HEADER HYDROLASE/HYDROLASE INHIBITOR 29-JUL-14 4QZX
TITLE YCP BETA5-C63F MUTANT IN COMPLEX WITH THE EPOXYKETONE INHIBITOR ONX
TITLE 2 0914
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-2;
COMPND 3 CHAIN: A, O;
COMPND 4 EC: 3.4.25.1;
COMPND 5 MUTATION: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-3;
COMPND 8 CHAIN: B, P;
COMPND 9 EC: 3.4.25.1;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-4;
COMPND 12 CHAIN: C, Q;
COMPND 13 EC: 3.4.25.1;
COMPND 14 MOL_ID: 4;
COMPND 15 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-5;
COMPND 16 CHAIN: D, R;
COMPND 17 EC: 3.4.25.1;
COMPND 18 MOL_ID: 5;
COMPND 19 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-6;
COMPND 20 CHAIN: E, S;
COMPND 21 EC: 3.4.25.1;
COMPND 22 MOL_ID: 6;
COMPND 23 MOLECULE: PROBABLE PROTEASOME SUBUNIT ALPHA TYPE-7;
COMPND 24 CHAIN: F, T;
COMPND 25 EC: 3.4.25.1;
COMPND 26 MOL_ID: 7;
COMPND 27 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-1;
COMPND 28 CHAIN: G, U;
COMPND 29 EC: 3.4.25.1;
COMPND 30 MOL_ID: 8;
COMPND 31 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-2;
COMPND 32 CHAIN: H, V;
COMPND 33 EC: 3.4.25.1;
COMPND 34 MOL_ID: 9;
COMPND 35 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-3;
COMPND 36 CHAIN: I, W;
COMPND 37 EC: 3.4.25.1;
COMPND 38 MOL_ID: 10;
COMPND 39 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-4;
COMPND 40 CHAIN: J, X;
COMPND 41 EC: 3.4.25.1;
COMPND 42 MOL_ID: 11;
COMPND 43 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-5;
COMPND 44 CHAIN: K, Y;
COMPND 45 EC: 3.4.25.1;
COMPND 46 ENGINEERED: YES;
COMPND 47 MOL_ID: 12;
COMPND 48 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-6;
COMPND 49 CHAIN: L, Z;
COMPND 50 EC: 3.4.25.1;
COMPND 51 MOL_ID: 13;
COMPND 52 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-7;
COMPND 53 CHAIN: M, a;
COMPND 54 EC: 3.4.25.1;
COMPND 55 MOL_ID: 14;
COMPND 56 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-1;
COMPND 57 CHAIN: N, b;
COMPND 58 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 GENE: PRE2, DOA3, PRG1, YPR103W, P8283.10;
SOURCE 57 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 58 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 59 EXPRESSION_SYSTEM_STRAIN: 4932;
SOURCE 60 MOL_ID: 12;
SOURCE 61 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 62 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 63 ORGANISM_TAXID: 559292;
SOURCE 64 STRAIN: ATCC 204508 / S288C;
SOURCE 65 MOL_ID: 13;
SOURCE 66 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 67 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 68 ORGANISM_TAXID: 559292;
SOURCE 69 STRAIN: ATCC 204508 / S288C;
SOURCE 70 MOL_ID: 14;
SOURCE 71 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 72 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 73 ORGANISM_TAXID: 559292;
SOURCE 74 STRAIN: ATCC 204508 / S288C
KEYWDS CANCER, PROTEASOME, BORTEZOMIB, DRUG RESISTANCE, BINDING ANALYSIS,
KEYWDS 2 HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR E.M.HUBER,W.HEINEMEYER,M.GROLL
REVDAT 3 20-SEP-23 4QZX 1 REMARK SEQADV LINK
REVDAT 2 18-FEB-15 4QZX 1 JRNL
REVDAT 1 04-FEB-15 4QZX 0
JRNL AUTH E.M.HUBER,W.HEINEMEYER,M.GROLL
JRNL TITL BORTEZOMIB-RESISTANT MUTANT PROTEASOMES: STRUCTURAL AND
JRNL TITL 2 BIOCHEMICAL EVALUATION WITH CARFILZOMIB AND ONX 0914.
JRNL REF STRUCTURE V. 23 407 2015
JRNL REFN ISSN 0969-2126
JRNL PMID 25599643
JRNL DOI 10.1016/J.STR.2014.11.019
REMARK 2
REMARK 2 RESOLUTION. 2.60 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) : 2.60
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 : 307698
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) : 0.198
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 16195
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 22322
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.51
REMARK 3 BIN R VALUE (WORKING SET) : 0.3210
REMARK 3 BIN FREE R VALUE SET COUNT : 1175
REMARK 3 BIN FREE R VALUE : 0.3460
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 49279
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 310
REMARK 3 SOLVENT ATOMS : 455
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 67.39
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.78000
REMARK 3 B22 (A**2) : -6.19000
REMARK 3 B33 (A**2) : 3.07000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.88000
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): 0.239
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.209
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 23.332
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 50511 ; 0.005 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 48263 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 68351 ; 0.893 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES):111143 ; 0.807 ; 3.003
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 6303 ; 5.070 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 2248 ;34.166 ;24.404
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 8728 ;14.084 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 284 ;14.128 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 7685 ; 0.051 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 57199 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 11329 ; 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): 25302 ; 2.614 ; 5.593
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 25301 ; 2.614 ; 5.593
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 31575 ; 3.505 ; 8.372
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 31576 ; 3.505 ; 8.372
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 25209 ; 2.409 ; 5.977
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 25209 ; 2.409 ; 5.977
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 36777 ; 3.012 ; 8.806
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 54011 ; 3.918 ;43.524
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 53960 ; 3.901 ;43.517
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 98774 ; 1.171 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 276 ;27.560 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 98039 ;19.496 ; 5.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 28
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 250
REMARK 3 RESIDUE RANGE : A 301 A 323
REMARK 3 ORIGIN FOR THE GROUP (A): 67.4220 -91.9141 45.9617
REMARK 3 T TENSOR
REMARK 3 T11: 0.1346 T22: 0.1025
REMARK 3 T33: 0.1372 T12: -0.0045
REMARK 3 T13: 0.0049 T23: -0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 0.0154 L22: 0.0028
REMARK 3 L33: 0.0004 L12: -0.0010
REMARK 3 L13: -0.0019 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: -0.0055 S12: 0.0215 S13: -0.0068
REMARK 3 S21: 0.0070 S22: 0.0052 S23: -0.0152
REMARK 3 S31: -0.0029 S32: -0.0032 S33: 0.0004
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 244
REMARK 3 RESIDUE RANGE : B 301 B 321
REMARK 3 ORIGIN FOR THE GROUP (A): 60.3436 -87.7772 16.2713
REMARK 3 T TENSOR
REMARK 3 T11: 0.1258 T22: 0.1073
REMARK 3 T33: 0.1300 T12: -0.0077
REMARK 3 T13: 0.0215 T23: 0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 0.0022 L22: 0.0002
REMARK 3 L33: 0.0021 L12: 0.0006
REMARK 3 L13: -0.0001 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: -0.0127 S12: -0.0095 S13: -0.0015
REMARK 3 S21: -0.0031 S22: -0.0028 S23: -0.0000
REMARK 3 S31: -0.0013 S32: 0.0041 S33: 0.0156
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1 C 240
REMARK 3 RESIDUE RANGE : C 301 C 316
REMARK 3 ORIGIN FOR THE GROUP (A): 32.9898 -87.2917 0.8448
REMARK 3 T TENSOR
REMARK 3 T11: 0.1525 T22: 0.1029
REMARK 3 T33: 0.1335 T12: 0.0001
REMARK 3 T13: -0.0000 T23: 0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 0.0343 L22: 0.0058
REMARK 3 L33: 0.0134 L12: 0.0133
REMARK 3 L13: -0.0184 L23: -0.0070
REMARK 3 S TENSOR
REMARK 3 S11: 0.0040 S12: 0.0009 S13: 0.0041
REMARK 3 S21: -0.0003 S22: 0.0095 S23: 0.0030
REMARK 3 S31: 0.0153 S32: 0.0057 S33: -0.0136
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 1 D 242
REMARK 3 RESIDUE RANGE : D 301 D 312
REMARK 3 ORIGIN FOR THE GROUP (A): 3.5511 -89.8832 13.3220
REMARK 3 T TENSOR
REMARK 3 T11: 0.1298 T22: 0.0719
REMARK 3 T33: 0.1497 T12: 0.0049
REMARK 3 T13: -0.0052 T23: 0.0105
REMARK 3 L TENSOR
REMARK 3 L11: 0.0006 L22: 0.0133
REMARK 3 L33: 0.0060 L12: -0.0012
REMARK 3 L13: 0.0016 L23: 0.0003
REMARK 3 S TENSOR
REMARK 3 S11: -0.0001 S12: 0.0062 S13: -0.0010
REMARK 3 S21: -0.0227 S22: -0.0089 S23: 0.0358
REMARK 3 S31: -0.0022 S32: 0.0200 S33: 0.0090
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 3 E 233
REMARK 3 RESIDUE RANGE : E 301 E 305
