILE D 59 ASP D 63 0
SHEET 2 AA9 5 ILE D 66 GLY D 72 -1 O CYS D 68 N VAL D 60
SHEET 3 AA9 5 VAL D 132 ASP D 140 -1 O ALA D 137 N GLY D 67
SHEET 4 AA9 5 GLY D 144 ALA D 150 -1 O PHE D 148 N ILE D 136
SHEET 5 AA9 5 PHE D 156 ARG D 158 -1 O TYR D 157 N HIS D 149
SHEET 1 AB1 5 GLY E 157 ILE E 160 0
SHEET 2 AB1 5 THR E 34 ARG E 38 -1 N GLY E 36 O THR E 158
SHEET 3 AB1 5 HIS E 42 LEU E 48 -1 O VAL E 46 N VAL E 35
SHEET 4 AB1 5 LEU E 210 GLY E 216 -1 O SER E 211 N ALA E 47
SHEET 5 AB1 5 THR E 219 TYR E 224 -1 O TYR E 224 N ILE E 212
SHEET 1 AB2 5 ILE E 62 ASP E 66 0
SHEET 2 AB2 5 MET E 69 GLY E 75 -1 O LEU E 71 N ILE E 63
SHEET 3 AB2 5 VAL E 129 ASP E 137 -1 O ILE E 134 N GLY E 70
SHEET 4 AB2 5 GLY E 140 PHE E 146 -1 O PHE E 146 N LEU E 131
SHEET 5 AB2 5 VAL E 152 GLU E 154 -1 O THR E 153 N GLU E 145
SHEET 1 AB3 5 GLY F 158 THR F 161 0
SHEET 2 AB3 5 SER F 33 LYS F 37 -1 N GLY F 35 O ALA F 159
SHEET 3 AB3 5 GLY F 41 LEU F 49 -1 O ALA F 45 N ILE F 34
SHEET 4 AB3 5 PHE F 208 SER F 216 -1 O SER F 213 N PHE F 44
SHEET 5 AB3 5 HIS F 224 PHE F 226 -1 O LYS F 225 N TRP F 214
SHEET 1 AB4 5 GLN F 64 VAL F 66 0
SHEET 2 AB4 5 ILE F 70 GLY F 76 -1 O CYS F 72 N GLN F 64
SHEET 3 AB4 5 VAL F 130 ASP F 138 -1 O ILE F 133 N VAL F 73
SHEET 4 AB4 5 GLY F 141 LEU F 147 -1 O TYR F 145 N PHE F 134
SHEET 5 AB4 5 TYR F 153 GLY F 155 -1 O TRP F 154 N MET F 146
SHEET 1 AB5 5 ALA G 159 THR G 162 0
SHEET 2 AB5 5 SER G 33 ARG G 37 -1 N SER G 33 O THR G 162
SHEET 3 AB5 5 THR G 42 GLN G 47 -1 O ILE G 45 N LEU G 34
SHEET 4 AB5 5 LEU G 214 THR G 220 -1 O GLY G 217 N VAL G 44
SHEET 5 AB5 5 LYS G 223 THR G 226 -1 O PHE G 225 N VAL G 218
SHEET 1 AB6 5 ILE G 63 CYS G 65 0
SHEET 2 AB6 5 GLY G 71 ASN G 75 -1 O MET G 72 N PHE G 64
SHEET 3 AB6 5 ILE G 131 ASP G 138 -1 O VAL G 135 N GLY G 71
SHEET 4 AB6 5 GLY G 142 THR G 148 -1 O TYR G 146 N PHE G 134
SHEET 5 AB6 5 TYR G 154 TYR G 157 -1 O TYR G 157 N ILE G 145
SHEET 1 AB7 2 SER H 20 GLN H 22 0
SHEET 2 AB7 2 ILE H 25 ASP H 28 -1 O ALA H 27 N SER H 20
SHEET 1 AB8 5 LEU H 34 SER H 38 0
SHEET 2 AB8 5 ILE H 41 GLY H 47 -1 O CYS H 43 N HIS H 35
SHEET 3 AB8 5 ALA H 96 ASP H 104 -1 O TYR H 97 N ALA H 46
SHEET 4 AB8 5 GLY H 107 ILE H 113 -1 O ILE H 113 N LEU H 98
SHEET 5 AB8 5 THR H 119 VAL H 121 -1 O ASP H 120 N SER H 112
SHEET 1 AB9 6 VAL H 212 VAL H 218 0
SHEET 2 AB9 6 GLU I 193 LEU I 199 -1 O VAL I 194 N VAL H 218
