HEADER SUGAR BINDING PROTEIN 03-AUG-15 5D0F
TITLE CRYSTAL STRUCTURE OF THE CANDIDA GLABRATA GLYCOGEN DEBRANCHING ENZYME
TITLE 2 (E564Q) IN COMPLEX WITH MALTOPENTAOSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CANDIDA GLABRATA (STRAIN ATCC 2001 / CBS 138 /
SOURCE 3 JCM 3761 / NBRC 0622 / NRRL Y-65);
SOURCE 4 ORGANISM_COMMON: YEAST;
SOURCE 5 ORGANISM_TAXID: 284593;
SOURCE 6 STRAIN: ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
SOURCE 7 GENE: CAGL0G09977G;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21 ROSETTA (DE3);
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PET26B
KEYWDS TIM BARREL, (ALPHA/ALPHA)6 BARREL, HYDROLASE, SUGAR BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR L.ZHAI,S.XIANG
REVDAT 4 08-NOV-23 5D0F 1 HETSYN
REVDAT 3 29-JUL-20 5D0F 1 COMPND REMARK HET HETNAM
REVDAT 3 2 1 HETSYN FORMUL LINK SITE
REVDAT 3 3 1 ATOM
REVDAT 2 14-DEC-16 5D0F 1 COMPND
REVDAT 1 18-MAY-16 5D0F 0
JRNL AUTH L.ZHAI,L.FENG,L.XIA,H.YIN,S.XIANG
JRNL TITL CRYSTAL STRUCTURE OF GLYCOGEN DEBRANCHING ENZYME AND
JRNL TITL 2 INSIGHTS INTO ITS CATALYSIS AND DISEASE-CAUSING MUTATIONS.
JRNL REF NAT COMMUN V. 7 11229 2016
JRNL REFN ESSN 2041-1723
JRNL PMID 27088557
JRNL DOI 10.1038/NCOMMS11229
REMARK 2
REMARK 2 RESOLUTION. 3.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.05
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 3 NUMBER OF REFLECTIONS : 59814
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.130
REMARK 3 FREE R VALUE TEST SET COUNT : 3069
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 49.0587 - 9.2272 0.93 2557 132 0.1596 0.1789
REMARK 3 2 9.2272 - 7.3317 0.96 2610 149 0.1483 0.1697
REMARK 3 3 7.3317 - 6.4072 0.91 2436 141 0.1706 0.2080
REMARK 3 4 6.4072 - 5.8225 0.92 2476 146 0.1813 0.2467
REMARK 3 5 5.8225 - 5.4057 0.95 2568 165 0.1862 0.2171
REMARK 3 6 5.4057 - 5.0873 0.96 2597 130 0.1672 0.2106
REMARK 3 7 5.0873 - 4.8328 0.96 2568 141 0.1639 0.2276
REMARK 3 8 4.8328 - 4.6226 0.96 2623 131 0.1624 0.1902
REMARK 3 9 4.6226 - 4.4447 0.97 2577 154 0.1634 0.1947
REMARK 3 10 4.4447 - 4.2915 0.97 2600 140 0.1712 0.2129
REMARK 3 11 4.2915 - 4.1573 0.97 2606 152 0.1801 0.2072
REMARK 3 12 4.1573 - 4.0386 0.97 2605 138 0.1916 0.2214
REMARK 3 13 4.0386 - 3.9323 0.97 2637 143 0.2049 0.2525
REMARK 3 14 3.9323 - 3.8364 0.98 2614 154 0.2149 0.2458
REMARK 3 15 3.8364 - 3.7492 0.98 2613 127 0.2310 0.2888
REMARK 3 16 3.7492 - 3.6694 0.97 2609 131 0.2417 0.2835
REMARK 3 17 3.6694 - 3.5961 0.97 2614 149 0.2559 0.3196
REMARK 3 18 3.5961 - 3.5282 0.97 2618 117 0.2661 0.3290
REMARK 3 19 3.5282 - 3.4652 0.97 2580 142 0.2862 0.3067
REMARK 3 20 3.4652 - 3.4065 0.95 2580 131 0.2875 0.3267
REMARK 3 21 3.4065 - 3.3516 0.95 2555 119 0.3127 0.3078
REMARK 3 22 3.3516 - 3.3000 0.94 2502 137 0.3172 0.3711
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.430
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.560
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 86.19
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.016 25727
REMARK 3 ANGLE : 2.021 34953
REMARK 3 CHIRALITY : 0.106 3873
REMARK 3 PLANARITY : 0.010 4436
REMARK 3 DIHEDRAL : 19.746 9728
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND ((RESSEQ 3:131))