REMARK 3 ORIGIN FOR THE GROUP (A): -2.9687 -94.2169 45.2290
REMARK 3 T TENSOR
REMARK 3 T11: 0.1102 T22: 0.0960
REMARK 3 T33: 0.1493 T12: 0.0077
REMARK 3 T13: 0.0249 T23: -0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 0.0363 L22: 0.0012
REMARK 3 L33: 0.0660 L12: -0.0028
REMARK 3 L13: 0.0470 L23: -0.0027
REMARK 3 S TENSOR
REMARK 3 S11: 0.0066 S12: -0.0110 S13: -0.0193
REMARK 3 S21: 0.0014 S22: 0.0080 S23: 0.0128
REMARK 3 S31: -0.0034 S32: 0.0054 S33: -0.0146
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 2 F 244
REMARK 3 RESIDUE RANGE : F 301 F 309
REMARK 3 ORIGIN FOR THE GROUP (A): 15.3777 -94.7623 69.5278
REMARK 3 T TENSOR
REMARK 3 T11: 0.1183 T22: 0.1010
REMARK 3 T33: 0.1279 T12: 0.0014
REMARK 3 T13: 0.0414 T23: -0.0087
REMARK 3 L TENSOR
REMARK 3 L11: 0.0035 L22: 0.0023
REMARK 3 L33: 0.0027 L12: -0.0001
REMARK 3 L13: 0.0007 L23: 0.0013
REMARK 3 S TENSOR
REMARK 3 S11: -0.0013 S12: 0.0093 S13: -0.0025
REMARK 3 S21: 0.0079 S22: -0.0129 S23: 0.0025
REMARK 3 S31: 0.0119 S32: -0.0017 S33: 0.0142
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 2 G 242
REMARK 3 RESIDUE RANGE : G 301 G 302
REMARK 3 RESIDUE RANGE : G 401 G 419
REMARK 3 ORIGIN FOR THE GROUP (A): 47.9431 -93.1712 70.9538
REMARK 3 T TENSOR
REMARK 3 T11: 0.1620 T22: 0.0896
REMARK 3 T33: 0.1189 T12: -0.0037
REMARK 3 T13: 0.0062 T23: -0.0117
REMARK 3 L TENSOR
REMARK 3 L11: 0.0026 L22: 0.0012
REMARK 3 L33: 0.0026 L12: -0.0003
REMARK 3 L13: -0.0021 L23: 0.0005
REMARK 3 S TENSOR
REMARK 3 S11: 0.0037 S12: 0.0147 S13: -0.0032
REMARK 3 S21: 0.0002 S22: -0.0041 S23: -0.0110
REMARK 3 S31: 0.0069 S32: -0.0144 S33: 0.0004
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 1 H 222
REMARK 3 RESIDUE RANGE : H 301 H 302
REMARK 3 RESIDUE RANGE : H 401 H 421
REMARK 3 ORIGIN FOR THE GROUP (A): 67.8027-129.9806 48.1031
REMARK 3 T TENSOR
REMARK 3 T11: 0.1202 T22: 0.0943
REMARK 3 T33: 0.1326 T12: -0.0043
REMARK 3 T13: 0.0025 T23: -0.0074
REMARK 3 L TENSOR
REMARK 3 L11: 0.0049 L22: 0.0299
REMARK 3 L33: 0.0044 L12: 0.0029
REMARK 3 L13: -0.0044 L23: -0.0001
REMARK 3 S TENSOR
REMARK 3 S11: 0.0124 S12: 0.0163 S13: 0.0037
REMARK 3 S21: 0.0423 S22: -0.0071 S23: -0.0432
REMARK 3 S31: -0.0065 S32: -0.0189 S33: -0.0053
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 1 I 204
REMARK 3 RESIDUE RANGE : I 301 I 301
REMARK 3 RESIDUE RANGE : I 401 I 422
REMARK 3 ORIGIN FOR THE GROUP (A): 69.0187-127.4803 20.8175
REMARK 3 T TENSOR
REMARK 3 T11: 0.1134 T22: 0.1104
REMARK 3 T33: 0.1390 T12: -0.0056
REMARK 3 T13: 0.0247 T23: -0.0001
REMARK 3 L TENSOR
REMARK 3 L11: 0.0047 L22: 0.0300
REMARK 3 L33: 0.0105 L12: 0.0073
REMARK 3 L13: -0.0062 L23: -0.0036
REMARK 3 S TENSOR
REMARK 3 S11: 0.0133 S12: 0.0102 S13: 0.0029
REMARK 3 S21: 0.0079 S22: -0.0108 S23: -0.0142
REMARK 3 S31: -0.0245 S32: -0.0214 S33: -0.0025
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 1 J 195
REMARK 3 RESIDUE RANGE : J 201 J 225
REMARK 3 ORIGIN FOR THE GROUP (A): 45.4656-126.5288 -0.7568
REMARK 3 T TENSOR
REMARK 3 T11: 0.1601 T22: 0.1047
REMARK 3 T33: 0.1230 T12: 0.0020
REMARK 3 T13: 0.0181 T23: -0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 0.0486 L22: 0.0238
REMARK 3 L33: 0.0052 L12: -0.0202
REMARK 3 L13: 0.0077 L23: -0.0102
REMARK 3 S TENSOR
REMARK 3 S11: 0.0060 S12: -0.0076 S13: 0.0002
REMARK 3 S21: -0.0165 S22: -0.0072 S23: -0.0093
REMARK 3 S31: -0.0027 S32: 0.0053 S33: 0.0012
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K 1 K 212
REMARK 3 RESIDUE RANGE : K 301 K 303
REMARK 3 RESIDUE RANGE : K 401 K 426
REMARK 3 ORIGIN FOR THE GROUP (A): 11.5442-130.7054 2.1504
REMARK 3 T TENSOR
REMARK 3 T11: 0.1538 T22: 0.0777
REMARK 3 T33: 0.1280 T12: 0.0028
REMARK 3 T13: -0.0134 T23: 0.0103
REMARK 3 L TENSOR
REMARK 3 L11: 0.0119 L22: 0.0195
REMARK 3 L33: 0.0032 L12: -0.0131
REMARK 3 L13: -0.0032 L23: 0.0012
REMARK 3 S TENSOR
REMARK 3 S11: 0.0047 S12: -0.0202 S13: 0.0096
REMARK 3 S21: -0.0222 S22: 0.0084 S23: 0.0036
REMARK 3 S31: -0.0099 S32: 0.0102 S33: -0.0131
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 1 L 222
REMARK 3 RESIDUE RANGE : L 301 L 317
REMARK 3 ORIGIN FOR THE GROUP (A): -4.1162-134.1347 28.2191
REMARK 3 T TENSOR
REMARK 3 T11: 0.1156 T22: 0.0964
REMARK 3 T33: 0.1514 T12: 0.0048
REMARK 3 T13: 0.0005 T23: 0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 0.0133 L22: 0.0022
REMARK 3 L33: 0.0401 L12: -0.0048
REMARK 3 L13: 0.0189 L23: -0.0088
REMARK 3 S TENSOR
REMARK 3 S11: 0.0049 S12: -0.0119 S13: -0.0005
REMARK 3 S21: 0.0012 S22: 0.0030 S23: 0.0066
REMARK 3 S31: -0.0127 S32: 0.0111 S33: -0.0079
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : M 1 M 231
REMARK 3 RESIDUE RANGE : M 301 M 321
REMARK 3 ORIGIN FOR THE GROUP (A): 7.8970-137.1794 60.0047
REMARK 3 T TENSOR
REMARK 3 T11: 0.1202 T22: 0.0933
REMARK 3 T33: 0.1141 T12: -0.0029
REMARK 3 T13: 0.0222 T23: -0.0068
REMARK 3 L TENSOR
REMARK 3 L11: 0.6474 L22: 0.0255
REMARK 3 L33: 0.3432 L12: 0.1169
REMARK 3 L13: 0.0458 L23: 0.0423
REMARK 3 S TENSOR
REMARK 3 S11: 0.0298 S12: 0.0283 S13: -0.0524
REMARK 3 S21: 0.0152 S22: -0.0036 S23: -0.0140
REMARK 3 S31: 0.0504 S32: 0.0087 S33: -0.0261
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : N 1 N 196
REMARK 3 RESIDUE RANGE : N 201 N 203
REMARK 3 RESIDUE RANGE : N 301 N 311
REMARK 3 ORIGIN FOR THE GROUP (A): 40.1440-133.9542 70.4015
REMARK 3 T TENSOR
REMARK 3 T11: 0.1549 T22: 0.0994
REMARK 3 T33: 0.1228 T12: -0.0047
REMARK 3 T13: 0.0078 T23: -0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 0.0101 L22: 0.0291
REMARK 3 L33: 0.0020 L12: 0.0170
REMARK 3 L13: -0.0036 L23: -0.0064
REMARK 3 S TENSOR
REMARK 3 S11: 0.0084 S12: 0.0007 S13: -0.0039
REMARK 3 S21: 0.0183 S22: -0.0020 S23: 0.0009
REMARK 3 S31: 0.0024 S32: 0.0023 S33: -0.0064
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : O 1 O 250
REMARK 3 RESIDUE RANGE : O 301 O 317
REMARK 3 ORIGIN FOR THE GROUP (A): 2.0576-206.3443 36.5286
REMARK 3 T TENSOR
REMARK 3 T11: 0.1277 T22: 0.0975
REMARK 3 T33: 0.1480 T12: -0.0129
REMARK 3 T13: -0.0036 T23: 0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 0.0056 L22: 0.0006
REMARK 3 L33: 0.0020 L12: -0.0002
REMARK 3 L13: 0.0011 L23: -0.0010
REMARK 3 S TENSOR
REMARK 3 S11: 0.0042 S12: 0.0192 S13: 0.0158
REMARK 3 S21: -0.0070 S22: -0.0012 S23: 0.0046
REMARK 3 S31: 0.0147 S32: 0.0031 S33: -0.0030
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : P 1 P 244
REMARK 3 RESIDUE RANGE : P 301 P 306
REMARK 3 ORIGIN FOR THE GROUP (A): 8.5821-205.2407 6.5053
REMARK 3 T TENSOR
REMARK 3 T11: 0.1517 T22: 0.0895
REMARK 3 T33: 0.1429 T12: 0.0016
REMARK 3 T13: -0.0186 T23: -0.0069
REMARK 3 L TENSOR
REMARK 3 L11: 0.0472 L22: 0.0043
REMARK 3 L33: 0.0301 L12: 0.0119
REMARK 3 L13: 0.0374 L23: 0.0089
REMARK 3 S TENSOR
REMARK 3 S11: -0.0131 S12: -0.0049 S13: 0.0043
REMARK 3 S21: -0.0029 S22: 0.0031 S23: -0.0122
REMARK 3 S31: -0.0072 S32: -0.0018 S33: 0.0101
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Q 1 Q 240
REMARK 3 RESIDUE RANGE : Q 301 Q 311
REMARK 3 ORIGIN FOR THE GROUP (A): 36.1674-203.2541 -9.2609
REMARK 3 T TENSOR
REMARK 3 T11: 0.1602 T22: 0.0692
REMARK 3 T33: 0.1067 T12: 0.0246
REMARK 3 T13: -0.0021 T23: -0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 0.0056 L22: 0.0075
REMARK 3 L33: 0.0135 L12: -0.0038
REMARK 3 L13: -0.0030 L23: 0.0017
REMARK 3 S TENSOR
REMARK 3 S11: 0.0183 S12: 0.0020 S13: -0.0057
REMARK 3 S21: -0.0148 S22: -0.0163 S23: 0.0257
REMARK 3 S31: -0.0078 S32: 0.0270 S33: -0.0021
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : R 1 R 242
REMARK 3 RESIDUE RANGE : R 301 R 306
REMARK 3 ORIGIN FOR THE GROUP (A): 65.6253-202.8145 3.4340
REMARK 3 T TENSOR
REMARK 3 T11: 0.1287 T22: 0.0682
REMARK 3 T33: 0.1372 T12: 0.0198
REMARK 3 T13: 0.0251 T23: -0.0103
REMARK 3 L TENSOR
REMARK 3 L11: 0.0093 L22: 0.0060
REMARK 3 L33: 0.0094 L12: 0.0025
REMARK 3 L13: 0.0093 L23: 0.0019
REMARK 3 S TENSOR
REMARK 3 S11: 0.0089 S12: -0.0213 S13: 0.0082
REMARK 3 S21: -0.0117 S22: -0.0151 S23: -0.0205
REMARK 3 S31: 0.0158 S32: -0.0196 S33: 0.0061
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : S 3 S 233
REMARK 3 RESIDUE RANGE : S 301 S 306
REMARK 3 ORIGIN FOR THE GROUP (A): 72.4907-203.8996 35.2459
REMARK 3 T TENSOR
REMARK 3 T11: 0.0883 T22: 0.0603
REMARK 3 T33: 0.1374 T12: -0.0026
REMARK 3 T13: -0.0135 T23: -0.0305
REMARK 3 L TENSOR
REMARK 3 L11: 0.0150 L22: 0.0346
REMARK 3 L33: 0.0195 L12: 0.0169
REMARK 3 L13: 0.0008 L23: 0.0181
REMARK 3 S TENSOR
REMARK 3 S11: 0.0336 S12: 0.0105 S13: -0.0150
REMARK 3 S21: 0.0405 S22: -0.0005 S23: -0.0503
REMARK 3 S31: 0.0072 S32: -0.0174 S33: -0.0330
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : T 2 T 244
REMARK 3 RESIDUE RANGE : T 301 T 313
