HEADER HYDROLASE/HYDROLASE INHIBITOR 13-JUN-14 4QLQ
TITLE YCP IN COMPLEX WITH TRIPEPTIDIC EPOXYKETONE INHIBITOR 8
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-2;
COMPND 3 CHAIN: A, O;
COMPND 4 SYNONYM: MACROPAIN SUBUNIT Y7, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 5 SUBUNIT Y7, PROTEASOME COMPONENT Y7, PROTEINASE YSCE SUBUNIT 7;
COMPND 6 EC: 3.4.25.1;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-3;
COMPND 9 CHAIN: B, P;
COMPND 10 SYNONYM: MACROPAIN SUBUNIT Y13, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 11 SUBUNIT Y13, PROTEASOME COMPONENT Y13, PROTEINASE YSCE SUBUNIT 13;
COMPND 12 EC: 3.4.25.1;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-4;
COMPND 15 CHAIN: C, Q;
COMPND 16 SYNONYM: MACROPAIN SUBUNIT PRE6, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 17 SUBUNIT PRE6, PROTEASOME COMPONENT PRE6, PROTEINASE YSCE SUBUNIT
COMPND 18 PRE6;
COMPND 19 EC: 3.4.25.1;
COMPND 20 MOL_ID: 4;
COMPND 21 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-5;
COMPND 22 CHAIN: D, R;
COMPND 23 SYNONYM: MACROPAIN SUBUNIT PUP2, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 24 SUBUNIT PUP2, PROTEASOME COMPONENT PUP2, PROTEINASE YSCE SUBUNIT
COMPND 25 PUP2;
COMPND 26 EC: 3.4.25.1;
COMPND 27 MOL_ID: 5;
COMPND 28 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-6;
COMPND 29 CHAIN: E, S;
COMPND 30 SYNONYM: MACROPAIN SUBUNIT PRE5, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 31 SUBUNIT PRE5, PROTEASOME COMPONENT PRE5, PROTEINASE YSCE SUBUNIT
COMPND 32 PRE5;
COMPND 33 EC: 3.4.25.1;
COMPND 34 MOL_ID: 6;
COMPND 35 MOLECULE: PROBABLE PROTEASOME SUBUNIT ALPHA TYPE-7;
COMPND 36 CHAIN: F, T;
COMPND 37 SYNONYM: MACROPAIN SUBUNIT C1, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 38 SUBUNIT C1, PROTEASOME COMPONENT C1, PROTEINASE YSCE SUBUNIT 1;
COMPND 39 EC: 3.4.25.1;
COMPND 40 MOL_ID: 7;
COMPND 41 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-1;
COMPND 42 CHAIN: G, U;
COMPND 43 SYNONYM: MACROPAIN SUBUNIT C7-ALPHA, MULTICATALYTIC ENDOPEPTIDASE
COMPND 44 COMPLEX C7, PROTEASOME COMPONENT C7-ALPHA, PROTEASOME COMPONENT Y8,
COMPND 45 PROTEINASE YSCE SUBUNIT 7, SCL1 SUPPRESSOR PROTEIN;
COMPND 46 EC: 3.4.25.1;
COMPND 47 MOL_ID: 8;
COMPND 48 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-2;
COMPND 49 CHAIN: H, V;
COMPND 50 FRAGMENT: UNP RESIDUES 30-261;
COMPND 51 SYNONYM: MACROPAIN SUBUNIT PUP1, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 52 SUBUNIT PUP1, PROTEASOME COMPONENT PUP1, PROTEINASE YSCE SUBUNIT
COMPND 53 PUP1;
COMPND 54 EC: 3.4.25.1;
COMPND 55 MOL_ID: 9;
COMPND 56 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-3;
COMPND 57 CHAIN: I, W;
COMPND 58 SYNONYM: MACROPAIN SUBUNIT PUP3, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 59 SUBUNIT PUP3, PROTEASOME COMPONENT PUP3;
COMPND 60 EC: 3.4.25.1;
COMPND 61 MOL_ID: 10;
COMPND 62 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-4;
COMPND 63 CHAIN: J, X;
COMPND 64 SYNONYM: MACROPAIN SUBUNIT C11, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 65 SUBUNIT C11, PROTEASOME COMPONENT C11, PROTEINASE YSCE SUBUNIT 11;
COMPND 66 EC: 3.4.25.1;
COMPND 67 MOL_ID: 11;
COMPND 68 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-5;
COMPND 69 CHAIN: K, Y;
COMPND 70 FRAGMENT: UNP RESIDUES 76-287;
COMPND 71 SYNONYM: MACROPAIN SUBUNIT PRE2, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 72 SUBUNIT PRE2, PROTEASOME COMPONENT PRE2, PROTEINASE YSCE SUBUNIT
COMPND 73 PRE2;
COMPND 74 EC: 3.4.25.1;
COMPND 75 MOL_ID: 12;
COMPND 76 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-6;
COMPND 77 CHAIN: L, Z;
COMPND 78 FRAGMENT: UNP RESIDUES 20-241;
COMPND 79 SYNONYM: MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C5, PROTEASOME
COMPND 80 COMPONENT C5;
COMPND 81 EC: 3.4.25.1;
COMPND 82 MOL_ID: 13;
COMPND 83 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-7;
COMPND 84 CHAIN: M, a;
COMPND 85 FRAGMENT: UNP RESIDUES 21-260;
COMPND 86 SYNONYM: MACROPAIN SUBUNIT PRE4, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 87 SUBUNIT PRE4, PROTEASOME COMPONENT PRE4, PROTEINASE YSCE SUBUNIT
COMPND 88 PRE4;
COMPND 89 EC: 3.4.25.1;
COMPND 90 MOL_ID: 14;
COMPND 91 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-1;
COMPND 92 CHAIN: N, b;
COMPND 93 FRAGMENT: UNP RESIDUES 20-215;
COMPND 94 SYNONYM: MACROPAIN SUBUNIT PRE3, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 95 SUBUNIT PRE3, PROTEASOME COMPONENT PRE3, PROTEINASE YSCE SUBUNIT
COMPND 96 PRE3;
COMPND 97 EC: 3.4.25.1
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
KEYWDS PROTEASOME, EPOXYKETONE, IMMUNOPROTEASOME INHIBITOR, BINDING
KEYWDS 2 ANALYSIS, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR G.DE BRUIN,E.HUBER,B.XIN,E.VAN ROODEN,K.AL-AYED,K.KIM,A.KISSELEV,
AUTHOR 2 C.DRIESSEN,G.VAN DER MAREL,M.GROLL,H.OVERKLEEFT
REVDAT 3 08-NOV-23 4QLQ 1 REMARK LINK
REVDAT 2 01-OCT-14 4QLQ 1 JRNL
REVDAT 1 23-JUL-14 4QLQ 0
JRNL AUTH G.DE BRUIN,E.M.HUBER,B.T.XIN,E.J.VAN ROODEN,K.AL-AYED,
JRNL AUTH 2 K.B.KIM,A.F.KISSELEV,C.DRIESSEN,M.VAN DER STELT,
JRNL AUTH 3 G.A.VAN DER MAREL,M.GROLL,H.S.OVERKLEEFT
JRNL TITL STRUCTURE-BASED DESIGN OF BETA 1I OR BETA 5I SPECIFIC
JRNL TITL 2 INHIBITORS OF HUMAN IMMUNOPROTEASOMES
JRNL REF J.MED.CHEM. V. 57 6197 2014
JRNL REFN ISSN 0022-2623
JRNL PMID 25006746
JRNL DOI 10.1021/JM500716S
REMARK 2
REMARK 2 RESOLUTION. 2.40 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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 389163
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 20483
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 28221
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.13
REMARK 3 BIN R VALUE (WORKING SET) : 0.3470
REMARK 3 BIN FREE R VALUE SET COUNT : 1486
REMARK 3 BIN FREE R VALUE : 0.3620
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 49296
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 224
REMARK 3 SOLVENT ATOMS : 812
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.86
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.61000
REMARK 3 B22 (A**2) : -6.78000
REMARK 3 B33 (A**2) : 3.18000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.32000
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): 0.190
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.157
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.137
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.952
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 50434 ; 0.005 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 48230 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 68240 ; 1.119 ; 1.968
REMARK 3 BOND ANGLES OTHERS (DEGREES):111088 ; 0.797 ; 3.002
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 6306 ; 6.346 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 2246 ;36.371 ;24.408
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 8738 ;18.150 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 284 ;19.223 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 7684 ; 0.063 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 57108 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 11284 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 25314 ; 1.925 ; 4.965
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 25313 ; 1.925 ; 4.965
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 31590 ; 2.169 ; 7.429
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 31591 ; 2.169 ; 7.430
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 25120 ; 2.193 ; 5.378
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 25120 ; 2.193 ; 5.378
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 36651 ; 2.116 ; 7.878
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 54921 ; 2.607 ;38.899
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 54793 ; 2.550 ;38.876
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 98664 ; 1.136 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 401 ;27.344 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 98169 ; 4.780 ; 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 : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 250
REMARK 3 ORIGIN FOR THE GROUP (A): 67.8089 -92.1444 45.9988
REMARK 3 T TENSOR
REMARK 3 T11: 0.1009 T22: 0.0425
REMARK 3 T33: 0.1136 T12: -0.0286
REMARK 3 T13: 0.0087 T23: -0.0215
REMARK 3 L TENSOR
REMARK 3 L11: 0.0487 L22: 0.1810
REMARK 3 L33: 0.0527 L12: 0.0371
REMARK 3 L13: -0.0146 L23: -0.0390
REMARK 3 S TENSOR
REMARK 3 S11: 0.0186 S12: 0.0222 S13: -0.0034
REMARK 3 S21: 0.0228 S22: -0.0034 S23: -0.0731
REMARK 3 S31: -0.0322 S32: -0.0011 S33: -0.0153
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 244
REMARK 3 ORIGIN FOR THE GROUP (A): 60.4743 -87.9094 16.4091
REMARK 3 T TENSOR
REMARK 3 T11: 0.1259 T22: 0.0634
REMARK 3 T33: 0.0856 T12: -0.0320
REMARK 3 T13: 0.0553 T23: 0.0293
REMARK 3 L TENSOR
REMARK 3 L11: 0.0640 L22: 0.1542
REMARK 3 L33: 0.0714 L12: -0.0492
REMARK 3 L13: 0.0226 L23: 0.0662
REMARK 3 S TENSOR
REMARK 3 S11: -0.0283 S12: 0.0159 S13: 0.0215
REMARK 3 S21: -0.0348 S22: 0.0030 S23: -0.0160
REMARK 3 S31: -0.0413 S32: 0.0235 S33: 0.0253
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1 C 240
REMARK 3 ORIGIN FOR THE GROUP (A): 33.0907 -87.2548 1.0955
REMARK 3 T TENSOR
REMARK 3 T11: 0.1467 T22: 0.0535
REMARK 3 T33: 0.0810 T12: -0.0063
REMARK 3 T13: 0.0057 T23: 0.0384
REMARK 3 L TENSOR
REMARK 3 L11: 0.1245 L22: 0.1161
REMARK 3 L33: 0.1681 L12: 0.1091
REMARK 3 L13: 0.1149 L23: 0.0726
REMARK 3 S TENSOR
REMARK 3 S11: -0.0418 S12: 0.0350 S13: 0.0238
REMARK 3 S21: -0.0670 S22: 0.0389 S23: 0.0284
REMARK 3 S31: -0.0169 S32: 0.0434 S33: 0.0029
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 1 D 242
REMARK 3 ORIGIN FOR THE GROUP (A): 3.8380 -89.8485 13.7774
REMARK 3 T TENSOR
REMARK 3 T11: 0.0842 T22: 0.0343
REMARK 3 T33: 0.2002 T12: 0.0312
REMARK 3 T13: -0.0391 T23: 0.0235
REMARK 3 L TENSOR
REMARK 3 L11: 0.0375 L22: 0.1278
REMARK 3 L33: 0.1386 L12: 0.0314
REMARK 3 L13: -0.0350 L23: 0.0652
REMARK 3 S TENSOR
REMARK 3 S11: -0.0269 S12: -0.0172 S13: 0.0471
REMARK 3 S21: -0.0395 S22: 0.0003 S23: 0.1423
REMARK 3 S31: -0.0244 S32: 0.0143 S33: 0.0266
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 3 E 233
REMARK 3 ORIGIN FOR THE GROUP (A): -2.4084 -94.0630 45.8422
REMARK 3 T TENSOR
REMARK 3 T11: 0.0555 T22: 0.0295
REMARK 3 T33: 0.2220 T12: 0.0324
REMARK 3 T13: 0.0624 T23: 0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 0.2566 L22: 0.0504
REMARK 3 L33: 0.2774 L12: -0.0008
REMARK 3 L13: 0.1522 L23: 0.0108
REMARK 3 S TENSOR
REMARK 3 S11: -0.0234 S12: -0.0030 S13: 0.0412
REMARK 3 S21: 0.0328 S22: 0.0039 S23: 0.1025
REMARK 3 S31: -0.0453 S32: -0.0351 S33: 0.0195
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 2 F 244
REMARK 3 ORIGIN FOR THE GROUP (A): 16.0839 -94.7744 70.0142
REMARK 3 T TENSOR
REMARK 3 T11: 0.1877 T22: 0.0483
REMARK 3 T33: 0.0813 T12: 0.0044
REMARK 3 T13: 0.0919 T23: -0.0367
REMARK 3 L TENSOR
REMARK 3 L11: 0.2688 L22: 0.1461
REMARK 3 L33: 0.0163 L12: 0.1154
REMARK 3 L13: -0.0098 L23: 0.0330
REMARK 3 S TENSOR
REMARK 3 S11: 0.0191 S12: -0.0312 S13: 0.0549
REMARK 3 S21: 0.0944 S22: -0.0274 S23: 0.0642
REMARK 3 S31: 0.0193 S32: -0.0075 S33: 0.0082
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 2 G 242
REMARK 3 ORIGIN FOR THE GROUP (A): 48.6247 -93.3765 71.2013
REMARK 3 T TENSOR
REMARK 3 T11: 0.2028 T22: 0.0377
REMARK 3 T33: 0.0447 T12: -0.0243
REMARK 3 T13: 0.0143 T23: -0.0245
REMARK 3 L TENSOR
REMARK 3 L11: 0.0443 L22: 0.2452
REMARK 3 L33: 0.1716 L12: 0.0760
