HEADER HYDROLASE/HYDROLASE INHIBITOR 20-DEC-15 5FGA
TITLE YEAST 20S PROTEASOME BETA5-K33A MUTANT (PROPEPTIDE EXPRESSED IN TRANS)
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 MOL_ID: 9;
COMPND 51 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-3;
COMPND 52 CHAIN: I, W;
COMPND 53 SYNONYM: MACROPAIN SUBUNIT PUP3,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 54 SUBUNIT PUP3,PROTEASOME COMPONENT PUP3;
COMPND 55 EC: 3.4.25.1;
COMPND 56 MOL_ID: 10;
COMPND 57 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-4;
COMPND 58 CHAIN: J, X;
COMPND 59 SYNONYM: MACROPAIN SUBUNIT C11,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 60 SUBUNIT C11,PROTEASOME COMPONENT C11,PROTEINASE YSCE SUBUNIT 11;
COMPND 61 EC: 3.4.25.1;
COMPND 62 MOL_ID: 11;
COMPND 63 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-5;
COMPND 64 CHAIN: K, Y;
COMPND 65 SYNONYM: MACROPAIN SUBUNIT PRE2,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 66 SUBUNIT PRE2,PROTEASOME COMPONENT PRE2,PROTEINASE YSCE SUBUNIT PRE2;
COMPND 67 EC: 3.4.25.1;
COMPND 68 ENGINEERED: YES;
COMPND 69 MOL_ID: 12;
COMPND 70 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-6;
COMPND 71 CHAIN: L, Z;
COMPND 72 SYNONYM: MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C5,PROTEASOME
COMPND 73 COMPONENT C5;
COMPND 74 EC: 3.4.25.1;
COMPND 75 MOL_ID: 13;
COMPND 76 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-7;
COMPND 77 CHAIN: M, a;
COMPND 78 SYNONYM: MACROPAIN SUBUNIT PRE4,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 79 SUBUNIT PRE4,PROTEASOME COMPONENT PRE4,PROTEINASE YSCE SUBUNIT PRE4;
COMPND 80 EC: 3.4.25.1;
COMPND 81 MOL_ID: 14;
COMPND 82 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-1;
COMPND 83 CHAIN: N, b;
COMPND 84 SYNONYM: MACROPAIN SUBUNIT PRE3,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 85 SUBUNIT PRE3,PROTEASOME COMPONENT PRE3,PROTEINASE YSCE SUBUNIT PRE3;
COMPND 86 EC: 3.4.25.1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE S288C;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 559292;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE S288C;
SOURCE 7 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 8 ORGANISM_TAXID: 559292;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE S288C;
SOURCE 11 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 12 ORGANISM_TAXID: 559292;
SOURCE 13 MOL_ID: 4;
SOURCE 14 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE S288C;
SOURCE 15 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 16 ORGANISM_TAXID: 559292;
SOURCE 17 MOL_ID: 5;
SOURCE 18 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE S288C;
SOURCE 19 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 20 ORGANISM_TAXID: 559292;
SOURCE 21 MOL_ID: 6;
SOURCE 22 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE S288C;
SOURCE 23 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 24 ORGANISM_TAXID: 559292;
SOURCE 25 MOL_ID: 7;
SOURCE 26 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE S288C;
SOURCE 27 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 28 ORGANISM_TAXID: 559292;
SOURCE 29 MOL_ID: 8;
SOURCE 30 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE S288C;
SOURCE 31 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 32 ORGANISM_TAXID: 559292;
SOURCE 33 MOL_ID: 9;
SOURCE 34 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE S288C;
SOURCE 35 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 36 ORGANISM_TAXID: 559292;
SOURCE 37 MOL_ID: 10;
SOURCE 38 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE S288C;
SOURCE 39 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 40 ORGANISM_TAXID: 559292;
SOURCE 41 MOL_ID: 11;
SOURCE 42 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE S288C;
SOURCE 43 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 44 ORGANISM_TAXID: 559292;
SOURCE 45 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE S288C;
SOURCE 46 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 47 EXPRESSION_SYSTEM_TAXID: 559292;
SOURCE 48 MOL_ID: 12;
SOURCE 49 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE S288C;
SOURCE 50 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 51 ORGANISM_TAXID: 559292;
SOURCE 52 MOL_ID: 13;
SOURCE 53 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE S288C;
SOURCE 54 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 55 ORGANISM_TAXID: 559292;
SOURCE 56 MOL_ID: 14;
SOURCE 57 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE S288C;
SOURCE 58 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 59 ORGANISM_TAXID: 559292
KEYWDS HYDROLASE COMPLEX, PROTEASOME, MUTANT, BINDING ANALYSIS, HYDROLASE-
KEYWDS 2 HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR E.M.HUBER,M.GROLL
REVDAT 3 10-JAN-24 5FGA 1 LINK
REVDAT 2 24-OCT-18 5FGA 1 COMPND SOURCE
REVDAT 1 23-MAR-16 5FGA 0
JRNL AUTH E.M.HUBER,W.HEINEMEYER,X.LI,C.S.ARENDT,M.HOCHSTRASSER,
JRNL AUTH 2 M.GROLL
JRNL TITL A UNIFIED MECHANISM FOR PROTEOLYSIS AND AUTOCATALYTIC
JRNL TITL 2 ACTIVATION IN THE 20S PROTEASOME.
JRNL REF NAT COMMUN V. 7 10900 2016
JRNL REFN ESSN 2041-1723
JRNL PMID 26964885
JRNL DOI 10.1038/NCOMMS10900
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 271226
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) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 14276
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) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 19300
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.93
REMARK 3 BIN R VALUE (WORKING SET) : 0.2910
REMARK 3 BIN FREE R VALUE SET COUNT : 1016
REMARK 3 BIN FREE R VALUE : 0.3170
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 49349
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 512
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 63.04
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.77000
REMARK 3 B22 (A**2) : -6.40000
REMARK 3 B33 (A**2) : 1.74000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.75000
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): 0.253
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.207
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 23.882
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 50257 ; 0.005 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 48025 ; 0.006 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 67989 ; 0.900 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES):110589 ; 0.742 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 6313 ; 5.088 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 2252 ;34.492 ;24.423
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 8748 ;14.502 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 284 ;14.234 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 7660 ; 0.049 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 57097 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 11267 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 25342 ; 2.221 ; 5.558
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 25341 ; 2.221 ; 5.557
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 31625 ; 2.960 ; 8.323
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 31626 ; 2.960 ; 8.324
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 24915 ; 2.267 ; 5.942
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 24915 ; 2.267 ; 5.942
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 36364 ; 2.820 ; 8.766
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 54393 ; 3.531 ;43.402
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 54332 ; 3.509 ;43.400
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 98282 ; 1.359 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 278 ;32.393 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 97628 ;15.377 ; 5.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 14
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A O
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 300 1
REMARK 3 1 O 1 O 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 3099 ; 0.080 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 A (A): 3189 ; 0.000 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 A (A): 3439 ; 0.000 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 A (A): 3598 ; 0.000 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 A (A): 2949 ; 0.000 ; 0.050
REMARK 3 TIGHT THERMAL 1 A (A**2): 3795 ; 6.830 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : B P
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 1 B 300 1
REMARK 3 1 P 1 P 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 2 B (A**2): 3756 ; 4.470 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : C Q
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C 1 C 300 1
REMARK 3 1 Q 1 Q 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 3 C (A**2): 3729 ; 9.450 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : D R
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 D 1 D 300 1
REMARK 3 1 R 1 R 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 4 D (A**2): 3578 ; 5.870 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 5
REMARK 3 CHAIN NAMES : E S
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 E 1 E 300 1
REMARK 3 1 S 1 S 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 5 E (A**2): 3509 ; 5.920 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 6
REMARK 3 CHAIN NAMES : F T
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 F 1 F 300 1
REMARK 3 1 T 1 T 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 6 F (A**2): 3749 ; 6.740 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 7
REMARK 3 CHAIN NAMES : G U
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 G 1 G 300 1
REMARK 3 1 U 1 U 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 7 G (A**2): 3770 ; 4.470 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 8
REMARK 3 CHAIN NAMES : H V
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 H 1 H 300 1
REMARK 3 1 V 1 V 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 8 H (A**2): 3403 ; 4.110 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 9
REMARK 3 CHAIN NAMES : I W
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 I 1 I 300 1
REMARK 3 1 W 1 W 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 9 I (A**2): 3119 ; 3.110 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 10
REMARK 3 CHAIN NAMES : J X
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 J 1 J 300 1
REMARK 3 1 X 1 X 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 10 J (A**2): 3099 ; 4.100 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 11
REMARK 3 CHAIN NAMES : K Y
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 K 1 K 300 1
REMARK 3 1 Y 1 Y 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 11 K (A**2): 3189 ; 3.200 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 12
REMARK 3 CHAIN NAMES : L Z
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 L 1 L 300 1
REMARK 3 1 Z 1 Z 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 12 L (A**2): 3439 ; 3.170 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 13
REMARK 3 CHAIN NAMES : M a
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 M 1 M 300 1
REMARK 3 1 a 1 a 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 13 M (A**2): 3598 ; 3.370 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 14
REMARK 3 CHAIN NAMES : N b
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 N 1 N 300 1
REMARK 3 1 b 1 b 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 14 N (A**2): 2949 ; 2.710 ; 0.500
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 28
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 250
REMARK 3 ORIGIN FOR THE GROUP (A): 66.3216 -91.8267 45.7087
REMARK 3 T TENSOR
REMARK 3 T11: 0.0632 T22: 0.0678
REMARK 3 T33: 0.0870 T12: -0.0085
REMARK 3 T13: 0.0099 T23: -0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 0.0312 L22: 0.0429
REMARK 3 L33: 0.0101 L12: -0.0233
REMARK 3 L13: 0.0077 L23: -0.0165
REMARK 3 S TENSOR
REMARK 3 S11: -0.0009 S12: 0.0072 S13: -0.0024
REMARK 3 S21: -0.0006 S22: 0.0010 S23: -0.0064
REMARK 3 S31: -0.0139 S32: -0.0047 S33: -0.0001
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): 58.9427 -87.6234 16.1311
REMARK 3 T TENSOR
REMARK 3 T11: 0.0747 T22: 0.0679
REMARK 3 T33: 0.0801 T12: -0.0016
REMARK 3 T13: 0.0187 T23: 0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 0.0379 L22: 0.0110
REMARK 3 L33: 0.0324 L12: 0.0191
REMARK 3 L13: 0.0331 L23: 0.0171
REMARK 3 S TENSOR
REMARK 3 S11: -0.0135 S12: -0.0013 S13: -0.0013
REMARK 3 S21: -0.0162 S22: 0.0036 S23: -0.0020
REMARK 3 S31: -0.0104 S32: 0.0114 S33: 0.0099
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): 31.7893 -87.2157 0.9470
