HEADER HYDROLASE/HYDROLASE INHIBITOR 16-FEB-15 4Y80
TITLE YEAST 20S PROTEASOME IN COMPLEX WITH AC-LAI-EP
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 MOL_ID: 12;
COMPND 69 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-6;
COMPND 70 CHAIN: L, Z;
COMPND 71 SYNONYM: MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C5,PROTEASOME
COMPND 72 COMPONENT C5;
COMPND 73 EC: 3.4.25.1;
COMPND 74 MOL_ID: 13;
COMPND 75 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-7;
COMPND 76 CHAIN: M, a;
COMPND 77 SYNONYM: MACROPAIN SUBUNIT PRE4,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 78 SUBUNIT PRE4,PROTEASOME COMPONENT PRE4,PROTEINASE YSCE SUBUNIT PRE4;
COMPND 79 EC: 3.4.25.1;
COMPND 80 MOL_ID: 14;
COMPND 81 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-1;
COMPND 82 CHAIN: N, b;
COMPND 83 SYNONYM: MACROPAIN SUBUNIT PRE3,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 84 SUBUNIT PRE3,PROTEASOME COMPONENT PRE3,PROTEINASE YSCE SUBUNIT PRE3;
COMPND 85 EC: 3.4.25.1;
COMPND 86 MOL_ID: 15;
COMPND 87 MOLECULE: AC-LAI-EP;
COMPND 88 CHAIN: c, d, e, f, g, h;
COMPND 89 ENGINEERED: YES
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 MOL_ID: 12;
SOURCE 46 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE S288C;
SOURCE 47 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 48 ORGANISM_TAXID: 559292;
SOURCE 49 MOL_ID: 13;
SOURCE 50 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE S288C;
SOURCE 51 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 52 ORGANISM_TAXID: 559292;
SOURCE 53 MOL_ID: 14;
SOURCE 54 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE S288C;
SOURCE 55 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 56 ORGANISM_TAXID: 559292;
SOURCE 57 MOL_ID: 15;
SOURCE 58 SYNTHETIC: YES;
SOURCE 59 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 60 ORGANISM_TAXID: 32630
KEYWDS HYDROLASE-HYDROLASE INHIBITOR COMPLEX, PROTEASOME, INHIBITOR, BINDING
KEYWDS 2 ANALYSIS
EXPDTA X-RAY DIFFRACTION
AUTHOR E.M.HUBER,M.GROLL
REVDAT 3 10-JAN-24 4Y80 1 LINK SITE ATOM
REVDAT 2 01-JUL-15 4Y80 1 JRNL
REVDAT 1 17-JUN-15 4Y80 0
JRNL AUTH E.M.HUBER,G.DE BRUIN,W.HEINEMEYER,G.PANIAGUA SORIANO,
JRNL AUTH 2 H.S.OVERKLEEFT,M.GROLL
JRNL TITL SYSTEMATIC ANALYSES OF SUBSTRATE PREFERENCES OF 20S
JRNL TITL 2 PROTEASOMES USING PEPTIDIC EPOXYKETONE INHIBITORS.
JRNL REF J.AM.CHEM.SOC. V. 137 7835 2015
JRNL REFN ESSN 1520-5126
JRNL PMID 26020686
JRNL DOI 10.1021/JACS.5B03688
REMARK 2
REMARK 2 RESOLUTION. 2.50 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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 341974
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) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 17999
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56
REMARK 3 REFLECTION IN BIN (WORKING SET) : 24685
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.76
REMARK 3 BIN R VALUE (WORKING SET) : 0.3240
REMARK 3 BIN FREE R VALUE SET COUNT : 1299
REMARK 3 BIN FREE R VALUE : 0.3470
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 49455
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 47
REMARK 3 SOLVENT ATOMS : 746
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 58.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.70000
REMARK 3 B22 (A**2) : -5.53000
REMARK 3 B33 (A**2) : 2.23000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.51000
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): 0.216
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.179
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.971
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.944
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 50412 ; 0.005 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 48245 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 68224 ; 0.922 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES):111081 ; 0.777 ; 3.002
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 6306 ; 5.270 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 2246 ;34.690 ;24.408
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 8736 ;15.192 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 284 ;14.758 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 7700 ; 0.053 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 57124 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 11280 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 25314 ; 1.558 ; 4.195
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 25313 ; 1.558 ; 4.195
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 31590 ; 1.968 ; 6.278
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 31591 ; 1.967 ; 6.278
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 25098 ; 1.503 ; 4.558
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 25098 ; 1.503 ; 4.558
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 36635 ; 1.708 ; 6.702
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 53798 ; 2.358 ;32.672
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 53694 ; 2.300 ;32.645
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 98657 ; 1.203 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 405 ;28.268 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 98106 ; 4.090 ; 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 ; 0.000 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 A (A): 3265 ; 0.010 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 A (A): 3439 ; 0.000 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 A (A): 3618 ; 0.000 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 A (A): 3013 ; 0.000 ; 0.050
REMARK 3 TIGHT THERMAL 1 A (A**2): 3795 ; 4.350 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : B P
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 1 B 300 1
REMARK 3 1 P 1 P 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 2 B (A**2): 3756 ; 3.460 ; 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 ; 9.510 ; 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 ; 4.180 ; 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 ; 4.860 ; 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 ; 4.830 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 7
REMARK 3 CHAIN NAMES : G U
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 G 1 G 300 1
REMARK 3 1 U 1 U 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 7 G (A**2): 3770 ; 3.230 ; 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): 3400 ; 2.480 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 9
REMARK 3 CHAIN NAMES : I W
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 I 1 I 300 1
REMARK 3 1 W 1 W 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 9 I (A**2): 3119 ; 2.340 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 10
REMARK 3 CHAIN NAMES : J X
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 J 1 J 300 1
REMARK 3 1 X 1 X 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 10 J (A**2): 3099 ; 2.330 ; 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): 3265 ; 2.100 ; 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 ; 1.690 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 13
REMARK 3 CHAIN NAMES : M a
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 M 1 M 300 1
REMARK 3 1 a 1 a 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 13 M (A**2): 3618 ; 2.570 ; 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): 3013 ; 1.870 ; 0.500
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 28
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 250
REMARK 3 ORIGIN FOR THE GROUP (A): 67.3224 -92.1866 46.1855
REMARK 3 T TENSOR
REMARK 3 T11: 0.1553 T22: 0.1569
REMARK 3 T33: 0.2100 T12: -0.0342
REMARK 3 T13: 0.0176 T23: -0.0418
REMARK 3 L TENSOR
REMARK 3 L11: 0.2579 L22: 0.1696
REMARK 3 L33: 0.1260 L12: -0.0757
REMARK 3 L13: 0.0913 L23: 0.0583
REMARK 3 S TENSOR
REMARK 3 S11: 0.0004 S12: 0.0416 S13: -0.0331
REMARK 3 S21: 0.0203 S22: 0.0328 S23: -0.0672
REMARK 3 S31: -0.0332 S32: -0.0184 S33: -0.0332
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): 60.1709 -88.0012 16.5113
REMARK 3 T TENSOR
REMARK 3 T11: 0.1836 T22: 0.1640
REMARK 3 T33: 0.1619 T12: -0.0519
REMARK 3 T13: 0.0907 T23: 0.0516
REMARK 3 L TENSOR
REMARK 3 L11: 0.1381 L22: 0.2010
REMARK 3 L33: 0.2109 L12: 0.0956
REMARK 3 L13: -0.0028 L23: 0.1630
REMARK 3 S TENSOR
REMARK 3 S11: -0.0640 S12: -0.0337 S13: -0.0393
REMARK 3 S21: -0.0857 S22: 0.0008 S23: 0.0096
REMARK 3 S31: -0.0628 S32: 0.0479 S33: 0.0632
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1 C 240
REMARK 3 ORIGIN FOR THE GROUP (A): 32.9225 -87.4516 1.0980
REMARK 3 T TENSOR
REMARK 3 T11: 0.2420 T22: 0.1435
REMARK 3 T33: 0.1359 T12: -0.0140
REMARK 3 T13: 0.0126 T23: 0.0771
REMARK 3 L TENSOR
REMARK 3 L11: 0.2218 L22: 0.2513
REMARK 3 L33: 0.4875 L12: 0.2278
REMARK 3 L13: 0.1277 L23: 0.1189
REMARK 3 S TENSOR
REMARK 3 S11: -0.0594 S12: 0.0246 S13: 0.0450
REMARK 3 S21: -0.1039 S22: 0.0734 S23: 0.0689
REMARK 3 S31: -0.0302 S32: 0.0938 S33: -0.0140
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): 3.5243 -90.0736 13.5211
REMARK 3 T TENSOR
REMARK 3 T11: 0.1608 T22: 0.0937
REMARK 3 T33: 0.3111 T12: 0.0339
REMARK 3 T13: -0.1033 T23: 0.0735
REMARK 3 L TENSOR
REMARK 3 L11: 0.1693 L22: 0.0738
REMARK 3 L33: 0.2312 L12: 0.0286
REMARK 3 L13: -0.1678 L23: -0.0069
REMARK 3 S TENSOR
REMARK 3 S11: -0.0219 S12: -0.0602 S13: 0.0280
REMARK 3 S21: -0.0693 S22: 0.0146 S23: 0.1467
REMARK 3 S31: -0.0284 S32: 0.0919 S33: 0.0073
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): -2.9262 -94.3011 45.5533
REMARK 3 T TENSOR
REMARK 3 T11: 0.0823 T22: 0.1049
REMARK 3 T33: 0.3238 T12: 0.0695
REMARK 3 T13: 0.0935 T23: 0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 0.0177 L22: 0.0648
REMARK 3 L33: 0.2654 L12: 0.0210
REMARK 3 L13: 0.0350 L23: -0.0027
REMARK 3 S TENSOR
REMARK 3 S11: -0.0104 S12: -0.0018 S13: -0.0137
REMARK 3 S21: 0.0279 S22: 0.0223 S23: 0.0737
REMARK 3 S31: -0.0727 S32: -0.0135 S33: -0.0118
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 2 F 244
REMARK 3 ORIGIN FOR THE GROUP (A): 15.4026 -94.9584 69.8215
REMARK 3 T TENSOR
REMARK 3 T11: 0.2265 T22: 0.1020
REMARK 3 T33: 0.1555 T12: 0.0135
REMARK 3 T13: 0.1551 T23: -0.0453
REMARK 3 L TENSOR
REMARK 3 L11: 0.2660 L22: 0.1050
REMARK 3 L33: 0.0759 L12: 0.0982
REMARK 3 L13: 0.0251 L23: 0.0505
REMARK 3 S TENSOR
REMARK 3 S11: -0.0038 S12: 0.0209 S13: 0.0554
REMARK 3 S21: 0.0790 S22: -0.0110 S23: 0.0759
REMARK 3 S31: 0.0378 S32: 0.0112 S33: 0.0148