REMARK 3 L13: -0.0177 L23: -0.0002
REMARK 3 S TENSOR
REMARK 3 S11: 0.0269 S12: 0.0078 S13: -0.0017
REMARK 3 S21: 0.1015 S22: -0.0204 S23: -0.0297
REMARK 3 S31: -0.0304 S32: -0.0051 S33: -0.0065
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 1 H 222
REMARK 3 ORIGIN FOR THE GROUP (A): 67.9821-130.1499 48.0593
REMARK 3 T TENSOR
REMARK 3 T11: 0.0909 T22: 0.0580
REMARK 3 T33: 0.1207 T12: -0.0055
REMARK 3 T13: -0.0234 T23: -0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 0.0198 L22: 0.2432
REMARK 3 L33: 0.0140 L12: 0.0565
REMARK 3 L13: 0.0095 L23: 0.0462
REMARK 3 S TENSOR
REMARK 3 S11: 0.0345 S12: 0.0041 S13: -0.0125
REMARK 3 S21: 0.0892 S22: -0.0138 S23: -0.1189
REMARK 3 S31: 0.0011 S32: -0.0001 S33: -0.0207
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 1 I 204
REMARK 3 ORIGIN FOR THE GROUP (A): 68.9732-127.6063 20.7830
REMARK 3 T TENSOR
REMARK 3 T11: 0.0724 T22: 0.0604
REMARK 3 T33: 0.1250 T12: -0.0103
REMARK 3 T13: 0.0441 T23: -0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 0.1154 L22: 0.4525
REMARK 3 L33: 0.0420 L12: 0.0506
REMARK 3 L13: -0.0530 L23: 0.0396
REMARK 3 S TENSOR
REMARK 3 S11: 0.0020 S12: 0.0342 S13: -0.0248
REMARK 3 S21: -0.0404 S22: -0.0128 S23: -0.1166
REMARK 3 S31: -0.0189 S32: -0.0230 S33: 0.0107
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 1 J 195
REMARK 3 ORIGIN FOR THE GROUP (A): 45.3109-126.5287 -0.5783
REMARK 3 T TENSOR
REMARK 3 T11: 0.1567 T22: 0.0639
REMARK 3 T33: 0.0373 T12: 0.0056
REMARK 3 T13: 0.0508 T23: 0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 0.0701 L22: 0.3803
REMARK 3 L33: 0.0107 L12: 0.1329
REMARK 3 L13: -0.0254 L23: -0.0423
REMARK 3 S TENSOR
REMARK 3 S11: 0.0070 S12: -0.0026 S13: 0.0057
REMARK 3 S21: -0.1233 S22: -0.0014 S23: -0.0145
REMARK 3 S31: -0.0111 S32: -0.0067 S33: -0.0056
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K 1 K 212
REMARK 3 ORIGIN FOR THE GROUP (A): 11.4559-130.6026 2.6709
REMARK 3 T TENSOR
REMARK 3 T11: 0.1085 T22: 0.0589
REMARK 3 T33: 0.1139 T12: 0.0092
REMARK 3 T13: -0.0442 T23: 0.0220
REMARK 3 L TENSOR
REMARK 3 L11: 0.0993 L22: 0.4823
REMARK 3 L33: 0.0507 L12: 0.0501
REMARK 3 L13: 0.0062 L23: 0.0322
REMARK 3 S TENSOR
REMARK 3 S11: 0.0285 S12: 0.0034 S13: 0.0241
REMARK 3 S21: -0.0970 S22: 0.0093 S23: 0.1436
REMARK 3 S31: -0.0133 S32: 0.0115 S33: -0.0378
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 1 L 222
REMARK 3 ORIGIN FOR THE GROUP (A): -3.9005-133.9640 28.8699
REMARK 3 T TENSOR
REMARK 3 T11: 0.0436 T22: 0.0480
REMARK 3 T33: 0.1857 T12: 0.0124
REMARK 3 T13: 0.0073 T23: 0.0249
REMARK 3 L TENSOR
REMARK 3 L11: 0.0032 L22: 0.2392
REMARK 3 L33: 0.1554 L12: 0.0113
REMARK 3 L13: 0.0110 L23: 0.0747
REMARK 3 S TENSOR
REMARK 3 S11: 0.0096 S12: 0.0032 S13: -0.0016
REMARK 3 S21: 0.0046 S22: 0.0070 S23: 0.1609
REMARK 3 S31: -0.0311 S32: 0.0189 S33: -0.0165
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : M 1 M 233
REMARK 3 ORIGIN FOR THE GROUP (A): 8.4012-137.5768 60.6677
REMARK 3 T TENSOR
REMARK 3 T11: 0.1170 T22: 0.0490
REMARK 3 T33: 0.0893 T12: -0.0103
REMARK 3 T13: 0.0918 T23: -0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 0.0434 L22: 0.3518
REMARK 3 L33: 0.1159 L12: -0.0208
REMARK 3 L13: 0.0525 L23: 0.0541
REMARK 3 S TENSOR
REMARK 3 S11: 0.0209 S12: -0.0059 S13: 0.0154
REMARK 3 S21: 0.0935 S22: -0.0293 S23: 0.0844
REMARK 3 S31: -0.0022 S32: -0.0048 S33: 0.0084
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : N 1 N 196
REMARK 3 ORIGIN FOR THE GROUP (A): 40.4599-133.8745 71.0853
REMARK 3 T TENSOR
REMARK 3 T11: 0.2552 T22: 0.1074
REMARK 3 T33: 0.0657 T12: -0.0177
REMARK 3 T13: -0.0012 T23: -0.0219
REMARK 3 L TENSOR
REMARK 3 L11: 0.0577 L22: 0.0273
REMARK 3 L33: 0.0007 L12: 0.0371
REMARK 3 L13: 0.0004 L23: -0.0012
REMARK 3 S TENSOR
REMARK 3 S11: 0.0265 S12: 0.0401 S13: -0.0537
REMARK 3 S21: 0.0470 S22: -0.0077 S23: -0.0352
REMARK 3 S31: -0.0098 S32: 0.0065 S33: -0.0188
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : O 1 O 250
REMARK 3 ORIGIN FOR THE GROUP (A): 2.0655-206.1233 37.0098
REMARK 3 T TENSOR
REMARK 3 T11: 0.0888 T22: 0.0303
REMARK 3 T33: 0.1468 T12: -0.0352
REMARK 3 T13: -0.0262 T23: 0.0304
REMARK 3 L TENSOR
REMARK 3 L11: 0.1922 L22: 0.0911
REMARK 3 L33: 0.1356 L12: -0.0110
REMARK 3 L13: -0.0829 L23: 0.0657
REMARK 3 S TENSOR
REMARK 3 S11: 0.0141 S12: 0.0188 S13: -0.0068
REMARK 3 S21: 0.0292 S22: 0.0073 S23: 0.0668
REMARK 3 S31: 0.0565 S32: -0.0152 S33: -0.0213
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : P 1 P 244
REMARK 3 ORIGIN FOR THE GROUP (A): 8.3471-205.0013 6.8484
REMARK 3 T TENSOR
REMARK 3 T11: 0.1201 T22: 0.0396
REMARK 3 T33: 0.1218 T12: -0.0144
REMARK 3 T13: -0.0607 T23: -0.0299
REMARK 3 L TENSOR
REMARK 3 L11: 0.0665 L22: 0.0902
REMARK 3 L33: 0.0552 L12: 0.0661
REMARK 3 L13: 0.0452 L23: 0.0206
REMARK 3 S TENSOR
REMARK 3 S11: -0.0207 S12: -0.0238 S13: -0.0013
REMARK 3 S21: -0.0636 S22: 0.0017 S23: -0.0094
REMARK 3 S31: 0.0177 S32: -0.0393 S33: 0.0190
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Q 1 Q 240
REMARK 3 ORIGIN FOR THE GROUP (A): 35.5127-203.1749 -9.0919
REMARK 3 T TENSOR
REMARK 3 T11: 0.2503 T22: 0.0316
REMARK 3 T33: 0.1176 T12: -0.0015
REMARK 3 T13: -0.0664 T23: -0.0481
REMARK 3 L TENSOR
REMARK 3 L11: 0.2337 L22: 0.1615
REMARK 3 L33: 0.0174 L12: 0.0710
REMARK 3 L13: 0.0468 L23: -0.0054
REMARK 3 S TENSOR
REMARK 3 S11: 0.0212 S12: 0.0132 S13: -0.0484
REMARK 3 S21: -0.1695 S22: 0.0083 S23: 0.0601
REMARK 3 S31: 0.0197 S32: 0.0156 S33: -0.0295
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : R 1 R 242
REMARK 3 ORIGIN FOR THE GROUP (A): 65.0866-202.6935 3.1213
REMARK 3 T TENSOR
REMARK 3 T11: 0.1613 T22: 0.0628
REMARK 3 T33: 0.1402 T12: 0.0621
REMARK 3 T13: 0.0805 T23: -0.0241
REMARK 3 L TENSOR
REMARK 3 L11: 0.0586 L22: 0.2685
REMARK 3 L33: 0.0794 L12: -0.0980
REMARK 3 L13: 0.0660 L23: -0.1315
REMARK 3 S TENSOR
REMARK 3 S11: 0.0254 S12: -0.0030 S13: 0.0249
REMARK 3 S21: -0.1375 S22: -0.0529 S23: -0.0879
REMARK 3 S31: 0.0455 S32: 0.0115 S33: 0.0275
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : S 3 S 233
REMARK 3 ORIGIN FOR THE GROUP (A): 72.2635-203.9570 35.1053
REMARK 3 T TENSOR
REMARK 3 T11: 0.0583 T22: 0.0357
REMARK 3 T33: 0.2676 T12: 0.0428
REMARK 3 T13: -0.0556 T23: -0.0218
REMARK 3 L TENSOR
REMARK 3 L11: 0.0431 L22: 0.1199
REMARK 3 L33: 0.3596 L12: 0.0034
REMARK 3 L13: 0.0223 L23: -0.1540
REMARK 3 S TENSOR
REMARK 3 S11: 0.0204 S12: 0.0191 S13: -0.0602
REMARK 3 S21: 0.0146 S22: -0.0136 S23: -0.1070
REMARK 3 S31: 0.0438 S32: 0.0591 S33: -0.0069
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : T 2 T 244
REMARK 3 ORIGIN FOR THE GROUP (A): 54.4030-207.5017 59.4561
REMARK 3 T TENSOR
REMARK 3 T11: 0.1498 T22: 0.0290
REMARK 3 T33: 0.1725 T12: -0.0074
REMARK 3 T13: -0.1186 T23: 0.0532
REMARK 3 L TENSOR
REMARK 3 L11: 0.1988 L22: 0.1971
REMARK 3 L33: 0.0579 L12: 0.1945
REMARK 3 L13: -0.0861 L23: -0.0954
REMARK 3 S TENSOR
REMARK 3 S11: 0.0401 S12: -0.0523 S13: -0.1176
REMARK 3 S21: 0.0649 S22: -0.0535 S23: -0.1086
REMARK 3 S31: -0.0298 S32: 0.0050 S33: 0.0134
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : U 2 U 242
REMARK 3 ORIGIN FOR THE GROUP (A): 22.0631-209.4404 61.2685
REMARK 3 T TENSOR
REMARK 3 T11: 0.1585 T22: 0.0241
REMARK 3 T33: 0.0984 T12: -0.0117
REMARK 3 T13: -0.0320 T23: 0.0413
REMARK 3 L TENSOR
REMARK 3 L11: 0.0184 L22: 0.2188
REMARK 3 L33: 0.0613 L12: -0.0124
REMARK 3 L13: -0.0313 L23: -0.0006
REMARK 3 S TENSOR
REMARK 3 S11: 0.0006 S12: -0.0019 S13: -0.0000
REMARK 3 S21: 0.0557 S22: 0.0114 S23: 0.0440
REMARK 3 S31: -0.0134 S32: 0.0051 S33: -0.0120
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : V 1 V 222
REMARK 3 ORIGIN FOR THE GROUP (A): 2.0475-169.0717 45.6646
REMARK 3 T TENSOR
REMARK 3 T11: 0.0861 T22: 0.0463
REMARK 3 T33: 0.1476 T12: -0.0126
REMARK 3 T13: 0.0224 T23: 0.0250
REMARK 3 L TENSOR
REMARK 3 L11: 0.0196 L22: 0.2432
REMARK 3 L33: 0.0156 L12: 0.0451
REMARK 3 L13: 0.0046 L23: -0.0253
REMARK 3 S TENSOR
REMARK 3 S11: 0.0349 S12: -0.0066 S13: 0.0078
REMARK 3 S21: 0.0666 S22: -0.0185 S23: 0.1409
REMARK 3 S31: 0.0217 S32: 0.0054 S33: -0.0164
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : W 1 W 204
REMARK 3 ORIGIN FOR THE GROUP (A): 0.2578-166.7988 18.3542
REMARK 3 T TENSOR
REMARK 3 T11: 0.0790 T22: 0.0475
REMARK 3 T33: 0.1549 T12: 0.0005
REMARK 3 T13: -0.0526 T23: 0.0101
REMARK 3 L TENSOR
REMARK 3 L11: 0.0217 L22: 0.3106
REMARK 3 L33: 0.0298 L12: 0.0662
REMARK 3 L13: 0.0211 L23: 0.0499
REMARK 3 S TENSOR
REMARK 3 S11: -0.0036 S12: 0.0180 S13: 0.0199
REMARK 3 S21: -0.0590 S22: 0.0044 S23: 0.1212
REMARK 3 S31: 0.0250 S32: 0.0154 S33: -0.0008
REMARK 3
REMARK 3 TLS GROUP : 24
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : X 1 X 195
REMARK 3 ORIGIN FOR THE GROUP (A): 23.3196-164.0758 -3.5993
REMARK 3 T TENSOR
REMARK 3 T11: 0.1622 T22: 0.0468
REMARK 3 T33: 0.0505 T12: 0.0016
REMARK 3 T13: -0.0445 T23: -0.0236
REMARK 3 L TENSOR
REMARK 3 L11: 0.1202 L22: 0.3096
REMARK 3 L33: 0.0169 L12: -0.0351
REMARK 3 L13: 0.0016 L23: 0.0577
REMARK 3 S TENSOR
REMARK 3 S11: 0.0044 S12: -0.0067 S13: -0.0362
REMARK 3 S21: -0.1453 S22: 0.0074 S23: 0.0336
REMARK 3 S31: -0.0100 S32: 0.0115 S33: -0.0118
REMARK 3
REMARK 3 TLS GROUP : 25
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Y 1 Y 212
REMARK 3 ORIGIN FOR THE GROUP (A): 57.2755-160.5643 -0.6194
REMARK 3 T TENSOR
REMARK 3 T11: 0.1290 T22: 0.0671
REMARK 3 T33: 0.0827 T12: 0.0149
REMARK 3 T13: 0.0736 T23: -0.0286
REMARK 3 L TENSOR
REMARK 3 L11: 0.1206 L22: 0.3872
REMARK 3 L33: 0.0938 L12: 0.0067
REMARK 3 L13: 0.1045 L23: 0.0018
REMARK 3 S TENSOR
REMARK 3 S11: 0.0294 S12: 0.0187 S13: -0.0376
REMARK 3 S21: -0.1002 S22: 0.0133 S23: -0.0944
REMARK 3 S31: 0.0172 S32: 0.0264 S33: -0.0428
REMARK 3
REMARK 3 TLS GROUP : 26
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Z 1 Z 222
REMARK 3 ORIGIN FOR THE GROUP (A): 73.3538-161.7676 25.2778
REMARK 3 T TENSOR
REMARK 3 T11: 0.0513 T22: 0.0656
REMARK 3 T33: 0.1607 T12: 0.0175
REMARK 3 T13: 0.0131 T23: -0.0252
REMARK 3 L TENSOR
REMARK 3 L11: 0.0192 L22: 0.3630
REMARK 3 L33: 0.1432 L12: 0.0220
REMARK 3 L13: -0.0253 L23: -0.0551
REMARK 3 S TENSOR
REMARK 3 S11: 0.0207 S12: 0.0112 S13: -0.0170
REMARK 3 S21: -0.0033 S22: -0.0176 S23: -0.1673
REMARK 3 S31: 0.0119 S32: -0.0141 S33: -0.0031
REMARK 3
REMARK 3 TLS GROUP : 27
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : a 1 a 233
REMARK 3 ORIGIN FOR THE GROUP (A): 61.9698-163.7491 57.5345
REMARK 3 T TENSOR
REMARK 3 T11: 0.1270 T22: 0.0371
REMARK 3 T33: 0.0949 T12: 0.0004
REMARK 3 T13: -0.0732 T23: 0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 0.0310 L22: 0.3123
REMARK 3 L33: 0.0178 L12: -0.0323
REMARK 3 L13: -0.0209 L23: 0.0452
REMARK 3 S TENSOR
REMARK 3 S11: 0.0094 S12: 0.0114 S13: -0.0235
REMARK 3 S21: 0.1082 S22: -0.0096 S23: -0.0953
REMARK 3 S31: -0.0001 S32: -0.0120 S33: 0.0001
REMARK 3
REMARK 3 TLS GROUP : 28
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : b 1 b 196
REMARK 3 ORIGIN FOR THE GROUP (A): 30.2354-169.3506 68.1497
REMARK 3 T TENSOR
REMARK 3 T11: 0.2300 T22: 0.0876
REMARK 3 T33: 0.0837 T12: -0.0306
REMARK 3 T13: 0.0067 T23: 0.0367
REMARK 3 L TENSOR
REMARK 3 L11: 0.0046 L22: 0.0069
REMARK 3 L33: 0.0016 L12: 0.0048
REMARK 3 L13: -0.0017 L23: -0.0005
REMARK 3 S TENSOR
REMARK 3 S11: 0.0106 S12: 0.0112 S13: 0.0171
REMARK 3 S21: 0.0302 S22: -0.0016 S23: 0.0164
REMARK 3 S31: 0.0028 S32: -0.0116 S33: -0.0089
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 4QLQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-JUN-14.