REMARK 3 T TENSOR
REMARK 3 T11: 0.0907 T22: 0.0670
REMARK 3 T33: 0.0739 T12: 0.0012
REMARK 3 T13: 0.0033 T23: 0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 0.0192 L22: 0.0591
REMARK 3 L33: 0.0402 L12: 0.0325
REMARK 3 L13: -0.0272 L23: -0.0478
REMARK 3 S TENSOR
REMARK 3 S11: 0.0002 S12: -0.0073 S13: 0.0023
REMARK 3 S21: -0.0087 S22: 0.0031 S23: 0.0164
REMARK 3 S31: 0.0144 S32: 0.0057 S33: -0.0034
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): 2.6667 -90.1766 13.5182
REMARK 3 T TENSOR
REMARK 3 T11: 0.0702 T22: 0.0617
REMARK 3 T33: 0.0958 T12: 0.0077
REMARK 3 T13: -0.0077 T23: 0.0111
REMARK 3 L TENSOR
REMARK 3 L11: 0.0077 L22: 0.0288
REMARK 3 L33: 0.0158 L12: -0.0139
REMARK 3 L13: -0.0104 L23: 0.0177
REMARK 3 S TENSOR
REMARK 3 S11: -0.0009 S12: -0.0056 S13: -0.0062
REMARK 3 S21: -0.0126 S22: 0.0040 S23: 0.0283
REMARK 3 S31: -0.0111 S32: 0.0129 S33: -0.0032
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): -3.5749 -94.6242 45.5135
REMARK 3 T TENSOR
REMARK 3 T11: 0.0200 T22: 0.0625
REMARK 3 T33: 0.0966 T12: 0.0126
REMARK 3 T13: 0.0179 T23: -0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 0.0480 L22: 0.0293
REMARK 3 L33: 0.0378 L12: 0.0170
REMARK 3 L13: 0.0269 L23: -0.0084
REMARK 3 S TENSOR
REMARK 3 S11: -0.0099 S12: -0.0041 S13: 0.0108
REMARK 3 S21: -0.0053 S22: 0.0100 S23: 0.0346
REMARK 3 S31: 0.0080 S32: -0.0038 S33: -0.0001
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): 14.8716 -95.1368 69.5734
REMARK 3 T TENSOR
REMARK 3 T11: 0.0725 T22: 0.0641
REMARK 3 T33: 0.0788 T12: 0.0046
REMARK 3 T13: 0.0210 T23: -0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 0.0002 L22: 0.0048
REMARK 3 L33: 0.0020 L12: -0.0002
REMARK 3 L13: 0.0002 L23: -0.0024
REMARK 3 S TENSOR
REMARK 3 S11: -0.0015 S12: -0.0031 S13: 0.0011
REMARK 3 S21: 0.0142 S22: -0.0076 S23: -0.0007
REMARK 3 S31: -0.0047 S32: 0.0032 S33: 0.0091
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): 47.1761 -93.3160 70.7529
REMARK 3 T TENSOR
REMARK 3 T11: 0.0853 T22: 0.0493
REMARK 3 T33: 0.0733 T12: 0.0014
REMARK 3 T13: 0.0092 T23: -0.0083
REMARK 3 L TENSOR
REMARK 3 L11: 0.0105 L22: 0.0079
REMARK 3 L33: 0.0568 L12: -0.0008
REMARK 3 L13: 0.0126 L23: 0.0008
REMARK 3 S TENSOR
REMARK 3 S11: 0.0033 S12: 0.0174 S13: 0.0028
REMARK 3 S21: 0.0188 S22: -0.0086 S23: -0.0126
REMARK 3 S31: 0.0046 S32: -0.0060 S33: 0.0052
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): 67.4965-129.0992 47.1855
REMARK 3 T TENSOR
REMARK 3 T11: 0.0662 T22: 0.0609
REMARK 3 T33: 0.0872 T12: -0.0042
REMARK 3 T13: 0.0059 T23: -0.0047
REMARK 3 L TENSOR
REMARK 3 L11: 0.0007 L22: 0.0278
REMARK 3 L33: 0.0095 L12: -0.0006
REMARK 3 L13: -0.0006 L23: 0.0141
REMARK 3 S TENSOR
REMARK 3 S11: 0.0050 S12: 0.0062 S13: 0.0015
REMARK 3 S21: 0.0184 S22: 0.0044 S23: -0.0264
REMARK 3 S31: -0.0009 S32: -0.0032 S33: -0.0094
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): 68.0045-126.8971 20.6917
REMARK 3 T TENSOR
REMARK 3 T11: 0.0737 T22: 0.0667
REMARK 3 T33: 0.0864 T12: -0.0033
REMARK 3 T13: 0.0351 T23: -0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 0.0664 L22: 0.1307
REMARK 3 L33: 0.0038 L12: -0.0879
REMARK 3 L13: -0.0133 L23: 0.0188
REMARK 3 S TENSOR
REMARK 3 S11: 0.0145 S12: -0.0023 S13: -0.0130
REMARK 3 S21: -0.0212 S22: -0.0065 S23: -0.0105
REMARK 3 S31: -0.0116 S32: 0.0002 S33: -0.0080
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): 44.4756-126.3881 -0.8907
REMARK 3 T TENSOR
REMARK 3 T11: 0.0984 T22: 0.0633
REMARK 3 T33: 0.0682 T12: -0.0008
REMARK 3 T13: 0.0136 T23: 0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 0.0449 L22: 0.1378
REMARK 3 L33: 0.0266 L12: 0.0386
REMARK 3 L13: 0.0269 L23: 0.0486
REMARK 3 S TENSOR
REMARK 3 S11: 0.0105 S12: -0.0087 S13: 0.0022
REMARK 3 S21: -0.0259 S22: 0.0042 S23: 0.0074
REMARK 3 S31: 0.0034 S32: 0.0046 S33: -0.0147
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): 10.9065-130.8881 2.3355
REMARK 3 T TENSOR
REMARK 3 T11: 0.0723 T22: 0.0649
REMARK 3 T33: 0.0897 T12: 0.0033
REMARK 3 T13: -0.0025 T23: 0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 0.0493 L22: 0.1981
REMARK 3 L33: 0.1035 L12: 0.0957
REMARK 3 L13: 0.0088 L23: 0.0383
REMARK 3 S TENSOR
REMARK 3 S11: -0.0145 S12: -0.0040 S13: 0.0120
REMARK 3 S21: -0.0516 S22: 0.0086 S23: 0.0430
REMARK 3 S31: -0.0059 S32: -0.0038 S33: 0.0059
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): -4.4157-134.6216 28.2088
REMARK 3 T TENSOR
REMARK 3 T11: 0.0311 T22: 0.0701
REMARK 3 T33: 0.0959 T12: -0.0031
REMARK 3 T13: 0.0281 T23: 0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 0.0423 L22: 0.1601
REMARK 3 L33: 0.0426 L12: -0.0702
REMARK 3 L13: 0.0343 L23: -0.0522
REMARK 3 S TENSOR
REMARK 3 S11: 0.0156 S12: -0.0050 S13: -0.0059
REMARK 3 S21: 0.0045 S22: -0.0055 S23: 0.0533
REMARK 3 S31: 0.0006 S32: 0.0026 S33: -0.0101
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): 7.7589-138.0125 60.0510
REMARK 3 T TENSOR
REMARK 3 T11: 0.0558 T22: 0.0727
REMARK 3 T33: 0.0664 T12: -0.0024
REMARK 3 T13: 0.0240 T23: -0.0054
REMARK 3 L TENSOR
REMARK 3 L11: 0.1152 L22: 0.2076
REMARK 3 L33: 0.0368 L12: -0.0242
REMARK 3 L13: 0.0593 L23: -0.0442
REMARK 3 S TENSOR
REMARK 3 S11: 0.0063 S12: 0.0059 S13: 0.0136
REMARK 3 S21: 0.0316 S22: -0.0012 S23: 0.0137
REMARK 3 S31: 0.0034 S32: -0.0007 S33: -0.0051
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): 39.6646-133.8974 70.4876
REMARK 3 T TENSOR
REMARK 3 T11: 0.0826 T22: 0.0632
REMARK 3 T33: 0.0657 T12: 0.0004
REMARK 3 T13: 0.0172 T23: -0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 0.0421 L22: 0.1122
REMARK 3 L33: 0.0337 L12: 0.0018
REMARK 3 L13: -0.0272 L23: -0.0432
REMARK 3 S TENSOR
REMARK 3 S11: 0.0004 S12: 0.0082 S13: 0.0064
REMARK 3 S21: 0.0248 S22: -0.0017 S23: -0.0068
REMARK 3 S31: -0.0039 S32: -0.0023 S33: 0.0012
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): 2.5401-206.7053 36.7250
REMARK 3 T TENSOR
REMARK 3 T11: 0.0565 T22: 0.0617
REMARK 3 T33: 0.0937 T12: -0.0110
REMARK 3 T13: 0.0015 T23: 0.0073
REMARK 3 L TENSOR
REMARK 3 L11: 0.0187 L22: 0.0058
REMARK 3 L33: 0.0341 L12: -0.0086
REMARK 3 L13: -0.0225 L23: 0.0115
REMARK 3 S TENSOR
REMARK 3 S11: -0.0163 S12: 0.0038 S13: 0.0017
REMARK 3 S21: 0.0030 S22: -0.0003 S23: 0.0102
REMARK 3 S31: 0.0287 S32: 0.0054 S33: 0.0166
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): 9.1641-205.7729 6.6931
REMARK 3 T TENSOR
REMARK 3 T11: 0.0867 T22: 0.0617
REMARK 3 T33: 0.0923 T12: -0.0014
REMARK 3 T13: -0.0160 T23: -0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 0.0288 L22: 0.0063
REMARK 3 L33: 0.0601 L12: -0.0078
REMARK 3 L13: 0.0121 L23: -0.0170
REMARK 3 S TENSOR
REMARK 3 S11: -0.0114 S12: -0.0038 S13: -0.0004
REMARK 3 S21: -0.0023 S22: 0.0091 S23: 0.0010
REMARK 3 S31: -0.0048 S32: -0.0116 S33: 0.0023
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 230
REMARK 3 ORIGIN FOR THE GROUP (A): 36.2287-203.7571 -9.0262
REMARK 3 T TENSOR
REMARK 3 T11: 0.0872 T22: 0.0509
REMARK 3 T33: 0.0715 T12: 0.0143
REMARK 3 T13: -0.0041 T23: -0.0042
REMARK 3 L TENSOR
REMARK 3 L11: 0.0056 L22: 0.0077
REMARK 3 L33: 0.0637 L12: 0.0034
REMARK 3 L13: 0.0100 L23: 0.0186
REMARK 3 S TENSOR
REMARK 3 S11: 0.0151 S12: -0.0148 S13: -0.0049
REMARK 3 S21: -0.0128 S22: 0.0040 S23: -0.0087
REMARK 3 S31: 0.0023 S32: -0.0114 S33: -0.0191
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): 65.5598-202.9391 3.3860
REMARK 3 T TENSOR
REMARK 3 T11: 0.0666 T22: 0.0601
REMARK 3 T33: 0.0816 T12: 0.0223
REMARK 3 T13: 0.0269 T23: -0.0108
REMARK 3 L TENSOR
REMARK 3 L11: 0.0016 L22: 0.0347
REMARK 3 L33: 0.0277 L12: -0.0059
REMARK 3 L13: 0.0021 L23: -0.0213
REMARK 3 S TENSOR
REMARK 3 S11: 0.0027 S12: -0.0010 S13: 0.0111
REMARK 3 S21: -0.0448 S22: -0.0080 S23: -0.0348
REMARK 3 S31: 0.0285 S32: -0.0163 S33: 0.0053
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): 72.4647-203.8221 35.4408
REMARK 3 T TENSOR
REMARK 3 T11: 0.0291 T22: 0.0437
REMARK 3 T33: 0.0767 T12: 0.0345
REMARK 3 T13: 0.0042 T23: -0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 0.0005 L22: 0.0021
REMARK 3 L33: 0.0050 L12: 0.0009
REMARK 3 L13: 0.0014 L23: 0.0032
REMARK 3 S TENSOR
REMARK 3 S11: 0.0055 S12: -0.0017 S13: -0.0048
REMARK 3 S21: -0.0030 S22: 0.0051 S23: -0.0120
REMARK 3 S31: -0.0061 S32: -0.0051 S33: -0.0106
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): 54.4603-207.4213 59.6054
REMARK 3 T TENSOR
REMARK 3 T11: 0.0779 T22: 0.0389
REMARK 3 T33: 0.0803 T12: 0.0141
REMARK 3 T13: -0.0168 T23: 0.0099
REMARK 3 L TENSOR
REMARK 3 L11: 0.0014 L22: 0.0040
REMARK 3 L33: 0.0070 L12: 0.0015
REMARK 3 L13: -0.0000 L23: -0.0040
REMARK 3 S TENSOR
REMARK 3 S11: -0.0019 S12: -0.0051 S13: -0.0034
REMARK 3 S21: 0.0116 S22: -0.0090 S23: -0.0145
REMARK 3 S31: -0.0107 S32: -0.0070 S33: 0.0109
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): 22.2325-209.6319 61.0804
REMARK 3 T TENSOR
REMARK 3 T11: 0.0939 T22: 0.0506
REMARK 3 T33: 0.0702 T12: -0.0059
REMARK 3 T13: -0.0017 T23: 0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 0.0342 L22: 0.0747
REMARK 3 L33: 0.0394 L12: -0.0463
REMARK 3 L13: 0.0078 L23: -0.0257
REMARK 3 S TENSOR
REMARK 3 S11: -0.0029 S12: 0.0018 S13: 0.0072
REMARK 3 S21: 0.0053 S22: 0.0068 S23: 0.0085
REMARK 3 S31: 0.0199 S32: 0.0151 S33: -0.0039
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): 1.5259-170.2234 44.4681
REMARK 3 T TENSOR
REMARK 3 T11: 0.0638 T22: 0.0596
REMARK 3 T33: 0.0942 T12: -0.0086
REMARK 3 T13: 0.0114 T23: 0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0074
REMARK 3 L33: 0.0015 L12: -0.0003
REMARK 3 L13: -0.0001 L23: 0.0015
REMARK 3 S TENSOR
REMARK 3 S11: 0.0008 S12: -0.0008 S13: -0.0008
REMARK 3 S21: 0.0151 S22: -0.0013 S23: 0.0212
REMARK 3 S31: 0.0092 S32: 0.0009 S33: 0.0005
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): 0.4938-167.9450 17.9514
REMARK 3 T TENSOR
REMARK 3 T11: 0.0685 T22: 0.0630
REMARK 3 T33: 0.0932 T12: -0.0081
REMARK 3 T13: -0.0001 T23: 0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 0.0060 L22: 0.1103
REMARK 3 L33: 0.0025 L12: -0.0080
REMARK 3 L13: -0.0019 L23: -0.0034
REMARK 3 S TENSOR
REMARK 3 S11: 0.0133 S12: 0.0062 S13: 0.0055
REMARK 3 S21: -0.0200 S22: -0.0145 S23: 0.0219
REMARK 3 S31: 0.0000 S32: 0.0030 S33: 0.0012
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): 23.5333-164.7279 -3.9216
REMARK 3 T TENSOR
REMARK 3 T11: 0.1153 T22: 0.0660
REMARK 3 T33: 0.0846 T12: 0.0013
REMARK 3 T13: -0.0206 T23: -0.0164
REMARK 3 L TENSOR
REMARK 3 L11: 0.3119 L22: 0.0463
REMARK 3 L33: 0.1089 L12: -0.0231
REMARK 3 L13: -0.0889 L23: -0.0544
REMARK 3 S TENSOR
REMARK 3 S11: 0.0366 S12: -0.0400 S13: 0.0815
REMARK 3 S21: 0.0324 S22: 0.0011 S23: 0.0017
REMARK 3 S31: -0.0614 S32: 0.0131 S33: -0.0376
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): 57.1702-160.8595 -0.7113
REMARK 3 T TENSOR
REMARK 3 T11: 0.0791 T22: 0.0707
REMARK 3 T33: 0.0807 T12: 0.0073
REMARK 3 T13: 0.0366 T23: -0.0111
REMARK 3 L TENSOR
REMARK 3 L11: 0.0328 L22: 0.1450
REMARK 3 L33: 0.0666 L12: 0.0380
REMARK 3 L13: 0.0110 L23: -0.0625
REMARK 3 S TENSOR
REMARK 3 S11: 0.0121 S12: 0.0032 S13: -0.0075
REMARK 3 S21: -0.0190 S22: 0.0085 S23: -0.0091
REMARK 3 S31: 0.0127 S32: 0.0103 S33: -0.0206
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): 73.0291-161.5109 25.0711
REMARK 3 T TENSOR
REMARK 3 T11: 0.0562 T22: 0.0738
REMARK 3 T33: 0.0875 T12: 0.0058
REMARK 3 T13: 0.0242 T23: -0.0135
REMARK 3 L TENSOR
REMARK 3 L11: 0.0516 L22: 0.1619
REMARK 3 L33: 0.0293 L12: -0.0401
REMARK 3 L13: -0.0339 L23: 0.0130
REMARK 3 S TENSOR
REMARK 3 S11: 0.0051 S12: -0.0091 S13: -0.0025
REMARK 3 S21: 0.0057 S22: -0.0005 S23: -0.0369
REMARK 3 S31: 0.0038 S32: 0.0039 S33: -0.0046
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): 61.5889-163.7590 57.2000
REMARK 3 T TENSOR
REMARK 3 T11: 0.0677 T22: 0.0563
REMARK 3 T33: 0.0825 T12: 0.0091
REMARK 3 T13: 0.0012 T23: -0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 0.0093 L22: 0.1582
REMARK 3 L33: 0.0031 L12: -0.0282
REMARK 3 L13: 0.0010 L23: 0.0001
REMARK 3 S TENSOR
REMARK 3 S11: 0.0094 S12: 0.0088 S13: -0.0103
REMARK 3 S21: 0.0105 S22: -0.0052 S23: -0.0142
REMARK 3 S31: 0.0076 S32: -0.0089 S33: -0.0042
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): 29.8524-169.4004 67.6311
REMARK 3 T TENSOR
REMARK 3 T11: 0.0824 T22: 0.0617
REMARK 3 T33: 0.0677 T12: -0.0004
REMARK 3 T13: 0.0177 T23: 0.0061
REMARK 3 L TENSOR
REMARK 3 L11: 0.0030 L22: 0.2086
REMARK 3 L33: 0.0085 L12: -0.0146
REMARK 3 L13: -0.0017 L23: 0.0395
REMARK 3 S TENSOR
REMARK 3 S11: 0.0089 S12: 0.0008 S13: -0.0039
REMARK 3 S21: 0.0201 S22: -0.0025 S23: 0.0048
REMARK 3 S31: 0.0066 S32: -0.0001 S33: -0.0063
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 5FGA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-DEC-15.
