HEADER HYDROLASE/HYDROLASE INHIBITOR 09-MAY-14 4QBY
TITLE YCP IN COMPLEX WITH BOC-ALA-ALA-ALA-CHO
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-2;
COMPND 3 CHAIN: A, O;
COMPND 4 FRAGMENT: ALPHA SUBUNIT;
COMPND 5 SYNONYM: MACROPAIN SUBUNIT Y7, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 6 SUBUNIT Y7, PROTEASOME COMPONENT Y7, PROTEINASE YSCE SUBUNIT 7;
COMPND 7 EC: 3.4.25.1;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-3;
COMPND 11 CHAIN: B, P;
COMPND 12 FRAGMENT: ALPHA SUBUNIT;
COMPND 13 SYNONYM: MACROPAIN SUBUNIT Y13, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 14 SUBUNIT Y13, PROTEASOME COMPONENT Y13, PROTEINASE YSCE SUBUNIT 13;
COMPND 15 EC: 3.4.25.1;
COMPND 16 MUTATION: YES;
COMPND 17 MOL_ID: 3;
COMPND 18 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-4;
COMPND 19 CHAIN: C, Q;
COMPND 20 FRAGMENT: ALPHA SUBUNIT;
COMPND 21 SYNONYM: MACROPAIN SUBUNIT PRE6, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 22 SUBUNIT PRE6, PROTEASOME COMPONENT PRE6, PROTEINASE YSCE SUBUNIT
COMPND 23 PRE6;
COMPND 24 EC: 3.4.25.1;
COMPND 25 MUTATION: YES;
COMPND 26 MOL_ID: 4;
COMPND 27 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-5;
COMPND 28 CHAIN: D, R;
COMPND 29 FRAGMENT: ALPHA SUBUNIT;
COMPND 30 SYNONYM: MACROPAIN SUBUNIT PUP2, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 31 SUBUNIT PUP2, PROTEASOME COMPONENT PUP2, PROTEINASE YSCE SUBUNIT
COMPND 32 PUP2;
COMPND 33 EC: 3.4.25.1;
COMPND 34 MUTATION: YES;
COMPND 35 MOL_ID: 5;
COMPND 36 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-6;
COMPND 37 CHAIN: E, S;
COMPND 38 FRAGMENT: ALPHA SUBUNIT;
COMPND 39 SYNONYM: MACROPAIN SUBUNIT PRE5, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 40 SUBUNIT PRE5, PROTEASOME COMPONENT PRE5, PROTEINASE YSCE SUBUNIT
COMPND 41 PRE5;
COMPND 42 EC: 3.4.25.1;
COMPND 43 MUTATION: YES;
COMPND 44 MOL_ID: 6;
COMPND 45 MOLECULE: PROBABLE PROTEASOME SUBUNIT ALPHA TYPE-7;
COMPND 46 CHAIN: F, T;
COMPND 47 FRAGMENT: ALPHA SUBUNIT;
COMPND 48 SYNONYM: MACROPAIN SUBUNIT C1, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 49 SUBUNIT C1, PROTEASOME COMPONENT C1, PROTEINASE YSCE SUBUNIT 1;
COMPND 50 EC: 3.4.25.1;
COMPND 51 MUTATION: YES;
COMPND 52 MOL_ID: 7;
COMPND 53 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-1;
COMPND 54 CHAIN: G, U;
COMPND 55 FRAGMENT: ALPHA SUBUNIT;
COMPND 56 SYNONYM: MACROPAIN SUBUNIT C7-ALPHA, MULTICATALYTIC ENDOPEPTIDASE
COMPND 57 COMPLEX C7, PROTEASOME COMPONENT C7-ALPHA, PROTEASOME COMPONENT Y8,
COMPND 58 PROTEINASE YSCE SUBUNIT 7, SCL1 SUPPRESSOR PROTEIN;
COMPND 59 EC: 3.4.25.1;
COMPND 60 MUTATION: YES;
COMPND 61 MOL_ID: 8;
COMPND 62 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-2;
COMPND 63 CHAIN: H, V;
COMPND 64 FRAGMENT: BETA SUBUNIT;
COMPND 65 SYNONYM: MACROPAIN SUBUNIT PUP1, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 66 SUBUNIT PUP1, PROTEASOME COMPONENT PUP1, PROTEINASE YSCE SUBUNIT
COMPND 67 PUP1;
COMPND 68 EC: 3.4.25.1;
COMPND 69 MUTATION: YES;
COMPND 70 MOL_ID: 9;
COMPND 71 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-3;
COMPND 72 CHAIN: I, W;
COMPND 73 FRAGMENT: ALPHA SUBUNIT;
COMPND 74 EC: 3.4.25.1;
COMPND 75 MUTATION: YES;
COMPND 76 MOL_ID: 10;
COMPND 77 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-4;
COMPND 78 CHAIN: J, X;
COMPND 79 FRAGMENT: BETA SUBUNIT;
COMPND 80 SYNONYM: MACROPAIN SUBUNIT PUP3, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 81 SUBUNIT PUP3, PROTEASOME COMPONENT PUP3;
COMPND 82 EC: 3.4.25.1;
COMPND 83 MUTATION: YES;
COMPND 84 MOL_ID: 11;
COMPND 85 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-5;
COMPND 86 CHAIN: K, Y;
COMPND 87 FRAGMENT: BETA SUBUNIT;
COMPND 88 SYNONYM: MACROPAIN SUBUNIT C11, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 89 SUBUNIT C11, PROTEASOME COMPONENT C11, PROTEINASE YSCE SUBUNIT 11;
COMPND 90 EC: 3.4.25.1;
COMPND 91 MUTATION: YES;
COMPND 92 MOL_ID: 12;
COMPND 93 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-6;
COMPND 94 CHAIN: L, Z;
COMPND 95 FRAGMENT: BETA SUBUNIT;
COMPND 96 SYNONYM: MACROPAIN SUBUNIT PRE2, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 97 SUBUNIT PRE2, PROTEASOME COMPONENT PRE2, PROTEINASE YSCE SUBUNIT
COMPND 98 PRE2;
COMPND 99 EC: 3.4.25.1;
COMPND 100 MUTATION: YES;
COMPND 101 MOL_ID: 13;
COMPND 102 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-7;
COMPND 103 CHAIN: M, a;
COMPND 104 FRAGMENT: BETA SUBUNIT;
COMPND 105 SYNONYM: MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C5, PROTEASOME
COMPND 106 COMPONENT C5;
COMPND 107 EC: 3.4.25.1;
COMPND 108 MUTATION: YES;
COMPND 109 MOL_ID: 14;
COMPND 110 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-1;
COMPND 111 CHAIN: N, b;
COMPND 112 FRAGMENT: BETA SUBUNIT;
COMPND 113 SYNONYM: MACROPAIN SUBUNIT PRE4, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 114 SUBUNIT PRE4, PROTEASOME COMPONENT PRE4, PROTEINASE YSCE SUBUNIT
COMPND 115 PRE4;
COMPND 116 EC: 3.4.25.1;
COMPND 117 MUTATION: YES;
COMPND 118 MOL_ID: 15;
COMPND 119 MOLECULE: BOC-ALA-ALA-ALA-CHO;
COMPND 120 CHAIN: 1, 2, 3, 4;
COMPND 121 SYNONYM: MACROPAIN SUBUNIT PRE3, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 122 SUBUNIT PRE3, PROTEASOME COMPONENT PRE3, PROTEINASE YSCE SUBUNIT
COMPND 123 PRE3;
COMPND 124 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 559292;
SOURCE 5 STRAIN: ATCC 204508 / S288C;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 8 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 9 ORGANISM_TAXID: 559292;
SOURCE 10 STRAIN: ATCC 204508 / S288C;
SOURCE 11 MOL_ID: 3;
SOURCE 12 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 13 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 14 ORGANISM_TAXID: 559292;
SOURCE 15 STRAIN: ATCC 204508 / S288C;
SOURCE 16 MOL_ID: 4;
SOURCE 17 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 18 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 19 ORGANISM_TAXID: 559292;
SOURCE 20 STRAIN: ATCC 204508 / S288C;
SOURCE 21 MOL_ID: 5;
SOURCE 22 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 23 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 24 ORGANISM_TAXID: 559292;
SOURCE 25 STRAIN: ATCC 204508 / S288C;
SOURCE 26 MOL_ID: 6;
SOURCE 27 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 28 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 29 ORGANISM_TAXID: 559292;
SOURCE 30 STRAIN: ATCC 204508 / S288C;
SOURCE 31 MOL_ID: 7;
SOURCE 32 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 33 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 34 ORGANISM_TAXID: 559292;
SOURCE 35 STRAIN: ATCC 204508 / S288C;
SOURCE 36 MOL_ID: 8;
SOURCE 37 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 38 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 39 ORGANISM_TAXID: 559292;
SOURCE 40 STRAIN: ATCC 204508 / S288C;
SOURCE 41 MOL_ID: 9;
SOURCE 42 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 43 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 44 ORGANISM_TAXID: 559292;
SOURCE 45 STRAIN: ATCC 204508 / S288C;
SOURCE 46 MOL_ID: 10;
SOURCE 47 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 48 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 49 ORGANISM_TAXID: 559292;
SOURCE 50 STRAIN: ATCC 204508 / S288C;
SOURCE 51 MOL_ID: 11;
SOURCE 52 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 53 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 54 ORGANISM_TAXID: 559292;
SOURCE 55 STRAIN: ATCC 204508 / S288C;
SOURCE 56 MOL_ID: 12;
SOURCE 57 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 58 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 59 ORGANISM_TAXID: 559292;
SOURCE 60 STRAIN: ATCC 204508 / S288C;
SOURCE 61 MOL_ID: 13;
SOURCE 62 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 63 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 64 ORGANISM_TAXID: 559292;
SOURCE 65 STRAIN: ATCC 204508 / S288C;
SOURCE 66 MOL_ID: 14;
SOURCE 67 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 68 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 69 ORGANISM_TAXID: 559292;
SOURCE 70 STRAIN: ATCC 204508 / S288C;
SOURCE 71 MOL_ID: 15;
SOURCE 72 SYNTHETIC: YES;
SOURCE 73 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 74 ORGANISM_TAXID: 4932
KEYWDS 20S PROTEASOME, PEPTIDE ALDEHYDE, ALLOSTERIC REGULATION, PCA
KEYWDS 2 ANALYSIS, IMMUNOPROTEASOME, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.ARCINIEGA,P.BECK,O.LANGE,M.GROLL,R.HUBER
REVDAT 4 15-NOV-23 4QBY 1 LINK ATOM
REVDAT 3 20-SEP-23 4QBY 1 REMARK LINK
REVDAT 2 16-JUL-14 4QBY 1 JRNL
REVDAT 1 18-JUN-14 4QBY 0
JRNL AUTH M.ARCINIEGA,P.BECK,O.F.LANGE,M.GROLL,R.HUBER
JRNL TITL DIFFERENTIAL GLOBAL STRUCTURAL CHANGES IN THE CORE PARTICLE
JRNL TITL 2 OF YEAST AND MOUSE PROTEASOME INDUCED BY LIGAND BINDING.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 111 9479 2014
JRNL REFN ISSN 0027-8424
JRNL PMID 24979800
JRNL DOI 10.1073/PNAS.1408018111
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.1
REMARK 3 NUMBER OF REFLECTIONS : 185233
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) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 9750
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) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 12608
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.50
REMARK 3 BIN R VALUE (WORKING SET) : 0.2960
REMARK 3 BIN FREE R VALUE SET COUNT : 664
REMARK 3 BIN FREE R VALUE : 0.3470
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 49454
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 11
REMARK 3 SOLVENT ATOMS : 180
