HEADER HYDROLASE 11-OCT-18 6HWC
TITLE YEAST 20S PROTEASOME BETA2-G45A MUTANT
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 MUTATION: YES;
COMPND 51 MOL_ID: 9;
COMPND 52 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-3;
COMPND 53 CHAIN: I, W;
COMPND 54 SYNONYM: MACROPAIN SUBUNIT PUP3,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 55 SUBUNIT PUP3,PROTEASOME COMPONENT PUP3;
COMPND 56 EC: 3.4.25.1;
COMPND 57 MOL_ID: 10;
COMPND 58 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-4;
COMPND 59 CHAIN: J, X;
COMPND 60 SYNONYM: MACROPAIN SUBUNIT C11,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 61 SUBUNIT C11,PROTEASOME COMPONENT C11,PROTEINASE YSCE SUBUNIT 11;
COMPND 62 EC: 3.4.25.1;
COMPND 63 MOL_ID: 11;
COMPND 64 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-5;
COMPND 65 CHAIN: K, Y;
COMPND 66 MOL_ID: 12;
COMPND 67 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-6;
COMPND 68 CHAIN: L, Z;
COMPND 69 SYNONYM: MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C5,PROTEASOME
COMPND 70 COMPONENT C5;
COMPND 71 EC: 3.4.25.1;
COMPND 72 MOL_ID: 13;
COMPND 73 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-7;
COMPND 74 CHAIN: M, a;
COMPND 75 SYNONYM: MACROPAIN SUBUNIT PRE4,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 76 SUBUNIT PRE4,PROTEASOME COMPONENT PRE4,PROTEINASE YSCE SUBUNIT PRE4;
COMPND 77 EC: 3.4.25.1;
COMPND 78 MOL_ID: 14;
COMPND 79 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-1;
COMPND 80 CHAIN: N, b;
COMPND 81 SYNONYM: MACROPAIN SUBUNIT PRE3,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 82 SUBUNIT PRE3,PROTEASOME COMPONENT PRE3,PROTEINASE YSCE SUBUNIT PRE3;
COMPND 83 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 STRAIN: ATCC 204508 / S288C;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 9 S288C);
SOURCE 10 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 11 ORGANISM_TAXID: 559292;
SOURCE 12 STRAIN: ATCC 204508 / S288C;
SOURCE 13 MOL_ID: 3;
SOURCE 14 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 15 S288C);
SOURCE 16 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 17 ORGANISM_TAXID: 559292;
SOURCE 18 STRAIN: ATCC 204508 / S288C;
SOURCE 19 MOL_ID: 4;
SOURCE 20 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 21 S288C);
SOURCE 22 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 23 ORGANISM_TAXID: 559292;
SOURCE 24 STRAIN: ATCC 204508 / S288C;
SOURCE 25 MOL_ID: 5;
SOURCE 26 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 27 S288C);
SOURCE 28 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 29 ORGANISM_TAXID: 559292;
SOURCE 30 STRAIN: ATCC 204508 / S288C;
SOURCE 31 MOL_ID: 6;
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 STRAIN: ATCC 204508 / S288C;
SOURCE 37 MOL_ID: 7;
SOURCE 38 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 39 S288C);
SOURCE 40 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 41 ORGANISM_TAXID: 559292;
SOURCE 42 STRAIN: ATCC 204508 / S288C;
SOURCE 43 MOL_ID: 8;
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 STRAIN: ATCC 204508 / S288C;
SOURCE 49 MOL_ID: 9;
SOURCE 50 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 51 S288C);
SOURCE 52 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 53 ORGANISM_TAXID: 559292;
SOURCE 54 STRAIN: ATCC 204508 / S288C;
SOURCE 55 MOL_ID: 10;
SOURCE 56 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 57 S288C);
SOURCE 58 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 59 ORGANISM_TAXID: 559292;
SOURCE 60 STRAIN: ATCC 204508 / S288C;
SOURCE 61 MOL_ID: 11;
SOURCE 62 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 63 S288C);
SOURCE 64 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 65 ORGANISM_TAXID: 559292;
SOURCE 66 STRAIN: ATCC 204508 / S288C;
SOURCE 67 MOL_ID: 12;
SOURCE 68 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 69 S288C);
SOURCE 70 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 71 ORGANISM_TAXID: 559292;
SOURCE 72 STRAIN: ATCC 204508 / S288C;
SOURCE 73 MOL_ID: 13;
SOURCE 74 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 75 S288C);
SOURCE 76 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 77 ORGANISM_TAXID: 559292;
SOURCE 78 STRAIN: ATCC 204508 / S288C;
SOURCE 79 MOL_ID: 14;
SOURCE 80 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 81 S288C);
SOURCE 82 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 83 ORGANISM_TAXID: 559292;
SOURCE 84 STRAIN: ATCC 204508 / S288C
KEYWDS PROTEASOME, MUTANT, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.M.HUBER,M.GROLL
REVDAT 3 24-JAN-24 6HWC 1 LINK
REVDAT 2 24-APR-19 6HWC 1 JRNL
REVDAT 1 30-JAN-19 6HWC 0
JRNL AUTH B.T.XIN,E.M.HUBER,G.DE BRUIN,W.HEINEMEYER,E.MAURITS,
JRNL AUTH 2 C.ESPINAL,Y.DU,M.JANSSENS,E.S.WEYBURNE,A.F.KISSELEV,
JRNL AUTH 3 B.I.FLOREA,C.DRIESSEN,G.A.VAN DER MAREL,M.GROLL,
JRNL AUTH 4 H.S.OVERKLEEFT
JRNL TITL STRUCTURE-BASED DESIGN OF INHIBITORS SELECTIVE FOR HUMAN
JRNL TITL 2 PROTEASOME BETA 2C OR BETA 2I SUBUNITS.
JRNL REF J.MED.CHEM. V. 62 1626 2019
JRNL REFN ISSN 0022-2623
JRNL PMID 30657666
JRNL DOI 10.1021/ACS.JMEDCHEM.8B01884
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
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 (%) : 95.5
REMARK 3 NUMBER OF REFLECTIONS : 236637
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) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 12455
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) : 17482
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.55
REMARK 3 BIN R VALUE (WORKING SET) : 0.3130
REMARK 3 BIN FREE R VALUE SET COUNT : 920
REMARK 3 BIN FREE R VALUE : 0.3270
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 49368
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 27
REMARK 3 SOLVENT ATOMS : 722
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 63.24
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.17000
REMARK 3 B22 (A**2) : -6.12000
REMARK 3 B33 (A**2) : 0.66000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.06000
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): 0.298
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.265
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 32.606
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.947