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): 47.9573 -93.4698 71.2300
REMARK 3 T TENSOR
REMARK 3 T11: 0.2873 T22: 0.1290
REMARK 3 T33: 0.1081 T12: -0.0303
REMARK 3 T13: 0.0248 T23: -0.0340
REMARK 3 L TENSOR
REMARK 3 L11: 0.0942 L22: 0.2509
REMARK 3 L33: 0.2322 L12: 0.0821
REMARK 3 L13: 0.0516 L23: 0.0660
REMARK 3 S TENSOR
REMARK 3 S11: 0.0302 S12: 0.0753 S13: -0.0024
REMARK 3 S21: 0.1503 S22: -0.0229 S23: -0.0329
REMARK 3 S31: 0.0008 S32: -0.0142 S33: -0.0072
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 1 H 222
REMARK 3 ORIGIN FOR THE GROUP (A): 67.8030-130.2182 48.3453
REMARK 3 T TENSOR
REMARK 3 T11: 0.1612 T22: 0.1681
REMARK 3 T33: 0.2153 T12: 0.0026
REMARK 3 T13: -0.0186 T23: -0.0287
REMARK 3 L TENSOR
REMARK 3 L11: 0.0182 L22: 0.1269
REMARK 3 L33: 0.0259 L12: 0.0225
REMARK 3 L13: -0.0048 L23: 0.0345
REMARK 3 S TENSOR
REMARK 3 S11: 0.0387 S12: 0.0326 S13: -0.0132
REMARK 3 S21: 0.0754 S22: -0.0233 S23: -0.1244
REMARK 3 S31: 0.0037 S32: -0.0539 S33: -0.0155
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): 68.8058-127.6235 21.0816
REMARK 3 T TENSOR
REMARK 3 T11: 0.1123 T22: 0.1752
REMARK 3 T33: 0.2152 T12: -0.0097
REMARK 3 T13: 0.0741 T23: -0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 0.0938 L22: 0.7499
REMARK 3 L33: 0.1192 L12: -0.0500
REMARK 3 L13: -0.0913 L23: 0.0037
REMARK 3 S TENSOR
REMARK 3 S11: 0.0307 S12: 0.0167 S13: -0.0135
REMARK 3 S21: -0.0065 S22: -0.0400 S23: -0.1582
REMARK 3 S31: -0.0404 S32: -0.0794 S33: 0.0092
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): 45.2579-126.7076 -0.4459
REMARK 3 T TENSOR
REMARK 3 T11: 0.2488 T22: 0.1714
REMARK 3 T33: 0.0945 T12: 0.0029
REMARK 3 T13: 0.0662 T23: 0.0117
REMARK 3 L TENSOR
REMARK 3 L11: 0.0720 L22: 0.6209
REMARK 3 L33: 0.2269 L12: -0.0020
REMARK 3 L13: 0.0991 L23: 0.0262
REMARK 3 S TENSOR
REMARK 3 S11: 0.0061 S12: -0.0579 S13: 0.0146
REMARK 3 S21: -0.1742 S22: 0.0205 S23: 0.0161
REMARK 3 S31: -0.0086 S32: -0.0056 S33: -0.0266
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): 11.3601-130.9138 2.4893
REMARK 3 T TENSOR
REMARK 3 T11: 0.1904 T22: 0.1421
REMARK 3 T33: 0.2060 T12: 0.0108
REMARK 3 T13: -0.1115 T23: 0.0437
REMARK 3 L TENSOR
REMARK 3 L11: 0.1302 L22: 0.5979
REMARK 3 L33: 0.1567 L12: 0.1965
REMARK 3 L13: -0.0025 L23: 0.1189
REMARK 3 S TENSOR
REMARK 3 S11: 0.0136 S12: -0.0351 S13: 0.0254
REMARK 3 S21: -0.1406 S22: 0.0229 S23: 0.1718
REMARK 3 S31: -0.0162 S32: 0.0957 S33: -0.0365
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): -4.2038-134.2367 28.5761
REMARK 3 T TENSOR
REMARK 3 T11: 0.0761 T22: 0.1436
REMARK 3 T33: 0.3148 T12: 0.0143
REMARK 3 T13: -0.0078 T23: 0.0422
REMARK 3 L TENSOR
REMARK 3 L11: 0.2656 L22: 0.2860
REMARK 3 L33: 0.3159 L12: 0.0883
REMARK 3 L13: 0.2568 L23: -0.0018
REMARK 3 S TENSOR
REMARK 3 S11: 0.0629 S12: -0.0048 S13: -0.0084
REMARK 3 S21: -0.0097 S22: -0.0052 S23: 0.1642
REMARK 3 S31: 0.0471 S32: 0.0592 S33: -0.0577
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 223
REMARK 3 ORIGIN FOR THE GROUP (A): 7.9468-137.7978 60.4208
REMARK 3 T TENSOR
REMARK 3 T11: 0.1467 T22: 0.1484
REMARK 3 T33: 0.1892 T12: -0.0114
REMARK 3 T13: 0.1220 T23: 0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 0.2629 L22: 0.5916
REMARK 3 L33: 0.1935 L12: 0.0474
REMARK 3 L13: 0.0763 L23: 0.0279
REMARK 3 S TENSOR
REMARK 3 S11: 0.0588 S12: 0.0265 S13: 0.0191
REMARK 3 S21: 0.1309 S22: -0.0353 S23: 0.0877
REMARK 3 S31: 0.0381 S32: 0.0350 S33: -0.0236
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : N 1 N 196
REMARK 3 ORIGIN FOR THE GROUP (A): 40.0777-134.1508 70.7156
REMARK 3 T TENSOR
REMARK 3 T11: 0.2696 T22: 0.1559
REMARK 3 T33: 0.0668 T12: -0.0147
REMARK 3 T13: 0.0009 T23: -0.0346
REMARK 3 L TENSOR
REMARK 3 L11: 0.3892 L22: 0.5903
REMARK 3 L33: 0.0993 L12: 0.0029
REMARK 3 L13: -0.1702 L23: 0.0853
REMARK 3 S TENSOR
REMARK 3 S11: 0.0767 S12: 0.0710 S13: 0.0314
REMARK 3 S21: 0.1273 S22: -0.0368 S23: -0.0405
REMARK 3 S31: 0.0065 S32: -0.0031 S33: -0.0399
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): 2.0238-206.4586 36.9087
REMARK 3 T TENSOR
REMARK 3 T11: 0.1557 T22: 0.0892
REMARK 3 T33: 0.2572 T12: -0.0755
REMARK 3 T13: -0.0542 T23: 0.0608
REMARK 3 L TENSOR
REMARK 3 L11: 0.3845 L22: 0.2178
REMARK 3 L33: 0.2276 L12: -0.0506
REMARK 3 L13: -0.1493 L23: 0.2063
REMARK 3 S TENSOR
REMARK 3 S11: -0.0134 S12: 0.0726 S13: 0.0531
REMARK 3 S21: 0.0876 S22: 0.0069 S23: 0.0502
REMARK 3 S31: 0.0763 S32: 0.0001 S33: 0.0065
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : P 1 P 244
REMARK 3 ORIGIN FOR THE GROUP (A): 8.5492-205.3933 6.8284
REMARK 3 T TENSOR
REMARK 3 T11: 0.1974 T22: 0.1236
REMARK 3 T33: 0.2045 T12: -0.0225
REMARK 3 T13: -0.1054 T23: -0.0593
REMARK 3 L TENSOR
REMARK 3 L11: 0.1789 L22: 0.3037
REMARK 3 L33: 0.2703 L12: 0.1176
REMARK 3 L13: 0.1661 L23: -0.0509
REMARK 3 S TENSOR
REMARK 3 S11: -0.0435 S12: -0.0553 S13: 0.0310
REMARK 3 S21: -0.1196 S22: -0.0099 S23: -0.0133
REMARK 3 S31: 0.0278 S32: -0.0603 S33: 0.0534
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Q 1 Q 240
REMARK 3 ORIGIN FOR THE GROUP (A): 35.8940-203.4956 -8.9975
REMARK 3 T TENSOR
REMARK 3 T11: 0.3674 T22: 0.0583
REMARK 3 T33: 0.1471 T12: 0.0403
REMARK 3 T13: -0.1692 T23: -0.0754
REMARK 3 L TENSOR
REMARK 3 L11: 0.2600 L22: 0.3065
REMARK 3 L33: 0.3766 L12: 0.1504
REMARK 3 L13: 0.2391 L23: 0.0008
REMARK 3 S TENSOR
REMARK 3 S11: 0.0853 S12: -0.0204 S13: 0.0052
REMARK 3 S21: -0.1846 S22: -0.0310 S23: 0.1588
REMARK 3 S31: 0.0756 S32: 0.0500 S33: -0.0543
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): 65.3895-202.9700 3.4398
REMARK 3 T TENSOR
REMARK 3 T11: 0.2747 T22: 0.1435
REMARK 3 T33: 0.1661 T12: 0.0859
REMARK 3 T13: 0.1004 T23: -0.0577
REMARK 3 L TENSOR
REMARK 3 L11: 0.0993 L22: 0.2766
REMARK 3 L33: 0.2388 L12: -0.1010
REMARK 3 L13: 0.1269 L23: -0.0757
REMARK 3 S TENSOR
REMARK 3 S11: 0.0563 S12: -0.0651 S13: 0.0721
REMARK 3 S21: -0.2221 S22: -0.0594 S23: -0.1106
REMARK 3 S31: 0.0742 S32: -0.0784 S33: 0.0031
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): 72.3191-204.2103 35.4569
REMARK 3 T TENSOR
REMARK 3 T11: 0.0889 T22: 0.0799
REMARK 3 T33: 0.3812 T12: 0.0766
REMARK 3 T13: -0.1365 T23: -0.0887
REMARK 3 L TENSOR
REMARK 3 L11: 0.2017 L22: 0.1197
REMARK 3 L33: 0.2534 L12: 0.1314
REMARK 3 L13: -0.1945 L23: -0.0820
REMARK 3 S TENSOR
REMARK 3 S11: 0.0367 S12: 0.0754 S13: -0.0442
REMARK 3 S21: 0.0691 S22: 0.0761 S23: -0.1395
REMARK 3 S31: 0.0090 S32: -0.0508 S33: -0.1128
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): 54.2994-207.7746 59.7007
REMARK 3 T TENSOR
REMARK 3 T11: 0.2631 T22: 0.0741
REMARK 3 T33: 0.2585 T12: 0.0007
REMARK 3 T13: -0.2134 T23: 0.0781
REMARK 3 L TENSOR
REMARK 3 L11: 0.5300 L22: 0.1831
REMARK 3 L33: 0.0633 L12: 0.3111
REMARK 3 L13: 0.0449 L23: 0.0241
REMARK 3 S TENSOR
REMARK 3 S11: 0.1214 S12: -0.0515 S13: -0.1984
REMARK 3 S21: 0.0929 S22: -0.0490 S23: -0.1228
REMARK 3 S31: -0.0242 S32: -0.0672 S33: -0.0724
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): 21.8390-209.6951 61.2943
REMARK 3 T TENSOR
REMARK 3 T11: 0.2772 T22: 0.0813
REMARK 3 T33: 0.1593 T12: -0.0072
REMARK 3 T13: -0.0700 T23: 0.0592
REMARK 3 L TENSOR
REMARK 3 L11: 0.0823 L22: 0.2036
REMARK 3 L33: 0.2029 L12: -0.0811
REMARK 3 L13: 0.0028 L23: -0.0947
REMARK 3 S TENSOR
REMARK 3 S11: 0.0140 S12: 0.0225 S13: -0.0050
REMARK 3 S21: 0.0806 S22: 0.0231 S23: 0.0494
REMARK 3 S31: -0.0125 S32: 0.0393 S33: -0.0371
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : V 1 V 222
REMARK 3 ORIGIN FOR THE GROUP (A): 1.6542-169.4182 45.5256
REMARK 3 T TENSOR
REMARK 3 T11: 0.1514 T22: 0.1391
REMARK 3 T33: 0.2644 T12: -0.0087
REMARK 3 T13: -0.0002 T23: 0.0495
REMARK 3 L TENSOR
REMARK 3 L11: 0.0128 L22: 0.1637
REMARK 3 L33: 0.0199 L12: 0.0358
REMARK 3 L13: 0.0105 L23: 0.0048
REMARK 3 S TENSOR
REMARK 3 S11: 0.0197 S12: 0.0106 S13: 0.0243
REMARK 3 S21: 0.0175 S22: -0.0193 S23: 0.1401
REMARK 3 S31: 0.0245 S32: 0.0398 S33: -0.0004
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): 0.2870-167.2701 18.1785
REMARK 3 T TENSOR
REMARK 3 T11: 0.1343 T22: 0.1216
REMARK 3 T33: 0.2766 T12: -0.0202
REMARK 3 T13: -0.0900 T23: 0.0153
REMARK 3 L TENSOR
REMARK 3 L11: 0.0634 L22: 0.3932
REMARK 3 L33: 0.1062 L12: 0.0185
REMARK 3 L13: 0.0648 L23: 0.0535
REMARK 3 S TENSOR
REMARK 3 S11: 0.0041 S12: 0.0207 S13: 0.0162
REMARK 3 S21: 0.0381 S22: -0.0107 S23: 0.1600
REMARK 3 S31: 0.0353 S32: 0.0746 S33: 0.0066
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): 23.5312-164.4542 -3.5902
REMARK 3 T TENSOR
REMARK 3 T11: 0.2609 T22: 0.1262
REMARK 3 T33: 0.1155 T12: 0.0049
REMARK 3 T13: -0.0964 T23: -0.0292
REMARK 3 L TENSOR
REMARK 3 L11: 0.2713 L22: 0.6324
REMARK 3 L33: 0.1744 L12: -0.0673
REMARK 3 L13: 0.0558 L23: -0.0045
REMARK 3 S TENSOR
REMARK 3 S11: 0.0345 S12: -0.0726 S13: -0.0283
REMARK 3 S21: -0.1717 S22: 0.0133 S23: 0.0745
REMARK 3 S31: -0.0150 S32: 0.0726 S33: -0.0477
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): 57.4733-160.7918 -0.4450
REMARK 3 T TENSOR
REMARK 3 T11: 0.2038 T22: 0.1599
REMARK 3 T33: 0.1376 T12: 0.0323
REMARK 3 T13: 0.0955 T23: -0.0530
REMARK 3 L TENSOR
REMARK 3 L11: 0.1568 L22: 0.7854
REMARK 3 L33: 0.1376 L12: 0.1583
REMARK 3 L13: 0.1085 L23: -0.0297
REMARK 3 S TENSOR
REMARK 3 S11: 0.0306 S12: -0.0475 S13: -0.0161
REMARK 3 S21: -0.1614 S22: 0.0338 S23: -0.0777
REMARK 3 S31: 0.0337 S32: -0.0208 S33: -0.0644
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): 73.3601-161.9653 25.5676
REMARK 3 T TENSOR
REMARK 3 T11: 0.0920 T22: 0.1797
REMARK 3 T33: 0.2572 T12: 0.0301
REMARK 3 T13: 0.0178 T23: -0.0491
REMARK 3 L TENSOR
REMARK 3 L11: 0.0841 L22: 0.5488
REMARK 3 L33: 0.1237 L12: -0.0513
REMARK 3 L13: -0.0622 L23: -0.0697
REMARK 3 S TENSOR
REMARK 3 S11: 0.0406 S12: 0.0182 S13: 0.0052
REMARK 3 S21: 0.0299 S22: -0.0249 S23: -0.1678
REMARK 3 S31: -0.0179 S32: -0.0483 S33: -0.0156
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): 61.6797-163.9263 57.7276
REMARK 3 T TENSOR
REMARK 3 T11: 0.1859 T22: 0.1483
REMARK 3 T33: 0.1724 T12: 0.0124
REMARK 3 T13: -0.0962 T23: -0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 0.2734 L22: 0.7740
REMARK 3 L33: 0.0520 L12: -0.0439
REMARK 3 L13: 0.0788 L23: 0.0514
REMARK 3 S TENSOR
REMARK 3 S11: 0.0369 S12: 0.0473 S13: -0.0159
REMARK 3 S21: 0.1709 S22: -0.0385 S23: -0.1124
REMARK 3 S31: 0.0019 S32: -0.0437 S33: 0.0016
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): 29.7241-169.3731 67.7748
REMARK 3 T TENSOR
REMARK 3 T11: 0.2630 T22: 0.1383