REMARK 3 ORIGIN FOR THE GROUP (A): 25.3102 -12.3389 49.7385
REMARK 3 T TENSOR
REMARK 3 T11: 0.3017 T22: 1.1846
REMARK 3 T33: 0.5601 T12: -0.1489
REMARK 3 T13: -0.0160 T23: 0.0810
REMARK 3 L TENSOR
REMARK 3 L11: 1.8585 L22: 3.9448
REMARK 3 L33: 2.2014 L12: 0.0873
REMARK 3 L13: 0.3262 L23: 0.4237
REMARK 3 S TENSOR
REMARK 3 S11: 0.1227 S12: -0.0987 S13: -0.0186
REMARK 3 S21: 0.1066 S22: 0.0361 S23: 0.4289
REMARK 3 S31: 0.2129 S32: -0.4133 S33: -0.0747
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'B' AND ((RESSEQ 3:131))
REMARK 3 ORIGIN FOR THE GROUP (A): -16.0887 -4.5048 37.4162
REMARK 3 T TENSOR
REMARK 3 T11: 0.2336 T22: 0.9564
REMARK 3 T33: 0.8357 T12: 0.0537
REMARK 3 T13: 0.0298 T23: -0.1391
REMARK 3 L TENSOR
REMARK 3 L11: 2.4473 L22: 3.7835
REMARK 3 L33: 2.4174 L12: -0.4456
REMARK 3 L13: -0.6722 L23: -0.1251
REMARK 3 S TENSOR
REMARK 3 S11: 0.2187 S12: 0.0185 S13: 0.3685
REMARK 3 S21: 0.0198 S22: 0.0965 S23: -0.4974
REMARK 3 S31: -0.2181 S32: 0.3368 S33: -0.2368
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND ((RESSEQ 132:237) OR (RESSEQ 499:749))
REMARK 3 ORIGIN FOR THE GROUP (A): 48.5051 -26.9550 43.2416
REMARK 3 T TENSOR
REMARK 3 T11: 0.4598 T22: 1.2055
REMARK 3 T33: 0.7481 T12: 0.0762
REMARK 3 T13: -0.1422 T23: 0.0306
REMARK 3 L TENSOR
REMARK 3 L11: 0.9424 L22: 1.1272
REMARK 3 L33: 1.0727 L12: -0.2092
REMARK 3 L13: 0.2928 L23: 0.2340
REMARK 3 S TENSOR
REMARK 3 S11: 0.1945 S12: 0.0336 S13: -0.2879
REMARK 3 S21: 0.0594 S22: 0.0170 S23: -0.0856
REMARK 3 S31: 0.4381 S32: 0.2758 S33: -0.2178
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND ((RESSEQ 132:237) OR (RESSEQ 499:749))
REMARK 3 ORIGIN FOR THE GROUP (A): -39.7287 10.7832 35.7238
REMARK 3 T TENSOR
REMARK 3 T11: 0.5402 T22: 1.0473
REMARK 3 T33: 0.8612 T12: 0.2751
REMARK 3 T13: 0.1899 T23: -0.0212
REMARK 3 L TENSOR
REMARK 3 L11: 0.8561 L22: 1.0649
REMARK 3 L33: 1.3077 L12: -0.3403
REMARK 3 L13: -0.3427 L23: 0.2320
REMARK 3 S TENSOR
REMARK 3 S11: 0.2240 S12: 0.0058 S13: 0.3618
REMARK 3 S21: -0.1192 S22: 0.0161 S23: -0.0951
REMARK 3 S31: -0.5486 S32: -0.3259 S33: -0.2349
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND ((RESSEQ 238:498))
REMARK 3 ORIGIN FOR THE GROUP (A): 32.1848 -32.4819 3.6290
REMARK 3 T TENSOR
REMARK 3 T11: 0.6563 T22: 1.3517
REMARK 3 T33: 0.7927 T12: -0.0652
REMARK 3 T13: -0.1067 T23: -0.0565
REMARK 3 L TENSOR
REMARK 3 L11: 0.5682 L22: 2.0424
REMARK 3 L33: 3.3215 L12: -0.5969
REMARK 3 L13: 1.3404 L23: -1.1399
REMARK 3 S TENSOR
REMARK 3 S11: 0.1127 S12: 0.2924 S13: -0.0035
REMARK 3 S21: -0.0350 S22: 0.0103 S23: -0.2872
REMARK 3 S31: 0.3557 S32: 0.3257 S33: -0.1364
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND ((RESSEQ 238:498))
REMARK 3 ORIGIN FOR THE GROUP (A): -31.8589 15.4727 -6.5177
REMARK 3 T TENSOR
REMARK 3 T11: 1.0377 T22: 1.4447
REMARK 3 T33: 1.0605 T12: 0.3197
REMARK 3 T13: 0.2055 T23: 0.1033
REMARK 3 L TENSOR
REMARK 3 L11: 0.7472 L22: 0.7049
REMARK 3 L33: 3.4191 L12: 0.1082
REMARK 3 L13: -0.9024 L23: 1.1337
REMARK 3 S TENSOR
REMARK 3 S11: -0.0765 S12: 0.4357 S13: -0.0997
REMARK 3 S21: -0.1226 S22: -0.0465 S23: 0.4674
REMARK 3 S31: -0.4445 S32: -0.5943 S33: 0.0273
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND ((RESSEQ 750:869))