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 50292 ; 0.007 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 46877 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 68036 ; 1.143 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES):108785 ; 0.891 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 6314 ; 5.741 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 2252 ;35.056 ;24.423
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 8758 ;14.536 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 284 ;13.945 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 7667 ; 0.065 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 56160 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 10076 ; 0.002 ; 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): 25346 ; 2.043 ; 4.392
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 25345 ; 2.043 ; 4.392
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 31630 ; 2.764 ; 6.578
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 31631 ; 2.763 ; 6.578
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 24946 ; 1.989 ; 4.651
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 24942 ; 1.989 ; 4.651
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 36401 ; 2.458 ; 6.882
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 52987 ; 3.331 ;50.482
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 52916 ; 3.272 ;50.464
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 97169 ; 0.955 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 505 ;34.274 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 96499 ; 5.772 ; 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 THERMAL 1 A (A**2): 3765 ; 4.60 ; 0.50
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): 3714 ; 3.13 ; 0.50
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): 3685 ; 5.97 ; 0.50
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): 3538 ; 2.91 ; 0.50
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): 3459 ; 3.69 ; 0.50
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): 3693 ; 3.67 ; 0.50
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): 3724 ; 3.06 ; 0.50
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): 3354 ; 2.87 ; 0.50
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): 3091 ; 2.50 ; 0.50
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 POSITIONAL 10 A (A): 3063 ; 0.01 ; 0.05
REMARK 3 TIGHT THERMAL 10 J (A**2): 3063 ; 2.21 ; 0.50
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 POSITIONAL 11 A (A): 3163 ; 0.01 ; 0.05
REMARK 3 TIGHT THERMAL 11 K (A**2): 3163 ; 1.98 ; 0.50
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 POSITIONAL 12 A (A): 3389 ; 0.01 ; 0.05
REMARK 3 TIGHT THERMAL 12 L (A**2): 3389 ; 2.02 ; 0.50
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 POSITIONAL 13 A (A): 3564 ; 0.01 ; 0.05
REMARK 3 TIGHT THERMAL 13 M (A**2): 3564 ; 2.23 ; 0.50
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 POSITIONAL 14 A (A): 2919 ; 0.01 ; 0.05
REMARK 3 TIGHT THERMAL 14 N (A**2): 2919 ; 2.20 ; 0.50
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): 66.6540 -91.9389 45.8611
REMARK 3 T TENSOR
REMARK 3 T11: 0.2285 T22: 0.1132
REMARK 3 T33: 0.2299 T12: -0.0474
REMARK 3 T13: -0.0230 T23: -0.0614
REMARK 3 L TENSOR
REMARK 3 L11: 0.2736 L22: 0.4517
REMARK 3 L33: 0.1350 L12: -0.3381
REMARK 3 L13: 0.1159 L23: -0.1455
REMARK 3 S TENSOR
REMARK 3 S11: -0.0300 S12: 0.0160 S13: 0.0313
REMARK 3 S21: 0.0465 S22: 0.0216 S23: -0.1235
REMARK 3 S31: -0.1280 S32: -0.0119 S33: 0.0083
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): 59.3052 -87.7130 16.2316
REMARK 3 T TENSOR
REMARK 3 T11: 0.2687 T22: 0.1234
REMARK 3 T33: 0.1630 T12: -0.0429
REMARK 3 T13: 0.0787 T23: 0.0499
REMARK 3 L TENSOR
REMARK 3 L11: 0.5435 L22: 0.5982
REMARK 3 L33: 0.5758 L12: 0.2695
REMARK 3 L13: 0.1209 L23: 0.0996
REMARK 3 S TENSOR
REMARK 3 S11: -0.0804 S12: 0.0089 S13: -0.0147
REMARK 3 S21: -0.1016 S22: 0.0158 S23: -0.1270
REMARK 3 S31: -0.1214 S32: 0.1114 S33: 0.0646
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): 32.0006 -87.3833 0.9692
REMARK 3 T TENSOR
REMARK 3 T11: 0.3085 T22: 0.0954
REMARK 3 T33: 0.1760 T12: -0.0115
REMARK 3 T13: -0.0274 T23: 0.0624
REMARK 3 L TENSOR
REMARK 3 L11: 0.4702 L22: 0.6510
REMARK 3 L33: 0.8952 L12: 0.2065
REMARK 3 L13: 0.1148 L23: -0.0317
REMARK 3 S TENSOR
REMARK 3 S11: -0.0125 S12: 0.0834 S13: 0.1219
REMARK 3 S21: -0.1315 S22: 0.0960 S23: -0.0510
REMARK 3 S31: -0.1245 S32: 0.1139 S33: -0.0834
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): 2.8348 -90.2231 13.5387
REMARK 3 T TENSOR
REMARK 3 T11: 0.2299 T22: 0.0981
REMARK 3 T33: 0.3370 T12: 0.0598
REMARK 3 T13: -0.1510 T23: 0.0702
REMARK 3 L TENSOR
REMARK 3 L11: 0.3421 L22: 0.5893
REMARK 3 L33: 0.3291 L12: 0.1728
REMARK 3 L13: -0.3296 L23: -0.1732
REMARK 3 S TENSOR
REMARK 3 S11: 0.0296 S12: -0.0670 S13: 0.0241
REMARK 3 S21: -0.0884 S22: 0.0248 S23: 0.2082
REMARK 3 S31: -0.0619 S32: 0.0340 S33: -0.0544
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): -3.5981 -94.7305 45.5212
REMARK 3 T TENSOR
REMARK 3 T11: 0.1327 T22: 0.1133
REMARK 3 T33: 0.4200 T12: 0.0847
REMARK 3 T13: -0.0166 T23: 0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 0.0638 L22: 0.4617
REMARK 3 L33: 0.9994 L12: 0.0442
REMARK 3 L13: 0.2264 L23: 0.0560
REMARK 3 S TENSOR
REMARK 3 S11: -0.0711 S12: -0.0409 S13: 0.0393
REMARK 3 S21: -0.0991 S22: 0.0649 S23: 0.2326
REMARK 3 S31: -0.1654 S32: -0.0661 S33: 0.0062
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): 14.9744 -95.2971 69.6929
REMARK 3 T TENSOR
REMARK 3 T11: 0.3573 T22: 0.1035
REMARK 3 T33: 0.1778 T12: 0.0471
REMARK 3 T13: 0.1068 T23: -0.1006
REMARK 3 L TENSOR
REMARK 3 L11: 0.7070 L22: 0.1648
REMARK 3 L33: 0.3632 L12: 0.0083
REMARK 3 L13: -0.0235 L23: -0.1774
REMARK 3 S TENSOR
REMARK 3 S11: 0.0049 S12: -0.0082 S13: 0.0817
REMARK 3 S21: 0.1067 S22: -0.0265 S23: 0.1042
REMARK 3 S31: -0.0107 S32: -0.0426 S33: 0.0217
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): 47.3843 -93.4826 70.9666
REMARK 3 T TENSOR
REMARK 3 T11: 0.3972 T22: 0.0767
REMARK 3 T33: 0.0918 T12: -0.0139
REMARK 3 T13: -0.0320 T23: -0.0643
REMARK 3 L TENSOR
REMARK 3 L11: 0.1467 L22: 0.5185
REMARK 3 L33: 0.7247 L12: -0.2258
REMARK 3 L13: -0.1318 L23: 0.0258
REMARK 3 S TENSOR
REMARK 3 S11: 0.0052 S12: 0.0111 S13: 0.0320
REMARK 3 S21: 0.2148 S22: -0.0065 S23: -0.0658
REMARK 3 S31: -0.0664 S32: -0.0170 S33: 0.0014
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 226
REMARK 3 ORIGIN FOR THE GROUP (A): 67.8127-129.2725 47.3784
REMARK 3 T TENSOR
REMARK 3 T11: 0.3414 T22: 0.3626