REMARK 3 T33: 0.1046 T12: -0.0153
REMARK 3 T13: 0.0219 T23: 0.0456
REMARK 3 L TENSOR
REMARK 3 L11: 0.3508 L22: 0.5844
REMARK 3 L33: 0.1000 L12: 0.0045
REMARK 3 L13: 0.1343 L23: 0.1032
REMARK 3 S TENSOR
REMARK 3 S11: 0.0840 S12: 0.0823 S13: -0.0109
REMARK 3 S21: 0.1498 S22: -0.0294 S23: 0.0514
REMARK 3 S31: 0.0370 S32: -0.0028 S33: -0.0546
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 4Y80 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-FEB-15.
REMARK 100 THE DEPOSITION ID IS D_1000206971.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-APR-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : LN2 COOLED FIXED-EXIT. SI(111)
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 359973
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.57800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
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 150.07500
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: 34-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, c,
REMARK 350 AND CHAINS: d, e, f, g, h
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET B 0
REMARK 465 LYS B 245
REMARK 465 LYS B 246
REMARK 465 ASP B 247
REMARK 465 GLU B 248
REMARK 465 ASP B 249
REMARK 465 GLU B 250
REMARK 465 GLU B 251
REMARK 465 ALA B 252
REMARK 465 ASP B 253
REMARK 465 GLU B 254
REMARK 465 ASP B 255
REMARK 465 MET B 256
REMARK 465 LYS B 257
REMARK 465 MET C -1
REMARK 465 SER C 0
REMARK 465 GLN C 241
REMARK 465 GLN C 242
REMARK 465 GLU C 243
REMARK 465 GLN C 244
REMARK 465 ASP C 245
REMARK 465 LYS C 246
REMARK 465 LYS C 247
REMARK 465 LYS C 248
REMARK 465 LYS C 249
REMARK 465 SER C 250
REMARK 465 ASN C 251
REMARK 465 HIS C 252
REMARK 465 MET D -7
REMARK 465 PHE D -6
REMARK 465 LEU D -5
REMARK 465 THR D -4
REMARK 465 ARG D -3
REMARK 465 SER D -2
REMARK 465 GLU D -1
REMARK 465 TYR D 0
REMARK 465 GLY D 118
REMARK 465 ALA D 119
REMARK 465 SER D 120
REMARK 465 GLY D 121
REMARK 465 GLU D 122
REMARK 465 GLU D 123
REMARK 465 ARG D 124
REMARK 465 SER D 243
REMARK 465 PRO D 244
REMARK 465 GLU D 245
REMARK 465 GLU D 246
REMARK 465 ALA D 247
REMARK 465 ASP D 248
REMARK 465 VAL D 249
REMARK 465 GLU D 250
REMARK 465 MET D 251
REMARK 465 SER D 252
REMARK 465 MET E 0
REMARK 465 PHE E 1
REMARK 465 ARG E 2
REMARK 465 MET F -3
REMARK 465 THR F -2
REMARK 465 SER F -1
REMARK 465 ILE F 0
REMARK 465 GLY F 1
REMARK 465 GLY F 245
REMARK 465 ASP F 246
REMARK 465 ASP F 247
REMARK 465 ASP F 248
REMARK 465 GLU F 249
REMARK 465 ASP F 250
REMARK 465 GLU F 251
REMARK 465 ASP F 252
REMARK 465 ASP F 253
REMARK 465 SER F 254
REMARK 465 ASP F 255
REMARK 465 ASN F 256
REMARK 465 VAL F 257
REMARK 465 MET F 258
REMARK 465 SER F 259
REMARK 465 SER F 260
REMARK 465 ASP F 261
REMARK 465 ASP F 262
REMARK 465 GLU F 263
REMARK 465 ASN F 264
REMARK 465 ALA F 265
REMARK 465 PRO F 266
REMARK 465 VAL F 267
REMARK 465 ALA F 268
REMARK 465 THR F 269
REMARK 465 ASN F 270
REMARK 465 ALA F 271
REMARK 465 ASN F 272
REMARK 465 ALA F 273
REMARK 465 THR F 274
REMARK 465 THR F 275
REMARK 465 ASP F 276
REMARK 465 GLN F 277
REMARK 465 GLU F 278
REMARK 465 GLY F 279
REMARK 465 ASP F 280
REMARK 465 ILE F 281
REMARK 465 HIS F 282
REMARK 465 LEU F 283
REMARK 465 GLU F 284
REMARK 465 MET G -8
REMARK 465 SER G -7
REMARK 465 GLY G -6
REMARK 465 ALA G -5
REMARK 465 ALA G -4
REMARK 465 ALA G -3
REMARK 465 ALA G -2
REMARK 465 SER G -1
REMARK 465 ALA G 0
REMARK 465 ALA G 1
REMARK 465 ASP G 243
REMARK 465 ILE H 223
REMARK 465 GLN H 224
REMARK 465 GLU H 225
REMARK 465 GLU H 226
REMARK 465 GLN H 227
REMARK 465 VAL H 228
REMARK 465 ASP H 229
REMARK 465 ILE H 230
REMARK 465 THR H 231
REMARK 465 ALA H 232
REMARK 465 MET I 0
REMARK 465 GLN J 196
REMARK 465 ALA J 197
REMARK 465 GLN J 198
REMARK 465 THR M -12
REMARK 465 GLN M -11
REMARK 465 ILE M -10
REMARK 465 ALA M -9
REMARK 465 ASN M -8
REMARK 465 ALA M -7
REMARK 465 GLY M -6
REMARK 465 ALA M -5
REMARK 465 SER M -4
REMARK 465 PRO M -3
REMARK 465 MET M -2
REMARK 465 VAL M -1
REMARK 465 ASN M 0
REMARK 465 ILE M 233
REMARK 465 MET P 0
REMARK 465 LYS P 245
REMARK 465 LYS P 246
REMARK 465 ASP P 247
REMARK 465 GLU P 248
REMARK 465 ASP P 249
REMARK 465 GLU P 250
REMARK 465 GLU P 251
REMARK 465 ALA P 252
REMARK 465 ASP P 253
REMARK 465 GLU P 254
REMARK 465 ASP P 255
REMARK 465 MET P 256
REMARK 465 LYS P 257
REMARK 465 MET Q -1
REMARK 465 SER Q 0
REMARK 465 GLN Q 241
REMARK 465 GLN Q 242
REMARK 465 GLU Q 243
REMARK 465 GLN Q 244
REMARK 465 ASP Q 245
REMARK 465 LYS Q 246
REMARK 465 LYS Q 247
REMARK 465 LYS Q 248
REMARK 465 LYS Q 249
REMARK 465 SER Q 250
REMARK 465 ASN Q 251
REMARK 465 HIS Q 252
REMARK 465 MET R -7
REMARK 465 PHE R -6
REMARK 465 LEU R -5
REMARK 465 THR R -4
REMARK 465 ARG R -3
REMARK 465 SER R -2
REMARK 465 GLU R -1
REMARK 465 TYR R 0
REMARK 465 GLY R 118
REMARK 465 ALA R 119
REMARK 465 SER R 120
REMARK 465 GLY R 121
REMARK 465 GLU R 122
REMARK 465 GLU R 123
REMARK 465 ARG R 124
REMARK 465 SER R 243
REMARK 465 PRO R 244
REMARK 465 GLU R 245
REMARK 465 GLU R 246
REMARK 465 ALA R 247
REMARK 465 ASP R 248
REMARK 465 VAL R 249
REMARK 465 GLU R 250
REMARK 465 MET R 251
REMARK 465 SER R 252
REMARK 465 MET S 0
REMARK 465 PHE S 1
REMARK 465 ARG S 2
REMARK 465 MET T -3
REMARK 465 THR T -2
REMARK 465 SER T -1
REMARK 465 ILE T 0
REMARK 465 GLY T 1
REMARK 465 GLY T 245
REMARK 465 ASP T 246
REMARK 465 ASP T 247
REMARK 465 ASP T 248
REMARK 465 GLU T 249
REMARK 465 ASP T 250
REMARK 465 GLU T 251
REMARK 465 ASP T 252
REMARK 465 ASP T 253
REMARK 465 SER T 254
REMARK 465 ASP T 255
REMARK 465 ASN T 256
REMARK 465 VAL T 257
REMARK 465 MET T 258
REMARK 465 SER T 259
REMARK 465 SER T 260
REMARK 465 ASP T 261
REMARK 465 ASP T 262
REMARK 465 GLU T 263
REMARK 465 ASN T 264
REMARK 465 ALA T 265
REMARK 465 PRO T 266
REMARK 465 VAL T 267
REMARK 465 ALA T 268
REMARK 465 THR T 269
REMARK 465 ASN T 270
REMARK 465 ALA T 271
REMARK 465 ASN T 272
REMARK 465 ALA T 273
REMARK 465 THR T 274
REMARK 465 THR T 275
REMARK 465 ASP T 276
REMARK 465 GLN T 277
REMARK 465 GLU T 278
REMARK 465 GLY T 279
REMARK 465 ASP T 280
REMARK 465 ILE T 281
REMARK 465 HIS T 282
REMARK 465 LEU T 283
REMARK 465 GLU T 284
REMARK 465 MET U -8
REMARK 465 SER U -7
REMARK 465 GLY U -6
REMARK 465 ALA U -5
REMARK 465 ALA U -4
REMARK 465 ALA U -3
REMARK 465 ALA U -2
REMARK 465 SER U -1
REMARK 465 ALA U 0
REMARK 465 ALA U 1
REMARK 465 ASP U 243
REMARK 465 ILE V 223
REMARK 465 GLN V 224
REMARK 465 GLU V 225
REMARK 465 GLU V 226
REMARK 465 GLN V 227
REMARK 465 VAL V 228
REMARK 465 ASP V 229
REMARK 465 ILE V 230
REMARK 465 THR V 231
REMARK 465 ALA V 232
REMARK 465 MET W 0
REMARK 465 GLN X 196
REMARK 465 ALA X 197
REMARK 465 GLN X 198
REMARK 465 THR a -12
REMARK 465 GLN a -11
REMARK 465 ILE a -10
REMARK 465 ALA a -9
REMARK 465 ASN a -8
REMARK 465 ALA a -7
REMARK 465 GLY a -6
REMARK 465 ALA a -5
REMARK 465 SER a -4
REMARK 465 PRO a -3
REMARK 465 MET a -2
REMARK 465 VAL a -1
REMARK 465 ASN a 0
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OG1 THR K 1 O IL0 d 4 2.17
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 LYS K 32 CB - CG - CD ANGL. DEV. = 21.5 DEGREES
REMARK 500 LYS Y 32 CB - CG - CD ANGL. DEV. = 22.8 DEGREES
REMARK 500 HIS Z 108 CA - C - O ANGL. DEV. = 13.9 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 2 150.66 68.72
REMARK 500 ASP A 3 98.29 -58.89
REMARK 500 TYR A 97 -62.63 -147.50
REMARK 500 ALA A 249 54.73 -91.00
REMARK 500 ARG B 8 71.28 56.97
REMARK 500 THR B 10 52.67 -118.47
REMARK 500 VAL B 51 105.31 -13.16
REMARK 500 GLU B 63 -39.64 -135.44
REMARK 500 ALA B 219 -158.17 -79.07
REMARK 500 ASP B 221 108.39 69.53
REMARK 500 ASN C 38 21.65 -141.38
REMARK 500 PRO C 183 109.85 -40.60
REMARK 500 GLN C 202 -101.75 139.00
REMARK 500 ALA C 205 -119.42 -81.75
REMARK 500 LYS C 206 41.82 -89.25
REMARK 500 GLN C 239 82.22 -68.81
REMARK 500 ARG D 45 76.75 57.02
REMARK 500 SER E 39 -154.31 -108.00
REMARK 500 ASP E 137 -159.15 -128.94
REMARK 500 ASP E 202 -22.40 65.45
REMARK 500 SER F 9 -2.70 82.70
REMARK 500 ASP F 67 -134.08 57.41
REMARK 500 LYS F 100 -56.29 74.01
REMARK 500 ASN F 203 40.39 -156.46
REMARK 500 LYS G 165 46.20 -102.39
REMARK 500 GLU G 241 36.88 -85.56
REMARK 500 ASN H 9 -69.12 -29.92
REMARK 500 ASN H 30 57.91 -150.38
REMARK 500 ASP H 145 60.05 63.78
REMARK 500 SER H 171 -113.53 64.42
REMARK 500 GLN I 31 -111.15 52.44
REMARK 500 ARG I 97 48.35 -104.40
REMARK 500 ASP I 134 -67.39 -104.81
REMARK 500 ASP I 192 38.10 -145.14
REMARK 500 GLN I 203 41.23 -109.04
REMARK 500 ASP J 2 -72.76 143.17
REMARK 500 VAL J 9 -166.02 -112.07
REMARK 500 SER J 31 29.89 -141.44
REMARK 500 LYS J 34 58.47 -91.19
REMARK 500 ASP L 32 -116.96 54.09
REMARK 500 LYS L 100 42.97 -108.35
REMARK 500 PHE L 103 69.21 -160.24
REMARK 500 ASP L 200 -62.95 70.12
REMARK 500 ILE M 5 -80.35 -104.41
REMARK 500 THR M 9 -152.19 -88.73
REMARK 500 ALA M 83 -116.39 -139.13
REMARK 500 LYS N 107 -140.96 58.41
REMARK 500 THR O 2 150.81 68.66
REMARK 500 ASP O 3 98.47 -59.07
REMARK 500 TYR O 97 -63.04 -147.88
REMARK 500
REMARK 500 THIS ENTRY HAS 94 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG G 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR G 8 OG1
REMARK 620 2 TYR G 119 O 82.0
REMARK 620 3 ARG G 122 O 85.0 79.9
REMARK 620 4 MET G 125 O 163.8 81.9 94.0
REMARK 620 5 HOH G 424 O 79.8 144.4 128.1 112.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG I 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA I 174 O
REMARK 620 2 ASP I 177 O 67.8
REMARK 620 3 SER I 180 O 83.0 78.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG I 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP I 204 O
REMARK 620 2 ALA Y 165 O 103.7
REMARK 620 3 ASP Y 168 O 159.0 96.5
REMARK 620 4 SER Y 171 O 95.4 91.4 89.7
REMARK 620 5 HOH Y 313 O 83.7 93.0 89.6 175.6
REMARK 620 N 1 2 3 4
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 99.5
REMARK 620 3 SER K 171 O 88.4 86.4
REMARK 620 4 ASP W 204 O 102.4 157.5 89.2
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 94.6
REMARK 620 3 ASP V 166 O 141.3 122.7
REMARK 620 4 SER V 169 O 87.5 92.8 81.3
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 ASP N 166 O 75.4
REMARK 620 3 SER N 169 O 105.5 75.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG Z 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR Z 192 O
REMARK 620 2 HIS Z 195 O 81.1
REMARK 620 3 VAL Z 198 O 103.2 80.6