REMARK 100 THE DEPOSITION ID IS D_1000086213.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-OCT-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 : 409646
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
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 (%) : 98.3
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.05200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.44300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
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 (%): 67.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20MM MGAC2, 100MM 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 149.79500
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: 28-MERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 28-MERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 117660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 214500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -349.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K, L, M, N, O, P, Q, R, S,
REMARK 350 AND CHAINS: T, U, V, W, X, Y, Z, a, b
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET B 0
REMARK 465 LYS B 245
REMARK 465 LYS B 246
REMARK 465 ASP B 247
REMARK 465 GLU B 248
REMARK 465 ASP B 249
REMARK 465 GLU B 250
REMARK 465 GLU B 251
REMARK 465 ALA B 252
REMARK 465 ASP B 253
REMARK 465 GLU B 254
REMARK 465 ASP B 255
REMARK 465 MET B 256
REMARK 465 LYS B 257
REMARK 465 MET C -1
REMARK 465 SER C 0
REMARK 465 GLN C 241
REMARK 465 GLN C 242
REMARK 465 GLU C 243
REMARK 465 GLN C 244
REMARK 465 ASP C 245
REMARK 465 LYS C 246
REMARK 465 LYS C 247
REMARK 465 LYS C 248
REMARK 465 LYS C 249
REMARK 465 SER C 250
REMARK 465 ASN C 251
REMARK 465 HIS C 252
REMARK 465 MET D -7
REMARK 465 PHE D -6
REMARK 465 LEU D -5
REMARK 465 THR D -4
REMARK 465 ARG D -3
REMARK 465 SER D -2
REMARK 465 GLU D -1
REMARK 465 TYR D 0
REMARK 465 GLY D 118
REMARK 465 ALA D 119
REMARK 465 SER D 120
REMARK 465 GLY D 121
REMARK 465 GLU D 122
REMARK 465 GLU D 123
REMARK 465 ARG D 124
REMARK 465 SER D 243
REMARK 465 PRO D 244
REMARK 465 GLU D 245
REMARK 465 GLU D 246
REMARK 465 ALA D 247
REMARK 465 ASP D 248
REMARK 465 VAL D 249
REMARK 465 GLU D 250
REMARK 465 MET D 251
REMARK 465 SER D 252
REMARK 465 MET E 0
REMARK 465 PHE E 1
REMARK 465 ARG E 2
REMARK 465 MET F -3
REMARK 465 THR F -2
REMARK 465 SER F -1
REMARK 465 ILE F 0
REMARK 465 GLY F 1
REMARK 465 GLY F 245
REMARK 465 ASP F 246
REMARK 465 ASP F 247
REMARK 465 ASP F 248
REMARK 465 GLU F 249
REMARK 465 ASP F 250
REMARK 465 GLU F 251
REMARK 465 ASP F 252
REMARK 465 ASP F 253
REMARK 465 SER F 254
REMARK 465 ASP F 255
REMARK 465 ASN F 256
REMARK 465 VAL F 257
REMARK 465 MET F 258
REMARK 465 SER F 259
REMARK 465 SER F 260
REMARK 465 ASP F 261
REMARK 465 ASP F 262
REMARK 465 GLU F 263
REMARK 465 ASN F 264
REMARK 465 ALA F 265
REMARK 465 PRO F 266
REMARK 465 VAL F 267
REMARK 465 ALA F 268
REMARK 465 THR F 269
REMARK 465 ASN F 270
REMARK 465 ALA F 271
REMARK 465 ASN F 272
REMARK 465 ALA F 273
REMARK 465 THR F 274
REMARK 465 THR F 275
REMARK 465 ASP F 276
REMARK 465 GLN F 277
REMARK 465 GLU F 278
REMARK 465 GLY F 279
REMARK 465 ASP F 280
REMARK 465 ILE F 281
REMARK 465 HIS F 282
REMARK 465 LEU F 283
REMARK 465 GLU F 284
REMARK 465 MET G -8
REMARK 465 SER G -7
REMARK 465 GLY G -6
REMARK 465 ALA G -5
REMARK 465 ALA G -4
REMARK 465 ALA G -3
REMARK 465 ALA G -2
REMARK 465 SER G -1
REMARK 465 ALA G 0
REMARK 465 ALA G 1
REMARK 465 ASP G 243
REMARK 465 ILE H 223
REMARK 465 GLN H 224
REMARK 465 GLU H 225
REMARK 465 GLU H 226
REMARK 465 GLN H 227
REMARK 465 VAL H 228
REMARK 465 ASP H 229
REMARK 465 ILE H 230
REMARK 465 THR H 231
REMARK 465 ALA H 232
REMARK 465 MET I 0
REMARK 465 GLN J 196
REMARK 465 ALA J 197
REMARK 465 GLN J 198
REMARK 465 THR M -12
REMARK 465 GLN M -11
REMARK 465 ILE M -10
REMARK 465 ALA M -9
REMARK 465 ASN M -8
REMARK 465 ALA M -7
REMARK 465 GLY M -6
REMARK 465 ALA M -5
REMARK 465 SER M -4
REMARK 465 PRO M -3
REMARK 465 MET M -2
REMARK 465 VAL M -1
REMARK 465 ASN M 0
REMARK 465 MET P 0
REMARK 465 LYS P 245
REMARK 465 LYS P 246
REMARK 465 ASP P 247
REMARK 465 GLU P 248
REMARK 465 ASP P 249
REMARK 465 GLU P 250
REMARK 465 GLU P 251
REMARK 465 ALA P 252
REMARK 465 ASP P 253
REMARK 465 GLU P 254
REMARK 465 ASP P 255
REMARK 465 MET P 256
REMARK 465 LYS P 257
REMARK 465 MET Q -1
REMARK 465 SER Q 0
REMARK 465 GLN Q 241
REMARK 465 GLN Q 242
REMARK 465 GLU Q 243
REMARK 465 GLN Q 244
REMARK 465 ASP Q 245
REMARK 465 LYS Q 246
REMARK 465 LYS Q 247
REMARK 465 LYS Q 248
REMARK 465 LYS Q 249
REMARK 465 SER Q 250
REMARK 465 ASN Q 251
REMARK 465 HIS Q 252
REMARK 465 MET R -7
REMARK 465 PHE R -6
REMARK 465 LEU R -5
REMARK 465 THR R -4
REMARK 465 ARG R -3
REMARK 465 SER R -2
REMARK 465 GLU R -1
REMARK 465 TYR R 0
REMARK 465 GLY R 118
REMARK 465 ALA R 119
REMARK 465 SER R 120
REMARK 465 GLY R 121
REMARK 465 GLU R 122
REMARK 465 GLU R 123
REMARK 465 ARG R 124
REMARK 465 SER R 243
REMARK 465 PRO R 244
REMARK 465 GLU R 245
REMARK 465 GLU R 246
REMARK 465 ALA R 247
REMARK 465 ASP R 248
REMARK 465 VAL R 249
REMARK 465 GLU R 250
REMARK 465 MET R 251
REMARK 465 SER R 252
REMARK 465 MET S 0
REMARK 465 PHE S 1
REMARK 465 ARG S 2
REMARK 465 MET T -3
REMARK 465 THR T -2
REMARK 465 SER T -1
REMARK 465 ILE T 0
REMARK 465 GLY T 1
REMARK 465 GLY T 245
REMARK 465 ASP T 246
REMARK 465 ASP T 247
REMARK 465 ASP T 248
REMARK 465 GLU T 249
REMARK 465 ASP T 250
REMARK 465 GLU T 251
REMARK 465 ASP T 252
REMARK 465 ASP T 253
REMARK 465 SER T 254
REMARK 465 ASP T 255
REMARK 465 ASN T 256
REMARK 465 VAL T 257
REMARK 465 MET T 258
REMARK 465 SER T 259
REMARK 465 SER T 260
REMARK 465 ASP T 261
REMARK 465 ASP T 262
REMARK 465 GLU T 263
REMARK 465 ASN T 264
REMARK 465 ALA T 265
REMARK 465 PRO T 266
REMARK 465 VAL T 267
REMARK 465 ALA T 268
REMARK 465 THR T 269
REMARK 465 ASN T 270
REMARK 465 ALA T 271
REMARK 465 ASN T 272
REMARK 465 ALA T 273
REMARK 465 THR T 274
REMARK 465 THR T 275
REMARK 465 ASP T 276
REMARK 465 GLN T 277
REMARK 465 GLU T 278
REMARK 465 GLY T 279
REMARK 465 ASP T 280
REMARK 465 ILE T 281
REMARK 465 HIS T 282
REMARK 465 LEU T 283
REMARK 465 GLU T 284
REMARK 465 MET U -8
REMARK 465 SER U -7
REMARK 465 GLY U -6
REMARK 465 ALA U -5
REMARK 465 ALA U -4
REMARK 465 ALA U -3
REMARK 465 ALA U -2
REMARK 465 SER U -1
REMARK 465 ALA U 0
REMARK 465 ALA U 1
REMARK 465 ASP U 243
REMARK 465 ILE V 223
REMARK 465 GLN V 224
REMARK 465 GLU V 225
REMARK 465 GLU V 226
REMARK 465 GLN V 227
REMARK 465 VAL V 228
REMARK 465 ASP V 229
REMARK 465 ILE V 230
REMARK 465 THR V 231
REMARK 465 ALA V 232
REMARK 465 MET W 0
REMARK 465 GLN X 196
REMARK 465 ALA X 197
REMARK 465 GLN X 198
REMARK 465 THR a -12
REMARK 465 GLN a -11
REMARK 465 ILE a -10
REMARK 465 ALA a -9
REMARK 465 ASN a -8
REMARK 465 ALA a -7
REMARK 465 GLY a -6
REMARK 465 ALA a -5
REMARK 465 SER a -4
REMARK 465 PRO a -3
REMARK 465 MET a -2
REMARK 465 VAL a -1
REMARK 465 ASN a 0
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OG1 THR H 1 C31 38N H 303 1.41
REMARK 500 OG1 THR K 1 C31 38N K 303 1.41
REMARK 500 OG1 THR V 1 C31 38N V 303 1.41
REMARK 500 OG1 THR Y 1 C31 38N Y 303 1.41
REMARK 500 N THR Y 1 C37 38N Y 303 1.54
REMARK 500 N THR K 1 C37 38N K 303 1.54
REMARK 500 N THR H 1 C37 38N H 303 1.55
REMARK 500 N THR V 1 C37 38N V 303 1.55
REMARK 500 O HOH J 235 O HOH J 240 2.11
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 2 153.69 51.17
REMARK 500 ASP A 3 109.36 -59.83
REMARK 500 TYR A 97 -65.65 -148.13
REMARK 500 GLN A 123 -37.72 -137.03
REMARK 500 LYS A 166 -75.38 -22.14
REMARK 500 ALA A 249 48.89 -83.89
REMARK 500 ARG B 3 -36.50 -39.12
REMARK 500 ARG B 8 72.80 54.40
REMARK 500 VAL B 51 91.05 -28.46
REMARK 500 THR B 52 156.01 -49.55
REMARK 500 GLU B 63 -29.78 -149.58
REMARK 500 LYS B 217 35.16 -81.44
REMARK 500 ALA B 219 -138.26 -118.53
REMARK 500 ASP B 221 104.35 66.78
REMARK 500 ASN C 38 14.80 -160.50
REMARK 500 LEU C 52 -1.25 94.93
REMARK 500 PRO C 183 94.28 -40.21
REMARK 500 GLN C 202 -115.93 143.65
REMARK 500 ALA C 205 -135.29 -60.78
REMARK 500 GLN C 239 93.27 -65.31
REMARK 500 SER D 48 144.31 -170.71
REMARK 500 GLU D 201 -70.79 -58.92
REMARK 500 ALA D 241 33.70 -72.39
REMARK 500 SER E 39 -160.85 -100.11
REMARK 500 GLN E 59 120.17 -33.48
REMARK 500 ASP E 137 -159.50 -125.53
REMARK 500 THR E 158 -179.19 -173.61
REMARK 500 GLN E 198 6.82 -68.51
REMARK 500 ASP E 202 4.37 54.08
REMARK 500 THR E 206 -166.08 -109.00
REMARK 500 LYS E 217 -52.52 -21.07
REMARK 500 LYS E 231 -19.78 -39.45
REMARK 500 SER F 9 -7.52 91.07
REMARK 500 ASP F 40 29.36 -141.25
REMARK 500 GLN F 58 -9.74 67.95
REMARK 500 ASP F 67 -130.79 53.96
REMARK 500 LYS F 100 -55.56 77.80
REMARK 500 ASP F 202 21.08 -79.61
REMARK 500 ASN F 203 34.66 -164.69
REMARK 500 ASP G 222 -0.56 75.81
REMARK 500 ASN H 9 -65.45 -28.13
REMARK 500 ASN H 30 62.98 -150.91
REMARK 500 ASP H 145 73.85 60.35
REMARK 500 SER H 171 -111.71 67.14
REMARK 500 CYS H 221 -145.47 -100.02
REMARK 500 SER I 5 33.77 -140.75
REMARK 500 GLN I 31 -113.16 52.58
REMARK 500 ASP I 134 -63.73 -106.87
REMARK 500 ASP I 192 47.17 -154.06
REMARK 500 ASP J 2 -68.94 106.55
REMARK 500
REMARK 500 THIS ENTRY HAS 118 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP I 192 GLU I 193 142.74
REMARK 500 GLN L 135 CYS L 136 -145.16
REMARK 500 THR M 1 GLN M 2 -140.05
REMARK 500 ASP W 192 GLU W 193 142.87
REMARK 500 GLN Z 135 CYS Z 136 -144.75
REMARK 500 THR a 1 GLN a 2 -140.24
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 86.4
REMARK 620 3 ARG G 122 O 91.4 88.2
REMARK 620 4 MET G 125 O 169.9 85.6 94.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG H 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN H 91 OE1
REMARK 620 2 HOH N 311 O 67.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG I 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA I 174 O
REMARK 620 2 ASP I 177 O 74.3
REMARK 620 3 SER I 180 O 92.3 85.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG Y 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP I 204 O
REMARK 620 2 ALA Y 165 O 96.6
REMARK 620 3 ASP Y 168 O 161.7 101.4
REMARK 620 4 SER Y 171 O 97.6 89.5 86.5
REMARK 620 5 HOH Y 408 O 86.9 92.7 88.4 174.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG K 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA K 165 O
REMARK 620 2 ASP K 168 O 97.0
REMARK 620 3 SER K 171 O 85.9 83.3
REMARK 620 4 ASP W 204 O 97.6 165.4 97.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG V 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP L 222 OXT
REMARK 620 2 ILE V 163 O 94.9
REMARK 620 3 ASP V 166 O 144.8 119.8
REMARK 620 4 SER V 169 O 91.0 92.8 82.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG N 201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE N 163 O
REMARK 620 2 ASP N 166 O 74.0
REMARK 620 3 SER N 169 O 101.4 69.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG Z 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR Z 192 O
REMARK 620 2 HIS Z 195 O 89.2
REMARK 620 3 VAL Z 198 O 99.5 76.4
REMARK 620 N 1 2
REMARK 630
REMARK 630 MOLECULE TYPE: NULL
REMARK 630 MOLECULE NAME: N-(MORPHOLIN-4-YLACETYL)-L-ALANYL-N-[(2S,4R)-1-
REMARK 630 CYCLOHEXYL-5-HYDROXY-4-METHYL-3-OXOPENTAN-2-YL]-O-METHYL-L-
REMARK 630 TYROSINAMIDE
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630 M RES C SSSEQI
REMARK 630 38N H 303
REMARK 630 38N K 303
REMARK 630 38N V 303
REMARK 630 38N Y 303
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: 00E ALA 0A1 0B2
REMARK 630 DETAILS: NULL