REMARK 3 T33: 0.3926 T12: 0.0052
REMARK 3 T13: -0.0645 T23: -0.0344
REMARK 3 L TENSOR
REMARK 3 L11: 0.0357 L22: 0.3835
REMARK 3 L33: 0.2758 L12: 0.0587
REMARK 3 L13: 0.0517 L23: 0.3137
REMARK 3 S TENSOR
REMARK 3 S11: 0.0668 S12: 0.0469 S13: 0.0238
REMARK 3 S21: 0.0561 S22: 0.0222 S23: -0.1810
REMARK 3 S31: -0.0096 S32: 0.0370 S33: -0.0891
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): 68.3523-127.1078 20.7462
REMARK 3 T TENSOR
REMARK 3 T11: 0.1906 T22: 0.1809
REMARK 3 T33: 0.2144 T12: -0.0152
REMARK 3 T13: 0.1047 T23: -0.0556
REMARK 3 L TENSOR
REMARK 3 L11: 0.2125 L22: 1.1548
REMARK 3 L33: 0.0778 L12: -0.4480
REMARK 3 L13: -0.0535 L23: 0.2269
REMARK 3 S TENSOR
REMARK 3 S11: -0.0511 S12: -0.0552 S13: 0.0191
REMARK 3 S21: -0.0527 S22: 0.1039 S23: -0.1428
REMARK 3 S31: -0.0821 S32: 0.0195 S33: -0.0528
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): 44.6754-126.6064 -0.9062
REMARK 3 T TENSOR
REMARK 3 T11: 0.3087 T22: 0.1485
REMARK 3 T33: 0.0540 T12: -0.0371
REMARK 3 T13: 0.0733 T23: 0.0159
REMARK 3 L TENSOR
REMARK 3 L11: 0.7433 L22: 1.2947
REMARK 3 L33: 0.1455 L12: -0.4947
REMARK 3 L13: 0.2441 L23: 0.0864
REMARK 3 S TENSOR
REMARK 3 S11: 0.0242 S12: -0.0255 S13: 0.0280
REMARK 3 S21: -0.2325 S22: -0.0123 S23: -0.0139
REMARK 3 S31: -0.0393 S32: -0.0128 S33: -0.0119
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): 10.9348-130.9895 2.3507
REMARK 3 T TENSOR
REMARK 3 T11: 0.2169 T22: 0.1247
REMARK 3 T33: 0.2222 T12: 0.0289
REMARK 3 T13: -0.1671 T23: 0.0439
REMARK 3 L TENSOR
REMARK 3 L11: 0.2373 L22: 1.4560
REMARK 3 L33: 0.5327 L12: 0.4241
REMARK 3 L13: 0.2457 L23: 0.0976
REMARK 3 S TENSOR
REMARK 3 S11: 0.0185 S12: 0.0402 S13: -0.0331
REMARK 3 S21: -0.1314 S22: 0.0431 S23: 0.2113
REMARK 3 S31: -0.0577 S32: 0.0664 S33: -0.0616
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): -4.5121-134.8391 28.2382
REMARK 3 T TENSOR
REMARK 3 T11: 0.0845 T22: 0.1395
REMARK 3 T33: 0.3456 T12: 0.0444
REMARK 3 T13: -0.0659 T23: 0.0552
REMARK 3 L TENSOR
REMARK 3 L11: 0.0362 L22: 0.9268
REMARK 3 L33: 0.1506 L12: 0.1168
REMARK 3 L13: 0.0699 L23: 0.2153
REMARK 3 S TENSOR
REMARK 3 S11: 0.0100 S12: 0.0060 S13: 0.0127
REMARK 3 S21: -0.0291 S22: -0.0049 S23: 0.2967
REMARK 3 S31: -0.0085 S32: 0.0031 S33: -0.0052
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): 7.7577-138.2232 60.0857
REMARK 3 T TENSOR
REMARK 3 T11: 0.2343 T22: 0.1591
REMARK 3 T33: 0.1510 T12: -0.0059
REMARK 3 T13: 0.1072 T23: -0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 0.2155 L22: 0.9043
REMARK 3 L33: 0.0719 L12: -0.0807
REMARK 3 L13: 0.1183 L23: -0.0909
REMARK 3 S TENSOR
REMARK 3 S11: 0.0046 S12: -0.0366 S13: 0.0411
REMARK 3 S21: 0.2895 S22: -0.0231 S23: 0.1619
REMARK 3 S31: -0.0319 S32: -0.0040 S33: 0.0185
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): 39.8045-134.1622 70.6522
REMARK 3 T TENSOR
REMARK 3 T11: 0.3827 T22: 0.1325
REMARK 3 T33: 0.0387 T12: -0.0093
REMARK 3 T13: -0.0382 T23: -0.0298
REMARK 3 L TENSOR
REMARK 3 L11: 0.1994 L22: 1.0032
REMARK 3 L33: 0.2028 L12: 0.0483
REMARK 3 L13: -0.1891 L23: -0.1356
REMARK 3 S TENSOR
REMARK 3 S11: 0.0473 S12: 0.0006 S13: 0.0339
REMARK 3 S21: 0.3155 S22: -0.0137 S23: 0.0192
REMARK 3 S31: -0.0154 S32: 0.0092 S33: -0.0336
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): 2.3403-207.0426 36.7334
REMARK 3 T TENSOR
REMARK 3 T11: 0.3023 T22: 0.0531
REMARK 3 T33: 0.2720 T12: -0.0891
REMARK 3 T13: -0.1001 T23: 0.0640
REMARK 3 L TENSOR
REMARK 3 L11: 0.6931 L22: 0.7618
REMARK 3 L33: 0.2348 L12: -0.5779
REMARK 3 L13: -0.2492 L23: 0.3618
REMARK 3 S TENSOR
REMARK 3 S11: -0.0744 S12: 0.0973 S13: -0.0792
REMARK 3 S21: 0.0852 S22: -0.0135 S23: 0.1710
REMARK 3 S31: 0.1588 S32: -0.0294 S33: 0.0879
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): 8.9155-206.0466 6.6471
REMARK 3 T TENSOR
REMARK 3 T11: 0.2230 T22: 0.0716
REMARK 3 T33: 0.2168 T12: -0.0266
REMARK 3 T13: -0.1339 T23: -0.0664
REMARK 3 L TENSOR
REMARK 3 L11: 0.5647 L22: 1.0965
REMARK 3 L33: 0.6550 L12: 0.0701
REMARK 3 L13: 0.2663 L23: -0.1606
REMARK 3 S TENSOR
REMARK 3 S11: -0.1087 S12: -0.0382 S13: 0.0678
REMARK 3 S21: -0.0402 S22: 0.0585 S23: 0.1127
REMARK 3 S31: 0.0506 S32: -0.0827 S33: 0.0502
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): 36.1127-203.9644 -9.1355
REMARK 3 T TENSOR
REMARK 3 T11: 0.4574 T22: 0.0744
REMARK 3 T33: 0.2874 T12: 0.0131
REMARK 3 T13: -0.2097 T23: -0.0707
REMARK 3 L TENSOR
REMARK 3 L11: 0.4480 L22: 0.9080
REMARK 3 L33: 0.4414 L12: 0.2437
REMARK 3 L13: -0.1785 L23: 0.1315
REMARK 3 S TENSOR
REMARK 3 S11: 0.0337 S12: 0.0436 S13: -0.0840
REMARK 3 S21: -0.2971 S22: 0.0708 S23: 0.1758
REMARK 3 S31: 0.1089 S32: 0.0158 S33: -0.1045
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): 65.5022-203.2162 3.2625
REMARK 3 T TENSOR
REMARK 3 T11: 0.4069 T22: 0.1214
REMARK 3 T33: 0.2278 T12: 0.1042
REMARK 3 T13: 0.1047 T23: -0.0890
REMARK 3 L TENSOR
REMARK 3 L11: 0.7379 L22: 0.7603
REMARK 3 L33: 0.2209 L12: 0.0055
REMARK 3 L13: 0.3911 L23: 0.0792
REMARK 3 S TENSOR
REMARK 3 S11: 0.0617 S12: -0.1101 S13: -0.0017
REMARK 3 S21: -0.2453 S22: -0.0251 S23: -0.1584
REMARK 3 S31: 0.0564 S32: -0.0378 S33: -0.0366
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): 72.5942-204.1124 35.3251
REMARK 3 T TENSOR
REMARK 3 T11: 0.1789 T22: 0.1116
REMARK 3 T33: 0.4408 T12: 0.1281
REMARK 3 T13: -0.1181 T23: -0.1096
REMARK 3 L TENSOR
REMARK 3 L11: 0.0962 L22: 0.7688
REMARK 3 L33: 0.7889 L12: 0.2473
REMARK 3 L13: -0.2546 L23: -0.6229
REMARK 3 S TENSOR
REMARK 3 S11: -0.0503 S12: 0.0048 S13: -0.0730
REMARK 3 S21: -0.0626 S22: 0.0633 S23: -0.2615
REMARK 3 S31: 0.2289 S32: 0.0655 S33: -0.0130
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): 54.5010-207.7070 59.5935
REMARK 3 T TENSOR
REMARK 3 T11: 0.4305 T22: 0.0607
REMARK 3 T33: 0.2984 T12: 0.0535
REMARK 3 T13: -0.2482 T23: 0.0576
REMARK 3 L TENSOR
REMARK 3 L11: 0.7868 L22: 0.1083
REMARK 3 L33: 0.3322 L12: 0.2154
REMARK 3 L13: -0.2425 L23: -0.1581
REMARK 3 S TENSOR
REMARK 3 S11: 0.0305 S12: -0.0927 S13: -0.2517
REMARK 3 S21: 0.0579 S22: -0.0233 S23: -0.0927
REMARK 3 S31: 0.0665 S32: 0.0230 S33: -0.0072
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): 22.1670-209.9192 61.1518
REMARK 3 T TENSOR
REMARK 3 T11: 0.4302 T22: 0.0469
REMARK 3 T33: 0.1472 T12: -0.0247
REMARK 3 T13: -0.0621 T23: 0.0737
REMARK 3 L TENSOR
REMARK 3 L11: 0.0896 L22: 0.3744
REMARK 3 L33: 0.6363 L12: -0.1048
REMARK 3 L13: 0.0683 L23: -0.2662