SHEET 3 AB9 6 ALA I 184 LYS I 190 -1 N ILE I 188 O VAL I 195
SHEET 4 AB9 6 CYS I 19 ASP I 25 -1 N VAL I 20 O ILE I 189
SHEET 5 AB9 6 ILE I 10 GLY I 16 -1 N VAL I 12 O ALA I 23
SHEET 6 AB9 6 PHE I 135 GLY I 139 -1 O ILE I 136 N ALA I 13
SHEET 1 AC1 2 LEU I 28 SER I 30 0
SHEET 2 AC1 2 LEU I 33 SER I 36 -1 O LEU I 33 N SER I 30
SHEET 1 AC2 5 ILE I 42 TYR I 45 0
SHEET 2 AC2 5 VAL I 48 GLY I 54 -1 O LEU I 50 N PHE I 43
SHEET 3 AC2 5 VAL I 104 ILE I 111 -1 O VAL I 107 N GLY I 51
SHEET 4 AC2 5 PRO I 118 PHE I 123 -1 O ALA I 121 N VAL I 108
SHEET 5 AC2 5 ILE I 129 ASP I 130 -1 O ASP I 130 N GLY I 122
SHEET 1 AC3 5 TYR J 130 HIS J 133 0
SHEET 2 AC3 5 ILE J 4 ARG J 8 -1 N GLY J 6 O GLY J 131
SHEET 3 AC3 5 SER J 12 SER J 18 -1 O ALA J 16 N LEU J 5
SHEET 4 AC3 5 VAL J 179 ASP J 185 -1 O VAL J 184 N VAL J 13
SHEET 5 AC3 5 GLY J 188 VAL J 192 -1 O ARG J 190 N ILE J 183
SHEET 1 AC4 2 VAL J 21 ARG J 23 0
SHEET 2 AC4 2 SER J 26 LYS J 29 -1 O LYS J 29 N VAL J 21
SHEET 1 AC5 5 THR J 35 SER J 39 0
SHEET 2 AC5 5 THR J 42 GLY J 48 -1 O THR J 42 N SER J 39
SHEET 3 AC5 5 VAL J 100 ASP J 108 -1 O GLY J 105 N LEU J 43
SHEET 4 AC5 5 LYS J 113 ILE J 119 -1 O ILE J 119 N VAL J 102
SHEET 5 AC5 5 LYS J 125 LEU J 128 -1 O VAL J 126 N GLN J 118
SHEET 1 AC6 5 ILE K 126 VAL K 129 0
SHEET 2 AC6 5 THR K 3 PHE K 8 -1 N THR K 3 O VAL K 129
SHEET 3 AC6 5 GLY K 11 VAL K 16 -1 O ALA K 15 N LEU K 4
SHEET 4 AC6 5 SER K 174 THR K 181 -1 O VAL K 180 N ILE K 12
SHEET 5 AC6 5 GLY K 184 ASP K 192 -1 O HIS K 188 N LEU K 177
SHEET 1 AC7 2 ALA K 20 ALA K 22 0
SHEET 2 AC7 2 TRP K 25 SER K 28 -1 O TRP K 25 N ALA K 22
SHEET 1 AC8 5 VAL K 34 ASN K 38 0
SHEET 2 AC8 5 LEU K 41 THR K 44 -1 O GLY K 43 N ILE K 35
SHEET 3 AC8 5 GLY K 98 THR K 105 -1 O CYS K 102 N LEU K 42
SHEET 4 AC8 5 GLY K 109 ASP K 116 -1 O VAL K 115 N THR K 99
SHEET 5 AC8 5 ARG K 121 LYS K 123 -1 O LEU K 122 N TYR K 114
SHEET 1 AC9 5 CYS L 136 GLY L 140 0
SHEET 2 AC9 5 THR L 11 ALA L 16 -1 N GLY L 14 O ARG L 137
SHEET 3 AC9 5 ALA L 21 ASP L 26 -1 O ALA L 24 N LEU L 13
SHEET 4 AC9 5 GLY L 201 THR L 208 -1 O VAL L 207 N ALA L 21
SHEET 5 AC9 5 GLY L 211 GLU L 218 -1 O TYR L 217 N LEU L 202
SHEET 1 AD1 2 ASN L 29 THR L 31 0
SHEET 2 AD1 2 SER L 34 SER L 37 -1 O ASN L 36 N ASN L 29
SHEET 1 AD2 5 VAL L 43 GLY L 47 0
SHEET 2 AD2 5 ILE L 50 GLY L 56 -1 O MET L 52 N PHE L 44