REMARK 100 THE DEPOSITION ID IS D_1000216541.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-DEC-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : LN2 COOLED FIXED-EXIT. SI(111)
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 285503
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.09700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.51400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: 1RYP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 MM MGAC2, 13% MPD, 0.1 M MES, PH
REMARK 280 6.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 150.25000
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 465 ILE a 233
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 CG MET J 1 N ASP J 2 1.09
REMARK 500 CG MET X 1 N ASP X 2 1.64
REMARK 500 NE2 GLN M 2 O HOH M 301 1.88
REMARK 500 OG1 THR K 1 O HOH K 401 1.91
REMARK 500 OG1 THR Y 1 O HOH Y 401 2.06
REMARK 500 O THR H 52 OG1 THR H 56 2.12
REMARK 500 O THR V 52 OG1 THR V 56 2.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 MET J 1 SD MET J 1 CE 0.477
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 MET J 1 CB - CA - C ANGL. DEV. = -25.4 DEGREES
REMARK 500 MET J 1 CA - CB - CG ANGL. DEV. = -16.0 DEGREES
REMARK 500 MET J 1 CG - SD - CE ANGL. DEV. = 24.3 DEGREES
REMARK 500 MET J 1 N - CA - C ANGL. DEV. = 23.5 DEGREES
REMARK 500 MET X 1 CB - CA - C ANGL. DEV. = -30.2 DEGREES
REMARK 500 MET X 1 CA - CB - CG ANGL. DEV. = -13.9 DEGREES
REMARK 500 MET X 1 CG - SD - CE ANGL. DEV. = 22.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR A 2 141.28 58.07
REMARK 500 LYS A 50 91.83 -69.28
REMARK 500 TYR A 97 -64.55 -150.65
REMARK 500 ALA A 249 39.98 -90.93
REMARK 500 ARG B 8 76.78 57.14
REMARK 500 THR B 10 54.07 -116.61
REMARK 500 VAL B 51 95.34 -12.69
REMARK 500 ASN B 220 94.80 -51.22
REMARK 500 ASP B 221 -128.75 96.44
REMARK 500 GLN C 120 39.15 -140.99
REMARK 500 PRO C 183 105.71 -45.19
REMARK 500 GLN C 202 -102.78 114.73
REMARK 500 ALA C 205 -108.77 -81.97
REMARK 500 SER E 39 -155.19 -109.27
REMARK 500 ASP E 137 -158.63 -126.54
REMARK 500 ASP E 202 -46.43 68.15
REMARK 500 ASP F 67 -130.77 54.49
REMARK 500 LYS F 100 -56.20 72.17
REMARK 500 ASP F 138 -164.79 -126.91
REMARK 500 LYS G 165 41.13 -107.45
REMARK 500 SER H 171 -114.09 63.54
REMARK 500 GLN I 31 -109.69 57.95
REMARK 500 ASP I 134 -70.77 -85.85
REMARK 500 ASP I 192 31.13 -144.94
REMARK 500 GLN I 203 43.75 -109.17
REMARK 500 ASP J 2 -155.54 -166.17
REMARK 500 VAL J 9 -163.95 -101.56
REMARK 500 SER J 31 29.38 -145.40
REMARK 500 ASP K 147 37.31 -88.20
REMARK 500 ASP L 32 -114.75 54.80
REMARK 500 PHE L 103 69.06 -158.54
REMARK 500 ASP L 200 -65.26 70.17
REMARK 500 ILE M 5 -75.98 -109.10
REMARK 500 THR M 9 -153.84 -90.77
REMARK 500 ALA M 83 -114.58 -145.90
REMARK 500 LYS N 107 -146.76 65.77
REMARK 500 THR O 2 141.30 58.19
REMARK 500 LYS O 50 92.10 -69.02
REMARK 500 TYR O 97 -64.60 -150.56
REMARK 500 ALA O 249 40.07 -90.96
REMARK 500 ARG P 8 76.69 57.35
REMARK 500 THR P 10 54.05 -116.44
REMARK 500 VAL P 51 95.35 -12.60
REMARK 500 ASN P 220 94.78 -51.26
REMARK 500 ASP P 221 -128.96 96.40
REMARK 500 GLN Q 120 39.09 -141.09
REMARK 500 PRO Q 183 105.65 -45.12
REMARK 500 GLN Q 202 -102.53 114.80
REMARK 500 ALA Q 205 -108.70 -82.16
REMARK 500 SER S 39 -155.25 -109.27
REMARK 500
REMARK 500 THIS ENTRY HAS 72 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP J 2 ILE J 3 -140.42
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 MET J 1 -10.80
REMARK 500 MET X 1 -14.15
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 B 314 DISTANCE = 5.96 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 78.9
REMARK 620 3 ARG G 122 O 81.7 76.6
REMARK 620 4 MET G 125 O 159.2 81.4 87.3
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 75.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG I 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP I 204 O
REMARK 620 2 ALA Y 165 O 97.8
REMARK 620 3 ASP Y 168 O 153.9 90.9
REMARK 620 4 SER Y 171 O 85.8 70.5 74.0
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 94.8
REMARK 620 3 SER K 171 O 77.1 79.3
REMARK 620 4 ASP W 204 O 104.4 155.3 89.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG L 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP L 222 OXT
REMARK 620 2 ILE V 163 O 101.2
REMARK 620 3 ASP V 166 O 143.2 115.5
REMARK 620 4 SER V 169 O 90.8 96.8 81.8
REMARK 620 N 1 2 3
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 87.6
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 ALA W 174 O
REMARK 620 2 ASP W 177 O 68.0
REMARK 620 3 SER W 180 O 83.1 76.3
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 VAL Z 198 O 94.0
REMARK 620 N 1
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 MG I 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG I 302
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 L 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG N 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL U 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG W 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
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 5FGA A 1 250 UNP P23639 PSA2_YEAST 1 250
DBREF 5FGA B 0 257 UNP P23638 PSA3_YEAST 1 258
DBREF 5FGA C -1 252 UNP P40303 PSA4_YEAST 1 254
DBREF 5FGA D -7 252 UNP P32379 PSA5_YEAST 1 260
DBREF 5FGA E 0 233 UNP P40302 PSA6_YEAST 1 234
DBREF 5FGA F -3 284 UNP P21242 PSA7_YEAST 1 288
DBREF 5FGA G -8 243 UNP P21243 PSA1_YEAST 1 252
DBREF 5FGA H 1 232 UNP P25043 PSB2_YEAST 30 261
DBREF 5FGA I 0 204 UNP P25451 PSB3_YEAST 1 205
DBREF 5FGA J 1 198 UNP P22141 PSB4_YEAST 1 198
DBREF 5FGA K 1 212 UNP P30656 PSB5_YEAST 76 287
DBREF 5FGA L 1 222 UNP P23724 PSB6_YEAST 20 241
DBREF 5FGA M -12 233 UNP P30657 PSB7_YEAST 21 266
DBREF 5FGA N 1 196 UNP P38624 PSB1_YEAST 20 215
DBREF 5FGA O 1 250 UNP P23639 PSA2_YEAST 1 250
DBREF 5FGA P 0 257 UNP P23638 PSA3_YEAST 1 258
DBREF 5FGA Q -1 252 UNP P40303 PSA4_YEAST 1 254
DBREF 5FGA R -7 252 UNP P32379 PSA5_YEAST 1 260
DBREF 5FGA S 0 233 UNP P40302 PSA6_YEAST 1 234
DBREF 5FGA T -3 284 UNP P21242 PSA7_YEAST 1 288
DBREF 5FGA U -8 243 UNP P21243 PSA1_YEAST 1 252
DBREF 5FGA V 1 232 UNP P25043 PSB2_YEAST 30 261
DBREF 5FGA W 0 204 UNP P25451 PSB3_YEAST 1 205
DBREF 5FGA X 1 198 UNP P22141 PSB4_YEAST 1 198
DBREF 5FGA Y 1 212 UNP P30656 PSB5_YEAST 76 287
DBREF 5FGA Z 1 222 UNP P23724 PSB6_YEAST 20 241
DBREF 5FGA a -12 233 UNP P30657 PSB7_YEAST 21 266
DBREF 5FGA b 1 196 UNP P38624 PSB1_YEAST 20 215
SEQADV 5FGA ALA K 33 UNP P30656 LYS 108 ENGINEERED MUTATION
SEQADV 5FGA ALA Y 33 UNP P30656 LYS 108 ENGINEERED MUTATION
SEQRES 1 A 250 MET THR ASP ARG TYR SER PHE SER LEU THR THR PHE SER
SEQRES 2 A 250 PRO SER GLY LYS LEU GLY GLN ILE ASP TYR ALA LEU THR
SEQRES 3 A 250 ALA VAL LYS GLN GLY VAL THR SER LEU GLY ILE LYS ALA
SEQRES 4 A 250 THR ASN GLY VAL VAL ILE ALA THR GLU LYS LYS SER SER
SEQRES 5 A 250 SER PRO LEU ALA MET SER GLU THR LEU SER LYS VAL SER
SEQRES 6 A 250 LEU LEU THR PRO ASP ILE GLY ALA VAL TYR SER GLY MET
SEQRES 7 A 250 GLY PRO ASP TYR ARG VAL LEU VAL ASP LYS SER ARG LYS
SEQRES 8 A 250 VAL ALA HIS THR SER TYR LYS ARG ILE TYR GLY GLU TYR
SEQRES 9 A 250 PRO PRO THR LYS LEU LEU VAL SER GLU VAL ALA LYS ILE
SEQRES 10 A 250 MET GLN GLU ALA THR GLN SER GLY GLY VAL ARG PRO PHE
SEQRES 11 A 250 GLY VAL SER LEU LEU ILE ALA GLY HIS ASP GLU PHE ASN
SEQRES 12 A 250 GLY PHE SER LEU TYR GLN VAL ASP PRO SER GLY SER TYR
SEQRES 13 A 250 PHE PRO TRP LYS ALA THR ALA ILE GLY LYS GLY SER VAL
SEQRES 14 A 250 ALA ALA LYS THR PHE LEU GLU LYS ARG TRP ASN ASP GLU
SEQRES 15 A 250 LEU GLU LEU GLU ASP ALA ILE HIS ILE ALA LEU LEU THR
SEQRES 16 A 250 LEU LYS GLU SER VAL GLU GLY GLU PHE ASN GLY ASP THR
SEQRES 17 A 250 ILE GLU LEU ALA ILE ILE GLY ASP GLU ASN PRO ASP LEU
SEQRES 18 A 250 LEU GLY TYR THR GLY ILE PRO THR ASP LYS GLY PRO ARG
SEQRES 19 A 250 PHE ARG LYS LEU THR SER GLN GLU ILE ASN ASP ARG LEU
SEQRES 20 A 250 GLU ALA LEU
SEQRES 1 B 258 MET GLY SER ARG ARG TYR ASP SER ARG THR THR ILE PHE
SEQRES 2 B 258 SER PRO GLU GLY ARG LEU TYR GLN VAL GLU TYR ALA LEU
SEQRES 3 B 258 GLU SER ILE SER HIS ALA GLY THR ALA ILE GLY ILE MET
SEQRES 4 B 258 ALA SER ASP GLY ILE VAL LEU ALA ALA GLU ARG LYS VAL
SEQRES 5 B 258 THR SER THR LEU LEU GLU GLN ASP THR SER THR GLU LYS
SEQRES 6 B 258 LEU TYR LYS LEU ASN ASP LYS ILE ALA VAL ALA VAL ALA
SEQRES 7 B 258 GLY LEU THR ALA ASP ALA GLU ILE LEU ILE ASN THR ALA
SEQRES 8 B 258 ARG ILE HIS ALA GLN ASN TYR LEU LYS THR TYR ASN GLU