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG G 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL G 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES H 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG I 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG I 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG K 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG L 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG N 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL N 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL U 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG Z 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL b 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES d 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES g 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Ligand residues IL0 AA 4
REMARK 800 through POL AA 5 bound to THR H 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Ligand POL AA 5 bound to THR H
REMARK 800 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Ligand residues IL0 AB 4
REMARK 800 through POL AB 5 bound to THR K 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Ligand POL AB 5 bound to THR K
REMARK 800 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Ligand residues IL0 AC 4
REMARK 800 through POL AC 5 bound to THR N 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Ligand POL AC 5 bound to THR N
REMARK 800 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Ligand residues IL0 AD 4
REMARK 800 through POL AD 5 bound to THR V 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Ligand POL AD 5 bound to THR V
REMARK 800 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Ligand residues IL0 AE 4
REMARK 800 through POL AE 5 bound to THR Y 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Ligand POL AE 5 bound to THR Y
REMARK 800 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Ligand residues IL0 AF 4
REMARK 800 through POL AF 5 bound to THR b 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Ligand POL AF 5 bound to THR b
REMARK 800 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ACE AA 1 and LEU AA
REMARK 800 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ACE AB 1 and LEU AB
REMARK 800 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ACE AC 1 and LEU AC
REMARK 800 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ACE AD 1 and LEU AD
REMARK 800 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ACE AE 1 and LEU AE
REMARK 800 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ACE AF 1 and LEU AF
REMARK 800 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1RYP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE 20S PROTEASOME FROM YEAST AT 2.4 ANGSTROMS
REMARK 900 RESOLUTION
DBREF 4Y80 A 1 250 UNP P23639 PSA2_YEAST 1 250
DBREF 4Y80 B 0 257 UNP P23638 PSA3_YEAST 1 258
DBREF 4Y80 C -1 252 UNP P40303 PSA4_YEAST 1 254
DBREF 4Y80 D -7 252 UNP P32379 PSA5_YEAST 1 260
DBREF 4Y80 E 0 233 UNP P40302 PSA6_YEAST 1 234
DBREF 4Y80 F -3 284 UNP P21242 PSA7_YEAST 1 288
DBREF 4Y80 G -8 243 UNP P21243 PSA1_YEAST 1 252
DBREF 4Y80 H 1 232 UNP P25043 PSB2_YEAST 30 261
DBREF 4Y80 I 0 204 UNP P25451 PSB3_YEAST 1 205
DBREF 4Y80 J 1 198 UNP P22141 PSB4_YEAST 1 198
DBREF 4Y80 K 1 212 UNP P30656 PSB5_YEAST 76 287
DBREF 4Y80 L 1 222 UNP P23724 PSB6_YEAST 20 241
DBREF 4Y80 M -12 233 UNP P30657 PSB7_YEAST 21 266
DBREF 4Y80 N 1 196 UNP P38624 PSB1_YEAST 20 215
DBREF 4Y80 O 1 250 UNP P23639 PSA2_YEAST 1 250
DBREF 4Y80 P 0 257 UNP P23638 PSA3_YEAST 1 258
DBREF 4Y80 Q -1 252 UNP P40303 PSA4_YEAST 1 254
DBREF 4Y80 R -7 252 UNP P32379 PSA5_YEAST 1 260
DBREF 4Y80 S 0 233 UNP P40302 PSA6_YEAST 1 234
DBREF 4Y80 T -3 284 UNP P21242 PSA7_YEAST 1 288
DBREF 4Y80 U -8 243 UNP P21243 PSA1_YEAST 1 252
DBREF 4Y80 V 1 232 UNP P25043 PSB2_YEAST 30 261
DBREF 4Y80 W 0 204 UNP P25451 PSB3_YEAST 1 205
DBREF 4Y80 X 1 198 UNP P22141 PSB4_YEAST 1 198
DBREF 4Y80 Y 1 212 UNP P30656 PSB5_YEAST 76 287
DBREF 4Y80 Z 1 222 UNP P23724 PSB6_YEAST 20 241
DBREF 4Y80 a -12 233 UNP P30657 PSB7_YEAST 21 266
DBREF 4Y80 b 1 196 UNP P38624 PSB1_YEAST 20 215
DBREF 4Y80 c 1 4 PDB 4Y80 4Y80 1 4
DBREF 4Y80 d 1 4 PDB 4Y80 4Y80 1 4
DBREF 4Y80 e 1 4 PDB 4Y80 4Y80 1 4
DBREF 4Y80 f 1 4 PDB 4Y80 4Y80 1 4
DBREF 4Y80 g 1 4 PDB 4Y80 4Y80 1 4
DBREF 4Y80 h 1 4 PDB 4Y80 4Y80 1 4
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 LYS VAL ILE GLU ILE ASN PRO
SEQRES 4 K 212 PHE LEU LEU GLY THR MET ALA GLY GLY ALA ALA ASP CYS
SEQRES 5 K 212 GLN PHE TRP GLU THR TRP LEU GLY SER GLN CYS ARG LEU
SEQRES 6 K 212 HIS GLU LEU ARG GLU LYS GLU ARG ILE SER VAL ALA ALA
SEQRES 7 K 212 ALA SER LYS ILE LEU SER ASN LEU VAL TYR GLN TYR LYS
SEQRES 8 K 212 GLY ALA GLY LEU SER MET GLY THR MET ILE CYS GLY TYR
SEQRES 9 K 212 THR ARG LYS GLU GLY PRO THR ILE TYR TYR VAL ASP SER
SEQRES 10 K 212 ASP GLY THR ARG LEU LYS GLY ASP ILE PHE CYS VAL GLY
SEQRES 11 K 212 SER GLY GLN THR PHE ALA TYR GLY VAL LEU ASP SER ASN
SEQRES 12 K 212 TYR LYS TRP ASP LEU SER VAL GLU ASP ALA LEU TYR LEU
SEQRES 13 K 212 GLY LYS ARG SER ILE LEU ALA ALA ALA HIS ARG ASP ALA
SEQRES 14 K 212 TYR SER GLY GLY SER VAL ASN LEU TYR HIS VAL THR GLU
SEQRES 15 K 212 ASP GLY TRP ILE TYR HIS GLY ASN HIS ASP VAL GLY GLU
SEQRES 16 K 212 LEU PHE TRP LYS VAL LYS GLU GLU GLU GLY SER PHE ASN
SEQRES 17 K 212 ASN VAL ILE GLY
SEQRES 1 L 222 GLN PHE ASN PRO TYR GLY ASP ASN GLY GLY THR ILE LEU
SEQRES 2 L 222 GLY ILE ALA GLY GLU ASP PHE ALA VAL LEU ALA GLY ASP
SEQRES 3 L 222 THR ARG ASN ILE THR ASP TYR SER ILE ASN SER ARG TYR
SEQRES 4 L 222 GLU PRO LYS VAL PHE ASP CYS GLY ASP ASN ILE VAL MET
SEQRES 5 L 222 SER ALA ASN GLY PHE ALA ALA ASP GLY ASP ALA LEU VAL
SEQRES 6 L 222 LYS ARG PHE LYS ASN SER VAL LYS TRP TYR HIS PHE ASP
SEQRES 7 L 222 HIS ASN ASP LYS LYS LEU SER ILE ASN SER ALA ALA ARG
SEQRES 8 L 222 ASN ILE GLN HIS LEU LEU TYR GLY LYS ARG PHE PHE PRO
SEQRES 9 L 222 TYR TYR VAL HIS THR ILE ILE ALA GLY LEU ASP GLU ASP
SEQRES 10 L 222 GLY LYS GLY ALA VAL TYR SER PHE ASP PRO VAL GLY SER
SEQRES 11 L 222 TYR GLU ARG GLU GLN CYS ARG ALA GLY GLY ALA ALA ALA
SEQRES 12 L 222 SER LEU ILE MET PRO PHE LEU ASP ASN GLN VAL ASN PHE
SEQRES 13 L 222 LYS ASN GLN TYR GLU PRO GLY THR ASN GLY LYS VAL LYS
SEQRES 14 L 222 LYS PRO LEU LYS TYR LEU SER VAL GLU GLU VAL ILE LYS
SEQRES 15 L 222 LEU VAL ARG ASP SER PHE THR SER ALA THR GLU ARG HIS
SEQRES 16 L 222 ILE GLN VAL GLY ASP GLY LEU GLU ILE LEU ILE VAL THR
SEQRES 17 L 222 LYS ASP GLY VAL ARG LYS GLU PHE TYR GLU LEU LYS ARG
SEQRES 18 L 222 ASP
SEQRES 1 M 246 THR GLN ILE ALA ASN ALA GLY ALA SER PRO MET VAL ASN
SEQRES 2 M 246 THR GLN GLN PRO ILE VAL THR GLY THR SER VAL ILE SER
SEQRES 3 M 246 MET LYS TYR ASP ASN GLY VAL ILE ILE ALA ALA ASP ASN
SEQRES 4 M 246 LEU GLY SER TYR GLY SER LEU LEU ARG PHE ASN GLY VAL
SEQRES 5 M 246 GLU ARG LEU ILE PRO VAL GLY ASP ASN THR VAL VAL GLY
SEQRES 6 M 246 ILE SER GLY ASP ILE SER ASP MET GLN HIS ILE GLU ARG
SEQRES 7 M 246 LEU LEU LYS ASP LEU VAL THR GLU ASN ALA TYR ASP ASN
SEQRES 8 M 246 PRO LEU ALA ASP ALA GLU GLU ALA LEU GLU PRO SER TYR
SEQRES 9 M 246 ILE PHE GLU TYR LEU ALA THR VAL MET TYR GLN ARG ARG
SEQRES 10 M 246 SER LYS MET ASN PRO LEU TRP ASN ALA ILE ILE VAL ALA
SEQRES 11 M 246 GLY VAL GLN SER ASN GLY ASP GLN PHE LEU ARG TYR VAL
SEQRES 12 M 246 ASN LEU LEU GLY VAL THR TYR SER SER PRO THR LEU ALA
SEQRES 13 M 246 THR GLY PHE GLY ALA HIS MET ALA ASN PRO LEU LEU ARG
SEQRES 14 M 246 LYS VAL VAL ASP ARG GLU SER ASP ILE PRO LYS THR THR
SEQRES 15 M 246 VAL GLN VAL ALA GLU GLU ALA ILE VAL ASN ALA MET ARG
SEQRES 16 M 246 VAL LEU TYR TYR ARG ASP ALA ARG SER SER ARG ASN PHE
SEQRES 17 M 246 SER LEU ALA ILE ILE ASP LYS ASN THR GLY LEU THR PHE
SEQRES 18 M 246 LYS LYS ASN LEU GLN VAL GLU ASN MET LYS TRP ASP PHE
SEQRES 19 M 246 ALA LYS ASP ILE LYS GLY TYR GLY THR GLN LYS ILE
SEQRES 1 N 196 THR SER ILE MET ALA VAL THR PHE LYS ASP GLY VAL ILE
SEQRES 2 N 196 LEU GLY ALA ASP SER ARG THR THR THR GLY ALA TYR ILE
SEQRES 3 N 196 ALA ASN ARG VAL THR ASP LYS LEU THR ARG VAL HIS ASP
SEQRES 4 N 196 LYS ILE TRP CYS CYS ARG SER GLY SER ALA ALA ASP THR
SEQRES 5 N 196 GLN ALA ILE ALA ASP ILE VAL GLN TYR HIS LEU GLU LEU
SEQRES 6 N 196 TYR THR SER GLN TYR GLY THR PRO SER THR GLU THR ALA
SEQRES 7 N 196 ALA SER VAL PHE LYS GLU LEU CYS TYR GLU ASN LYS ASP
SEQRES 8 N 196 ASN LEU THR ALA GLY ILE ILE VAL ALA GLY TYR ASP ASP
SEQRES 9 N 196 LYS ASN LYS GLY GLU VAL TYR THR ILE PRO LEU GLY GLY
SEQRES 10 N 196 SER VAL HIS LYS LEU PRO TYR ALA ILE ALA GLY SER GLY
SEQRES 11 N 196 SER THR PHE ILE TYR GLY TYR CYS ASP LYS ASN PHE ARG
SEQRES 12 N 196 GLU ASN MET SER LYS GLU GLU THR VAL ASP PHE ILE LYS
SEQRES 13 N 196 HIS SER LEU SER GLN ALA ILE LYS TRP ASP GLY SER SER
SEQRES 14 N 196 GLY GLY VAL ILE ARG MET VAL VAL LEU THR ALA ALA GLY
SEQRES 15 N 196 VAL GLU ARG LEU ILE PHE TYR PRO ASP GLU TYR GLU GLN
SEQRES 16 N 196 LEU
SEQRES 1 O 250 MET THR ASP ARG TYR SER PHE SER LEU THR THR PHE SER
SEQRES 2 O 250 PRO SER GLY LYS LEU GLY GLN ILE ASP TYR ALA LEU THR
SEQRES 3 O 250 ALA VAL LYS GLN GLY VAL THR SER LEU GLY ILE LYS ALA
SEQRES 4 O 250 THR ASN GLY VAL VAL ILE ALA THR GLU LYS LYS SER SER
SEQRES 5 O 250 SER PRO LEU ALA MET SER GLU THR LEU SER LYS VAL SER
SEQRES 6 O 250 LEU LEU THR PRO ASP ILE GLY ALA VAL TYR SER GLY MET
SEQRES 7 O 250 GLY PRO ASP TYR ARG VAL LEU VAL ASP LYS SER ARG LYS
SEQRES 8 O 250 VAL ALA HIS THR SER TYR LYS ARG ILE TYR GLY GLU TYR
SEQRES 9 O 250 PRO PRO THR LYS LEU LEU VAL SER GLU VAL ALA LYS ILE
SEQRES 10 O 250 MET GLN GLU ALA THR GLN SER GLY GLY VAL ARG PRO PHE
SEQRES 11 O 250 GLY VAL SER LEU LEU ILE ALA GLY HIS ASP GLU PHE ASN
SEQRES 12 O 250 GLY PHE SER LEU TYR GLN VAL ASP PRO SER GLY SER TYR
SEQRES 13 O 250 PHE PRO TRP LYS ALA THR ALA ILE GLY LYS GLY SER VAL
SEQRES 14 O 250 ALA ALA LYS THR PHE LEU GLU LYS ARG TRP ASN ASP GLU
SEQRES 15 O 250 LEU GLU LEU GLU ASP ALA ILE HIS ILE ALA LEU LEU THR
SEQRES 16 O 250 LEU LYS GLU SER VAL GLU GLY GLU PHE ASN GLY ASP THR
SEQRES 17 O 250 ILE GLU LEU ALA ILE ILE GLY ASP GLU ASN PRO ASP LEU
SEQRES 18 O 250 LEU GLY TYR THR GLY ILE PRO THR ASP LYS GLY PRO ARG
SEQRES 19 O 250 PHE ARG LYS LEU THR SER GLN GLU ILE ASN ASP ARG LEU
SEQRES 20 O 250 GLU ALA LEU
SEQRES 1 P 258 MET GLY SER ARG ARG TYR ASP SER ARG THR THR ILE PHE
SEQRES 2 P 258 SER PRO GLU GLY ARG LEU TYR GLN VAL GLU TYR ALA LEU
SEQRES 3 P 258 GLU SER ILE SER HIS ALA GLY THR ALA ILE GLY ILE MET
SEQRES 4 P 258 ALA SER ASP GLY ILE VAL LEU ALA ALA GLU ARG LYS VAL
SEQRES 5 P 258 THR SER THR LEU LEU GLU GLN ASP THR SER THR GLU LYS
SEQRES 6 P 258 LEU TYR LYS LEU ASN ASP LYS ILE ALA VAL ALA VAL ALA
SEQRES 7 P 258 GLY LEU THR ALA ASP ALA GLU ILE LEU ILE ASN THR ALA
SEQRES 8 P 258 ARG ILE HIS ALA GLN ASN TYR LEU LYS THR TYR ASN GLU