REMARK 3 ORIGIN FOR THE GROUP (A): 71.2446 -12.3502 45.2424
REMARK 3 T TENSOR
REMARK 3 T11: -0.1853 T22: 1.7831
REMARK 3 T33: 0.6646 T12: 0.2188
REMARK 3 T13: -0.1703 T23: -0.0550
REMARK 3 L TENSOR
REMARK 3 L11: 2.2743 L22: 1.0844
REMARK 3 L33: 1.2607 L12: 0.9830
REMARK 3 L13: 0.9472 L23: 0.1447
REMARK 3 S TENSOR
REMARK 3 S11: 0.0523 S12: 0.1454 S13: 0.0315
REMARK 3 S21: -0.1609 S22: -0.0623 S23: -0.1770
REMARK 3 S31: 0.2669 S32: 0.5254 S33: -0.0163
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND ((RESSEQ 750:869))
REMARK 3 ORIGIN FOR THE GROUP (A): -61.9593 -3.1004 42.6296
REMARK 3 T TENSOR
REMARK 3 T11: 0.0638 T22: 1.5879
REMARK 3 T33: 0.7536 T12: 0.3531
REMARK 3 T13: 0.0854 T23: 0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 1.8903 L22: 1.2641
REMARK 3 L33: 1.7061 L12: 0.6341
REMARK 3 L13: -1.0746 L23: -0.0861
REMARK 3 S TENSOR
REMARK 3 S11: 0.1030 S12: -0.0120 S13: 0.0424
REMARK 3 S21: -0.1326 S22: -0.1704 S23: -0.0490
REMARK 3 S31: -0.1209 S32: -0.6330 S33: 0.1067
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND ((RESSEQ 870:1022))
REMARK 3 ORIGIN FOR THE GROUP (A): 45.0922 15.2641 59.5814
REMARK 3 T TENSOR
REMARK 3 T11: 0.1879 T22: 1.2857
REMARK 3 T33: 0.6689 T12: -0.1189
REMARK 3 T13: -0.0921 T23: -0.0568
REMARK 3 L TENSOR
REMARK 3 L11: 1.2749 L22: 3.1841
REMARK 3 L33: 1.9170 L12: -0.1269
REMARK 3 L13: 0.2673 L23: 0.4150
REMARK 3 S TENSOR
REMARK 3 S11: -0.0565 S12: -0.1347 S13: 0.2989
REMARK 3 S21: 0.3960 S22: 0.1530 S23: -0.5617
REMARK 3 S31: -0.3260 S32: 0.3326 S33: -0.0277
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND ((RESSEQ 870:1022))
REMARK 3 ORIGIN FOR THE GROUP (A): -34.3291 -31.2817 51.4234
REMARK 3 T TENSOR
REMARK 3 T11: 0.3283 T22: 1.0095
REMARK 3 T33: 0.8026 T12: 0.1138
REMARK 3 T13: 0.1195 T23: 0.1661
REMARK 3 L TENSOR
REMARK 3 L11: 2.2239 L22: 3.6128
REMARK 3 L33: 2.3869 L12: -0.4763
REMARK 3 L13: -0.4164 L23: -0.0665
REMARK 3 S TENSOR
REMARK 3 S11: -0.2034 S12: -0.3473 S13: -0.3786
REMARK 3 S21: 0.5226 S22: 0.2437 S23: 0.7248
REMARK 3 S31: 0.2719 S32: -0.3750 S33: -0.0618
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'A' AND ((RESSEQ 1023:1528))
REMARK 3 ORIGIN FOR THE GROUP (A): 12.4097 32.1155 52.4465
REMARK 3 T TENSOR
REMARK 3 T11: 0.4492 T22: 1.0962
REMARK 3 T33: 1.3410 T12: 0.2099
REMARK 3 T13: -0.0533 T23: 0.0494
REMARK 3 L TENSOR
REMARK 3 L11: 2.1174 L22: 3.7112
REMARK 3 L33: 2.0070 L12: 0.3744
REMARK 3 L13: 0.4684 L23: 0.4125
REMARK 3 S TENSOR
REMARK 3 S11: -0.1333 S12: -0.1331 S13: 0.8435
REMARK 3 S21: -0.2353 S22: 0.0197 S23: 1.2993
REMARK 3 S31: -0.5442 S32: -0.5752 S33: 0.1376
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND ((RESSEQ 1023:1528))
REMARK 3 ORIGIN FOR THE GROUP (A): -4.7216 -49.3335 37.2582
REMARK 3 T TENSOR
REMARK 3 T11: 0.5525 T22: 0.8950
REMARK 3 T33: 1.0237 T12: 0.3140
REMARK 3 T13: -0.0190 T23: -0.0944
REMARK 3 L TENSOR
REMARK 3 L11: 2.0045 L22: 3.0695
REMARK 3 L33: 2.4916 L12: 0.0444
REMARK 3 L13: -0.4666 L23: -0.3518
REMARK 3 S TENSOR
REMARK 3 S11: -0.2775 S12: -0.0950 S13: -0.7970
REMARK 3 S21: -0.0160 S22: 0.1829 S23: -0.1976
REMARK 3 S31: 0.7356 S32: 0.4950 S33: 0.1067
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5D0F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-AUG-15.