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 68.74
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.97000
REMARK 3 B22 (A**2) : -7.17000
REMARK 3 B33 (A**2) : 2.08000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.43000
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): 0.336
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.246
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 32.174
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 50362 ; 0.005 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 48152 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 68138 ; 1.102 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES):110862 ; 0.747 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 6314 ; 6.450 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 2252 ;38.290 ;24.423
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 8754 ;19.587 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 284 ;18.350 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 7682 ; 0.062 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 57168 ; 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): 25346 ; 2.799 ; 6.083
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 25345 ; 2.799 ; 6.083
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 31630 ; 3.419 ; 9.109
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 31631 ; 3.418 ; 9.109
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 25016 ; 2.851 ; 6.434
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 25016 ; 2.850 ; 6.434
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 36508 ; 3.152 ; 9.507
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 54467 ; 3.834 ;47.678
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 54455 ; 3.829 ;47.680
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 98514 ; 2.173 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 139 ;32.981 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 97668 ; 6.813 ; 5.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
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 : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 250
REMARK 3 RESIDUE RANGE : A 301 A 307
REMARK 3 ORIGIN FOR THE GROUP (A): 66.988 -91.930 46.109
REMARK 3 T TENSOR
REMARK 3 T11: 0.0498 T22: 0.0780
REMARK 3 T33: 0.1167 T12: -0.0212
REMARK 3 T13: 0.0139 T23: -0.0181
REMARK 3 L TENSOR
REMARK 3 L11: 0.0240 L22: 0.0059
REMARK 3 L33: 0.0155 L12: -0.0071
REMARK 3 L13: 0.0141 L23: -0.0056
REMARK 3 S TENSOR
REMARK 3 S11: -0.0190 S12: 0.0007 S13: 0.0238
REMARK 3 S21: -0.0005 S22: 0.0079 S23: -0.0248
REMARK 3 S31: -0.0141 S32: -0.0189 S33: 0.0111
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 244
REMARK 3 RESIDUE RANGE : B 301 B 306
REMARK 3 ORIGIN FOR THE GROUP (A): 59.595 -87.727 16.524
REMARK 3 T TENSOR
REMARK 3 T11: 0.0737 T22: 0.0813
REMARK 3 T33: 0.0847 T12: -0.0288
REMARK 3 T13: 0.0465 T23: 0.0316
REMARK 3 L TENSOR
REMARK 3 L11: 0.0454 L22: 0.0432
REMARK 3 L33: 0.1928 L12: 0.0155
REMARK 3 L13: 0.0558 L23: 0.0874
REMARK 3 S TENSOR
REMARK 3 S11: -0.0373 S12: 0.0083 S13: -0.0081
REMARK 3 S21: -0.0200 S22: 0.0149 S23: 0.0206
REMARK 3 S31: -0.0620 S32: 0.0461 S33: 0.0224
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1 C 240
REMARK 3 RESIDUE RANGE : C 301 C 305
REMARK 3 ORIGIN FOR THE GROUP (A): 32.307 -87.280 1.161
REMARK 3 T TENSOR
REMARK 3 T11: 0.0892 T22: 0.0563
REMARK 3 T33: 0.0510 T12: -0.0009
REMARK 3 T13: -0.0035 T23: 0.0402
REMARK 3 L TENSOR
REMARK 3 L11: 0.1360 L22: 0.2199
REMARK 3 L33: 0.2231 L12: 0.1679
REMARK 3 L13: -0.0194 L23: 0.0153
REMARK 3 S TENSOR
REMARK 3 S11: -0.0146 S12: 0.0133 S13: 0.0172
REMARK 3 S21: -0.0411 S22: 0.0372 S23: 0.0289
REMARK 3 S31: -0.0213 S32: 0.0407 S33: -0.0226
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 1 D 242
REMARK 3 RESIDUE RANGE : D 301 D 305
REMARK 3 ORIGIN FOR THE GROUP (A): 3.076 -90.067 13.709
REMARK 3 T TENSOR
REMARK 3 T11: 0.0813 T22: 0.0488
REMARK 3 T33: 0.1315 T12: 0.0346
REMARK 3 T13: -0.0365 T23: 0.0450
REMARK 3 L TENSOR
REMARK 3 L11: 0.0780 L22: 0.0082
REMARK 3 L33: 0.1926 L12: 0.0017
REMARK 3 L13: -0.0752 L23: 0.0256
REMARK 3 S TENSOR
REMARK 3 S11: -0.0309 S12: -0.0024 S13: 0.0336
REMARK 3 S21: -0.0161 S22: -0.0017 S23: 0.0293
REMARK 3 S31: -0.0642 S32: -0.0136 S33: 0.0327
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 3 E 233
REMARK 3 RESIDUE RANGE : E 301 E 305
REMARK 3 ORIGIN FOR THE GROUP (A): -3.219 -94.323 45.779
REMARK 3 T TENSOR
REMARK 3 T11: 0.0346 T22: 0.0653
REMARK 3 T33: 0.1966 T12: 0.0297
REMARK 3 T13: 0.0533 T23: 0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 0.0122 L22: 0.0151
REMARK 3 L33: 0.3658 L12: -0.0132
REMARK 3 L13: 0.0510 L23: -0.0434
REMARK 3 S TENSOR
REMARK 3 S11: -0.0204 S12: -0.0105 S13: -0.0298
REMARK 3 S21: 0.0213 S22: 0.0086 S23: 0.0425
REMARK 3 S31: -0.0719 S32: -0.0569 S33: 0.0117
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 2 F 244
REMARK 3 RESIDUE RANGE : F 301 F 306
REMARK 3 ORIGIN FOR THE GROUP (A): 15.302 -94.943 69.981
REMARK 3 T TENSOR
REMARK 3 T11: 0.1135 T22: 0.0726
REMARK 3 T33: 0.0810 T12: 0.0048
REMARK 3 T13: 0.0859 T23: -0.0304
REMARK 3 L TENSOR
REMARK 3 L11: 0.3090 L22: 0.0705
REMARK 3 L33: 0.0848 L12: 0.0230
REMARK 3 L13: 0.0966 L23: 0.0570
REMARK 3 S TENSOR
REMARK 3 S11: 0.0227 S12: -0.0415 S13: 0.0350
REMARK 3 S21: 0.0400 S22: -0.0295 S23: 0.0437
REMARK 3 S31: -0.0023 S32: -0.0272 S33: 0.0069
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 2 G 242
REMARK 3 RESIDUE RANGE : G 301 G 301
REMARK 3 RESIDUE RANGE : G 401 G 410
REMARK 3 ORIGIN FOR THE GROUP (A): 47.807 -93.349 71.271
REMARK 3 T TENSOR
REMARK 3 T11: 0.1218 T22: 0.0569
REMARK 3 T33: 0.0212 T12: -0.0160
REMARK 3 T13: 0.0127 T23: -0.0212
REMARK 3 L TENSOR
REMARK 3 L11: 0.0439 L22: 0.2634
REMARK 3 L33: 0.1305 L12: -0.0782
REMARK 3 L13: 0.0666 L23: -0.1040
REMARK 3 S TENSOR
REMARK 3 S11: 0.0157 S12: 0.0093 S13: 0.0202
REMARK 3 S21: 0.0503 S22: -0.0558 S23: -0.0153
REMARK 3 S31: -0.0151 S32: 0.0024 S33: 0.0401
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 1 H 226
REMARK 3 RESIDUE RANGE : H 301 H 301
REMARK 3 RESIDUE RANGE : H 401 H 408
REMARK 3 ORIGIN FOR THE GROUP (A): 67.767 -129.359 47.498
REMARK 3 T TENSOR
REMARK 3 T11: 0.0616 T22: 0.0772
REMARK 3 T33: 0.1368 T12: -0.0032
REMARK 3 T13: -0.0157 T23: -0.0207
REMARK 3 L TENSOR
REMARK 3 L11: 0.0097 L22: 0.1240
REMARK 3 L33: 0.0262 L12: 0.0240
REMARK 3 L13: 0.0056 L23: -0.0070
REMARK 3 S TENSOR
REMARK 3 S11: 0.0180 S12: 0.0050 S13: -0.0248
REMARK 3 S21: 0.0550 S22: 0.0019 S23: -0.1071
REMARK 3 S31: -0.0175 S32: 0.0011 S33: -0.0200
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 1 I 204
REMARK 3 RESIDUE RANGE : I 301 I 302
REMARK 3 RESIDUE RANGE : I 401 I 404
REMARK 3 ORIGIN FOR THE GROUP (A): 68.519 -127.347 20.916
REMARK 3 T TENSOR
REMARK 3 T11: 0.0356 T22: 0.1100
REMARK 3 T33: 0.0858 T12: 0.0025
REMARK 3 T13: 0.0547 T23: 0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 0.0412 L22: 0.2838
REMARK 3 L33: 0.0053 L12: 0.0748
REMARK 3 L13: -0.0137 L23: -0.0343
REMARK 3 S TENSOR
REMARK 3 S11: 0.0154 S12: 0.0245 S13: 0.0128
REMARK 3 S21: -0.0275 S22: -0.0209 S23: -0.0628
REMARK 3 S31: 0.0003 S32: -0.0072 S33: 0.0055
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 1 J 195
REMARK 3 RESIDUE RANGE : J 201 J 201
REMARK 3 RESIDUE RANGE : J 301 J 308
REMARK 3 ORIGIN FOR THE GROUP (A): 44.767 -126.430 -0.533
REMARK 3 T TENSOR
REMARK 3 T11: 0.0905 T22: 0.0735
REMARK 3 T33: 0.0415 T12: 0.0021
REMARK 3 T13: 0.0587 T23: 0.0121
REMARK 3 L TENSOR
REMARK 3 L11: 0.1413 L22: 0.0654
REMARK 3 L33: 0.3118 L12: 0.0775
REMARK 3 L13: 0.2030 L23: 0.1270
REMARK 3 S TENSOR
REMARK 3 S11: -0.0072 S12: -0.0157 S13: 0.0080
REMARK 3 S21: -0.0482 S22: 0.0032 S23: -0.0223
REMARK 3 S31: -0.0336 S32: 0.0100 S33: 0.0040
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K 1 K 212
REMARK 3 RESIDUE RANGE : K 301 K 302
REMARK 3 RESIDUE RANGE : K 401 K 403
REMARK 3 ORIGIN FOR THE GROUP (A): 10.955 -130.757 2.659
REMARK 3 T TENSOR
REMARK 3 T11: 0.0428 T22: 0.0823
REMARK 3 T33: 0.1089 T12: 0.0116
REMARK 3 T13: -0.0568 T23: 0.0220
REMARK 3 L TENSOR
REMARK 3 L11: 0.1453 L22: 0.1146
REMARK 3 L33: 0.1066 L12: 0.1252
REMARK 3 L13: -0.1233 L23: -0.1098
REMARK 3 S TENSOR
REMARK 3 S11: 0.0099 S12: 0.0299 S13: 0.0369
REMARK 3 S21: -0.0073 S22: 0.0339 S23: 0.0576
REMARK 3 S31: 0.0014 S32: -0.0272 S33: -0.0438
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 1 L 222
REMARK 3 RESIDUE RANGE : L 301 L 307
REMARK 3 ORIGIN FOR THE GROUP (A): -4.413 -134.354 28.663
REMARK 3 T TENSOR
REMARK 3 T11: 0.0121 T22: 0.0851
REMARK 3 T33: 0.1425 T12: 0.0091
REMARK 3 T13: 0.0013 T23: 0.0383
REMARK 3 L TENSOR
REMARK 3 L11: 0.0066 L22: 0.1666
REMARK 3 L33: 0.1008 L12: -0.0259
REMARK 3 L13: -0.0149 L23: 0.1228
REMARK 3 S TENSOR
REMARK 3 S11: 0.0014 S12: 0.0035 S13: -0.0223
REMARK 3 S21: -0.0056 S22: -0.0133 S23: 0.0645
REMARK 3 S31: -0.0043 S32: -0.0113 S33: 0.0119
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : M 1 M 233
REMARK 3 RESIDUE RANGE : M 301 M 310
REMARK 3 ORIGIN FOR THE GROUP (A): 7.901 -137.797 60.486
REMARK 3 T TENSOR
REMARK 3 T11: 0.0782 T22: 0.0820
REMARK 3 T33: 0.0786 T12: -0.0051
REMARK 3 T13: 0.0709 T23: 0.0073
REMARK 3 L TENSOR
REMARK 3 L11: 0.0336 L22: 0.2470
REMARK 3 L33: 0.0134 L12: -0.0425
REMARK 3 L13: 0.0064 L23: 0.0358
REMARK 3 S TENSOR
REMARK 3 S11: 0.0036 S12: -0.0156 S13: -0.0132
REMARK 3 S21: 0.0938 S22: -0.0067 S23: 0.0777
REMARK 3 S31: 0.0135 S32: -0.0101 S33: 0.0031
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : N 1 N 196