SHEET 3 AD2 5 VAL L 107 LEU L 114 -1 O HIS L 108 N ASN L 55
SHEET 4 AD2 5 GLY L 120 PHE L 125 -1 O PHE L 125 N THR L 109
SHEET 5 AD2 5 TYR L 131 GLU L 134 -1 O GLU L 134 N VAL L 122
SHEET 1 AD3 5 LEU M 33 PHE M 36 0
SHEET 2 AD3 5 GLY M 28 TYR M 30 -1 N TYR M 30 O LEU M 33
SHEET 3 AD3 5 VAL M 6 GLY M 8 -1 N THR M 7 O SER M 29
SHEET 4 AD3 5 THR M 49 ASP M 56 -1 O GLY M 55 N GLY M 8
SHEET 5 AD3 5 LEU M 42 PRO M 44 -1 N ILE M 43 O VAL M 51
SHEET 1 AD4 7 LEU M 33 PHE M 36 0
SHEET 2 AD4 7 GLY M 28 TYR M 30 -1 N TYR M 30 O LEU M 33
SHEET 3 AD4 7 VAL M 6 GLY M 8 -1 N THR M 7 O SER M 29
SHEET 4 AD4 7 THR M 49 ASP M 56 -1 O GLY M 55 N GLY M 8
SHEET 5 AD4 7 ASN M 112 VAL M 119 -1 O ALA M 117 N VAL M 50
SHEET 6 AD4 7 GLN M 125 ASN M 131 -1 O VAL M 130 N ILE M 114
SHEET 7 AD4 7 THR M 136 TYR M 137 -1 O TYR M 137 N TYR M 129
SHEET 1 AD5 5 THR M 141 ALA M 143 0
SHEET 2 AD5 5 VAL M 11 TYR M 16 -1 N SER M 13 O LEU M 142
SHEET 3 AD5 5 GLY M 19 ASP M 25 -1 O GLY M 19 N TYR M 16
SHEET 4 AD5 5 ASN M 194 ASP M 201 -1 O ALA M 198 N ILE M 22
SHEET 5 AD5 5 GLY M 205 GLN M 213 -1 O LYS M 209 N LEU M 197
SHEET 1 AD6 5 TYR N 124 ALA N 127 0
SHEET 2 AD6 5 ILE N 3 PHE N 8 -1 N ALA N 5 O ALA N 125
SHEET 3 AD6 5 GLY N 11 ALA N 16 -1 O GLY N 15 N MET N 4
SHEET 4 AD6 5 ILE N 173 THR N 179 -1 O LEU N 178 N VAL N 12
SHEET 5 AD6 5 VAL N 183 PHE N 188 -1 O GLU N 184 N VAL N 177
SHEET 1 AD7 2 THR N 20 THR N 22 0
SHEET 2 AD7 2 TYR N 25 ASN N 28 -1 O TYR N 25 N THR N 22
SHEET 1 AD8 5 LEU N 34 HIS N 38 0
SHEET 2 AD8 5 ILE N 41 GLY N 47 -1 O CYS N 43 N THR N 35
SHEET 3 AD8 5 ALA N 95 TYR N 102 -1 O GLY N 96 N SER N 46
SHEET 4 AD8 5 GLY N 108 ILE N 113 -1 O TYR N 111 N VAL N 99
SHEET 5 AD8 5 HIS N 120 LEU N 122 -1 O HIS N 120 N THR N 112
SHEET 1 AD9 5 ALA O 161 ILE O 164 0
SHEET 2 AD9 5 SER O 34 LYS O 38 -1 N SER O 34 O ILE O 164
SHEET 3 AD9 5 VAL O 43 GLU O 48 -1 O VAL O 44 N ILE O 37
SHEET 4 AD9 5 ILE O 209 ILE O 214 -1 O ILE O 214 N VAL O 43
SHEET 5 AD9 5 PHE O 235 LYS O 237 -1 O ARG O 236 N ILE O 213
SHEET 1 AE1 6 ALA O 56 MET O 57 0
SHEET 2 AE1 6 TYR U 154 TYR U 157 -1 O GLY U 156 N MET O 57
SHEET 3 AE1 6 GLY U 142 THR U 148 -1 N ILE U 145 O TYR U 157
SHEET 4 AE1 6 ILE U 131 ASP U 138 -1 N PHE U 134 O TYR U 146
SHEET 5 AE1 6 GLY U 71 ASN U 75 -1 N GLY U 71 O VAL U 135
SHEET 6 AE1 6 ILE U 63 CYS U 65 -1 N PHE U 64 O MET U 72