REMARK 100 THE DEPOSITION ID IS D_1000212482.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-APR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM 7.2.0
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.21
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59857
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300
REMARK 200 RESOLUTION RANGE LOW (A) : 132.609
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.48
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.48800
REMARK 200 R SYM FOR SHELL (I) : 0.48800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP 11.2.08
REMARK 200 STARTING MODEL: 5D06
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 5000 MME, 0.1 M HEPES, 5%
REMARK 280 TACSIMATE PH 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 79.03500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 101.00500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 79.03500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 101.00500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, D, E, F, G, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, I, J, K, L, M
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 A 1
REMARK 465 SER A 2
REMARK 465 MET B 1
REMARK 465 SER B 2
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 O ALA A 1062 OE1 GLN A 1508 1.92
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 31 C - N - CA ANGL. DEV. = 9.4 DEGREES
REMARK 500 ARG A 61 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 533 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A1014 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A1014 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A1469 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG A1474 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ALA A1488 N - CA - CB ANGL. DEV. = 8.8 DEGREES
REMARK 500 ARG B 61 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG B 79 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG B 533 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG B 553 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ASP B 640 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 PRO B 652 C - N - CA ANGL. DEV. = -9.1 DEGREES
REMARK 500 ARG B 984 N - CA - CB ANGL. DEV. = 11.3 DEGREES
REMARK 500 ARG B1014 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG B1014 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG B1469 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG B1469 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG B1474 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 HIS A 4 109.13 -55.41
REMARK 500 ASP A 13 -36.95 -36.89
REMARK 500 GLN A 25 107.65 -47.00
REMARK 500 PRO A 31 137.49 -30.32
REMARK 500 PRO A 58 -28.05 -39.68
REMARK 500 GLN A 76 151.17 -46.76
REMARK 500 ASN A 115 174.39 -53.60
REMARK 500 ASP A 118 14.73 54.53
REMARK 500 ASN A 137 -81.48 -134.71
REMARK 500 ASP A 202 113.08 -39.44
REMARK 500 ARG A 218 -70.04 -61.27
REMARK 500 HIS A 246 66.51 -150.77
REMARK 500 LYS A 268 40.65 -89.23
REMARK 500 LEU A 269 -39.52 -136.08
REMARK 500 ALA A 278 4.55 -68.64
REMARK 500 PRO A 282 40.04 -106.88
REMARK 500 VAL A 302 -44.34 -130.54
REMARK 500 LYS A 307 60.79 65.72
REMARK 500 LEU A 308 7.92 50.11