SEQRES 9 P 258 ASP ILE PRO VAL GLU ILE LEU VAL ARG ARG LEU SER ASP
SEQRES 10 P 258 ILE LYS GLN GLY TYR THR GLN HIS GLY GLY LEU ARG PRO
SEQRES 11 P 258 PHE GLY VAL SER PHE ILE TYR ALA GLY TYR ASP ASP ARG
SEQRES 12 P 258 TYR GLY TYR GLN LEU TYR THR SER ASN PRO SER GLY ASN
SEQRES 13 P 258 TYR THR GLY TRP LYS ALA ILE SER VAL GLY ALA ASN THR
SEQRES 14 P 258 SER ALA ALA GLN THR LEU LEU GLN MET ASP TYR LYS ASP
SEQRES 15 P 258 ASP MET LYS VAL ASP ASP ALA ILE GLU LEU ALA LEU LYS
SEQRES 16 P 258 THR LEU SER LYS THR THR ASP SER SER ALA LEU THR TYR
SEQRES 17 P 258 ASP ARG LEU GLU PHE ALA THR ILE ARG LYS GLY ALA ASN
SEQRES 18 P 258 ASP GLY GLU VAL TYR GLN LYS ILE PHE LYS PRO GLN GLU
SEQRES 19 P 258 ILE LYS ASP ILE LEU VAL LYS THR GLY ILE THR LYS LYS
SEQRES 20 P 258 ASP GLU ASP GLU GLU ALA ASP GLU ASP MET LYS
SEQRES 1 Q 254 MET SER GLY TYR ASP ARG ALA LEU SER ILE PHE SER PRO
SEQRES 2 Q 254 ASP GLY HIS ILE PHE GLN VAL GLU TYR ALA LEU GLU ALA
SEQRES 3 Q 254 VAL LYS ARG GLY THR CYS ALA VAL GLY VAL LYS GLY LYS
SEQRES 4 Q 254 ASN CYS VAL VAL LEU GLY CYS GLU ARG ARG SER THR LEU
SEQRES 5 Q 254 LYS LEU GLN ASP THR ARG ILE THR PRO SER LYS VAL SER
SEQRES 6 Q 254 LYS ILE ASP SER HIS VAL VAL LEU SER PHE SER GLY LEU
SEQRES 7 Q 254 ASN ALA ASP SER ARG ILE LEU ILE GLU LYS ALA ARG VAL
SEQRES 8 Q 254 GLU ALA GLN SER HIS ARG LEU THR LEU GLU ASP PRO VAL
SEQRES 9 Q 254 THR VAL GLU TYR LEU THR ARG TYR VAL ALA GLY VAL GLN
SEQRES 10 Q 254 GLN ARG TYR THR GLN SER GLY GLY VAL ARG PRO PHE GLY
SEQRES 11 Q 254 VAL SER THR LEU ILE ALA GLY PHE ASP PRO ARG ASP ASP
SEQRES 12 Q 254 GLU PRO LYS LEU TYR GLN THR GLU PRO SER GLY ILE TYR
SEQRES 13 Q 254 SER SER TRP SER ALA GLN THR ILE GLY ARG ASN SER LYS
SEQRES 14 Q 254 THR VAL ARG GLU PHE LEU GLU LYS ASN TYR ASP ARG LYS
SEQRES 15 Q 254 GLU PRO PRO ALA THR VAL GLU GLU CYS VAL LYS LEU THR
SEQRES 16 Q 254 VAL ARG SER LEU LEU GLU VAL VAL GLN THR GLY ALA LYS
SEQRES 17 Q 254 ASN ILE GLU ILE THR VAL VAL LYS PRO ASP SER ASP ILE
SEQRES 18 Q 254 VAL ALA LEU SER SER GLU GLU ILE ASN GLN TYR VAL THR
SEQRES 19 Q 254 GLN ILE GLU GLN GLU LYS GLN GLU GLN GLN GLU GLN ASP
SEQRES 20 Q 254 LYS LYS LYS LYS SER ASN HIS
SEQRES 1 R 260 MET PHE LEU THR ARG SER GLU TYR ASP ARG GLY VAL SER
SEQRES 2 R 260 THR PHE SER PRO GLU GLY ARG LEU PHE GLN VAL GLU TYR
SEQRES 3 R 260 SER LEU GLU ALA ILE LYS LEU GLY SER THR ALA ILE GLY
SEQRES 4 R 260 ILE ALA THR LYS GLU GLY VAL VAL LEU GLY VAL GLU LYS
SEQRES 5 R 260 ARG ALA THR SER PRO LEU LEU GLU SER ASP SER ILE GLU
SEQRES 6 R 260 LYS ILE VAL GLU ILE ASP ARG HIS ILE GLY CYS ALA MET
SEQRES 7 R 260 SER GLY LEU THR ALA ASP ALA ARG SER MET ILE GLU HIS
SEQRES 8 R 260 ALA ARG THR ALA ALA VAL THR HIS ASN LEU TYR TYR ASP
SEQRES 9 R 260 GLU ASP ILE ASN VAL GLU SER LEU THR GLN SER VAL CYS
SEQRES 10 R 260 ASP LEU ALA LEU ARG PHE GLY GLU GLY ALA SER GLY GLU
SEQRES 11 R 260 GLU ARG LEU MET SER ARG PRO PHE GLY VAL ALA LEU LEU
SEQRES 12 R 260 ILE ALA GLY HIS ASP ALA ASP ASP GLY TYR GLN LEU PHE
SEQRES 13 R 260 HIS ALA GLU PRO SER GLY THR PHE TYR ARG TYR ASN ALA
SEQRES 14 R 260 LYS ALA ILE GLY SER GLY SER GLU GLY ALA GLN ALA GLU
SEQRES 15 R 260 LEU LEU ASN GLU TRP HIS SER SER LEU THR LEU LYS GLU
SEQRES 16 R 260 ALA GLU LEU LEU VAL LEU LYS ILE LEU LYS GLN VAL MET
SEQRES 17 R 260 GLU GLU LYS LEU ASP GLU ASN ASN ALA GLN LEU SER CYS
SEQRES 18 R 260 ILE THR LYS GLN ASP GLY PHE LYS ILE TYR ASP ASN GLU
SEQRES 19 R 260 LYS THR ALA GLU LEU ILE LYS GLU LEU LYS GLU LYS GLU
SEQRES 20 R 260 ALA ALA GLU SER PRO GLU GLU ALA ASP VAL GLU MET SER
SEQRES 1 S 234 MET PHE ARG ASN ASN TYR ASP GLY ASP THR VAL THR PHE
SEQRES 2 S 234 SER PRO THR GLY ARG LEU PHE GLN VAL GLU TYR ALA LEU
SEQRES 3 S 234 GLU ALA ILE LYS GLN GLY SER VAL THR VAL GLY LEU ARG
SEQRES 4 S 234 SER ASN THR HIS ALA VAL LEU VAL ALA LEU LYS ARG ASN
SEQRES 5 S 234 ALA ASP GLU LEU SER SER TYR GLN LYS LYS ILE ILE LYS
SEQRES 6 S 234 CYS ASP GLU HIS MET GLY LEU SER LEU ALA GLY LEU ALA
SEQRES 7 S 234 PRO ASP ALA ARG VAL LEU SER ASN TYR LEU ARG GLN GLN
SEQRES 8 S 234 CYS ASN TYR SER SER LEU VAL PHE ASN ARG LYS LEU ALA
SEQRES 9 S 234 VAL GLU ARG ALA GLY HIS LEU LEU CYS ASP LYS ALA GLN
SEQRES 10 S 234 LYS ASN THR GLN SER TYR GLY GLY ARG PRO TYR GLY VAL
SEQRES 11 S 234 GLY LEU LEU ILE ILE GLY TYR ASP LYS SER GLY ALA HIS
SEQRES 12 S 234 LEU LEU GLU PHE GLN PRO SER GLY ASN VAL THR GLU LEU
SEQRES 13 S 234 TYR GLY THR ALA ILE GLY ALA ARG SER GLN GLY ALA LYS
SEQRES 14 S 234 THR TYR LEU GLU ARG THR LEU ASP THR PHE ILE LYS ILE
SEQRES 15 S 234 ASP GLY ASN PRO ASP GLU LEU ILE LYS ALA GLY VAL GLU
SEQRES 16 S 234 ALA ILE SER GLN SER LEU ARG ASP GLU SER LEU THR VAL
SEQRES 17 S 234 ASP ASN LEU SER ILE ALA ILE VAL GLY LYS ASP THR PRO
SEQRES 18 S 234 PHE THR ILE TYR ASP GLY GLU ALA VAL ALA LYS TYR ILE
SEQRES 1 T 288 MET THR SER ILE GLY THR GLY TYR ASP LEU SER ASN SER
SEQRES 2 T 288 VAL PHE SER PRO ASP GLY ARG ASN PHE GLN VAL GLU TYR
SEQRES 3 T 288 ALA VAL LYS ALA VAL GLU ASN GLY THR THR SER ILE GLY
SEQRES 4 T 288 ILE LYS CYS ASN ASP GLY VAL VAL PHE ALA VAL GLU LYS
SEQRES 5 T 288 LEU ILE THR SER LYS LEU LEU VAL PRO GLN LYS ASN VAL
SEQRES 6 T 288 LYS ILE GLN VAL VAL ASP ARG HIS ILE GLY CYS VAL TYR
SEQRES 7 T 288 SER GLY LEU ILE PRO ASP GLY ARG HIS LEU VAL ASN ARG
SEQRES 8 T 288 GLY ARG GLU GLU ALA ALA SER PHE LYS LYS LEU TYR LYS
SEQRES 9 T 288 THR PRO ILE PRO ILE PRO ALA PHE ALA ASP ARG LEU GLY
SEQRES 10 T 288 GLN TYR VAL GLN ALA HIS THR LEU TYR ASN SER VAL ARG
SEQRES 11 T 288 PRO PHE GLY VAL SER THR ILE PHE GLY GLY VAL ASP LYS
SEQRES 12 T 288 ASN GLY ALA HIS LEU TYR MET LEU GLU PRO SER GLY SER
SEQRES 13 T 288 TYR TRP GLY TYR LYS GLY ALA ALA THR GLY LYS GLY ARG
SEQRES 14 T 288 GLN SER ALA LYS ALA GLU LEU GLU LYS LEU VAL ASP HIS
SEQRES 15 T 288 HIS PRO GLU GLY LEU SER ALA ARG GLU ALA VAL LYS GLN
SEQRES 16 T 288 ALA ALA LYS ILE ILE TYR LEU ALA HIS GLU ASP ASN LYS
SEQRES 17 T 288 GLU LYS ASP PHE GLU LEU GLU ILE SER TRP CYS SER LEU
SEQRES 18 T 288 SER GLU THR ASN GLY LEU HIS LYS PHE VAL LYS GLY ASP
SEQRES 19 T 288 LEU LEU GLN GLU ALA ILE ASP PHE ALA GLN LYS GLU ILE
SEQRES 20 T 288 ASN GLY ASP ASP ASP GLU ASP GLU ASP ASP SER ASP ASN
SEQRES 21 T 288 VAL MET SER SER ASP ASP GLU ASN ALA PRO VAL ALA THR
SEQRES 22 T 288 ASN ALA ASN ALA THR THR ASP GLN GLU GLY ASP ILE HIS
SEQRES 23 T 288 LEU GLU
SEQRES 1 U 252 MET SER GLY ALA ALA ALA ALA SER ALA ALA GLY TYR ASP
SEQRES 2 U 252 ARG HIS ILE THR ILE PHE SER PRO GLU GLY ARG LEU TYR
SEQRES 3 U 252 GLN VAL GLU TYR ALA PHE LYS ALA THR ASN GLN THR ASN
SEQRES 4 U 252 ILE ASN SER LEU ALA VAL ARG GLY LYS ASP CYS THR VAL
SEQRES 5 U 252 VAL ILE SER GLN LYS LYS VAL PRO ASP LYS LEU LEU ASP
SEQRES 6 U 252 PRO THR THR VAL SER TYR ILE PHE CYS ILE SER ARG THR
SEQRES 7 U 252 ILE GLY MET VAL VAL ASN GLY PRO ILE PRO ASP ALA ARG
SEQRES 8 U 252 ASN ALA ALA LEU ARG ALA LYS ALA GLU ALA ALA GLU PHE
SEQRES 9 U 252 ARG TYR LYS TYR GLY TYR ASP MET PRO CYS ASP VAL LEU
SEQRES 10 U 252 ALA LYS ARG MET ALA ASN LEU SER GLN ILE TYR THR GLN
SEQRES 11 U 252 ARG ALA TYR MET ARG PRO LEU GLY VAL ILE LEU THR PHE
SEQRES 12 U 252 VAL SER VAL ASP GLU GLU LEU GLY PRO SER ILE TYR LYS
SEQRES 13 U 252 THR ASP PRO ALA GLY TYR TYR VAL GLY TYR LYS ALA THR
SEQRES 14 U 252 ALA THR GLY PRO LYS GLN GLN GLU ILE THR THR ASN LEU
SEQRES 15 U 252 GLU ASN HIS PHE LYS LYS SER LYS ILE ASP HIS ILE ASN
SEQRES 16 U 252 GLU GLU SER TRP GLU LYS VAL VAL GLU PHE ALA ILE THR
SEQRES 17 U 252 HIS MET ILE ASP ALA LEU GLY THR GLU PHE SER LYS ASN
SEQRES 18 U 252 ASP LEU GLU VAL GLY VAL ALA THR LYS ASP LYS PHE PHE
SEQRES 19 U 252 THR LEU SER ALA GLU ASN ILE GLU GLU ARG LEU VAL ALA
SEQRES 20 U 252 ILE ALA GLU GLN ASP
SEQRES 1 V 232 THR THR ILE VAL GLY VAL LYS PHE ASN ASN GLY VAL VAL
SEQRES 2 V 232 ILE ALA ALA ASP THR ARG SER THR GLN GLY PRO ILE VAL
SEQRES 3 V 232 ALA ASP LYS ASN CYS ALA LYS LEU HIS ARG ILE SER PRO
SEQRES 4 V 232 LYS ILE TRP CYS ALA GLY ALA GLY THR ALA ALA ASP THR
SEQRES 5 V 232 GLU ALA VAL THR GLN LEU ILE GLY SER ASN ILE GLU LEU
SEQRES 6 V 232 HIS SER LEU TYR THR SER ARG GLU PRO ARG VAL VAL SER
SEQRES 7 V 232 ALA LEU GLN MET LEU LYS GLN HIS LEU PHE LYS TYR GLN
SEQRES 8 V 232 GLY HIS ILE GLY ALA TYR LEU ILE VAL ALA GLY VAL ASP
SEQRES 9 V 232 PRO THR GLY SER HIS LEU PHE SER ILE HIS ALA HIS GLY
SEQRES 10 V 232 SER THR ASP VAL GLY TYR TYR LEU SER LEU GLY SER GLY
SEQRES 11 V 232 SER LEU ALA ALA MET ALA VAL LEU GLU SER HIS TRP LYS
SEQRES 12 V 232 GLN ASP LEU THR LYS GLU GLU ALA ILE LYS LEU ALA SER
SEQRES 13 V 232 ASP ALA ILE GLN ALA GLY ILE TRP ASN ASP LEU GLY SER
SEQRES 14 V 232 GLY SER ASN VAL ASP VAL CYS VAL MET GLU ILE GLY LYS
SEQRES 15 V 232 ASP ALA GLU TYR LEU ARG ASN TYR LEU THR PRO ASN VAL
SEQRES 16 V 232 ARG GLU GLU LYS GLN LYS SER TYR LYS PHE PRO ARG GLY
SEQRES 17 V 232 THR THR ALA VAL LEU LYS GLU SER ILE VAL ASN ILE CYS
SEQRES 18 V 232 ASP ILE GLN GLU GLU GLN VAL ASP ILE THR ALA
SEQRES 1 W 205 MET SER ASP PRO SER SER ILE ASN GLY GLY ILE VAL VAL
SEQRES 2 W 205 ALA MET THR GLY LYS ASP CYS VAL ALA ILE ALA CYS ASP
SEQRES 3 W 205 LEU ARG LEU GLY SER GLN SER LEU GLY VAL SER ASN LYS
SEQRES 4 W 205 PHE GLU LYS ILE PHE HIS TYR GLY HIS VAL PHE LEU GLY
SEQRES 5 W 205 ILE THR GLY LEU ALA THR ASP VAL THR THR LEU ASN GLU
SEQRES 6 W 205 MET PHE ARG TYR LYS THR ASN LEU TYR LYS LEU LYS GLU
SEQRES 7 W 205 GLU ARG ALA ILE GLU PRO GLU THR PHE THR GLN LEU VAL
SEQRES 8 W 205 SER SER SER LEU TYR GLU ARG ARG PHE GLY PRO TYR PHE
SEQRES 9 W 205 VAL GLY PRO VAL VAL ALA GLY ILE ASN SER LYS SER GLY
SEQRES 10 W 205 LYS PRO PHE ILE ALA GLY PHE ASP LEU ILE GLY CYS ILE
SEQRES 11 W 205 ASP GLU ALA LYS ASP PHE ILE VAL SER GLY THR ALA SER
SEQRES 12 W 205 ASP GLN LEU PHE GLY MET CYS GLU SER LEU TYR GLU PRO
SEQRES 13 W 205 ASN LEU GLU PRO GLU ASP LEU PHE GLU THR ILE SER GLN
SEQRES 14 W 205 ALA LEU LEU ASN ALA ALA ASP ARG ASP ALA LEU SER GLY
SEQRES 15 W 205 TRP GLY ALA VAL VAL TYR ILE ILE LYS LYS ASP GLU VAL
SEQRES 16 W 205 VAL LYS ARG TYR LEU LYS MET ARG GLN ASP
SEQRES 1 X 198 MET ASP ILE ILE LEU GLY ILE ARG VAL GLN ASP SER VAL
SEQRES 2 X 198 ILE LEU ALA SER SER LYS ALA VAL THR ARG GLY ILE SER
SEQRES 3 X 198 VAL LEU LYS ASP SER ASP ASP LYS THR ARG GLN LEU SER
SEQRES 4 X 198 PRO HIS THR LEU MET SER PHE ALA GLY GLU ALA GLY ASP
SEQRES 5 X 198 THR VAL GLN PHE ALA GLU TYR ILE GLN ALA ASN ILE GLN
SEQRES 6 X 198 LEU TYR SER ILE ARG GLU ASP TYR GLU LEU SER PRO GLN
SEQRES 7 X 198 ALA VAL SER SER PHE VAL ARG GLN GLU LEU ALA LYS SER
SEQRES 8 X 198 ILE ARG SER ARG ARG PRO TYR GLN VAL ASN VAL LEU ILE
SEQRES 9 X 198 GLY GLY TYR ASP LYS LYS LYS ASN LYS PRO GLU LEU TYR