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 MES H 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 38N H 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG I 301
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 MES K 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 38N K 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG N 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG V 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES V 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 38N V 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Y 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES Y 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 38N Y 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Z 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1RYP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE 20S PROTEASOME FROM YEAST AT 2.4 ANGSTROMS
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 1G65 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF EPOXOMICIN:20S PROTEASOME REVEALS A MOLECULAR
REMARK 900 BASIS FOR SELECTIVITY OF ALPHA,BETA-EPOXYKETONE PROTEASOME
REMARK 900 INHIBITORS
REMARK 900 RELATED ID: 4QLS RELATED DB: PDB
REMARK 900 RELATED ID: 4QLT RELATED DB: PDB
REMARK 900 RELATED ID: 4QLU RELATED DB: PDB
REMARK 900 RELATED ID: 4QLV RELATED DB: PDB
DBREF 4QLQ A 1 250 UNP P23639 PSA2_YEAST 1 250
DBREF 4QLQ B 0 257 UNP P23638 PSA3_YEAST 1 258
DBREF 4QLQ C -1 252 UNP P40303 PSA4_YEAST 1 254
DBREF 4QLQ D -7 252 UNP P32379 PSA5_YEAST 1 260
DBREF 4QLQ E 0 233 UNP P40302 PSA6_YEAST 1 234
DBREF 4QLQ F -3 284 UNP P21242 PSA7_YEAST 1 288
DBREF 4QLQ G -8 243 UNP P21243 PSA1_YEAST 1 252
DBREF 4QLQ H 1 232 UNP P25043 PSB2_YEAST 30 261
DBREF 4QLQ I 0 204 UNP P25451 PSB3_YEAST 1 205
DBREF 4QLQ J 1 198 UNP P22141 PSB4_YEAST 1 198
DBREF 4QLQ K 1 212 UNP P30656 PSB5_YEAST 76 287
DBREF 4QLQ L 1 222 UNP P23724 PSB6_YEAST 20 241
DBREF 4QLQ M -12 233 UNP P30657 PSB7_YEAST 21 266
DBREF 4QLQ N 1 196 UNP P38624 PSB1_YEAST 20 215
DBREF 4QLQ O 1 250 UNP P23639 PSA2_YEAST 1 250
DBREF 4QLQ P 0 257 UNP P23638 PSA3_YEAST 1 258
DBREF 4QLQ Q -1 252 UNP P40303 PSA4_YEAST 1 254
DBREF 4QLQ R -7 252 UNP P32379 PSA5_YEAST 1 260
DBREF 4QLQ S 0 233 UNP P40302 PSA6_YEAST 1 234
DBREF 4QLQ T -3 284 UNP P21242 PSA7_YEAST 1 288
DBREF 4QLQ U -8 243 UNP P21243 PSA1_YEAST 1 252
DBREF 4QLQ V 1 232 UNP P25043 PSB2_YEAST 30 261
DBREF 4QLQ W 0 204 UNP P25451 PSB3_YEAST 1 205
DBREF 4QLQ X 1 198 UNP P22141 PSB4_YEAST 1 198
DBREF 4QLQ Y 1 212 UNP P30656 PSB5_YEAST 76 287
DBREF 4QLQ Z 1 222 UNP P23724 PSB6_YEAST 20 241
DBREF 4QLQ a -12 233 UNP P30657 PSB7_YEAST 21 266
DBREF 4QLQ b 1 196 UNP P38624 PSB1_YEAST 20 215
SEQRES 1 A 250 MET THR ASP ARG TYR SER PHE SER LEU THR THR PHE SER
SEQRES 2 A 250 PRO SER GLY LYS LEU GLY GLN ILE ASP TYR ALA LEU THR
SEQRES 3 A 250 ALA VAL LYS GLN GLY VAL THR SER LEU GLY ILE LYS ALA
SEQRES 4 A 250 THR ASN GLY VAL VAL ILE ALA THR GLU LYS LYS SER SER
SEQRES 5 A 250 SER PRO LEU ALA MET SER GLU THR LEU SER LYS VAL SER
SEQRES 6 A 250 LEU LEU THR PRO ASP ILE GLY ALA VAL TYR SER GLY MET
SEQRES 7 A 250 GLY PRO ASP TYR ARG VAL LEU VAL ASP LYS SER ARG LYS
SEQRES 8 A 250 VAL ALA HIS THR SER TYR LYS ARG ILE TYR GLY GLU TYR
SEQRES 9 A 250 PRO PRO THR LYS LEU LEU VAL SER GLU VAL ALA LYS ILE
SEQRES 10 A 250 MET GLN GLU ALA THR GLN SER GLY GLY VAL ARG PRO PHE
SEQRES 11 A 250 GLY VAL SER LEU LEU ILE ALA GLY HIS ASP GLU PHE ASN
SEQRES 12 A 250 GLY PHE SER LEU TYR GLN VAL ASP PRO SER GLY SER TYR
SEQRES 13 A 250 PHE PRO TRP LYS ALA THR ALA ILE GLY LYS GLY SER VAL
SEQRES 14 A 250 ALA ALA LYS THR PHE LEU GLU LYS ARG TRP ASN ASP GLU
SEQRES 15 A 250 LEU GLU LEU GLU ASP ALA ILE HIS ILE ALA LEU LEU THR
SEQRES 16 A 250 LEU LYS GLU SER VAL GLU GLY GLU PHE ASN GLY ASP THR
SEQRES 17 A 250 ILE GLU LEU ALA ILE ILE GLY ASP GLU ASN PRO ASP LEU
SEQRES 18 A 250 LEU GLY TYR THR GLY ILE PRO THR ASP LYS GLY PRO ARG
SEQRES 19 A 250 PHE ARG LYS LEU THR SER GLN GLU ILE ASN ASP ARG LEU
SEQRES 20 A 250 GLU ALA LEU
SEQRES 1 B 258 MET GLY SER ARG ARG TYR ASP SER ARG THR THR ILE PHE
SEQRES 2 B 258 SER PRO GLU GLY ARG LEU TYR GLN VAL GLU TYR ALA LEU
SEQRES 3 B 258 GLU SER ILE SER HIS ALA GLY THR ALA ILE GLY ILE MET
SEQRES 4 B 258 ALA SER ASP GLY ILE VAL LEU ALA ALA GLU ARG LYS VAL
SEQRES 5 B 258 THR SER THR LEU LEU GLU GLN ASP THR SER THR GLU LYS
SEQRES 6 B 258 LEU TYR LYS LEU ASN ASP LYS ILE ALA VAL ALA VAL ALA
SEQRES 7 B 258 GLY LEU THR ALA ASP ALA GLU ILE LEU ILE ASN THR ALA
SEQRES 8 B 258 ARG ILE HIS ALA GLN ASN TYR LEU LYS THR TYR ASN GLU
SEQRES 9 B 258 ASP ILE PRO VAL GLU ILE LEU VAL ARG ARG LEU SER ASP
SEQRES 10 B 258 ILE LYS GLN GLY TYR THR GLN HIS GLY GLY LEU ARG PRO
SEQRES 11 B 258 PHE GLY VAL SER PHE ILE TYR ALA GLY TYR ASP ASP ARG
SEQRES 12 B 258 TYR GLY TYR GLN LEU TYR THR SER ASN PRO SER GLY ASN
SEQRES 13 B 258 TYR THR GLY TRP LYS ALA ILE SER VAL GLY ALA ASN THR
SEQRES 14 B 258 SER ALA ALA GLN THR LEU LEU GLN MET ASP TYR LYS ASP
SEQRES 15 B 258 ASP MET LYS VAL ASP ASP ALA ILE GLU LEU ALA LEU LYS
SEQRES 16 B 258 THR LEU SER LYS THR THR ASP SER SER ALA LEU THR TYR
SEQRES 17 B 258 ASP ARG LEU GLU PHE ALA THR ILE ARG LYS GLY ALA ASN
SEQRES 18 B 258 ASP GLY GLU VAL TYR GLN LYS ILE PHE LYS PRO GLN GLU
SEQRES 19 B 258 ILE LYS ASP ILE LEU VAL LYS THR GLY ILE THR LYS LYS
SEQRES 20 B 258 ASP GLU ASP GLU GLU ALA ASP GLU ASP MET LYS
SEQRES 1 C 254 MET SER GLY TYR ASP ARG ALA LEU SER ILE PHE SER PRO
SEQRES 2 C 254 ASP GLY HIS ILE PHE GLN VAL GLU TYR ALA LEU GLU ALA
SEQRES 3 C 254 VAL LYS ARG GLY THR CYS ALA VAL GLY VAL LYS GLY LYS
SEQRES 4 C 254 ASN CYS VAL VAL LEU GLY CYS GLU ARG ARG SER THR LEU
SEQRES 5 C 254 LYS LEU GLN ASP THR ARG ILE THR PRO SER LYS VAL SER
SEQRES 6 C 254 LYS ILE ASP SER HIS VAL VAL LEU SER PHE SER GLY LEU
SEQRES 7 C 254 ASN ALA ASP SER ARG ILE LEU ILE GLU LYS ALA ARG VAL
SEQRES 8 C 254 GLU ALA GLN SER HIS ARG LEU THR LEU GLU ASP PRO VAL
SEQRES 9 C 254 THR VAL GLU TYR LEU THR ARG TYR VAL ALA GLY VAL GLN
SEQRES 10 C 254 GLN ARG TYR THR GLN SER GLY GLY VAL ARG PRO PHE GLY
SEQRES 11 C 254 VAL SER THR LEU ILE ALA GLY PHE ASP PRO ARG ASP ASP
SEQRES 12 C 254 GLU PRO LYS LEU TYR GLN THR GLU PRO SER GLY ILE TYR
SEQRES 13 C 254 SER SER TRP SER ALA GLN THR ILE GLY ARG ASN SER LYS
SEQRES 14 C 254 THR VAL ARG GLU PHE LEU GLU LYS ASN TYR ASP ARG LYS
SEQRES 15 C 254 GLU PRO PRO ALA THR VAL GLU GLU CYS VAL LYS LEU THR
SEQRES 16 C 254 VAL ARG SER LEU LEU GLU VAL VAL GLN THR GLY ALA LYS
SEQRES 17 C 254 ASN ILE GLU ILE THR VAL VAL LYS PRO ASP SER ASP ILE
SEQRES 18 C 254 VAL ALA LEU SER SER GLU GLU ILE ASN GLN TYR VAL THR
SEQRES 19 C 254 GLN ILE GLU GLN GLU LYS GLN GLU GLN GLN GLU GLN ASP
SEQRES 20 C 254 LYS LYS LYS LYS SER ASN HIS
SEQRES 1 D 260 MET PHE LEU THR ARG SER GLU TYR ASP ARG GLY VAL SER
SEQRES 2 D 260 THR PHE SER PRO GLU GLY ARG LEU PHE GLN VAL GLU TYR
SEQRES 3 D 260 SER LEU GLU ALA ILE LYS LEU GLY SER THR ALA ILE GLY
SEQRES 4 D 260 ILE ALA THR LYS GLU GLY VAL VAL LEU GLY VAL GLU LYS
SEQRES 5 D 260 ARG ALA THR SER PRO LEU LEU GLU SER ASP SER ILE GLU
SEQRES 6 D 260 LYS ILE VAL GLU ILE ASP ARG HIS ILE GLY CYS ALA MET
SEQRES 7 D 260 SER GLY LEU THR ALA ASP ALA ARG SER MET ILE GLU HIS
SEQRES 8 D 260 ALA ARG THR ALA ALA VAL THR HIS ASN LEU TYR TYR ASP
SEQRES 9 D 260 GLU ASP ILE ASN VAL GLU SER LEU THR GLN SER VAL CYS
SEQRES 10 D 260 ASP LEU ALA LEU ARG PHE GLY GLU GLY ALA SER GLY GLU
SEQRES 11 D 260 GLU ARG LEU MET SER ARG PRO PHE GLY VAL ALA LEU LEU
SEQRES 12 D 260 ILE ALA GLY HIS ASP ALA ASP ASP GLY TYR GLN LEU PHE
SEQRES 13 D 260 HIS ALA GLU PRO SER GLY THR PHE TYR ARG TYR ASN ALA
SEQRES 14 D 260 LYS ALA ILE GLY SER GLY SER GLU GLY ALA GLN ALA GLU
SEQRES 15 D 260 LEU LEU ASN GLU TRP HIS SER SER LEU THR LEU LYS GLU
SEQRES 16 D 260 ALA GLU LEU LEU VAL LEU LYS ILE LEU LYS GLN VAL MET
SEQRES 17 D 260 GLU GLU LYS LEU ASP GLU ASN ASN ALA GLN LEU SER CYS
SEQRES 18 D 260 ILE THR LYS GLN ASP GLY PHE LYS ILE TYR ASP ASN GLU
SEQRES 19 D 260 LYS THR ALA GLU LEU ILE LYS GLU LEU LYS GLU LYS GLU
SEQRES 20 D 260 ALA ALA GLU SER PRO GLU GLU ALA ASP VAL GLU MET SER
SEQRES 1 E 234 MET PHE ARG ASN ASN TYR ASP GLY ASP THR VAL THR PHE
SEQRES 2 E 234 SER PRO THR GLY ARG LEU PHE GLN VAL GLU TYR ALA LEU
SEQRES 3 E 234 GLU ALA ILE LYS GLN GLY SER VAL THR VAL GLY LEU ARG
SEQRES 4 E 234 SER ASN THR HIS ALA VAL LEU VAL ALA LEU LYS ARG ASN
SEQRES 5 E 234 ALA ASP GLU LEU SER SER TYR GLN LYS LYS ILE ILE LYS
SEQRES 6 E 234 CYS ASP GLU HIS MET GLY LEU SER LEU ALA GLY LEU ALA
SEQRES 7 E 234 PRO ASP ALA ARG VAL LEU SER ASN TYR LEU ARG GLN GLN
SEQRES 8 E 234 CYS ASN TYR SER SER LEU VAL PHE ASN ARG LYS LEU ALA
SEQRES 9 E 234 VAL GLU ARG ALA GLY HIS LEU LEU CYS ASP LYS ALA GLN
SEQRES 10 E 234 LYS ASN THR GLN SER TYR GLY GLY ARG PRO TYR GLY VAL
SEQRES 11 E 234 GLY LEU LEU ILE ILE GLY TYR ASP LYS SER GLY ALA HIS
SEQRES 12 E 234 LEU LEU GLU PHE GLN PRO SER GLY ASN VAL THR GLU LEU
SEQRES 13 E 234 TYR GLY THR ALA ILE GLY ALA ARG SER GLN GLY ALA LYS
SEQRES 14 E 234 THR TYR LEU GLU ARG THR LEU ASP THR PHE ILE LYS ILE
SEQRES 15 E 234 ASP GLY ASN PRO ASP GLU LEU ILE LYS ALA GLY VAL GLU
SEQRES 16 E 234 ALA ILE SER GLN SER LEU ARG ASP GLU SER LEU THR VAL
SEQRES 17 E 234 ASP ASN LEU SER ILE ALA ILE VAL GLY LYS ASP THR PRO
SEQRES 18 E 234 PHE THR ILE TYR ASP GLY GLU ALA VAL ALA LYS TYR ILE
SEQRES 1 F 288 MET THR SER ILE GLY THR GLY TYR ASP LEU SER ASN SER
SEQRES 2 F 288 VAL PHE SER PRO ASP GLY ARG ASN PHE GLN VAL GLU TYR
SEQRES 3 F 288 ALA VAL LYS ALA VAL GLU ASN GLY THR THR SER ILE GLY
SEQRES 4 F 288 ILE LYS CYS ASN ASP GLY VAL VAL PHE ALA VAL GLU LYS
SEQRES 5 F 288 LEU ILE THR SER LYS LEU LEU VAL PRO GLN LYS ASN VAL
SEQRES 6 F 288 LYS ILE GLN VAL VAL ASP ARG HIS ILE GLY CYS VAL TYR
SEQRES 7 F 288 SER GLY LEU ILE PRO ASP GLY ARG HIS LEU VAL ASN ARG
SEQRES 8 F 288 GLY ARG GLU GLU ALA ALA SER PHE LYS LYS LEU TYR LYS
SEQRES 9 F 288 THR PRO ILE PRO ILE PRO ALA PHE ALA ASP ARG LEU GLY
SEQRES 10 F 288 GLN TYR VAL GLN ALA HIS THR LEU TYR ASN SER VAL ARG
SEQRES 11 F 288 PRO PHE GLY VAL SER THR ILE PHE GLY GLY VAL ASP LYS
SEQRES 12 F 288 ASN GLY ALA HIS LEU TYR MET LEU GLU PRO SER GLY SER
SEQRES 13 F 288 TYR TRP GLY TYR LYS GLY ALA ALA THR GLY LYS GLY ARG
SEQRES 14 F 288 GLN SER ALA LYS ALA GLU LEU GLU LYS LEU VAL ASP HIS
SEQRES 15 F 288 HIS PRO GLU GLY LEU SER ALA ARG GLU ALA VAL LYS GLN
SEQRES 16 F 288 ALA ALA LYS ILE ILE TYR LEU ALA HIS GLU ASP ASN LYS
SEQRES 17 F 288 GLU LYS ASP PHE GLU LEU GLU ILE SER TRP CYS SER LEU
SEQRES 18 F 288 SER GLU THR ASN GLY LEU HIS LYS PHE VAL LYS GLY ASP
SEQRES 19 F 288 LEU LEU GLN GLU ALA ILE ASP PHE ALA GLN LYS GLU ILE
SEQRES 20 F 288 ASN GLY ASP ASP ASP GLU ASP GLU ASP ASP SER ASP ASN
SEQRES 21 F 288 VAL MET SER SER ASP ASP GLU ASN ALA PRO VAL ALA THR
SEQRES 22 F 288 ASN ALA ASN ALA THR THR ASP GLN GLU GLY ASP ILE HIS
SEQRES 23 F 288 LEU GLU
SEQRES 1 G 252 MET SER GLY ALA ALA ALA ALA SER ALA ALA GLY TYR ASP
SEQRES 2 G 252 ARG HIS ILE THR ILE PHE SER PRO GLU GLY ARG LEU TYR
SEQRES 3 G 252 GLN VAL GLU TYR ALA PHE LYS ALA THR ASN GLN THR ASN
SEQRES 4 G 252 ILE ASN SER LEU ALA VAL ARG GLY LYS ASP CYS THR VAL
SEQRES 5 G 252 VAL ILE SER GLN LYS LYS VAL PRO ASP LYS LEU LEU ASP
SEQRES 6 G 252 PRO THR THR VAL SER TYR ILE PHE CYS ILE SER ARG THR
SEQRES 7 G 252 ILE GLY MET VAL VAL ASN GLY PRO ILE PRO ASP ALA ARG
SEQRES 8 G 252 ASN ALA ALA LEU ARG ALA LYS ALA GLU ALA ALA GLU PHE
SEQRES 9 G 252 ARG TYR LYS TYR GLY TYR ASP MET PRO CYS ASP VAL LEU