REMARK 500 TRP A 309 74.24 59.71
REMARK 500 GLU A 310 -13.50 -49.49
REMARK 500 ASN A 329 -49.30 -132.96
REMARK 500 SER A 330 37.00 -90.42
REMARK 500 LYS A 331 -123.00 47.11
REMARK 500 SER A 332 -166.00 -119.36
REMARK 500 SER A 368 37.41 -97.97
REMARK 500 ASN A 390 59.38 -95.47
REMARK 500 GLU A 394 -71.17 -64.56
REMARK 500 ASP A 433 -81.47 -121.54
REMARK 500 LYS A 437 67.38 -157.18
REMARK 500 PRO A 440 -79.54 -57.13
REMARK 500 LEU A 445 57.90 -164.54
REMARK 500 PRO A 450 108.79 -45.45
REMARK 500 ALA A 464 84.51 -155.29
REMARK 500 SER A 511 34.24 -150.51
REMARK 500 SER A 539 40.25 -105.42
REMARK 500 ASN A 558 38.85 -95.61
REMARK 500 MET A 590 -4.62 -59.33
REMARK 500 PRO A 609 159.78 -44.56
REMARK 500 SER A 612 145.72 -39.54
REMARK 500 LEU A 618 -114.13 -120.84
REMARK 500 TYR A 633 53.82 34.97
REMARK 500 SER A 647 -167.57 -122.93
REMARK 500 MET A 650 37.71 -87.71
REMARK 500 ARG A 678 -101.35 -128.46
REMARK 500 THR A 683 -34.62 -38.93
REMARK 500 SER A 695 170.22 177.43
REMARK 500 VAL A 714 -64.15 -99.21
REMARK 500 ALA A 723 97.33 -52.63
REMARK 500 GLU A 745 -77.45 -63.97
REMARK 500
REMARK 500 THIS ENTRY HAS 197 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LEU A 306 LYS A 307 144.66
REMARK 500 THR A 442 LYS A 443 147.68
REMARK 500 GLU A 1492 LEU A 1493 -140.22
REMARK 500 GLN B 241 TRP B 242 149.33
REMARK 500 LEU B 306 LYS B 307 145.73
REMARK 500 THR B 442 LYS B 443 147.48
REMARK 500 GLU B 1492 LEU B 1493 -141.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 GLC E 1
REMARK 610 GLC H 1
REMARK 610 GLC K 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5D06 RELATED DB: PDB
DBREF 5D0F A 1 1528 UNP Q6FSK0 Q6FSK0_CANGA 1 1528
DBREF 5D0F B 1 1528 UNP Q6FSK0 Q6FSK0_CANGA 1 1528
SEQADV 5D0F GLN A 564 UNP Q6FSK0 GLU 564 ENGINEERED MUTATION
SEQADV 5D0F GLN B 564 UNP Q6FSK0 GLU 564 ENGINEERED MUTATION
SEQRES 1 A 1528 MET SER ALA HIS ARG THR LEU LEU LEU ARG LEU SER ASP
SEQRES 2 A 1528 SER GLY GLU PRO VAL THR SER CYS SER TYR GLY GLN GLY
SEQRES 3 A 1528 VAL LEU THR LEU PRO SER LEU PRO LEU PRO GLN GLY LYS
SEQRES 4 A 1528 LYS LEU GLY ASP MET PRO VAL TYR THR VAL LYS LEU ALA
SEQRES 5 A 1528 ILE PRO ALA GLY SER PRO VAL THR ARG ASP GLY LEU ILE
SEQRES 6 A 1528 TRP THR ASN CYS PRO PRO ASP PHE SER THR GLN PHE ASP
SEQRES 7 A 1528 ARG GLU LYS PHE TYR LYS LYS ILE ILE LYS THR SER PHE
SEQRES 8 A 1528 HIS GLU ASP ASP HIS ILE ASP LEU ASP ILE TYR VAL PRO
SEQRES 9 A 1528 GLY THR TYR CYS PHE TYR LEU SER PHE LYS ASN ASP LYS
SEQRES 10 A 1528 ASP GLU LEU GLU THR THR ARG LYS PHE TYR PHE VAL VAL
SEQRES 11 A 1528 LEU PRO ILE LEU SER VAL ASN ASP LYS PHE ILE PRO LEU
SEQRES 12 A 1528 ASN SER ILE ALA MET GLN SER VAL VAL SER LYS TRP MET
SEQRES 13 A 1528 GLY PRO THR ILE LYS ASP TRP GLU LYS VAL PHE ALA ARG
SEQRES 14 A 1528 VAL ALA SER LYS LYS TYR ASN MET ILE HIS PHE THR PRO
SEQRES 15 A 1528 LEU GLN HIS ARG GLY GLU SER ASN SER PRO TYR SER ILE
SEQRES 16 A 1528 TYR ASP GLN LEU GLU PHE ASP PRO THR VAL PHE LYS SER
SEQRES 17 A 1528 GLU LYS GLU VAL ALA ASP MET VAL GLU ARG LEU ARG THR
SEQRES 18 A 1528 GLU HIS ASN ILE LEU SER LEU THR ASP ILE VAL PHE ASN
SEQRES 19 A 1528 HIS THR ALA ASN ASN SER GLN TRP LEU LEU ASP HIS PRO
SEQRES 20 A 1528 GLU ALA GLY TYR ASN HIS LYS THR SER PRO HIS LEU ILE