REMARK 3 RESIDUE RANGE : N 201 N 201
REMARK 3 RESIDUE RANGE : N 301 N 306
REMARK 3 ORIGIN FOR THE GROUP (A): 39.957 -133.892 71.033
REMARK 3 T TENSOR
REMARK 3 T11: 0.1313 T22: 0.0688
REMARK 3 T33: 0.0042 T12: -0.0221
REMARK 3 T13: 0.0035 T23: -0.0151
REMARK 3 L TENSOR
REMARK 3 L11: 0.0819 L22: 0.2704
REMARK 3 L33: 0.2313 L12: -0.1321
REMARK 3 L13: -0.1175 L23: 0.1714
REMARK 3 S TENSOR
REMARK 3 S11: 0.0124 S12: 0.0029 S13: 0.0002
REMARK 3 S21: 0.0696 S22: -0.0145 S23: -0.0003
REMARK 3 S31: -0.0100 S32: 0.0355 S33: 0.0021
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : O 1 O 250
REMARK 3 RESIDUE RANGE : O 301 O 305
REMARK 3 ORIGIN FOR THE GROUP (A): 2.152 -206.495 37.122
REMARK 3 T TENSOR
REMARK 3 T11: 0.0715 T22: 0.0547
REMARK 3 T33: 0.1109 T12: -0.0416
REMARK 3 T13: -0.0107 T23: 0.0286
REMARK 3 L TENSOR
REMARK 3 L11: 0.0931 L22: 0.0446
REMARK 3 L33: 0.1925 L12: -0.0067
REMARK 3 L13: -0.0440 L23: 0.0768
REMARK 3 S TENSOR
REMARK 3 S11: -0.0124 S12: -0.0128 S13: 0.0105
REMARK 3 S21: 0.0003 S22: 0.0105 S23: 0.0188
REMARK 3 S31: 0.0607 S32: -0.0232 S33: 0.0019
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : P 1 P 244
REMARK 3 RESIDUE RANGE : P 301 P 308
REMARK 3 ORIGIN FOR THE GROUP (A): 8.527 -205.441 6.983
REMARK 3 T TENSOR
REMARK 3 T11: 0.0963 T22: 0.0795
REMARK 3 T33: 0.0800 T12: -0.0235
REMARK 3 T13: -0.0394 T23: -0.0255
REMARK 3 L TENSOR
REMARK 3 L11: 0.1517 L22: 0.0990
REMARK 3 L33: 0.0248 L12: -0.0173
REMARK 3 L13: -0.0563 L23: 0.0006
REMARK 3 S TENSOR
REMARK 3 S11: -0.0550 S12: -0.0174 S13: 0.0134
REMARK 3 S21: -0.0719 S22: 0.0442 S23: 0.0051
REMARK 3 S31: 0.0214 S32: -0.0079 S33: 0.0108
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Q 1 Q 240
REMARK 3 RESIDUE RANGE : Q 301 Q 306
REMARK 3 ORIGIN FOR THE GROUP (A): 35.607 -203.496 -8.878
REMARK 3 T TENSOR
REMARK 3 T11: 0.1320 T22: 0.0502
REMARK 3 T33: 0.0771 T12: 0.0148
REMARK 3 T13: -0.0293 T23: -0.0430
REMARK 3 L TENSOR
REMARK 3 L11: 0.0905 L22: 0.1289
REMARK 3 L33: 0.2300 L12: 0.0964
REMARK 3 L13: 0.0662 L23: 0.0577
REMARK 3 S TENSOR
REMARK 3 S11: 0.0197 S12: 0.0128 S13: 0.0081
REMARK 3 S21: -0.0489 S22: 0.0245 S23: 0.0165
REMARK 3 S31: 0.0316 S32: -0.0101 S33: -0.0441
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : R 1 R 242
REMARK 3 RESIDUE RANGE : R 301 R 303
REMARK 3 ORIGIN FOR THE GROUP (A): 65.159 -202.766 3.380
REMARK 3 T TENSOR
REMARK 3 T11: 0.1112 T22: 0.0608
REMARK 3 T33: 0.1061 T12: 0.0400
REMARK 3 T13: 0.0706 T23: -0.0275
REMARK 3 L TENSOR
REMARK 3 L11: 0.1757 L22: 0.0469
REMARK 3 L33: 0.2039 L12: 0.0529
REMARK 3 L13: 0.1318 L23: 0.0076
REMARK 3 S TENSOR
REMARK 3 S11: -0.0002 S12: -0.0267 S13: 0.0166
REMARK 3 S21: -0.0570 S22: -0.0165 S23: -0.0397
REMARK 3 S31: 0.0517 S32: 0.0333 S33: 0.0168
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : S 3 S 233
REMARK 3 RESIDUE RANGE : S 301 S 301
REMARK 3 ORIGIN FOR THE GROUP (A): 72.347 -203.894 35.370
REMARK 3 T TENSOR
REMARK 3 T11: 0.0501 T22: 0.0649
REMARK 3 T33: 0.1917 T12: 0.0532
REMARK 3 T13: -0.0280 T23: -0.0508
REMARK 3 L TENSOR
REMARK 3 L11: 0.0385 L22: 0.0229
REMARK 3 L33: 0.2088 L12: 0.0119
REMARK 3 L13: -0.0619 L23: -0.0590
REMARK 3 S TENSOR
REMARK 3 S11: 0.0057 S12: 0.0004 S13: 0.0015
REMARK 3 S21: -0.0158 S22: -0.0087 S23: -0.0311
REMARK 3 S31: 0.0541 S32: 0.0506 S33: 0.0030
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : T 2 T 244
REMARK 3 RESIDUE RANGE : T 301 T 307
REMARK 3 ORIGIN FOR THE GROUP (A): 54.492 -207.421 59.719
REMARK 3 T TENSOR
REMARK 3 T11: 0.1424 T22: 0.0395
REMARK 3 T33: 0.1170 T12: 0.0166
REMARK 3 T13: -0.0970 T23: 0.0305
REMARK 3 L TENSOR
REMARK 3 L11: 0.1911 L22: 0.0293
REMARK 3 L33: 0.1241 L12: 0.0448
REMARK 3 L13: -0.0267 L23: -0.0227
REMARK 3 S TENSOR
REMARK 3 S11: 0.0396 S12: -0.0400 S13: -0.0861
REMARK 3 S21: 0.0404 S22: -0.0159 S23: -0.0504
REMARK 3 S31: 0.0279 S32: -0.0137 S33: -0.0237
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : U 2 U 242
REMARK 3 RESIDUE RANGE : U 301 U 305
REMARK 3 ORIGIN FOR THE GROUP (A): 22.110 -209.536 61.450
REMARK 3 T TENSOR
REMARK 3 T11: 0.1087 T22: 0.0462
REMARK 3 T33: 0.0653 T12: -0.0138
REMARK 3 T13: -0.0211 T23: 0.0220
REMARK 3 L TENSOR
REMARK 3 L11: 0.0173 L22: 0.2030
REMARK 3 L33: 0.1042 L12: 0.0031
REMARK 3 L13: 0.0065 L23: -0.0162
REMARK 3 S TENSOR
REMARK 3 S11: 0.0293 S12: 0.0038 S13: -0.0229
REMARK 3 S21: 0.0186 S22: 0.0092 S23: 0.0231
REMARK 3 S31: -0.0219 S32: 0.0043 S33: -0.0384
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : V 1 V 226
REMARK 3 RESIDUE RANGE : V 301 V 301
REMARK 3 RESIDUE RANGE : V 401 V 411
REMARK 3 ORIGIN FOR THE GROUP (A): 1.555 -169.853 44.896
REMARK 3 T TENSOR
REMARK 3 T11: 0.0372 T22: 0.0774
REMARK 3 T33: 0.1165 T12: -0.0090
REMARK 3 T13: 0.0220 T23: 0.0275
REMARK 3 L TENSOR
REMARK 3 L11: 0.0654 L22: 0.2006
REMARK 3 L33: 0.0035 L12: 0.0873
REMARK 3 L13: 0.0140 L23: 0.0248
REMARK 3 S TENSOR
REMARK 3 S11: 0.0184 S12: -0.0015 S13: -0.0001
REMARK 3 S21: 0.0542 S22: -0.0186 S23: 0.0897
REMARK 3 S31: 0.0072 S32: -0.0024 S33: 0.0002
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : W 1 W 204
REMARK 3 RESIDUE RANGE : W 301 W 303
REMARK 3 ORIGIN FOR THE GROUP (A): 0.056 -167.287 18.327
REMARK 3 T TENSOR
REMARK 3 T11: 0.0346 T22: 0.0877
REMARK 3 T33: 0.0871 T12: -0.0033
REMARK 3 T13: -0.0461 T23: 0.0109
REMARK 3 L TENSOR
REMARK 3 L11: 0.1214 L22: 0.4115
REMARK 3 L33: 0.0192 L12: -0.0600
REMARK 3 L13: -0.0432 L23: -0.0135
REMARK 3 S TENSOR
REMARK 3 S11: 0.0049 S12: 0.0402 S13: -0.0023
REMARK 3 S21: -0.1082 S22: 0.0042 S23: 0.1072
REMARK 3 S31: 0.0091 S32: -0.0100 S33: -0.0091
REMARK 3
REMARK 3 TLS GROUP : 24
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : X 1 X 195
REMARK 3 RESIDUE RANGE : X 201 X 207
REMARK 3 ORIGIN FOR THE GROUP (A): 23.196 -164.458 -3.572
REMARK 3 T TENSOR
REMARK 3 T11: 0.1068 T22: 0.0708
REMARK 3 T33: 0.0575 T12: 0.0120
REMARK 3 T13: -0.0209 T23: 0.0073
REMARK 3 L TENSOR
REMARK 3 L11: 0.0048 L22: 0.1741
REMARK 3 L33: 0.0614 L12: -0.0248
REMARK 3 L13: 0.0136 L23: -0.0958
REMARK 3 S TENSOR
REMARK 3 S11: 0.0009 S12: -0.0138 S13: -0.0012
REMARK 3 S21: -0.0786 S22: 0.0337 S23: 0.0197
REMARK 3 S31: 0.0279 S32: -0.0343 S33: -0.0346
REMARK 3
REMARK 3 TLS GROUP : 25
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Y 1 Y 212
REMARK 3 RESIDUE RANGE : Y 301 Y 301
REMARK 3 RESIDUE RANGE : Y 401 Y 405
REMARK 3 ORIGIN FOR THE GROUP (A): 57.111 -160.704 -0.520
REMARK 3 T TENSOR
REMARK 3 T11: 0.0776 T22: 0.0919
REMARK 3 T33: 0.1038 T12: 0.0077
REMARK 3 T13: 0.0668 T23: -0.0287
REMARK 3 L TENSOR
REMARK 3 L11: 0.2110 L22: 0.1964
REMARK 3 L33: 0.1193 L12: 0.1767
REMARK 3 L13: 0.1253 L23: 0.0734
REMARK 3 S TENSOR
REMARK 3 S11: -0.0044 S12: 0.0492 S13: -0.0351
REMARK 3 S21: -0.0514 S22: 0.0488 S23: -0.0660
REMARK 3 S31: 0.0176 S32: 0.0199 S33: -0.0444
REMARK 3
REMARK 3 TLS GROUP : 26
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Z 1 Z 222
REMARK 3 RESIDUE RANGE : Z 301 Z 301
REMARK 3 RESIDUE RANGE : Z 401 Z 404
REMARK 3 ORIGIN FOR THE GROUP (A): 73.185 -161.568 25.327
REMARK 3 T TENSOR
REMARK 3 T11: 0.0194 T22: 0.0927
REMARK 3 T33: 0.1249 T12: 0.0217
REMARK 3 T13: 0.0192 T23: -0.0291
REMARK 3 L TENSOR
REMARK 3 L11: 0.0856 L22: 0.3635
REMARK 3 L33: 0.2058 L12: -0.0775
REMARK 3 L13: -0.0967 L23: -0.0666
REMARK 3 S TENSOR
REMARK 3 S11: 0.0076 S12: -0.0045 S13: 0.0283
REMARK 3 S21: -0.0161 S22: -0.0031 S23: -0.1135
REMARK 3 S31: 0.0106 S32: 0.0239 S33: -0.0045
REMARK 3
REMARK 3 TLS GROUP : 27
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : a 1 a 233
REMARK 3 RESIDUE RANGE : a 301 a 316
REMARK 3 ORIGIN FOR THE GROUP (A): 61.773 -163.612 57.538
REMARK 3 T TENSOR
REMARK 3 T11: 0.0649 T22: 0.0689
REMARK 3 T33: 0.0752 T12: 0.0184
REMARK 3 T13: -0.0389 T23: -0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 0.0388 L22: 0.1546
REMARK 3 L33: 0.0277 L12: 0.0104
REMARK 3 L13: 0.0196 L23: -0.0465
REMARK 3 S TENSOR
REMARK 3 S11: 0.0030 S12: 0.0196 S13: -0.0298
REMARK 3 S21: 0.0486 S22: -0.0057 S23: -0.0551
REMARK 3 S31: -0.0160 S32: 0.0133 S33: 0.0027
REMARK 3
REMARK 3 TLS GROUP : 28
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : b 1 b 196
REMARK 3 RESIDUE RANGE : b 201 b 205
REMARK 3 ORIGIN FOR THE GROUP (A): 30.013 -169.376 68.129
REMARK 3 T TENSOR
REMARK 3 T11: 0.1097 T22: 0.0607
REMARK 3 T33: 0.0225 T12: -0.0187
REMARK 3 T13: 0.0135 T23: 0.0280
REMARK 3 L TENSOR
REMARK 3 L11: 0.0336 L22: 0.1914
REMARK 3 L33: 0.2604 L12: -0.0164
REMARK 3 L13: 0.0710 L23: -0.1732
REMARK 3 S TENSOR
REMARK 3 S11: 0.0083 S12: 0.0016 S13: -0.0018
REMARK 3 S21: 0.0723 S22: 0.0060 S23: 0.0042
REMARK 3 S31: -0.0152 S32: -0.0212 S33: -0.0143
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 4QBY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAY-14.
REMARK 100 THE DEPOSITION ID IS D_1000085861.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-NOV-13
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 : XDS, XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 194983
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.0
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.08600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.54100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
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 (%): 66.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 MM MGAC2, 100 MM MES, 13% MPD , 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 150.06500
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 300 REMARK: AU CONTAINS ONE BIOLOGICAL ASSEMBLY.