REMARK 3 ORIGIN FOR THE GROUP (A): 54.3999-207.5943 59.4553
REMARK 3 T TENSOR
REMARK 3 T11: 0.1582 T22: 0.0589
REMARK 3 T33: 0.1443 T12: -0.0031
REMARK 3 T13: -0.0531 T23: 0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 0.0145 L22: 0.0056
REMARK 3 L33: 0.0071 L12: 0.0071
REMARK 3 L13: -0.0041 L23: -0.0008
REMARK 3 S TENSOR
REMARK 3 S11: 0.0310 S12: -0.0027 S13: -0.0250
REMARK 3 S21: 0.0189 S22: -0.0192 S23: -0.0266
REMARK 3 S31: -0.0157 S32: -0.0178 S33: -0.0118
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : U 2 U 242
REMARK 3 RESIDUE RANGE : U 301 U 301
REMARK 3 RESIDUE RANGE : U 401 U 415
REMARK 3 ORIGIN FOR THE GROUP (A): 21.8956-209.5797 60.9508
REMARK 3 T TENSOR
REMARK 3 T11: 0.1645 T22: 0.0839
REMARK 3 T33: 0.1361 T12: -0.0084
REMARK 3 T13: -0.0124 T23: 0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 0.0036 L22: 0.0030
REMARK 3 L33: 0.0165 L12: 0.0017
REMARK 3 L13: -0.0006 L23: -0.0062
REMARK 3 S TENSOR
REMARK 3 S11: -0.0037 S12: 0.0171 S13: 0.0013
REMARK 3 S21: 0.0004 S22: 0.0101 S23: 0.0058
REMARK 3 S31: -0.0016 S32: -0.0017 S33: -0.0064
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : V 1 V 222
REMARK 3 RESIDUE RANGE : V 301 V 303
REMARK 3 RESIDUE RANGE : V 401 V 420
REMARK 3 ORIGIN FOR THE GROUP (A): 1.8242-169.2437 45.1362
REMARK 3 T TENSOR
REMARK 3 T11: 0.1177 T22: 0.0910
REMARK 3 T33: 0.1405 T12: -0.0107
REMARK 3 T13: 0.0119 T23: 0.0106
REMARK 3 L TENSOR
REMARK 3 L11: 0.0023 L22: 0.0032
REMARK 3 L33: 0.0065 L12: -0.0005
REMARK 3 L13: 0.0036 L23: 0.0004
REMARK 3 S TENSOR
REMARK 3 S11: 0.0094 S12: 0.0060 S13: -0.0087
REMARK 3 S21: 0.0107 S22: -0.0032 S23: 0.0183
REMARK 3 S31: 0.0191 S32: 0.0142 S33: -0.0061
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : W 1 W 204
REMARK 3 RESIDUE RANGE : W 301 W 315
REMARK 3 ORIGIN FOR THE GROUP (A): 0.2740-167.0107 17.7748
REMARK 3 T TENSOR
REMARK 3 T11: 0.1359 T22: 0.0900
REMARK 3 T33: 0.1542 T12: -0.0060
REMARK 3 T13: -0.0131 T23: 0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 0.0061 L22: 0.0263
REMARK 3 L33: 0.0112 L12: 0.0117
REMARK 3 L13: 0.0031 L23: 0.0095
REMARK 3 S TENSOR
REMARK 3 S11: 0.0017 S12: -0.0057 S13: 0.0057
REMARK 3 S21: -0.0036 S22: 0.0031 S23: 0.0120
REMARK 3 S31: 0.0178 S32: 0.0218 S33: -0.0048
REMARK 3
REMARK 3 TLS GROUP : 24
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : X 1 X 195
REMARK 3 RESIDUE RANGE : X 201 X 228
REMARK 3 ORIGIN FOR THE GROUP (A): 23.5937-164.2333 -3.9396
REMARK 3 T TENSOR
REMARK 3 T11: 0.1689 T22: 0.0829
REMARK 3 T33: 0.1298 T12: 0.0044
REMARK 3 T13: -0.0172 T23: -0.0112
REMARK 3 L TENSOR
REMARK 3 L11: 0.0058 L22: 0.0003
REMARK 3 L33: 0.0006 L12: -0.0001
REMARK 3 L13: -0.0002 L23: -0.0001
REMARK 3 S TENSOR
REMARK 3 S11: 0.0110 S12: -0.0133 S13: -0.0171
REMARK 3 S21: 0.0048 S22: -0.0033 S23: 0.0038
REMARK 3 S31: 0.0025 S32: 0.0057 S33: -0.0078
REMARK 3
REMARK 3 TLS GROUP : 25
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Y 1 Y 212
REMARK 3 RESIDUE RANGE : Y 301 Y 303
REMARK 3 RESIDUE RANGE : Y 401 Y 415
REMARK 3 ORIGIN FOR THE GROUP (A): 57.5580-160.6154 -0.6737
REMARK 3 T TENSOR
REMARK 3 T11: 0.1344 T22: 0.1004
REMARK 3 T33: 0.1103 T12: 0.0060
REMARK 3 T13: 0.0281 T23: -0.0100
REMARK 3 L TENSOR
REMARK 3 L11: 0.0107 L22: 0.0044
REMARK 3 L33: 0.0059 L12: -0.0059
REMARK 3 L13: 0.0058 L23: -0.0025
REMARK 3 S TENSOR
REMARK 3 S11: 0.0264 S12: -0.0106 S13: -0.0069
REMARK 3 S21: -0.0240 S22: -0.0032 S23: -0.0047
REMARK 3 S31: 0.0139 S32: 0.0042 S33: -0.0232
REMARK 3
REMARK 3 TLS GROUP : 26
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Z 1 Z 222
REMARK 3 RESIDUE RANGE : Z 301 Z 301
REMARK 3 RESIDUE RANGE : Z 401 Z 419
REMARK 3 ORIGIN FOR THE GROUP (A): 73.4768-161.6849 25.3991
REMARK 3 T TENSOR
REMARK 3 T11: 0.1082 T22: 0.0962
REMARK 3 T33: 0.1485 T12: 0.0103
REMARK 3 T13: 0.0214 T23: -0.0074
REMARK 3 L TENSOR
REMARK 3 L11: 0.0010 L22: 0.0672
REMARK 3 L33: 0.0263 L12: 0.0002
REMARK 3 L13: 0.0032 L23: -0.0289
REMARK 3 S TENSOR
REMARK 3 S11: 0.0082 S12: -0.0023 S13: -0.0079
REMARK 3 S21: -0.0042 S22: 0.0006 S23: -0.0240
REMARK 3 S31: 0.0163 S32: -0.0226 S33: -0.0087
REMARK 3
REMARK 3 TLS GROUP : 27
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : a 1 a 232
REMARK 3 RESIDUE RANGE : a 301 a 322
REMARK 3 ORIGIN FOR THE GROUP (A): 61.8098-163.8660 57.4338
REMARK 3 T TENSOR
REMARK 3 T11: 0.1307 T22: 0.0615
REMARK 3 T33: 0.1230 T12: 0.0034
REMARK 3 T13: -0.0062 T23: 0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 0.6395 L22: 0.0711
REMARK 3 L33: 0.4356 L12: 0.1486
REMARK 3 L13: 0.1022 L23: -0.0854
REMARK 3 S TENSOR
REMARK 3 S11: 0.0022 S12: 0.0047 S13: 0.0360
REMARK 3 S21: 0.0080 S22: 0.0014 S23: 0.0196
REMARK 3 S31: -0.0946 S32: -0.0635 S33: -0.0036
REMARK 3
REMARK 3 TLS GROUP : 28
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : b 1 b 196
REMARK 3 RESIDUE RANGE : b 201 b 201
REMARK 3 RESIDUE RANGE : b 301 b 314
REMARK 3 ORIGIN FOR THE GROUP (A): 29.7462-169.1407 67.4540
REMARK 3 T TENSOR
REMARK 3 T11: 0.1581 T22: 0.0953
REMARK 3 T33: 0.1256 T12: -0.0060
REMARK 3 T13: 0.0028 T23: 0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 0.0043 L22: 0.0027
REMARK 3 L33: 0.0009 L12: 0.0025
REMARK 3 L13: 0.0006 L23: -0.0001
REMARK 3 S TENSOR
REMARK 3 S11: 0.0211 S12: 0.0040 S13: 0.0006
REMARK 3 S21: 0.0166 S22: -0.0078 S23: 0.0104
REMARK 3 S31: 0.0051 S32: -0.0038 S33: -0.0133
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 4QZX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-JUL-14.
REMARK 100 THE DEPOSITION ID IS D_1000086724.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-AUG-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 : 323894
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.45500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: 1RYP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 MM MGAC2, 13% MPD, PH 6.8, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 150.40500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 28-MERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 28-MERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 121720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 214360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -443.0 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 LYS M 232
REMARK 465 ILE M 233
REMARK 465 MET P 0
REMARK 465 LYS P 245
REMARK 465 LYS P 246
REMARK 465 ASP P 247
REMARK 465 GLU P 248
REMARK 465 ASP P 249
REMARK 465 GLU P 250
REMARK 465 GLU P 251
REMARK 465 ALA P 252
REMARK 465 ASP P 253
REMARK 465 GLU P 254
REMARK 465 ASP P 255
REMARK 465 MET P 256
REMARK 465 LYS P 257
REMARK 465 MET Q -1
REMARK 465 SER Q 0
REMARK 465 GLN Q 241
REMARK 465 GLN Q 242
REMARK 465 GLU Q 243
REMARK 465 GLN Q 244
REMARK 465 ASP Q 245
REMARK 465 LYS Q 246
REMARK 465 LYS Q 247
REMARK 465 LYS Q 248
REMARK 465 LYS Q 249
REMARK 465 SER Q 250
REMARK 465 ASN Q 251
REMARK 465 HIS Q 252
REMARK 465 MET R -7
REMARK 465 PHE R -6
REMARK 465 LEU R -5
REMARK 465 THR R -4
REMARK 465 ARG R -3
REMARK 465 SER R -2
REMARK 465 GLU R -1
REMARK 465 TYR R 0
REMARK 465 GLY R 118
REMARK 465 ALA R 119
REMARK 465 SER R 120
REMARK 465 GLY R 121
REMARK 465 GLU R 122
REMARK 465 GLU R 123
REMARK 465 ARG R 124
REMARK 465 SER R 243
REMARK 465 PRO R 244
REMARK 465 GLU R 245
REMARK 465 GLU R 246
REMARK 465 ALA R 247
REMARK 465 ASP R 248
REMARK 465 VAL R 249
REMARK 465 GLU R 250
REMARK 465 MET R 251
REMARK 465 SER R 252
REMARK 465 MET S 0
REMARK 465 PHE S 1
REMARK 465 ARG S 2
REMARK 465 MET T -3
REMARK 465 THR T -2
REMARK 465 SER T -1
REMARK 465 ILE T 0
REMARK 465 GLY T 1
REMARK 465 GLY T 245
REMARK 465 ASP T 246
REMARK 465 ASP T 247
REMARK 465 ASP T 248
REMARK 465 GLU T 249
REMARK 465 ASP T 250
REMARK 465 GLU T 251
REMARK 465 ASP T 252
REMARK 465 ASP T 253
REMARK 465 SER T 254
REMARK 465 ASP T 255
REMARK 465 ASN T 256
REMARK 465 VAL T 257
REMARK 465 MET T 258
REMARK 465 SER T 259
REMARK 465 SER T 260
REMARK 465 ASP T 261
REMARK 465 ASP T 262
REMARK 465 GLU T 263
REMARK 465 ASN T 264
REMARK 465 ALA T 265
REMARK 465 PRO T 266
REMARK 465 VAL T 267
REMARK 465 ALA T 268
REMARK 465 THR T 269
REMARK 465 ASN T 270
REMARK 465 ALA T 271
REMARK 465 ASN T 272
REMARK 465 ALA T 273
REMARK 465 THR T 274
REMARK 465 THR T 275
REMARK 465 ASP T 276
REMARK 465 GLN T 277
REMARK 465 GLU T 278
REMARK 465 GLY T 279
REMARK 465 ASP T 280
REMARK 465 ILE T 281
REMARK 465 HIS T 282
REMARK 465 LEU T 283
REMARK 465 GLU T 284
REMARK 465 MET U -8
REMARK 465 SER U -7
REMARK 465 GLY U -6
REMARK 465 ALA U -5
REMARK 465 ALA U -4
REMARK 465 ALA U -3
REMARK 465 ALA U -2
REMARK 465 SER U -1
REMARK 465 ALA U 0
REMARK 465 ALA U 1
REMARK 465 ASP U 243
REMARK 465 ILE V 223