REMARK 3 S TENSOR
REMARK 3 S11: 0.0164 S12: -0.0041 S13: -0.0548
REMARK 3 S21: 0.1185 S22: -0.0019 S23: 0.0748
REMARK 3 S31: 0.0572 S32: 0.0161 S33: -0.0146
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 226
REMARK 3 ORIGIN FOR THE GROUP (A): 1.2836-170.5318 44.5885
REMARK 3 T TENSOR
REMARK 3 T11: 0.3397 T22: 0.3333
REMARK 3 T33: 0.4211 T12: -0.0454
REMARK 3 T13: 0.0231 T23: 0.0596
REMARK 3 L TENSOR
REMARK 3 L11: 0.2036 L22: 0.4278
REMARK 3 L33: 0.0219 L12: -0.0958
REMARK 3 L13: 0.0045 L23: 0.0497
REMARK 3 S TENSOR
REMARK 3 S11: 0.0652 S12: 0.0274 S13: -0.0332
REMARK 3 S21: 0.1097 S22: -0.0507 S23: 0.1852
REMARK 3 S31: 0.0770 S32: -0.0286 S33: -0.0145
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): 0.2286-168.1223 17.9718
REMARK 3 T TENSOR
REMARK 3 T11: 0.1935 T22: 0.1280
REMARK 3 T33: 0.2771 T12: -0.0215
REMARK 3 T13: -0.1626 T23: 0.0209
REMARK 3 L TENSOR
REMARK 3 L11: 0.2323 L22: 1.0722
REMARK 3 L33: 0.1172 L12: -0.4134
REMARK 3 L13: 0.1216 L23: -0.3433
REMARK 3 S TENSOR
REMARK 3 S11: -0.0352 S12: -0.0793 S13: -0.0405
REMARK 3 S21: -0.0335 S22: 0.1191 S23: 0.1651
REMARK 3 S31: 0.0390 S32: -0.0231 S33: -0.0838
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): 23.4315-164.9078 -3.9985
REMARK 3 T TENSOR
REMARK 3 T11: 0.3302 T22: 0.1167
REMARK 3 T33: 0.0822 T12: 0.0102
REMARK 3 T13: -0.1154 T23: -0.0380
REMARK 3 L TENSOR
REMARK 3 L11: 0.6429 L22: 1.5307
REMARK 3 L33: 0.0216 L12: -0.0750
REMARK 3 L13: 0.0900 L23: 0.0829
REMARK 3 S TENSOR
REMARK 3 S11: -0.0044 S12: 0.0147 S13: -0.0808
REMARK 3 S21: -0.3090 S22: 0.0384 S23: 0.0043
REMARK 3 S31: -0.0106 S32: 0.0101 S33: -0.0340
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): 57.2479-161.0999 -0.7497
REMARK 3 T TENSOR
REMARK 3 T11: 0.3192 T22: 0.1552
REMARK 3 T33: 0.1629 T12: 0.0451
REMARK 3 T13: 0.1077 T23: -0.0769
REMARK 3 L TENSOR
REMARK 3 L11: 0.2818 L22: 1.1924
REMARK 3 L33: 0.1361 L12: 0.4281
REMARK 3 L13: 0.0631 L23: -0.0861
REMARK 3 S TENSOR
REMARK 3 S11: 0.0129 S12: 0.0379 S13: -0.0193
REMARK 3 S21: -0.3303 S22: 0.0688 S23: -0.0843
REMARK 3 S31: 0.0710 S32: 0.0477 S33: -0.0817
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): 73.2110-161.6801 25.0746
REMARK 3 T TENSOR
REMARK 3 T11: 0.0896 T22: 0.1603
REMARK 3 T33: 0.2953 T12: 0.0672
REMARK 3 T13: 0.0174 T23: -0.0798
REMARK 3 L TENSOR
REMARK 3 L11: 0.0540 L22: 0.9817
REMARK 3 L33: 0.1781 L12: -0.1557
REMARK 3 L13: -0.0614 L23: -0.0265
REMARK 3 S TENSOR
REMARK 3 S11: 0.0073 S12: -0.0017 S13: 0.0150
REMARK 3 S21: -0.1073 S22: -0.0077 S23: -0.2646
REMARK 3 S31: 0.0062 S32: -0.0027 S33: 0.0004
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): 61.6098-163.7522 57.2903
REMARK 3 T TENSOR
REMARK 3 T11: 0.2368 T22: 0.1336
REMARK 3 T33: 0.2068 T12: 0.0252
REMARK 3 T13: -0.1568 T23: -0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 0.0859 L22: 0.7448
REMARK 3 L33: 0.0812 L12: -0.2189
REMARK 3 L13: 0.0565 L23: -0.1722
REMARK 3 S TENSOR
REMARK 3 S11: -0.0229 S12: 0.0078 S13: -0.0113
REMARK 3 S21: 0.2100 S22: 0.0112 S23: -0.1650
REMARK 3 S31: 0.0118 S32: -0.0449 S33: 0.0117
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): 29.8142-169.6271 67.7517
REMARK 3 T TENSOR
REMARK 3 T11: 0.3674 T22: 0.1170
REMARK 3 T33: 0.0521 T12: -0.0193
REMARK 3 T13: -0.0181 T23: 0.0638
REMARK 3 L TENSOR
REMARK 3 L11: 0.2063 L22: 0.7093
REMARK 3 L33: 0.0991 L12: -0.0132
REMARK 3 L13: 0.0902 L23: 0.0556
REMARK 3 S TENSOR
REMARK 3 S11: 0.0586 S12: -0.0055 S13: -0.0462
REMARK 3 S21: 0.2906 S22: -0.0167 S23: -0.0094
REMARK 3 S31: 0.1242 S32: -0.0600 S33: -0.0419
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 6HWC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-OCT-18.
REMARK 100 THE DEPOSITION ID IS D_1200012267.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-JUN-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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 250653
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 (%) : 96.0
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.09100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.5000
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 (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.49300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
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: 5CZ4
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 150.58500
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 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 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 O THR V 52 OG1 THR V 56 2.04
REMARK 500 O THR H 52 OG1 THR H 56 2.08
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 B 51 CB VAL B 51 CG1 -0.165
REMARK 500 VAL P 51 CB VAL P 51 CG2 -0.201
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 B 51 CA - CB - CG1 ANGL. DEV. = -15.0 DEGREES
REMARK 500 VAL P 51 CB - CA - C ANGL. DEV. = -18.0 DEGREES
REMARK 500 VAL P 51 CA - CB - CG2 ANGL. DEV. = -13.9 DEGREES
REMARK 500 VAL P 224 CG1 - CB - CG2 ANGL. DEV. = 9.6 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 TYR A 97 -65.10 -148.61
REMARK 500 ALA A 249 52.59 -93.99
REMARK 500 ARG B 8 75.51 63.84
REMARK 500 THR B 10 55.75 -112.38
REMARK 500 THR B 52 107.92 4.76
REMARK 500 LYS B 217 53.81 -91.90
REMARK 500 PRO C 183 106.00 -49.02
REMARK 500 ARG D 2 147.30 -176.95
REMARK 500 SER D 5 30.31 -96.28
REMARK 500 SER E 39 -162.06 -111.40
REMARK 500 ASP E 137 -160.27 -124.18
REMARK 500 ASN E 184 80.17 -150.76
REMARK 500 ASP E 202 -57.74 68.66
REMARK 500 ASP F 67 -133.38 57.50
REMARK 500 LYS F 100 -57.31 72.61
REMARK 500 ASP F 138 -169.49 -122.93
REMARK 500 SER H 171 -108.90 67.83
REMARK 500 GLN I 31 -109.96 55.85
REMARK 500 ARG I 97 40.13 -105.07
REMARK 500 ASP I 134 -70.02 -85.72
REMARK 500 ASP I 192 32.56 -144.58
REMARK 500 GLN I 203 45.55 -105.41
REMARK 500 ASP J 2 -94.75 -95.36
REMARK 500 VAL J 9 -162.90 -104.13
REMARK 500 SER J 31 32.52 -148.93
REMARK 500 LYS J 34 57.28 -92.67
REMARK 500 ASP K 147 32.13 -86.60
REMARK 500 ASP L 32 -117.62 52.91
REMARK 500 LYS L 100 41.20 -107.94
REMARK 500 PHE L 103 68.44 -156.75
REMARK 500 ASN L 165 72.86 55.84
REMARK 500 ASP L 200 -66.94 70.51
REMARK 500 ILE M 5 -73.84 -111.33
REMARK 500 THR M 9 -152.64 -89.64
REMARK 500 ASN M 26 33.38 -98.29
REMARK 500 ALA M 83 -117.28 -147.44
REMARK 500 ASN M 108 70.51 -150.29
REMARK 500 LYS N 107 -144.98 68.04
REMARK 500 TYR O 97 -65.15 -148.21
REMARK 500 ALA O 249 52.68 -94.05