SHEET 1 AE2 5 SER O 65 THR O 68 0
SHEET 2 AE2 5 ILE O 71 GLY O 77 -1 O ALA O 73 N SER O 65
SHEET 3 AE2 5 VAL O 132 ASP O 140 -1 O ALA O 137 N GLY O 72
SHEET 4 AE2 5 GLY O 144 VAL O 150 -1 O TYR O 148 N ILE O 136
SHEET 5 AE2 5 TYR O 156 PRO O 158 -1 O PHE O 157 N GLN O 149
SHEET 1 AE3 6 TYR O 224 THR O 225 0
SHEET 2 AE3 6 ALA V 184 LEU V 191 1 O TYR V 186 N THR O 225
SHEET 3 AE3 6 VAL V 173 GLU V 179 -1 N VAL V 175 O LEU V 187
SHEET 4 AE3 6 GLY V 11 ALA V 16 -1 N VAL V 12 O MET V 178
SHEET 5 AE3 6 ILE V 3 PHE V 8 -1 N VAL V 6 O VAL V 13
SHEET 6 AE3 6 TYR V 124 LEU V 127 -1 O LEU V 125 N GLY V 5
SHEET 1 AE4 5 ALA P 161 VAL P 164 0
SHEET 2 AE4 5 ALA P 34 ALA P 39 -1 N GLY P 36 O ILE P 162
SHEET 3 AE4 5 GLY P 42 GLU P 48 -1 O ALA P 46 N ILE P 35
SHEET 4 AE4 5 LEU P 210 ARG P 216 -1 O ALA P 213 N LEU P 45
SHEET 5 AE4 5 TYR P 225 ILE P 228 -1 O TYR P 225 N ARG P 216
SHEET 1 AE5 5 LEU P 65 LYS P 67 0
SHEET 2 AE5 5 ILE P 72 GLY P 78 -1 O VAL P 74 N TYR P 66
SHEET 3 AE5 5 VAL P 132 ASP P 140 -1 O ALA P 137 N ALA P 73
SHEET 4 AE5 5 GLY P 144 SER P 150 -1 O TYR P 148 N TYR P 136
SHEET 5 AE5 5 TYR P 156 TRP P 159 -1 O TRP P 159 N LEU P 147
SHEET 1 AE6 5 ALA Q 159 ILE Q 162 0
SHEET 2 AE6 5 ALA Q 31 LYS Q 35 -1 N GLY Q 33 O GLN Q 160
SHEET 3 AE6 5 VAL Q 40 GLU Q 45 -1 O GLY Q 43 N VAL Q 32
SHEET 4 AE6 5 ILE Q 208 LYS Q 214 -1 O VAL Q 213 N VAL Q 40
SHEET 5 AE6 5 ASP Q 218 ALA Q 221 -1 O ASP Q 218 N LYS Q 214
SHEET 1 AE7 5 SER Q 63 LYS Q 64 0
SHEET 2 AE7 5 VAL Q 69 GLY Q 75 -1 O LEU Q 71 N SER Q 63
SHEET 3 AE7 5 VAL Q 129 GLY Q 135 -1 O ALA Q 134 N VAL Q 70
SHEET 4 AE7 5 LYS Q 144 THR Q 148 -1 O TYR Q 146 N ILE Q 133
SHEET 5 AE7 5 TYR Q 154 SER Q 156 -1 O SER Q 155 N GLN Q 147
SHEET 1 AE8 5 ALA R 161 ILE R 164 0
SHEET 2 AE8 5 ALA R 29 ALA R 33 -1 N GLY R 31 O LYS R 162
SHEET 3 AE8 5 VAL R 38 GLU R 43 -1 O GLY R 41 N ILE R 30
SHEET 4 AE8 5 ALA R 209 THR R 215 -1 O SER R 212 N LEU R 40
SHEET 5 AE8 5 GLY R 219 ILE R 222 -1 O LYS R 221 N CYS R 213
SHEET 1 AE9 5 ILE R 59 ASP R 63 0
SHEET 2 AE9 5 ILE R 66 GLY R 72 -1 O CYS R 68 N VAL R 60
SHEET 3 AE9 5 VAL R 132 ASP R 140 -1 O ALA R 137 N GLY R 67
SHEET 4 AE9 5 GLY R 144 ALA R 150 -1 O PHE R 148 N ILE R 136
SHEET 5 AE9 5 PHE R 156 ARG R 158 -1 O TYR R 157 N HIS R 149
SHEET 1 AF1 5 GLY S 157 ILE S 160 0
SHEET 2 AF1 5 THR S 34 ARG S 38 -1 N GLY S 36 O THR S 158