REMARK 465 GLN V 224
REMARK 465 GLU V 225
REMARK 465 GLU V 226
REMARK 465 GLN V 227
REMARK 465 VAL V 228
REMARK 465 ASP V 229
REMARK 465 ILE V 230
REMARK 465 THR V 231
REMARK 465 ALA V 232
REMARK 465 MET W 0
REMARK 465 GLN X 196
REMARK 465 ALA X 197
REMARK 465 GLN X 198
REMARK 465 THR a -12
REMARK 465 GLN a -11
REMARK 465 ILE a -10
REMARK 465 ALA a -9
REMARK 465 ASN a -8
REMARK 465 ALA a -7
REMARK 465 GLY a -6
REMARK 465 ALA a -5
REMARK 465 SER a -4
REMARK 465 PRO a -3
REMARK 465 MET a -2
REMARK 465 VAL a -1
REMARK 465 ASN a 0
REMARK 465 ILE a 233
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O13 04C N 201 O HOH N 301 2.10
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 2 151.53 72.15
REMARK 500 ASP A 3 97.63 -63.86
REMARK 500 TYR A 97 -64.77 -147.06
REMARK 500 ALA A 249 57.45 -92.60
REMARK 500 ARG B 8 74.14 58.54
REMARK 500 THR B 10 52.27 -113.43
REMARK 500 VAL B 51 95.85 3.78
REMARK 500 THR B 60 41.74 -98.31
REMARK 500 LYS B 217 37.82 -98.40
REMARK 500 ASP B 221 104.78 67.66
REMARK 500 ARG C 4 129.99 -38.19
REMARK 500 GLN C 202 -85.24 137.37
REMARK 500 ALA C 205 -115.99 -83.71
REMARK 500 LYS C 206 38.93 -91.46
REMARK 500 GLN C 239 84.85 -66.56
REMARK 500 SER D 5 44.50 -102.36
REMARK 500 ARG D 45 77.87 57.42
REMARK 500 SER E 39 -152.36 -107.62
REMARK 500 ASP E 137 -160.58 -125.82
REMARK 500 ASP E 202 -41.75 69.22
REMARK 500 SER F 9 3.70 80.07
REMARK 500 ASP F 67 -134.07 54.84
REMARK 500 LYS F 100 -57.08 73.39
REMARK 500 ASP F 138 -169.82 -129.42
REMARK 500 ASN F 203 44.69 -156.90
REMARK 500 LYS G 165 45.96 -100.65
REMARK 500 GLU G 241 46.28 -87.54
REMARK 500 ASN H 30 58.49 -151.28
REMARK 500 SER H 171 -115.37 62.76
REMARK 500 GLN I 31 -113.12 51.32
REMARK 500 ARG I 97 48.04 -102.29
REMARK 500 ASP I 134 -63.56 -94.15
REMARK 500 ASP I 192 35.37 -144.22
REMARK 500 GLN I 203 48.81 -106.05
REMARK 500 ASP J 2 -69.77 159.23
REMARK 500 VAL J 9 -167.65 -114.33
REMARK 500 SER J 31 33.79 -143.61
REMARK 500 LYS J 34 59.80 -94.72
REMARK 500 ASP L 32 -116.21 54.77
REMARK 500 PHE L 103 68.09 -159.37
REMARK 500 ASP L 200 -66.69 68.46
REMARK 500 ILE M 5 -84.89 -99.49
REMARK 500 THR M 9 -152.33 -89.45
REMARK 500 ALA M 83 -114.85 -145.11
REMARK 500 LYS N 107 -143.88 59.70
REMARK 500 THR O 2 151.72 72.06
REMARK 500 ASP O 3 97.54 -63.94
REMARK 500 TYR O 97 -65.05 -147.22
REMARK 500 ALA O 249 57.47 -92.66
REMARK 500 ARG P 8 73.93 59.02
REMARK 500
REMARK 500 THIS ENTRY HAS 89 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG G 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR G 8 OG1
REMARK 620 2 TYR G 119 O 75.4
REMARK 620 3 ARG G 122 O 77.7 69.0
REMARK 620 4 MET G 125 O 149.0 74.9 83.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG N 203 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN H 91 OE1
REMARK 620 2 ASP N 51 OD1 152.2
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 69.0
REMARK 620 3 SER I 180 O 83.7 82.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG Y 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP I 204 O
REMARK 620 2 ALA Y 165 O 97.4
REMARK 620 3 ASP Y 168 O 165.1 86.9
REMARK 620 4 SER Y 171 O 88.9 70.4 79.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG K 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA K 165 O
REMARK 620 2 ASP K 168 O 93.7
REMARK 620 3 SER K 171 O 73.6 77.9
REMARK 620 4 ASP W 204 O 103.5 150.8 84.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG V 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP L 222 OXT
REMARK 620 2 ILE V 163 O 100.7
REMARK 620 3 ASP V 166 O 129.4 121.7
REMARK 620 4 SER V 169 O 84.8 85.9 73.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG N 202 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE N 163 O
REMARK 620 2 ASP N 166 O 65.3
REMARK 620 3 SER N 169 O 94.2 68.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG Z 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR Z 192 O
REMARK 620 2 VAL Z 198 O 99.4
REMARK 620 N 1
REMARK 630
REMARK 630 MOLECULE TYPE: PEPTIDE-LIKE INHIBITOR
REMARK 630 MOLECULE NAME: 1,2,4-TRIDEOXY-4-METHYL-2-{[N-(MORPHOLIN-4-YLACETYL)
REMARK 630 -L-ALANYL-O-METHYL-L-TYROSYL]AMINO}-1-PHENYL-D-XYLITOL
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 04C H 301
REMARK 630 04C K 301
REMARK 630 04C N 201
REMARK 630 04C V 301
REMARK 630 04C Y 301
REMARK 630 04C b 201
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: 00E ALA 0A1 04B
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 CL G 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 04C H 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES H 302
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 04C K 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG K 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES K 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 04C N 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG N 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG N 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL U 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 04C V 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG V 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES V 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 04C Y 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Y 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES Y 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Z 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 04C b 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4QTR RELATED DB: PDB
REMARK 900 RELATED ID: 4QUX RELATED DB: PDB
REMARK 900 RELATED ID: 4QUY RELATED DB: PDB
REMARK 900 RELATED ID: 4QV0 RELATED DB: PDB
REMARK 900 RELATED ID: 4QV1 RELATED DB: PDB
REMARK 900 RELATED ID: 4QV3 RELATED DB: PDB
REMARK 900 RELATED ID: 4QV4 RELATED DB: PDB
REMARK 900 RELATED ID: 4QV5 RELATED DB: PDB
REMARK 900 RELATED ID: 4QV6 RELATED DB: PDB
REMARK 900 RELATED ID: 4QV7 RELATED DB: PDB
REMARK 900 RELATED ID: 4QV8 RELATED DB: PDB
REMARK 900 RELATED ID: 4QV9 RELATED DB: PDB
REMARK 900 RELATED ID: 4QVL RELATED DB: PDB
REMARK 900 RELATED ID: 4QVM RELATED DB: PDB
REMARK 900 RELATED ID: 4QVN RELATED DB: PDB
REMARK 900 RELATED ID: 4QVP RELATED DB: PDB
REMARK 900 RELATED ID: 4QVQ RELATED DB: PDB
REMARK 900 RELATED ID: 1RYP RELATED DB: PDB
REMARK 900 RELATED ID: 4QWR RELATED DB: PDB
REMARK 900 RELATED ID: 4QWS RELATED DB: PDB
REMARK 900 RELATED ID: 4QWX RELATED DB: PDB
REMARK 900 RELATED ID: 4QZ0 RELATED DB: PDB
REMARK 900 RELATED ID: 4QZ1 RELATED DB: PDB
REMARK 900 RELATED ID: 4QZ2 RELATED DB: PDB
REMARK 900 RELATED ID: 4QZ3 RELATED DB: PDB
REMARK 900 RELATED ID: 4QZ5 RELATED DB: PDB
REMARK 900 RELATED ID: 4QZ6 RELATED DB: PDB
REMARK 900 RELATED ID: 4QZX RELATED DB: PDB
REMARK 900 RELATED ID: 4QZZ RELATED DB: PDB
DBREF 4QZX A 1 250 UNP P23639 PSA2_YEAST 1 250
DBREF 4QZX B 0 257 UNP P23638 PSA3_YEAST 1 258
DBREF 4QZX C -1 252 UNP P40303 PSA4_YEAST 1 254
DBREF 4QZX D -7 252 UNP P32379 PSA5_YEAST 1 260
DBREF 4QZX E 0 233 UNP P40302 PSA6_YEAST 1 234
DBREF 4QZX F -3 284 UNP P21242 PSA7_YEAST 1 288
DBREF 4QZX G -8 243 UNP P21243 PSA1_YEAST 1 252
DBREF 4QZX H 1 232 UNP P25043 PSB2_YEAST 30 261
DBREF 4QZX I 0 204 UNP P25451 PSB3_YEAST 1 205
DBREF 4QZX J 1 198 UNP P22141 PSB4_YEAST 1 198
DBREF 4QZX K 1 212 UNP P30656 PSB5_YEAST 76 287
DBREF 4QZX L 1 222 UNP P23724 PSB6_YEAST 20 241
DBREF 4QZX M -12 233 UNP P30657 PSB7_YEAST 21 266
DBREF 4QZX N 1 196 UNP P38624 PSB1_YEAST 20 215
DBREF 4QZX O 1 250 UNP P23639 PSA2_YEAST 1 250
DBREF 4QZX P 0 257 UNP P23638 PSA3_YEAST 1 258
DBREF 4QZX Q -1 252 UNP P40303 PSA4_YEAST 1 254
DBREF 4QZX R -7 252 UNP P32379 PSA5_YEAST 1 260
DBREF 4QZX S 0 233 UNP P40302 PSA6_YEAST 1 234
DBREF 4QZX T -3 284 UNP P21242 PSA7_YEAST 1 288
DBREF 4QZX U -8 243 UNP P21243 PSA1_YEAST 1 252
DBREF 4QZX V 1 232 UNP P25043 PSB2_YEAST 30 261
DBREF 4QZX W 0 204 UNP P25451 PSB3_YEAST 1 205
DBREF 4QZX X 1 198 UNP P22141 PSB4_YEAST 1 198
DBREF 4QZX Y 1 212 UNP P30656 PSB5_YEAST 76 287
DBREF 4QZX Z 1 222 UNP P23724 PSB6_YEAST 20 241
DBREF 4QZX a -12 233 UNP P30657 PSB7_YEAST 21 266
DBREF 4QZX b 1 196 UNP P38624 PSB1_YEAST 20 215
SEQADV 4QZX PHE K 63 UNP P30656 CYS 138 ENGINEERED MUTATION
SEQADV 4QZX PHE Y 63 UNP P30656 CYS 138 ENGINEERED MUTATION
SEQRES 1 A 250 MET THR ASP ARG TYR SER PHE SER LEU THR THR PHE SER
SEQRES 2 A 250 PRO SER GLY LYS LEU GLY GLN ILE ASP TYR ALA LEU THR
SEQRES 3 A 250 ALA VAL LYS GLN GLY VAL THR SER LEU GLY ILE LYS ALA
SEQRES 4 A 250 THR ASN GLY VAL VAL ILE ALA THR GLU LYS LYS SER SER
SEQRES 5 A 250 SER PRO LEU ALA MET SER GLU THR LEU SER LYS VAL SER
SEQRES 6 A 250 LEU LEU THR PRO ASP ILE GLY ALA VAL TYR SER GLY MET