SEQRES 9 B 258 ASP ILE PRO VAL GLU ILE LEU VAL ARG ARG LEU SER ASP
SEQRES 10 B 258 ILE LYS GLN GLY TYR THR GLN HIS GLY GLY LEU ARG PRO
SEQRES 11 B 258 PHE GLY VAL SER PHE ILE TYR ALA GLY TYR ASP ASP ARG
SEQRES 12 B 258 TYR GLY TYR GLN LEU TYR THR SER ASN PRO SER GLY ASN
SEQRES 13 B 258 TYR THR GLY TRP LYS ALA ILE SER VAL GLY ALA ASN THR
SEQRES 14 B 258 SER ALA ALA GLN THR LEU LEU GLN MET ASP TYR LYS ASP
SEQRES 15 B 258 ASP MET LYS VAL ASP ASP ALA ILE GLU LEU ALA LEU LYS
SEQRES 16 B 258 THR LEU SER LYS THR THR ASP SER SER ALA LEU THR TYR
SEQRES 17 B 258 ASP ARG LEU GLU PHE ALA THR ILE ARG LYS GLY ALA ASN
SEQRES 18 B 258 ASP GLY GLU VAL TYR GLN LYS ILE PHE LYS PRO GLN GLU
SEQRES 19 B 258 ILE LYS ASP ILE LEU VAL LYS THR GLY ILE THR LYS LYS
SEQRES 20 B 258 ASP GLU ASP GLU GLU ALA ASP GLU ASP MET LYS
SEQRES 1 C 254 MET SER GLY TYR ASP ARG ALA LEU SER ILE PHE SER PRO
SEQRES 2 C 254 ASP GLY HIS ILE PHE GLN VAL GLU TYR ALA LEU GLU ALA
SEQRES 3 C 254 VAL LYS ARG GLY THR CYS ALA VAL GLY VAL LYS GLY LYS
SEQRES 4 C 254 ASN CYS VAL VAL LEU GLY CYS GLU ARG ARG SER THR LEU
SEQRES 5 C 254 LYS LEU GLN ASP THR ARG ILE THR PRO SER LYS VAL SER
SEQRES 6 C 254 LYS ILE ASP SER HIS VAL VAL LEU SER PHE SER GLY LEU
SEQRES 7 C 254 ASN ALA ASP SER ARG ILE LEU ILE GLU LYS ALA ARG VAL
SEQRES 8 C 254 GLU ALA GLN SER HIS ARG LEU THR LEU GLU ASP PRO VAL
SEQRES 9 C 254 THR VAL GLU TYR LEU THR ARG TYR VAL ALA GLY VAL GLN
SEQRES 10 C 254 GLN ARG TYR THR GLN SER GLY GLY VAL ARG PRO PHE GLY
SEQRES 11 C 254 VAL SER THR LEU ILE ALA GLY PHE ASP PRO ARG ASP ASP
SEQRES 12 C 254 GLU PRO LYS LEU TYR GLN THR GLU PRO SER GLY ILE TYR
SEQRES 13 C 254 SER SER TRP SER ALA GLN THR ILE GLY ARG ASN SER LYS
SEQRES 14 C 254 THR VAL ARG GLU PHE LEU GLU LYS ASN TYR ASP ARG LYS
SEQRES 15 C 254 GLU PRO PRO ALA THR VAL GLU GLU CYS VAL LYS LEU THR
SEQRES 16 C 254 VAL ARG SER LEU LEU GLU VAL VAL GLN THR GLY ALA LYS
SEQRES 17 C 254 ASN ILE GLU ILE THR VAL VAL LYS PRO ASP SER ASP ILE
SEQRES 18 C 254 VAL ALA LEU SER SER GLU GLU ILE ASN GLN TYR VAL THR
SEQRES 19 C 254 GLN ILE GLU GLN GLU LYS GLN GLU GLN GLN GLU GLN ASP
SEQRES 20 C 254 LYS LYS LYS LYS SER ASN HIS
SEQRES 1 D 260 MET PHE LEU THR ARG SER GLU TYR ASP ARG GLY VAL SER
SEQRES 2 D 260 THR PHE SER PRO GLU GLY ARG LEU PHE GLN VAL GLU TYR
SEQRES 3 D 260 SER LEU GLU ALA ILE LYS LEU GLY SER THR ALA ILE GLY
SEQRES 4 D 260 ILE ALA THR LYS GLU GLY VAL VAL LEU GLY VAL GLU LYS
SEQRES 5 D 260 ARG ALA THR SER PRO LEU LEU GLU SER ASP SER ILE GLU
SEQRES 6 D 260 LYS ILE VAL GLU ILE ASP ARG HIS ILE GLY CYS ALA MET
SEQRES 7 D 260 SER GLY LEU THR ALA ASP ALA ARG SER MET ILE GLU HIS
SEQRES 8 D 260 ALA ARG THR ALA ALA VAL THR HIS ASN LEU TYR TYR ASP
SEQRES 9 D 260 GLU ASP ILE ASN VAL GLU SER LEU THR GLN SER VAL CYS
SEQRES 10 D 260 ASP LEU ALA LEU ARG PHE GLY GLU GLY ALA SER GLY GLU
SEQRES 11 D 260 GLU ARG LEU MET SER ARG PRO PHE GLY VAL ALA LEU LEU
SEQRES 12 D 260 ILE ALA GLY HIS ASP ALA ASP ASP GLY TYR GLN LEU PHE
SEQRES 13 D 260 HIS ALA GLU PRO SER GLY THR PHE TYR ARG TYR ASN ALA
SEQRES 14 D 260 LYS ALA ILE GLY SER GLY SER GLU GLY ALA GLN ALA GLU
SEQRES 15 D 260 LEU LEU ASN GLU TRP HIS SER SER LEU THR LEU LYS GLU
SEQRES 16 D 260 ALA GLU LEU LEU VAL LEU LYS ILE LEU LYS GLN VAL MET
SEQRES 17 D 260 GLU GLU LYS LEU ASP GLU ASN ASN ALA GLN LEU SER CYS
SEQRES 18 D 260 ILE THR LYS GLN ASP GLY PHE LYS ILE TYR ASP ASN GLU
SEQRES 19 D 260 LYS THR ALA GLU LEU ILE LYS GLU LEU LYS GLU LYS GLU
SEQRES 20 D 260 ALA ALA GLU SER PRO GLU GLU ALA ASP VAL GLU MET SER
SEQRES 1 E 234 MET PHE ARG ASN ASN TYR ASP GLY ASP THR VAL THR PHE
SEQRES 2 E 234 SER PRO THR GLY ARG LEU PHE GLN VAL GLU TYR ALA LEU
SEQRES 3 E 234 GLU ALA ILE LYS GLN GLY SER VAL THR VAL GLY LEU ARG
SEQRES 4 E 234 SER ASN THR HIS ALA VAL LEU VAL ALA LEU LYS ARG ASN
SEQRES 5 E 234 ALA ASP GLU LEU SER SER TYR GLN LYS LYS ILE ILE LYS
SEQRES 6 E 234 CYS ASP GLU HIS MET GLY LEU SER LEU ALA GLY LEU ALA
SEQRES 7 E 234 PRO ASP ALA ARG VAL LEU SER ASN TYR LEU ARG GLN GLN
SEQRES 8 E 234 CYS ASN TYR SER SER LEU VAL PHE ASN ARG LYS LEU ALA
SEQRES 9 E 234 VAL GLU ARG ALA GLY HIS LEU LEU CYS ASP LYS ALA GLN
SEQRES 10 E 234 LYS ASN THR GLN SER TYR GLY GLY ARG PRO TYR GLY VAL
SEQRES 11 E 234 GLY LEU LEU ILE ILE GLY TYR ASP LYS SER GLY ALA HIS
SEQRES 12 E 234 LEU LEU GLU PHE GLN PRO SER GLY ASN VAL THR GLU LEU
SEQRES 13 E 234 TYR GLY THR ALA ILE GLY ALA ARG SER GLN GLY ALA LYS
SEQRES 14 E 234 THR TYR LEU GLU ARG THR LEU ASP THR PHE ILE LYS ILE
SEQRES 15 E 234 ASP GLY ASN PRO ASP GLU LEU ILE LYS ALA GLY VAL GLU
SEQRES 16 E 234 ALA ILE SER GLN SER LEU ARG ASP GLU SER LEU THR VAL
SEQRES 17 E 234 ASP ASN LEU SER ILE ALA ILE VAL GLY LYS ASP THR PRO
SEQRES 18 E 234 PHE THR ILE TYR ASP GLY GLU ALA VAL ALA LYS TYR ILE
SEQRES 1 F 288 MET THR SER ILE GLY THR GLY TYR ASP LEU SER ASN SER
SEQRES 2 F 288 VAL PHE SER PRO ASP GLY ARG ASN PHE GLN VAL GLU TYR
SEQRES 3 F 288 ALA VAL LYS ALA VAL GLU ASN GLY THR THR SER ILE GLY
SEQRES 4 F 288 ILE LYS CYS ASN ASP GLY VAL VAL PHE ALA VAL GLU LYS
SEQRES 5 F 288 LEU ILE THR SER LYS LEU LEU VAL PRO GLN LYS ASN VAL
SEQRES 6 F 288 LYS ILE GLN VAL VAL ASP ARG HIS ILE GLY CYS VAL TYR
SEQRES 7 F 288 SER GLY LEU ILE PRO ASP GLY ARG HIS LEU VAL ASN ARG
SEQRES 8 F 288 GLY ARG GLU GLU ALA ALA SER PHE LYS LYS LEU TYR LYS
SEQRES 9 F 288 THR PRO ILE PRO ILE PRO ALA PHE ALA ASP ARG LEU GLY
SEQRES 10 F 288 GLN TYR VAL GLN ALA HIS THR LEU TYR ASN SER VAL ARG
SEQRES 11 F 288 PRO PHE GLY VAL SER THR ILE PHE GLY GLY VAL ASP LYS
SEQRES 12 F 288 ASN GLY ALA HIS LEU TYR MET LEU GLU PRO SER GLY SER
SEQRES 13 F 288 TYR TRP GLY TYR LYS GLY ALA ALA THR GLY LYS GLY ARG
SEQRES 14 F 288 GLN SER ALA LYS ALA GLU LEU GLU LYS LEU VAL ASP HIS
SEQRES 15 F 288 HIS PRO GLU GLY LEU SER ALA ARG GLU ALA VAL LYS GLN
SEQRES 16 F 288 ALA ALA LYS ILE ILE TYR LEU ALA HIS GLU ASP ASN LYS
SEQRES 17 F 288 GLU LYS ASP PHE GLU LEU GLU ILE SER TRP CYS SER LEU
SEQRES 18 F 288 SER GLU THR ASN GLY LEU HIS LYS PHE VAL LYS GLY ASP
SEQRES 19 F 288 LEU LEU GLN GLU ALA ILE ASP PHE ALA GLN LYS GLU ILE
SEQRES 20 F 288 ASN GLY ASP ASP ASP GLU ASP GLU ASP ASP SER ASP ASN
SEQRES 21 F 288 VAL MET SER SER ASP ASP GLU ASN ALA PRO VAL ALA THR
SEQRES 22 F 288 ASN ALA ASN ALA THR THR ASP GLN GLU GLY ASP ILE HIS
SEQRES 23 F 288 LEU GLU
SEQRES 1 G 252 MET SER GLY ALA ALA ALA ALA SER ALA ALA GLY TYR ASP
SEQRES 2 G 252 ARG HIS ILE THR ILE PHE SER PRO GLU GLY ARG LEU TYR
SEQRES 3 G 252 GLN VAL GLU TYR ALA PHE LYS ALA THR ASN GLN THR ASN
SEQRES 4 G 252 ILE ASN SER LEU ALA VAL ARG GLY LYS ASP CYS THR VAL
SEQRES 5 G 252 VAL ILE SER GLN LYS LYS VAL PRO ASP LYS LEU LEU ASP
SEQRES 6 G 252 PRO THR THR VAL SER TYR ILE PHE CYS ILE SER ARG THR
SEQRES 7 G 252 ILE GLY MET VAL VAL ASN GLY PRO ILE PRO ASP ALA ARG
SEQRES 8 G 252 ASN ALA ALA LEU ARG ALA LYS ALA GLU ALA ALA GLU PHE
SEQRES 9 G 252 ARG TYR LYS TYR GLY TYR ASP MET PRO CYS ASP VAL LEU
SEQRES 10 G 252 ALA LYS ARG MET ALA ASN LEU SER GLN ILE TYR THR GLN
SEQRES 11 G 252 ARG ALA TYR MET ARG PRO LEU GLY VAL ILE LEU THR PHE
SEQRES 12 G 252 VAL SER VAL ASP GLU GLU LEU GLY PRO SER ILE TYR LYS
SEQRES 13 G 252 THR ASP PRO ALA GLY TYR TYR VAL GLY TYR LYS ALA THR
SEQRES 14 G 252 ALA THR GLY PRO LYS GLN GLN GLU ILE THR THR ASN LEU
SEQRES 15 G 252 GLU ASN HIS PHE LYS LYS SER LYS ILE ASP HIS ILE ASN
SEQRES 16 G 252 GLU GLU SER TRP GLU LYS VAL VAL GLU PHE ALA ILE THR
SEQRES 17 G 252 HIS MET ILE ASP ALA LEU GLY THR GLU PHE SER LYS ASN
SEQRES 18 G 252 ASP LEU GLU VAL GLY VAL ALA THR LYS ASP LYS PHE PHE
SEQRES 19 G 252 THR LEU SER ALA GLU ASN ILE GLU GLU ARG LEU VAL ALA
SEQRES 20 G 252 ILE ALA GLU GLN ASP
SEQRES 1 H 232 THR THR ILE VAL GLY VAL LYS PHE ASN ASN GLY VAL VAL
SEQRES 2 H 232 ILE ALA ALA ASP THR ARG SER THR GLN GLY PRO ILE VAL
SEQRES 3 H 232 ALA ASP LYS ASN CYS ALA LYS LEU HIS ARG ILE SER PRO
SEQRES 4 H 232 LYS ILE TRP CYS ALA GLY ALA GLY THR ALA ALA ASP THR
SEQRES 5 H 232 GLU ALA VAL THR GLN LEU ILE GLY SER ASN ILE GLU LEU
SEQRES 6 H 232 HIS SER LEU TYR THR SER ARG GLU PRO ARG VAL VAL SER
SEQRES 7 H 232 ALA LEU GLN MET LEU LYS GLN HIS LEU PHE LYS TYR GLN
SEQRES 8 H 232 GLY HIS ILE GLY ALA TYR LEU ILE VAL ALA GLY VAL ASP
SEQRES 9 H 232 PRO THR GLY SER HIS LEU PHE SER ILE HIS ALA HIS GLY
SEQRES 10 H 232 SER THR ASP VAL GLY TYR TYR LEU SER LEU GLY SER GLY
SEQRES 11 H 232 SER LEU ALA ALA MET ALA VAL LEU GLU SER HIS TRP LYS
SEQRES 12 H 232 GLN ASP LEU THR LYS GLU GLU ALA ILE LYS LEU ALA SER