SHEET 3 AF1 5 HIS S 42 LEU S 48 -1 O VAL S 46 N VAL S 35
SHEET 4 AF1 5 LEU S 210 GLY S 216 -1 O SER S 211 N ALA S 47
SHEET 5 AF1 5 THR S 219 TYR S 224 -1 O TYR S 224 N ILE S 212
SHEET 1 AF2 5 ILE S 62 ASP S 66 0
SHEET 2 AF2 5 MET S 69 GLY S 75 -1 O LEU S 71 N ILE S 63
SHEET 3 AF2 5 VAL S 129 ASP S 137 -1 O ILE S 134 N GLY S 70
SHEET 4 AF2 5 GLY S 140 PHE S 146 -1 O PHE S 146 N LEU S 131
SHEET 5 AF2 5 VAL S 152 GLU S 154 -1 O THR S 153 N GLU S 145
SHEET 1 AF3 5 GLY T 158 THR T 161 0
SHEET 2 AF3 5 SER T 33 LYS T 37 -1 N GLY T 35 O ALA T 159
SHEET 3 AF3 5 GLY T 41 LEU T 49 -1 O ALA T 45 N ILE T 34
SHEET 4 AF3 5 PHE T 208 SER T 216 -1 O SER T 213 N PHE T 44
SHEET 5 AF3 5 HIS T 224 PHE T 226 -1 O LYS T 225 N TRP T 214
SHEET 1 AF4 5 GLN T 64 VAL T 66 0
SHEET 2 AF4 5 ILE T 70 GLY T 76 -1 O CYS T 72 N GLN T 64
SHEET 3 AF4 5 VAL T 130 ASP T 138 -1 O ILE T 133 N VAL T 73
SHEET 4 AF4 5 GLY T 141 LEU T 147 -1 O TYR T 145 N PHE T 134
SHEET 5 AF4 5 TYR T 153 GLY T 155 -1 O TRP T 154 N MET T 146
SHEET 1 AF5 5 ALA U 159 THR U 162 0
SHEET 2 AF5 5 SER U 33 ARG U 37 -1 N SER U 33 O THR U 162
SHEET 3 AF5 5 THR U 42 GLN U 47 -1 O ILE U 45 N LEU U 34
SHEET 4 AF5 5 LEU U 214 THR U 220 -1 O GLY U 217 N VAL U 44
SHEET 5 AF5 5 LYS U 223 THR U 226 -1 O PHE U 225 N VAL U 218
SHEET 1 AF6 2 SER V 20 GLN V 22 0
SHEET 2 AF6 2 ILE V 25 ASP V 28 -1 O ALA V 27 N SER V 20
SHEET 1 AF7 5 LEU V 34 SER V 38 0
SHEET 2 AF7 5 ILE V 41 GLY V 47 -1 O ILE V 41 N ILE V 37
SHEET 3 AF7 5 ALA V 96 ASP V 104 -1 O TYR V 97 N ALA V 46
SHEET 4 AF7 5 GLY V 107 ILE V 113 -1 O ILE V 113 N LEU V 98
SHEET 5 AF7 5 THR V 119 VAL V 121 -1 O ASP V 120 N SER V 112
SHEET 1 AF8 6 VAL V 212 ILE V 217 0
SHEET 2 AF8 6 GLU W 193 LEU W 199 -1 O TYR W 198 N LEU V 213
SHEET 3 AF8 6 ALA W 184 LYS W 190 -1 N ILE W 188 O VAL W 195
SHEET 4 AF8 6 CYS W 19 ASP W 25 -1 N ILE W 22 O TYR W 187
SHEET 5 AF8 6 ILE W 10 GLY W 16 -1 N VAL W 12 O ALA W 23
SHEET 6 AF8 6 PHE W 135 GLY W 139 -1 O ILE W 136 N ALA W 13
SHEET 1 AF9 2 LEU W 28 SER W 30 0
SHEET 2 AF9 2 LEU W 33 SER W 36 -1 O LEU W 33 N SER W 30
SHEET 1 AG1 5 ILE W 42 TYR W 45 0
SHEET 2 AG1 5 VAL W 48 GLY W 54 -1 O LEU W 50 N PHE W 43
SHEET 3 AG1 5 VAL W 104 ILE W 111 -1 O VAL W 107 N GLY W 51
SHEET 4 AG1 5 PRO W 118 PHE W 123 -1 O ALA W 121 N VAL W 108
SHEET 5 AG1 5 ILE W 129 ASP W 130 -1 O ASP W 130 N GLY W 122