SEQRES 10 G 252 ALA LYS ARG MET ALA ASN LEU SER GLN ILE TYR THR GLN
SEQRES 11 G 252 ARG ALA TYR MET ARG PRO LEU GLY VAL ILE LEU THR PHE
SEQRES 12 G 252 VAL SER VAL ASP GLU GLU LEU GLY PRO SER ILE TYR LYS
SEQRES 13 G 252 THR ASP PRO ALA GLY TYR TYR VAL GLY TYR LYS ALA THR
SEQRES 14 G 252 ALA THR GLY PRO LYS GLN GLN GLU ILE THR THR ASN LEU
SEQRES 15 G 252 GLU ASN HIS PHE LYS LYS SER LYS ILE ASP HIS ILE ASN
SEQRES 16 G 252 GLU GLU SER TRP GLU LYS VAL VAL GLU PHE ALA ILE THR
SEQRES 17 G 252 HIS MET ILE ASP ALA LEU GLY THR GLU PHE SER LYS ASN
SEQRES 18 G 252 ASP LEU GLU VAL GLY VAL ALA THR LYS ASP LYS PHE PHE
SEQRES 19 G 252 THR LEU SER ALA GLU ASN ILE GLU GLU ARG LEU VAL ALA
SEQRES 20 G 252 ILE ALA GLU GLN ASP
SEQRES 1 H 232 THR THR ILE VAL GLY VAL LYS PHE ASN ASN GLY VAL VAL
SEQRES 2 H 232 ILE ALA ALA ASP THR ARG SER THR GLN GLY PRO ILE VAL
SEQRES 3 H 232 ALA ASP LYS ASN CYS ALA LYS LEU HIS ARG ILE SER PRO
SEQRES 4 H 232 LYS ILE TRP CYS ALA GLY ALA GLY THR ALA ALA ASP THR
SEQRES 5 H 232 GLU ALA VAL THR GLN LEU ILE GLY SER ASN ILE GLU LEU
SEQRES 6 H 232 HIS SER LEU TYR THR SER ARG GLU PRO ARG VAL VAL SER
SEQRES 7 H 232 ALA LEU GLN MET LEU LYS GLN HIS LEU PHE LYS TYR GLN
SEQRES 8 H 232 GLY HIS ILE GLY ALA TYR LEU ILE VAL ALA GLY VAL ASP
SEQRES 9 H 232 PRO THR GLY SER HIS LEU PHE SER ILE HIS ALA HIS GLY
SEQRES 10 H 232 SER THR ASP VAL GLY TYR TYR LEU SER LEU GLY SER GLY
SEQRES 11 H 232 SER LEU ALA ALA MET ALA VAL LEU GLU SER HIS TRP LYS
SEQRES 12 H 232 GLN ASP LEU THR LYS GLU GLU ALA ILE LYS LEU ALA SER
SEQRES 13 H 232 ASP ALA ILE GLN ALA GLY ILE TRP ASN ASP LEU GLY SER
SEQRES 14 H 232 GLY SER ASN VAL ASP VAL CYS VAL MET GLU ILE GLY LYS
SEQRES 15 H 232 ASP ALA GLU TYR LEU ARG ASN TYR LEU THR PRO ASN VAL
SEQRES 16 H 232 ARG GLU GLU LYS GLN LYS SER TYR LYS PHE PRO ARG GLY
SEQRES 17 H 232 THR THR ALA VAL LEU LYS GLU SER ILE VAL ASN ILE CYS
SEQRES 18 H 232 ASP ILE GLN GLU GLU GLN VAL ASP ILE THR ALA
SEQRES 1 I 205 MET SER ASP PRO SER SER ILE ASN GLY GLY ILE VAL VAL
SEQRES 2 I 205 ALA MET THR GLY LYS ASP CYS VAL ALA ILE ALA CYS ASP
SEQRES 3 I 205 LEU ARG LEU GLY SER GLN SER LEU GLY VAL SER ASN LYS
SEQRES 4 I 205 PHE GLU LYS ILE PHE HIS TYR GLY HIS VAL PHE LEU GLY
SEQRES 5 I 205 ILE THR GLY LEU ALA THR ASP VAL THR THR LEU ASN GLU
SEQRES 6 I 205 MET PHE ARG TYR LYS THR ASN LEU TYR LYS LEU LYS GLU
SEQRES 7 I 205 GLU ARG ALA ILE GLU PRO GLU THR PHE THR GLN LEU VAL
SEQRES 8 I 205 SER SER SER LEU TYR GLU ARG ARG PHE GLY PRO TYR PHE
SEQRES 9 I 205 VAL GLY PRO VAL VAL ALA GLY ILE ASN SER LYS SER GLY
SEQRES 10 I 205 LYS PRO PHE ILE ALA GLY PHE ASP LEU ILE GLY CYS ILE
SEQRES 11 I 205 ASP GLU ALA LYS ASP PHE ILE VAL SER GLY THR ALA SER
SEQRES 12 I 205 ASP GLN LEU PHE GLY MET CYS GLU SER LEU TYR GLU PRO
SEQRES 13 I 205 ASN LEU GLU PRO GLU ASP LEU PHE GLU THR ILE SER GLN
SEQRES 14 I 205 ALA LEU LEU ASN ALA ALA ASP ARG ASP ALA LEU SER GLY
SEQRES 15 I 205 TRP GLY ALA VAL VAL TYR ILE ILE LYS LYS ASP GLU VAL
SEQRES 16 I 205 VAL LYS ARG TYR LEU LYS MET ARG GLN ASP
SEQRES 1 J 198 MET ASP ILE ILE LEU GLY ILE ARG VAL GLN ASP SER VAL
SEQRES 2 J 198 ILE LEU ALA SER SER LYS ALA VAL THR ARG GLY ILE SER
SEQRES 3 J 198 VAL LEU LYS ASP SER ASP ASP LYS THR ARG GLN LEU SER
SEQRES 4 J 198 PRO HIS THR LEU MET SER PHE ALA GLY GLU ALA GLY ASP
SEQRES 5 J 198 THR VAL GLN PHE ALA GLU TYR ILE GLN ALA ASN ILE GLN
SEQRES 6 J 198 LEU TYR SER ILE ARG GLU ASP TYR GLU LEU SER PRO GLN
SEQRES 7 J 198 ALA VAL SER SER PHE VAL ARG GLN GLU LEU ALA LYS SER
SEQRES 8 J 198 ILE ARG SER ARG ARG PRO TYR GLN VAL ASN VAL LEU ILE
SEQRES 9 J 198 GLY GLY TYR ASP LYS LYS LYS ASN LYS PRO GLU LEU TYR
SEQRES 10 J 198 GLN ILE ASP TYR LEU GLY THR LYS VAL GLU LEU PRO TYR
SEQRES 11 J 198 GLY ALA HIS GLY TYR SER GLY PHE TYR THR PHE SER LEU
SEQRES 12 J 198 LEU ASP HIS HIS TYR ARG PRO ASP MET THR THR GLU GLU
SEQRES 13 J 198 GLY LEU ASP LEU LEU LYS LEU CYS VAL GLN GLU LEU GLU
SEQRES 14 J 198 LYS ARG MET PRO MET ASP PHE LYS GLY VAL ILE VAL LYS
SEQRES 15 J 198 ILE VAL ASP LYS ASP GLY ILE ARG GLN VAL ASP ASP PHE
SEQRES 16 J 198 GLN ALA GLN
SEQRES 1 K 212 THR THR THR LEU ALA PHE ARG PHE GLN GLY GLY ILE ILE
SEQRES 2 K 212 VAL ALA VAL ASP SER ARG ALA THR ALA GLY ASN TRP VAL
SEQRES 3 K 212 ALA SER GLN THR VAL LYS LYS VAL ILE GLU ILE ASN PRO
SEQRES 4 K 212 PHE LEU LEU GLY THR MET ALA GLY GLY ALA ALA ASP CYS
SEQRES 5 K 212 GLN PHE TRP GLU THR TRP LEU GLY SER GLN CYS ARG LEU
SEQRES 6 K 212 HIS GLU LEU ARG GLU LYS GLU ARG ILE SER VAL ALA ALA
SEQRES 7 K 212 ALA SER LYS ILE LEU SER ASN LEU VAL TYR GLN TYR LYS
SEQRES 8 K 212 GLY ALA GLY LEU SER MET GLY THR MET ILE CYS GLY TYR
SEQRES 9 K 212 THR ARG LYS GLU GLY PRO THR ILE TYR TYR VAL ASP SER
SEQRES 10 K 212 ASP GLY THR ARG LEU LYS GLY ASP ILE PHE CYS VAL GLY
SEQRES 11 K 212 SER GLY GLN THR PHE ALA TYR GLY VAL LEU ASP SER ASN
SEQRES 12 K 212 TYR LYS TRP ASP LEU SER VAL GLU ASP ALA LEU TYR LEU
SEQRES 13 K 212 GLY LYS ARG SER ILE LEU ALA ALA ALA HIS ARG ASP ALA
SEQRES 14 K 212 TYR SER GLY GLY SER VAL ASN LEU TYR HIS VAL THR GLU
SEQRES 15 K 212 ASP GLY TRP ILE TYR HIS GLY ASN HIS ASP VAL GLY GLU
SEQRES 16 K 212 LEU PHE TRP LYS VAL LYS GLU GLU GLU GLY SER PHE ASN
SEQRES 17 K 212 ASN VAL ILE GLY
SEQRES 1 L 222 GLN PHE ASN PRO TYR GLY ASP ASN GLY GLY THR ILE LEU
SEQRES 2 L 222 GLY ILE ALA GLY GLU ASP PHE ALA VAL LEU ALA GLY ASP
SEQRES 3 L 222 THR ARG ASN ILE THR ASP TYR SER ILE ASN SER ARG TYR
SEQRES 4 L 222 GLU PRO LYS VAL PHE ASP CYS GLY ASP ASN ILE VAL MET
SEQRES 5 L 222 SER ALA ASN GLY PHE ALA ALA ASP GLY ASP ALA LEU VAL
SEQRES 6 L 222 LYS ARG PHE LYS ASN SER VAL LYS TRP TYR HIS PHE ASP
SEQRES 7 L 222 HIS ASN ASP LYS LYS LEU SER ILE ASN SER ALA ALA ARG
SEQRES 8 L 222 ASN ILE GLN HIS LEU LEU TYR GLY LYS ARG PHE PHE PRO
SEQRES 9 L 222 TYR TYR VAL HIS THR ILE ILE ALA GLY LEU ASP GLU ASP
SEQRES 10 L 222 GLY LYS GLY ALA VAL TYR SER PHE ASP PRO VAL GLY SER
SEQRES 11 L 222 TYR GLU ARG GLU GLN CYS ARG ALA GLY GLY ALA ALA ALA
SEQRES 12 L 222 SER LEU ILE MET PRO PHE LEU ASP ASN GLN VAL ASN PHE
SEQRES 13 L 222 LYS ASN GLN TYR GLU PRO GLY THR ASN GLY LYS VAL LYS
SEQRES 14 L 222 LYS PRO LEU LYS TYR LEU SER VAL GLU GLU VAL ILE LYS
SEQRES 15 L 222 LEU VAL ARG ASP SER PHE THR SER ALA THR GLU ARG HIS
SEQRES 16 L 222 ILE GLN VAL GLY ASP GLY LEU GLU ILE LEU ILE VAL THR
SEQRES 17 L 222 LYS ASP GLY VAL ARG LYS GLU PHE TYR GLU LEU LYS ARG
SEQRES 18 L 222 ASP
SEQRES 1 M 246 THR GLN ILE ALA ASN ALA GLY ALA SER PRO MET VAL ASN
SEQRES 2 M 246 THR GLN GLN PRO ILE VAL THR GLY THR SER VAL ILE SER
SEQRES 3 M 246 MET LYS TYR ASP ASN GLY VAL ILE ILE ALA ALA ASP ASN
SEQRES 4 M 246 LEU GLY SER TYR GLY SER LEU LEU ARG PHE ASN GLY VAL
SEQRES 5 M 246 GLU ARG LEU ILE PRO VAL GLY ASP ASN THR VAL VAL GLY
SEQRES 6 M 246 ILE SER GLY ASP ILE SER ASP MET GLN HIS ILE GLU ARG
SEQRES 7 M 246 LEU LEU LYS ASP LEU VAL THR GLU ASN ALA TYR ASP ASN
SEQRES 8 M 246 PRO LEU ALA ASP ALA GLU GLU ALA LEU GLU PRO SER TYR
SEQRES 9 M 246 ILE PHE GLU TYR LEU ALA THR VAL MET TYR GLN ARG ARG
SEQRES 10 M 246 SER LYS MET ASN PRO LEU TRP ASN ALA ILE ILE VAL ALA
SEQRES 11 M 246 GLY VAL GLN SER ASN GLY ASP GLN PHE LEU ARG TYR VAL
SEQRES 12 M 246 ASN LEU LEU GLY VAL THR TYR SER SER PRO THR LEU ALA
SEQRES 13 M 246 THR GLY PHE GLY ALA HIS MET ALA ASN PRO LEU LEU ARG
SEQRES 14 M 246 LYS VAL VAL ASP ARG GLU SER ASP ILE PRO LYS THR THR
SEQRES 15 M 246 VAL GLN VAL ALA GLU GLU ALA ILE VAL ASN ALA MET ARG
SEQRES 16 M 246 VAL LEU TYR TYR ARG ASP ALA ARG SER SER ARG ASN PHE
SEQRES 17 M 246 SER LEU ALA ILE ILE ASP LYS ASN THR GLY LEU THR PHE
SEQRES 18 M 246 LYS LYS ASN LEU GLN VAL GLU ASN MET LYS TRP ASP PHE
SEQRES 19 M 246 ALA LYS ASP ILE LYS GLY TYR GLY THR GLN LYS ILE
SEQRES 1 N 196 THR SER ILE MET ALA VAL THR PHE LYS ASP GLY VAL ILE
SEQRES 2 N 196 LEU GLY ALA ASP SER ARG THR THR THR GLY ALA TYR ILE
SEQRES 3 N 196 ALA ASN ARG VAL THR ASP LYS LEU THR ARG VAL HIS ASP
SEQRES 4 N 196 LYS ILE TRP CYS CYS ARG SER GLY SER ALA ALA ASP THR
SEQRES 5 N 196 GLN ALA ILE ALA ASP ILE VAL GLN TYR HIS LEU GLU LEU
SEQRES 6 N 196 TYR THR SER GLN TYR GLY THR PRO SER THR GLU THR ALA
SEQRES 7 N 196 ALA SER VAL PHE LYS GLU LEU CYS TYR GLU ASN LYS ASP
SEQRES 8 N 196 ASN LEU THR ALA GLY ILE ILE VAL ALA GLY TYR ASP ASP
SEQRES 9 N 196 LYS ASN LYS GLY GLU VAL TYR THR ILE PRO LEU GLY GLY
SEQRES 10 N 196 SER VAL HIS LYS LEU PRO TYR ALA ILE ALA GLY SER GLY
SEQRES 11 N 196 SER THR PHE ILE TYR GLY TYR CYS ASP LYS ASN PHE ARG
SEQRES 12 N 196 GLU ASN MET SER LYS GLU GLU THR VAL ASP PHE ILE LYS
SEQRES 13 N 196 HIS SER LEU SER GLN ALA ILE LYS TRP ASP GLY SER SER
SEQRES 14 N 196 GLY GLY VAL ILE ARG MET VAL VAL LEU THR ALA ALA GLY
SEQRES 15 N 196 VAL GLU ARG LEU ILE PHE TYR PRO ASP GLU TYR GLU GLN
SEQRES 16 N 196 LEU
SEQRES 1 O 250 MET THR ASP ARG TYR SER PHE SER LEU THR THR PHE SER
SEQRES 2 O 250 PRO SER GLY LYS LEU GLY GLN ILE ASP TYR ALA LEU THR
SEQRES 3 O 250 ALA VAL LYS GLN GLY VAL THR SER LEU GLY ILE LYS ALA
SEQRES 4 O 250 THR ASN GLY VAL VAL ILE ALA THR GLU LYS LYS SER SER
SEQRES 5 O 250 SER PRO LEU ALA MET SER GLU THR LEU SER LYS VAL SER
SEQRES 6 O 250 LEU LEU THR PRO ASP ILE GLY ALA VAL TYR SER GLY MET
SEQRES 7 O 250 GLY PRO ASP TYR ARG VAL LEU VAL ASP LYS SER ARG LYS
SEQRES 8 O 250 VAL ALA HIS THR SER TYR LYS ARG ILE TYR GLY GLU TYR
SEQRES 9 O 250 PRO PRO THR LYS LEU LEU VAL SER GLU VAL ALA LYS ILE
SEQRES 10 O 250 MET GLN GLU ALA THR GLN SER GLY GLY VAL ARG PRO PHE
SEQRES 11 O 250 GLY VAL SER LEU LEU ILE ALA GLY HIS ASP GLU PHE ASN
SEQRES 12 O 250 GLY PHE SER LEU TYR GLN VAL ASP PRO SER GLY SER TYR
SEQRES 13 O 250 PHE PRO TRP LYS ALA THR ALA ILE GLY LYS GLY SER VAL
SEQRES 14 O 250 ALA ALA LYS THR PHE LEU GLU LYS ARG TRP ASN ASP GLU
SEQRES 15 O 250 LEU GLU LEU GLU ASP ALA ILE HIS ILE ALA LEU LEU THR
SEQRES 16 O 250 LEU LYS GLU SER VAL GLU GLY GLU PHE ASN GLY ASP THR
SEQRES 17 O 250 ILE GLU LEU ALA ILE ILE GLY ASP GLU ASN PRO ASP LEU
SEQRES 18 O 250 LEU GLY TYR THR GLY ILE PRO THR ASP LYS GLY PRO ARG
SEQRES 19 O 250 PHE ARG LYS LEU THR SER GLN GLU ILE ASN ASP ARG LEU
SEQRES 20 O 250 GLU ALA LEU
SEQRES 1 P 258 MET GLY SER ARG ARG TYR ASP SER ARG THR THR ILE PHE
SEQRES 2 P 258 SER PRO GLU GLY ARG LEU TYR GLN VAL GLU TYR ALA LEU
SEQRES 3 P 258 GLU SER ILE SER HIS ALA GLY THR ALA ILE GLY ILE MET
SEQRES 4 P 258 ALA SER ASP GLY ILE VAL LEU ALA ALA GLU ARG LYS VAL
SEQRES 5 P 258 THR SER THR LEU LEU GLU GLN ASP THR SER THR GLU LYS
SEQRES 6 P 258 LEU TYR LYS LEU ASN ASP LYS ILE ALA VAL ALA VAL ALA
SEQRES 7 P 258 GLY LEU THR ALA ASP ALA GLU ILE LEU ILE ASN THR ALA
SEQRES 8 P 258 ARG ILE HIS ALA GLN ASN TYR LEU LYS THR TYR ASN GLU
SEQRES 9 P 258 ASP ILE PRO VAL GLU ILE LEU VAL ARG ARG LEU SER ASP
SEQRES 10 P 258 ILE LYS GLN GLY TYR THR GLN HIS GLY GLY LEU ARG PRO
SEQRES 11 P 258 PHE GLY VAL SER PHE ILE TYR ALA GLY TYR ASP ASP ARG
SEQRES 12 P 258 TYR GLY TYR GLN LEU TYR THR SER ASN PRO SER GLY ASN
SEQRES 13 P 258 TYR THR GLY TRP LYS ALA ILE SER VAL GLY ALA ASN THR
SEQRES 14 P 258 SER ALA ALA GLN THR LEU LEU GLN MET ASP TYR LYS ASP
SEQRES 15 P 258 ASP MET LYS VAL ASP ASP ALA ILE GLU LEU ALA LEU LYS
SEQRES 16 P 258 THR LEU SER LYS THR THR ASP SER SER ALA LEU THR TYR
SEQRES 17 P 258 ASP ARG LEU GLU PHE ALA THR ILE ARG LYS GLY ALA ASN
SEQRES 18 P 258 ASP GLY GLU VAL TYR GLN LYS ILE PHE LYS PRO GLN GLU
SEQRES 19 P 258 ILE LYS ASP ILE LEU VAL LYS THR GLY ILE THR LYS LYS
SEQRES 20 P 258 ASP GLU ASP GLU GLU ALA ASP GLU ASP MET LYS
SEQRES 1 Q 254 MET SER GLY TYR ASP ARG ALA LEU SER ILE PHE SER PRO
SEQRES 2 Q 254 ASP GLY HIS ILE PHE GLN VAL GLU TYR ALA LEU GLU ALA