SEQRES 13 H 232 ASP ALA ILE GLN ALA GLY ILE TRP ASN ASP LEU GLY SER
SEQRES 14 H 232 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 ALA VAL ILE GLU ILE ASN PRO
SEQRES 4 K 212 PHE LEU LEU GLY THR MET ALA GLY GLY ALA ALA ASP CYS
SEQRES 5 K 212 GLN PHE TRP GLU THR TRP LEU GLY SER GLN CYS ARG LEU
SEQRES 6 K 212 HIS GLU LEU ARG GLU LYS GLU ARG ILE SER VAL ALA ALA
SEQRES 7 K 212 ALA SER LYS ILE LEU SER ASN LEU VAL TYR GLN TYR LYS
SEQRES 8 K 212 GLY ALA GLY LEU SER MET GLY THR MET ILE CYS GLY TYR
SEQRES 9 K 212 THR ARG LYS GLU GLY PRO THR ILE TYR TYR VAL ASP SER
SEQRES 10 K 212 ASP GLY THR ARG LEU LYS GLY ASP ILE PHE CYS VAL GLY
SEQRES 11 K 212 SER GLY GLN THR PHE ALA TYR GLY VAL LEU ASP SER ASN
SEQRES 12 K 212 TYR LYS TRP ASP LEU SER VAL GLU ASP ALA LEU TYR LEU
SEQRES 13 K 212 GLY LYS ARG SER ILE LEU ALA ALA ALA HIS ARG ASP ALA
SEQRES 14 K 212 TYR SER GLY GLY SER VAL ASN LEU TYR HIS VAL THR GLU
SEQRES 15 K 212 ASP GLY TRP ILE TYR HIS GLY ASN HIS ASP VAL GLY GLU
SEQRES 16 K 212 LEU PHE TRP LYS VAL LYS GLU GLU GLU GLY SER PHE ASN
SEQRES 17 K 212 ASN VAL ILE GLY
SEQRES 1 L 222 GLN PHE ASN PRO TYR GLY ASP ASN GLY GLY THR ILE LEU
SEQRES 2 L 222 GLY ILE ALA GLY GLU ASP PHE ALA VAL LEU ALA GLY ASP
SEQRES 3 L 222 THR ARG ASN ILE THR ASP TYR SER ILE ASN SER ARG TYR
SEQRES 4 L 222 GLU PRO LYS VAL PHE ASP CYS GLY ASP ASN ILE VAL MET
SEQRES 5 L 222 SER ALA ASN GLY PHE ALA ALA ASP GLY ASP ALA LEU VAL
SEQRES 6 L 222 LYS ARG PHE LYS ASN SER VAL LYS TRP TYR HIS PHE ASP
SEQRES 7 L 222 HIS ASN ASP LYS LYS LEU SER ILE ASN SER ALA ALA ARG
SEQRES 8 L 222 ASN ILE GLN HIS LEU LEU TYR GLY LYS ARG PHE PHE PRO
SEQRES 9 L 222 TYR TYR VAL HIS THR ILE ILE ALA GLY LEU ASP GLU ASP
SEQRES 10 L 222 GLY LYS GLY ALA VAL TYR SER PHE ASP PRO VAL GLY SER
SEQRES 11 L 222 TYR GLU ARG GLU GLN CYS ARG ALA GLY GLY ALA ALA ALA
SEQRES 12 L 222 SER LEU ILE MET PRO PHE LEU ASP ASN GLN VAL ASN PHE
SEQRES 13 L 222 LYS ASN GLN TYR GLU PRO GLY THR ASN GLY LYS VAL LYS
SEQRES 14 L 222 LYS PRO LEU LYS TYR LEU SER VAL GLU GLU VAL ILE LYS
SEQRES 15 L 222 LEU VAL ARG ASP SER PHE THR SER ALA THR GLU ARG HIS
SEQRES 16 L 222 ILE GLN VAL GLY ASP GLY LEU GLU ILE LEU ILE VAL THR
SEQRES 17 L 222 LYS ASP GLY VAL ARG LYS GLU PHE TYR GLU LEU LYS ARG
SEQRES 18 L 222 ASP
SEQRES 1 M 246 THR GLN ILE ALA ASN ALA GLY ALA SER PRO MET VAL ASN
SEQRES 2 M 246 THR GLN GLN PRO ILE VAL THR GLY THR SER VAL ILE SER
SEQRES 3 M 246 MET LYS TYR ASP ASN GLY VAL ILE ILE ALA ALA ASP ASN
SEQRES 4 M 246 LEU GLY SER TYR GLY SER LEU LEU ARG PHE ASN GLY VAL
SEQRES 5 M 246 GLU ARG LEU ILE PRO VAL GLY ASP ASN THR VAL VAL GLY
SEQRES 6 M 246 ILE SER GLY ASP ILE SER ASP MET GLN HIS ILE GLU ARG
SEQRES 7 M 246 LEU LEU LYS ASP LEU VAL THR GLU ASN ALA TYR ASP ASN
SEQRES 8 M 246 PRO LEU ALA ASP ALA GLU GLU ALA LEU GLU PRO SER TYR
SEQRES 9 M 246 ILE PHE GLU TYR LEU ALA THR VAL MET TYR GLN ARG ARG
SEQRES 10 M 246 SER LYS MET ASN PRO LEU TRP ASN ALA ILE ILE VAL ALA
SEQRES 11 M 246 GLY VAL GLN SER ASN GLY ASP GLN PHE LEU ARG TYR VAL
SEQRES 12 M 246 ASN LEU LEU GLY VAL THR TYR SER SER PRO THR LEU ALA
SEQRES 13 M 246 THR GLY PHE GLY ALA HIS MET ALA ASN PRO LEU LEU ARG
SEQRES 14 M 246 LYS VAL VAL ASP ARG GLU SER ASP ILE PRO LYS THR THR
SEQRES 15 M 246 VAL GLN VAL ALA GLU GLU ALA ILE VAL ASN ALA MET ARG
SEQRES 16 M 246 VAL LEU TYR TYR ARG ASP ALA ARG SER SER ARG ASN PHE
SEQRES 17 M 246 SER LEU ALA ILE ILE ASP LYS ASN THR GLY LEU THR PHE
SEQRES 18 M 246 LYS LYS ASN LEU GLN VAL GLU ASN MET LYS TRP ASP PHE
SEQRES 19 M 246 ALA LYS ASP ILE LYS GLY TYR GLY THR GLN LYS ILE
SEQRES 1 N 196 THR SER ILE MET ALA VAL THR PHE LYS ASP GLY VAL ILE
SEQRES 2 N 196 LEU GLY ALA ASP SER ARG THR THR THR GLY ALA TYR ILE
SEQRES 3 N 196 ALA ASN ARG VAL THR ASP LYS LEU THR ARG VAL HIS ASP
SEQRES 4 N 196 LYS ILE TRP CYS CYS ARG SER GLY SER ALA ALA ASP THR
SEQRES 5 N 196 GLN ALA ILE ALA ASP ILE VAL GLN TYR HIS LEU GLU LEU
SEQRES 6 N 196 TYR THR SER GLN TYR GLY THR PRO SER THR GLU THR ALA
SEQRES 7 N 196 ALA SER VAL PHE LYS GLU LEU CYS TYR GLU ASN LYS ASP
SEQRES 8 N 196 ASN LEU THR ALA GLY ILE ILE VAL ALA GLY TYR ASP ASP
SEQRES 9 N 196 LYS ASN LYS GLY GLU VAL TYR THR ILE PRO LEU GLY GLY
SEQRES 10 N 196 SER VAL HIS LYS LEU PRO TYR ALA ILE ALA GLY SER GLY
SEQRES 11 N 196 SER THR PHE ILE TYR GLY TYR CYS ASP LYS ASN PHE ARG
SEQRES 12 N 196 GLU ASN MET SER LYS GLU GLU THR VAL ASP PHE ILE LYS
SEQRES 13 N 196 HIS SER LEU SER GLN ALA ILE LYS TRP ASP GLY SER SER
SEQRES 14 N 196 GLY GLY VAL ILE ARG MET VAL VAL LEU THR ALA ALA GLY
SEQRES 15 N 196 VAL GLU ARG LEU ILE PHE TYR PRO ASP GLU TYR GLU GLN
SEQRES 16 N 196 LEU
SEQRES 1 O 250 MET THR ASP ARG TYR SER PHE SER LEU THR THR PHE SER
SEQRES 2 O 250 PRO SER GLY LYS LEU GLY GLN ILE ASP TYR ALA LEU THR
SEQRES 3 O 250 ALA VAL LYS GLN GLY VAL THR SER LEU GLY ILE LYS ALA
SEQRES 4 O 250 THR ASN GLY VAL VAL ILE ALA THR GLU LYS LYS SER SER
SEQRES 5 O 250 SER PRO LEU ALA MET SER GLU THR LEU SER LYS VAL SER
SEQRES 6 O 250 LEU LEU THR PRO ASP ILE GLY ALA VAL TYR SER GLY MET
SEQRES 7 O 250 GLY PRO ASP TYR ARG VAL LEU VAL ASP LYS SER ARG LYS
SEQRES 8 O 250 VAL ALA HIS THR SER TYR LYS ARG ILE TYR GLY GLU TYR
SEQRES 9 O 250 PRO PRO THR LYS LEU LEU VAL SER GLU VAL ALA LYS ILE
SEQRES 10 O 250 MET GLN GLU ALA THR GLN SER GLY GLY VAL ARG PRO PHE
SEQRES 11 O 250 GLY VAL SER LEU LEU ILE ALA GLY HIS ASP GLU PHE ASN
SEQRES 12 O 250 GLY PHE SER LEU TYR GLN VAL ASP PRO SER GLY SER TYR
SEQRES 13 O 250 PHE PRO TRP LYS ALA THR ALA ILE GLY LYS GLY SER VAL
SEQRES 14 O 250 ALA ALA LYS THR PHE LEU GLU LYS ARG TRP ASN ASP GLU
SEQRES 15 O 250 LEU GLU LEU GLU ASP ALA ILE HIS ILE ALA LEU LEU THR
SEQRES 16 O 250 LEU LYS GLU SER VAL GLU GLY GLU PHE ASN GLY ASP THR
SEQRES 17 O 250 ILE GLU LEU ALA ILE ILE GLY ASP GLU ASN PRO ASP LEU
SEQRES 18 O 250 LEU GLY TYR THR GLY ILE PRO THR ASP LYS GLY PRO ARG
SEQRES 19 O 250 PHE ARG LYS LEU THR SER GLN GLU ILE ASN ASP ARG LEU
SEQRES 20 O 250 GLU ALA LEU
SEQRES 1 P 258 MET GLY SER ARG ARG TYR ASP SER ARG THR THR ILE PHE
SEQRES 2 P 258 SER PRO GLU GLY ARG LEU TYR GLN VAL GLU TYR ALA LEU
SEQRES 3 P 258 GLU SER ILE SER HIS ALA GLY THR ALA ILE GLY ILE MET
SEQRES 4 P 258 ALA SER ASP GLY ILE VAL LEU ALA ALA GLU ARG LYS VAL
SEQRES 5 P 258 THR SER THR LEU LEU GLU GLN ASP THR SER THR GLU LYS
SEQRES 6 P 258 LEU TYR LYS LEU ASN ASP LYS ILE ALA VAL ALA VAL ALA
SEQRES 7 P 258 GLY LEU THR ALA ASP ALA GLU ILE LEU ILE ASN THR ALA
SEQRES 8 P 258 ARG ILE HIS ALA GLN ASN TYR LEU LYS THR TYR ASN GLU
SEQRES 9 P 258 ASP ILE PRO VAL GLU ILE LEU VAL ARG ARG LEU SER ASP
SEQRES 10 P 258 ILE LYS GLN GLY TYR THR GLN HIS GLY GLY LEU ARG PRO
SEQRES 11 P 258 PHE GLY VAL SER PHE ILE TYR ALA GLY TYR ASP ASP ARG
SEQRES 12 P 258 TYR GLY TYR GLN LEU TYR THR SER ASN PRO SER GLY ASN
SEQRES 13 P 258 TYR THR GLY TRP LYS ALA ILE SER VAL GLY ALA ASN THR
SEQRES 14 P 258 SER ALA ALA GLN THR LEU LEU GLN MET ASP TYR LYS ASP
SEQRES 15 P 258 ASP MET LYS VAL ASP ASP ALA ILE GLU LEU ALA LEU LYS
SEQRES 16 P 258 THR LEU SER LYS THR THR ASP SER SER ALA LEU THR TYR
SEQRES 17 P 258 ASP ARG LEU GLU PHE ALA THR ILE ARG LYS GLY ALA ASN
SEQRES 18 P 258 ASP GLY GLU VAL TYR GLN LYS ILE PHE LYS PRO GLN GLU
SEQRES 19 P 258 ILE LYS ASP ILE LEU VAL LYS THR GLY ILE THR LYS LYS
SEQRES 20 P 258 ASP GLU ASP GLU GLU ALA ASP GLU ASP MET LYS
SEQRES 1 Q 254 MET SER GLY TYR ASP ARG ALA LEU SER ILE PHE SER PRO
SEQRES 2 Q 254 ASP GLY HIS ILE PHE GLN VAL GLU TYR ALA LEU GLU ALA
SEQRES 3 Q 254 VAL LYS ARG GLY THR CYS ALA VAL GLY VAL LYS GLY LYS
SEQRES 4 Q 254 ASN CYS VAL VAL LEU GLY CYS GLU ARG ARG SER THR LEU
SEQRES 5 Q 254 LYS LEU GLN ASP THR ARG ILE THR PRO SER LYS VAL SER
SEQRES 6 Q 254 LYS ILE ASP SER HIS VAL VAL LEU SER PHE SER GLY LEU
SEQRES 7 Q 254 ASN ALA ASP SER ARG ILE LEU ILE GLU LYS ALA ARG VAL
SEQRES 8 Q 254 GLU ALA GLN SER HIS ARG LEU THR LEU GLU ASP PRO VAL
SEQRES 9 Q 254 THR VAL GLU TYR LEU THR ARG TYR VAL ALA GLY VAL GLN
SEQRES 10 Q 254 GLN ARG TYR THR GLN SER GLY GLY VAL ARG PRO PHE GLY
SEQRES 11 Q 254 VAL SER THR LEU ILE ALA GLY PHE ASP PRO ARG ASP ASP
SEQRES 12 Q 254 GLU PRO LYS LEU TYR GLN THR GLU PRO SER GLY ILE TYR
SEQRES 13 Q 254 SER SER TRP SER ALA GLN THR ILE GLY ARG ASN SER LYS
SEQRES 14 Q 254 THR VAL ARG GLU PHE LEU GLU LYS ASN TYR ASP ARG LYS
SEQRES 15 Q 254 GLU PRO PRO ALA THR VAL GLU GLU CYS VAL LYS LEU THR
SEQRES 16 Q 254 VAL ARG SER LEU LEU GLU VAL VAL GLN THR GLY ALA LYS
SEQRES 17 Q 254 ASN ILE GLU ILE THR VAL VAL LYS PRO ASP SER ASP ILE
SEQRES 18 Q 254 VAL ALA LEU SER SER GLU GLU ILE ASN GLN TYR VAL THR