SHEET 1 AG2 5 TYR X 130 HIS X 133 0
SHEET 2 AG2 5 ILE X 4 ARG X 8 -1 N GLY X 6 O GLY X 131
SHEET 3 AG2 5 SER X 12 SER X 18 -1 O ALA X 16 N LEU X 5
SHEET 4 AG2 5 VAL X 179 ASP X 185 -1 O VAL X 184 N VAL X 13
SHEET 5 AG2 5 GLY X 188 VAL X 192 -1 O ARG X 190 N ILE X 183
SHEET 1 AG3 2 VAL X 21 ARG X 23 0
SHEET 2 AG3 2 SER X 26 LYS X 29 -1 O LYS X 29 N VAL X 21
SHEET 1 AG4 5 THR X 35 SER X 39 0
SHEET 2 AG4 5 THR X 42 GLY X 48 -1 O THR X 42 N SER X 39
SHEET 3 AG4 5 VAL X 100 ASP X 108 -1 O GLY X 105 N LEU X 43
SHEET 4 AG4 5 LYS X 113 ILE X 119 -1 O ILE X 119 N VAL X 102
SHEET 5 AG4 5 LYS X 125 LEU X 128 -1 O VAL X 126 N GLN X 118
SHEET 1 AG5 5 ILE Y 126 VAL Y 129 0
SHEET 2 AG5 5 THR Y 3 PHE Y 8 -1 N THR Y 3 O VAL Y 129
SHEET 3 AG5 5 GLY Y 11 VAL Y 16 -1 O ALA Y 15 N LEU Y 4
SHEET 4 AG5 5 SER Y 174 THR Y 181 -1 O VAL Y 180 N ILE Y 12
SHEET 5 AG5 5 GLY Y 184 ASP Y 192 -1 O HIS Y 188 N LEU Y 177
SHEET 1 AG6 2 ALA Y 20 ALA Y 22 0
SHEET 2 AG6 2 TRP Y 25 SER Y 28 -1 O TRP Y 25 N ALA Y 22
SHEET 1 AG7 5 VAL Y 34 ASN Y 38 0
SHEET 2 AG7 5 LEU Y 41 THR Y 44 -1 O GLY Y 43 N ILE Y 35
SHEET 3 AG7 5 GLY Y 98 THR Y 105 -1 O CYS Y 102 N LEU Y 42
SHEET 4 AG7 5 GLY Y 109 ASP Y 116 -1 O VAL Y 115 N THR Y 99
SHEET 5 AG7 5 ARG Y 121 LYS Y 123 -1 O LEU Y 122 N TYR Y 114
SHEET 1 AG8 5 CYS Z 136 GLY Z 140 0
SHEET 2 AG8 5 THR Z 11 ALA Z 16 -1 N ILE Z 12 O GLY Z 139
SHEET 3 AG8 5 ALA Z 21 ASP Z 26 -1 O ALA Z 24 N LEU Z 13
SHEET 4 AG8 5 GLY Z 201 THR Z 208 -1 O VAL Z 207 N ALA Z 21
SHEET 5 AG8 5 GLY Z 211 GLU Z 218 -1 O TYR Z 217 N LEU Z 202
SHEET 1 AG9 2 ASN Z 29 THR Z 31 0
SHEET 2 AG9 2 SER Z 34 SER Z 37 -1 O ASN Z 36 N ASN Z 29
SHEET 1 AH1 5 VAL Z 43 GLY Z 47 0
SHEET 2 AH1 5 ILE Z 50 GLY Z 56 -1 O MET Z 52 N PHE Z 44
SHEET 3 AH1 5 VAL Z 107 LEU Z 114 -1 O HIS Z 108 N ASN Z 55
SHEET 4 AH1 5 GLY Z 120 PHE Z 125 -1 O PHE Z 125 N THR Z 109
SHEET 5 AH1 5 TYR Z 131 GLU Z 134 -1 O GLU Z 134 N VAL Z 122
SHEET 1 AH2 5 LEU a 33 PHE a 36 0
SHEET 2 AH2 5 GLY a 28 TYR a 30 -1 N TYR a 30 O LEU a 33
SHEET 3 AH2 5 VAL a 6 GLY a 8 -1 N THR a 7 O SER a 29
SHEET 4 AH2 5 THR a 49 ASP a 56 -1 O GLY a 55 N GLY a 8
SHEET 5 AH2 5 LEU a 42 PRO a 44 -1 N ILE a 43 O VAL a 51
SHEET 1 AH3 7 LEU a 33 PHE a 36 0
SHEET 2 AH3 7 GLY a 28 TYR a 30 -1 N TYR a 30 O LEU a 33
SHEET 3 AH3 7 VAL a 6 GLY a 8 -1 N THR a 7 O SER a 29
SHEET 4 AH3 7 THR a 49 ASP a 56 -1 O GLY a 55 N GLY a 8