SEQRES 21 A 1528 SER ALA ILE GLU LEU ASP LYS LYS LEU LEU ASP PHE SER
SEQRES 22 A 1528 GLU GLN MET GLU ALA LEU GLY TYR PRO VAL ASP LEU LYS
SEQRES 23 A 1528 THR VAL ASP ASP LEU ILE LYS VAL MET ASP GLY ILE LYS
SEQRES 24 A 1528 GLU HIS VAL ILE GLY GLU LEU LYS LEU TRP GLU PHE TYR
SEQRES 25 A 1528 VAL VAL ASP VAL LYS GLN THR VAL SER GLU LEU ARG GLU
SEQRES 26 A 1528 LYS TRP GLY ASN SER LYS SER TRP SER ASP ASP ASN ILE
SEQRES 27 A 1528 PRO SER LYS ASP ASP SER THR ASN LEU ALA GLN PHE VAL
SEQRES 28 A 1528 ARG ASP ASN ALA THR GLU PRO GLY PHE GLY SER LEU GLY
SEQRES 29 A 1528 GLU ARG GLY SER ASN LYS ILE ASN ILE ASP LYS PHE ALA
SEQRES 30 A 1528 ALA ILE LEU LYS LYS LEU HIS SER GLU ASP TYR ASN ASN
SEQRES 31 A 1528 GLY ILE GLU GLU LEU ALA THR LYS ILE LEU ASN ASP ILE
SEQRES 32 A 1528 ASN LEU PRO PHE TYR LYS GLU TYR ASP ASP ASP ILE ASN
SEQRES 33 A 1528 GLU VAL LEU GLU GLN LEU PHE ASN ARG ILE LYS TYR LEU
SEQRES 34 A 1528 ARG ILE ASP ASP HIS GLY PRO LYS GLN GLY PRO ILE THR
SEQRES 35 A 1528 LYS LYS LEU PRO LEU SER GLU PRO TYR PHE THR ARG PHE
SEQRES 36 A 1528 LYS ALA LYS ASP GLY GLU GLU TYR ALA LEU ALA ASN ASN
SEQRES 37 A 1528 GLY TRP ILE TRP ASP GLY ASN PRO LEU VAL ASP PHE ALA
SEQRES 38 A 1528 SER SER GLN SER LYS ALA TYR LEU ARG ARG GLU VAL ILE
SEQRES 39 A 1528 VAL TRP GLY ASP CYS VAL LYS LEU ARG TYR GLY LYS GLY
SEQRES 40 A 1528 PRO SER ASP SER PRO TYR LEU TRP GLU ARG MET SER LYS
SEQRES 41 A 1528 TYR VAL GLU MET ASN ALA ARG ILE PHE ASN GLY PHE ARG
SEQRES 42 A 1528 ILE ASP ASN CYS HIS SER THR PRO LEU HIS VAL GLY GLN
SEQRES 43 A 1528 TYR PHE LEU ASP VAL ALA ARG ARG VAL ASN PRO ASN LEU
SEQRES 44 A 1528 TYR VAL VAL ALA GLN LEU PHE SER GLY SER GLU ALA MET
SEQRES 45 A 1528 ASP CYS LEU PHE VAL GLU ARG LEU GLY ILE SER SER LEU
SEQRES 46 A 1528 ILE ARG GLU ALA MET GLN ALA TRP SER GLU GLU GLU LEU
SEQRES 47 A 1528 SER ARG LEU VAL HIS ARG HIS GLY GLY ARG PRO ILE GLY
SEQRES 48 A 1528 SER TYR LYS PHE VAL PRO LEU ASP ASP PHE PRO TYR PRO
SEQRES 49 A 1528 ALA ASP VAL LYS ILE ASP GLU GLU TYR CYS ALA TYR ASN
SEQRES 50 A 1528 PRO ASP ASP HIS SER VAL LYS CYS VAL SER GLU ILE MET
SEQRES 51 A 1528 ILE PRO LYS THR LEU THR ALA THR PRO PRO HIS ALA LEU
SEQRES 52 A 1528 PHE MET ASP CYS THR HIS ASP ASN GLU THR PRO ASN GLN
SEQRES 53 A 1528 LYS ARG THR VAL GLU ASP THR LEU PRO ASN ALA ALA LEU
SEQRES 54 A 1528 VAL ALA PHE CYS SER SER ALA ILE GLY SER VAL TYR GLY
SEQRES 55 A 1528 TYR ASP GLU VAL PHE PRO GLN LEU LEU ASP LEU VAL GLN
SEQRES 56 A 1528 GLU LYS ARG THR TYR SER CYS ALA GLU ASN THR GLY ILE
SEQRES 57 A 1528 SER LYS VAL LYS THR LEU LEU ASN ASN MET ARG GLU GLU
SEQRES 58 A 1528 ILE ALA SER GLU ALA VAL ASP ILE GLU ASP SER GLU MET
SEQRES 59 A 1528 HIS VAL HIS HIS ASP GLY GLN TYR ILE THR PHE HIS ARG
SEQRES 60 A 1528 THR ASN ALA LYS ASN GLY LYS GLY TRP TYR LEU VAL ALA
SEQRES 61 A 1528 ARG THR LYS PHE HIS SER SER GLY ASP GLN MET LEU PRO
SEQRES 62 A 1528 ARG ILE LYS LEU SER GLN THR LYS ALA THR PHE LYS ALA
SEQRES 63 A 1528 ALA PHE SER LEU GLU ARG THR GLY ASP ALA PRO ILE SER
SEQRES 64 A 1528 ASP GLU ILE ILE GLU GLY ILE PRO THR LYS LEU ARG GLU
SEQRES 65 A 1528 LEU THR GLY PHE ASP ILE GLY PHE ASP GLU ASN THR LYS
SEQRES 66 A 1528 GLU THR SER ILE LEU LEU PRO GLN ASP PHE PRO GLN GLY
SEQRES 67 A 1528 SER ILE VAL ILE PHE GLU THR GLN GLN LEU GLY ILE ASP