SEQRES 19 Q 254 GLN ILE GLU GLN GLU LYS GLN GLU GLN GLN GLU GLN ASP
SEQRES 20 Q 254 LYS LYS LYS LYS SER ASN HIS
SEQRES 1 R 260 MET PHE LEU THR ARG SER GLU TYR ASP ARG GLY VAL SER
SEQRES 2 R 260 THR PHE SER PRO GLU GLY ARG LEU PHE GLN VAL GLU TYR
SEQRES 3 R 260 SER LEU GLU ALA ILE LYS LEU GLY SER THR ALA ILE GLY
SEQRES 4 R 260 ILE ALA THR LYS GLU GLY VAL VAL LEU GLY VAL GLU LYS
SEQRES 5 R 260 ARG ALA THR SER PRO LEU LEU GLU SER ASP SER ILE GLU
SEQRES 6 R 260 LYS ILE VAL GLU ILE ASP ARG HIS ILE GLY CYS ALA MET
SEQRES 7 R 260 SER GLY LEU THR ALA ASP ALA ARG SER MET ILE GLU HIS
SEQRES 8 R 260 ALA ARG THR ALA ALA VAL THR HIS ASN LEU TYR TYR ASP
SEQRES 9 R 260 GLU ASP ILE ASN VAL GLU SER LEU THR GLN SER VAL CYS
SEQRES 10 R 260 ASP LEU ALA LEU ARG PHE GLY GLU GLY ALA SER GLY GLU
SEQRES 11 R 260 GLU ARG LEU MET SER ARG PRO PHE GLY VAL ALA LEU LEU
SEQRES 12 R 260 ILE ALA GLY HIS ASP ALA ASP ASP GLY TYR GLN LEU PHE
SEQRES 13 R 260 HIS ALA GLU PRO SER GLY THR PHE TYR ARG TYR ASN ALA
SEQRES 14 R 260 LYS ALA ILE GLY SER GLY SER GLU GLY ALA GLN ALA GLU
SEQRES 15 R 260 LEU LEU ASN GLU TRP HIS SER SER LEU THR LEU LYS GLU
SEQRES 16 R 260 ALA GLU LEU LEU VAL LEU LYS ILE LEU LYS GLN VAL MET
SEQRES 17 R 260 GLU GLU LYS LEU ASP GLU ASN ASN ALA GLN LEU SER CYS
SEQRES 18 R 260 ILE THR LYS GLN ASP GLY PHE LYS ILE TYR ASP ASN GLU
SEQRES 19 R 260 LYS THR ALA GLU LEU ILE LYS GLU LEU LYS GLU LYS GLU
SEQRES 20 R 260 ALA ALA GLU SER PRO GLU GLU ALA ASP VAL GLU MET SER
SEQRES 1 S 234 MET PHE ARG ASN ASN TYR ASP GLY ASP THR VAL THR PHE
SEQRES 2 S 234 SER PRO THR GLY ARG LEU PHE GLN VAL GLU TYR ALA LEU
SEQRES 3 S 234 GLU ALA ILE LYS GLN GLY SER VAL THR VAL GLY LEU ARG
SEQRES 4 S 234 SER ASN THR HIS ALA VAL LEU VAL ALA LEU LYS ARG ASN
SEQRES 5 S 234 ALA ASP GLU LEU SER SER TYR GLN LYS LYS ILE ILE LYS
SEQRES 6 S 234 CYS ASP GLU HIS MET GLY LEU SER LEU ALA GLY LEU ALA
SEQRES 7 S 234 PRO ASP ALA ARG VAL LEU SER ASN TYR LEU ARG GLN GLN
SEQRES 8 S 234 CYS ASN TYR SER SER LEU VAL PHE ASN ARG LYS LEU ALA
SEQRES 9 S 234 VAL GLU ARG ALA GLY HIS LEU LEU CYS ASP LYS ALA GLN
SEQRES 10 S 234 LYS ASN THR GLN SER TYR GLY GLY ARG PRO TYR GLY VAL
SEQRES 11 S 234 GLY LEU LEU ILE ILE GLY TYR ASP LYS SER GLY ALA HIS
SEQRES 12 S 234 LEU LEU GLU PHE GLN PRO SER GLY ASN VAL THR GLU LEU
SEQRES 13 S 234 TYR GLY THR ALA ILE GLY ALA ARG SER GLN GLY ALA LYS
SEQRES 14 S 234 THR TYR LEU GLU ARG THR LEU ASP THR PHE ILE LYS ILE
SEQRES 15 S 234 ASP GLY ASN PRO ASP GLU LEU ILE LYS ALA GLY VAL GLU
SEQRES 16 S 234 ALA ILE SER GLN SER LEU ARG ASP GLU SER LEU THR VAL
SEQRES 17 S 234 ASP ASN LEU SER ILE ALA ILE VAL GLY LYS ASP THR PRO
SEQRES 18 S 234 PHE THR ILE TYR ASP GLY GLU ALA VAL ALA LYS TYR ILE
SEQRES 1 T 288 MET THR SER ILE GLY THR GLY TYR ASP LEU SER ASN SER
SEQRES 2 T 288 VAL PHE SER PRO ASP GLY ARG ASN PHE GLN VAL GLU TYR
SEQRES 3 T 288 ALA VAL LYS ALA VAL GLU ASN GLY THR THR SER ILE GLY
SEQRES 4 T 288 ILE LYS CYS ASN ASP GLY VAL VAL PHE ALA VAL GLU LYS
SEQRES 5 T 288 LEU ILE THR SER LYS LEU LEU VAL PRO GLN LYS ASN VAL
SEQRES 6 T 288 LYS ILE GLN VAL VAL ASP ARG HIS ILE GLY CYS VAL TYR
SEQRES 7 T 288 SER GLY LEU ILE PRO ASP GLY ARG HIS LEU VAL ASN ARG
SEQRES 8 T 288 GLY ARG GLU GLU ALA ALA SER PHE LYS LYS LEU TYR LYS
SEQRES 9 T 288 THR PRO ILE PRO ILE PRO ALA PHE ALA ASP ARG LEU GLY
SEQRES 10 T 288 GLN TYR VAL GLN ALA HIS THR LEU TYR ASN SER VAL ARG
SEQRES 11 T 288 PRO PHE GLY VAL SER THR ILE PHE GLY GLY VAL ASP LYS
SEQRES 12 T 288 ASN GLY ALA HIS LEU TYR MET LEU GLU PRO SER GLY SER
SEQRES 13 T 288 TYR TRP GLY TYR LYS GLY ALA ALA THR GLY LYS GLY ARG
SEQRES 14 T 288 GLN SER ALA LYS ALA GLU LEU GLU LYS LEU VAL ASP HIS
SEQRES 15 T 288 HIS PRO GLU GLY LEU SER ALA ARG GLU ALA VAL LYS GLN
SEQRES 16 T 288 ALA ALA LYS ILE ILE TYR LEU ALA HIS GLU ASP ASN LYS
SEQRES 17 T 288 GLU LYS ASP PHE GLU LEU GLU ILE SER TRP CYS SER LEU
SEQRES 18 T 288 SER GLU THR ASN GLY LEU HIS LYS PHE VAL LYS GLY ASP
SEQRES 19 T 288 LEU LEU GLN GLU ALA ILE ASP PHE ALA GLN LYS GLU ILE
SEQRES 20 T 288 ASN GLY ASP ASP ASP GLU ASP GLU ASP ASP SER ASP ASN
SEQRES 21 T 288 VAL MET SER SER ASP ASP GLU ASN ALA PRO VAL ALA THR
SEQRES 22 T 288 ASN ALA ASN ALA THR THR ASP GLN GLU GLY ASP ILE HIS
SEQRES 23 T 288 LEU GLU
SEQRES 1 U 252 MET SER GLY ALA ALA ALA ALA SER ALA ALA GLY TYR ASP
SEQRES 2 U 252 ARG HIS ILE THR ILE PHE SER PRO GLU GLY ARG LEU TYR
SEQRES 3 U 252 GLN VAL GLU TYR ALA PHE LYS ALA THR ASN GLN THR ASN
SEQRES 4 U 252 ILE ASN SER LEU ALA VAL ARG GLY LYS ASP CYS THR VAL
SEQRES 5 U 252 VAL ILE SER GLN LYS LYS VAL PRO ASP LYS LEU LEU ASP
SEQRES 6 U 252 PRO THR THR VAL SER TYR ILE PHE CYS ILE SER ARG THR
SEQRES 7 U 252 ILE GLY MET VAL VAL ASN GLY PRO ILE PRO ASP ALA ARG
SEQRES 8 U 252 ASN ALA ALA LEU ARG ALA LYS ALA GLU ALA ALA GLU PHE
SEQRES 9 U 252 ARG TYR LYS TYR GLY TYR ASP MET PRO CYS ASP VAL LEU
SEQRES 10 U 252 ALA LYS ARG MET ALA ASN LEU SER GLN ILE TYR THR GLN
SEQRES 11 U 252 ARG ALA TYR MET ARG PRO LEU GLY VAL ILE LEU THR PHE
SEQRES 12 U 252 VAL SER VAL ASP GLU GLU LEU GLY PRO SER ILE TYR LYS
SEQRES 13 U 252 THR ASP PRO ALA GLY TYR TYR VAL GLY TYR LYS ALA THR
SEQRES 14 U 252 ALA THR GLY PRO LYS GLN GLN GLU ILE THR THR ASN LEU
SEQRES 15 U 252 GLU ASN HIS PHE LYS LYS SER LYS ILE ASP HIS ILE ASN
SEQRES 16 U 252 GLU GLU SER TRP GLU LYS VAL VAL GLU PHE ALA ILE THR
SEQRES 17 U 252 HIS MET ILE ASP ALA LEU GLY THR GLU PHE SER LYS ASN
SEQRES 18 U 252 ASP LEU GLU VAL GLY VAL ALA THR LYS ASP LYS PHE PHE
SEQRES 19 U 252 THR LEU SER ALA GLU ASN ILE GLU GLU ARG LEU VAL ALA
SEQRES 20 U 252 ILE ALA GLU GLN ASP
SEQRES 1 V 232 THR THR ILE VAL GLY VAL LYS PHE ASN ASN GLY VAL VAL
SEQRES 2 V 232 ILE ALA ALA ASP THR ARG SER THR GLN GLY PRO ILE VAL
SEQRES 3 V 232 ALA ASP LYS ASN CYS ALA LYS LEU HIS ARG ILE SER PRO
SEQRES 4 V 232 LYS ILE TRP CYS ALA GLY ALA GLY THR ALA ALA ASP THR
SEQRES 5 V 232 GLU ALA VAL THR GLN LEU ILE GLY SER ASN ILE GLU LEU
SEQRES 6 V 232 HIS SER LEU TYR THR SER ARG GLU PRO ARG VAL VAL SER
SEQRES 7 V 232 ALA LEU GLN MET LEU LYS GLN HIS LEU PHE LYS TYR GLN
SEQRES 8 V 232 GLY HIS ILE GLY ALA TYR LEU ILE VAL ALA GLY VAL ASP
SEQRES 9 V 232 PRO THR GLY SER HIS LEU PHE SER ILE HIS ALA HIS GLY
SEQRES 10 V 232 SER THR ASP VAL GLY TYR TYR LEU SER LEU GLY SER GLY
SEQRES 11 V 232 SER LEU ALA ALA MET ALA VAL LEU GLU SER HIS TRP LYS
SEQRES 12 V 232 GLN ASP LEU THR LYS GLU GLU ALA ILE LYS LEU ALA SER
SEQRES 13 V 232 ASP ALA ILE GLN ALA GLY ILE TRP ASN ASP LEU GLY SER
SEQRES 14 V 232 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 ALA 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 MG I 301 1
HET MG I 302 1
HET MG K 301 1
HET MG L 301 1
HET MG N 201 1
HET CL U 301 1
HET MG W 301 1
HET MG Z 301 1
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
FORMUL 29 MG 8(MG 2+)
FORMUL 30 CL 2(CL 1-)
FORMUL 39 HOH *512(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 GLU C 199 1 15
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 SER D 53 ILE D 56 5 4
HELIX 25 AC7 ASP D 76 ASP D 96 1 21
HELIX 26 AC8 ASN D 100 LEU D 113 1 14
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 ASP E 225 ILE E 233 5 9
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 ARG J 93 1 18
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 VAL M 159 1 15
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 GLY N 128 PHE N 133 5 6
HELIX 83 AJ2 ILE N 134 PHE N 142 1 9
HELIX 84 AJ3 SER N 147 ASP N 166 1 20
HELIX 85 AJ4 TYR N 189 GLU N 194 1 6
HELIX 86 AJ5 LEU O 18 GLY O 31 1 14
HELIX 87 AJ6 MET O 78 SER O 96 1 19
HELIX 88 AJ7 TYR O 97 GLY O 102 1 6
HELIX 89 AJ8 PRO O 106 ALA O 121 1 16
HELIX 90 AJ9 GLY O 167 TRP O 179 1 13
HELIX 91 AK1 GLU O 184 VAL O 200 1 17
HELIX 92 AK2 ASN O 218 LEU O 222 5 5
HELIX 93 AK3 THR O 239 ALA O 249 1 11
HELIX 94 AK4 GLY P 1 ASP P 6 5 6
HELIX 95 AK5 LEU P 18 SER P 29 1 12
HELIX 96 AK6 LEU P 79 ASN P 102 1 24
HELIX 97 AK7 PRO P 106 HIS P 124 1 19
HELIX 98 AK8 ASN P 167 TYR P 179 1 13
HELIX 99 AK9 LYS P 184 THR P 200 1 17
HELIX 100 AL1 THR P 206 ASP P 208 5 3
HELIX 101 AL2 LYS P 230 THR P 241 1 12
HELIX 102 AL3 ILE Q 15 GLY Q 28 1 14
HELIX 103 AL4 LEU Q 76 GLU Q 99 1 24
HELIX 104 AL5 THR Q 103 TYR Q 118 1 16
HELIX 105 AL6 ASN Q 165 TYR Q 177 1 13
HELIX 106 AL7 THR Q 185 GLU Q 199 1 15
HELIX 107 AL8 SER Q 223 GLN Q 239 1 17
HELIX 108 AL9 LEU R 13 LEU R 25 1 13
HELIX 109 AM1 SER R 53 ILE R 56 5 4
HELIX 110 AM2 ASP R 76 ASP R 96 1 21
HELIX 111 AM3 ASN R 100 LEU R 113 1 14