SHEET 5 AH3 7 ASN a 112 VAL a 119 -1 O ALA a 117 N VAL a 50
SHEET 6 AH3 7 GLN a 125 ASN a 131 -1 O VAL a 130 N ILE a 114
SHEET 7 AH3 7 THR a 136 TYR a 137 -1 O TYR a 137 N TYR a 129
SHEET 1 AH4 5 THR a 141 ALA a 143 0
SHEET 2 AH4 5 VAL a 11 TYR a 16 -1 N SER a 13 O LEU a 142
SHEET 3 AH4 5 GLY a 19 ASP a 25 -1 O GLY a 19 N TYR a 16
SHEET 4 AH4 5 ASN a 194 ASP a 201 -1 O ALA a 198 N ILE a 22
SHEET 5 AH4 5 GLY a 205 GLN a 213 -1 O LYS a 209 N LEU a 197
SHEET 1 AH5 5 TYR b 124 ALA b 127 0
SHEET 2 AH5 5 ILE b 3 PHE b 8 -1 N ILE b 3 O ALA b 127
SHEET 3 AH5 5 GLY b 11 ALA b 16 -1 O GLY b 15 N MET b 4
SHEET 4 AH5 5 ILE b 173 THR b 179 -1 O LEU b 178 N VAL b 12
SHEET 5 AH5 5 VAL b 183 PHE b 188 -1 O GLU b 184 N VAL b 177
SHEET 1 AH6 2 THR b 20 THR b 22 0
SHEET 2 AH6 2 TYR b 25 ASN b 28 -1 O TYR b 25 N THR b 22
SHEET 1 AH7 5 LEU b 34 HIS b 38 0
SHEET 2 AH7 5 ILE b 41 GLY b 47 -1 O CYS b 43 N THR b 35
SHEET 3 AH7 5 ALA b 95 TYR b 102 -1 O GLY b 96 N SER b 46
SHEET 4 AH7 5 GLY b 108 ILE b 113 -1 O TYR b 111 N VAL b 99
SHEET 5 AH7 5 HIS b 120 LEU b 122 -1 O HIS b 120 N THR b 112
LINK OG1 THR H 1 B26 BO2 H 301 1555 1555 1.41
LINK OG1 THR K 1 B26 BO2 K 301 1555 1555 1.43
LINK OG1 THR N 1 B26 BO2 N 201 1555 1555 1.44
LINK OG1 THR V 1 B26 BO2 V 301 1555 1555 1.42
LINK OG1 THR Y 1 B26 BO2 Y 301 1555 1555 1.44
LINK OG1 THR b 1 B26 BO2 b 201 1555 1555 1.44
LINK OG1 THR G 8 MG MG G 301 1555 1555 2.60
LINK O TYR G 119 MG MG G 301 1555 1555 2.98
LINK O ARG G 122 MG MG G 301 1555 1555 2.63
LINK O MET G 125 MG MG G 301 1555 1555 2.26
LINK O ILE H 163 MG MG H 302 1555 1555 2.07
LINK O ASP H 166 MG MG H 302 1555 1555 2.10
LINK O SER H 169 MG MG H 302 1555 1555 2.17
LINK O ALA I 174 MG MG I 301 1555 1555 2.87
LINK O ASP I 177 MG MG I 301 1555 1555 2.27
LINK O SER I 180 MG MG I 301 1555 1555 2.67
LINK O ASP I 204 MG MG I 302 1555 1555 2.20
LINK MG MG I 302 O ALA Y 165 1555 1555 2.42
LINK MG MG I 302 O ASP Y 168 1555 1555 2.23
LINK MG MG I 302 O SER Y 171 1555 1555 2.70
LINK O ALA K 165 MG MG K 302 1555 1555 2.27
LINK O ASP K 168 MG MG K 302 1555 1555 2.06
LINK MG MG K 302 O ASP W 204 1555 1555 2.40
LINK OXT ASP L 222 MG MG L 301 1555 1555 2.04
LINK MG MG L 301 O ILE V 163 1555 1555 2.11
LINK MG MG L 301 O ASP V 166 1555 1555 1.94
LINK MG MG L 301 O SER V 169 1555 1555 2.18
LINK O ILE N 163 MG MG N 202 1555 1555 2.57