REMARK 500 ARG P 8 75.81 64.18
REMARK 500 THR P 10 54.81 -112.28
REMARK 500 LYS P 217 53.71 -92.32
REMARK 500 PRO Q 183 106.37 -49.25
REMARK 500 ARG R 2 147.89 -176.14
REMARK 500 SER S 39 -162.53 -111.28
REMARK 500 ASP S 137 -161.78 -124.50
REMARK 500 ASN S 184 80.87 -151.02
REMARK 500 ASP S 202 -57.86 68.69
REMARK 500 ASP T 67 -133.16 57.25
REMARK 500
REMARK 500 THIS ENTRY HAS 69 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH D 327 DISTANCE = 7.77 ANGSTROMS
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 81.0
REMARK 620 3 ARG G 122 O 79.1 79.0
REMARK 620 4 MET G 125 O 163.1 87.3 86.9
REMARK 620 N 1 2 3
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 ASP I 177 O
REMARK 620 2 SER I 180 O 70.4
REMARK 620 3 HOH I 411 O 129.3 82.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG Y 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP I 204 O
REMARK 620 2 ALA Y 165 O 99.5
REMARK 620 3 ASP Y 168 O 153.8 93.7
REMARK 620 4 SER Y 171 O 88.7 73.5 73.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG K 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA K 165 O
REMARK 620 2 ASP K 168 O 95.0
REMARK 620 3 SER K 171 O 75.5 73.2
REMARK 620 4 ASP W 204 O 103.9 151.6 91.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG V 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP L 222 OXT
REMARK 620 2 ILE V 163 O 94.0
REMARK 620 3 ASP V 166 O 120.0 102.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG N 201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE N 163 O
REMARK 620 2 SER N 169 O 93.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG W 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP W 177 O
REMARK 620 2 SER W 180 O 80.3
REMARK 620 3 HOH W 417 O 144.7 96.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG Z 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR Z 192 O
REMARK 620 2 HIS Z 195 O 73.3
REMARK 620 3 VAL Z 198 O 87.4 73.3
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 MES 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 K 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG N 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL U 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG V 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 V 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG W 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG Y 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG Z 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5CZ4 RELATED DB: PDB
REMARK 900 YEAST 20S PROTEASOME AT 2.3 A RESOLUTION
DBREF 6HWC A 1 250 UNP P23639 PSA2_YEAST 1 250
DBREF 6HWC B 0 257 UNP P23638 PSA3_YEAST 1 258
DBREF 6HWC C -1 252 UNP P40303 PSA4_YEAST 1 254
DBREF 6HWC D -7 252 UNP P32379 PSA5_YEAST 1 260
DBREF 6HWC E 0 233 UNP P40302 PSA6_YEAST 1 234
DBREF 6HWC F -3 284 UNP P21242 PSA7_YEAST 1 288
DBREF 6HWC G -8 243 UNP P21243 PSA1_YEAST 1 252
DBREF 6HWC H 1 232 UNP P25043 PSB2_YEAST 30 261
DBREF 6HWC I 0 204 UNP P25451 PSB3_YEAST 1 205
DBREF 6HWC J 1 198 UNP P22141 PSB4_YEAST 1 198
DBREF 6HWC K 1 212 UNP P30656 PSB5_YEAST 76 287
DBREF 6HWC L 1 222 UNP P23724 PSB6_YEAST 20 241
DBREF 6HWC M -12 233 UNP P30657 PSB7_YEAST 21 266
DBREF 6HWC N 1 196 UNP P38624 PSB1_YEAST 20 215
DBREF 6HWC O 1 250 UNP P23639 PSA2_YEAST 1 250
DBREF 6HWC P 0 257 UNP P23638 PSA3_YEAST 1 258
DBREF 6HWC Q -1 252 UNP P40303 PSA4_YEAST 1 254
DBREF 6HWC R -7 252 UNP P32379 PSA5_YEAST 1 260
DBREF 6HWC S 0 233 UNP P40302 PSA6_YEAST 1 234
DBREF 6HWC T -3 284 UNP P21242 PSA7_YEAST 1 288
DBREF 6HWC U -8 243 UNP P21243 PSA1_YEAST 1 252
DBREF 6HWC V 1 232 UNP P25043 PSB2_YEAST 30 261
DBREF 6HWC W 0 204 UNP P25451 PSB3_YEAST 1 205
DBREF 6HWC X 1 198 UNP P22141 PSB4_YEAST 1 198
DBREF 6HWC Y 1 212 UNP P30656 PSB5_YEAST 76 287
DBREF 6HWC Z 1 222 UNP P23724 PSB6_YEAST 20 241
DBREF 6HWC a -12 233 UNP P30657 PSB7_YEAST 21 266
DBREF 6HWC b 1 196 UNP P38624 PSB1_YEAST 20 215
SEQADV 6HWC ALA H 45 UNP P25043 GLY 74 ENGINEERED MUTATION
SEQADV 6HWC ALA V 45 UNP P25043 GLY 74 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 ALA ALA GLY THR ALA ALA ASP THR
SEQRES 5 H 232 GLU ALA VAL THR GLN LEU ILE GLY SER ASN ILE GLU LEU
SEQRES 6 H 232 HIS SER LEU TYR THR SER ARG GLU PRO ARG VAL VAL SER
SEQRES 7 H 232 ALA LEU GLN MET LEU LYS GLN HIS LEU PHE LYS TYR GLN
SEQRES 8 H 232 GLY HIS ILE GLY ALA TYR LEU ILE VAL ALA GLY VAL ASP
SEQRES 9 H 232 PRO THR GLY SER HIS LEU PHE SER ILE HIS ALA HIS GLY
SEQRES 10 H 232 SER THR ASP VAL GLY TYR TYR LEU SER LEU GLY SER GLY
SEQRES 11 H 232 SER LEU ALA ALA MET ALA VAL LEU GLU SER HIS TRP LYS
SEQRES 12 H 232 GLN ASP LEU THR LYS GLU GLU ALA ILE LYS LEU ALA SER
SEQRES 13 H 232 ASP ALA ILE GLN ALA GLY ILE TRP ASN ASP LEU GLY SER
SEQRES 14 H 232 GLY SER ASN VAL ASP VAL CYS VAL MET GLU ILE GLY LYS
SEQRES 15 H 232 ASP ALA GLU TYR LEU ARG ASN TYR LEU THR PRO ASN VAL
SEQRES 16 H 232 ARG GLU GLU LYS GLN LYS SER TYR LYS PHE PRO ARG GLY
SEQRES 17 H 232 THR THR ALA VAL LEU LYS GLU SER ILE VAL ASN ILE CYS
SEQRES 18 H 232 ASP ILE GLN GLU GLU GLN VAL ASP ILE THR ALA
SEQRES 1 I 205 MET SER ASP PRO SER SER ILE ASN GLY GLY ILE VAL VAL
SEQRES 2 I 205 ALA MET THR GLY LYS ASP CYS VAL ALA ILE ALA CYS ASP
SEQRES 3 I 205 LEU ARG LEU GLY SER GLN SER LEU GLY VAL SER ASN LYS
SEQRES 4 I 205 PHE GLU LYS ILE PHE HIS TYR GLY HIS VAL PHE LEU GLY
SEQRES 5 I 205 ILE THR GLY LEU ALA THR ASP VAL THR THR LEU ASN GLU
SEQRES 6 I 205 MET PHE ARG TYR LYS THR ASN LEU TYR LYS LEU LYS GLU
SEQRES 7 I 205 GLU ARG ALA ILE GLU PRO GLU THR PHE THR GLN LEU VAL
SEQRES 8 I 205 SER SER SER LEU TYR GLU ARG ARG PHE GLY PRO TYR PHE
SEQRES 9 I 205 VAL GLY PRO VAL VAL ALA GLY ILE ASN SER LYS SER GLY
SEQRES 10 I 205 LYS PRO PHE ILE ALA GLY PHE ASP LEU ILE GLY CYS ILE
SEQRES 11 I 205 ASP GLU ALA LYS ASP PHE ILE VAL SER GLY THR ALA SER
SEQRES 12 I 205 ASP GLN LEU PHE GLY MET CYS GLU SER LEU TYR GLU PRO
SEQRES 13 I 205 ASN LEU GLU PRO GLU ASP LEU PHE GLU THR ILE SER GLN
SEQRES 14 I 205 ALA LEU LEU ASN ALA ALA ASP ARG ASP ALA LEU SER GLY
SEQRES 15 I 205 TRP GLY ALA VAL VAL TYR ILE ILE LYS LYS ASP GLU VAL
SEQRES 16 I 205 VAL LYS ARG TYR LEU LYS MET ARG GLN ASP
SEQRES 1 J 198 MET ASP ILE ILE LEU GLY ILE ARG VAL GLN ASP SER VAL
SEQRES 2 J 198 ILE LEU ALA SER SER LYS ALA VAL THR ARG GLY ILE SER
SEQRES 3 J 198 VAL LEU LYS ASP SER ASP ASP LYS THR ARG GLN LEU SER
SEQRES 4 J 198 PRO HIS THR LEU MET SER PHE ALA GLY GLU ALA GLY ASP
SEQRES 5 J 198 THR VAL GLN PHE ALA GLU TYR ILE GLN ALA ASN ILE GLN