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: 32-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, 1, Z, 2, a,
REMARK 350 AND CHAINS: 3, b, 4
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 400
REMARK 400 COMPOUND
REMARK 400
REMARK 400 THE BOC-ALA-ALA-ALA-AL-CHO IS PEPTIDE-LIKE, A MEMBER OF INHIBITOR
REMARK 400 CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: BOC-ALA-ALA-ALA-AL-CHO
REMARK 400 CHAIN: 1, 2, 3, 4
REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER
REMARK 400 DESCRIPTION: NULL
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET B 0
REMARK 465 LYS B 245
REMARK 465 LYS B 246
REMARK 465 ASP B 247
REMARK 465 GLU B 248
REMARK 465 ASP B 249
REMARK 465 GLU B 250
REMARK 465 GLU B 251
REMARK 465 ALA B 252
REMARK 465 ASP B 253
REMARK 465 GLU B 254
REMARK 465 ASP B 255
REMARK 465 MET B 256
REMARK 465 LYS B 257
REMARK 465 MET C -1
REMARK 465 SER C 0
REMARK 465 GLN C 241
REMARK 465 GLN C 242
REMARK 465 GLU C 243
REMARK 465 GLN C 244
REMARK 465 ASP C 245
REMARK 465 LYS C 246
REMARK 465 LYS C 247
REMARK 465 LYS C 248
REMARK 465 LYS C 249
REMARK 465 SER C 250
REMARK 465 ASN C 251
REMARK 465 HIS C 252
REMARK 465 MET D -7
REMARK 465 PHE D -6
REMARK 465 LEU D -5
REMARK 465 THR D -4
REMARK 465 ARG D -3
REMARK 465 SER D -2
REMARK 465 GLU D -1
REMARK 465 TYR D 0
REMARK 465 GLY D 118
REMARK 465 ALA D 119
REMARK 465 SER D 120
REMARK 465 GLY D 121
REMARK 465 GLU D 122
REMARK 465 GLU D 123
REMARK 465 ARG D 124
REMARK 465 SER D 243
REMARK 465 PRO D 244
REMARK 465 GLU D 245
REMARK 465 GLU D 246
REMARK 465 ALA D 247
REMARK 465 ASP D 248
REMARK 465 VAL D 249
REMARK 465 GLU D 250
REMARK 465 MET D 251
REMARK 465 SER D 252
REMARK 465 MET E 0
REMARK 465 PHE E 1
REMARK 465 ARG E 2
REMARK 465 MET F -3
REMARK 465 THR F -2
REMARK 465 SER F -1
REMARK 465 ILE F 0
REMARK 465 GLY F 1
REMARK 465 GLY F 245
REMARK 465 ASP F 246
REMARK 465 ASP F 247
REMARK 465 ASP F 248
REMARK 465 GLU F 249
REMARK 465 ASP F 250
REMARK 465 GLU F 251
REMARK 465 ASP F 252
REMARK 465 ASP F 253
REMARK 465 SER F 254
REMARK 465 ASP F 255
REMARK 465 ASN F 256
REMARK 465 VAL F 257
REMARK 465 MET F 258
REMARK 465 SER F 259
REMARK 465 SER F 260
REMARK 465 ASP F 261
REMARK 465 ASP F 262
REMARK 465 GLU F 263
REMARK 465 ASN F 264
REMARK 465 ALA F 265
REMARK 465 PRO F 266
REMARK 465 VAL F 267
REMARK 465 ALA F 268
REMARK 465 THR F 269
REMARK 465 ASN F 270
REMARK 465 ALA F 271
REMARK 465 ASN F 272
REMARK 465 ALA F 273
REMARK 465 THR F 274
REMARK 465 THR F 275
REMARK 465 ASP F 276
REMARK 465 GLN F 277
REMARK 465 GLU F 278
REMARK 465 GLY F 279
REMARK 465 ASP F 280
REMARK 465 ILE F 281
REMARK 465 HIS F 282
REMARK 465 LEU F 283
REMARK 465 GLU F 284
REMARK 465 MET G -8
REMARK 465 SER G -7
REMARK 465 GLY G -6
REMARK 465 ALA G -5
REMARK 465 ALA G -4
REMARK 465 ALA G -3
REMARK 465 ALA G -2
REMARK 465 SER G -1
REMARK 465 ALA G 0
REMARK 465 ALA G 1
REMARK 465 ASP G 243
REMARK 465 GLN H 227
REMARK 465 VAL H 228
REMARK 465 ASP H 229
REMARK 465 ILE H 230
REMARK 465 THR H 231
REMARK 465 ALA H 232
REMARK 465 MET I 0
REMARK 465 GLN J 196
REMARK 465 ALA J 197
REMARK 465 GLN J 198
REMARK 465 THR M -12
REMARK 465 GLN M -11
REMARK 465 ILE M -10
REMARK 465 ALA M -9
REMARK 465 ASN M -8
REMARK 465 ALA M -7
REMARK 465 GLY M -6
REMARK 465 ALA M -5
REMARK 465 SER M -4
REMARK 465 PRO M -3
REMARK 465 MET M -2
REMARK 465 VAL M -1
REMARK 465 ASN M 0
REMARK 465 MET P 0
REMARK 465 LYS P 245
REMARK 465 LYS P 246
REMARK 465 ASP P 247
REMARK 465 GLU P 248
REMARK 465 ASP P 249
REMARK 465 GLU P 250
REMARK 465 GLU P 251
REMARK 465 ALA P 252
REMARK 465 ASP P 253
REMARK 465 GLU P 254
REMARK 465 ASP P 255
REMARK 465 MET P 256
REMARK 465 LYS P 257
REMARK 465 MET Q -1
REMARK 465 SER Q 0
REMARK 465 GLN Q 241
REMARK 465 GLN Q 242
REMARK 465 GLU Q 243
REMARK 465 GLN Q 244
REMARK 465 ASP Q 245
REMARK 465 LYS Q 246
REMARK 465 LYS Q 247
REMARK 465 LYS Q 248
REMARK 465 LYS Q 249
REMARK 465 SER Q 250
REMARK 465 ASN Q 251
REMARK 465 HIS Q 252
REMARK 465 MET R -7
REMARK 465 PHE R -6
REMARK 465 LEU R -5
REMARK 465 THR R -4
REMARK 465 ARG R -3
REMARK 465 SER R -2
REMARK 465 GLU R -1
REMARK 465 TYR R 0
REMARK 465 GLY R 118
REMARK 465 ALA R 119
REMARK 465 SER R 120
REMARK 465 GLY R 121
REMARK 465 GLU R 122
REMARK 465 GLU R 123
REMARK 465 ARG R 124
REMARK 465 SER R 243
REMARK 465 PRO R 244
REMARK 465 GLU R 245
REMARK 465 GLU R 246
REMARK 465 ALA R 247
REMARK 465 ASP R 248
REMARK 465 VAL R 249
REMARK 465 GLU R 250
REMARK 465 MET R 251
REMARK 465 SER R 252
REMARK 465 MET S 0
REMARK 465 PHE S 1
REMARK 465 ARG S 2
REMARK 465 MET T -3
REMARK 465 THR T -2
REMARK 465 SER T -1
REMARK 465 ILE T 0
REMARK 465 GLY T 1
REMARK 465 GLY T 245
REMARK 465 ASP T 246
REMARK 465 ASP T 247
REMARK 465 ASP T 248
REMARK 465 GLU T 249
REMARK 465 ASP T 250
REMARK 465 GLU T 251
REMARK 465 ASP T 252
REMARK 465 ASP T 253
REMARK 465 SER T 254
REMARK 465 ASP T 255
REMARK 465 ASN T 256
REMARK 465 VAL T 257
REMARK 465 MET T 258
REMARK 465 SER T 259
REMARK 465 SER T 260
REMARK 465 ASP T 261
REMARK 465 ASP T 262
REMARK 465 GLU T 263
REMARK 465 ASN T 264
REMARK 465 ALA T 265
REMARK 465 PRO T 266
REMARK 465 VAL T 267
REMARK 465 ALA T 268
REMARK 465 THR T 269
REMARK 465 ASN T 270
REMARK 465 ALA T 271
REMARK 465 ASN T 272
REMARK 465 ALA T 273
REMARK 465 THR T 274
REMARK 465 THR T 275
REMARK 465 ASP T 276
REMARK 465 GLN T 277
REMARK 465 GLU T 278
REMARK 465 GLY T 279
REMARK 465 ASP T 280
REMARK 465 ILE T 281
REMARK 465 HIS T 282
REMARK 465 LEU T 283
REMARK 465 GLU T 284
REMARK 465 MET U -8
REMARK 465 SER U -7
REMARK 465 GLY U -6
REMARK 465 ALA U -5
REMARK 465 ALA U -4
REMARK 465 ALA U -3
REMARK 465 ALA U -2
REMARK 465 SER U -1
REMARK 465 ALA U 0
REMARK 465 ALA U 1
REMARK 465 ASP U 243
REMARK 465 GLN V 227
REMARK 465 VAL V 228
REMARK 465 ASP V 229
REMARK 465 ILE V 230
REMARK 465 THR V 231
REMARK 465 ALA V 232
REMARK 465 MET W 0
REMARK 465 GLN X 196
REMARK 465 ALA X 197
REMARK 465 GLN X 198
REMARK 465 THR a -12
REMARK 465 GLN a -11
REMARK 465 ILE a -10
REMARK 465 ALA a -9
REMARK 465 ASN a -8
REMARK 465 ALA a -7
REMARK 465 GLY a -6
REMARK 465 ALA a -5
REMARK 465 SER a -4
REMARK 465 PRO a -3
REMARK 465 MET a -2
REMARK 465 VAL a -1
REMARK 465 ASN a 0
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 ND2 ASN K 209 OH TYR X 130 1.93
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 -148.74 28.24
REMARK 500 TYR A 97 -68.45 -142.47
REMARK 500 LYS A 166 -75.44 -24.20
REMARK 500 ALA A 249 42.43 -89.27
REMARK 500 ARG B 8 81.63 64.15
REMARK 500 THR B 10 51.50 -112.40
REMARK 500 VAL B 51 90.43 -36.83
REMARK 500 GLU B 57 96.27 -67.56
REMARK 500 GLU B 63 -11.18 -146.31
REMARK 500 MET B 183 137.42 -34.89
REMARK 500 ALA B 219 -148.79 -179.97
REMARK 500 ASN B 220 50.80 -91.72
REMARK 500 ASP B 221 129.86 69.39
REMARK 500 ARG C 4 131.98 -38.92
REMARK 500 ASN C 38 24.12 -144.70
REMARK 500 LEU C 52 6.39 94.11
REMARK 500 ASP C 66 -163.13 -125.69
REMARK 500 PRO C 183 106.39 -53.77
REMARK 500 GLN C 202 -104.58 97.76
REMARK 500 ALA C 205 -143.10 -5.01
REMARK 500 ASP C 218 76.33 -103.68
REMARK 500 ARG D 2 156.63 127.18
REMARK 500 ARG D 45 61.01 63.47
REMARK 500 LEU D 73 93.56 -69.18
REMARK 500 GLU D 201 -75.39 -61.03
REMARK 500 SER E 39 -149.34 -93.75
REMARK 500 ASP E 53 -159.65 -151.31
REMARK 500 GLN E 59 111.85 -17.69
REMARK 500 ASP E 137 -162.91 -125.40
REMARK 500 ASP E 202 -38.55 68.13
REMARK 500 LYS E 231 -30.24 -29.41
REMARK 500 SER F 9 4.83 88.15
REMARK 500 LYS F 53 4.25 -69.07
REMARK 500 GLN F 58 -19.22 81.37
REMARK 500 ASP F 67 -138.28 59.85
REMARK 500 LYS F 100 -43.04 71.52
REMARK 500 HIS F 179 54.43 -147.74
REMARK 500 ASN F 203 45.11 -95.10
REMARK 500 GLU F 205 -71.90 -46.83
REMARK 500 ILE F 243 39.55 -85.19
REMARK 500 LYS G 221 105.26 -37.82
REMARK 500 ASP G 222 -10.03 79.61
REMARK 500 GLU G 241 40.41 -100.70
REMARK 500 ASP H 145 62.78 64.40