SEQRES 7 A 250 GLY PRO ASP TYR ARG VAL LEU VAL ASP LYS SER ARG LYS
SEQRES 8 A 250 VAL ALA HIS THR SER TYR LYS ARG ILE TYR GLY GLU TYR
SEQRES 9 A 250 PRO PRO THR LYS LEU LEU VAL SER GLU VAL ALA LYS ILE
SEQRES 10 A 250 MET GLN GLU ALA THR GLN SER GLY GLY VAL ARG PRO PHE
SEQRES 11 A 250 GLY VAL SER LEU LEU ILE ALA GLY HIS ASP GLU PHE ASN
SEQRES 12 A 250 GLY PHE SER LEU TYR GLN VAL ASP PRO SER GLY SER TYR
SEQRES 13 A 250 PHE PRO TRP LYS ALA THR ALA ILE GLY LYS GLY SER VAL
SEQRES 14 A 250 ALA ALA LYS THR PHE LEU GLU LYS ARG TRP ASN ASP GLU
SEQRES 15 A 250 LEU GLU LEU GLU ASP ALA ILE HIS ILE ALA LEU LEU THR
SEQRES 16 A 250 LEU LYS GLU SER VAL GLU GLY GLU PHE ASN GLY ASP THR
SEQRES 17 A 250 ILE GLU LEU ALA ILE ILE GLY ASP GLU ASN PRO ASP LEU
SEQRES 18 A 250 LEU GLY TYR THR GLY ILE PRO THR ASP LYS GLY PRO ARG
SEQRES 19 A 250 PHE ARG LYS LEU THR SER GLN GLU ILE ASN ASP ARG LEU
SEQRES 20 A 250 GLU ALA LEU
SEQRES 1 B 258 MET GLY SER ARG ARG TYR ASP SER ARG THR THR ILE PHE
SEQRES 2 B 258 SER PRO GLU GLY ARG LEU TYR GLN VAL GLU TYR ALA LEU
SEQRES 3 B 258 GLU SER ILE SER HIS ALA GLY THR ALA ILE GLY ILE MET
SEQRES 4 B 258 ALA SER ASP GLY ILE VAL LEU ALA ALA GLU ARG LYS VAL
SEQRES 5 B 258 THR SER THR LEU LEU GLU GLN ASP THR SER THR GLU LYS
SEQRES 6 B 258 LEU TYR LYS LEU ASN ASP LYS ILE ALA VAL ALA VAL ALA
SEQRES 7 B 258 GLY LEU THR ALA ASP ALA GLU ILE LEU ILE ASN THR ALA
SEQRES 8 B 258 ARG ILE HIS ALA GLN ASN TYR LEU LYS THR TYR ASN GLU
SEQRES 9 B 258 ASP ILE PRO VAL GLU ILE LEU VAL ARG ARG LEU SER ASP
SEQRES 10 B 258 ILE LYS GLN GLY TYR THR GLN HIS GLY GLY LEU ARG PRO
SEQRES 11 B 258 PHE GLY VAL SER PHE ILE TYR ALA GLY TYR ASP ASP ARG
SEQRES 12 B 258 TYR GLY TYR GLN LEU TYR THR SER ASN PRO SER GLY ASN
SEQRES 13 B 258 TYR THR GLY TRP LYS ALA ILE SER VAL GLY ALA ASN THR
SEQRES 14 B 258 SER ALA ALA GLN THR LEU LEU GLN MET ASP TYR LYS ASP
SEQRES 15 B 258 ASP MET LYS VAL ASP ASP ALA ILE GLU LEU ALA LEU LYS
SEQRES 16 B 258 THR LEU SER LYS THR THR ASP SER SER ALA LEU THR TYR
SEQRES 17 B 258 ASP ARG LEU GLU PHE ALA THR ILE ARG LYS GLY ALA ASN
SEQRES 18 B 258 ASP GLY GLU VAL TYR GLN LYS ILE PHE LYS PRO GLN GLU
SEQRES 19 B 258 ILE LYS ASP ILE LEU VAL LYS THR GLY ILE THR LYS LYS
SEQRES 20 B 258 ASP GLU ASP GLU GLU ALA ASP GLU ASP MET LYS
SEQRES 1 C 254 MET SER GLY TYR ASP ARG ALA LEU SER ILE PHE SER PRO
SEQRES 2 C 254 ASP GLY HIS ILE PHE GLN VAL GLU TYR ALA LEU GLU ALA
SEQRES 3 C 254 VAL LYS ARG GLY THR CYS ALA VAL GLY VAL LYS GLY LYS
SEQRES 4 C 254 ASN CYS VAL VAL LEU GLY CYS GLU ARG ARG SER THR LEU
SEQRES 5 C 254 LYS LEU GLN ASP THR ARG ILE THR PRO SER LYS VAL SER
SEQRES 6 C 254 LYS ILE ASP SER HIS VAL VAL LEU SER PHE SER GLY LEU
SEQRES 7 C 254 ASN ALA ASP SER ARG ILE LEU ILE GLU LYS ALA ARG VAL
SEQRES 8 C 254 GLU ALA GLN SER HIS ARG LEU THR LEU GLU ASP PRO VAL
SEQRES 9 C 254 THR VAL GLU TYR LEU THR ARG TYR VAL ALA GLY VAL GLN
SEQRES 10 C 254 GLN ARG TYR THR GLN SER GLY GLY VAL ARG PRO PHE GLY
SEQRES 11 C 254 VAL SER THR LEU ILE ALA GLY PHE ASP PRO ARG ASP ASP
SEQRES 12 C 254 GLU PRO LYS LEU TYR GLN THR GLU PRO SER GLY ILE TYR
SEQRES 13 C 254 SER SER TRP SER ALA GLN THR ILE GLY ARG ASN SER LYS
SEQRES 14 C 254 THR VAL ARG GLU PHE LEU GLU LYS ASN TYR ASP ARG LYS
SEQRES 15 C 254 GLU PRO PRO ALA THR VAL GLU GLU CYS VAL LYS LEU THR
SEQRES 16 C 254 VAL ARG SER LEU LEU GLU VAL VAL GLN THR GLY ALA LYS
SEQRES 17 C 254 ASN ILE GLU ILE THR VAL VAL LYS PRO ASP SER ASP ILE
SEQRES 18 C 254 VAL ALA LEU SER SER GLU GLU ILE ASN GLN TYR VAL THR
SEQRES 19 C 254 GLN ILE GLU GLN GLU LYS GLN GLU GLN GLN GLU GLN ASP
SEQRES 20 C 254 LYS LYS LYS LYS SER ASN HIS
SEQRES 1 D 260 MET PHE LEU THR ARG SER GLU TYR ASP ARG GLY VAL SER
SEQRES 2 D 260 THR PHE SER PRO GLU GLY ARG LEU PHE GLN VAL GLU TYR
SEQRES 3 D 260 SER LEU GLU ALA ILE LYS LEU GLY SER THR ALA ILE GLY
SEQRES 4 D 260 ILE ALA THR LYS GLU GLY VAL VAL LEU GLY VAL GLU LYS
SEQRES 5 D 260 ARG ALA THR SER PRO LEU LEU GLU SER ASP SER ILE GLU
SEQRES 6 D 260 LYS ILE VAL GLU ILE ASP ARG HIS ILE GLY CYS ALA MET
SEQRES 7 D 260 SER GLY LEU THR ALA ASP ALA ARG SER MET ILE GLU HIS
SEQRES 8 D 260 ALA ARG THR ALA ALA VAL THR HIS ASN LEU TYR TYR ASP
SEQRES 9 D 260 GLU ASP ILE ASN VAL GLU SER LEU THR GLN SER VAL CYS
SEQRES 10 D 260 ASP LEU ALA LEU ARG PHE GLY GLU GLY ALA SER GLY GLU
SEQRES 11 D 260 GLU ARG LEU MET SER ARG PRO PHE GLY VAL ALA LEU LEU
SEQRES 12 D 260 ILE ALA GLY HIS ASP ALA ASP ASP GLY TYR GLN LEU PHE
SEQRES 13 D 260 HIS ALA GLU PRO SER GLY THR PHE TYR ARG TYR ASN ALA
SEQRES 14 D 260 LYS ALA ILE GLY SER GLY SER GLU GLY ALA GLN ALA GLU
SEQRES 15 D 260 LEU LEU ASN GLU TRP HIS SER SER LEU THR LEU LYS GLU
SEQRES 16 D 260 ALA GLU LEU LEU VAL LEU LYS ILE LEU LYS GLN VAL MET
SEQRES 17 D 260 GLU GLU LYS LEU ASP GLU ASN ASN ALA GLN LEU SER CYS
SEQRES 18 D 260 ILE THR LYS GLN ASP GLY PHE LYS ILE TYR ASP ASN GLU
SEQRES 19 D 260 LYS THR ALA GLU LEU ILE LYS GLU LEU LYS GLU LYS GLU
SEQRES 20 D 260 ALA ALA GLU SER PRO GLU GLU ALA ASP VAL GLU MET SER
SEQRES 1 E 234 MET PHE ARG ASN ASN TYR ASP GLY ASP THR VAL THR PHE
SEQRES 2 E 234 SER PRO THR GLY ARG LEU PHE GLN VAL GLU TYR ALA LEU
SEQRES 3 E 234 GLU ALA ILE LYS GLN GLY SER VAL THR VAL GLY LEU ARG
SEQRES 4 E 234 SER ASN THR HIS ALA VAL LEU VAL ALA LEU LYS ARG ASN
SEQRES 5 E 234 ALA ASP GLU LEU SER SER TYR GLN LYS LYS ILE ILE LYS
SEQRES 6 E 234 CYS ASP GLU HIS MET GLY LEU SER LEU ALA GLY LEU ALA
SEQRES 7 E 234 PRO ASP ALA ARG VAL LEU SER ASN TYR LEU ARG GLN GLN
SEQRES 8 E 234 CYS ASN TYR SER SER LEU VAL PHE ASN ARG LYS LEU ALA
SEQRES 9 E 234 VAL GLU ARG ALA GLY HIS LEU LEU CYS ASP LYS ALA GLN
SEQRES 10 E 234 LYS ASN THR GLN SER TYR GLY GLY ARG PRO TYR GLY VAL
SEQRES 11 E 234 GLY LEU LEU ILE ILE GLY TYR ASP LYS SER GLY ALA HIS
SEQRES 12 E 234 LEU LEU GLU PHE GLN PRO SER GLY ASN VAL THR GLU LEU
SEQRES 13 E 234 TYR GLY THR ALA ILE GLY ALA ARG SER GLN GLY ALA LYS
SEQRES 14 E 234 THR TYR LEU GLU ARG THR LEU ASP THR PHE ILE LYS ILE
SEQRES 15 E 234 ASP GLY ASN PRO ASP GLU LEU ILE LYS ALA GLY VAL GLU
SEQRES 16 E 234 ALA ILE SER GLN SER LEU ARG ASP GLU SER LEU THR VAL
SEQRES 17 E 234 ASP ASN LEU SER ILE ALA ILE VAL GLY LYS ASP THR PRO
SEQRES 18 E 234 PHE THR ILE TYR ASP GLY GLU ALA VAL ALA LYS TYR ILE
SEQRES 1 F 288 MET THR SER ILE GLY THR GLY TYR ASP LEU SER ASN SER
SEQRES 2 F 288 VAL PHE SER PRO ASP GLY ARG ASN PHE GLN VAL GLU TYR
SEQRES 3 F 288 ALA VAL LYS ALA VAL GLU ASN GLY THR THR SER ILE GLY
SEQRES 4 F 288 ILE LYS CYS ASN ASP GLY VAL VAL PHE ALA VAL GLU LYS
SEQRES 5 F 288 LEU ILE THR SER LYS LEU LEU VAL PRO GLN LYS ASN VAL
SEQRES 6 F 288 LYS ILE GLN VAL VAL ASP ARG HIS ILE GLY CYS VAL TYR
SEQRES 7 F 288 SER GLY LEU ILE PRO ASP GLY ARG HIS LEU VAL ASN ARG
SEQRES 8 F 288 GLY ARG GLU GLU ALA ALA SER PHE LYS LYS LEU TYR LYS
SEQRES 9 F 288 THR PRO ILE PRO ILE PRO ALA PHE ALA ASP ARG LEU GLY
SEQRES 10 F 288 GLN TYR VAL GLN ALA HIS THR LEU TYR ASN SER VAL ARG
SEQRES 11 F 288 PRO PHE GLY VAL SER THR ILE PHE GLY GLY VAL ASP LYS
SEQRES 12 F 288 ASN GLY ALA HIS LEU TYR MET LEU GLU PRO SER GLY SER
SEQRES 13 F 288 TYR TRP GLY TYR LYS GLY ALA ALA THR GLY LYS GLY ARG
SEQRES 14 F 288 GLN SER ALA LYS ALA GLU LEU GLU LYS LEU VAL ASP HIS
SEQRES 15 F 288 HIS PRO GLU GLY LEU SER ALA ARG GLU ALA VAL LYS GLN
SEQRES 16 F 288 ALA ALA LYS ILE ILE TYR LEU ALA HIS GLU ASP ASN LYS
SEQRES 17 F 288 GLU LYS ASP PHE GLU LEU GLU ILE SER TRP CYS SER LEU
SEQRES 18 F 288 SER GLU THR ASN GLY LEU HIS LYS PHE VAL LYS GLY ASP
SEQRES 19 F 288 LEU LEU GLN GLU ALA ILE ASP PHE ALA GLN LYS GLU ILE
SEQRES 20 F 288 ASN GLY ASP ASP ASP GLU ASP GLU ASP ASP SER ASP ASN
SEQRES 21 F 288 VAL MET SER SER ASP ASP GLU ASN ALA PRO VAL ALA THR
SEQRES 22 F 288 ASN ALA ASN ALA THR THR ASP GLN GLU GLY ASP ILE HIS
SEQRES 23 F 288 LEU GLU
SEQRES 1 G 252 MET SER GLY ALA ALA ALA ALA SER ALA ALA GLY TYR ASP
SEQRES 2 G 252 ARG HIS ILE THR ILE PHE SER PRO GLU GLY ARG LEU TYR
SEQRES 3 G 252 GLN VAL GLU TYR ALA PHE LYS ALA THR ASN GLN THR ASN
SEQRES 4 G 252 ILE ASN SER LEU ALA VAL ARG GLY LYS ASP CYS THR VAL
SEQRES 5 G 252 VAL ILE SER GLN LYS LYS VAL PRO ASP LYS LEU LEU ASP
SEQRES 6 G 252 PRO THR THR VAL SER TYR ILE PHE CYS ILE SER ARG THR
SEQRES 7 G 252 ILE GLY MET VAL VAL ASN GLY PRO ILE PRO ASP ALA ARG
SEQRES 8 G 252 ASN ALA ALA LEU ARG ALA LYS ALA GLU ALA ALA GLU PHE
SEQRES 9 G 252 ARG TYR LYS TYR GLY TYR ASP MET PRO CYS ASP VAL LEU
SEQRES 10 G 252 ALA LYS ARG MET ALA ASN LEU SER GLN ILE TYR THR GLN
SEQRES 11 G 252 ARG ALA TYR MET ARG PRO LEU GLY VAL ILE LEU THR PHE
SEQRES 12 G 252 VAL SER VAL ASP GLU GLU LEU GLY PRO SER ILE TYR LYS
SEQRES 13 G 252 THR ASP PRO ALA GLY TYR TYR VAL GLY TYR LYS ALA THR
SEQRES 14 G 252 ALA THR GLY PRO LYS GLN GLN GLU ILE THR THR ASN LEU