SEQRES 6 J 198 LEU TYR SER ILE ARG GLU ASP TYR GLU LEU SER PRO GLN
SEQRES 7 J 198 ALA VAL SER SER PHE VAL ARG GLN GLU LEU ALA LYS SER
SEQRES 8 J 198 ILE ARG SER ARG ARG PRO TYR GLN VAL ASN VAL LEU ILE
SEQRES 9 J 198 GLY GLY TYR ASP LYS LYS LYS ASN LYS PRO GLU LEU TYR
SEQRES 10 J 198 GLN ILE ASP TYR LEU GLY THR LYS VAL GLU LEU PRO TYR
SEQRES 11 J 198 GLY ALA HIS GLY TYR SER GLY PHE TYR THR PHE SER LEU
SEQRES 12 J 198 LEU ASP HIS HIS TYR ARG PRO ASP MET THR THR GLU GLU
SEQRES 13 J 198 GLY LEU ASP LEU LEU LYS LEU CYS VAL GLN GLU LEU GLU
SEQRES 14 J 198 LYS ARG MET PRO MET ASP PHE LYS GLY VAL ILE VAL LYS
SEQRES 15 J 198 ILE VAL ASP LYS ASP GLY ILE ARG GLN VAL ASP ASP PHE
SEQRES 16 J 198 GLN ALA GLN
SEQRES 1 K 212 THR THR THR LEU ALA PHE ARG PHE GLN GLY GLY ILE ILE
SEQRES 2 K 212 VAL ALA VAL ASP SER ARG ALA THR ALA GLY ASN TRP VAL
SEQRES 3 K 212 ALA SER GLN THR VAL LYS LYS VAL ILE GLU ILE ASN PRO
SEQRES 4 K 212 PHE LEU LEU GLY THR MET ALA GLY GLY ALA ALA ASP CYS
SEQRES 5 K 212 GLN PHE TRP GLU THR TRP LEU GLY SER GLN CYS ARG LEU
SEQRES 6 K 212 HIS GLU LEU ARG GLU LYS GLU ARG ILE SER VAL ALA ALA
SEQRES 7 K 212 ALA SER LYS ILE LEU SER ASN LEU VAL TYR GLN TYR LYS
SEQRES 8 K 212 GLY ALA GLY LEU SER MET GLY THR MET ILE CYS GLY TYR
SEQRES 9 K 212 THR ARG LYS GLU GLY PRO THR ILE TYR TYR VAL ASP SER
SEQRES 10 K 212 ASP GLY THR ARG LEU LYS GLY ASP ILE PHE CYS VAL GLY
SEQRES 11 K 212 SER GLY GLN THR PHE ALA TYR GLY VAL LEU ASP SER ASN
SEQRES 12 K 212 TYR LYS TRP ASP LEU SER VAL GLU ASP ALA LEU TYR LEU
SEQRES 13 K 212 GLY LYS ARG SER ILE LEU ALA ALA ALA HIS ARG ASP ALA
SEQRES 14 K 212 TYR SER GLY GLY SER VAL ASN LEU TYR HIS VAL THR GLU
SEQRES 15 K 212 ASP GLY TRP ILE TYR HIS GLY ASN HIS ASP VAL GLY GLU
SEQRES 16 K 212 LEU PHE TRP LYS VAL LYS GLU GLU GLU GLY SER PHE ASN
SEQRES 17 K 212 ASN VAL ILE GLY
SEQRES 1 L 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 ALA ALA GLY THR ALA ALA ASP THR
SEQRES 5 V 232 GLU ALA VAL THR GLN LEU ILE GLY SER ASN ILE GLU LEU
SEQRES 6 V 232 HIS SER LEU TYR THR SER ARG GLU PRO ARG VAL VAL SER
SEQRES 7 V 232 ALA LEU GLN MET LEU LYS GLN HIS LEU PHE LYS TYR GLN
SEQRES 8 V 232 GLY HIS ILE GLY ALA TYR LEU ILE VAL ALA GLY VAL ASP
SEQRES 9 V 232 PRO THR GLY SER HIS LEU PHE SER ILE HIS ALA HIS GLY
SEQRES 10 V 232 SER THR ASP VAL GLY TYR TYR LEU SER LEU GLY SER GLY
SEQRES 11 V 232 SER LEU ALA ALA MET ALA VAL LEU GLU SER HIS TRP LYS
SEQRES 12 V 232 GLN ASP LEU THR LYS GLU GLU ALA ILE LYS LEU ALA SER
SEQRES 13 V 232 ASP ALA ILE GLN ALA GLY ILE TRP ASN ASP LEU GLY SER
SEQRES 14 V 232 GLY SER ASN VAL ASP VAL CYS VAL MET GLU ILE GLY LYS
SEQRES 15 V 232 ASP ALA GLU TYR LEU ARG ASN TYR LEU THR PRO ASN VAL
SEQRES 16 V 232 ARG GLU GLU LYS GLN LYS SER TYR LYS PHE PRO ARG GLY
SEQRES 17 V 232 THR THR ALA VAL LEU LYS GLU SER ILE VAL ASN ILE CYS
SEQRES 18 V 232 ASP ILE GLN GLU GLU GLN VAL ASP ILE THR ALA
SEQRES 1 W 205 MET SER ASP PRO SER SER ILE ASN GLY GLY ILE VAL VAL
SEQRES 2 W 205 ALA MET THR GLY LYS ASP CYS VAL ALA ILE ALA CYS ASP
SEQRES 3 W 205 LEU ARG LEU GLY SER GLN SER LEU GLY VAL SER ASN LYS
SEQRES 4 W 205 PHE GLU LYS ILE PHE HIS TYR GLY HIS VAL PHE LEU GLY
SEQRES 5 W 205 ILE THR GLY LEU ALA THR ASP VAL THR THR LEU ASN GLU
SEQRES 6 W 205 MET PHE ARG TYR LYS THR ASN LEU TYR LYS LEU LYS GLU
SEQRES 7 W 205 GLU ARG ALA ILE GLU PRO GLU THR PHE THR GLN LEU VAL
SEQRES 8 W 205 SER SER SER LEU TYR GLU ARG ARG PHE GLY PRO TYR PHE
SEQRES 9 W 205 VAL GLY PRO VAL VAL ALA GLY ILE ASN SER LYS SER GLY
SEQRES 10 W 205 LYS PRO PHE ILE ALA GLY PHE ASP LEU ILE GLY CYS ILE
SEQRES 11 W 205 ASP GLU ALA LYS ASP PHE ILE VAL SER GLY THR ALA SER
SEQRES 12 W 205 ASP GLN LEU PHE GLY MET CYS GLU SER LEU TYR GLU PRO
SEQRES 13 W 205 ASN LEU GLU PRO GLU ASP LEU PHE GLU THR ILE SER GLN
SEQRES 14 W 205 ALA LEU LEU ASN ALA ALA ASP ARG ASP ALA LEU SER GLY
SEQRES 15 W 205 TRP GLY ALA VAL VAL TYR ILE ILE LYS LYS ASP GLU VAL
SEQRES 16 W 205 VAL LYS ARG TYR LEU LYS MET ARG GLN ASP
SEQRES 1 X 198 MET ASP ILE ILE LEU GLY ILE ARG VAL GLN ASP SER VAL
SEQRES 2 X 198 ILE LEU ALA SER SER LYS ALA VAL THR ARG GLY ILE SER
SEQRES 3 X 198 VAL LEU LYS ASP SER ASP ASP LYS THR ARG GLN LEU SER
SEQRES 4 X 198 PRO HIS THR LEU MET SER PHE ALA GLY GLU ALA GLY ASP
SEQRES 5 X 198 THR VAL GLN PHE ALA GLU TYR ILE GLN ALA ASN ILE GLN
SEQRES 6 X 198 LEU TYR SER ILE ARG GLU ASP TYR GLU LEU SER PRO GLN
SEQRES 7 X 198 ALA VAL SER SER PHE VAL ARG GLN GLU LEU ALA LYS SER
SEQRES 8 X 198 ILE ARG SER ARG ARG PRO TYR GLN VAL ASN VAL LEU ILE
SEQRES 9 X 198 GLY GLY TYR ASP LYS LYS LYS ASN LYS PRO GLU LEU TYR
SEQRES 10 X 198 GLN ILE ASP TYR LEU GLY THR LYS VAL GLU LEU PRO TYR
SEQRES 11 X 198 GLY ALA HIS GLY TYR SER GLY PHE TYR THR PHE SER LEU
SEQRES 12 X 198 LEU ASP HIS HIS TYR ARG PRO ASP MET THR THR GLU GLU
SEQRES 13 X 198 GLY LEU ASP LEU LEU LYS LEU CYS VAL GLN GLU LEU GLU
SEQRES 14 X 198 LYS ARG MET PRO MET ASP PHE LYS GLY VAL ILE VAL LYS
SEQRES 15 X 198 ILE VAL ASP LYS ASP GLY ILE ARG GLN VAL ASP ASP PHE
SEQRES 16 X 198 GLN ALA GLN
SEQRES 1 Y 212 THR THR THR LEU ALA PHE ARG PHE GLN GLY GLY ILE ILE
SEQRES 2 Y 212 VAL ALA VAL ASP SER ARG ALA THR ALA GLY ASN TRP VAL
SEQRES 3 Y 212 ALA SER GLN THR VAL LYS LYS VAL ILE GLU ILE ASN PRO
SEQRES 4 Y 212 PHE LEU LEU GLY THR MET ALA GLY GLY ALA ALA ASP CYS
SEQRES 5 Y 212 GLN PHE TRP GLU THR TRP LEU GLY SER GLN CYS ARG LEU
SEQRES 6 Y 212 HIS GLU LEU ARG GLU LYS GLU ARG ILE SER VAL ALA ALA
SEQRES 7 Y 212 ALA SER LYS ILE LEU SER ASN LEU VAL TYR GLN TYR LYS
SEQRES 8 Y 212 GLY ALA GLY LEU SER MET GLY THR MET ILE CYS GLY TYR
SEQRES 9 Y 212 THR ARG LYS GLU GLY PRO THR ILE TYR TYR VAL ASP SER
SEQRES 10 Y 212 ASP GLY THR ARG LEU LYS GLY ASP ILE PHE CYS VAL GLY
SEQRES 11 Y 212 SER GLY GLN THR PHE ALA TYR GLY VAL LEU ASP SER ASN
SEQRES 12 Y 212 TYR LYS TRP ASP LEU SER VAL GLU ASP ALA LEU TYR LEU
SEQRES 13 Y 212 GLY LYS ARG SER ILE LEU ALA ALA ALA HIS ARG ASP ALA
SEQRES 14 Y 212 TYR SER GLY GLY SER VAL ASN LEU TYR HIS VAL THR GLU
SEQRES 15 Y 212 ASP GLY TRP ILE TYR HIS GLY ASN HIS ASP VAL GLY GLU
SEQRES 16 Y 212 LEU PHE TRP LYS VAL LYS GLU GLU GLU GLY SER PHE ASN
SEQRES 17 Y 212 ASN VAL ILE GLY
SEQRES 1 Z 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 MES H 301 12
HET MG I 301 1
HET MG K 301 1
HET MG N 201 1
HET CL U 301 1
HET MG V 301 1
HET SO4 V 302 5
HET MG W 301 1
HET MG Y 301 1
HET MG Z 301 1
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM SO4 SULFATE ION