REMARK 500 SER H 171 -113.37 62.63
REMARK 500 THR H 192 52.86 -145.31
REMARK 500 SER I 5 41.11 -144.28
REMARK 500 GLN I 31 -113.21 51.64
REMARK 500 ARG I 97 31.84 -98.96
REMARK 500 ASP I 134 -70.18 -95.30
REMARK 500
REMARK 500 THIS ENTRY HAS 166 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 76.8
REMARK 620 3 ARG G 122 O 79.2 74.5
REMARK 620 4 MET G 125 O 158.2 82.1 90.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG I 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP I 177 O
REMARK 620 2 SER I 180 O 81.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG Y 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP I 204 O
REMARK 620 2 ALA Y 165 O 104.8
REMARK 620 3 ASP Y 168 O 157.1 94.0
REMARK 620 4 SER Y 171 O 93.8 80.7 76.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG K 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA K 165 O
REMARK 620 2 ASP K 168 O 100.1
REMARK 620 3 SER K 171 O 79.9 78.9
REMARK 620 4 ASP W 204 O 99.1 154.1 87.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG V 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP L 222 OXT
REMARK 620 2 ILE V 163 O 103.4
REMARK 620 3 ASP V 166 O 141.0 107.7
REMARK 620 4 SER V 169 O 111.8 89.6 91.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG N 201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE N 163 O
REMARK 620 2 SER N 169 O 95.9
REMARK 620 N 1
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 83.8
REMARK 620 3 VAL Z 198 O 90.0 76.0
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 MG H 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG I 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG I 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG J 201
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 K 302
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 MG V 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Y 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Z 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN 1 OF BOC-ALA-ALA-ALA-CHO
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN 2 OF BOC-ALA-ALA-ALA-CHO
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN 3 OF BOC-ALA-ALA-ALA-CHO
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN 4 OF BOC-ALA-ALA-ALA-CHO
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 4QBY A 1 250 UNP P23639 PSA2_YEAST 1 250
DBREF 4QBY B 0 257 UNP P23638 PSA3_YEAST 1 258
DBREF 4QBY C -1 252 UNP P40303 PSA4_YEAST 1 254
DBREF 4QBY D -7 252 UNP P32379 PSA5_YEAST 1 260
DBREF 4QBY E 0 233 UNP P40302 PSA6_YEAST 1 234
DBREF 4QBY F -3 284 UNP P21242 PSA7_YEAST 1 288
DBREF 4QBY G -8 243 UNP P21243 PSA1_YEAST 1 252
DBREF 4QBY H 1 232 UNP P25043 PSB2_YEAST 30 261
DBREF 4QBY I 0 204 UNP P25451 PSB3_YEAST 1 205
DBREF 4QBY J 1 198 UNP P22141 PSB4_YEAST 1 198
DBREF 4QBY K 1 212 UNP P30656 PSB5_YEAST 76 287
DBREF 4QBY L 1 222 UNP P23724 PSB6_YEAST 20 241
DBREF 4QBY M -12 233 UNP P30657 PSB7_YEAST 21 266
DBREF 4QBY N 1 196 UNP P38624 PSB1_YEAST 20 215
DBREF 4QBY O 1 250 UNP P23639 PSA2_YEAST 1 250
DBREF 4QBY P 0 257 UNP P23638 PSA3_YEAST 1 258
DBREF 4QBY Q -1 252 UNP P40303 PSA4_YEAST 1 254
DBREF 4QBY R -7 252 UNP P32379 PSA5_YEAST 1 260
DBREF 4QBY S 0 233 UNP P40302 PSA6_YEAST 1 234
DBREF 4QBY T -3 284 UNP P21242 PSA7_YEAST 1 288
DBREF 4QBY U -8 243 UNP P21243 PSA1_YEAST 1 252
DBREF 4QBY V 1 232 UNP P25043 PSB2_YEAST 30 261
DBREF 4QBY W 0 204 UNP P25451 PSB3_YEAST 1 205
DBREF 4QBY X 1 198 UNP P22141 PSB4_YEAST 1 198
DBREF 4QBY Y 1 212 UNP P30656 PSB5_YEAST 76 287
DBREF 4QBY Z 1 222 UNP P23724 PSB6_YEAST 20 241
DBREF 4QBY a -12 233 UNP P30657 PSB7_YEAST 21 266
DBREF 4QBY b 1 196 UNP P38624 PSB1_YEAST 20 215
DBREF 4QBY 1 1 4 PDB 4QBY 4QBY 1 4
DBREF 4QBY 2 1 4 PDB 4QBY 4QBY 1 4
DBREF 4QBY 3 1 4 PDB 4QBY 4QBY 1 4
DBREF 4QBY 4 1 4 PDB 4QBY 4QBY 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 1 4 BOC ALA ALA 2A1
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 2 4 BOC ALA ALA 2A1
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 3 4 BOC ALA ALA 2A1
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 4 4 BOC ALA ALA 2A1
HET BOC 1 1 7
HET 2A1 1 4 5
HET BOC 2 1 7
HET 2A1 2 4 5
HET BOC 3 1 7
HET 2A1 3 4 5
HET BOC 4 1 7
HET 2A1 4 4 5
HET MG G 301 1
HET MG H 301 1
HET MG I 301 1
HET MG I 302 1
HET MG J 201 1
HET MG K 301 1
HET MG K 302 1
HET MG N 201 1
HET MG V 301 1
HET MG Y 301 1
HET MG Z 301 1
HETNAM BOC TERT-BUTYL HYDROGEN CARBONATE
HETNAM 2A1 (2S)-2-AMINOPROPAN-1-OL
HETNAM MG MAGNESIUM ION
FORMUL 26 BOC 4(C5 H10 O3)
FORMUL 26 2A1 4(C3 H9 N O)
FORMUL 33 MG 11(MG 2+)
FORMUL 44 HOH *180(H2 O)
HELIX 1 1 LEU A 18 GLY A 31 1 14
HELIX 2 2 MET A 78 SER A 96 1 19
HELIX 3 3 TYR A 97 GLY A 102 1 6
HELIX 4 4 PRO A 106 ALA A 121 1 16
HELIX 5 5 GLY A 167 TRP A 179 1 13
HELIX 6 6 GLU A 184 SER A 199 1 16
HELIX 7 7 ASN A 218 LEU A 222 5 5
HELIX 8 8 THR A 239 ALA A 249 1 11
HELIX 9 9 GLY B 1 ASP B 6 5 6
HELIX 10 10 LEU B 18 SER B 29 1 12
HELIX 11 11 LEU B 79 ASN B 102 1 24
HELIX 12 12 PRO B 106 HIS B 124 1 19
HELIX 13 13 ASN B 167 TYR B 179 1 13
HELIX 14 14 LYS B 184 THR B 200 1 17
HELIX 15 15 THR B 206 ASP B 208 5 3
HELIX 16 16 LYS B 230 THR B 241 1 12
HELIX 17 17 ILE C 15 GLY C 28 1 14
HELIX 18 18 LEU C 76 GLU C 99 1 24
HELIX 19 19 THR C 103 TYR C 118 1 16
HELIX 20 20 ASN C 165 TYR C 177 1 13
HELIX 21 21 THR C 185 LEU C 198 1 14
HELIX 22 22 SER C 223 GLN C 236 1 14
HELIX 23 23 LEU D 13 LEU D 25 1 13
HELIX 24 24 GLU D 52 ILE D 56 5 5
HELIX 25 25 THR D 74 ASP D 76 5 3
HELIX 26 26 ALA D 77 ASP D 96 1 20
HELIX 27 27 ASN D 100 LEU D 113 1 14
HELIX 28 28 GLY D 167 TRP D 179 1 13
HELIX 29 29 THR D 184 MET D 200 1 17
HELIX 30 30 ASP D 224 ALA D 241 1 18
HELIX 31 31 LEU E 18 GLY E 31 1 14
HELIX 32 32 LEU E 76 ASN E 99 1 24
HELIX 33 33 ALA E 103 ASN E 118 1 16
HELIX 34 34 ARG E 163 ILE E 179 1 17
HELIX 35 35 ASN E 184 GLN E 198 1 15
HELIX 36 36 GLY E 226 LYS E 231 1 6
HELIX 37 37 ASN F 17 ASN F 29 1 13
HELIX 38 38 LEU F 77 LYS F 100 1 24
HELIX 39 39 PRO F 104 HIS F 119 1 16
HELIX 40 40 GLY F 164 HIS F 179 1 16
HELIX 41 41 SER F 184 ALA F 199 1 16
HELIX 42 42 HIS F 200 ASP F 202 5 3
HELIX 43 43 LYS F 228 LYS F 241 1 14
HELIX 44 44 GLY G 2 HIS G 6 5 5
HELIX 45 45 LEU G 16 THR G 26 1 11
HELIX 46 46 ASP G 56 VAL G 60 5 5
HELIX 47 47 PRO G 77 GLY G 100 1 24
HELIX 48 48 PRO G 104 ARG G 122 1 19
HELIX 49 49 LYS G 165 LYS G 181 1 17
HELIX 50 50 SER G 189 GLY G 206 1 18
HELIX 51 51 SER G 228 ALA G 240 1 13
HELIX 52 52 THR H 48 THR H 70 1 23
HELIX 53 53 ARG H 75 TYR H 90 1 16
HELIX 54 54 GLY H 130 TRP H 142 1 13
HELIX 55 55 THR H 147 ASP H 166 1 20
HELIX 56 56 ASP I 2 ILE I 6 5 5
HELIX 57 57 LEU I 55 GLU I 78 1 24
HELIX 58 58 GLU I 82 GLU I 96 1 15
HELIX 59 59 ALA I 141 TYR I 153 1 13
HELIX 60 60 GLU I 158 ASP I 175 1 18
HELIX 61 61 GLY J 51 ASP J 72 1 22
HELIX 62 62 SER J 76 ILE J 92 1 17
HELIX 63 63 TYR J 135 TYR J 148 1 14
HELIX 64 64 THR J 153 MET J 172 1 20
HELIX 65 65 GLY K 48 LYS K 71 1 24
HELIX 66 66 SER K 75 TYR K 90 1 16
HELIX 67 67 GLY K 132 TYR K 144 1 13
HELIX 68 68 SER K 149 ASP K 168 1 20
HELIX 69 69 VAL K 193 GLY K 205 1 13
HELIX 70 70 PHE L 57 HIS L 79 1 23
HELIX 71 71 SER L 85 GLY L 99 1 15
HELIX 72 72 ALA L 142 VAL L 154 1 13
HELIX 73 73 SER L 176 HIS L 195 1 20
HELIX 74 74 ILE M 57 TYR M 76 1 20
HELIX 75 75 GLU M 88 LYS M 106 1 19
HELIX 76 76 GLY M 145 LYS M 157 1 13
HELIX 77 77 ARG M 161 ILE M 165 5 5
HELIX 78 78 THR M 169 ASP M 188 1 20
HELIX 79 79 TRP M 219 ILE M 225 5 7
HELIX 80 80 SER N 48 GLY N 71 1 24
HELIX 81 81 SER N 74 ASN N 89 1 16
HELIX 82 82 LYS N 90 LEU N 93 5 4
HELIX 83 83 GLY N 128 PHE N 133 5 6
HELIX 84 84 ILE N 134 PHE N 142 1 9
HELIX 85 85 SER N 147 ASP N 166 1 20
HELIX 86 86 TYR N 189 GLU N 194 1 6
HELIX 87 87 LEU O 18 GLY O 31 1 14
HELIX 88 88 MET O 78 SER O 96 1 19
HELIX 89 89 TYR O 97 GLY O 102 1 6