SEQRES 3 Q 254 VAL LYS ARG GLY THR CYS ALA VAL GLY VAL LYS GLY LYS
SEQRES 4 Q 254 ASN CYS VAL VAL LEU GLY CYS GLU ARG ARG SER THR LEU
SEQRES 5 Q 254 LYS LEU GLN ASP THR ARG ILE THR PRO SER LYS VAL SER
SEQRES 6 Q 254 LYS ILE ASP SER HIS VAL VAL LEU SER PHE SER GLY LEU
SEQRES 7 Q 254 ASN ALA ASP SER ARG ILE LEU ILE GLU LYS ALA ARG VAL
SEQRES 8 Q 254 GLU ALA GLN SER HIS ARG LEU THR LEU GLU ASP PRO VAL
SEQRES 9 Q 254 THR VAL GLU TYR LEU THR ARG TYR VAL ALA GLY VAL GLN
SEQRES 10 Q 254 GLN ARG TYR THR GLN SER GLY GLY VAL ARG PRO PHE GLY
SEQRES 11 Q 254 VAL SER THR LEU ILE ALA GLY PHE ASP PRO ARG ASP ASP
SEQRES 12 Q 254 GLU PRO LYS LEU TYR GLN THR GLU PRO SER GLY ILE TYR
SEQRES 13 Q 254 SER SER TRP SER ALA GLN THR ILE GLY ARG ASN SER LYS
SEQRES 14 Q 254 THR VAL ARG GLU PHE LEU GLU LYS ASN TYR ASP ARG LYS
SEQRES 15 Q 254 GLU PRO PRO ALA THR VAL GLU GLU CYS VAL LYS LEU THR
SEQRES 16 Q 254 VAL ARG SER LEU LEU GLU VAL VAL GLN THR GLY ALA LYS
SEQRES 17 Q 254 ASN ILE GLU ILE THR VAL VAL LYS PRO ASP SER ASP ILE
SEQRES 18 Q 254 VAL ALA LEU SER SER GLU GLU ILE ASN GLN TYR VAL THR
SEQRES 19 Q 254 GLN ILE GLU GLN GLU LYS GLN GLU GLN GLN GLU GLN ASP
SEQRES 20 Q 254 LYS LYS LYS LYS SER ASN HIS
SEQRES 1 R 260 MET PHE LEU THR ARG SER GLU TYR ASP ARG GLY VAL SER
SEQRES 2 R 260 THR PHE SER PRO GLU GLY ARG LEU PHE GLN VAL GLU TYR
SEQRES 3 R 260 SER LEU GLU ALA ILE LYS LEU GLY SER THR ALA ILE GLY
SEQRES 4 R 260 ILE ALA THR LYS GLU GLY VAL VAL LEU GLY VAL GLU LYS
SEQRES 5 R 260 ARG ALA THR SER PRO LEU LEU GLU SER ASP SER ILE GLU
SEQRES 6 R 260 LYS ILE VAL GLU ILE ASP ARG HIS ILE GLY CYS ALA MET
SEQRES 7 R 260 SER GLY LEU THR ALA ASP ALA ARG SER MET ILE GLU HIS
SEQRES 8 R 260 ALA ARG THR ALA ALA VAL THR HIS ASN LEU TYR TYR ASP
SEQRES 9 R 260 GLU ASP ILE ASN VAL GLU SER LEU THR GLN SER VAL CYS
SEQRES 10 R 260 ASP LEU ALA LEU ARG PHE GLY GLU GLY ALA SER GLY GLU
SEQRES 11 R 260 GLU ARG LEU MET SER ARG PRO PHE GLY VAL ALA LEU LEU
SEQRES 12 R 260 ILE ALA GLY HIS ASP ALA ASP ASP GLY TYR GLN LEU PHE
SEQRES 13 R 260 HIS ALA GLU PRO SER GLY THR PHE TYR ARG TYR ASN ALA
SEQRES 14 R 260 LYS ALA ILE GLY SER GLY SER GLU GLY ALA GLN ALA GLU
SEQRES 15 R 260 LEU LEU ASN GLU TRP HIS SER SER LEU THR LEU LYS GLU
SEQRES 16 R 260 ALA GLU LEU LEU VAL LEU LYS ILE LEU LYS GLN VAL MET
SEQRES 17 R 260 GLU GLU LYS LEU ASP GLU ASN ASN ALA GLN LEU SER CYS
SEQRES 18 R 260 ILE THR LYS GLN ASP GLY PHE LYS ILE TYR ASP ASN GLU
SEQRES 19 R 260 LYS THR ALA GLU LEU ILE LYS GLU LEU LYS GLU LYS GLU
SEQRES 20 R 260 ALA ALA GLU SER PRO GLU GLU ALA ASP VAL GLU MET SER
SEQRES 1 S 234 MET PHE ARG ASN ASN TYR ASP GLY ASP THR VAL THR PHE
SEQRES 2 S 234 SER PRO THR GLY ARG LEU PHE GLN VAL GLU TYR ALA LEU
SEQRES 3 S 234 GLU ALA ILE LYS GLN GLY SER VAL THR VAL GLY LEU ARG
SEQRES 4 S 234 SER ASN THR HIS ALA VAL LEU VAL ALA LEU LYS ARG ASN
SEQRES 5 S 234 ALA ASP GLU LEU SER SER TYR GLN LYS LYS ILE ILE LYS
SEQRES 6 S 234 CYS ASP GLU HIS MET GLY LEU SER LEU ALA GLY LEU ALA
SEQRES 7 S 234 PRO ASP ALA ARG VAL LEU SER ASN TYR LEU ARG GLN GLN
SEQRES 8 S 234 CYS ASN TYR SER SER LEU VAL PHE ASN ARG LYS LEU ALA
SEQRES 9 S 234 VAL GLU ARG ALA GLY HIS LEU LEU CYS ASP LYS ALA GLN
SEQRES 10 S 234 LYS ASN THR GLN SER TYR GLY GLY ARG PRO TYR GLY VAL
SEQRES 11 S 234 GLY LEU LEU ILE ILE GLY TYR ASP LYS SER GLY ALA HIS
SEQRES 12 S 234 LEU LEU GLU PHE GLN PRO SER GLY ASN VAL THR GLU LEU
SEQRES 13 S 234 TYR GLY THR ALA ILE GLY ALA ARG SER GLN GLY ALA LYS
SEQRES 14 S 234 THR TYR LEU GLU ARG THR LEU ASP THR PHE ILE LYS ILE
SEQRES 15 S 234 ASP GLY ASN PRO ASP GLU LEU ILE LYS ALA GLY VAL GLU
SEQRES 16 S 234 ALA ILE SER GLN SER LEU ARG ASP GLU SER LEU THR VAL
SEQRES 17 S 234 ASP ASN LEU SER ILE ALA ILE VAL GLY LYS ASP THR PRO
SEQRES 18 S 234 PHE THR ILE TYR ASP GLY GLU ALA VAL ALA LYS TYR ILE
SEQRES 1 T 288 MET THR SER ILE GLY THR GLY TYR ASP LEU SER ASN SER
SEQRES 2 T 288 VAL PHE SER PRO ASP GLY ARG ASN PHE GLN VAL GLU TYR
SEQRES 3 T 288 ALA VAL LYS ALA VAL GLU ASN GLY THR THR SER ILE GLY
SEQRES 4 T 288 ILE LYS CYS ASN ASP GLY VAL VAL PHE ALA VAL GLU LYS
SEQRES 5 T 288 LEU ILE THR SER LYS LEU LEU VAL PRO GLN LYS ASN VAL
SEQRES 6 T 288 LYS ILE GLN VAL VAL ASP ARG HIS ILE GLY CYS VAL TYR
SEQRES 7 T 288 SER GLY LEU ILE PRO ASP GLY ARG HIS LEU VAL ASN ARG
SEQRES 8 T 288 GLY ARG GLU GLU ALA ALA SER PHE LYS LYS LEU TYR LYS
SEQRES 9 T 288 THR PRO ILE PRO ILE PRO ALA PHE ALA ASP ARG LEU GLY
SEQRES 10 T 288 GLN TYR VAL GLN ALA HIS THR LEU TYR ASN SER VAL ARG
SEQRES 11 T 288 PRO PHE GLY VAL SER THR ILE PHE GLY GLY VAL ASP LYS
SEQRES 12 T 288 ASN GLY ALA HIS LEU TYR MET LEU GLU PRO SER GLY SER
SEQRES 13 T 288 TYR TRP GLY TYR LYS GLY ALA ALA THR GLY LYS GLY ARG
SEQRES 14 T 288 GLN SER ALA LYS ALA GLU LEU GLU LYS LEU VAL ASP HIS
SEQRES 15 T 288 HIS PRO GLU GLY LEU SER ALA ARG GLU ALA VAL LYS GLN
SEQRES 16 T 288 ALA ALA LYS ILE ILE TYR LEU ALA HIS GLU ASP ASN LYS
SEQRES 17 T 288 GLU LYS ASP PHE GLU LEU GLU ILE SER TRP CYS SER LEU
SEQRES 18 T 288 SER GLU THR ASN GLY LEU HIS LYS PHE VAL LYS GLY ASP
SEQRES 19 T 288 LEU LEU GLN GLU ALA ILE ASP PHE ALA GLN LYS GLU ILE
SEQRES 20 T 288 ASN GLY ASP ASP ASP GLU ASP GLU ASP ASP SER ASP ASN
SEQRES 21 T 288 VAL MET SER SER ASP ASP GLU ASN ALA PRO VAL ALA THR
SEQRES 22 T 288 ASN ALA ASN ALA THR THR ASP GLN GLU GLY ASP ILE HIS
SEQRES 23 T 288 LEU GLU
SEQRES 1 U 252 MET SER GLY ALA ALA ALA ALA SER ALA ALA GLY TYR ASP
SEQRES 2 U 252 ARG HIS ILE THR ILE PHE SER PRO GLU GLY ARG LEU TYR
SEQRES 3 U 252 GLN VAL GLU TYR ALA PHE LYS ALA THR ASN GLN THR ASN
SEQRES 4 U 252 ILE ASN SER LEU ALA VAL ARG GLY LYS ASP CYS THR VAL
SEQRES 5 U 252 VAL ILE SER GLN LYS LYS VAL PRO ASP LYS LEU LEU ASP
SEQRES 6 U 252 PRO THR THR VAL SER TYR ILE PHE CYS ILE SER ARG THR
SEQRES 7 U 252 ILE GLY MET VAL VAL ASN GLY PRO ILE PRO ASP ALA ARG
SEQRES 8 U 252 ASN ALA ALA LEU ARG ALA LYS ALA GLU ALA ALA GLU PHE
SEQRES 9 U 252 ARG TYR LYS TYR GLY TYR ASP MET PRO CYS ASP VAL LEU
SEQRES 10 U 252 ALA LYS ARG MET ALA ASN LEU SER GLN ILE TYR THR GLN
SEQRES 11 U 252 ARG ALA TYR MET ARG PRO LEU GLY VAL ILE LEU THR PHE
SEQRES 12 U 252 VAL SER VAL ASP GLU GLU LEU GLY PRO SER ILE TYR LYS
SEQRES 13 U 252 THR ASP PRO ALA GLY TYR TYR VAL GLY TYR LYS ALA THR
SEQRES 14 U 252 ALA THR GLY PRO LYS GLN GLN GLU ILE THR THR ASN LEU
SEQRES 15 U 252 GLU ASN HIS PHE LYS LYS SER LYS ILE ASP HIS ILE ASN
SEQRES 16 U 252 GLU GLU SER TRP GLU LYS VAL VAL GLU PHE ALA ILE THR
SEQRES 17 U 252 HIS MET ILE ASP ALA LEU GLY THR GLU PHE SER LYS ASN
SEQRES 18 U 252 ASP LEU GLU VAL GLY VAL ALA THR LYS ASP LYS PHE PHE
SEQRES 19 U 252 THR LEU SER ALA GLU ASN ILE GLU GLU ARG LEU VAL ALA
SEQRES 20 U 252 ILE ALA GLU GLN ASP
SEQRES 1 V 232 THR THR ILE VAL GLY VAL LYS PHE ASN ASN GLY VAL VAL
SEQRES 2 V 232 ILE ALA ALA ASP THR ARG SER THR GLN GLY PRO ILE VAL
SEQRES 3 V 232 ALA ASP LYS ASN CYS ALA LYS LEU HIS ARG ILE SER PRO
SEQRES 4 V 232 LYS ILE TRP CYS ALA GLY ALA GLY THR ALA ALA ASP THR
SEQRES 5 V 232 GLU ALA VAL THR GLN LEU ILE GLY SER ASN ILE GLU LEU
SEQRES 6 V 232 HIS SER LEU TYR THR SER ARG GLU PRO ARG VAL VAL SER
SEQRES 7 V 232 ALA LEU GLN MET LEU LYS GLN HIS LEU PHE LYS TYR GLN
SEQRES 8 V 232 GLY HIS ILE GLY ALA TYR LEU ILE VAL ALA GLY VAL ASP
SEQRES 9 V 232 PRO THR GLY SER HIS LEU PHE SER ILE HIS ALA HIS GLY
SEQRES 10 V 232 SER THR ASP VAL GLY TYR TYR LEU SER LEU GLY SER GLY
SEQRES 11 V 232 SER LEU ALA ALA MET ALA VAL LEU GLU SER HIS TRP LYS
SEQRES 12 V 232 GLN ASP LEU THR LYS GLU GLU ALA ILE LYS LEU ALA SER
SEQRES 13 V 232 ASP ALA ILE GLN ALA GLY ILE TRP ASN ASP LEU GLY SER
SEQRES 14 V 232 GLY SER ASN VAL ASP VAL CYS VAL MET GLU ILE GLY LYS
SEQRES 15 V 232 ASP ALA GLU TYR LEU ARG ASN TYR LEU THR PRO ASN VAL
SEQRES 16 V 232 ARG GLU GLU LYS GLN LYS SER TYR LYS PHE PRO ARG GLY
SEQRES 17 V 232 THR THR ALA VAL LEU LYS GLU SER ILE VAL ASN ILE CYS
SEQRES 18 V 232 ASP ILE GLN GLU GLU GLN VAL ASP ILE THR ALA
SEQRES 1 W 205 MET SER ASP PRO SER SER ILE ASN GLY GLY ILE VAL VAL
SEQRES 2 W 205 ALA MET THR GLY LYS ASP CYS VAL ALA ILE ALA CYS ASP
SEQRES 3 W 205 LEU ARG LEU GLY SER GLN SER LEU GLY VAL SER ASN LYS
SEQRES 4 W 205 PHE GLU LYS ILE PHE HIS TYR GLY HIS VAL PHE LEU GLY
SEQRES 5 W 205 ILE THR GLY LEU ALA THR ASP VAL THR THR LEU ASN GLU
SEQRES 6 W 205 MET PHE ARG TYR LYS THR ASN LEU TYR LYS LEU LYS GLU
SEQRES 7 W 205 GLU ARG ALA ILE GLU PRO GLU THR PHE THR GLN LEU VAL
SEQRES 8 W 205 SER SER SER LEU TYR GLU ARG ARG PHE GLY PRO TYR PHE
SEQRES 9 W 205 VAL GLY PRO VAL VAL ALA GLY ILE ASN SER LYS SER GLY
SEQRES 10 W 205 LYS PRO PHE ILE ALA GLY PHE ASP LEU ILE GLY CYS ILE
SEQRES 11 W 205 ASP GLU ALA LYS ASP PHE ILE VAL SER GLY THR ALA SER
SEQRES 12 W 205 ASP GLN LEU PHE GLY MET CYS GLU SER LEU TYR GLU PRO
SEQRES 13 W 205 ASN LEU GLU PRO GLU ASP LEU PHE GLU THR ILE SER GLN
SEQRES 14 W 205 ALA LEU LEU ASN ALA ALA ASP ARG ASP ALA LEU SER GLY
SEQRES 15 W 205 TRP GLY ALA VAL VAL TYR ILE ILE LYS LYS ASP GLU VAL
SEQRES 16 W 205 VAL LYS ARG TYR LEU LYS MET ARG GLN ASP
SEQRES 1 X 198 MET ASP ILE ILE LEU GLY ILE ARG VAL GLN ASP SER VAL
SEQRES 2 X 198 ILE LEU ALA SER SER LYS ALA VAL THR ARG GLY ILE SER
SEQRES 3 X 198 VAL LEU LYS ASP SER ASP ASP LYS THR ARG GLN LEU SER
SEQRES 4 X 198 PRO HIS THR LEU MET SER PHE ALA GLY GLU ALA GLY ASP
SEQRES 5 X 198 THR VAL GLN PHE ALA GLU TYR ILE GLN ALA ASN ILE GLN
SEQRES 6 X 198 LEU TYR SER ILE ARG GLU ASP TYR GLU LEU SER PRO GLN
SEQRES 7 X 198 ALA VAL SER SER PHE VAL ARG GLN GLU LEU ALA LYS SER
SEQRES 8 X 198 ILE ARG SER ARG ARG PRO TYR GLN VAL ASN VAL LEU ILE
SEQRES 9 X 198 GLY GLY TYR ASP LYS LYS LYS ASN LYS PRO GLU LEU TYR
SEQRES 10 X 198 GLN ILE ASP TYR LEU GLY THR LYS VAL GLU LEU PRO TYR
SEQRES 11 X 198 GLY ALA HIS GLY TYR SER GLY PHE TYR THR PHE SER LEU
SEQRES 12 X 198 LEU ASP HIS HIS TYR ARG PRO ASP MET THR THR GLU GLU
SEQRES 13 X 198 GLY LEU ASP LEU LEU LYS LEU CYS VAL GLN GLU LEU GLU
SEQRES 14 X 198 LYS ARG MET PRO MET ASP PHE LYS GLY VAL ILE VAL LYS
SEQRES 15 X 198 ILE VAL ASP LYS ASP GLY ILE ARG GLN VAL ASP ASP PHE
SEQRES 16 X 198 GLN ALA GLN
SEQRES 1 Y 212 THR THR THR LEU ALA PHE ARG PHE GLN GLY GLY ILE ILE
SEQRES 2 Y 212 VAL ALA VAL ASP SER ARG ALA THR ALA GLY ASN TRP VAL
SEQRES 3 Y 212 ALA SER GLN THR VAL LYS LYS VAL ILE GLU ILE ASN PRO
SEQRES 4 Y 212 PHE LEU LEU GLY THR MET ALA GLY GLY ALA ALA ASP CYS
SEQRES 5 Y 212 GLN PHE TRP GLU THR TRP LEU GLY SER GLN CYS ARG LEU
SEQRES 6 Y 212 HIS GLU LEU ARG GLU LYS GLU ARG ILE SER VAL ALA ALA
SEQRES 7 Y 212 ALA SER LYS ILE LEU SER ASN LEU VAL TYR GLN TYR LYS
SEQRES 8 Y 212 GLY ALA GLY LEU SER MET GLY THR MET ILE CYS GLY TYR
SEQRES 9 Y 212 THR ARG LYS GLU GLY PRO THR ILE TYR TYR VAL ASP SER
SEQRES 10 Y 212 ASP GLY THR ARG LEU LYS GLY ASP ILE PHE CYS VAL GLY
SEQRES 11 Y 212 SER GLY GLN THR PHE ALA TYR GLY VAL LEU ASP SER ASN
SEQRES 12 Y 212 TYR LYS TRP ASP LEU SER VAL GLU ASP ALA LEU TYR LEU
SEQRES 13 Y 212 GLY LYS ARG SER ILE LEU ALA ALA ALA HIS ARG ASP ALA
SEQRES 14 Y 212 TYR SER GLY GLY SER VAL ASN LEU TYR HIS VAL THR GLU
SEQRES 15 Y 212 ASP GLY TRP ILE TYR HIS GLY ASN HIS ASP VAL GLY GLU
SEQRES 16 Y 212 LEU PHE TRP LYS VAL LYS GLU GLU GLU GLY SER PHE ASN
SEQRES 17 Y 212 ASN VAL ILE GLY
SEQRES 1 Z 222 GLN PHE ASN PRO TYR GLY ASP ASN GLY GLY THR ILE LEU
SEQRES 2 Z 222 GLY ILE ALA GLY GLU ASP PHE ALA VAL LEU ALA GLY ASP
SEQRES 3 Z 222 THR ARG ASN ILE THR ASP TYR SER ILE ASN SER ARG TYR
SEQRES 4 Z 222 GLU PRO LYS VAL PHE ASP CYS GLY ASP ASN ILE VAL MET
SEQRES 5 Z 222 SER ALA ASN GLY PHE ALA ALA ASP GLY ASP ALA LEU VAL