SEQRES 15 G 252 GLU ASN HIS PHE LYS LYS SER LYS ILE ASP HIS ILE ASN
SEQRES 16 G 252 GLU GLU SER TRP GLU LYS VAL VAL GLU PHE ALA ILE THR
SEQRES 17 G 252 HIS MET ILE ASP ALA LEU GLY THR GLU PHE SER LYS ASN
SEQRES 18 G 252 ASP LEU GLU VAL GLY VAL ALA THR LYS ASP LYS PHE PHE
SEQRES 19 G 252 THR LEU SER ALA GLU ASN ILE GLU GLU ARG LEU VAL ALA
SEQRES 20 G 252 ILE ALA GLU GLN ASP
SEQRES 1 H 232 THR THR ILE VAL GLY VAL LYS PHE ASN ASN GLY VAL VAL
SEQRES 2 H 232 ILE ALA ALA ASP THR ARG SER THR GLN GLY PRO ILE VAL
SEQRES 3 H 232 ALA ASP LYS ASN CYS ALA LYS LEU HIS ARG ILE SER PRO
SEQRES 4 H 232 LYS ILE TRP CYS ALA GLY ALA GLY THR ALA ALA ASP THR
SEQRES 5 H 232 GLU ALA VAL THR GLN LEU ILE GLY SER ASN ILE GLU LEU
SEQRES 6 H 232 HIS SER LEU TYR THR SER ARG GLU PRO ARG VAL VAL SER
SEQRES 7 H 232 ALA LEU GLN MET LEU LYS GLN HIS LEU PHE LYS TYR GLN
SEQRES 8 H 232 GLY HIS ILE GLY ALA TYR LEU ILE VAL ALA GLY VAL ASP
SEQRES 9 H 232 PRO THR GLY SER HIS LEU PHE SER ILE HIS ALA HIS GLY
SEQRES 10 H 232 SER THR ASP VAL GLY TYR TYR LEU SER LEU GLY SER GLY
SEQRES 11 H 232 SER LEU ALA ALA MET ALA VAL LEU GLU SER HIS TRP LYS
SEQRES 12 H 232 GLN ASP LEU THR LYS GLU GLU ALA ILE LYS LEU ALA SER
SEQRES 13 H 232 ASP ALA ILE GLN ALA GLY ILE TRP ASN ASP LEU GLY SER
SEQRES 14 H 232 GLY SER ASN VAL ASP VAL CYS VAL MET GLU ILE GLY LYS
SEQRES 15 H 232 ASP ALA GLU TYR LEU ARG ASN TYR LEU THR PRO ASN VAL
SEQRES 16 H 232 ARG GLU GLU LYS GLN LYS SER TYR LYS PHE PRO ARG GLY
SEQRES 17 H 232 THR THR ALA VAL LEU LYS GLU SER ILE VAL ASN ILE CYS
SEQRES 18 H 232 ASP ILE GLN GLU GLU GLN VAL ASP ILE THR ALA
SEQRES 1 I 205 MET SER ASP PRO SER SER ILE ASN GLY GLY ILE VAL VAL
SEQRES 2 I 205 ALA MET THR GLY LYS ASP CYS VAL ALA ILE ALA CYS ASP
SEQRES 3 I 205 LEU ARG LEU GLY SER GLN SER LEU GLY VAL SER ASN LYS
SEQRES 4 I 205 PHE GLU LYS ILE PHE HIS TYR GLY HIS VAL PHE LEU GLY
SEQRES 5 I 205 ILE THR GLY LEU ALA THR ASP VAL THR THR LEU ASN GLU
SEQRES 6 I 205 MET PHE ARG TYR LYS THR ASN LEU TYR LYS LEU LYS GLU
SEQRES 7 I 205 GLU ARG ALA ILE GLU PRO GLU THR PHE THR GLN LEU VAL
SEQRES 8 I 205 SER SER SER LEU TYR GLU ARG ARG PHE GLY PRO TYR PHE
SEQRES 9 I 205 VAL GLY PRO VAL VAL ALA GLY ILE ASN SER LYS SER GLY
SEQRES 10 I 205 LYS PRO PHE ILE ALA GLY PHE ASP LEU ILE GLY CYS ILE
SEQRES 11 I 205 ASP GLU ALA LYS ASP PHE ILE VAL SER GLY THR ALA SER
SEQRES 12 I 205 ASP GLN LEU PHE GLY MET CYS GLU SER LEU TYR GLU PRO
SEQRES 13 I 205 ASN LEU GLU PRO GLU ASP LEU PHE GLU THR ILE SER GLN
SEQRES 14 I 205 ALA LEU LEU ASN ALA ALA ASP ARG ASP ALA LEU SER GLY
SEQRES 15 I 205 TRP GLY ALA VAL VAL TYR ILE ILE LYS LYS ASP GLU VAL
SEQRES 16 I 205 VAL LYS ARG TYR LEU LYS MET ARG GLN ASP
SEQRES 1 J 198 MET ASP ILE ILE LEU GLY ILE ARG VAL GLN ASP SER VAL
SEQRES 2 J 198 ILE LEU ALA SER SER LYS ALA VAL THR ARG GLY ILE SER
SEQRES 3 J 198 VAL LEU LYS ASP SER ASP ASP LYS THR ARG GLN LEU SER
SEQRES 4 J 198 PRO HIS THR LEU MET SER PHE ALA GLY GLU ALA GLY ASP
SEQRES 5 J 198 THR VAL GLN PHE ALA GLU TYR ILE GLN ALA ASN ILE GLN
SEQRES 6 J 198 LEU TYR SER ILE ARG GLU ASP TYR GLU LEU SER PRO GLN
SEQRES 7 J 198 ALA VAL SER SER PHE VAL ARG GLN GLU LEU ALA LYS SER
SEQRES 8 J 198 ILE ARG SER ARG ARG PRO TYR GLN VAL ASN VAL LEU ILE
SEQRES 9 J 198 GLY GLY TYR ASP LYS LYS LYS ASN LYS PRO GLU LEU TYR
SEQRES 10 J 198 GLN ILE ASP TYR LEU GLY THR LYS VAL GLU LEU PRO TYR
SEQRES 11 J 198 GLY ALA HIS GLY TYR SER GLY PHE TYR THR PHE SER LEU
SEQRES 12 J 198 LEU ASP HIS HIS TYR ARG PRO ASP MET THR THR GLU GLU
SEQRES 13 J 198 GLY LEU ASP LEU LEU LYS LEU CYS VAL GLN GLU LEU GLU
SEQRES 14 J 198 LYS ARG MET PRO MET ASP PHE LYS GLY VAL ILE VAL LYS
SEQRES 15 J 198 ILE VAL ASP LYS ASP GLY ILE ARG GLN VAL ASP ASP PHE
SEQRES 16 J 198 GLN ALA GLN
SEQRES 1 K 212 THR THR THR LEU ALA PHE ARG PHE GLN GLY GLY ILE ILE
SEQRES 2 K 212 VAL ALA VAL ASP SER ARG ALA THR ALA GLY ASN TRP VAL
SEQRES 3 K 212 ALA SER GLN THR VAL LYS 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 PHE 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 PHE ARG LEU
SEQRES 6 Y 212 HIS GLU LEU ARG GLU LYS GLU ARG ILE SER VAL ALA ALA
SEQRES 7 Y 212 ALA SER LYS ILE LEU SER ASN LEU VAL TYR GLN TYR LYS
SEQRES 8 Y 212 GLY ALA GLY LEU SER MET GLY THR MET ILE CYS GLY TYR
SEQRES 9 Y 212 THR ARG LYS GLU GLY PRO THR ILE TYR TYR VAL ASP SER
SEQRES 10 Y 212 ASP GLY THR ARG LEU LYS GLY ASP ILE PHE CYS VAL GLY
SEQRES 11 Y 212 SER GLY GLN THR PHE ALA TYR GLY VAL LEU ASP SER ASN
SEQRES 12 Y 212 TYR LYS TRP ASP LEU SER VAL GLU ASP ALA LEU TYR LEU
SEQRES 13 Y 212 GLY LYS ARG SER ILE LEU ALA ALA ALA HIS ARG ASP ALA
SEQRES 14 Y 212 TYR SER GLY GLY SER VAL ASN LEU TYR HIS VAL THR GLU
SEQRES 15 Y 212 ASP GLY TRP ILE TYR HIS GLY ASN HIS ASP VAL GLY GLU
SEQRES 16 Y 212 LEU PHE TRP LYS VAL LYS GLU GLU GLU GLY SER PHE ASN
SEQRES 17 Y 212 ASN VAL ILE GLY
SEQRES 1 Z 222 GLN PHE ASN PRO TYR GLY ASP ASN GLY GLY THR ILE LEU
SEQRES 2 Z 222 GLY ILE ALA GLY GLU ASP PHE ALA VAL LEU ALA GLY ASP
SEQRES 3 Z 222 THR ARG ASN ILE THR ASP TYR SER ILE ASN SER ARG TYR
SEQRES 4 Z 222 GLU PRO LYS VAL PHE ASP CYS GLY ASP ASN ILE VAL MET
SEQRES 5 Z 222 SER ALA ASN GLY PHE ALA ALA ASP GLY ASP ALA LEU VAL
SEQRES 6 Z 222 LYS ARG PHE LYS ASN SER VAL LYS TRP TYR HIS PHE ASP
SEQRES 7 Z 222 HIS ASN ASP LYS LYS LEU SER ILE ASN SER ALA ALA ARG
SEQRES 8 Z 222 ASN ILE GLN HIS LEU LEU TYR GLY LYS ARG PHE PHE PRO
SEQRES 9 Z 222 TYR TYR VAL HIS THR ILE ILE ALA GLY LEU ASP GLU ASP
SEQRES 10 Z 222 GLY LYS GLY ALA VAL TYR SER PHE ASP PRO VAL GLY SER
SEQRES 11 Z 222 TYR GLU ARG GLU GLN CYS ARG ALA GLY GLY ALA ALA ALA
SEQRES 12 Z 222 SER LEU ILE MET PRO PHE LEU ASP ASN GLN VAL ASN PHE
SEQRES 13 Z 222 LYS ASN GLN TYR GLU PRO GLY THR ASN GLY LYS VAL LYS
SEQRES 14 Z 222 LYS PRO LEU LYS TYR LEU SER VAL GLU GLU VAL ILE LYS
SEQRES 15 Z 222 LEU VAL ARG ASP SER PHE THR SER ALA THR GLU ARG HIS
SEQRES 16 Z 222 ILE GLN VAL GLY ASP GLY LEU GLU ILE LEU ILE VAL THR
SEQRES 17 Z 222 LYS ASP GLY VAL ARG LYS GLU PHE TYR GLU LEU LYS ARG
SEQRES 18 Z 222 ASP
SEQRES 1 a 246 THR GLN ILE ALA ASN ALA GLY ALA SER PRO MET VAL ASN
SEQRES 2 a 246 THR GLN GLN PRO ILE VAL THR GLY THR SER VAL ILE SER
SEQRES 3 a 246 MET LYS TYR ASP ASN GLY VAL ILE ILE ALA ALA ASP ASN
SEQRES 4 a 246 LEU GLY SER TYR GLY SER LEU LEU ARG PHE ASN GLY VAL
SEQRES 5 a 246 GLU ARG LEU ILE PRO VAL GLY ASP ASN THR VAL VAL GLY
SEQRES 6 a 246 ILE SER GLY ASP ILE SER ASP MET GLN HIS ILE GLU ARG
SEQRES 7 a 246 LEU LEU LYS ASP LEU VAL THR GLU ASN ALA TYR ASP ASN
SEQRES 8 a 246 PRO LEU ALA ASP ALA GLU GLU ALA LEU GLU PRO SER TYR
SEQRES 9 a 246 ILE PHE GLU TYR LEU ALA THR VAL MET TYR GLN ARG ARG
SEQRES 10 a 246 SER LYS MET ASN PRO LEU TRP ASN ALA ILE ILE VAL ALA
SEQRES 11 a 246 GLY VAL GLN SER ASN GLY ASP GLN PHE LEU ARG TYR VAL
SEQRES 12 a 246 ASN LEU LEU GLY VAL THR TYR SER SER PRO THR LEU ALA
SEQRES 13 a 246 THR GLY PHE GLY ALA HIS MET ALA ASN PRO LEU LEU ARG
SEQRES 14 a 246 LYS VAL VAL ASP ARG GLU SER ASP ILE PRO LYS THR THR
SEQRES 15 a 246 VAL GLN VAL ALA GLU GLU ALA ILE VAL ASN ALA MET ARG
SEQRES 16 a 246 VAL LEU TYR TYR ARG ASP ALA ARG SER SER ARG ASN PHE
SEQRES 17 a 246 SER LEU ALA ILE ILE ASP LYS ASN THR GLY LEU THR PHE
SEQRES 18 a 246 LYS LYS ASN LEU GLN VAL GLU ASN MET LYS TRP ASP PHE
SEQRES 19 a 246 ALA LYS ASP ILE LYS GLY TYR GLY THR GLN LYS ILE
SEQRES 1 b 196 THR SER ILE MET ALA VAL THR PHE LYS ASP GLY VAL ILE
SEQRES 2 b 196 LEU GLY ALA ASP SER ARG THR THR THR GLY ALA TYR ILE
SEQRES 3 b 196 ALA ASN ARG VAL THR ASP LYS LEU THR ARG VAL HIS ASP
SEQRES 4 b 196 LYS ILE TRP CYS CYS ARG SER GLY SER ALA ALA ASP THR
SEQRES 5 b 196 GLN ALA ILE ALA ASP ILE VAL GLN TYR HIS LEU GLU LEU
SEQRES 6 b 196 TYR THR SER GLN TYR GLY THR PRO SER THR GLU THR ALA
SEQRES 7 b 196 ALA SER VAL PHE LYS GLU LEU CYS TYR GLU ASN LYS ASP
SEQRES 8 b 196 ASN LEU THR ALA GLY ILE ILE VAL ALA GLY TYR ASP ASP
SEQRES 9 b 196 LYS ASN LYS GLY GLU VAL TYR THR ILE PRO LEU GLY GLY
SEQRES 10 b 196 SER VAL HIS LYS LEU PRO TYR ALA ILE ALA GLY SER GLY
SEQRES 11 b 196 SER THR PHE ILE TYR GLY TYR CYS ASP LYS ASN PHE ARG
SEQRES 12 b 196 GLU ASN MET SER LYS GLU GLU THR VAL ASP PHE ILE LYS
SEQRES 13 b 196 HIS SER LEU SER GLN ALA ILE LYS TRP ASP GLY SER SER
SEQRES 14 b 196 GLY GLY VAL ILE ARG MET VAL VAL LEU THR ALA ALA GLY
SEQRES 15 b 196 VAL GLU ARG LEU ILE PHE TYR PRO ASP GLU TYR GLU GLN
SEQRES 16 b 196 LEU
HET MG G 301 1
HET CL G 302 1
HET 04C H 301 42
HET MES H 302 12
HET MG I 301 1
HET 04C K 301 42
HET MG K 302 1
HET MES K 303 12
HET 04C N 201 42
HET MG N 202 1
HET MG N 203 1
HET CL U 301 1
HET 04C V 301 42
HET MG V 302 1
HET MES V 303 12
HET 04C Y 301 42
HET MG Y 302 1
HET MES Y 303 12
HET MG Z 301 1
HET 04C b 201 42