FORMUL 29 MG 8(MG 2+)
FORMUL 30 CL 2(CL 1-)
FORMUL 31 MES C6 H13 N O4 S
FORMUL 37 SO4 O4 S 2-
FORMUL 41 HOH *722(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 LEU B 79 ASN B 102 1 24
HELIX 12 AB3 PRO B 106 HIS B 124 1 19
HELIX 13 AB4 ASN B 167 TYR B 179 1 13
HELIX 14 AB5 LYS B 184 THR B 200 1 17
HELIX 15 AB6 THR B 206 ASP B 208 5 3
HELIX 16 AB7 LYS B 230 THR B 241 1 12
HELIX 17 AB8 ILE C 15 GLY C 28 1 14
HELIX 18 AB9 LEU C 76 GLU C 99 1 24
HELIX 19 AC1 THR C 103 TYR C 118 1 16
HELIX 20 AC2 ASN C 165 TYR C 177 1 13
HELIX 21 AC3 THR C 185 GLN C 202 1 18
HELIX 22 AC4 SER C 223 GLN C 239 1 17
HELIX 23 AC5 LEU D 13 LEU D 25 1 13
HELIX 24 AC6 GLU D 52 ILE D 56 5 5
HELIX 25 AC7 ASP D 76 ASP D 96 1 21
HELIX 26 AC8 ASN D 100 ALA D 112 1 13
HELIX 27 AC9 GLY D 167 TRP D 179 1 13
HELIX 28 AD1 THR D 184 MET D 200 1 17
HELIX 29 AD2 ASP D 224 ALA D 241 1 18
HELIX 30 AD3 LEU E 18 GLY E 31 1 14
HELIX 31 AD4 LEU E 76 ASN E 99 1 24
HELIX 32 AD5 ALA E 103 SER E 121 1 19
HELIX 33 AD6 ARG E 163 ILE E 179 1 17
HELIX 34 AD7 ASN E 184 SER E 197 1 14
HELIX 35 AD8 GLN E 198 LEU E 200 5 3
HELIX 36 AD9 GLU E 227 ILE E 233 5 7
HELIX 37 AE1 ASN F 17 GLY F 30 1 14
HELIX 38 AE2 LEU F 77 LYS F 100 1 24
HELIX 39 AE3 PRO F 104 HIS F 119 1 16
HELIX 40 AE4 GLY F 164 HIS F 179 1 16
HELIX 41 AE5 SER F 184 HIS F 200 1 17
HELIX 42 AE6 GLU F 201 LYS F 204 5 4
HELIX 43 AE7 LYS F 228 ASN F 244 1 17
HELIX 44 AE8 GLY G 2 HIS G 6 5 5
HELIX 45 AE9 LEU G 16 THR G 26 1 11
HELIX 46 AF1 ASP G 56 VAL G 60 5 5
HELIX 47 AF2 PRO G 77 GLY G 100 1 24
HELIX 48 AF3 PRO G 104 ARG G 122 1 19
HELIX 49 AF4 LYS G 165 LYS G 181 1 17
HELIX 50 AF5 SER G 189 GLY G 206 1 18
HELIX 51 AF6 SER G 228 GLU G 241 1 14
HELIX 52 AF7 THR H 48 SER H 71 1 24
HELIX 53 AF8 ARG H 75 TYR H 90 1 16
HELIX 54 AF9 GLY H 130 TRP H 142 1 13
HELIX 55 AG1 THR H 147 ASP H 166 1 20
HELIX 56 AG2 ASP I 2 ILE I 6 5 5
HELIX 57 AG3 LEU I 55 GLU I 78 1 24
HELIX 58 AG4 GLU I 82 GLU I 96 1 15
HELIX 59 AG5 ALA I 141 TYR I 153 1 13
HELIX 60 AG6 GLU I 158 ASP I 175 1 18
HELIX 61 AG7 GLY J 51 ASP J 72 1 22
HELIX 62 AG8 SER J 76 ILE J 92 1 17
HELIX 63 AG9 TYR J 135 TYR J 148 1 14
HELIX 64 AH1 THR J 153 MET J 172 1 20
HELIX 65 AH2 GLY K 48 LYS K 71 1 24
HELIX 66 AH3 SER K 75 TYR K 90 1 16
HELIX 67 AH4 GLY K 132 TYR K 144 1 13
HELIX 68 AH5 SER K 149 ASP K 168 1 20
HELIX 69 AH6 VAL K 193 GLY K 205 1 13
HELIX 70 AH7 PHE L 57 HIS L 79 1 23
HELIX 71 AH8 SER L 85 GLY L 99 1 15
HELIX 72 AH9 ALA L 142 VAL L 154 1 13
HELIX 73 AI1 SER L 176 HIS L 195 1 20
HELIX 74 AI2 ILE M 57 TYR M 76 1 20
HELIX 75 AI3 GLU M 88 LYS M 106 1 19
HELIX 76 AI4 GLY M 145 LYS M 157 1 13
HELIX 77 AI5 ARG M 161 ILE M 165 5 5
HELIX 78 AI6 THR M 169 ASP M 188 1 20
HELIX 79 AI7 TRP M 219 ILE M 225 5 7
HELIX 80 AI8 SER N 48 GLY N 71 1 24
HELIX 81 AI9 SER N 74 ASN N 89 1 16
HELIX 82 AJ1 LYS N 90 LEU N 93 5 4
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 LEU P 79 ASN P 102 1 24
HELIX 98 AK8 PRO P 106 HIS P 124 1 19
HELIX 99 AK9 ASN P 167 TYR P 179 1 13
HELIX 100 AL1 LYS P 184 THR P 200 1 17
HELIX 101 AL2 THR P 206 ASP P 208 5 3
HELIX 102 AL3 LYS P 230 THR P 241 1 12
HELIX 103 AL4 ILE Q 15 GLY Q 28 1 14
HELIX 104 AL5 LEU Q 76 GLU Q 99 1 24
HELIX 105 AL6 THR Q 103 TYR Q 118 1 16
HELIX 106 AL7 ASN Q 165 TYR Q 177 1 13
HELIX 107 AL8 THR Q 185 GLN Q 202 1 18
HELIX 108 AL9 SER Q 223 GLN Q 239 1 17
HELIX 109 AM1 LEU R 13 LEU R 25 1 13
HELIX 110 AM2 GLU R 52 ILE R 56 5 5
HELIX 111 AM3 ASP R 76 ASP R 96 1 21
HELIX 112 AM4 ASN R 100 ALA R 112 1 13
HELIX 113 AM5 GLY R 167 TRP R 179 1 13
HELIX 114 AM6 THR R 184 MET R 200 1 17
HELIX 115 AM7 ASP R 224 ALA R 241 1 18
HELIX 116 AM8 LEU S 18 GLY S 31 1 14
HELIX 117 AM9 LEU S 76 ASN S 99 1 24
HELIX 118 AN1 ALA S 103 SER S 121 1 19
HELIX 119 AN2 ARG S 163 ILE S 179 1 17
HELIX 120 AN3 ASN S 184 SER S 197 1 14
HELIX 121 AN4 GLN S 198 LEU S 200 5 3
HELIX 122 AN5 ASP S 225 ILE S 233 5 9
HELIX 123 AN6 ASN T 17 GLY T 30 1 14
HELIX 124 AN7 LEU T 77 LYS T 100 1 24
HELIX 125 AN8 PRO T 104 HIS T 119 1 16
HELIX 126 AN9 GLY T 164 HIS T 179 1 16
HELIX 127 AO1 SER T 184 HIS T 200 1 17
HELIX 128 AO2 GLU T 201 LYS T 204 5 4
HELIX 129 AO3 LYS T 228 ASN T 244 1 17
HELIX 130 AO4 GLY U 2 HIS U 6 5 5
HELIX 131 AO5 LEU U 16 THR U 26 1 11
HELIX 132 AO6 ASP U 56 VAL U 60 5 5
HELIX 133 AO7 PRO U 77 GLY U 100 1 24
HELIX 134 AO8 PRO U 104 ARG U 122 1 19
HELIX 135 AO9 LYS U 165 LYS U 181 1 17
HELIX 136 AP1 SER U 189 GLY U 206 1 18
HELIX 137 AP2 SER U 228 GLU U 241 1 14
HELIX 138 AP3 THR V 48 SER V 71 1 24
HELIX 139 AP4 ARG V 75 TYR V 90 1 16
HELIX 140 AP5 GLY V 130 TRP V 142 1 13
HELIX 141 AP6 THR V 147 ASP V 166 1 20
HELIX 142 AP7 ASP W 2 ILE W 6 5 5
HELIX 143 AP8 LEU W 55 GLU W 78 1 24
HELIX 144 AP9 GLU W 82 GLU W 96 1 15
HELIX 145 AQ1 ALA W 141 TYR W 153 1 13
HELIX 146 AQ2 GLU W 158 ASP W 175 1 18
HELIX 147 AQ3 GLY X 51 ASP X 72 1 22
HELIX 148 AQ4 SER X 76 ILE X 92 1 17
HELIX 149 AQ5 TYR X 135 TYR X 148 1 14
HELIX 150 AQ6 THR X 153 MET X 172 1 20
HELIX 151 AQ7 GLY Y 48 LYS Y 71 1 24
HELIX 152 AQ8 SER Y 75 TYR Y 90 1 16
HELIX 153 AQ9 GLY Y 132 TYR Y 144 1 13
HELIX 154 AR1 SER Y 149 ASP Y 168 1 20
HELIX 155 AR2 VAL Y 193 GLY Y 205 1 13
HELIX 156 AR3 PHE Z 57 HIS Z 79 1 23
HELIX 157 AR4 SER Z 85 GLY Z 99 1 15
HELIX 158 AR5 ALA Z 142 VAL Z 154 1 13
HELIX 159 AR6 SER Z 176 HIS Z 195 1 20
HELIX 160 AR7 ILE a 57 TYR a 76 1 20
HELIX 161 AR8 GLU a 88 LYS a 106 1 19
HELIX 162 AR9 GLY a 145 LYS a 157 1 13
HELIX 163 AS1 ARG a 161 ILE a 165 5 5
HELIX 164 AS2 THR a 169 ASP a 188 1 20
HELIX 165 AS3 TRP a 219 ILE a 225 5 7
HELIX 166 AS4 SER b 48 GLY b 71 1 24
HELIX 167 AS5 SER b 74 ASN b 89 1 16
HELIX 168 AS6 LYS b 90 LEU b 93 5 4
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 ASP H 17 -1 N ALA H 16 O ASP H 174
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 127 N ILE H 3
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 GLN B 146 N GLY B 138
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 THR C 211 N LEU C 42
SHEET 5 AA6 5 ASP C 218 ALA C 221 -1 O VAL C 220 N VAL C 212
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 GLN D 146 N GLY D 138
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 ASP E 225 -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 LEU E 155 -1 O LEU E 155 N LEU E 143
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 VAL F 43 N ILE F 36
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 LYS G 223 N THR G 220
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 ILE H 25 N GLN H 22