HELIX 90 90 PRO O 106 ALA O 121 1 16
HELIX 91 91 GLY O 167 TRP O 179 1 13
HELIX 92 92 GLU O 184 SER O 199 1 16
HELIX 93 93 ASN O 218 LEU O 222 5 5
HELIX 94 94 THR O 239 ALA O 249 1 11
HELIX 95 95 GLY P 1 ASP P 6 5 6
HELIX 96 96 LEU P 18 SER P 29 1 12
HELIX 97 97 LEU P 79 ASN P 102 1 24
HELIX 98 98 PRO P 106 HIS P 124 1 19
HELIX 99 99 ASN P 167 TYR P 179 1 13
HELIX 100 100 LYS P 184 THR P 200 1 17
HELIX 101 101 THR P 206 ASP P 208 5 3
HELIX 102 102 LYS P 230 THR P 241 1 12
HELIX 103 103 ILE Q 15 GLY Q 28 1 14
HELIX 104 104 LEU Q 76 GLU Q 99 1 24
HELIX 105 105 THR Q 103 TYR Q 118 1 16
HELIX 106 106 ASN Q 165 TYR Q 177 1 13
HELIX 107 107 THR Q 185 LEU Q 198 1 14
HELIX 108 108 SER Q 223 GLN Q 236 1 14
HELIX 109 109 LEU R 13 LEU R 25 1 13
HELIX 110 110 GLU R 52 ILE R 56 5 5
HELIX 111 111 THR R 74 ASP R 76 5 3
HELIX 112 112 ALA R 77 ASP R 96 1 20
HELIX 113 113 ASN R 100 LEU R 113 1 14
HELIX 114 114 GLY R 167 TRP R 179 1 13
HELIX 115 115 THR R 184 MET R 200 1 17
HELIX 116 116 ASP R 224 ALA R 241 1 18
HELIX 117 117 LEU S 18 GLY S 31 1 14
HELIX 118 118 LEU S 76 ASN S 99 1 24
HELIX 119 119 ALA S 103 ASN S 118 1 16
HELIX 120 120 ARG S 163 ILE S 179 1 17
HELIX 121 121 ASN S 184 GLN S 198 1 15
HELIX 122 122 GLY S 226 LYS S 231 1 6
HELIX 123 123 ASN T 17 ASN T 29 1 13
HELIX 124 124 LEU T 77 LYS T 100 1 24
HELIX 125 125 PRO T 104 HIS T 119 1 16
HELIX 126 126 GLY T 164 HIS T 179 1 16
HELIX 127 127 SER T 184 ALA T 199 1 16
HELIX 128 128 HIS T 200 ASP T 202 5 3
HELIX 129 129 LYS T 228 LYS T 241 1 14
HELIX 130 130 GLY U 2 HIS U 6 5 5
HELIX 131 131 LEU U 16 THR U 26 1 11
HELIX 132 132 ASP U 56 VAL U 60 5 5
HELIX 133 133 PRO U 77 GLY U 100 1 24
HELIX 134 134 PRO U 104 ARG U 122 1 19
HELIX 135 135 LYS U 165 LYS U 181 1 17
HELIX 136 136 SER U 189 GLY U 206 1 18
HELIX 137 137 SER U 228 ALA U 240 1 13
HELIX 138 138 THR V 48 THR V 70 1 23
HELIX 139 139 ARG V 75 TYR V 90 1 16
HELIX 140 140 GLY V 130 TRP V 142 1 13
HELIX 141 141 THR V 147 ASP V 166 1 20
HELIX 142 142 ASP W 2 ILE W 6 5 5
HELIX 143 143 LEU W 55 GLU W 78 1 24
HELIX 144 144 GLU W 82 GLU W 96 1 15
HELIX 145 145 ALA W 141 TYR W 153 1 13
HELIX 146 146 GLU W 158 ASP W 175 1 18
HELIX 147 147 GLY X 51 ASP X 72 1 22
HELIX 148 148 SER X 76 ILE X 92 1 17
HELIX 149 149 TYR X 135 TYR X 148 1 14
HELIX 150 150 THR X 153 MET X 172 1 20
HELIX 151 151 GLY Y 48 LYS Y 71 1 24
HELIX 152 152 SER Y 75 TYR Y 90 1 16
HELIX 153 153 GLY Y 132 TYR Y 144 1 13
HELIX 154 154 SER Y 149 ASP Y 168 1 20
HELIX 155 155 VAL Y 193 GLY Y 205 1 13
HELIX 156 156 PHE Z 57 HIS Z 79 1 23
HELIX 157 157 SER Z 85 GLY Z 99 1 15
HELIX 158 158 ALA Z 142 VAL Z 154 1 13
HELIX 159 159 SER Z 176 HIS Z 195 1 20
HELIX 160 160 ILE a 57 TYR a 76 1 20
HELIX 161 161 GLU a 88 LYS a 106 1 19
HELIX 162 162 GLY a 145 LYS a 157 1 13
HELIX 163 163 ARG a 161 ILE a 165 5 5
HELIX 164 164 THR a 169 ASP a 188 1 20
HELIX 165 165 TRP a 219 ILE a 225 5 7
HELIX 166 166 SER b 48 GLY b 71 1 24
HELIX 167 167 SER b 74 ASN b 89 1 16
HELIX 168 168 LYS b 90 LEU b 93 5 4
HELIX 169 169 GLY b 128 PHE b 133 5 6
HELIX 170 170 ILE b 134 PHE b 142 1 9
HELIX 171 171 SER b 147 ASP b 166 1 20
HELIX 172 172 TYR b 189 GLU b 194 1 6
SHEET 1 A 5 ALA A 161 ILE A 164 0
SHEET 2 A 5 SER A 34 LYS A 38 -1 N SER A 34 O ILE A 164
SHEET 3 A 5 VAL A 43 GLU A 48 -1 O VAL A 44 N ILE A 37
SHEET 4 A 5 ILE A 209 ILE A 214 -1 O ILE A 214 N VAL A 43
SHEET 5 A 5 PHE A 235 LYS A 237 -1 O ARG A 236 N ILE A 213
SHEET 1 B 5 SER A 65 THR A 68 0
SHEET 2 B 5 ILE A 71 GLY A 77 -1 O ILE A 71 N LEU A 67
SHEET 3 B 5 VAL A 132 ASP A 140 -1 O LEU A 135 N VAL A 74
SHEET 4 B 5 GLY A 144 VAL A 150 -1 O TYR A 148 N ILE A 136
SHEET 5 B 5 TYR A 156 PRO A 158 -1 O PHE A 157 N GLN A 149
SHEET 1 C 6 TYR A 224 THR A 225 0
SHEET 2 C 6 ALA H 184 LEU H 191 1 O TYR H 186 N THR A 225
SHEET 3 C 6 VAL H 173 GLU H 179 -1 N VAL H 177 O GLU H 185
SHEET 4 C 6 GLY H 11 ALA H 16 -1 N VAL H 12 O MET H 178
SHEET 5 C 6 ILE H 3 PHE H 8 -1 N VAL H 6 O VAL H 13
SHEET 6 C 6 TYR H 124 LEU H 127 -1 O LEU H 125 N GLY H 5
SHEET 1 D 5 ALA B 161 VAL B 164 0
SHEET 2 D 5 ALA B 34 ALA B 39 -1 N GLY B 36 O ILE B 162
SHEET 3 D 5 GLY B 42 GLU B 48 -1 O ALA B 46 N ILE B 35
SHEET 4 D 5 LEU B 210 ARG B 216 -1 O ALA B 213 N LEU B 45
SHEET 5 D 5 TYR B 225 ILE B 228 -1 O LYS B 227 N THR B 214
SHEET 1 E 5 LEU B 65 LYS B 67 0
SHEET 2 E 5 ILE B 72 GLY B 78 -1 O VAL B 74 N TYR B 66
SHEET 3 E 5 VAL B 132 ASP B 140 -1 O ALA B 137 N ALA B 73
SHEET 4 E 5 GLY B 144 SER B 150 -1 O TYR B 148 N TYR B 136
SHEET 5 E 5 TYR B 156 GLY B 158 -1 O THR B 157 N THR B 149
SHEET 1 F 5 ALA C 159 ILE C 162 0
SHEET 2 F 5 ALA C 31 LYS C 35 -1 N ALA C 31 O ILE C 162
SHEET 3 F 5 VAL C 40 GLU C 45 -1 O GLY C 43 N VAL C 32
SHEET 4 F 5 ILE C 208 LYS C 214 -1 O THR C 211 N LEU C 42
SHEET 5 F 5 ASP C 218 ALA C 221 -1 O VAL C 220 N VAL C 212
SHEET 1 G 5 SER C 63 LYS C 64 0
SHEET 2 G 5 VAL C 69 GLY C 75 -1 O LEU C 71 N SER C 63
SHEET 3 G 5 VAL C 129 PHE C 136 -1 O ALA C 134 N VAL C 70
SHEET 4 G 5 PRO C 143 THR C 148 -1 O TYR C 146 N ILE C 133
SHEET 5 G 5 TYR C 154 SER C 156 -1 O SER C 155 N GLN C 147
SHEET 1 H 5 ALA D 161 ILE D 164 0
SHEET 2 H 5 ALA D 29 THR D 34 -1 N ALA D 29 O ILE D 164
SHEET 3 H 5 GLY D 37 GLU D 43 -1 O GLY D 41 N ILE D 30
SHEET 4 H 5 ALA D 209 THR D 215 -1 O SER D 212 N LEU D 40
SHEET 5 H 5 GLY D 219 ILE D 222 -1 O GLY D 219 N THR D 215
SHEET 1 I 5 ILE D 59 ASP D 63 0
SHEET 2 I 5 ILE D 66 GLY D 72 -1 O CYS D 68 N VAL D 60
SHEET 3 I 5 VAL D 132 ASP D 140 -1 O ALA D 137 N GLY D 67
SHEET 4 I 5 GLY D 144 ALA D 150 -1 O PHE D 148 N ILE D 136
SHEET 5 I 5 PHE D 156 ARG D 158 -1 O TYR D 157 N HIS D 149
SHEET 1 J 5 GLY E 157 ILE E 160 0
SHEET 2 J 5 THR E 34 ARG E 38 -1 N GLY E 36 O THR E 158
SHEET 3 J 5 HIS E 42 LEU E 48 -1 O VAL E 46 N VAL E 35
SHEET 4 J 5 LEU E 210 GLY E 216 -1 O ALA E 213 N LEU E 45
SHEET 5 J 5 THR E 219 ASP E 225 -1 O TYR E 224 N ILE E 212
SHEET 1 K 5 ILE E 62 ASP E 66 0
SHEET 2 K 5 MET E 69 GLY E 75 -1 O LEU E 71 N ILE E 63
SHEET 3 K 5 VAL E 129 ASP E 137 -1 O ILE E 134 N GLY E 70
SHEET 4 K 5 GLY E 140 PHE E 146 -1 O PHE E 146 N LEU E 131
SHEET 5 K 5 VAL E 152 LEU E 155 -1 O THR E 153 N GLU E 145
SHEET 1 L 5 GLY F 158 THR F 161 0
SHEET 2 L 5 SER F 33 LYS F 37 -1 N GLY F 35 O ALA F 159
SHEET 3 L 5 GLY F 41 LEU F 49 -1 O ALA F 45 N ILE F 34
SHEET 4 L 5 PHE F 208 SER F 216 -1 O SER F 213 N PHE F 44
SHEET 5 L 5 LYS F 225 PHE F 226 -1 O LYS F 225 N TRP F 214
SHEET 1 M 5 GLN F 64 VAL F 66 0
SHEET 2 M 5 ILE F 70 GLY F 76 -1 O CYS F 72 N GLN F 64
SHEET 3 M 5 VAL F 130 ASP F 138 -1 O ILE F 133 N VAL F 73
SHEET 4 M 5 GLY F 141 LEU F 147 -1 O TYR F 145 N PHE F 134
SHEET 5 M 5 TYR F 153 GLY F 155 -1 O TRP F 154 N MET F 146
SHEET 1 N 5 ALA G 159 THR G 162 0
SHEET 2 N 5 SER G 33 ARG G 37 -1 N ALA G 35 O THR G 160
SHEET 3 N 5 CYS G 41 GLN G 47 -1 O ILE G 45 N LEU G 34
SHEET 4 N 5 LEU G 214 THR G 220 -1 O ALA G 219 N THR G 42
SHEET 5 N 5 LYS G 223 THR G 226 -1 O PHE G 225 N VAL G 218
SHEET 1 O 5 ILE G 63 CYS G 65 0
SHEET 2 O 5 GLY G 71 ASN G 75 -1 O MET G 72 N PHE G 64
SHEET 3 O 5 ILE G 131 ASP G 138 -1 O VAL G 135 N GLY G 71
SHEET 4 O 5 GLY G 142 THR G 148 -1 O TYR G 146 N PHE G 134
SHEET 5 O 5 TYR G 154 GLY G 156 -1 O VAL G 155 N LYS G 147
SHEET 1 P 2 SER H 20 GLN H 22 0
SHEET 2 P 2 ILE H 25 ASP H 28 -1 O ILE H 25 N GLN H 22
SHEET 1 Q 5 LEU H 34 SER H 38 0
SHEET 2 Q 5 ILE H 41 GLY H 47 -1 O CYS H 43 N HIS H 35
SHEET 3 Q 5 ALA H 96 ASP H 104 -1 O TYR H 97 N ALA H 46
SHEET 4 Q 5 GLY H 107 ILE H 113 -1 O ILE H 113 N LEU H 98
SHEET 5 Q 5 THR H 119 VAL H 121 -1 O ASP H 120 N SER H 112
SHEET 1 R 6 VAL H 212 ILE H 217 0
SHEET 2 R 6 VAL I 194 LEU I 199 -1 O TYR I 198 N LEU H 213
SHEET 3 R 6 ALA I 184 LYS I 190 -1 N ILE I 188 O VAL I 195
SHEET 4 R 6 CYS I 19 ASP I 25 -1 N VAL I 20 O ILE I 189
SHEET 5 R 6 ILE I 10 THR I 15 -1 N VAL I 12 O ALA I 23