SEQRES 10 X 198 GLN ILE ASP TYR LEU GLY THR LYS VAL GLU LEU PRO TYR
SEQRES 11 X 198 GLY ALA HIS GLY TYR SER GLY PHE TYR THR PHE SER LEU
SEQRES 12 X 198 LEU ASP HIS HIS TYR ARG PRO ASP MET THR THR GLU GLU
SEQRES 13 X 198 GLY LEU ASP LEU LEU LYS LEU CYS VAL GLN GLU LEU GLU
SEQRES 14 X 198 LYS ARG MET PRO MET ASP PHE LYS GLY VAL ILE VAL LYS
SEQRES 15 X 198 ILE VAL ASP LYS ASP GLY ILE ARG GLN VAL ASP ASP PHE
SEQRES 16 X 198 GLN ALA GLN
SEQRES 1 Y 212 THR THR THR LEU ALA PHE ARG PHE GLN GLY GLY ILE ILE
SEQRES 2 Y 212 VAL ALA VAL ASP SER ARG ALA THR ALA GLY ASN TRP VAL
SEQRES 3 Y 212 ALA SER GLN THR VAL LYS LYS VAL ILE GLU ILE ASN PRO
SEQRES 4 Y 212 PHE LEU LEU GLY THR MET ALA GLY GLY ALA ALA ASP CYS
SEQRES 5 Y 212 GLN PHE TRP GLU THR TRP LEU GLY SER GLN CYS ARG LEU
SEQRES 6 Y 212 HIS GLU LEU ARG GLU LYS GLU ARG ILE SER VAL ALA ALA
SEQRES 7 Y 212 ALA SER LYS ILE LEU SER ASN LEU VAL TYR GLN TYR LYS
SEQRES 8 Y 212 GLY ALA GLY LEU SER MET GLY THR MET ILE CYS GLY TYR
SEQRES 9 Y 212 THR ARG LYS GLU GLY PRO THR ILE TYR TYR VAL ASP SER
SEQRES 10 Y 212 ASP GLY THR ARG LEU LYS GLY ASP ILE PHE CYS VAL GLY
SEQRES 11 Y 212 SER GLY GLN THR PHE ALA TYR GLY VAL LEU ASP SER ASN
SEQRES 12 Y 212 TYR LYS TRP ASP LEU SER VAL GLU ASP ALA LEU TYR LEU
SEQRES 13 Y 212 GLY LYS ARG SER ILE LEU ALA ALA ALA HIS ARG ASP ALA
SEQRES 14 Y 212 TYR SER GLY GLY SER VAL ASN LEU TYR HIS VAL THR GLU
SEQRES 15 Y 212 ASP GLY TRP ILE TYR HIS GLY ASN HIS ASP VAL GLY GLU
SEQRES 16 Y 212 LEU PHE TRP LYS VAL LYS GLU GLU GLU GLY SER PHE ASN
SEQRES 17 Y 212 ASN VAL ILE GLY
SEQRES 1 Z 222 GLN PHE ASN PRO TYR GLY ASP ASN GLY GLY THR ILE LEU
SEQRES 2 Z 222 GLY ILE ALA GLY GLU ASP PHE ALA VAL LEU ALA GLY ASP
SEQRES 3 Z 222 THR ARG ASN ILE THR ASP TYR SER ILE ASN SER ARG TYR
SEQRES 4 Z 222 GLU PRO LYS VAL PHE ASP CYS GLY ASP ASN ILE VAL MET
SEQRES 5 Z 222 SER ALA ASN GLY PHE ALA ALA ASP GLY ASP ALA LEU VAL
SEQRES 6 Z 222 LYS ARG PHE LYS ASN SER VAL LYS TRP TYR HIS PHE ASP
SEQRES 7 Z 222 HIS ASN ASP LYS LYS LEU SER ILE ASN SER ALA ALA ARG
SEQRES 8 Z 222 ASN ILE GLN HIS LEU LEU TYR GLY LYS ARG PHE PHE PRO
SEQRES 9 Z 222 TYR TYR VAL HIS THR ILE ILE ALA GLY LEU ASP GLU ASP
SEQRES 10 Z 222 GLY LYS GLY ALA VAL TYR SER PHE ASP PRO VAL GLY SER
SEQRES 11 Z 222 TYR GLU ARG GLU GLN CYS ARG ALA GLY GLY ALA ALA ALA
SEQRES 12 Z 222 SER LEU ILE MET PRO PHE LEU ASP ASN GLN VAL ASN PHE
SEQRES 13 Z 222 LYS ASN GLN TYR GLU PRO GLY THR ASN GLY LYS VAL LYS
SEQRES 14 Z 222 LYS PRO LEU LYS TYR LEU SER VAL GLU GLU VAL ILE LYS
SEQRES 15 Z 222 LEU VAL ARG ASP SER PHE THR SER ALA THR GLU ARG HIS
SEQRES 16 Z 222 ILE GLN VAL GLY ASP GLY LEU GLU ILE LEU ILE VAL THR
SEQRES 17 Z 222 LYS ASP GLY VAL ARG LYS GLU PHE TYR GLU LEU LYS ARG
SEQRES 18 Z 222 ASP
SEQRES 1 a 246 THR GLN ILE ALA ASN ALA GLY ALA SER PRO MET VAL ASN
SEQRES 2 a 246 THR GLN GLN PRO ILE VAL THR GLY THR SER VAL ILE SER
SEQRES 3 a 246 MET LYS TYR ASP ASN GLY VAL ILE ILE ALA ALA ASP ASN
SEQRES 4 a 246 LEU GLY SER TYR GLY SER LEU LEU ARG PHE ASN GLY VAL
SEQRES 5 a 246 GLU ARG LEU ILE PRO VAL GLY ASP ASN THR VAL VAL GLY
SEQRES 6 a 246 ILE SER GLY ASP ILE SER ASP MET GLN HIS ILE GLU ARG
SEQRES 7 a 246 LEU LEU LYS ASP LEU VAL THR GLU ASN ALA TYR ASP ASN
SEQRES 8 a 246 PRO LEU ALA ASP ALA GLU GLU ALA LEU GLU PRO SER TYR
SEQRES 9 a 246 ILE PHE GLU TYR LEU ALA THR VAL MET TYR GLN ARG ARG
SEQRES 10 a 246 SER LYS MET ASN PRO LEU TRP ASN ALA ILE ILE VAL ALA
SEQRES 11 a 246 GLY VAL GLN SER ASN GLY ASP GLN PHE LEU ARG TYR VAL
SEQRES 12 a 246 ASN LEU LEU GLY VAL THR TYR SER SER PRO THR LEU ALA
SEQRES 13 a 246 THR GLY PHE GLY ALA HIS MET ALA ASN PRO LEU LEU ARG
SEQRES 14 a 246 LYS VAL VAL ASP ARG GLU SER ASP ILE PRO LYS THR THR
SEQRES 15 a 246 VAL GLN VAL ALA GLU GLU ALA ILE VAL ASN ALA MET ARG
SEQRES 16 a 246 VAL LEU TYR TYR ARG ASP ALA ARG SER SER ARG ASN PHE
SEQRES 17 a 246 SER LEU ALA ILE ILE ASP LYS ASN THR GLY LEU THR PHE
SEQRES 18 a 246 LYS LYS ASN LEU GLN VAL GLU ASN MET LYS TRP ASP PHE
SEQRES 19 a 246 ALA LYS ASP ILE LYS GLY TYR GLY THR GLN LYS ILE
SEQRES 1 b 196 THR SER ILE MET ALA VAL THR PHE LYS ASP GLY VAL ILE
SEQRES 2 b 196 LEU GLY ALA ASP SER ARG THR THR THR GLY ALA TYR ILE
SEQRES 3 b 196 ALA ASN ARG VAL THR ASP LYS LEU THR ARG VAL HIS ASP
SEQRES 4 b 196 LYS ILE TRP CYS CYS ARG SER GLY SER ALA ALA ASP THR
SEQRES 5 b 196 GLN ALA ILE ALA ASP ILE VAL GLN TYR HIS LEU GLU LEU
SEQRES 6 b 196 TYR THR SER GLN TYR GLY THR PRO SER THR GLU THR ALA
SEQRES 7 b 196 ALA SER VAL PHE LYS GLU LEU CYS TYR GLU ASN LYS ASP
SEQRES 8 b 196 ASN LEU THR ALA GLY ILE ILE VAL ALA GLY TYR ASP ASP
SEQRES 9 b 196 LYS ASN LYS GLY GLU VAL TYR THR ILE PRO LEU GLY GLY
SEQRES 10 b 196 SER VAL HIS LYS LEU PRO TYR ALA ILE ALA GLY SER GLY
SEQRES 11 b 196 SER THR PHE ILE TYR GLY TYR CYS ASP LYS ASN PHE ARG
SEQRES 12 b 196 GLU ASN MET SER LYS GLU GLU THR VAL ASP PHE ILE LYS
SEQRES 13 b 196 HIS SER LEU SER GLN ALA ILE LYS TRP ASP GLY SER SER
SEQRES 14 b 196 GLY GLY VAL ILE ARG MET VAL VAL LEU THR ALA ALA GLY
SEQRES 15 b 196 VAL GLU ARG LEU ILE PHE TYR PRO ASP GLU TYR GLU GLN
SEQRES 16 b 196 LEU
SEQRES 1 c 5 ACE LEU ALA IL0 POL
SEQRES 1 d 5 ACE LEU ALA IL0 POL
SEQRES 1 e 5 ACE LEU ALA IL0 POL
SEQRES 1 f 5 ACE LEU ALA IL0 POL
SEQRES 1 g 5 ACE LEU ALA IL0 POL
SEQRES 1 h 5 ACE LEU ALA IL0 POL
HET ACE c 1 3
HET IL0 c 4 8
HET POL c 5 4
HET ACE d 1 3
HET IL0 d 4 8
HET POL d 5 4
HET ACE e 1 3
HET IL0 e 4 8
HET POL e 5 4
HET ACE f 1 3
HET IL0 f 4 8
HET POL f 5 4
HET ACE g 1 3
HET IL0 g 4 8
HET POL g 5 4
HET ACE h 1 3
HET IL0 h 4 8
HET POL h 5 4
HET MG G 301 1
HET CL G 302 1
HET MES H 301 12
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 N 202 1
HET CL U 301 1
HET MG Z 301 1
HET CL b 201 1
HET MES d 101 12
HET MES g 101 12
HETNAM ACE ACETYL GROUP
HETNAM IL0 (2S,3S)-2-AMINO-3-METHYLPENTANE-1,1-DIOL
HETNAM POL N-PROPANOL
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETSYN POL 1-PROPONOL
FORMUL 29 ACE 6(C2 H4 O)
FORMUL 29 IL0 6(C6 H15 N O2)
FORMUL 29 POL 6(C3 H8 O)
FORMUL 35 MG 7(MG 2+)
FORMUL 36 CL 4(CL 1-)
FORMUL 37 MES 3(C6 H13 N O4 S)
FORMUL 49 HOH *746(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 GLU D 52 ILE D 56 5 5
HELIX 25 AC7 ASP D 76 ASP D 96 1 21
HELIX 26 AC8 ASN D 100 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 ASN E 118 1 16
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 ASN F 29 1 13
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 ALA H 49 SER H 71 1 23
HELIX 53 AF8 ARG H 75 TYR H 90 1 16
HELIX 54 AF9 GLY H 130 TRP H 142 1 13
HELIX 55 AG1 THR H 147 ASP H 166 1 20
HELIX 56 AG2 ASP I 2 ILE I 6 5 5
HELIX 57 AG3 LEU I 55 GLU I 78 1 24
HELIX 58 AG4 GLU I 82 GLU I 96 1 15
HELIX 59 AG5 ALA I 141 TYR I 153 1 13
HELIX 60 AG6 GLU I 158 ASP I 175 1 18
HELIX 61 AG7 GLY J 51 ASP J 72 1 22
HELIX 62 AG8 SER J 76 ILE J 92 1 17
HELIX 63 AG9 SER J 136 TYR J 148 1 13
HELIX 64 AH1 THR J 153 MET J 172 1 20
HELIX 65 AH2 ALA K 49 LYS K 71 1 23
HELIX 66 AH3 SER K 75 TYR K 90 1 16
HELIX 67 AH4 GLY K 132 SER K 142 1 11
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 ARG M 156 1 12
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 ALA N 49 GLY N 71 1 23
HELIX 81 AI9 SER N 74 ASN N 89 1 16
HELIX 82 AJ1 LYS N 90 LEU N 93 5 4
HELIX 83 AJ2 GLY N 128 PHE N 133 5 6
HELIX 84 AJ3 ILE N 134 PHE N 142 1 9
HELIX 85 AJ4 SER N 147 ASP N 166 1 20
HELIX 86 AJ5 TYR N 189 GLU N 194 1 6
HELIX 87 AJ6 LEU O 18 GLY O 31 1 14
HELIX 88 AJ7 MET O 78 SER O 96 1 19
HELIX 89 AJ8 TYR O 97 GLY O 102 1 6
HELIX 90 AJ9 PRO O 106 ALA O 121 1 16
HELIX 91 AK1 GLY O 167 TRP O 179 1 13
HELIX 92 AK2 GLU O 184 VAL O 200 1 17
HELIX 93 AK3 ASN O 218 LEU O 222 5 5
HELIX 94 AK4 THR O 239 ALA O 249 1 11
HELIX 95 AK5 GLY P 1 ASP P 6 5 6
HELIX 96 AK6 LEU P 18 SER P 29 1 12
HELIX 97 AK7 LEU P 79 ASN P 102 1 24
HELIX 98 AK8 PRO P 106 HIS P 124 1 19
HELIX 99 AK9 ASN P 167 TYR P 179 1 13
HELIX 100 AL1 LYS P 184 THR P 200 1 17
HELIX 101 AL2 THR P 206 ASP P 208 5 3
HELIX 102 AL3 LYS P 230 THR P 241 1 12
HELIX 103 AL4 ILE Q 15 GLY Q 28 1 14
HELIX 104 AL5 LEU Q 76 GLU Q 99 1 24
HELIX 105 AL6 THR Q 103 TYR Q 118 1 16
HELIX 106 AL7 ASN Q 165 TYR Q 177 1 13
HELIX 107 AL8 THR Q 185 GLU Q 199 1 15
HELIX 108 AL9 SER Q 223 GLN Q 239 1 17
HELIX 109 AM1 LEU R 13 LEU R 25 1 13
HELIX 110 AM2 GLU R 52 ILE R 56 5 5
HELIX 111 AM3 ASP R 76 ASP R 96 1 21
HELIX 112 AM4 ASN R 100 LEU R 113 1 14
HELIX 113 AM5 GLY R 167 TRP R 179 1 13
HELIX 114 AM6 THR R 184 MET R 200 1 17
HELIX 115 AM7 ASP R 224 ALA R 241 1 18
HELIX 116 AM8 LEU S 18 GLY S 31 1 14
HELIX 117 AM9 LEU S 76 ASN S 99 1 24
HELIX 118 AN1 ALA S 103 ASN S 118 1 16
HELIX 119 AN2 ARG S 163 ILE S 179 1 17
HELIX 120 AN3 ASN S 184 SER S 197 1 14
HELIX 121 AN4 GLN S 198 LEU S 200 5 3
HELIX 122 AN5 ASP S 225 ILE S 233 5 9
HELIX 123 AN6 ASN T 17 ASN T 29 1 13
HELIX 124 AN7 LEU T 77 LYS T 100 1 24
HELIX 125 AN8 PRO T 104 HIS T 119 1 16
HELIX 126 AN9 GLY T 164 HIS T 179 1 16
HELIX 127 AO1 SER T 184 HIS T 200 1 17
HELIX 128 AO2 GLU T 201 LYS T 204 5 4
HELIX 129 AO3 LYS T 228 ASN T 244 1 17
HELIX 130 AO4 GLY U 2 HIS U 6 5 5
HELIX 131 AO5 LEU U 16 THR U 26 1 11
HELIX 132 AO6 ASP U 56 VAL U 60 5 5
HELIX 133 AO7 PRO U 77 GLY U 100 1 24
HELIX 134 AO8 PRO U 104 ARG U 122 1 19
HELIX 135 AO9 LYS U 165 LYS U 181 1 17
HELIX 136 AP1 SER U 189 GLY U 206 1 18
HELIX 137 AP2 SER U 228 GLU U 241 1 14
HELIX 138 AP3 ALA V 49 SER V 71 1 23
HELIX 139 AP4 ARG V 75 TYR V 90 1 16
HELIX 140 AP5 GLY V 130 TRP V 142 1 13
HELIX 141 AP6 THR V 147 ASP V 166 1 20
HELIX 142 AP7 ASP W 2 ILE W 6 5 5
HELIX 143 AP8 LEU W 55 GLU W 78 1 24
HELIX 144 AP9 GLU W 82 GLU W 96 1 15
HELIX 145 AQ1 ALA W 141 TYR W 153 1 13
HELIX 146 AQ2 GLU W 158 ASP W 175 1 18
HELIX 147 AQ3 GLY X 51 ASP X 72 1 22
HELIX 148 AQ4 SER X 76 ILE X 92 1 17
HELIX 149 AQ5 SER X 136 TYR X 148 1 13
HELIX 150 AQ6 THR X 153 MET X 172 1 20
HELIX 151 AQ7 ALA Y 49 LYS Y 71 1 23
HELIX 152 AQ8 SER Y 75 TYR Y 90 1 16
HELIX 153 AQ9 GLY Y 132 SER Y 142 1 11
HELIX 154 AR1 SER Y 149 ASP Y 168 1 20
HELIX 155 AR2 VAL Y 193 GLY Y 205 1 13
HELIX 156 AR3 PHE Z 57 HIS Z 79 1 23
HELIX 157 AR4 SER Z 85 GLY Z 99 1 15
HELIX 158 AR5 ALA Z 142 VAL Z 154 1 13
HELIX 159 AR6 SER Z 176 HIS Z 195 1 20
HELIX 160 AR7 ILE a 57 TYR a 76 1 20
HELIX 161 AR8 GLU a 88 LYS a 106 1 19
HELIX 162 AR9 GLY a 145 VAL a 159 1 15
HELIX 163 AS1 ARG a 161 ILE a 165 5 5
HELIX 164 AS2 THR a 169 ASP a 188 1 20
HELIX 165 AS3 TRP a 219 ILE a 225 5 7
HELIX 166 AS4 ALA b 49 GLY b 71 1 23
HELIX 167 AS5 SER b 74 ASN b 89 1 16
HELIX 168 AS6 LYS b 90 LEU b 93 5 4
HELIX 169 AS7 GLY b 128 PHE b 133 5 6