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 ILE H 99 N ALA H 44
SHEET 4 AB8 5 GLY H 107 ILE H 113 -1 O PHE H 111 N VAL H 100
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 ILE H 217 0
SHEET 2 AB9 6 GLU I 193 LEU I 199 -1 O TYR I 198 N LEU H 213
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 ILE I 22 O TYR I 187
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 ALA J 132 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 MET J 44 N ARG J 36
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 GLU J 127 -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 ALA K 5 O PHE K 127
SHEET 3 AC6 5 GLY K 11 VAL K 16 -1 O GLY K 11 N PHE K 8
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 GLU K 36 0
SHEET 2 AC8 5 LEU K 42 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 GLY K 124 -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 ILE L 12 O GLY L 139
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 GLU L 215 N ILE L 204
SHEET 1 AD1 2 ASN L 29 THR L 31 0
SHEET 2 AD1 2 SER L 34 SER L 37 -1 O SER L 37 N ASN L 29
SHEET 1 AD2 5 VAL L 43 ASP L 45 0
SHEET 2 AD2 5 VAL L 51 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 VAL M 45 -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 ILE M 115 N GLY M 52
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 SER M 138 -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 THR N 7 -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 GLY N 182 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 ILE N 41 N VAL N 37
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 VAL U 73 O THR U 133
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 ASP V 17 -1 N ALA V 16 O ASP V 174
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 127 N ILE V 3
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 GLN P 146 N GLY P 138
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 THR Q 211 N LEU Q 42
SHEET 5 AE6 5 ASP Q 218 ALA Q 221 -1 O VAL Q 220 N VAL Q 212
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 GLN R 146 N GLY R 138
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 MET S 69 N ASP S 66
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 CYS T 38 -1 N GLY T 35 O ALA T 159
SHEET 3 AF3 5 GLY T 41 LEU T 49 -1 O VAL T 43 N ILE T 36
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 ALA U 219 N THR U 42
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 ILE V 25 N GLN V 22
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 ALA V 101 N TRP V 42
SHEET 4 AF7 5 GLY V 107 ILE V 113 -1 O PHE V 111 N VAL V 100
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 MET W 14 O ALA W 21
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 ALA W 109 N PHE W 49
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 ALA X 132 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 SER X 26 N ARG X 23
SHEET 1 AG4 5 THR X 35 SER X 39 0
SHEET 2 AG4 5 THR X 42 GLY X 48 -1 O MET X 44 N ARG X 36
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 GLU X 127 -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 ALA Y 5 O PHE Y 127
SHEET 3 AG5 5 GLY Y 11 VAL Y 16 -1 O GLY Y 11 N PHE Y 8
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 GLU Y 36 0
SHEET 2 AG7 5 LEU Y 42 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 GLY Y 124 -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 GLY Z 14 O ARG Z 137
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 ARG Z 213 N ILE Z 206
SHEET 1 AG9 2 ASN Z 29 THR Z 31 0
SHEET 2 AG9 2 SER Z 34 SER Z 37 -1 O SER Z 37 N ASN Z 29
SHEET 1 AH1 5 VAL Z 43 ASP Z 45 0
SHEET 2 AH1 5 VAL Z 51 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 VAL a 45 -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 ILE a 115 N GLY a 52
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 SER a 138 -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 ALA b 5 O ALA b 125
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 GLY b 182 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 ALA b 100 N TRP b 42
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 G 8 MG MG G 301 1555 1555 2.75
LINK O TYR G 119 MG MG G 301 1555 1555 2.57
LINK O ARG G 122 MG MG G 301 1555 1555 2.65
LINK O MET G 125 MG MG G 301 1555 1555 2.13
LINK O ASP I 177 MG MG I 301 1555 1555 2.64
LINK O SER I 180 MG MG I 301 1555 1555 2.93
LINK O ASP I 204 MG MG Y 301 1555 1555 2.50
LINK MG MG I 301 O HOH I 411 1555 1555 2.54
LINK O ALA K 165 MG MG K 301 1555 1555 2.36
LINK O ASP K 168 MG MG K 301 1555 1555 2.39
LINK O SER K 171 MG MG K 301 1555 1555 2.91
LINK MG MG K 301 O ASP W 204 1555 1555 2.40
LINK OXT ASP L 222 MG MG V 301 1555 1555 2.21
LINK O ILE N 163 MG MG N 201 1555 1555 2.74
LINK O SER N 169 MG MG N 201 1555 1555 2.72
LINK O ILE V 163 MG MG V 301 1555 1555 2.24
LINK O ASP V 166 MG MG V 301 1555 1555 2.39
LINK O ASP W 177 MG MG W 301 1555 1555 2.32
LINK O SER W 180 MG MG W 301 1555 1555 2.72
LINK MG MG W 301 O HOH W 417 1555 1555 2.67
LINK O ALA Y 165 MG MG Y 301 1555 1555 2.51
LINK O ASP Y 168 MG MG Y 301 1555 1555 2.31
LINK O SER Y 171 MG MG Y 301 1555 1555 2.96
LINK O THR Z 192 MG MG Z 301 1555 1555 2.97
LINK O HIS Z 195 MG MG Z 301 1555 1555 2.88
LINK O VAL Z 198 MG MG Z 301 1555 1555 2.68
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 5 THR H 1 GLY H 47 GLY H 128 SER H 129
SITE 2 AC3 5 HOH H 404
SITE 1 AC4 5 ALA I 174 ASP I 177 SER I 180 ASP I 204
SITE 2 AC4 5 HOH I 411
SITE 1 AC5 4 ALA K 165 ASP K 168 SER K 171 ASP W 204
SITE 1 AC6 4 ILE N 163 ASP N 166 SER N 169 LEU a 34
SITE 1 AC7 3 ARG U 111 ASN U 114 TYR V 69
SITE 1 AC8 5 ASP L 222 ILE V 163 TRP V 164 ASP V 166
SITE 2 AC8 5 SER V 169
SITE 1 AC9 6 THR V 1 ALA V 46 GLY V 47 GLY V 128
SITE 2 AC9 6 SER V 129 HOH V 412
SITE 1 AD1 5 ALA W 174 ASP W 177 SER W 180 ASP W 204
SITE 2 AD1 5 HOH W 417
SITE 1 AD2 5 ASP I 204 ALA Y 165 ASP Y 168 ALA Y 169
SITE 2 AD2 5 SER Y 171
SITE 1 AD3 6 ARG Z 28 THR Z 192 HIS Z 195 ILE Z 196
SITE 2 AD3 6 VAL Z 198 ASP Z 222
CRYST1 135.420 301.170 144.610 90.00 113.03 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 0.007384 0.000000 0.003138 0.00000
SCALE2 0.000000 0.003320 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007514 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 -0.999610 -0.002248 0.027837 67.50897 1
MTRIX2 2 -0.002496 -0.985574 -0.169229 -289.76889 1
MTRIX3 2 0.027815 -0.169232 0.985184 -25.43170 1
(ATOM LINES ARE NOT SHOWN.)
END