SHEET 6 R 6 PHE I 135 GLY I 139 -1 O ILE I 136 N ALA I 13
SHEET 1 S 2 LEU I 28 SER I 30 0
SHEET 2 S 2 LEU I 33 SER I 36 -1 O SER I 36 N LEU I 28
SHEET 1 T 5 ILE I 42 TYR I 45 0
SHEET 2 T 5 VAL I 48 GLY I 54 -1 O LEU I 50 N PHE I 43
SHEET 3 T 5 VAL I 104 ILE I 111 -1 O ALA I 109 N PHE I 49
SHEET 4 T 5 PRO I 118 PHE I 123 -1 O ALA I 121 N VAL I 108
SHEET 5 T 5 ILE I 129 GLU I 131 -1 O ASP I 130 N GLY I 122
SHEET 1 U 5 TYR J 130 HIS J 133 0
SHEET 2 U 5 ILE J 4 ARG J 8 -1 N GLY J 6 O GLY J 131
SHEET 3 U 5 VAL J 13 SER J 18 -1 O ALA J 16 N LEU J 5
SHEET 4 U 5 VAL J 179 ASP J 185 -1 O VAL J 184 N VAL J 13
SHEET 5 U 5 GLY J 188 VAL J 192 -1 O GLY J 188 N ASP J 185
SHEET 1 V 2 VAL J 21 ARG J 23 0
SHEET 2 V 2 SER J 26 LYS J 29 -1 O SER J 26 N ARG J 23
SHEET 1 W 5 THR J 35 SER J 39 0
SHEET 2 W 5 THR J 42 GLY J 48 -1 O MET J 44 N ARG J 36
SHEET 3 W 5 VAL J 100 ASP J 108 -1 O ASN J 101 N ALA J 47
SHEET 4 W 5 LYS J 113 ASP J 120 -1 O ILE J 119 N VAL J 102
SHEET 5 W 5 THR J 124 GLU J 127 -1 O VAL J 126 N GLN J 118
SHEET 1 X 5 ILE K 126 VAL K 129 0
SHEET 2 X 5 THR K 3 PHE K 8 -1 N THR K 3 O VAL K 129
SHEET 3 X 5 GLY K 11 VAL K 16 -1 O ALA K 15 N LEU K 4
SHEET 4 X 5 SER K 174 THR K 181 -1 O VAL K 180 N ILE K 12
SHEET 5 X 5 GLY K 184 ASP K 192 -1 O ILE K 186 N HIS K 179
SHEET 1 Y 2 ALA K 20 ALA K 22 0
SHEET 2 Y 2 TRP K 25 SER K 28 -1 O SER K 28 N ALA K 20
SHEET 1 Z 5 VAL K 34 ASN K 38 0
SHEET 2 Z 5 LEU K 41 THR K 44 -1 O GLY K 43 N ILE K 35
SHEET 3 Z 5 GLY K 98 THR K 105 -1 O CYS K 102 N LEU K 42
SHEET 4 Z 5 GLY K 109 ASP K 116 -1 O TYR K 113 N ILE K 101
SHEET 5 Z 5 ARG K 121 GLY K 124 -1 O LEU K 122 N TYR K 114
SHEET 1 AA 5 CYS L 136 GLY L 140 0
SHEET 2 AA 5 THR L 11 ALA L 16 -1 N ILE L 12 O GLY L 139
SHEET 3 AA 5 ALA L 21 ASP L 26 -1 O ALA L 24 N LEU L 13
SHEET 4 AA 5 GLY L 201 THR L 208 -1 O VAL L 207 N ALA L 21
SHEET 5 AA 5 GLY L 211 GLU L 218 -1 O TYR L 217 N LEU L 202
SHEET 1 AB 2 ASN L 29 THR L 31 0
SHEET 2 AB 2 SER L 34 SER L 37 -1 O ASN L 36 N ASN L 29
SHEET 1 AC 5 PHE L 44 ASP L 45 0
SHEET 2 AC 5 VAL L 51 GLY L 56 -1 O MET L 52 N PHE L 44
SHEET 3 AC 5 VAL L 107 LEU L 114 -1 O HIS L 108 N ASN L 55
SHEET 4 AC 5 GLY L 120 PHE L 125 -1 O PHE L 125 N THR L 109
SHEET 5 AC 5 TYR L 131 GLU L 134 -1 O GLU L 134 N VAL L 122
SHEET 1 AD 5 LEU M 33 PHE M 36 0
SHEET 2 AD 5 GLY M 28 TYR M 30 -1 N TYR M 30 O LEU M 33
SHEET 3 AD 5 VAL M 6 GLY M 8 -1 N THR M 7 O SER M 29
SHEET 4 AD 5 THR M 49 ASP M 56 -1 O GLY M 55 N GLY M 8
SHEET 5 AD 5 LEU M 42 VAL M 45 -1 N ILE M 43 O VAL M 51
SHEET 1 AE 7 LEU M 33 PHE M 36 0
SHEET 2 AE 7 GLY M 28 TYR M 30 -1 N TYR M 30 O LEU M 33
SHEET 3 AE 7 VAL M 6 GLY M 8 -1 N THR M 7 O SER M 29
SHEET 4 AE 7 THR M 49 ASP M 56 -1 O GLY M 55 N GLY M 8
SHEET 5 AE 7 ASN M 112 VAL M 119 -1 O ALA M 117 N VAL M 50
SHEET 6 AE 7 GLN M 125 ASN M 131 -1 O VAL M 130 N ILE M 114
SHEET 7 AE 7 THR M 136 TYR M 137 -1 O TYR M 137 N TYR M 129
SHEET 1 AF 5 THR M 141 ALA M 143 0
SHEET 2 AF 5 ILE M 12 LYS M 15 -1 N SER M 13 O LEU M 142
SHEET 3 AF 5 GLY M 19 ASP M 25 -1 O ALA M 23 N ILE M 12
SHEET 4 AF 5 ASN M 194 ASP M 201 -1 O ALA M 198 N ILE M 22
SHEET 5 AF 5 GLY M 205 GLN M 213 -1 O LYS M 209 N LEU M 197
SHEET 1 AG 5 TYR N 124 ALA N 127 0
SHEET 2 AG 5 ILE N 3 THR N 7 -1 N ILE N 3 O ALA N 127
SHEET 3 AG 5 GLY N 11 ALA N 16 -1 O ILE N 13 N VAL N 6
SHEET 4 AG 5 ILE N 173 THR N 179 -1 O LEU N 178 N VAL N 12
SHEET 5 AG 5 GLY N 182 PHE N 188 -1 O GLU N 184 N VAL N 177
SHEET 1 AH 2 THR N 20 THR N 22 0
SHEET 2 AH 2 TYR N 25 ASN N 28 -1 O TYR N 25 N THR N 22
SHEET 1 AI 5 LEU N 34 HIS N 38 0
SHEET 2 AI 5 ILE N 41 GLY N 47 -1 O CYS N 43 N THR N 35
SHEET 3 AI 5 ALA N 95 TYR N 102 -1 O GLY N 96 N SER N 46
SHEET 4 AI 5 GLY N 108 ILE N 113 -1 O TYR N 111 N VAL N 99
SHEET 5 AI 5 HIS N 120 LEU N 122 -1 O HIS N 120 N THR N 112
SHEET 1 AJ 5 ALA O 161 ILE O 164 0
SHEET 2 AJ 5 SER O 34 LYS O 38 -1 N SER O 34 O ILE O 164
SHEET 3 AJ 5 VAL O 43 GLU O 48 -1 O VAL O 44 N ILE O 37
SHEET 4 AJ 5 ILE O 209 ILE O 214 -1 O ILE O 214 N VAL O 43
SHEET 5 AJ 5 PHE O 235 LYS O 237 -1 O ARG O 236 N ILE O 213
SHEET 1 AK 5 SER O 65 THR O 68 0
SHEET 2 AK 5 ILE O 71 GLY O 77 -1 O ILE O 71 N LEU O 67
SHEET 3 AK 5 VAL O 132 ASP O 140 -1 O LEU O 135 N VAL O 74
SHEET 4 AK 5 GLY O 144 VAL O 150 -1 O TYR O 148 N ILE O 136
SHEET 5 AK 5 TYR O 156 PRO O 158 -1 O PHE O 157 N GLN O 149
SHEET 1 AL 6 TYR O 224 THR O 225 0
SHEET 2 AL 6 ALA V 184 LEU V 191 1 O TYR V 186 N THR O 225
SHEET 3 AL 6 VAL V 173 GLU V 179 -1 N VAL V 177 O GLU V 185
SHEET 4 AL 6 GLY V 11 ALA V 16 -1 N VAL V 12 O MET V 178
SHEET 5 AL 6 ILE V 3 PHE V 8 -1 N VAL V 6 O VAL V 13
SHEET 6 AL 6 TYR V 124 LEU V 127 -1 O LEU V 125 N GLY V 5
SHEET 1 AM 5 ALA P 161 VAL P 164 0
SHEET 2 AM 5 ALA P 34 ALA P 39 -1 N GLY P 36 O ILE P 162
SHEET 3 AM 5 GLY P 42 GLU P 48 -1 O ALA P 46 N ILE P 35
SHEET 4 AM 5 LEU P 210 ARG P 216 -1 O ALA P 213 N LEU P 45
SHEET 5 AM 5 TYR P 225 ILE P 228 -1 O LYS P 227 N THR P 214
SHEET 1 AN 5 LEU P 65 LYS P 67 0
SHEET 2 AN 5 ILE P 72 GLY P 78 -1 O VAL P 74 N TYR P 66
SHEET 3 AN 5 VAL P 132 ASP P 140 -1 O ALA P 137 N ALA P 73
SHEET 4 AN 5 GLY P 144 SER P 150 -1 O TYR P 148 N TYR P 136
SHEET 5 AN 5 TYR P 156 GLY P 158 -1 O THR P 157 N THR P 149
SHEET 1 AO 5 ALA Q 159 ILE Q 162 0
SHEET 2 AO 5 ALA Q 31 LYS Q 35 -1 N ALA Q 31 O ILE Q 162
SHEET 3 AO 5 VAL Q 40 GLU Q 45 -1 O GLY Q 43 N VAL Q 32
SHEET 4 AO 5 ILE Q 208 LYS Q 214 -1 O THR Q 211 N LEU Q 42
SHEET 5 AO 5 ASP Q 218 ALA Q 221 -1 O VAL Q 220 N VAL Q 212
SHEET 1 AP 5 SER Q 63 LYS Q 64 0
SHEET 2 AP 5 VAL Q 69 GLY Q 75 -1 O LEU Q 71 N SER Q 63
SHEET 3 AP 5 VAL Q 129 PHE Q 136 -1 O ALA Q 134 N VAL Q 70
SHEET 4 AP 5 PRO Q 143 THR Q 148 -1 O TYR Q 146 N ILE Q 133
SHEET 5 AP 5 TYR Q 154 SER Q 156 -1 O SER Q 155 N GLN Q 147
SHEET 1 AQ 5 ALA R 161 ILE R 164 0
SHEET 2 AQ 5 ALA R 29 THR R 34 -1 N ALA R 29 O ILE R 164
SHEET 3 AQ 5 GLY R 37 GLU R 43 -1 O GLY R 41 N ILE R 30
SHEET 4 AQ 5 ALA R 209 THR R 215 -1 O SER R 212 N LEU R 40
SHEET 5 AQ 5 GLY R 219 ILE R 222 -1 O GLY R 219 N THR R 215
SHEET 1 AR 5 ILE R 59 ASP R 63 0
SHEET 2 AR 5 ILE R 66 GLY R 72 -1 O CYS R 68 N VAL R 60
SHEET 3 AR 5 VAL R 132 ASP R 140 -1 O ALA R 137 N GLY R 67
SHEET 4 AR 5 GLY R 144 ALA R 150 -1 O PHE R 148 N ILE R 136
SHEET 5 AR 5 PHE R 156 ARG R 158 -1 O TYR R 157 N HIS R 149
SHEET 1 AS 5 GLY S 157 ILE S 160 0
SHEET 2 AS 5 THR S 34 ARG S 38 -1 N GLY S 36 O THR S 158
SHEET 3 AS 5 HIS S 42 LEU S 48 -1 O VAL S 46 N VAL S 35
SHEET 4 AS 5 LEU S 210 GLY S 216 -1 O ALA S 213 N LEU S 45
SHEET 5 AS 5 THR S 219 ASP S 225 -1 O TYR S 224 N ILE S 212
SHEET 1 AT 5 ILE S 62 ASP S 66 0
SHEET 2 AT 5 MET S 69 GLY S 75 -1 O LEU S 71 N ILE S 63
SHEET 3 AT 5 VAL S 129 ASP S 137 -1 O ILE S 134 N GLY S 70
SHEET 4 AT 5 GLY S 140 PHE S 146 -1 O PHE S 146 N LEU S 131
SHEET 5 AT 5 VAL S 152 LEU S 155 -1 O THR S 153 N GLU S 145
SHEET 1 AU 5 GLY T 158 THR T 161 0
SHEET 2 AU 5 SER T 33 CYS T 38 -1 N GLY T 35 O ALA T 159
SHEET 3 AU 5 GLY T 41 LEU T 49 -1 O ALA T 45 N ILE T 34
SHEET 4 AU 5 PHE T 208 SER T 216 -1 O SER T 213 N PHE T 44
SHEET 5 AU 5 LYS T 225 PHE T 226 -1 O LYS T 225 N TRP T 214
SHEET 1 AV 5 GLN T 64 VAL T 66 0
SHEET 2 AV 5 ILE T 70 GLY T 76 -1 O CYS T 72 N GLN T 64
SHEET 3 AV 5 VAL T 130 ASP T 138 -1 O ILE T 133 N VAL T 73
SHEET 4 AV 5 GLY T 141 LEU T 147 -1 O TYR T 145 N PHE T 134
SHEET 5 AV 5 TYR T 153 GLY T 155 -1 O TRP T 154 N MET T 146
SHEET 1 AW 5 ALA U 159 THR U 162 0
SHEET 2 AW 5 SER U 33 ARG U 37 -1 N ALA U 35 O THR U 160
SHEET 3 AW 5 CYS U 41 GLN U 47 -1 O ILE U 45 N LEU U 34
SHEET 4 AW 5 LEU U 214 THR U 220 -1 O ALA U 219 N THR U 42
SHEET 5 AW 5 LYS U 223 THR U 226 -1 O PHE U 225 N VAL U 218
SHEET 1 AX 5 ILE U 63 CYS U 65 0
SHEET 2 AX 5 GLY U 71 ASN U 75 -1 O MET U 72 N PHE U 64
SHEET 3 AX 5 ILE U 131 ASP U 138 -1 O VAL U 135 N GLY U 71
SHEET 4 AX 5 GLY U 142 THR U 148 -1 O TYR U 146 N PHE U 134