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
HETNAM 04C 1,2,4-TRIDEOXY-4-METHYL-2-{[N-(MORPHOLIN-4-YLACETYL)-L-
HETNAM 2 04C ALANYL-O-METHYL-L-TYROSYL]AMINO}-1-PHENYL-D-XYLITOL
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
FORMUL 29 MG 8(MG 2+)
FORMUL 30 CL 2(CL 1-)
FORMUL 31 04C 6(C31 H44 N4 O7)
FORMUL 32 MES 4(C6 H13 N O4 S)
FORMUL 49 HOH *455(H2 O)
HELIX 1 1 LEU A 18 GLY A 31 1 14
HELIX 2 2 MET A 78 SER A 96 1 19
HELIX 3 3 TYR A 97 GLY A 102 1 6
HELIX 4 4 PRO A 106 SER A 124 1 19
HELIX 5 5 GLY A 167 TRP A 179 1 13
HELIX 6 6 GLU A 184 VAL A 200 1 17
HELIX 7 7 ASN A 218 LEU A 222 5 5
HELIX 8 8 THR A 239 ALA A 249 1 11
HELIX 9 9 GLY B 1 ASP B 6 5 6
HELIX 10 10 LEU B 18 SER B 29 1 12
HELIX 11 11 LEU B 79 ASN B 102 1 24
HELIX 12 12 PRO B 106 HIS B 124 1 19
HELIX 13 13 ASN B 167 TYR B 179 1 13
HELIX 14 14 LYS B 184 THR B 200 1 17
HELIX 15 15 THR B 206 ASP B 208 5 3
HELIX 16 16 LYS B 230 THR B 241 1 12
HELIX 17 17 ILE C 15 GLY C 28 1 14
HELIX 18 18 LEU C 76 GLU C 99 1 24
HELIX 19 19 THR C 103 TYR C 118 1 16
HELIX 20 20 ASN C 165 TYR C 177 1 13
HELIX 21 21 THR C 185 GLU C 199 1 15
HELIX 22 22 SER C 223 GLN C 239 1 17
HELIX 23 23 LEU D 13 GLY D 26 1 14
HELIX 24 24 GLU D 52 ILE D 56 5 5
HELIX 25 25 ASP D 76 ASP D 96 1 21
HELIX 26 26 ASN D 100 LEU D 113 1 14
HELIX 27 27 GLY D 167 TRP D 179 1 13
HELIX 28 28 THR D 184 MET D 200 1 17
HELIX 29 29 ASP D 224 ALA D 241 1 18
HELIX 30 30 LEU E 18 GLY E 31 1 14
HELIX 31 31 LEU E 76 ASN E 99 1 24
HELIX 32 32 ALA E 103 ASN E 118 1 16
HELIX 33 33 ARG E 163 ILE E 179 1 17
HELIX 34 34 ASN E 184 SER E 197 1 14
HELIX 35 35 GLN E 198 LEU E 200 5 3
HELIX 36 36 ASP E 225 ILE E 233 5 9
HELIX 37 37 ASN F 17 GLY F 30 1 14
HELIX 38 38 LEU F 77 LYS F 100 1 24
HELIX 39 39 PRO F 104 HIS F 119 1 16
HELIX 40 40 GLY F 164 HIS F 179 1 16
HELIX 41 41 SER F 184 HIS F 200 1 17
HELIX 42 42 GLU F 201 LYS F 204 5 4
HELIX 43 43 LYS F 228 ASN F 244 1 17
HELIX 44 44 GLY G 2 HIS G 6 5 5
HELIX 45 45 LEU G 16 THR G 26 1 11
HELIX 46 46 ASN G 27 ASN G 30 5 4
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 MET O 78 SER O 96 1 19
HELIX 89 89 TYR O 97 GLY O 102 1 6
HELIX 90 90 PRO O 106 SER O 124 1 19
HELIX 91 91 GLY O 167 TRP O 179 1 13
HELIX 92 92 GLU O 184 VAL O 200 1 17
HELIX 93 93 ASN O 218 LEU O 222 5 5
HELIX 94 94 THR O 239 ALA O 249 1 11
HELIX 95 95 GLY P 1 ASP P 6 5 6
HELIX 96 96 LEU P 18 SER P 29 1 12
HELIX 97 97 LEU P 79 ASN P 102 1 24
HELIX 98 98 PRO P 106 HIS P 124 1 19
HELIX 99 99 ASN P 167 TYR P 179 1 13
HELIX 100 100 LYS P 184 THR P 200 1 17
HELIX 101 101 THR P 206 ASP P 208 5 3
HELIX 102 102 LYS P 230 THR P 241 1 12
HELIX 103 103 ILE Q 15 GLY Q 28 1 14
HELIX 104 104 LEU Q 76 GLU Q 99 1 24
HELIX 105 105 THR Q 103 TYR Q 118 1 16
HELIX 106 106 ASN Q 165 TYR Q 177 1 13
HELIX 107 107 THR Q 185 GLU Q 199 1 15
HELIX 108 108 SER Q 223 GLN Q 239 1 17
HELIX 109 109 LEU R 13 GLY R 26 1 14
HELIX 110 110 GLU R 52 ILE R 56 5 5
HELIX 111 111 ASP R 76 ASP R 96 1 21
HELIX 112 112 ASN R 100 LEU R 113 1 14
HELIX 113 113 GLY R 167 TRP R 179 1 13
HELIX 114 114 THR R 184 MET R 200 1 17
HELIX 115 115 ASP R 224 ALA R 241 1 18
HELIX 116 116 LEU S 18 GLY S 31 1 14
HELIX 117 117 LEU S 76 ASN S 99 1 24
HELIX 118 118 ALA S 103 ASN S 118 1 16
HELIX 119 119 ARG S 163 ILE S 179 1 17
HELIX 120 120 ASN S 184 SER S 197 1 14
HELIX 121 121 GLN S 198 LEU S 200 5 3
HELIX 122 122 ASP S 225 ILE S 233 5 9
HELIX 123 123 ASN T 17 GLY T 30 1 14
HELIX 124 124 LEU T 77 LYS T 100 1 24
HELIX 125 125 PRO T 104 HIS T 119 1 16
HELIX 126 126 GLY T 164 HIS T 179 1 16
HELIX 127 127 SER T 184 HIS T 200 1 17
HELIX 128 128 GLU T 201 LYS T 204 5 4
HELIX 129 129 LYS T 228 ASN T 244 1 17
HELIX 130 130 GLY U 2 HIS U 6 5 5
HELIX 131 131 LEU U 16 THR U 26 1 11
HELIX 132 132 ASN U 27 ASN U 30 5 4
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 VAL A 44 N ILE A 37
SHEET 4 A 5 ILE A 209 ILE A 214 -1 O ILE A 214 N VAL A 43
SHEET 5 A 5 PHE A 235 LYS A 237 -1 O ARG A 236 N ILE A 213
SHEET 1 B 6 ALA A 56 MET A 57 0
SHEET 2 B 6 TYR G 154 TYR G 157 -1 O GLY G 156 N MET A 57
SHEET 3 B 6 GLY G 142 THR G 148 -1 N ILE G 145 O TYR G 157
SHEET 4 B 6 ILE G 131 ASP G 138 -1 N PHE G 134 O TYR G 146
SHEET 5 B 6 GLY G 71 ASN G 75 -1 N GLY G 71 O VAL G 135
SHEET 6 B 6 ILE G 63 CYS G 65 -1 N PHE G 64 O MET G 72
SHEET 1 C 5 SER A 65 THR A 68 0
SHEET 2 C 5 ILE A 71 GLY A 77 -1 O ALA A 73 N SER A 65
SHEET 3 C 5 VAL A 132 ASP A 140 -1 O ALA A 137 N GLY A 72
SHEET 4 C 5 GLY A 144 VAL A 150 -1 O TYR A 148 N ILE A 136
SHEET 5 C 5 TYR A 156 PRO A 158 -1 O PHE A 157 N GLN A 149
SHEET 1 D 6 TYR A 224 THR A 225 0
SHEET 2 D 6 ALA H 184 LEU H 191 1 O TYR H 186 N THR A 225
SHEET 3 D 6 VAL H 173 GLU H 179 -1 N VAL H 175 O LEU H 187
SHEET 4 D 6 GLY H 11 ASP H 17 -1 N ALA H 16 O ASP H 174
SHEET 5 D 6 THR H 2 PHE H 8 -1 N VAL H 6 O VAL H 13
SHEET 6 D 6 TYR H 124 GLY H 128 -1 O LEU H 125 N GLY H 5
SHEET 1 E 5 ALA B 161 VAL B 164 0
SHEET 2 E 5 ALA B 34 ALA B 39 -1 N GLY B 36 O ILE B 162
SHEET 3 E 5 GLY B 42 GLU B 48 -1 O ALA B 46 N ILE B 35
SHEET 4 E 5 LEU B 210 ARG B 216 -1 O ALA B 213 N LEU B 45
SHEET 5 E 5 TYR B 225 ILE B 228 -1 O LYS B 227 N THR B 214
SHEET 1 F 5 LEU B 65 LYS B 67 0
SHEET 2 F 5 ILE B 72 GLY B 78 -1 O VAL B 74 N TYR B 66
SHEET 3 F 5 VAL B 132 ASP B 140 -1 O ALA B 137 N ALA B 73
SHEET 4 F 5 GLY B 144 SER B 150 -1 O GLN B 146 N GLY B 138
SHEET 5 F 5 TYR B 156 TRP B 159 -1 O TRP B 159 N LEU B 147
SHEET 1 G 5 ALA C 159 ILE C 162 0
SHEET 2 G 5 ALA C 31 LYS C 35 -1 N GLY C 33 O GLN C 160
SHEET 3 G 5 VAL C 40 GLU C 45 -1 O GLY C 43 N VAL C 32
SHEET 4 G 5 ILE C 208 LYS C 214 -1 O THR C 211 N LEU C 42
SHEET 5 G 5 ASP C 218 ALA C 221 -1 O ASP C 218 N LYS C 214
SHEET 1 H 5 SER C 63 LYS C 64 0
SHEET 2 H 5 VAL C 69 GLY C 75 -1 O LEU C 71 N SER C 63
SHEET 3 H 5 VAL C 129 GLY C 135 -1 O ALA C 134 N VAL C 70
SHEET 4 H 5 LYS C 144 THR C 148 -1 O TYR C 146 N ILE C 133
SHEET 5 H 5 TYR C 154 SER C 156 -1 O SER C 155 N GLN C 147
SHEET 1 I 5 ALA D 161 ILE D 164 0
SHEET 2 I 5 ALA D 29 ALA D 33 -1 N ALA D 29 O ILE D 164
SHEET 3 I 5 VAL D 38 GLU D 43 -1 O GLY D 41 N ILE D 30
SHEET 4 I 5 ALA D 209 THR D 215 -1 O SER D 212 N LEU D 40
SHEET 5 I 5 GLY D 219 ILE D 222 -1 O LYS D 221 N CYS D 213
SHEET 1 J 5 ILE D 59 ASP D 63 0
SHEET 2 J 5 ILE D 66 GLY D 72 -1 O CYS D 68 N VAL D 60
SHEET 3 J 5 VAL D 132 ASP D 140 -1 O ALA D 137 N GLY D 67
SHEET 4 J 5 GLY D 144 ALA D 150 -1 O PHE D 148 N ILE D 136
SHEET 5 J 5 PHE D 156 ARG D 158 -1 O TYR D 157 N HIS D 149
SHEET 1 K 5 GLY E 157 ILE E 160 0
SHEET 2 K 5 THR E 34 ARG E 38 -1 N GLY E 36 O THR E 158
SHEET 3 K 5 HIS E 42 LEU E 48 -1 O VAL E 46 N VAL E 35
SHEET 4 K 5 LEU E 210 GLY E 216 -1 O SER E 211 N ALA E 47
SHEET 5 K 5 THR E 219 TYR E 224 -1 O TYR E 224 N ILE E 212
SHEET 1 L 5 ILE E 62 ASP E 66 0
SHEET 2 L 5 MET E 69 GLY E 75 -1 O LEU E 71 N ILE E 63
SHEET 3 L 5 VAL E 129 ASP E 137 -1 O ILE E 134 N GLY E 70
SHEET 4 L 5 GLY E 140 PHE E 146 -1 O LEU E 144 N ILE E 133
SHEET 5 L 5 VAL E 152 GLU E 154 -1 O THR E 153 N GLU E 145
SHEET 1 M 5 GLY F 158 THR F 161 0
SHEET 2 M 5 SER F 33 CYS F 38 -1 N GLY F 35 O ALA F 159
SHEET 3 M 5 GLY F 41 LEU F 49 -1 O VAL F 43 N ILE F 36
SHEET 4 M 5 PHE F 208 SER F 216 -1 O SER F 213 N PHE F 44
SHEET 5 M 5 HIS F 224 PHE F 226 -1 O LYS F 225 N TRP F 214
SHEET 1 N 5 GLN F 64 VAL F 66 0
SHEET 2 N 5 ILE F 70 GLY F 76 -1 O CYS F 72 N GLN F 64
SHEET 3 N 5 VAL F 130 ASP F 138 -1 O ILE F 133 N VAL F 73
SHEET 4 N 5 GLY F 141 LEU F 147 -1 O TYR F 145 N PHE F 134
SHEET 5 N 5 TYR F 153 GLY F 155 -1 O TRP F 154 N MET F 146
SHEET 1 O 5 ALA G 159 THR G 162 0
SHEET 2 O 5 SER G 33 ARG G 37 -1 N SER G 33 O THR G 162
SHEET 3 O 5 THR G 42 GLN G 47 -1 O ILE G 45 N LEU G 34
SHEET 4 O 5 LEU G 214 THR G 220 -1 O GLY G 217 N VAL G 44
SHEET 5 O 5 LYS G 223 THR G 226 -1 O PHE G 225 N VAL G 218
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 ILE H 217 0
SHEET 2 R 6 VAL I 194 LEU I 199 -1 O TYR I 198 N LEU H 213
SHEET 3 R 6 ALA I 184 ILE I 189 -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 ALA I 121 N VAL I 108
SHEET 5 T 5 ILE I 129 GLU I 131 -1 O ASP I 130 N GLY I 122
SHEET 1 U 5 TYR J 130 HIS J 133 0
SHEET 2 U 5 ILE J 4 ARG J 8 -1 N GLY J 6 O GLY J 131
SHEET 3 U 5 VAL J 13 SER J 18 -1 O ALA J 16 N LEU J 5
SHEET 4 U 5 VAL J 179 ASP J 185 -1 O ILE J 180 N SER J 17
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 GLU J 115 N GLY J 106
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 ALA K 15 N LEU K 4
SHEET 4 X 5 SER K 174 THR K 181 -1 O VAL K 180 N ILE K 12
SHEET 5 X 5 GLY K 184 ASP K 192 -1 O 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 ILE L 12 O GLY L 139
SHEET 3 AA 5 ALA L 21 ASP L 26 -1 O ALA L 24 N LEU L 13