HELIX 170 AS8 ILE b 134 PHE b 142 1 9
HELIX 171 AS9 SER b 147 ASP b 166 1 20
HELIX 172 AT1 TYR b 189 GLU b 194 1 6
SHEET 1 AA1 5 ALA A 161 ILE A 164 0
SHEET 2 AA1 5 SER A 34 ALA A 39 -1 N SER A 34 O ILE A 164
SHEET 3 AA1 5 GLY A 42 GLU A 48 -1 O GLY A 42 N ALA A 39
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 PHE G 134 O TYR G 146
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 ILE A 71 N LEU A 67
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 ALA H 16 -1 N VAL H 12 O MET H 178
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 125 N GLY H 5
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 ARG B 216 -1 O ALA B 213 N LEU B 45
SHEET 5 AA5 5 TYR B 225 ILE B 228 -1 O LYS B 227 N THR B 214
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 THR C 211 N LEU C 42
SHEET 5 AA7 5 ASP C 218 ALA C 221 -1 O ASP C 218 N LYS C 214
SHEET 1 AA8 5 SER C 63 LYS C 64 0
SHEET 2 AA8 5 VAL C 69 GLY C 75 -1 O LEU C 71 N SER C 63
SHEET 3 AA8 5 VAL C 129 GLY C 135 -1 O ALA C 134 N VAL C 70
SHEET 4 AA8 5 LYS C 144 THR C 148 -1 O TYR C 146 N ILE C 133
SHEET 5 AA8 5 TYR C 154 SER C 156 -1 O SER C 155 N GLN C 147
SHEET 1 AA9 5 ALA D 161 ILE D 164 0
SHEET 2 AA9 5 ALA D 29 ALA D 33 -1 N ALA D 29 O ILE D 164
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 ALA D 137 N GLY D 67
SHEET 4 AB1 5 GLY D 144 ALA D 150 -1 O ALA D 150 N LEU D 134
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 ILE E 134 N GLY E 70
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 CYS F 38 -1 N GLY F 35 O ALA F 159
SHEET 3 AB4 5 GLY F 41 LEU F 49 -1 O GLY F 41 N CYS F 38
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 THR G 160 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 THR H 48 -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 3 LEU H 34 SER H 38 0
SHEET 2 AB9 3 ILE H 41 THR H 48 -1 O CYS H 43 N HIS H 35
SHEET 3 AB9 3 ALA c 3 IL0 c 4 -1 O IL0 c 4 N GLY H 47
SHEET 1 AC1 6 VAL H 212 VAL H 218 0
SHEET 2 AC1 6 GLU I 193 LEU I 199 -1 O VAL I 194 N VAL H 218
SHEET 3 AC1 6 ALA I 184 LYS I 190 -1 N ILE I 188 O VAL I 195
SHEET 4 AC1 6 CYS I 19 ASP I 25 -1 N VAL I 20 O ILE I 189
SHEET 5 AC1 6 ILE I 10 GLY I 16 -1 N VAL I 12 O ALA I 23
SHEET 6 AC1 6 PHE I 135 GLY I 139 -1 O ILE I 136 N ALA I 13
SHEET 1 AC2 2 LEU I 28 SER I 30 0
SHEET 2 AC2 2 LEU I 33 SER I 36 -1 O LEU I 33 N SER I 30
SHEET 1 AC3 5 ILE I 42 TYR I 45 0
SHEET 2 AC3 5 VAL I 48 GLY I 54 -1 O LEU I 50 N PHE I 43
SHEET 3 AC3 5 VAL I 104 ILE I 111 -1 O VAL I 107 N GLY I 51
SHEET 4 AC3 5 PRO I 118 PHE I 123 -1 O PHE I 119 N GLY I 110
SHEET 5 AC3 5 ILE I 129 GLU I 131 -1 O ASP I 130 N GLY I 122
SHEET 1 AC4 5 TYR J 130 HIS J 133 0
SHEET 2 AC4 5 ILE J 4 ARG J 8 -1 N GLY J 6 O GLY J 131
SHEET 3 AC4 5 VAL J 13 SER J 18 -1 O ALA J 16 N LEU J 5
SHEET 4 AC4 5 VAL J 179 ASP J 185 -1 O VAL J 184 N VAL J 13
SHEET 5 AC4 5 GLY J 188 VAL J 192 -1 O ARG J 190 N ILE J 183
SHEET 1 AC5 2 VAL J 21 ARG J 23 0
SHEET 2 AC5 2 SER J 26 LYS J 29 -1 O SER J 26 N ARG J 23
SHEET 1 AC6 5 THR J 35 SER J 39 0
SHEET 2 AC6 5 THR J 42 GLY J 48 -1 O MET J 44 N ARG J 36
SHEET 3 AC6 5 VAL J 100 ASP J 108 -1 O ASN J 101 N ALA J 47
SHEET 4 AC6 5 LYS J 113 ILE J 119 -1 O ILE J 119 N VAL J 102
SHEET 5 AC6 5 LYS J 125 GLU J 127 -1 O VAL J 126 N GLN J 118
SHEET 1 AC7 5 ILE K 126 VAL K 129 0
SHEET 2 AC7 5 THR K 3 PHE K 8 -1 N THR K 3 O VAL K 129
SHEET 3 AC7 5 GLY K 11 VAL K 16 -1 O ALA K 15 N LEU K 4
SHEET 4 AC7 5 SER K 174 THR K 181 -1 O VAL K 180 N ILE K 12
SHEET 5 AC7 5 GLY K 184 ASP K 192 -1 O GLY K 184 N THR K 181
SHEET 1 AC8 2 ALA K 20 ALA K 22 0
SHEET 2 AC8 2 TRP K 25 SER K 28 -1 O SER K 28 N ALA K 20
SHEET 1 AC9 5 VAL K 34 ASN K 38 0
SHEET 2 AC9 5 LEU K 41 THR K 44 -1 O GLY K 43 N ILE K 35
SHEET 3 AC9 5 GLY K 98 THR K 105 -1 O CYS K 102 N LEU K 42
SHEET 4 AC9 5 GLY K 109 ASP K 116 -1 O VAL K 115 N THR K 99
SHEET 5 AC9 5 ARG K 121 LYS K 123 -1 O LEU K 122 N TYR K 114
SHEET 1 AD1 2 GLY K 47 GLY K 48 0
SHEET 2 AD1 2 ALA d 3 IL0 d 4 -1 O IL0 d 4 N GLY K 47
SHEET 1 AD2 5 CYS L 136 GLY L 140 0
SHEET 2 AD2 5 THR L 11 ALA L 16 -1 N ILE L 12 O GLY L 139
SHEET 3 AD2 5 ALA L 21 ASP L 26 -1 O ALA L 24 N LEU L 13
SHEET 4 AD2 5 GLY L 201 THR L 208 -1 O VAL L 207 N ALA L 21
SHEET 5 AD2 5 GLY L 211 GLU L 218 -1 O TYR L 217 N LEU L 202
SHEET 1 AD3 2 ASN L 29 THR L 31 0
SHEET 2 AD3 2 SER L 34 SER L 37 -1 O ASN L 36 N ASN L 29
SHEET 1 AD4 5 PHE L 44 ASP L 45 0
SHEET 2 AD4 5 VAL L 51 GLY L 56 -1 O MET L 52 N PHE L 44
SHEET 3 AD4 5 VAL L 107 LEU L 114 -1 O HIS L 108 N ASN L 55
SHEET 4 AD4 5 GLY L 120 PHE L 125 -1 O ALA L 121 N GLY L 113
SHEET 5 AD4 5 TYR L 131 GLU L 134 -1 O GLU L 134 N VAL L 122
SHEET 1 AD5 5 LEU M 33 PHE M 36 0
SHEET 2 AD5 5 GLY M 28 TYR M 30 -1 N TYR M 30 O LEU M 33
SHEET 3 AD5 5 VAL M 6 GLY M 8 -1 N THR M 7 O SER M 29
SHEET 4 AD5 5 THR M 49 ASP M 56 -1 O GLY M 55 N GLY M 8
SHEET 5 AD5 5 LEU M 42 PRO M 44 -1 N ILE M 43 O VAL M 51
SHEET 1 AD6 7 LEU M 33 PHE M 36 0
SHEET 2 AD6 7 GLY M 28 TYR M 30 -1 N TYR M 30 O LEU M 33
SHEET 3 AD6 7 VAL M 6 GLY M 8 -1 N THR M 7 O SER M 29
SHEET 4 AD6 7 THR M 49 ASP M 56 -1 O GLY M 55 N GLY M 8
SHEET 5 AD6 7 ASN M 112 VAL M 119 -1 O ALA M 117 N VAL M 50
SHEET 6 AD6 7 GLN M 125 ASN M 131 -1 O VAL M 130 N ILE M 114
SHEET 7 AD6 7 THR M 136 TYR M 137 -1 O TYR M 137 N TYR M 129
SHEET 1 AD7 5 THR M 141 ALA M 143 0
SHEET 2 AD7 5 VAL M 11 LYS M 15 -1 N SER M 13 O LEU M 142
SHEET 3 AD7 5 GLY M 19 ASP M 25 -1 O ALA M 23 N ILE M 12
SHEET 4 AD7 5 ASN M 194 ASP M 201 -1 O ALA M 198 N ILE M 22
SHEET 5 AD7 5 GLY M 205 GLN M 213 -1 O LYS M 209 N LEU M 197
SHEET 1 AD8 5 TYR N 124 ALA N 127 0
SHEET 2 AD8 5 ILE N 3 THR N 7 -1 N ILE N 3 O ALA N 127
SHEET 3 AD8 5 GLY N 11 ALA N 16 -1 O GLY N 15 N MET N 4
SHEET 4 AD8 5 ILE N 173 THR N 179 -1 O LEU N 178 N VAL N 12
SHEET 5 AD8 5 VAL N 183 PHE N 188 -1 O GLU N 184 N VAL N 177
SHEET 1 AD9 2 THR N 20 THR N 22 0
SHEET 2 AD9 2 TYR N 25 ASN N 28 -1 O TYR N 25 N THR N 22
SHEET 1 AE1 5 LEU N 34 HIS N 38 0
SHEET 2 AE1 5 ILE N 41 SER N 48 -1 O CYS N 43 N THR N 35
SHEET 3 AE1 5 ALA N 95 TYR N 102 -1 O ALA N 100 N TRP N 42
SHEET 4 AE1 5 GLY N 108 ILE N 113 -1 O TYR N 111 N VAL N 99
SHEET 5 AE1 5 HIS N 120 LEU N 122 -1 O HIS N 120 N THR N 112
SHEET 1 AE2 3 LEU N 34 HIS N 38 0
SHEET 2 AE2 3 ILE N 41 SER N 48 -1 O CYS N 43 N THR N 35
SHEET 3 AE2 3 ALA e 3 IL0 e 4 -1 O IL0 e 4 N GLY N 47
SHEET 1 AE3 5 ALA O 161 ILE O 164 0
SHEET 2 AE3 5 SER O 34 ALA O 39 -1 N SER O 34 O ILE O 164
SHEET 3 AE3 5 GLY O 42 GLU O 48 -1 O GLY O 42 N ALA O 39
SHEET 4 AE3 5 ILE O 209 ILE O 214 -1 O ILE O 214 N VAL O 43
SHEET 5 AE3 5 PHE O 235 LYS O 237 -1 O ARG O 236 N ILE O 213
SHEET 1 AE4 6 ALA O 56 MET O 57 0
SHEET 2 AE4 6 TYR U 154 TYR U 157 -1 O GLY U 156 N MET O 57
SHEET 3 AE4 6 GLY U 142 THR U 148 -1 N ILE U 145 O TYR U 157
SHEET 4 AE4 6 ILE U 131 ASP U 138 -1 N PHE U 134 O TYR U 146
SHEET 5 AE4 6 GLY U 71 ASN U 75 -1 N GLY U 71 O VAL U 135
SHEET 6 AE4 6 ILE U 63 CYS U 65 -1 N PHE U 64 O MET U 72
SHEET 1 AE5 5 SER O 65 THR O 68 0
SHEET 2 AE5 5 ILE O 71 GLY O 77 -1 O ILE O 71 N LEU O 67
SHEET 3 AE5 5 VAL O 132 ASP O 140 -1 O LEU O 135 N VAL O 74
SHEET 4 AE5 5 GLY O 144 VAL O 150 -1 O TYR O 148 N ILE O 136
SHEET 5 AE5 5 TYR O 156 PRO O 158 -1 O PHE O 157 N GLN O 149
SHEET 1 AE6 6 TYR O 224 THR O 225 0
SHEET 2 AE6 6 ALA V 184 LEU V 191 1 O TYR V 186 N THR O 225
SHEET 3 AE6 6 VAL V 173 GLU V 179 -1 N VAL V 175 O LEU V 187
SHEET 4 AE6 6 GLY V 11 ALA V 16 -1 N VAL V 12 O MET V 178
SHEET 5 AE6 6 ILE V 3 PHE V 8 -1 N VAL V 6 O VAL V 13
SHEET 6 AE6 6 TYR V 124 LEU V 127 -1 O LEU V 125 N GLY V 5
SHEET 1 AE7 5 ALA P 161 VAL P 164 0
SHEET 2 AE7 5 ALA P 34 ALA P 39 -1 N GLY P 36 O ILE P 162
SHEET 3 AE7 5 GLY P 42 GLU P 48 -1 O ALA P 46 N ILE P 35
SHEET 4 AE7 5 LEU P 210 ARG P 216 -1 O ALA P 213 N LEU P 45
SHEET 5 AE7 5 TYR P 225 ILE P 228 -1 O LYS P 227 N THR P 214
SHEET 1 AE8 5 LEU P 65 LYS P 67 0
SHEET 2 AE8 5 ILE P 72 GLY P 78 -1 O VAL P 74 N TYR P 66
SHEET 3 AE8 5 VAL P 132 ASP P 140 -1 O ALA P 137 N ALA P 73
SHEET 4 AE8 5 GLY P 144 SER P 150 -1 O TYR P 148 N TYR P 136
SHEET 5 AE8 5 TYR P 156 TRP P 159 -1 O TRP P 159 N LEU P 147
SHEET 1 AE9 5 ALA Q 159 ILE Q 162 0
SHEET 2 AE9 5 ALA Q 31 LYS Q 35 -1 N GLY Q 33 O GLN Q 160
SHEET 3 AE9 5 VAL Q 40 GLU Q 45 -1 O VAL Q 41 N VAL Q 34
SHEET 4 AE9 5 ILE Q 208 LYS Q 214 -1 O THR Q 211 N LEU Q 42
SHEET 5 AE9 5 ASP Q 218 ALA Q 221 -1 O ASP Q 218 N LYS Q 214
SHEET 1 AF1 5 SER Q 63 LYS Q 64 0
SHEET 2 AF1 5 VAL Q 69 GLY Q 75 -1 O LEU Q 71 N SER Q 63
SHEET 3 AF1 5 VAL Q 129 GLY Q 135 -1 O ALA Q 134 N VAL Q 70
SHEET 4 AF1 5 LYS Q 144 THR Q 148 -1 O TYR Q 146 N ILE Q 133
SHEET 5 AF1 5 TYR Q 154 SER Q 156 -1 O SER Q 155 N GLN Q 147
SHEET 1 AF2 5 ALA R 161 ILE R 164 0
SHEET 2 AF2 5 ALA R 29 ALA R 33 -1 N ALA R 29 O ILE R 164
SHEET 3 AF2 5 VAL R 38 GLU R 43 -1 O GLY R 41 N ILE R 30
SHEET 4 AF2 5 ALA R 209 THR R 215 -1 O SER R 212 N LEU R 40
SHEET 5 AF2 5 GLY R 219 ILE R 222 -1 O LYS R 221 N CYS R 213
SHEET 1 AF3 5 ILE R 59 ASP R 63 0
SHEET 2 AF3 5 ILE R 66 GLY R 72 -1 O CYS R 68 N VAL R 60
SHEET 3 AF3 5 VAL R 132 ASP R 140 -1 O ALA R 137 N GLY R 67
SHEET 4 AF3 5 GLY R 144 ALA R 150 -1 O ALA R 150 N LEU R 134
SHEET 5 AF3 5 PHE R 156 ARG R 158 -1 O TYR R 157 N HIS R 149
SHEET 1 AF4 5 GLY S 157 ILE S 160 0
SHEET 2 AF4 5 THR S 34 ARG S 38 -1 N GLY S 36 O THR S 158
SHEET 3 AF4 5 HIS S 42 LEU S 48 -1 O VAL S 46 N VAL S 35
SHEET 4 AF4 5 LEU S 210 GLY S 216 -1 O SER S 211 N ALA S 47
SHEET 5 AF4 5 THR S 219 TYR S 224 -1 O TYR S 224 N ILE S 212
SHEET 1 AF5 5 ILE S 62 ASP S 66 0
SHEET 2 AF5 5 MET S 69 GLY S 75 -1 O LEU S 71 N ILE S 63
SHEET 3 AF5 5 VAL S 129 ASP S 137 -1 O ILE S 134 N GLY S 70
SHEET 4 AF5 5 GLY S 140 PHE S 146 -1 O PHE S 146 N LEU S 131
SHEET 5 AF5 5 VAL S 152 GLU S 154 -1 O THR S 153 N GLU S 145
SHEET 1 AF6 5 GLY T 158 THR T 161 0
SHEET 2 AF6 5 SER T 33 CYS T 38 -1 N GLY T 35 O ALA T 159
SHEET 3 AF6 5 GLY T 41 LEU T 49 -1 O GLY T 41 N CYS T 38
SHEET 4 AF6 5 PHE T 208 SER T 216 -1 O SER T 213 N PHE T 44
SHEET 5 AF6 5 HIS T 224 PHE T 226 -1 O LYS T 225 N TRP T 214
SHEET 1 AF7 5 GLN T 64 VAL T 66 0
SHEET 2 AF7 5 ILE T 70 GLY T 76 -1 O CYS T 72 N GLN T 64
SHEET 3 AF7 5 VAL T 130 ASP T 138 -1 O ILE T 133 N VAL T 73
SHEET 4 AF7 5 GLY T 141 LEU T 147 -1 O TYR T 145 N PHE T 134
SHEET 5 AF7 5 TYR T 153 GLY T 155 -1 O TRP T 154 N MET T 146
SHEET 1 AF8 5 THR U 160 THR U 162 0
SHEET 2 AF8 5 SER U 33 ARG U 37 -1 N SER U 33 O THR U 162
SHEET 3 AF8 5 THR U 42 GLN U 47 -1 O ILE U 45 N LEU U 34
SHEET 4 AF8 5 LEU U 214 THR U 220 -1 O GLY U 217 N VAL U 44