SEQRES 6 Z 222 LYS ARG PHE LYS ASN SER VAL LYS TRP TYR HIS PHE ASP
SEQRES 7 Z 222 HIS ASN ASP LYS LYS LEU SER ILE ASN SER ALA ALA ARG
SEQRES 8 Z 222 ASN ILE GLN HIS LEU LEU TYR GLY LYS ARG PHE PHE PRO
SEQRES 9 Z 222 TYR TYR VAL HIS THR ILE ILE ALA GLY LEU ASP GLU ASP
SEQRES 10 Z 222 GLY LYS GLY ALA VAL TYR SER PHE ASP PRO VAL GLY SER
SEQRES 11 Z 222 TYR GLU ARG GLU GLN CYS ARG ALA GLY GLY ALA ALA ALA
SEQRES 12 Z 222 SER LEU ILE MET PRO PHE LEU ASP ASN GLN VAL ASN PHE
SEQRES 13 Z 222 LYS ASN GLN TYR GLU PRO GLY THR ASN GLY LYS VAL LYS
SEQRES 14 Z 222 LYS PRO LEU LYS TYR LEU SER VAL GLU GLU VAL ILE LYS
SEQRES 15 Z 222 LEU VAL ARG ASP SER PHE THR SER ALA THR GLU ARG HIS
SEQRES 16 Z 222 ILE GLN VAL GLY ASP GLY LEU GLU ILE LEU ILE VAL THR
SEQRES 17 Z 222 LYS ASP GLY VAL ARG LYS GLU PHE TYR GLU LEU LYS ARG
SEQRES 18 Z 222 ASP
SEQRES 1 a 246 THR GLN ILE ALA ASN ALA GLY ALA SER PRO MET VAL ASN
SEQRES 2 a 246 THR GLN GLN PRO ILE VAL THR GLY THR SER VAL ILE SER
SEQRES 3 a 246 MET LYS TYR ASP ASN GLY VAL ILE ILE ALA ALA ASP ASN
SEQRES 4 a 246 LEU GLY SER TYR GLY SER LEU LEU ARG PHE ASN GLY VAL
SEQRES 5 a 246 GLU ARG LEU ILE PRO VAL GLY ASP ASN THR VAL VAL GLY
SEQRES 6 a 246 ILE SER GLY ASP ILE SER ASP MET GLN HIS ILE GLU ARG
SEQRES 7 a 246 LEU LEU LYS ASP LEU VAL THR GLU ASN ALA TYR ASP ASN
SEQRES 8 a 246 PRO LEU ALA ASP ALA GLU GLU ALA LEU GLU PRO SER TYR
SEQRES 9 a 246 ILE PHE GLU TYR LEU ALA THR VAL MET TYR GLN ARG ARG
SEQRES 10 a 246 SER LYS MET ASN PRO LEU TRP ASN ALA ILE ILE VAL ALA
SEQRES 11 a 246 GLY VAL GLN SER ASN GLY ASP GLN PHE LEU ARG TYR VAL
SEQRES 12 a 246 ASN LEU LEU GLY VAL THR TYR SER SER PRO THR LEU ALA
SEQRES 13 a 246 THR GLY PHE GLY ALA HIS MET ALA ASN PRO LEU LEU ARG
SEQRES 14 a 246 LYS VAL VAL ASP ARG GLU SER ASP ILE PRO LYS THR THR
SEQRES 15 a 246 VAL GLN VAL ALA GLU GLU ALA ILE VAL ASN ALA MET ARG
SEQRES 16 a 246 VAL LEU TYR TYR ARG ASP ALA ARG SER SER ARG ASN PHE
SEQRES 17 a 246 SER LEU ALA ILE ILE ASP LYS ASN THR GLY LEU THR PHE
SEQRES 18 a 246 LYS LYS ASN LEU GLN VAL GLU ASN MET LYS TRP ASP PHE
SEQRES 19 a 246 ALA LYS ASP ILE LYS GLY TYR GLY THR GLN LYS ILE
SEQRES 1 b 196 THR SER ILE MET ALA VAL THR PHE LYS ASP GLY VAL ILE
SEQRES 2 b 196 LEU GLY ALA ASP SER ARG THR THR THR GLY ALA TYR ILE
SEQRES 3 b 196 ALA ASN ARG VAL THR ASP LYS LEU THR ARG VAL HIS ASP
SEQRES 4 b 196 LYS ILE TRP CYS CYS ARG SER GLY SER ALA ALA ASP THR
SEQRES 5 b 196 GLN ALA ILE ALA ASP ILE VAL GLN TYR HIS LEU GLU LEU
SEQRES 6 b 196 TYR THR SER GLN TYR GLY THR PRO SER THR GLU THR ALA
SEQRES 7 b 196 ALA SER VAL PHE LYS GLU LEU CYS TYR GLU ASN LYS ASP
SEQRES 8 b 196 ASN LEU THR ALA GLY ILE ILE VAL ALA GLY TYR ASP ASP
SEQRES 9 b 196 LYS ASN LYS GLY GLU VAL TYR THR ILE PRO LEU GLY GLY
SEQRES 10 b 196 SER VAL HIS LYS LEU PRO TYR ALA ILE ALA GLY SER GLY
SEQRES 11 b 196 SER THR PHE ILE TYR GLY TYR CYS ASP LYS ASN PHE ARG
SEQRES 12 b 196 GLU ASN MET SER LYS GLU GLU THR VAL ASP PHE ILE LYS
SEQRES 13 b 196 HIS SER LEU SER GLN ALA ILE LYS TRP ASP GLY SER SER
SEQRES 14 b 196 GLY GLY VAL ILE ARG MET VAL VAL LEU THR ALA ALA GLY
SEQRES 15 b 196 VAL GLU ARG LEU ILE PHE TYR PRO ASP GLU TYR GLU GLN
SEQRES 16 b 196 LEU
HET MG G 301 1
HET MG H 301 1
HET MES H 302 12
HET 38N H 303 42
HET MG I 301 1
HET MG K 301 1
HET MES K 302 12
HET 38N K 303 42
HET MG N 201 1
HET MG V 301 1
HET MES V 302 12
HET 38N V 303 42
HET MG Y 301 1
HET MES Y 302 12
HET 38N Y 303 42
HET MG Z 301 1
HETNAM MG MAGNESIUM ION
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM 38N N-(MORPHOLIN-4-YLACETYL)-L-ALANYL-N-[(2S,4R)-1-
HETNAM 2 38N CYCLOHEXYL-5-HYDROXY-4-METHYL-3-OXOPENTAN-2-YL]-O-
HETNAM 3 38N METHYL-L-TYROSINAMIDE
FORMUL 29 MG 8(MG 2+)
FORMUL 31 MES 4(C6 H13 N O4 S)
FORMUL 32 38N 4(C31 H48 N4 O7)
FORMUL 45 HOH *812(H2 O)
HELIX 1 1 LEU A 18 GLY A 31 1 14
HELIX 2 2 MET A 57 LEU A 61 5 5
HELIX 3 3 MET A 78 SER A 96 1 19
HELIX 4 4 TYR A 97 GLY A 102 1 6
HELIX 5 5 PRO A 106 ALA A 121 1 16
HELIX 6 6 GLY A 167 TRP A 179 1 13
HELIX 7 7 GLU A 184 VAL A 200 1 17
HELIX 8 8 ASN A 218 LEU A 222 5 5
HELIX 9 9 THR A 239 ALA A 249 1 11
HELIX 10 10 GLY B 1 ASP B 6 5 6
HELIX 11 11 LEU B 18 SER B 29 1 12
HELIX 12 12 LEU B 79 ASN B 102 1 24
HELIX 13 13 PRO B 106 HIS B 124 1 19
HELIX 14 14 ASN B 167 TYR B 179 1 13
HELIX 15 15 LYS B 184 THR B 200 1 17
HELIX 16 16 THR B 206 ASP B 208 5 3
HELIX 17 17 LYS B 230 THR B 241 1 12
HELIX 18 18 ILE C 15 GLY C 28 1 14
HELIX 19 19 LEU C 76 GLU C 99 1 24
HELIX 20 20 THR C 103 TYR C 118 1 16
HELIX 21 21 ASN C 165 TYR C 177 1 13
HELIX 22 22 THR C 185 GLU C 199 1 15
HELIX 23 23 SER C 223 GLN C 239 1 17
HELIX 24 24 LEU D 13 LEU D 25 1 13
HELIX 25 25 GLU D 52 ILE D 56 5 5
HELIX 26 26 THR D 74 ASP D 76 5 3
HELIX 27 27 ALA D 77 ASP D 96 1 20
HELIX 28 28 ASN D 100 LEU D 111 1 12
HELIX 29 29 GLY D 167 TRP D 179 1 13
HELIX 30 30 THR D 184 MET D 200 1 17
HELIX 31 31 ASP D 224 ALA D 241 1 18
HELIX 32 32 LEU E 18 GLN E 30 1 13
HELIX 33 33 LEU E 76 ASN E 99 1 24
HELIX 34 34 ALA E 103 ASN E 118 1 16
HELIX 35 35 ARG E 163 ILE E 179 1 17
HELIX 36 36 ASN E 184 GLN E 198 1 15
HELIX 37 37 GLY E 226 LYS E 231 1 6
HELIX 38 38 ASN F 17 ASN F 29 1 13
HELIX 39 39 LEU F 77 LYS F 100 1 24
HELIX 40 40 PRO F 104 HIS F 119 1 16
HELIX 41 41 GLY F 164 HIS F 179 1 16
HELIX 42 42 SER F 184 HIS F 200 1 17
HELIX 43 43 GLU F 201 LYS F 204 5 4
HELIX 44 44 LYS F 228 ASN F 244 1 17
HELIX 45 45 GLY G 2 HIS G 6 5 5
HELIX 46 46 LEU G 16 THR G 26 1 11
HELIX 47 47 ASP G 56 VAL G 60 5 5
HELIX 48 48 PRO G 77 GLY G 100 1 24
HELIX 49 49 PRO G 104 ARG G 122 1 19
HELIX 50 50 LYS G 165 LYS G 181 1 17
HELIX 51 51 SER G 189 GLY G 206 1 18
HELIX 52 52 SER G 228 GLU G 241 1 14
HELIX 53 53 THR H 48 SER H 71 1 24
HELIX 54 54 ARG H 75 TYR H 90 1 16
HELIX 55 55 GLY H 130 TRP H 142 1 13
HELIX 56 56 THR H 147 ASP H 166 1 20
HELIX 57 57 ASP I 2 ILE I 6 5 5
HELIX 58 58 LEU I 55 GLU I 78 1 24
HELIX 59 59 GLU I 82 GLU I 96 1 15
HELIX 60 60 ALA I 141 TYR I 153 1 13
HELIX 61 61 GLU I 158 ASP I 175 1 18
HELIX 62 62 GLY J 51 ASP J 72 1 22
HELIX 63 63 SER J 76 ILE J 92 1 17
HELIX 64 64 SER J 136 TYR J 148 1 13
HELIX 65 65 THR J 153 MET J 172 1 20
HELIX 66 66 GLY K 48 LYS K 71 1 24
HELIX 67 67 SER K 75 TYR K 90 1 16
HELIX 68 68 GLY K 132 TYR K 144 1 13
HELIX 69 69 SER K 149 ASP K 168 1 20
HELIX 70 70 VAL K 193 GLY K 205 1 13
HELIX 71 71 PHE L 57 HIS L 79 1 23
HELIX 72 72 SER L 85 GLY L 99 1 15
HELIX 73 73 ALA L 142 VAL L 154 1 13
HELIX 74 74 SER L 176 HIS L 195 1 20
HELIX 75 75 ILE M 57 TYR M 76 1 20
HELIX 76 76 GLU M 88 LYS M 106 1 19
HELIX 77 77 GLY M 145 VAL M 159 1 15
HELIX 78 78 ARG M 161 ILE M 165 5 5
HELIX 79 79 THR M 169 ASP M 188 1 20
HELIX 80 80 TRP M 219 ILE M 225 5 7
HELIX 81 81 SER N 48 GLY N 71 1 24
HELIX 82 82 SER N 74 ASN N 89 1 16
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 SER O 58 LEU O 61 5 4
HELIX 89 89 MET O 78 SER O 96 1 19
HELIX 90 90 TYR O 97 GLY O 102 1 6
HELIX 91 91 PRO O 106 ALA O 121 1 16
HELIX 92 92 GLY O 167 TRP O 179 1 13
HELIX 93 93 GLU O 184 VAL O 200 1 17
HELIX 94 94 ASN O 218 LEU O 222 5 5
HELIX 95 95 THR O 239 ALA O 249 1 11
HELIX 96 96 GLY P 1 ASP P 6 5 6
HELIX 97 97 LEU P 18 SER P 29 1 12
HELIX 98 98 LEU P 79 ASN P 102 1 24
HELIX 99 99 PRO P 106 HIS P 124 1 19
HELIX 100 100 ASN P 167 TYR P 179 1 13
HELIX 101 101 LYS P 184 THR P 200 1 17
HELIX 102 102 THR P 206 ASP P 208 5 3
HELIX 103 103 LYS P 230 THR P 241 1 12
HELIX 104 104 ILE Q 15 GLY Q 28 1 14
HELIX 105 105 LEU Q 76 GLU Q 99 1 24
HELIX 106 106 THR Q 103 TYR Q 118 1 16
HELIX 107 107 ASN Q 165 TYR Q 177 1 13
HELIX 108 108 THR Q 185 GLU Q 199 1 15
HELIX 109 109 SER Q 223 GLN Q 239 1 17
HELIX 110 110 LEU R 13 LEU R 25 1 13
HELIX 111 111 GLU R 52 ILE R 56 5 5
HELIX 112 112 THR R 74 ASP R 76 5 3
HELIX 113 113 ALA R 77 ASP R 96 1 20
HELIX 114 114 ASN R 100 LEU R 111 1 12
HELIX 115 115 GLY R 167 TRP R 179 1 13
HELIX 116 116 THR R 184 MET R 200 1 17
HELIX 117 117 ASP R 224 ALA R 241 1 18
HELIX 118 118 LEU S 18 GLN S 30 1 13
HELIX 119 119 LEU S 76 ASN S 99 1 24
HELIX 120 120 ALA S 103 ASN S 118 1 16
HELIX 121 121 ARG S 163 ILE S 179 1 17
HELIX 122 122 ASN S 184 GLN S 198 1 15
HELIX 123 123 GLY S 226 LYS S 231 1 6
HELIX 124 124 ASN T 17 ASN T 29 1 13
HELIX 125 125 LEU T 77 LYS T 100 1 24
HELIX 126 126 PRO T 104 HIS T 119 1 16
HELIX 127 127 GLY T 164 HIS T 179 1 16
HELIX 128 128 SER T 184 HIS T 200 1 17
HELIX 129 129 GLU T 201 LYS T 204 5 4
HELIX 130 130 LYS T 228 ASN T 244 1 17
HELIX 131 131 GLY U 2 HIS U 6 5 5
HELIX 132 132 LEU U 16 THR U 26 1 11
HELIX 133 133 ASP U 56 VAL U 60 5 5
HELIX 134 134 PRO U 77 GLY U 100 1 24
HELIX 135 135 PRO U 104 ARG U 122 1 19
HELIX 136 136 LYS U 165 LYS U 181 1 17
HELIX 137 137 SER U 189 GLY U 206 1 18
HELIX 138 138 SER U 228 GLU U 241 1 14
HELIX 139 139 THR V 48 SER V 71 1 24
HELIX 140 140 ARG V 75 TYR V 90 1 16
HELIX 141 141 GLY V 130 TRP V 142 1 13
HELIX 142 142 THR V 147 ASP V 166 1 20
HELIX 143 143 ASP W 2 ILE W 6 5 5
HELIX 144 144 LEU W 55 GLU W 78 1 24
HELIX 145 145 GLU W 82 GLU W 96 1 15
HELIX 146 146 ALA W 141 TYR W 153 1 13
HELIX 147 147 GLU W 158 ASP W 175 1 18
HELIX 148 148 GLY X 51 ASP X 72 1 22
HELIX 149 149 SER X 76 ILE X 92 1 17
HELIX 150 150 SER X 136 TYR X 148 1 13
HELIX 151 151 THR X 153 MET X 172 1 20
HELIX 152 152 GLY Y 48 LYS Y 71 1 24
HELIX 153 153 SER Y 75 TYR Y 90 1 16
HELIX 154 154 GLY Y 132 TYR Y 144 1 13
HELIX 155 155 SER Y 149 ASP Y 168 1 20
HELIX 156 156 VAL Y 193 GLY Y 205 1 13
HELIX 157 157 PHE Z 57 HIS Z 79 1 23
HELIX 158 158 SER Z 85 GLY Z 99 1 15
HELIX 159 159 ALA Z 142 VAL Z 154 1 13
HELIX 160 160 SER Z 176 HIS Z 195 1 20
HELIX 161 161 ILE a 57 TYR a 76 1 20
HELIX 162 162 GLU a 88 LYS a 106 1 19
HELIX 163 163 GLY a 145 VAL a 159 1 15
HELIX 164 164 ARG a 161 ILE a 165 5 5
HELIX 165 165 THR a 169 ASP a 188 1 20
HELIX 166 166 TRP a 219 ILE a 225 5 7
HELIX 167 167 SER b 48 GLY b 71 1 24
HELIX 168 168 SER b 74 ASN b 89 1 16
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 ALA A 46 N LEU A 35
SHEET 4 A 5 ILE A 209 ILE A 214 -1 O GLU A 210 N THR A 47
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 ALA A 137 N GLY A 72
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 175 O LEU H 187
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 TYR B 225 N ARG B 216
SHEET 1 E 5 LEU B 65 ASN B 69 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 TRP B 159 -1 O TRP B 159 N LEU B 147
SHEET 1 F 5 ALA C 159 ILE C 162 0
SHEET 2 F 5 ALA C 31 LYS C 35 -1 N GLY C 33 O GLN C 160
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 VAL C 213 N VAL C 40
SHEET 5 F 5 ASP C 218 ALA C 221 -1 O ASP C 218 N LYS C 214
SHEET 1 G 5 SER C 63 ASP C 66 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 GLY C 135 -1 O ALA C 134 N VAL C 70
SHEET 4 G 5 LYS C 144 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 LYS D 221 N CYS D 213
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 GLN D 146 N GLY D 138
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 SER E 211 N ALA E 47
SHEET 5 J 5 THR E 219 TYR E 224 -1 O THR E 219 N GLY E 216
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 GLY E 130 N ALA E 74
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 CYS F 38 -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 VAL F 227 -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 THR G 42 GLN G 47 -1 O ILE G 45 N LEU G 34
SHEET 4 N 5 LEU G 214 THR G 220 -1 O GLY G 217 N VAL G 44
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 THR G 133 N VAL G 73