SHEET 4 AA 5 GLY L 201 THR L 208 -1 O VAL L 207 N ALA L 21
SHEET 5 AA 5 GLY L 211 GLU L 218 -1 O TYR L 217 N LEU L 202
SHEET 1 AB 2 ASN L 29 THR L 31 0
SHEET 2 AB 2 SER L 34 SER L 37 -1 O ASN L 36 N ASN L 29
SHEET 1 AC 5 PHE L 44 ASP L 45 0
SHEET 2 AC 5 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 HIS L 108 N ASN L 55
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 SER M 138 -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 ALA M 198 N ILE M 22
SHEET 5 AF 5 GLY M 205 GLN M 213 -1 O LYS M 209 N LEU M 197
SHEET 1 AG 5 TYR N 124 ALA N 127 0
SHEET 2 AG 5 ILE N 3 THR N 7 -1 N ALA N 5 O ALA N 125
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 LEU N 178 N VAL N 12
SHEET 5 AG 5 VAL N 183 PHE N 188 -1 O LEU N 186 N MET N 175
SHEET 1 AH 2 THR N 20 THR N 22 0
SHEET 2 AH 2 TYR N 25 ASN N 28 -1 O TYR N 25 N THR N 22
SHEET 1 AI 5 LEU N 34 HIS N 38 0
SHEET 2 AI 5 ILE N 41 GLY N 47 -1 O CYS N 43 N THR N 35
SHEET 3 AI 5 ALA N 95 TYR N 102 -1 O ALA N 100 N TRP N 42
SHEET 4 AI 5 GLY N 108 ILE N 113 -1 O TYR N 111 N VAL N 99
SHEET 5 AI 5 HIS N 120 LEU N 122 -1 O HIS N 120 N THR N 112
SHEET 1 AJ 5 ALA O 161 ILE O 164 0
SHEET 2 AJ 5 SER O 34 LYS O 38 -1 N SER O 34 O ILE O 164
SHEET 3 AJ 5 VAL O 43 GLU O 48 -1 O VAL O 44 N ILE O 37
SHEET 4 AJ 5 ILE O 209 ILE O 214 -1 O ILE O 214 N VAL O 43
SHEET 5 AJ 5 PHE O 235 LYS O 237 -1 O ARG O 236 N ILE O 213
SHEET 1 AK 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 GLY U 71 O VAL U 135
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 ALA O 73 N SER O 65
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 ASP V 17 -1 N ALA V 16 O ASP V 174
SHEET 5 AM 6 THR V 2 PHE V 8 -1 N VAL V 6 O VAL V 13
SHEET 6 AM 6 TYR V 124 GLY V 128 -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 LYS P 227 N THR P 214
SHEET 1 AO 5 LEU P 65 LYS P 67 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 GLN P 146 N GLY P 138
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 THR Q 211 N LEU Q 42
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 LYS Q 64 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 ALA R 33 -1 N ALA R 29 O ILE R 164
SHEET 3 AR 5 VAL R 38 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 TYR S 224 N ILE S 212
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 ILE S 134 N GLY S 70
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 GLU S 154 -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 VAL T 43 N ILE T 36
SHEET 4 AV 5 PHE T 208 SER T 216 -1 O SER T 213 N PHE T 44
SHEET 5 AV 5 HIS T 224 PHE T 226 -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 ALA U 219 N THR U 42
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 ILE V 217 0
SHEET 2 BA 6 VAL W 194 LEU W 199 -1 O TYR W 198 N LEU V 213
SHEET 3 BA 6 ALA W 184 ILE W 189 -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 ALA W 121 N VAL W 108
SHEET 5 BC 5 ILE W 129 ALA W 132 -1 O ASP W 130 N GLY W 122
SHEET 1 BD 5 TYR X 130 HIS X 133 0
SHEET 2 BD 5 ILE X 4 ARG X 8 -1 N GLY X 6 O GLY X 131
SHEET 3 BD 5 VAL X 13 SER X 18 -1 O ALA X 16 N LEU X 5
SHEET 4 BD 5 VAL X 179 ASP X 185 -1 O VAL X 184 N VAL X 13
SHEET 5 BD 5 GLY X 188 VAL X 192 -1 O 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 GLU X 115 N GLY X 106
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 ALA Y 15 N LEU Y 4
SHEET 4 BG 5 SER Y 174 THR Y 181 -1 O VAL Y 180 N ILE Y 12
SHEET 5 BG 5 GLY Y 184 ASP Y 192 -1 O 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 ILE Z 12 O GLY Z 139
SHEET 3 BJ 5 ALA Z 21 ASP Z 26 -1 O ALA Z 24 N LEU Z 13
SHEET 4 BJ 5 GLY Z 201 THR Z 208 -1 O VAL Z 207 N ALA Z 21
SHEET 5 BJ 5 GLY Z 211 GLU Z 218 -1 O TYR Z 217 N LEU Z 202
SHEET 1 BK 2 ASN Z 29 THR Z 31 0
SHEET 2 BK 2 SER Z 34 SER Z 37 -1 O ASN Z 36 N ASN Z 29
SHEET 1 BL 5 PHE Z 44 ASP Z 45 0
SHEET 2 BL 5 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 HIS Z 108 N ASN Z 55
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 SER a 138 -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 ALA a 198 N ILE a 22
SHEET 5 BO 5 GLY a 205 GLN a 213 -1 O LYS a 209 N LEU a 197
SHEET 1 BP 5 TYR b 124 ALA b 127 0
SHEET 2 BP 5 ILE b 3 THR b 7 -1 N ILE b 3 O ALA b 127
SHEET 3 BP 5 GLY b 11 ALA b 16 -1 O GLY b 15 N MET b 4
SHEET 4 BP 5 ILE b 173 THR b 179 -1 O LEU b 178 N VAL b 12
SHEET 5 BP 5 VAL b 183 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 TYR b 102 -1 O ALA b 100 N TRP b 42
SHEET 4 BR 5 GLY b 108 ILE b 113 -1 O TYR b 111 N VAL b 99
SHEET 5 BR 5 HIS b 120 LEU b 122 -1 O HIS b 120 N THR b 112
LINK OG1 THR H 1 C9 04C H 301 1555 1555 1.43
LINK N THR H 1 C10 04C H 301 1555 1555 1.52
LINK OG1 THR K 1 C9 04C K 301 1555 1555 1.44
LINK N THR K 1 C10 04C K 301 1555 1555 1.51
LINK OG1 THR N 1 C9 04C N 201 1555 1555 1.45
LINK N THR N 1 C10 04C N 201 1555 1555 1.53
LINK OG1 THR V 1 C9 04C V 301 1555 1555 1.44
LINK N THR V 1 C10 04C V 301 1555 1555 1.52
LINK OG1 THR Y 1 C9 04C Y 301 1555 1555 1.44
LINK N THR Y 1 C10 04C Y 301 1555 1555 1.51
LINK OG1 THR b 1 C9 04C b 201 1555 1555 1.44
LINK N THR b 1 C10 04C b 201 1555 1555 1.53
LINK OG1 THR G 8 MG MG G 301 1555 1555 2.55
LINK O TYR G 119 MG MG G 301 1555 1555 2.98
LINK O ARG G 122 MG MG G 301 1555 1555 2.63
LINK O MET G 125 MG MG G 301 1555 1555 2.39
LINK OE1 GLN H 91 MG MG N 203 1555 1555 2.66
LINK O ALA I 174 MG MG I 301 1555 1555 2.69
LINK O ASP I 177 MG MG I 301 1555 1555 2.46
LINK O SER I 180 MG MG I 301 1555 1555 2.48
LINK O ASP I 204 MG MG Y 302 1555 1555 2.40
LINK O ALA K 165 MG MG K 302 1555 1555 2.44
LINK O ASP K 168 MG MG K 302 1555 1555 2.27
LINK O SER K 171 MG MG K 302 1555 1555 2.94
LINK MG MG K 302 O ASP W 204 1555 1555 2.48
LINK OXT ASP L 222 MG MG V 302 1555 1555 2.21
LINK OD1 ASP N 51 MG MG N 203 1555 1555 2.46
LINK O ILE N 163 MG MG N 202 1555 1555 2.72
LINK O ASP N 166 MG MG N 202 1555 1555 2.96
LINK O SER N 169 MG MG N 202 1555 1555 2.55
LINK O ILE V 163 MG MG V 302 1555 1555 2.09
LINK O ASP V 166 MG MG V 302 1555 1555 2.18
LINK O SER V 169 MG MG V 302 1555 1555 2.68
LINK O ALA Y 165 MG MG Y 302 1555 1555 2.74
LINK O ASP Y 168 MG MG Y 302 1555 1555 2.25
LINK O SER Y 171 MG MG Y 302 1555 1555 2.87
LINK O THR Z 192 MG MG Z 301 1555 1555 2.65
LINK O VAL Z 198 MG MG Z 301 1555 1555 2.46
SITE 1 AC1 5 THR G 8 TYR G 119 ARG G 122 ALA G 123
SITE 2 AC1 5 MET G 125
SITE 1 AC2 3 ARG G 111 ASN G 114 TYR H 69
SITE 1 AC3 14 THR H 1 ARG H 19 SER H 20 THR H 21
SITE 2 AC3 14 GLN H 22 CYS H 31 GLY H 47 THR H 48
SITE 3 AC3 14 ALA H 49 THR H 52 GLY H 168 MES H 302
SITE 4 AC3 14 HOH H 401 ASP I 124
SITE 1 AC4 4 GLY H 47 SER H 129 04C H 301 TYR Z 33
SITE 1 AC5 4 ALA I 174 ASP I 177 SER I 180 ASP I 204
SITE 1 AC6 13 THR K 1 ARG K 19 ALA K 20 THR K 21
SITE 2 AC6 13 VAL K 31 LYS K 33 GLY K 47 GLY K 48
SITE 3 AC6 13 ALA K 49 TYR K 170 MES K 303 HOH K 401
SITE 4 AC6 13 ASP L 126
SITE 1 AC7 6 ALA K 165 HIS K 166 ASP K 168 ALA K 169
SITE 2 AC7 6 SER K 171 ASP W 204
SITE 1 AC8 9 ARG J 23 THR K 1 GLY K 47 SER K 96
SITE 2 AC8 9 MET K 97 GLY K 98 GLY K 130 SER K 131
SITE 3 AC8 9 04C K 301
SITE 1 AC9 14 THR N 1 ARG N 19 THR N 20 THR N 21
SITE 2 AC9 14 THR N 22 THR N 31 ARG N 45 SER N 46
SITE 3 AC9 14 GLY N 47 SER N 48 ALA N 49 SER N 168
SITE 4 AC9 14 HOH N 301 HOH N 304
SITE 1 BC1 4 ARG N 19 ILE N 163 ASP N 166 SER N 169
SITE 1 BC2 3 GLN H 91 ASP N 51 ASN N 92
SITE 1 BC3 3 ARG U 111 ASN U 114 TYR V 69
SITE 1 BC4 14 THR V 1 ARG V 19 SER V 20 THR V 21
SITE 2 BC4 14 GLN V 22 CYS V 31 GLY V 47 THR V 48
SITE 3 BC4 14 ALA V 49 THR V 52 GLY V 168 MES V 303
SITE 4 BC4 14 HOH V 401 ASP W 124
SITE 1 BC5 4 ASP L 222 ILE V 163 ASP V 166 SER V 169
SITE 1 BC6 4 TYR L 33 GLY V 47 SER V 129 04C V 301
SITE 1 BC7 12 THR Y 1 ARG Y 19 ALA Y 20 THR Y 21
SITE 2 BC7 12 VAL Y 31 LYS Y 33 GLY Y 47 GLY Y 48
SITE 3 BC7 12 ALA Y 49 TYR Y 170 MES Y 303 ASP Z 126
SITE 1 BC8 5 ASP I 204 ALA Y 165 ASP Y 168 ALA Y 169
SITE 2 BC8 5 SER Y 171
SITE 1 BC9 9 ARG X 23 THR Y 1 GLY Y 47 SER Y 96
SITE 2 BC9 9 MET Y 97 GLY Y 98 GLY Y 130 SER Y 131
SITE 3 BC9 9 04C Y 301
SITE 1 CC1 5 ARG Z 28 THR Z 192 HIS Z 195 VAL Z 198
SITE 2 CC1 5 ASP Z 222
SITE 1 CC2 12 THR b 1 ARG b 19 THR b 20 THR b 21
SITE 2 CC2 12 THR b 31 ARG b 45 SER b 46 GLY b 47
SITE 3 CC2 12 SER b 48 ALA b 49 SER b 168 HOH b 301
CRYST1 137.210 300.810 145.090 90.00 113.52 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 0.007288 0.000000 0.003172 0.00000
SCALE2 0.000000 0.003324 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007517 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 -0.999799 -0.000668 0.020033 68.61070 1
MTRIX2 2 -0.002783 -0.985141 -0.171726 -288.91348 1
MTRIX3 2 0.019850 -0.171747 0.984941 -25.49699 1
(ATOM LINES ARE NOT SHOWN.)
END