LINK O ASP N 166 MG MG N 202 1555 1555 2.78
LINK O SER N 169 MG MG N 202 1555 1555 2.56
LINK O VAL Z 198 MG MG Z 301 1555 1555 2.81
SITE 1 AC1 5 THR G 8 TYR G 119 ARG G 122 ALA G 123
SITE 2 AC1 5 MET G 125
SITE 1 AC2 3 ARG G 111 ASN G 114 TYR H 69
SITE 1 AC3 6 THR H 1 SER H 20 THR H 21 ALA H 46
SITE 2 AC3 6 GLY H 47 ALA H 49
SITE 1 AC4 3 ALA I 174 ASP I 177 SER I 180
SITE 1 AC5 1 GLN J 118
SITE 1 AC6 6 THR K 1 ALA K 20 THR K 21 GLY K 47
SITE 2 AC6 6 ALA K 49 ASP L 126
SITE 1 AC7 6 ALA K 165 HIS K 166 ASP K 168 ALA K 169
SITE 2 AC7 6 SER K 171 ASP W 204
SITE 1 AC8 8 SER H 118 THR N 1 THR N 20 THR N 21
SITE 2 AC8 8 THR N 22 ARG N 45 GLY N 47 ALA N 49
SITE 1 AC9 5 ARG N 19 ILE N 163 ASP N 166 SER N 169
SITE 2 AC9 5 LEU a 34
SITE 1 AD1 3 THR N 31 ARG N 45 GLN N 53
SITE 1 AD2 3 ARG U 111 ASN U 114 TYR V 69
SITE 1 AD3 5 ASP L 222 GLY V 162 ILE V 163 ASP V 166
SITE 2 AD3 5 SER V 169
SITE 1 AD4 5 ASP I 204 ALA Y 165 ASP Y 168 ALA Y 169
SITE 2 AD4 5 SER Y 171
SITE 1 AD5 6 ARG Z 28 THR Z 192 HIS Z 195 ILE Z 196
SITE 2 AD5 6 VAL Z 198 ASP Z 222
SITE 1 AD6 4 ILE H 163 ASP H 166 SER H 169 ASP Z 222
SITE 1 AD7 2 ARG b 45 GLN b 53
SITE 1 AD8 14 THR V 2 ASP V 17 SER V 20 THR V 21
SITE 2 AD8 14 GLN V 22 LYS V 33 ALA V 46 GLY V 47
SITE 3 AD8 14 ALA V 49 GLY V 128 SER V 129 GLY V 130
SITE 4 AD8 14 GLY V 168 SER V 169
SITE 1 AD9 14 THR Y 2 ASP Y 17 ALA Y 20 THR Y 21
SITE 2 AD9 14 LYS Y 33 ALA Y 46 GLY Y 47 ALA Y 49
SITE 3 AD9 14 GLY Y 130 SER Y 131 GLY Y 132 TYR Y 170
SITE 4 AD9 14 SER Y 171 ASP Z 126
SITE 1 AE1 17 SER V 118 SER b 2 ASP b 17 THR b 20
SITE 2 AE1 17 THR b 21 THR b 22 LYS b 33 ARG b 45
SITE 3 AE1 17 GLY b 47 ALA b 49 GLY b 128 SER b 129
SITE 4 AE1 17 GLY b 130 ASP b 166 SER b 168 SER b 169
SITE 5 AE1 17 HOH b 301
CRYST1 134.220 300.860 144.100 90.00 112.32 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 0.007450 0.000000 0.003058 0.00000
SCALE2 0.000000 0.003324 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007501 0.00000
MTRIX1 1 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 1 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 1 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 2 -0.999097 -0.007701 0.041780 66.01672 1
MTRIX2 2 0.000303 -0.984701 -0.174251 -289.43356 1
MTRIX3 2 0.042482 -0.174081 0.983814 -25.92445 1
(ATOM LINES ARE NOT SHOWN.)
END