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 PHE H 111 N VAL H 100
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 VAL H 218 0
SHEET 2 R 6 GLU I 193 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 GLY I 16 -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 LEU I 33 N SER I 30
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 VAL I 107 N GLY I 51
SHEET 4 T 5 PRO I 118 PHE I 123 -1 O PHE I 119 N GLY I 110
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 ILE J 14 N ILE J 7
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 ARG J 190 N ILE J 183
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 ILE J 119 -1 O ILE J 119 N VAL J 102
SHEET 5 W 5 LYS J 125 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 GLY K 11 N PHE K 8
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 GLY K 184 N THR K 181
SHEET 1 Y 2 ALA K 20 ALA K 22 0
SHEET 2 Y 2 TRP K 25 SER K 28 -1 O TRP K 25 N ALA K 22
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 VAL K 115 N THR K 99
SHEET 5 Z 5 ARG K 121 LYS K 123 -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 GLY L 14 O ARG L 137
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 ARG L 213 N ILE L 206
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 ILE L 50 GLY L 56 -1 O MET L 52 N PHE L 44
SHEET 3 AC 5 VAL L 107 LEU L 114 -1 O ILE L 110 N SER L 53
SHEET 4 AC 5 GLY L 120 PHE L 125 -1 O ALA L 121 N GLY L 113
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 PRO M 44 -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 VAL M 11 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 ILE M 200 N VAL M 20
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 PHE N 8 -1 N ILE N 3 O ALA N 127
SHEET 3 AG 5 GLY N 11 ALA N 16 -1 O GLY N 15 N MET N 4
SHEET 4 AG 5 ILE N 173 THR N 179 -1 O ARG N 174 N ALA N 16
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 ASP N 103 -1 O ALA N 100 N TRP N 42
SHEET 4 AI 5 LYS N 107 ILE N 113 -1 O TYR N 111 N VAL N 99
SHEET 5 AI 5 HIS N 120 LEU N 122 -1 O LEU N 122 N VAL N 110
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 ALA O 46 N LEU O 35
SHEET 4 AJ 5 ILE O 209 ILE O 214 -1 O GLU O 210 N THR O 47
SHEET 5 AJ 5 PHE O 235 LYS O 237 -1 O ARG O 236 N ILE O 213
SHEET 1 AK 6 ALA O 56 MET O 57 0
SHEET 2 AK 6 TYR U 154 TYR U 157 -1 O GLY U 156 N MET O 57
SHEET 3 AK 6 GLY U 142 THR U 148 -1 N ILE U 145 O TYR U 157
SHEET 4 AK 6 ILE U 131 ASP U 138 -1 N PHE U 134 O TYR U 146
SHEET 5 AK 6 GLY U 71 ASN U 75 -1 N VAL U 73 O THR U 133
SHEET 6 AK 6 ILE U 63 CYS U 65 -1 N PHE U 64 O MET U 72
SHEET 1 AL 5 SER O 65 THR O 68 0
SHEET 2 AL 5 ILE O 71 GLY O 77 -1 O ILE O 71 N LEU O 67
SHEET 3 AL 5 VAL O 132 ASP O 140 -1 O ALA O 137 N GLY O 72
SHEET 4 AL 5 GLY O 144 VAL O 150 -1 O TYR O 148 N ILE O 136
SHEET 5 AL 5 TYR O 156 PRO O 158 -1 O PHE O 157 N GLN O 149
SHEET 1 AM 6 TYR O 224 THR O 225 0
SHEET 2 AM 6 ALA V 184 LEU V 191 1 O TYR V 186 N THR O 225
SHEET 3 AM 6 VAL V 173 GLU V 179 -1 N VAL V 175 O LEU V 187
SHEET 4 AM 6 GLY V 11 ALA V 16 -1 N VAL V 12 O MET V 178
SHEET 5 AM 6 ILE V 3 PHE V 8 -1 N VAL V 6 O VAL V 13
SHEET 6 AM 6 TYR V 124 LEU V 127 -1 O LEU V 125 N GLY V 5
SHEET 1 AN 5 ALA P 161 VAL P 164 0
SHEET 2 AN 5 ALA P 34 ALA P 39 -1 N GLY P 36 O ILE P 162
SHEET 3 AN 5 GLY P 42 GLU P 48 -1 O ALA P 46 N ILE P 35
SHEET 4 AN 5 LEU P 210 ARG P 216 -1 O ALA P 213 N LEU P 45
SHEET 5 AN 5 TYR P 225 ILE P 228 -1 O TYR P 225 N ARG P 216
SHEET 1 AO 5 LEU P 65 ASN P 69 0
SHEET 2 AO 5 ILE P 72 GLY P 78 -1 O VAL P 74 N TYR P 66
SHEET 3 AO 5 VAL P 132 ASP P 140 -1 O ALA P 137 N ALA P 73
SHEET 4 AO 5 GLY P 144 SER P 150 -1 O TYR P 148 N TYR P 136
SHEET 5 AO 5 TYR P 156 TRP P 159 -1 O TRP P 159 N LEU P 147
SHEET 1 AP 5 ALA Q 159 ILE Q 162 0
SHEET 2 AP 5 ALA Q 31 LYS Q 35 -1 N GLY Q 33 O GLN Q 160
SHEET 3 AP 5 VAL Q 40 GLU Q 45 -1 O GLY Q 43 N VAL Q 32
SHEET 4 AP 5 ILE Q 208 LYS Q 214 -1 O VAL Q 213 N VAL Q 40
SHEET 5 AP 5 ASP Q 218 ALA Q 221 -1 O ASP Q 218 N LYS Q 214
SHEET 1 AQ 5 SER Q 63 ASP Q 66 0
SHEET 2 AQ 5 VAL Q 69 GLY Q 75 -1 O LEU Q 71 N SER Q 63
SHEET 3 AQ 5 VAL Q 129 GLY Q 135 -1 O ALA Q 134 N VAL Q 70
SHEET 4 AQ 5 LYS Q 144 THR Q 148 -1 O TYR Q 146 N ILE Q 133
SHEET 5 AQ 5 TYR Q 154 SER Q 156 -1 O SER Q 155 N GLN Q 147
SHEET 1 AR 5 ALA R 161 ILE R 164 0
SHEET 2 AR 5 ALA R 29 THR R 34 -1 N ALA R 29 O ILE R 164
SHEET 3 AR 5 GLY R 37 GLU R 43 -1 O GLY R 41 N ILE R 30
SHEET 4 AR 5 ALA R 209 THR R 215 -1 O SER R 212 N LEU R 40
SHEET 5 AR 5 GLY R 219 ILE R 222 -1 O LYS R 221 N CYS R 213
SHEET 1 AS 5 ILE R 59 ASP R 63 0
SHEET 2 AS 5 ILE R 66 GLY R 72 -1 O CYS R 68 N VAL R 60
SHEET 3 AS 5 VAL R 132 ASP R 140 -1 O ALA R 137 N GLY R 67
SHEET 4 AS 5 GLY R 144 ALA R 150 -1 O PHE R 148 N ILE R 136
SHEET 5 AS 5 PHE R 156 ARG R 158 -1 O TYR R 157 N HIS R 149
SHEET 1 AT 5 GLY S 157 ILE S 160 0
SHEET 2 AT 5 THR S 34 ARG S 38 -1 N GLY S 36 O THR S 158
SHEET 3 AT 5 HIS S 42 LEU S 48 -1 O VAL S 46 N VAL S 35
SHEET 4 AT 5 LEU S 210 GLY S 216 -1 O SER S 211 N ALA S 47
SHEET 5 AT 5 THR S 219 TYR S 224 -1 O THR S 219 N GLY S 216
SHEET 1 AU 5 ILE S 62 ASP S 66 0
SHEET 2 AU 5 MET S 69 GLY S 75 -1 O LEU S 71 N ILE S 63
SHEET 3 AU 5 VAL S 129 ASP S 137 -1 O GLY S 130 N ALA S 74
SHEET 4 AU 5 GLY S 140 PHE S 146 -1 O PHE S 146 N LEU S 131
SHEET 5 AU 5 VAL S 152 LEU S 155 -1 O THR S 153 N GLU S 145
SHEET 1 AV 5 GLY T 158 THR T 161 0
SHEET 2 AV 5 SER T 33 CYS T 38 -1 N GLY T 35 O ALA T 159
SHEET 3 AV 5 GLY T 41 LEU T 49 -1 O ALA T 45 N ILE T 34
SHEET 4 AV 5 PHE T 208 SER T 216 -1 O SER T 213 N PHE T 44
SHEET 5 AV 5 LYS T 225 VAL T 227 -1 O LYS T 225 N TRP T 214
SHEET 1 AW 5 GLN T 64 VAL T 66 0
SHEET 2 AW 5 ILE T 70 GLY T 76 -1 O CYS T 72 N GLN T 64
SHEET 3 AW 5 VAL T 130 ASP T 138 -1 O ILE T 133 N VAL T 73
SHEET 4 AW 5 GLY T 141 LEU T 147 -1 O TYR T 145 N PHE T 134
SHEET 5 AW 5 TYR T 153 GLY T 155 -1 O TRP T 154 N MET T 146
SHEET 1 AX 5 ALA U 159 THR U 162 0
SHEET 2 AX 5 SER U 33 ARG U 37 -1 N SER U 33 O THR U 162
SHEET 3 AX 5 THR U 42 GLN U 47 -1 O ILE U 45 N LEU U 34
SHEET 4 AX 5 LEU U 214 THR U 220 -1 O GLY U 217 N VAL U 44
SHEET 5 AX 5 LYS U 223 THR U 226 -1 O PHE U 225 N VAL U 218
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 PHE V 111 N VAL V 100
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 VAL V 218 0
SHEET 2 BA 6 GLU W 193 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 GLY W 16 -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 LEU W 33 N SER W 30
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 VAL W 107 N GLY W 51
SHEET 4 BC 5 PRO W 118 PHE W 123 -1 O PHE W 119 N GLY W 110
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 ILE X 14 N ILE X 7
SHEET 4 BD 5 VAL X 179 ASP X 185 -1 O ILE X 180 N SER X 17
SHEET 5 BD 5 GLY X 188 VAL X 192 -1 O ARG X 190 N ILE X 183
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 ILE X 119 -1 O ILE X 119 N VAL X 102
SHEET 5 BF 5 LYS X 125 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 GLY Y 11 N PHE Y 8
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 GLY Y 184 N THR Y 181
SHEET 1 BH 2 ALA Y 20 ALA Y 22 0
SHEET 2 BH 2 TRP Y 25 SER Y 28 -1 O TRP Y 25 N ALA Y 22
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 VAL Y 115 N THR Y 99
SHEET 5 BI 5 ARG Y 121 LYS Y 123 -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 GLY Z 14 O ARG Z 137
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 ARG Z 213 N ILE Z 206
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 ILE Z 50 GLY Z 56 -1 O MET Z 52 N PHE Z 44
SHEET 3 BL 5 VAL Z 107 LEU Z 114 -1 O ILE Z 110 N SER Z 53
SHEET 4 BL 5 GLY Z 120 PHE Z 125 -1 O ALA Z 121 N GLY Z 113
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 PRO a 44 -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 VAL a 11 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 ILE a 200 N VAL a 20
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 PHE b 8 -1 N ILE b 3 O ALA b 127
SHEET 3 BP 5 GLY b 11 ALA b 16 -1 O GLY b 15 N MET b 4
SHEET 4 BP 5 ILE b 173 THR b 179 -1 O ARG b 174 N ALA b 16
SHEET 5 BP 5 GLY b 182 PHE b 188 -1 O GLU b 184 N VAL b 177
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 ASP b 103 -1 O ALA b 100 N TRP b 42
SHEET 4 BR 5 LYS b 107 ILE b 113 -1 O TYR b 111 N VAL b 99
SHEET 5 BR 5 HIS b 120 LEU b 122 -1 O LEU b 122 N VAL b 110
LINK OG1 THR G 8 MG MG G 301 1555 1555 2.63
LINK O TYR G 119 MG MG G 301 1555 1555 2.52
LINK O ARG G 122 MG MG G 301 1555 1555 2.45
LINK O MET G 125 MG MG G 301 1555 1555 2.31
LINK OE1 GLN H 91 MG MG H 301 1555 1555 2.71
LINK MG MG H 301 O HOH N 311 1555 1555 2.83
LINK O ALA I 174 MG MG I 301 1555 1555 2.45
LINK O ASP I 177 MG MG I 301 1555 1555 2.42
LINK O SER I 180 MG MG I 301 1555 1555 2.44
LINK O ASP I 204 MG MG Y 301 1555 1555 2.53
LINK O ALA K 165 MG MG K 301 1555 1555 2.52
LINK O ASP K 168 MG MG K 301 1555 1555 2.38
LINK O SER K 171 MG MG K 301 1555 1555 2.44
LINK MG MG K 301 O ASP W 204 1555 1555 2.45
LINK OXT ASP L 222 MG MG V 301 1555 1555 2.24
LINK O ILE N 163 MG MG N 201 1555 1555 2.54
LINK O ASP N 166 MG MG N 201 1555 1555 2.89
LINK O SER N 169 MG MG N 201 1555 1555 2.66
LINK O ILE V 163 MG MG V 301 1555 1555 2.31
LINK O ASP V 166 MG MG V 301 1555 1555 2.17
LINK O SER V 169 MG MG V 301 1555 1555 2.20
LINK O ALA Y 165 MG MG Y 301 1555 1555 2.45
LINK O ASP Y 168 MG MG Y 301 1555 1555 2.30
LINK O SER Y 171 MG MG Y 301 1555 1555 2.34
LINK MG MG Y 301 O HOH Y 408 1555 1555 2.42
LINK O THR Z 192 MG MG Z 301 1555 1555 2.57
LINK O HIS Z 195 MG MG Z 301 1555 1555 2.77
LINK O VAL Z 198 MG MG Z 301 1555 1555 2.62
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 4 GLN H 91 ASN N 92 HOH N 310 HOH N 311
SITE 1 AC3 4 GLY H 47 SER H 129 38N H 303 TYR Z 33
SITE 1 AC4 17 THR H 1 ARG H 19 SER H 20 THR H 21
SITE 2 AC4 17 GLN H 22 CYS H 31 ALA H 46 GLY H 47
SITE 3 AC4 17 THR H 48 ALA H 49 THR H 52 GLY H 168
SITE 4 AC4 17 MES H 302 HOH H 432 ASP I 124 HOH I 403
SITE 5 AC4 17 HOH Z 403
SITE 1 AC5 3 ALA I 174 ASP I 177 SER I 180
SITE 1 AC6 5 ARG K 19 ALA K 165 ASP K 168 SER K 171
SITE 2 AC6 5 ASP W 204
SITE 1 AC7 7 THR K 1 GLY K 47 SER K 96 MET K 97
SITE 2 AC7 7 GLY K 130 SER K 131 38N K 303
SITE 1 AC8 12 THR K 1 ARG K 19 ALA K 20 THR K 21
SITE 2 AC8 12 VAL K 31 GLY K 47 GLY K 48 ALA K 49
SITE 3 AC8 12 TYR K 170 MES K 302 ASP L 126 HOH L 302
SITE 1 AC9 5 ARG N 19 ILE N 163 ASP N 166 SER N 169
SITE 2 AC9 5 LEU a 34
SITE 1 BC1 4 ASP L 222 ILE V 163 ASP V 166 SER V 169
SITE 1 BC2 4 TYR L 33 GLY V 47 SER V 129 38N V 303
SITE 1 BC3 15 THR V 1 ARG V 19 SER V 20 THR V 21
SITE 2 BC3 15 GLN V 22 CYS V 31 ALA V 46 GLY V 47
SITE 3 BC3 15 THR V 48 ALA V 49 THR V 52 GLY V 168
SITE 4 BC3 15 MES V 302 HOH V 403 ASP W 124
SITE 1 BC4 6 ASP I 204 ARG Y 19 ALA Y 165 ASP Y 168
SITE 2 BC4 6 SER Y 171 HOH Y 408
SITE 1 BC5 7 THR Y 1 GLY Y 47 SER Y 96 MET Y 97
SITE 2 BC5 7 GLY Y 130 SER Y 131 38N Y 303
SITE 1 BC6 13 THR Y 1 ARG Y 19 ALA Y 20 THR Y 21
SITE 2 BC6 13 VAL Y 31 GLY Y 47 GLY Y 48 ALA Y 49
SITE 3 BC6 13 TYR Y 170 MES Y 302 HOH Y 434 ASP Z 126
SITE 4 BC6 13 HOH Z 410
SITE 1 BC7 3 THR Z 192 HIS Z 195 VAL Z 198
CRYST1 136.650 299.590 144.820 90.00 112.85 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.007318 0.000000 0.003084 0.00000
SCALE2 0.000000 0.003338 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007493 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 -0.999292 -0.005755 0.037173 67.31113 1
MTRIX2 2 -0.000743 -0.985013 -0.172479 -288.79517 1
MTRIX3 2 0.037609 -0.172384 0.984312 -26.03921 1
(ATOM LINES ARE NOT SHOWN.)
END