SHEET 5 AX 5 TYR U 154 GLY U 156 -1 O VAL U 155 N LYS U 147
SHEET 1 AY 2 SER V 20 GLN V 22 0
SHEET 2 AY 2 ILE V 25 ASP V 28 -1 O ILE V 25 N GLN V 22
SHEET 1 AZ 5 LEU V 34 SER V 38 0
SHEET 2 AZ 5 ILE V 41 GLY V 47 -1 O CYS V 43 N HIS V 35
SHEET 3 AZ 5 ALA V 96 ASP V 104 -1 O TYR V 97 N ALA V 46
SHEET 4 AZ 5 GLY V 107 ILE V 113 -1 O ILE V 113 N LEU V 98
SHEET 5 AZ 5 THR V 119 VAL V 121 -1 O ASP V 120 N SER V 112
SHEET 1 BA 6 VAL V 212 ILE V 217 0
SHEET 2 BA 6 VAL W 194 LEU W 199 -1 O TYR W 198 N LEU V 213
SHEET 3 BA 6 ALA W 184 LYS W 190 -1 N ILE W 188 O VAL W 195
SHEET 4 BA 6 CYS W 19 ASP W 25 -1 N VAL W 20 O ILE W 189
SHEET 5 BA 6 ILE W 10 THR W 15 -1 N VAL W 12 O ALA W 23
SHEET 6 BA 6 PHE W 135 GLY W 139 -1 O ILE W 136 N ALA W 13
SHEET 1 BB 2 LEU W 28 SER W 30 0
SHEET 2 BB 2 LEU W 33 SER W 36 -1 O VAL W 35 N LEU W 28
SHEET 1 BC 5 ILE W 42 TYR W 45 0
SHEET 2 BC 5 VAL W 48 GLY W 54 -1 O LEU W 50 N PHE W 43
SHEET 3 BC 5 VAL W 104 ILE W 111 -1 O ALA W 109 N PHE W 49
SHEET 4 BC 5 PRO W 118 PHE W 123 -1 O ALA W 121 N VAL W 108
SHEET 5 BC 5 ILE W 129 GLU W 131 -1 O ASP W 130 N GLY W 122
SHEET 1 BD 5 TYR X 130 HIS X 133 0
SHEET 2 BD 5 ILE X 4 ARG X 8 -1 N GLY X 6 O GLY X 131
SHEET 3 BD 5 VAL X 13 SER X 18 -1 O ALA X 16 N LEU X 5
SHEET 4 BD 5 VAL X 179 ASP X 185 -1 O VAL X 184 N VAL X 13
SHEET 5 BD 5 GLY X 188 VAL X 192 -1 O GLY X 188 N ASP X 185
SHEET 1 BE 2 VAL X 21 ARG X 23 0
SHEET 2 BE 2 SER X 26 LYS X 29 -1 O SER X 26 N ARG X 23
SHEET 1 BF 5 THR X 35 SER X 39 0
SHEET 2 BF 5 THR X 42 GLY X 48 -1 O MET X 44 N ARG X 36
SHEET 3 BF 5 VAL X 100 ASP X 108 -1 O ASN X 101 N ALA X 47
SHEET 4 BF 5 LYS X 113 ASP X 120 -1 O ILE X 119 N VAL X 102
SHEET 5 BF 5 THR X 124 GLU X 127 -1 O VAL X 126 N GLN X 118
SHEET 1 BG 5 ILE Y 126 VAL Y 129 0
SHEET 2 BG 5 THR Y 3 PHE Y 8 -1 N THR Y 3 O VAL Y 129
SHEET 3 BG 5 GLY Y 11 VAL Y 16 -1 O ALA Y 15 N LEU Y 4
SHEET 4 BG 5 SER Y 174 THR Y 181 -1 O VAL Y 180 N ILE Y 12
SHEET 5 BG 5 GLY Y 184 ASP Y 192 -1 O ILE Y 186 N HIS Y 179
SHEET 1 BH 2 ALA Y 20 ALA Y 22 0
SHEET 2 BH 2 TRP Y 25 SER Y 28 -1 O SER Y 28 N ALA Y 20
SHEET 1 BI 5 VAL Y 34 ASN Y 38 0
SHEET 2 BI 5 LEU Y 41 THR Y 44 -1 O GLY Y 43 N ILE Y 35
SHEET 3 BI 5 GLY Y 98 THR Y 105 -1 O CYS Y 102 N LEU Y 42
SHEET 4 BI 5 GLY Y 109 ASP Y 116 -1 O TYR Y 113 N ILE Y 101
SHEET 5 BI 5 ARG Y 121 GLY Y 124 -1 O LEU Y 122 N TYR Y 114
SHEET 1 BJ 5 CYS Z 136 GLY Z 140 0
SHEET 2 BJ 5 THR Z 11 ALA Z 16 -1 N ILE Z 12 O GLY Z 139
SHEET 3 BJ 5 ALA Z 21 ASP Z 26 -1 O ALA Z 24 N LEU Z 13
SHEET 4 BJ 5 GLY Z 201 THR Z 208 -1 O VAL Z 207 N ALA Z 21
SHEET 5 BJ 5 GLY Z 211 GLU Z 218 -1 O TYR Z 217 N LEU Z 202
SHEET 1 BK 2 ASN Z 29 THR Z 31 0
SHEET 2 BK 2 SER Z 34 SER Z 37 -1 O ASN Z 36 N ASN Z 29
SHEET 1 BL 5 PHE Z 44 ASP Z 45 0
SHEET 2 BL 5 VAL Z 51 GLY Z 56 -1 O MET Z 52 N PHE Z 44
SHEET 3 BL 5 VAL Z 107 LEU Z 114 -1 O HIS Z 108 N ASN Z 55
SHEET 4 BL 5 GLY Z 120 PHE Z 125 -1 O PHE Z 125 N THR Z 109
SHEET 5 BL 5 TYR Z 131 GLU Z 134 -1 O GLU Z 134 N VAL Z 122
SHEET 1 BM 5 LEU a 33 PHE a 36 0
SHEET 2 BM 5 GLY a 28 TYR a 30 -1 N TYR a 30 O LEU a 33
SHEET 3 BM 5 VAL a 6 GLY a 8 -1 N THR a 7 O SER a 29
SHEET 4 BM 5 THR a 49 ASP a 56 -1 O GLY a 55 N GLY a 8
SHEET 5 BM 5 LEU a 42 VAL a 45 -1 N ILE a 43 O VAL a 51
SHEET 1 BN 7 LEU a 33 PHE a 36 0
SHEET 2 BN 7 GLY a 28 TYR a 30 -1 N TYR a 30 O LEU a 33
SHEET 3 BN 7 VAL a 6 GLY a 8 -1 N THR a 7 O SER a 29
SHEET 4 BN 7 THR a 49 ASP a 56 -1 O GLY a 55 N GLY a 8
SHEET 5 BN 7 ASN a 112 VAL a 119 -1 O ALA a 117 N VAL a 50
SHEET 6 BN 7 GLN a 125 ASN a 131 -1 O VAL a 130 N ILE a 114
SHEET 7 BN 7 THR a 136 TYR a 137 -1 O TYR a 137 N TYR a 129
SHEET 1 BO 5 THR a 141 ALA a 143 0
SHEET 2 BO 5 ILE a 12 LYS a 15 -1 N SER a 13 O LEU a 142
SHEET 3 BO 5 GLY a 19 ASP a 25 -1 O ALA a 23 N ILE a 12
SHEET 4 BO 5 ASN a 194 ASP a 201 -1 O ALA a 198 N ILE a 22
SHEET 5 BO 5 GLY a 205 GLN a 213 -1 O LYS a 209 N LEU a 197
SHEET 1 BP 5 TYR b 124 ALA b 127 0
SHEET 2 BP 5 ILE b 3 THR b 7 -1 N ILE b 3 O ALA b 127
SHEET 3 BP 5 GLY b 11 ALA b 16 -1 O ILE b 13 N VAL b 6
SHEET 4 BP 5 ILE b 173 THR b 179 -1 O LEU b 178 N VAL b 12
SHEET 5 BP 5 GLY b 182 PHE b 188 -1 O LEU b 186 N MET b 175
SHEET 1 BQ 2 THR b 20 THR b 22 0
SHEET 2 BQ 2 TYR b 25 ASN b 28 -1 O TYR b 25 N THR b 22
SHEET 1 BR 5 LEU b 34 HIS b 38 0
SHEET 2 BR 5 ILE b 41 GLY b 47 -1 O CYS b 43 N THR b 35
SHEET 3 BR 5 ALA b 95 TYR b 102 -1 O GLY b 96 N SER b 46
SHEET 4 BR 5 GLY b 108 ILE b 113 -1 O TYR b 111 N VAL b 99
SHEET 5 BR 5 HIS b 120 LEU b 122 -1 O HIS b 120 N THR b 112
LINK OG1 THR H 1 C 2A1 1 4 1555 1555 1.45
LINK OG1 THR K 1 C 2A1 2 4 1555 1555 1.43
LINK OG1 THR V 1 C 2A1 3 4 1555 1555 1.45
LINK OG1 THR Y 1 C 2A1 4 4 1555 1555 1.43
LINK C BOC 1 1 N ALA 1 2 1555 1555 1.35
LINK C ALA 1 3 N 2A1 1 4 1555 1555 1.35
LINK C BOC 2 1 N ALA 2 2 1555 1555 1.35
LINK C ALA 2 3 N 2A1 2 4 1555 1555 1.34
LINK C BOC 3 1 N ALA 3 2 1555 1555 1.35
LINK C ALA 3 3 N 2A1 3 4 1555 1555 1.35
LINK C BOC 4 1 N ALA 4 2 1555 1555 1.35
LINK C ALA 4 3 N 2A1 4 4 1555 1555 1.34
LINK OG1 THR G 8 MG MG G 301 1555 1555 2.80
LINK O TYR G 119 MG MG G 301 1555 1555 2.66
LINK O ARG G 122 MG MG G 301 1555 1555 2.70
LINK O MET G 125 MG MG G 301 1555 1555 2.23
LINK OE1 GLN H 91 MG MG H 301 1555 1555 2.76
LINK O ASP I 177 MG MG I 301 1555 1555 2.34
LINK O SER I 180 MG MG I 301 1555 1555 2.90
LINK O ASP I 204 MG MG Y 301 1555 1555 2.46
LINK O ILE K 82 MG MG K 302 1555 1555 2.86
LINK O ALA K 165 MG MG K 301 1555 1555 2.41
LINK O ASP K 168 MG MG K 301 1555 1555 2.28
LINK O SER K 171 MG MG K 301 1555 1555 2.86
LINK MG MG K 301 O ASP W 204 1555 1555 2.60
LINK OXT ASP L 222 MG MG V 301 1555 1555 1.95
LINK O ILE N 163 MG MG N 201 1555 1555 2.70
LINK O SER N 169 MG MG N 201 1555 1555 2.70
LINK O ILE V 163 MG MG V 301 1555 1555 2.22
LINK O ASP V 166 MG MG V 301 1555 1555 1.99
LINK O SER V 169 MG MG V 301 1555 1555 2.13
LINK O ALA Y 165 MG MG Y 301 1555 1555 2.42
LINK O ASP Y 168 MG MG Y 301 1555 1555 2.49
LINK O SER Y 171 MG MG Y 301 1555 1555 2.82
LINK O THR Z 192 MG MG Z 301 1555 1555 2.68
LINK O HIS Z 195 MG MG Z 301 1555 1555 2.52
LINK O VAL Z 198 MG MG Z 301 1555 1555 2.76
SITE 1 AC1 5 THR G 8 TYR G 119 ARG G 122 ALA G 123
SITE 2 AC1 5 MET G 125
SITE 1 AC2 2 GLN H 91 ASP N 51
SITE 1 AC3 3 ALA I 174 ASP I 177 SER I 180
SITE 1 AC4 5 ARG I 27 TRP I 182 ASP I 204 HIS Y 166
SITE 2 AC4 5 MG Y 301
SITE 1 AC5 3 GLN J 118 ASP J 120 THR J 124
SITE 1 AC6 6 ALA K 165 HIS K 166 ASP K 168 ALA K 169
SITE 2 AC6 6 SER K 171 ASP W 204
SITE 1 AC7 2 ILE K 82 ASN K 85
SITE 1 AC8 4 ARG N 19 ILE N 163 ASP N 166 SER N 169
SITE 1 AC9 4 ASP L 222 ILE V 163 ASP V 166 SER V 169
SITE 1 BC1 8 ASP I 204 MG I 302 ARG Y 19 ALA Y 165
SITE 2 BC1 8 HIS Y 166 ASP Y 168 ALA Y 169 SER Y 171
SITE 1 BC2 5 THR Z 192 HIS Z 195 ILE Z 196 VAL Z 198
SITE 2 BC2 5 ASP Z 222
SITE 1 BC3 10 THR H 1 SER H 20 THR H 21 GLN H 22
SITE 2 BC3 10 GLY H 45 ALA H 46 GLY H 47 ALA H 49
SITE 3 BC3 10 ASP I 124 LEU I 125
SITE 1 BC4 9 HOH 2 101 THR K 1 ALA K 20 THR K 21
SITE 2 BC4 9 MET K 45 GLY K 47 ALA K 49 ASP L 126
SITE 3 BC4 9 VAL L 128
SITE 1 BC5 11 HOH 3 101 THR V 1 SER V 20 THR V 21
SITE 2 BC5 11 GLN V 22 GLY V 45 ALA V 46 GLY V 47
SITE 3 BC5 11 ALA V 49 ASP W 124 LEU W 125
SITE 1 BC6 9 HOH 4 101 THR Y 1 ALA Y 20 THR Y 21
SITE 2 BC6 9 MET Y 45 GLY Y 47 ALA Y 49 ASP Z 126
SITE 3 BC6 9 VAL Z 128
CRYST1 134.990 300.130 144.800 90.00 112.51 90.00 P 1 21 1 8
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 0.007408 0.000000 0.003070 0.00000
SCALE2 0.000000 0.003332 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007476 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 -0.999440 -0.003073 0.033333 67.27092 1
MTRIX2 2 -0.002667 -0.985301 -0.170809 -289.04437 1
MTRIX3 2 0.033368 -0.170802 0.984740 -25.78635 1
(ATOM LINES ARE NOT SHOWN.)
END