SHEET 5 AF8 5 LYS U 223 THR U 226 -1 O PHE U 225 N VAL U 218
SHEET 1 AF9 2 SER V 20 GLN V 22 0
SHEET 2 AF9 2 ILE V 25 ASP V 28 -1 O ILE V 25 N GLN V 22
SHEET 1 AG1 5 LEU V 34 SER V 38 0
SHEET 2 AG1 5 ILE V 41 THR V 48 -1 O CYS V 43 N HIS V 35
SHEET 3 AG1 5 ALA V 96 ASP V 104 -1 O TYR V 97 N ALA V 46
SHEET 4 AG1 5 GLY V 107 ILE V 113 -1 O PHE V 111 N VAL V 100
SHEET 5 AG1 5 THR V 119 VAL V 121 -1 O ASP V 120 N SER V 112
SHEET 1 AG2 3 LEU V 34 SER V 38 0
SHEET 2 AG2 3 ILE V 41 THR V 48 -1 O CYS V 43 N HIS V 35
SHEET 3 AG2 3 ALA f 3 IL0 f 4 -1 O IL0 f 4 N GLY V 47
SHEET 1 AG3 6 VAL V 212 VAL V 218 0
SHEET 2 AG3 6 GLU W 193 LEU W 199 -1 O VAL W 194 N VAL V 218
SHEET 3 AG3 6 ALA W 184 LYS W 190 -1 N ILE W 188 O VAL W 195
SHEET 4 AG3 6 CYS W 19 ASP W 25 -1 N VAL W 20 O ILE W 189
SHEET 5 AG3 6 ILE W 10 GLY W 16 -1 N VAL W 12 O ALA W 23
SHEET 6 AG3 6 PHE W 135 GLY W 139 -1 O ILE W 136 N ALA W 13
SHEET 1 AG4 2 LEU W 28 SER W 30 0
SHEET 2 AG4 2 LEU W 33 SER W 36 -1 O LEU W 33 N SER W 30
SHEET 1 AG5 5 ILE W 42 TYR W 45 0
SHEET 2 AG5 5 VAL W 48 GLY W 54 -1 O LEU W 50 N PHE W 43
SHEET 3 AG5 5 VAL W 104 ILE W 111 -1 O VAL W 107 N GLY W 51
SHEET 4 AG5 5 PRO W 118 PHE W 123 -1 O PHE W 119 N GLY W 110
SHEET 5 AG5 5 ILE W 129 GLU W 131 -1 O ASP W 130 N GLY W 122
SHEET 1 AG6 5 TYR X 130 HIS X 133 0
SHEET 2 AG6 5 ILE X 4 ARG X 8 -1 N GLY X 6 O GLY X 131
SHEET 3 AG6 5 VAL X 13 SER X 18 -1 O ALA X 16 N LEU X 5
SHEET 4 AG6 5 VAL X 179 ASP X 185 -1 O VAL X 184 N VAL X 13
SHEET 5 AG6 5 GLY X 188 VAL X 192 -1 O ARG X 190 N ILE X 183
SHEET 1 AG7 2 VAL X 21 ARG X 23 0
SHEET 2 AG7 2 SER X 26 LYS X 29 -1 O SER X 26 N ARG X 23
SHEET 1 AG8 5 THR X 35 SER X 39 0
SHEET 2 AG8 5 THR X 42 GLY X 48 -1 O MET X 44 N ARG X 36
SHEET 3 AG8 5 VAL X 100 ASP X 108 -1 O ASN X 101 N ALA X 47
SHEET 4 AG8 5 LYS X 113 ILE X 119 -1 O ILE X 119 N VAL X 102
SHEET 5 AG8 5 LYS X 125 GLU X 127 -1 O VAL X 126 N GLN X 118
SHEET 1 AG9 5 ILE Y 126 VAL Y 129 0
SHEET 2 AG9 5 THR Y 3 PHE Y 8 -1 N THR Y 3 O VAL Y 129
SHEET 3 AG9 5 GLY Y 11 VAL Y 16 -1 O ALA Y 15 N LEU Y 4
SHEET 4 AG9 5 SER Y 174 THR Y 181 -1 O VAL Y 180 N ILE Y 12
SHEET 5 AG9 5 GLY Y 184 ASP Y 192 -1 O GLY Y 184 N THR Y 181
SHEET 1 AH1 2 ALA Y 20 ALA Y 22 0
SHEET 2 AH1 2 TRP Y 25 SER Y 28 -1 O SER Y 28 N ALA Y 20
SHEET 1 AH2 5 VAL Y 34 ASN Y 38 0
SHEET 2 AH2 5 LEU Y 41 THR Y 44 -1 O GLY Y 43 N ILE Y 35
SHEET 3 AH2 5 GLY Y 98 THR Y 105 -1 O CYS Y 102 N LEU Y 42
SHEET 4 AH2 5 GLY Y 109 ASP Y 116 -1 O VAL Y 115 N THR Y 99
SHEET 5 AH2 5 ARG Y 121 LYS Y 123 -1 O LEU Y 122 N TYR Y 114
SHEET 1 AH3 2 GLY Y 47 GLY Y 48 0
SHEET 2 AH3 2 ALA g 3 IL0 g 4 -1 O IL0 g 4 N GLY Y 47
SHEET 1 AH4 5 CYS Z 136 GLY Z 140 0
SHEET 2 AH4 5 THR Z 11 ALA Z 16 -1 N ILE Z 12 O GLY Z 139
SHEET 3 AH4 5 ALA Z 21 ASP Z 26 -1 O ALA Z 24 N LEU Z 13
SHEET 4 AH4 5 GLY Z 201 THR Z 208 -1 O VAL Z 207 N ALA Z 21
SHEET 5 AH4 5 GLY Z 211 GLU Z 218 -1 O TYR Z 217 N LEU Z 202
SHEET 1 AH5 2 ASN Z 29 THR Z 31 0
SHEET 2 AH5 2 SER Z 34 SER Z 37 -1 O ASN Z 36 N ASN Z 29
SHEET 1 AH6 5 PHE Z 44 ASP Z 45 0
SHEET 2 AH6 5 VAL Z 51 GLY Z 56 -1 O MET Z 52 N PHE Z 44
SHEET 3 AH6 5 VAL Z 107 LEU Z 114 -1 O HIS Z 108 N ASN Z 55
SHEET 4 AH6 5 GLY Z 120 PHE Z 125 -1 O PHE Z 125 N THR Z 109
SHEET 5 AH6 5 TYR Z 131 GLU Z 134 -1 O GLU Z 134 N VAL Z 122
SHEET 1 AH7 5 LEU a 33 PHE a 36 0
SHEET 2 AH7 5 GLY a 28 TYR a 30 -1 N TYR a 30 O LEU a 33
SHEET 3 AH7 5 VAL a 6 GLY a 8 -1 N THR a 7 O SER a 29
SHEET 4 AH7 5 THR a 49 ASP a 56 -1 O GLY a 55 N GLY a 8
SHEET 5 AH7 5 LEU a 42 PRO a 44 -1 N ILE a 43 O VAL a 51
SHEET 1 AH8 7 LEU a 33 PHE a 36 0
SHEET 2 AH8 7 GLY a 28 TYR a 30 -1 N TYR a 30 O LEU a 33
SHEET 3 AH8 7 VAL a 6 GLY a 8 -1 N THR a 7 O SER a 29
SHEET 4 AH8 7 THR a 49 ASP a 56 -1 O GLY a 55 N GLY a 8
SHEET 5 AH8 7 ASN a 112 VAL a 119 -1 O ALA a 117 N VAL a 50
SHEET 6 AH8 7 GLN a 125 ASN a 131 -1 O VAL a 130 N ILE a 114
SHEET 7 AH8 7 THR a 136 TYR a 137 -1 O TYR a 137 N TYR a 129
SHEET 1 AH9 5 THR a 141 ALA a 143 0
SHEET 2 AH9 5 VAL a 11 LYS a 15 -1 N SER a 13 O LEU a 142
SHEET 3 AH9 5 GLY a 19 ASP a 25 -1 O ALA a 23 N ILE a 12
SHEET 4 AH9 5 ASN a 194 ASP a 201 -1 O ALA a 198 N ILE a 22
SHEET 5 AH9 5 GLY a 205 GLN a 213 -1 O LYS a 209 N LEU a 197
SHEET 1 AI1 5 TYR b 124 ALA b 127 0
SHEET 2 AI1 5 ILE b 3 THR b 7 -1 N ILE b 3 O ALA b 127
SHEET 3 AI1 5 GLY b 11 ALA b 16 -1 O GLY b 15 N MET b 4
SHEET 4 AI1 5 ILE b 173 THR b 179 -1 O LEU b 178 N VAL b 12
SHEET 5 AI1 5 VAL b 183 PHE b 188 -1 O GLU b 184 N VAL b 177
SHEET 1 AI2 2 THR b 20 THR b 22 0
SHEET 2 AI2 2 TYR b 25 ASN b 28 -1 O TYR b 25 N THR b 22
SHEET 1 AI3 5 LEU b 34 HIS b 38 0
SHEET 2 AI3 5 ILE b 41 SER b 48 -1 O CYS b 43 N THR b 35
SHEET 3 AI3 5 ALA b 95 TYR b 102 -1 O ALA b 100 N TRP b 42
SHEET 4 AI3 5 GLY b 108 ILE b 113 -1 O TYR b 111 N VAL b 99
SHEET 5 AI3 5 HIS b 120 LEU b 122 -1 O HIS b 120 N THR b 112
SHEET 1 AI4 3 LEU b 34 HIS b 38 0
SHEET 2 AI4 3 ILE b 41 SER b 48 -1 O CYS b 43 N THR b 35
SHEET 3 AI4 3 ALA h 3 IL0 h 4 -1 O IL0 h 4 N GLY b 47
LINK OG1 THR H 1 C IL0 c 4 1555 1555 1.41
LINK N THR H 1 C2 POL c 5 1555 1555 1.52
LINK OG1 THR K 1 C IL0 d 4 1555 1555 1.39
LINK N THR K 1 C2 POL d 5 1555 1555 1.50
LINK OG1 THR N 1 C IL0 e 4 1555 1555 1.42
LINK N THR N 1 C2 POL e 5 1555 1555 1.51
LINK OG1 THR V 1 C IL0 f 4 1555 1555 1.43
LINK N THR V 1 C2 POL f 5 1555 1555 1.51
LINK OG1 THR Y 1 C IL0 g 4 1555 1555 1.44
LINK N THR Y 1 C2 POL g 5 1555 1555 1.50
LINK OG1 THR b 1 C IL0 h 4 1555 1555 1.46
LINK N THR b 1 C2 POL h 5 1555 1555 1.49
LINK C ACE c 1 N LEU c 2 1555 1555 1.31
LINK C ALA c 3 N IL0 c 4 1555 1555 1.32
LINK C IL0 c 4 C2 POL c 5 1555 1555 1.61
LINK C ACE d 1 N LEU d 2 1555 1555 1.30
LINK C ALA d 3 N IL0 d 4 1555 1555 1.32
LINK C IL0 d 4 C2 POL d 5 1555 1555 1.63
LINK C ACE e 1 N LEU e 2 1555 1555 1.34
LINK C ALA e 3 N IL0 e 4 1555 1555 1.32
LINK C IL0 e 4 C2 POL e 5 1555 1555 1.62
LINK C ACE f 1 N LEU f 2 1555 1555 1.35
LINK C ALA f 3 N IL0 f 4 1555 1555 1.34
LINK C IL0 f 4 C2 POL f 5 1555 1555 1.60
LINK C ACE g 1 N LEU g 2 1555 1555 1.34
LINK C ALA g 3 N IL0 g 4 1555 1555 1.34
LINK C IL0 g 4 C2 POL g 5 1555 1555 1.62
LINK C ACE h 1 N LEU h 2 1555 1555 1.35
LINK C ALA h 3 N IL0 h 4 1555 1555 1.35
LINK C IL0 h 4 C2 POL h 5 1555 1555 1.62
LINK OG1 THR G 8 MG MG G 301 1555 1555 2.58
LINK O TYR G 119 MG MG G 301 1555 1555 2.66
LINK O ARG G 122 MG MG G 301 1555 1555 2.31
LINK O MET G 125 MG MG G 301 1555 1555 2.33
LINK MG MG G 301 O HOH G 424 1555 1555 2.21
LINK O ALA I 174 MG MG I 301 1555 1555 2.58
LINK O ASP I 177 MG MG I 301 1555 1555 2.63
LINK O SER I 180 MG MG I 301 1555 1555 2.54
LINK O ASP I 204 MG MG I 302 1555 1555 2.32
LINK MG MG I 302 O ALA Y 165 1555 1555 2.31
LINK MG MG I 302 O ASP Y 168 1555 1555 2.21
LINK MG MG I 302 O SER Y 171 1555 1555 2.32
LINK MG MG I 302 O HOH Y 313 1555 1555 2.49
LINK O ALA K 165 MG MG K 301 1555 1555 2.26
LINK O ASP K 168 MG MG K 301 1555 1555 2.17
LINK O SER K 171 MG MG K 301 1555 1555 2.52
LINK MG MG K 301 O ASP W 204 1555 1555 2.35
LINK OXT ASP L 222 MG MG L 301 1555 1555 2.32
LINK MG MG L 301 O ILE V 163 1555 1555 2.23
LINK MG MG L 301 O ASP V 166 1555 1555 2.06
LINK MG MG L 301 O SER V 169 1555 1555 2.38
LINK O ILE N 163 MG MG N 201 1555 1555 2.45
LINK O ASP N 166 MG MG N 201 1555 1555 2.73
LINK O SER N 169 MG MG N 201 1555 1555 2.42
LINK O THR Z 192 MG MG Z 301 1555 1555 2.61
LINK O HIS Z 195 MG MG Z 301 1555 1555 2.77
LINK O VAL Z 198 MG MG Z 301 1555 1555 2.40
SITE 1 AC1 6 THR G 8 TYR G 119 ARG G 122 ALA G 123
SITE 2 AC1 6 MET G 125 HOH G 424
SITE 1 AC2 3 ARG G 111 ASN G 114 TYR H 69
SITE 1 AC3 5 IL0 c 4 POL c 5 GLY H 47 GLY H 128
SITE 2 AC3 5 SER H 129
SITE 1 AC4 3 ALA I 174 ASP I 177 SER I 180
SITE 1 AC5 6 ASP I 204 ALA Y 165 ASP Y 168 ALA Y 169
SITE 2 AC5 6 SER Y 171 HOH Y 313
SITE 1 AC6 5 ALA K 165 ASP K 168 ALA K 169 SER K 171
SITE 2 AC6 5 ASP W 204
SITE 1 AC7 4 ASP L 222 ILE V 163 ASP V 166 SER V 169
SITE 1 AC8 4 ILE N 163 ASP N 166 SER N 169 LEU a 34
SITE 1 AC9 3 THR N 31 ARG N 45 GLN N 53
SITE 1 AD1 3 ARG U 111 ASN U 114 TYR V 69
SITE 1 AD2 4 ARG Z 28 THR Z 192 HIS Z 195 VAL Z 198
SITE 1 AD3 3 THR b 31 ARG b 45 GLN b 53
SITE 1 AD4 6 IL0 d 4 POL d 5 GLY K 47 MET K 97
SITE 2 AD4 6 GLY K 130 SER K 131
SITE 1 AD5 10 IL0 g 4 POL g 5 HOH g 202 THR Y 1
SITE 2 AD5 10 GLY Y 47 SER Y 96 MET Y 97 SER Y 117
SITE 3 AD5 10 GLY Y 130 SER Y 131
SITE 1 AD6 12 LEU c 2 THR H 1 ARG H 19 SER H 20
SITE 2 AD6 12 THR H 21 GLY H 45 ALA H 46 GLY H 47
SITE 3 AD6 12 ALA H 49 THR H 52 GLY H 168 MES H 301
SITE 1 AD7 6 ALA c 3 IL0 c 4 THR H 1 THR H 21
SITE 2 AD7 6 GLY H 168 MES H 301
SITE 1 AD8 10 LEU d 2 MES d 101 THR K 1 ARG K 19
SITE 2 AD8 10 ALA K 20 THR K 21 LYS K 33 GLY K 47
SITE 3 AD8 10 SER K 131 TYR K 170
SITE 1 AD9 6 ALA d 3 IL0 d 4 MES d 101 THR K 1
SITE 2 AD9 6 SER K 131 TYR K 170
SITE 1 AE1 10 LEU e 2 HOH e 101 THR N 1 ARG N 19
SITE 2 AE1 10 THR N 20 THR N 21 LYS N 33 ARG N 45
SITE 3 AE1 10 GLY N 47 SER N 168
SITE 1 AE2 6 ALA e 3 IL0 e 4 HOH e 101 THR N 1
SITE 2 AE2 6 ARG N 19 SER N 168
SITE 1 AE3 12 LEU f 2 HOH f 101 THR V 1 ARG V 19
SITE 2 AE3 12 SER V 20 THR V 21 LYS V 33 GLY V 45
SITE 3 AE3 12 GLY V 47 ALA V 49 THR V 52 GLY V 168
SITE 1 AE4 6 ALA f 3 IL0 f 4 THR V 1 ARG V 19
SITE 2 AE4 6 THR V 21 GLY V 168
SITE 1 AE5 9 LEU g 2 MES g 101 THR Y 1 ARG Y 19
SITE 2 AE5 9 ALA Y 20 THR Y 21 LYS Y 33 GLY Y 47
SITE 3 AE5 9 TYR Y 170
SITE 1 AE6 7 ALA g 3 IL0 g 4 MES g 101 THR Y 1
SITE 2 AE6 7 ARG Y 19 THR Y 21 TYR Y 170
SITE 1 AE7 10 LEU h 2 HOH h 101 THR b 1 ARG b 19
SITE 2 AE7 10 THR b 20 THR b 21 LYS b 33 ARG b 45
SITE 3 AE7 10 GLY b 47 SER b 168
SITE 1 AE8 7 ALA h 3 IL0 h 4 HOH h 101 THR b 1
SITE 2 AE8 7 ARG b 19 LYS b 33 SER b 168
SITE 1 AE9 4 ALA c 3 THR H 21 ALA H 49 ASP I 124
SITE 1 AF1 5 ALA d 3 THR K 21 ALA K 27 ALA K 49
SITE 2 AF1 5 ASP L 126
SITE 1 AF2 2 ALA e 3 ALA N 49
SITE 1 AF3 5 ALA f 3 GLN V 22 ALA V 27 ALA V 49
SITE 2 AF3 5 ASP W 124
SITE 1 AF4 6 ALA g 3 HOH g 201 THR Y 21 ALA Y 27
SITE 2 AF4 6 ALA Y 49 ASP Z 126
SITE 1 AF5 6 ALA h 3 HOH h 102 HIS V 114 SER V 118
SITE 2 AF5 6 THR b 22 ALA b 49
CRYST1 136.630 300.150 145.430 90.00 113.22 90.00 P 1 21 1 12
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 0.007319 0.000000 0.003141 0.00000
SCALE2 0.000000 0.003332 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007483 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 -0.999722 -0.000578 0.023568 68.35744 1
MTRIX2 2 -0.003452 -0.985335 -0.170593 -289.31433 1
MTRIX3 2 0.023321 -0.170627 0.985060 -25.44608 1
(ATOM LINES ARE NOT SHOWN.)
END