SEQRES 68 A 1528 ASP SER LEU ASP HIS PHE ILE ARG SER GLY ALA ILE LYS
SEQRES 69 A 1528 ALA THR GLU LYS LEU SER LEU GLU SER ILE ASN TYR VAL
SEQRES 70 A 1528 LEU TYR ARG ALA GLU GLN GLU GLU TYR ASP TYR SER GLU
SEQRES 71 A 1528 GLY ARG SER GLY ALA TYR ASP ILE PRO ASP TYR GLY LYS
SEQRES 72 A 1528 PRO VAL TYR CYS GLY LEU GLN GLY TRP VAL SER ILE LEU
SEQRES 73 A 1528 ARG LYS ILE ILE PHE TYR ASN ASP LEU ALA HIS PRO LEU
SEQRES 74 A 1528 SER ASN ASN LEU ARG ASN GLY HIS TRP ALA VAL ASP TYR
SEQRES 75 A 1528 VAL VAL ASN ARG LEU ASP LEU TYR LYS ASP LYS GLU GLY
SEQRES 76 A 1528 VAL ALA GLU VAL GLN GLU TRP LEU ARG SER ARG MET GLU
SEQRES 77 A 1528 ARG ILE LYS GLN LEU PRO SER TYR LEU VAL PRO SER PHE
SEQRES 78 A 1528 PHE ALA LEU VAL VAL GLY ILE MET TYR GLY CYS CYS ARG
SEQRES 79 A 1528 LEU ARG ALA MET GLN LEU MET SER ASP ASN VAL GLY LYS
SEQRES 80 A 1528 SER THR VAL PHE VAL GLN SER LEU ALA MET THR SER ILE
SEQRES 81 A 1528 GLN MET VAL SER ALA MET LYS SER THR SER ILE LEU PRO
SEQRES 82 A 1528 ASP GLN ASN ILE ALA ALA MET ALA ALA GLY LEU PRO HIS
SEQRES 83 A 1528 PHE SER THR ASN TYR MET ARG CYS TRP GLY ARG ASP VAL
SEQRES 84 A 1528 PHE ILE SER LEU ARG GLY LEU LEU LEU THR THR GLY ARG
SEQRES 85 A 1528 TYR GLU GLU ALA LYS GLU HIS ILE LEU ALA PHE ALA LYS
SEQRES 86 A 1528 THR LEU LYS HIS GLY LEU ILE PRO ASN LEU LEU ASP ALA
SEQRES 87 A 1528 GLY ARG ASN PRO ARG TYR ASN ALA ARG ASP ALA ALA TRP
SEQRES 88 A 1528 PHE PHE VAL GLN ALA ILE GLN ASP TYR VAL THR ILE VAL
SEQRES 89 A 1528 PRO GLY GLY VAL SER LEU LEU GLN GLU LYS VAL THR ARG
SEQRES 90 A 1528 ARG PHE PRO LEU ASP ASP GLU TYR ILE PRO TYR ASP ASP
SEQRES 91 A 1528 PRO LYS ALA PHE SER TYR SER SER THR ILE GLU GLU ILE
SEQRES 92 A 1528 ILE TYR GLU ILE LEU ASN ARG HIS ALA GLY GLY ILE LYS
SEQRES 93 A 1528 TYR ARG GLU ALA ASN ALA GLY PRO ASN LEU ASP ARG VAL
SEQRES 94 A 1528 MET LYS ASP GLU GLY PHE ASN VAL GLU VAL ASN VAL ASP
SEQRES 95 A 1528 TRP GLU THR GLY LEU ILE HIS GLY GLY SER GLN PHE ASN
SEQRES 96 A 1528 CYS GLY THR TRP MET ASP LYS MET GLY GLU SER GLU LYS
SEQRES 97 A 1528 ALA ASN SER VAL GLY VAL PRO GLY THR PRO ARG ASP GLY
SEQRES 98 A 1528 ALA ALA VAL GLU ILE ASN GLY LEU LEU LYS SER CYS LEU
SEQRES 99 A 1528 ARG PHE VAL LEU GLN LEU SER LYS ASP GLY LYS PHE LYS
SEQRES 100 A 1528 TYR THR GLU VAL THR LYS PRO ASP GLY SER LYS ILE SER
SEQRES 101 A 1528 LEU SER SER TRP ASN ASP LEU LEU GLN GLU ASN PHE GLU
SEQRES 102 A 1528 ARG CYS PHE TYR VAL PRO LYS ASN LYS GLU ASP ASP ASN
SEQRES 103 A 1528 LYS PHE GLU ILE ASP ALA THR ILE ILE ASN ARG ARG GLY
SEQRES 104 A 1528 ILE TYR LYS ASP LEU TYR ARG SER GLY LYS PRO TYR GLU
SEQRES 105 A 1528 ASP TYR GLN PHE ARG PRO ASN PHE THR ILE ALA MET VAL
SEQRES 106 A 1528 VAL ALA PRO GLU LEU PHE THR PRO ASP TYR ALA ALA GLY
SEQRES 107 A 1528 ALA ILE GLU LEU ALA ASP GLN VAL LEU ARG GLY PRO VAL
SEQRES 108 A 1528 GLY MET ARG THR LEU ASP PRO SER ASP TYR ASN TYR ARG
SEQRES 109 A 1528 PRO TYR TYR ASN ASN GLY GLU ASP SER ASP ASP PHE ALA
SEQRES 110 A 1528 THR SER LYS GLY ARG ASN TYR HIS GLN GLY PRO GLU TRP
SEQRES 111 A 1528 VAL TRP CYS TYR GLY TYR PHE ILE ARG ALA TYR HIS TYR
SEQRES 112 A 1528 PHE ASN PHE LEU THR ASN PRO LYS CYS GLN VAL GLU GLY
SEQRES 113 A 1528 SER ALA LYS LYS LEU LYS PRO SER SER TYR LEU TYR ARG