HELIX 112 AM4 GLY R 167 TRP R 179 1 13
HELIX 113 AM5 THR R 184 MET R 200 1 17
HELIX 114 AM6 ASP R 224 ALA R 241 1 18
HELIX 115 AM7 LEU S 18 GLY S 31 1 14
HELIX 116 AM8 LEU S 76 ASN S 99 1 24
HELIX 117 AM9 ALA S 103 SER S 121 1 19
HELIX 118 AN1 ARG S 163 ILE S 179 1 17
HELIX 119 AN2 ASN S 184 SER S 197 1 14
HELIX 120 AN3 GLN S 198 LEU S 200 5 3
HELIX 121 AN4 ASP S 225 ILE S 233 5 9
HELIX 122 AN5 ASN T 17 GLY T 30 1 14
HELIX 123 AN6 LEU T 77 LYS T 100 1 24
HELIX 124 AN7 PRO T 104 HIS T 119 1 16
HELIX 125 AN8 GLY T 164 HIS T 179 1 16
HELIX 126 AN9 SER T 184 HIS T 200 1 17
HELIX 127 AO1 GLU T 201 LYS T 204 5 4
HELIX 128 AO2 LYS T 228 ASN T 244 1 17
HELIX 129 AO3 GLY U 2 HIS U 6 5 5
HELIX 130 AO4 LEU U 16 THR U 26 1 11
HELIX 131 AO5 ASP U 56 VAL U 60 5 5
HELIX 132 AO6 PRO U 77 GLY U 100 1 24
HELIX 133 AO7 PRO U 104 ARG U 122 1 19
HELIX 134 AO8 LYS U 165 LYS U 181 1 17
HELIX 135 AO9 SER U 189 GLY U 206 1 18
HELIX 136 AP1 SER U 228 GLU U 241 1 14
HELIX 137 AP2 THR V 48 SER V 71 1 24
HELIX 138 AP3 ARG V 75 TYR V 90 1 16
HELIX 139 AP4 GLY V 130 TRP V 142 1 13
HELIX 140 AP5 THR V 147 ASP V 166 1 20
HELIX 141 AP6 ASP W 2 ILE W 6 5 5
HELIX 142 AP7 LEU W 55 GLU W 78 1 24
HELIX 143 AP8 GLU W 82 GLU W 96 1 15
HELIX 144 AP9 ALA W 141 TYR W 153 1 13
HELIX 145 AQ1 GLU W 158 ASP W 175 1 18
HELIX 146 AQ2 GLY X 51 ASP X 72 1 22
HELIX 147 AQ3 SER X 76 ARG X 93 1 18
HELIX 148 AQ4 TYR X 135 TYR X 148 1 14
HELIX 149 AQ5 THR X 153 MET X 172 1 20
HELIX 150 AQ6 GLY Y 48 LYS Y 71 1 24
HELIX 151 AQ7 SER Y 75 TYR Y 90 1 16
HELIX 152 AQ8 GLY Y 132 TYR Y 144 1 13
HELIX 153 AQ9 SER Y 149 ASP Y 168 1 20
HELIX 154 AR1 VAL Y 193 GLY Y 205 1 13
HELIX 155 AR2 PHE Z 57 HIS Z 79 1 23
HELIX 156 AR3 SER Z 85 GLY Z 99 1 15
HELIX 157 AR4 ALA Z 142 VAL Z 154 1 13
HELIX 158 AR5 SER Z 176 HIS Z 195 1 20
HELIX 159 AR6 ILE a 57 TYR a 76 1 20
HELIX 160 AR7 GLU a 88 LYS a 106 1 19
HELIX 161 AR8 GLY a 145 VAL a 159 1 15
HELIX 162 AR9 ARG a 161 ILE a 165 5 5
HELIX 163 AS1 THR a 169 ASP a 188 1 20
HELIX 164 AS2 TRP a 219 ILE a 225 5 7
HELIX 165 AS3 SER b 48 GLY b 71 1 24
HELIX 166 AS4 SER b 74 ASN b 89 1 16
HELIX 167 AS5 GLY b 128 PHE b 133 5 6
HELIX 168 AS6 ILE b 134 PHE b 142 1 9
HELIX 169 AS7 SER b 147 ASP b 166 1 20
HELIX 170 AS8 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 6 ALA A 56 MET A 57 0
SHEET 2 AA2 6 TYR G 154 TYR G 157 -1 O GLY G 156 N MET A 57
SHEET 3 AA2 6 GLY G 142 THR G 148 -1 N ILE G 145 O TYR G 157
SHEET 4 AA2 6 ILE G 131 ASP G 138 -1 N LEU G 132 O THR G 148
SHEET 5 AA2 6 GLY G 71 ASN G 75 -1 N GLY G 71 O VAL G 135
SHEET 6 AA2 6 ILE G 63 CYS G 65 -1 N PHE G 64 O MET G 72
SHEET 1 AA3 5 SER A 65 THR A 68 0
SHEET 2 AA3 5 ILE A 71 GLY A 77 -1 O ALA A 73 N SER A 65
SHEET 3 AA3 5 VAL A 132 ASP A 140 -1 O LEU A 135 N VAL A 74
SHEET 4 AA3 5 GLY A 144 VAL A 150 -1 O TYR A 148 N ILE A 136
SHEET 5 AA3 5 TYR A 156 PRO A 158 -1 O PHE A 157 N GLN A 149
SHEET 1 AA4 6 TYR A 224 THR A 225 0
SHEET 2 AA4 6 ALA H 184 LEU H 191 1 O TYR H 186 N THR A 225
SHEET 3 AA4 6 VAL H 173 GLU H 179 -1 N VAL H 175 O LEU H 187
SHEET 4 AA4 6 GLY H 11 ASP H 17 -1 N ALA H 16 O ASP H 174
SHEET 5 AA4 6 ILE H 3 PHE H 8 -1 N VAL H 6 O VAL H 13
SHEET 6 AA4 6 TYR H 124 LEU H 127 -1 O LEU H 127 N ILE H 3
SHEET 1 AA5 5 ALA B 161 VAL B 164 0
SHEET 2 AA5 5 ALA B 34 ALA B 39 -1 N GLY B 36 O ILE B 162
SHEET 3 AA5 5 GLY B 42 GLU B 48 -1 O ALA B 46 N ILE B 35
SHEET 4 AA5 5 LEU B 210 ALA B 219 -1 O ALA B 213 N LEU B 45
SHEET 5 AA5 5 GLU B 223 ILE B 228 -1 O TYR B 225 N ARG B 216
SHEET 1 AA6 5 LEU B 65 LYS B 67 0
SHEET 2 AA6 5 ILE B 72 GLY B 78 -1 O VAL B 74 N TYR B 66
SHEET 3 AA6 5 VAL B 132 ASP B 140 -1 O ALA B 137 N ALA B 73
SHEET 4 AA6 5 GLY B 144 SER B 150 -1 O TYR B 148 N TYR B 136
SHEET 5 AA6 5 TYR B 156 TRP B 159 -1 O TRP B 159 N LEU B 147
SHEET 1 AA7 5 ALA C 159 ILE C 162 0
SHEET 2 AA7 5 ALA C 31 LYS C 35 -1 N GLY C 33 O GLN C 160
SHEET 3 AA7 5 VAL C 40 GLU C 45 -1 O VAL C 41 N VAL C 34
SHEET 4 AA7 5 ILE C 208 LYS C 214 -1 O VAL C 213 N VAL C 40
SHEET 5 AA7 5 ASP C 218 ALA C 221 -1 O ASP C 218 N LYS C 214
SHEET 1 AA8 6 SER C 63 LYS C 64 0
SHEET 2 AA8 6 VAL C 69 GLY C 75 -1 O LEU C 71 N SER C 63
SHEET 3 AA8 6 VAL C 129 GLY C 135 -1 O ALA C 134 N VAL C 70
SHEET 4 AA8 6 LYS C 144 THR C 148 -1 O TYR C 146 N ILE C 133
SHEET 5 AA8 6 TYR C 154 TRP C 157 -1 O TRP C 157 N LEU C 145
SHEET 6 AA8 6 LEU D 51 GLU D 52 -1 O GLU D 52 N SER C 156
SHEET 1 AA9 5 ALA D 161 ILE D 164 0
SHEET 2 AA9 5 ALA D 29 ALA D 33 -1 N GLY D 31 O LYS D 162
SHEET 3 AA9 5 VAL D 38 GLU D 43 -1 O GLY D 41 N ILE D 30
SHEET 4 AA9 5 ALA D 209 THR D 215 -1 O SER D 212 N LEU D 40
SHEET 5 AA9 5 GLY D 219 ILE D 222 -1 O LYS D 221 N CYS D 213
SHEET 1 AB1 5 ILE D 59 ASP D 63 0
SHEET 2 AB1 5 ILE D 66 GLY D 72 -1 O CYS D 68 N VAL D 60
SHEET 3 AB1 5 VAL D 132 ASP D 140 -1 O LEU D 135 N ALA D 69
SHEET 4 AB1 5 GLY D 144 ALA D 150 -1 O PHE D 148 N ILE D 136
SHEET 5 AB1 5 PHE D 156 ARG D 158 -1 O TYR D 157 N HIS D 149
SHEET 1 AB2 5 GLY E 157 ILE E 160 0
SHEET 2 AB2 5 THR E 34 ARG E 38 -1 N GLY E 36 O THR E 158
SHEET 3 AB2 5 HIS E 42 LEU E 48 -1 O VAL E 46 N VAL E 35
SHEET 4 AB2 5 LEU E 210 GLY E 216 -1 O SER E 211 N ALA E 47
SHEET 5 AB2 5 THR E 219 TYR E 224 -1 O TYR E 224 N ILE E 212
SHEET 1 AB3 5 ILE E 62 ASP E 66 0
SHEET 2 AB3 5 MET E 69 GLY E 75 -1 O LEU E 71 N ILE E 63
SHEET 3 AB3 5 VAL E 129 ASP E 137 -1 O GLY E 130 N ALA E 74
SHEET 4 AB3 5 GLY E 140 PHE E 146 -1 O PHE E 146 N LEU E 131
SHEET 5 AB3 5 VAL E 152 GLU E 154 -1 O THR E 153 N GLU E 145
SHEET 1 AB4 5 GLY F 158 THR F 161 0
SHEET 2 AB4 5 SER F 33 LYS F 37 -1 N GLY F 35 O ALA F 159
SHEET 3 AB4 5 GLY F 41 LEU F 49 -1 O ALA F 45 N ILE F 34
SHEET 4 AB4 5 PHE F 208 SER F 216 -1 O SER F 213 N PHE F 44
SHEET 5 AB4 5 HIS F 224 PHE F 226 -1 O LYS F 225 N TRP F 214
SHEET 1 AB5 5 GLN F 64 VAL F 66 0
SHEET 2 AB5 5 ILE F 70 GLY F 76 -1 O CYS F 72 N GLN F 64
SHEET 3 AB5 5 VAL F 130 ASP F 138 -1 O ILE F 133 N VAL F 73
SHEET 4 AB5 5 GLY F 141 LEU F 147 -1 O TYR F 145 N PHE F 134
SHEET 5 AB5 5 TYR F 153 GLY F 155 -1 O TRP F 154 N MET F 146
SHEET 1 AB6 5 ALA G 159 THR G 162 0
SHEET 2 AB6 5 SER G 33 ARG G 37 -1 N SER G 33 O THR G 162
SHEET 3 AB6 5 THR G 42 GLN G 47 -1 O ILE G 45 N LEU G 34
SHEET 4 AB6 5 LEU G 214 THR G 220 -1 O GLY G 217 N VAL G 44
SHEET 5 AB6 5 LYS G 223 THR G 226 -1 O PHE G 225 N VAL G 218
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 TYR H 97 N ALA H 46
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 VAL H 218 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 VAL I 35 N LEU I 28
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 ILE J 180 N SER J 17
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 ASN J 101 N ALA J 47
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 GLY K 130 0
SHEET 2 AC6 5 THR K 2 PHE K 8 -1 N THR K 3 O VAL K 129
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 LYS K 123 -1 O LEU K 122 N TYR K 114
SHEET 1 AC9 5 CYS L 136 GLY L 140 0
SHEET 2 AC9 5 THR L 11 ALA L 16 -1 N 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 TYR L 217 N LEU L 202
SHEET 1 AD1 2 ASN L 29 THR L 31 0
SHEET 2 AD1 2 SER L 34 SER L 37 -1 O ASN L 36 N ASN L 29
SHEET 1 AD2 5 PHE L 44 GLY L 47 0
SHEET 2 AD2 5 ILE L 50 GLY L 56 -1 O MET L 52 N PHE L 44
SHEET 3 AD2 5 VAL L 107 LEU L 114 -1 O HIS L 108 N ASN L 55
SHEET 4 AD2 5 GLY L 120 PHE L 125 -1 O PHE L 125 N THR L 109
SHEET 5 AD2 5 TYR L 131 GLU L 134 -1 O GLU L 134 N VAL L 122
SHEET 1 AD3 5 LEU M 33 PHE M 36 0
SHEET 2 AD3 5 GLY M 28 TYR M 30 -1 N TYR M 30 O LEU M 33
SHEET 3 AD3 5 VAL M 6 GLY M 8 -1 N THR M 7 O SER M 29
SHEET 4 AD3 5 THR M 49 ASP M 56 -1 O GLY M 55 N GLY M 8
SHEET 5 AD3 5 LEU M 42 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 ALA M 117 N VAL M 50
SHEET 6 AD4 7 GLN M 125 ASN M 131 -1 O VAL M 130 N ILE M 114
SHEET 7 AD4 7 THR M 136 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 PHE N 8 -1 N ALA N 5 O ALA N 125
SHEET 3 AD6 5 GLY N 11 ALA N 16 -1 O GLY N 15 N MET N 4
SHEET 4 AD6 5 ILE N 173 THR N 179 -1 O LEU N 178 N VAL N 12
SHEET 5 AD6 5 VAL N 183 PHE N 188 -1 O GLU N 184 N VAL N 177
SHEET 1 AD7 2 THR N 20 THR N 22 0
SHEET 2 AD7 2 TYR N 25 ASN N 28 -1 O TYR N 25 N THR N 22
SHEET 1 AD8 5 LEU N 34 HIS N 38 0
SHEET 2 AD8 5 ILE N 41 GLY N 47 -1 O CYS N 43 N THR N 35
SHEET 3 AD8 5 ALA N 95 TYR N 102 -1 O GLY N 96 N SER N 46
SHEET 4 AD8 5 GLY N 108 ILE N 113 -1 O TYR N 111 N VAL N 99
SHEET 5 AD8 5 HIS N 120 LEU N 122 -1 O HIS N 120 N THR N 112
SHEET 1 AD9 5 ALA O 161 ILE O 164 0
SHEET 2 AD9 5 SER O 34 LYS O 38 -1 N SER O 34 O ILE O 164
SHEET 3 AD9 5 VAL O 43 GLU O 48 -1 O VAL O 44 N ILE O 37
SHEET 4 AD9 5 ILE O 209 ILE O 214 -1 O ILE O 214 N VAL O 43
SHEET 5 AD9 5 PHE O 235 LYS O 237 -1 O ARG O 236 N ILE O 213
SHEET 1 AE1 6 ALA O 56 MET O 57 0
SHEET 2 AE1 6 TYR U 154 TYR U 157 -1 O GLY U 156 N MET O 57
SHEET 3 AE1 6 GLY U 142 THR U 148 -1 N ILE U 145 O TYR U 157
SHEET 4 AE1 6 ILE U 131 ASP U 138 -1 N PHE U 134 O TYR U 146
SHEET 5 AE1 6 GLY U 71 ASN U 75 -1 N GLY U 71 O VAL U 135
SHEET 6 AE1 6 ILE U 63 CYS U 65 -1 N PHE U 64 O MET U 72
SHEET 1 AE2 5 SER O 65 THR O 68 0
SHEET 2 AE2 5 ILE O 71 GLY O 77 -1 O ALA O 73 N SER O 65
SHEET 3 AE2 5 VAL O 132 ASP O 140 -1 O LEU O 135 N VAL O 74
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 ALA P 219 -1 O ALA P 213 N LEU P 45
SHEET 5 AE4 5 GLU P 223 ILE P 228 -1 O TYR P 225 N ARG P 216
SHEET 1 AE5 5 LEU P 65 LYS P 67 0
SHEET 2 AE5 5 ILE P 72 GLY P 78 -1 O VAL P 74 N TYR P 66
SHEET 3 AE5 5 VAL P 132 ASP P 140 -1 O ALA P 137 N ALA P 73
SHEET 4 AE5 5 GLY P 144 SER P 150 -1 O TYR P 148 N TYR P 136
SHEET 5 AE5 5 TYR P 156 TRP P 159 -1 O TRP P 159 N LEU P 147
SHEET 1 AE6 5 ALA Q 159 ILE Q 162 0
SHEET 2 AE6 5 ALA Q 31 LYS Q 35 -1 N GLY Q 33 O GLN Q 160
SHEET 3 AE6 5 VAL Q 40 GLU Q 45 -1 O VAL Q 41 N VAL Q 34
SHEET 4 AE6 5 ILE Q 208 LYS Q 214 -1 O VAL Q 213 N VAL Q 40
SHEET 5 AE6 5 ASP Q 218 ALA Q 221 -1 O ASP Q 218 N LYS Q 214
SHEET 1 AE7 6 SER Q 63 LYS Q 64 0
SHEET 2 AE7 6 VAL Q 69 GLY Q 75 -1 O LEU Q 71 N SER Q 63
SHEET 3 AE7 6 VAL Q 129 GLY Q 135 -1 O ALA Q 134 N VAL Q 70
SHEET 4 AE7 6 LYS Q 144 THR Q 148 -1 O TYR Q 146 N ILE Q 133
SHEET 5 AE7 6 TYR Q 154 TRP Q 157 -1 O TRP Q 157 N LEU Q 145
SHEET 6 AE7 6 LEU R 51 GLU R 52 -1 O GLU R 52 N SER Q 156
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 LEU R 135 N ALA R 69
SHEET 4 AE9 5 GLY R 144 ALA R 150 -1 O PHE R 148 N ILE R 136
SHEET 5 AE9 5 PHE R 156 ARG R 158 -1 O TYR R 157 N HIS R 149
SHEET 1 AF1 5 GLY S 157 ILE S 160 0
SHEET 2 AF1 5 THR S 34 ARG S 38 -1 N GLY S 36 O THR S 158
SHEET 3 AF1 5 HIS S 42 LEU S 48 -1 O VAL S 46 N VAL S 35
SHEET 4 AF1 5 LEU S 210 GLY S 216 -1 O SER S 211 N ALA S 47
SHEET 5 AF1 5 THR S 219 TYR S 224 -1 O TYR S 224 N ILE S 212
SHEET 1 AF2 5 ILE S 62 ASP S 66 0
SHEET 2 AF2 5 MET S 69 GLY S 75 -1 O LEU S 71 N ILE S 63
SHEET 3 AF2 5 VAL S 129 ASP S 137 -1 O GLY S 130 N ALA S 74
SHEET 4 AF2 5 GLY S 140 PHE S 146 -1 O PHE S 146 N LEU S 131
SHEET 5 AF2 5 VAL S 152 GLU S 154 -1 O THR S 153 N GLU S 145
SHEET 1 AF3 5 GLY T 158 THR T 161 0
SHEET 2 AF3 5 SER T 33 LYS T 37 -1 N GLY T 35 O ALA T 159
SHEET 3 AF3 5 GLY T 41 LEU T 49 -1 O ALA T 45 N ILE T 34
SHEET 4 AF3 5 PHE T 208 SER T 216 -1 O SER T 213 N PHE T 44
SHEET 5 AF3 5 HIS T 224 PHE T 226 -1 O LYS T 225 N TRP T 214
SHEET 1 AF4 5 GLN T 64 VAL T 66 0
SHEET 2 AF4 5 ILE T 70 GLY T 76 -1 O CYS T 72 N GLN T 64
SHEET 3 AF4 5 VAL T 130 ASP T 138 -1 O ILE T 133 N VAL T 73
SHEET 4 AF4 5 GLY T 141 LEU T 147 -1 O TYR T 145 N PHE T 134
SHEET 5 AF4 5 TYR T 153 GLY T 155 -1 O TRP T 154 N MET T 146
SHEET 1 AF5 5 ALA U 159 THR U 162 0
SHEET 2 AF5 5 SER U 33 ARG U 37 -1 N SER U 33 O THR U 162
SHEET 3 AF5 5 THR U 42 GLN U 47 -1 O ILE U 45 N LEU U 34
SHEET 4 AF5 5 LEU U 214 THR U 220 -1 O GLY U 217 N VAL U 44
SHEET 5 AF5 5 LYS U 223 THR U 226 -1 O PHE U 225 N VAL U 218
SHEET 1 AF6 2 SER V 20 GLN V 22 0
SHEET 2 AF6 2 ILE V 25 ASP V 28 -1 O 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 CYS V 43 N HIS V 35
SHEET 3 AF7 5 ALA V 96 ASP V 104 -1 O TYR V 97 N ALA V 46
SHEET 4 AF7 5 GLY V 107 ILE V 113 -1 O 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 VAL V 218 0
SHEET 2 AF8 6 GLU W 193 LEU W 199 -1 O VAL W 194 N VAL V 218
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 VAL W 35 N LEU W 28
SHEET 1 AG1 5 ILE W 42 TYR W 45 0
SHEET 2 AG1 5 VAL W 48 GLY W 54 -1 O LEU W 50 N PHE W 43
SHEET 3 AG1 5 VAL W 104 ILE W 111 -1 O VAL W 107 N GLY W 51
SHEET 4 AG1 5 PRO W 118 PHE W 123 -1 O ALA W 121 N VAL W 108
SHEET 5 AG1 5 ILE W 129 ASP W 130 -1 O ASP W 130 N GLY W 122
SHEET 1 AG2 5 TYR X 130 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 ILE X 180 N SER X 17
SHEET 5 AG2 5 GLY X 188 VAL X 192 -1 O ARG X 190 N ILE X 183
SHEET 1 AG3 2 VAL X 21 ARG X 23 0
SHEET 2 AG3 2 SER X 26 LYS X 29 -1 O LYS X 29 N VAL X 21
SHEET 1 AG4 5 THR X 35 SER X 39 0
SHEET 2 AG4 5 THR X 42 GLY X 48 -1 O MET X 44 N ARG X 36
SHEET 3 AG4 5 VAL X 100 ASP X 108 -1 O ASN X 101 N ALA X 47
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 GLY Y 130 0
SHEET 2 AG5 5 THR Y 2 PHE Y 8 -1 N THR Y 3 O VAL Y 129
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 LYS Y 123 -1 O LEU Y 122 N TYR Y 114
SHEET 1 AG8 5 CYS Z 136 GLY Z 140 0
SHEET 2 AG8 5 THR Z 11 ALA Z 16 -1 N ILE Z 12 O GLY Z 139
SHEET 3 AG8 5 ALA Z 21 ASP Z 26 -1 O ALA Z 24 N LEU Z 13
SHEET 4 AG8 5 GLY Z 201 THR Z 208 -1 O VAL Z 207 N ALA Z 21
SHEET 5 AG8 5 GLY Z 211 GLU Z 218 -1 O TYR Z 217 N LEU Z 202
SHEET 1 AG9 2 ASN Z 29 THR Z 31 0
SHEET 2 AG9 2 SER Z 34 SER Z 37 -1 O ASN Z 36 N ASN Z 29
SHEET 1 AH1 5 PHE Z 44 GLY Z 47 0
SHEET 2 AH1 5 ILE Z 50 GLY Z 56 -1 O MET Z 52 N PHE Z 44
SHEET 3 AH1 5 VAL Z 107 LEU Z 114 -1 O HIS Z 108 N ASN Z 55
SHEET 4 AH1 5 GLY Z 120 PHE Z 125 -1 O PHE Z 125 N THR Z 109
SHEET 5 AH1 5 TYR Z 131 GLU Z 134 -1 O GLU Z 134 N VAL Z 122
SHEET 1 AH2 5 LEU a 33 PHE a 36 0
SHEET 2 AH2 5 GLY a 28 TYR a 30 -1 N TYR a 30 O LEU a 33
SHEET 3 AH2 5 VAL a 6 GLY a 8 -1 N THR a 7 O SER a 29
SHEET 4 AH2 5 THR a 49 ASP a 56 -1 O GLY a 55 N GLY a 8
SHEET 5 AH2 5 LEU a 42 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 ALA a 117 N VAL a 50
SHEET 6 AH3 7 GLN a 125 ASN a 131 -1 O VAL a 130 N ILE a 114
SHEET 7 AH3 7 THR a 136 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 ILE b 3 O ALA b 127
SHEET 3 AH5 5 GLY b 11 ALA b 16 -1 O GLY b 15 N MET b 4
SHEET 4 AH5 5 ILE b 173 THR b 179 -1 O LEU b 178 N VAL b 12
SHEET 5 AH5 5 VAL b 183 PHE b 188 -1 O GLU b 184 N VAL b 177
SHEET 1 AH6 2 THR b 20 THR b 22 0
SHEET 2 AH6 2 TYR b 25 ASN b 28 -1 O TYR b 25 N THR b 22
SHEET 1 AH7 5 LEU b 34 HIS b 38 0
SHEET 2 AH7 5 ILE b 41 GLY b 47 -1 O CYS b 43 N THR b 35
SHEET 3 AH7 5 ALA b 95 TYR b 102 -1 O GLY b 96 N SER b 46
SHEET 4 AH7 5 GLY b 108 ILE b 113 -1 O TYR b 111 N VAL b 99
SHEET 5 AH7 5 HIS b 120 LEU b 122 -1 O HIS b 120 N THR b 112
LINK OG1 THR G 8 MG MG G 301 1555 1555 2.64
LINK O TYR G 119 MG MG G 301 1555 1555 2.68
LINK O ARG G 122 MG MG G 301 1555 1555 2.51
LINK O MET G 125 MG MG G 301 1555 1555 2.17
LINK O ASP I 177 MG MG I 301 1555 1555 2.50
LINK O SER I 180 MG MG I 301 1555 1555 2.79
LINK O ASP I 204 MG MG I 302 1555 1555 2.36
LINK MG MG I 302 O ALA Y 165 1555 1555 2.47
LINK MG MG I 302 O ASP Y 168 1555 1555 2.21
LINK MG MG I 302 O SER Y 171 1555 1555 2.91
LINK O ALA K 165 MG MG K 301 1555 1555 2.35
LINK O ASP K 168 MG MG K 301 1555 1555 2.21
LINK O SER K 171 MG MG K 301 1555 1555 2.67
LINK MG MG K 301 O ASP W 204 1555 1555 2.32
LINK OXT ASP L 222 MG MG L 301 1555 1555 2.25
LINK MG MG L 301 O ILE V 163 1555 1555 2.12
LINK MG MG L 301 O ASP V 166 1555 1555 2.10
LINK MG MG L 301 O SER V 169 1555 1555 2.30
LINK O ILE N 163 MG MG N 201 1555 1555 2.93
LINK O SER N 169 MG MG N 201 1555 1555 2.82
LINK O ALA W 174 MG MG W 301 1555 1555 2.60
LINK O ASP W 177 MG MG W 301 1555 1555 2.55
LINK O SER W 180 MG MG W 301 1555 1555 2.70
LINK O THR Z 192 MG MG Z 301 1555 1555 2.77
LINK O VAL Z 198 MG MG Z 301 1555 1555 2.50
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 4 ALA I 174 ASP I 177 SER I 180 ASP I 204
SITE 1 AC4 5 ASP I 204 ALA Y 165 ASP Y 168 ALA Y 169
SITE 2 AC4 5 SER Y 171
SITE 1 AC5 5 ALA K 165 ASP K 168 ALA K 169 SER K 171
SITE 2 AC5 5 ASP W 204
SITE 1 AC6 4 ASP L 222 ILE V 163 ASP V 166 SER V 169
SITE 1 AC7 5 ARG N 19 ILE N 163 ASP N 166 SER N 169
SITE 2 AC7 5 LEU a 34
SITE 1 AC8 3 ARG U 111 ASN U 114 TYR V 69
SITE 1 AC9 3 ALA W 174 ASP W 177 SER W 180
SITE 1 AD1 5 ARG Z 28 THR Z 192 HIS Z 195 VAL Z 198
SITE 2 AD1 5 ASP Z 222
CRYST1 135.350 300.500 144.440 90.00 113.10 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 0.007388 0.000000 0.003151 0.00000
SCALE2 0.000000 0.003328 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007527 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 -0.999617 -0.001457 0.027620 67.54777 1
MTRIX2 2 -0.003334 -0.984981 -0.172632 -289.07657 1
MTRIX3 2 0.027457 -0.172658 0.984599 -26.21016 1
(ATOM LINES ARE NOT SHOWN.)
END