SEQRES 114 A 1528 LYS LEU TYR SER ARG LEU LEU LYS HIS ARG GLU TRP ILE
SEQRES 115 A 1528 GLU ASN SER PRO TRP ALA GLY LEU ALA GLU LEU THR ASN
SEQRES 116 A 1528 LYS ASP GLY GLU VAL CYS ASN ASP SER SER PRO THR GLN
SEQRES 117 A 1528 ALA TRP SER THR GLY CYS LEU LEU ASP LEU PHE TYR ASP
SEQRES 118 A 1528 LEU TRP ILE SER TYR GLU GLU
SEQRES 1 B 1528 MET SER ALA HIS ARG THR LEU LEU LEU ARG LEU SER ASP
SEQRES 2 B 1528 SER GLY GLU PRO VAL THR SER CYS SER TYR GLY GLN GLY
SEQRES 3 B 1528 VAL LEU THR LEU PRO SER LEU PRO LEU PRO GLN GLY LYS
SEQRES 4 B 1528 LYS LEU GLY ASP MET PRO VAL TYR THR VAL LYS LEU ALA
SEQRES 5 B 1528 ILE PRO ALA GLY SER PRO VAL THR ARG ASP GLY LEU ILE
SEQRES 6 B 1528 TRP THR ASN CYS PRO PRO ASP PHE SER THR GLN PHE ASP
SEQRES 7 B 1528 ARG GLU LYS PHE TYR LYS LYS ILE ILE LYS THR SER PHE
SEQRES 8 B 1528 HIS GLU ASP ASP HIS ILE ASP LEU ASP ILE TYR VAL PRO
SEQRES 9 B 1528 GLY THR TYR CYS PHE TYR LEU SER PHE LYS ASN ASP LYS
SEQRES 10 B 1528 ASP GLU LEU GLU THR THR ARG LYS PHE TYR PHE VAL VAL
SEQRES 11 B 1528 LEU PRO ILE LEU SER VAL ASN ASP LYS PHE ILE PRO LEU
SEQRES 12 B 1528 ASN SER ILE ALA MET GLN SER VAL VAL SER LYS TRP MET
SEQRES 13 B 1528 GLY PRO THR ILE LYS ASP TRP GLU LYS VAL PHE ALA ARG
SEQRES 14 B 1528 VAL ALA SER LYS LYS TYR ASN MET ILE HIS PHE THR PRO
SEQRES 15 B 1528 LEU GLN HIS ARG GLY GLU SER ASN SER PRO TYR SER ILE
SEQRES 16 B 1528 TYR ASP GLN LEU GLU PHE ASP PRO THR VAL PHE LYS SER
SEQRES 17 B 1528 GLU LYS GLU VAL ALA ASP MET VAL GLU ARG LEU ARG THR
SEQRES 18 B 1528 GLU HIS ASN ILE LEU SER LEU THR ASP ILE VAL PHE ASN
SEQRES 19 B 1528 HIS THR ALA ASN ASN SER GLN TRP LEU LEU ASP HIS PRO
SEQRES 20 B 1528 GLU ALA GLY TYR ASN HIS LYS THR SER PRO HIS LEU ILE
SEQRES 21 B 1528 SER ALA ILE GLU LEU ASP LYS LYS LEU LEU ASP PHE SER
SEQRES 22 B 1528 GLU GLN MET GLU ALA LEU GLY TYR PRO VAL ASP LEU LYS
SEQRES 23 B 1528 THR VAL ASP ASP LEU ILE LYS VAL MET ASP GLY ILE LYS
SEQRES 24 B 1528 GLU HIS VAL ILE GLY GLU LEU LYS LEU TRP GLU PHE TYR
SEQRES 25 B 1528 VAL VAL ASP VAL LYS GLN THR VAL SER GLU LEU ARG GLU
SEQRES 26 B 1528 LYS TRP GLY ASN SER LYS SER TRP SER ASP ASP ASN ILE
SEQRES 27 B 1528 PRO SER LYS ASP ASP SER THR ASN LEU ALA GLN PHE VAL
SEQRES 28 B 1528 ARG ASP ASN ALA THR GLU PRO GLY PHE GLY SER LEU GLY
SEQRES 29 B 1528 GLU ARG GLY SER ASN LYS ILE ASN ILE ASP LYS PHE ALA
SEQRES 30 B 1528 ALA ILE LEU LYS LYS LEU HIS SER GLU ASP TYR ASN ASN
SEQRES 31 B 1528 GLY ILE GLU GLU LEU ALA THR LYS ILE LEU ASN ASP ILE
SEQRES 32 B 1528 ASN LEU PRO PHE TYR LYS GLU TYR ASP ASP ASP ILE ASN
SEQRES 33 B 1528 GLU VAL LEU GLU GLN LEU PHE ASN ARG ILE LYS TYR LEU
SEQRES 34 B 1528 ARG ILE ASP ASP HIS GLY PRO LYS GLN GLY PRO ILE THR
SEQRES 35 B 1528 LYS LYS LEU PRO LEU SER GLU PRO TYR PHE THR ARG PHE
SEQRES 36 B 1528 LYS ALA LYS ASP GLY GLU GLU TYR ALA LEU ALA ASN ASN
SEQRES 37 B 1528 GLY TRP ILE TRP ASP GLY ASN PRO LEU VAL ASP PHE ALA
SEQRES 38 B 1528 SER SER GLN SER LYS ALA TYR LEU ARG ARG GLU VAL ILE
SEQRES 39 B 1528 VAL TRP GLY ASP CYS VAL LYS LEU ARG TYR GLY LYS GLY
SEQRES 40 B 1528 PRO SER ASP SER PRO TYR LEU TRP GLU ARG MET SER LYS
SEQRES 41 B 1528 TYR VAL GLU MET ASN ALA ARG ILE PHE ASN GLY PHE ARG
SEQRES 42 B 1528 ILE ASP ASN CYS HIS SER THR PRO LEU HIS VAL GLY GLN
SEQRES 43 B 1528 TYR PHE LEU ASP VAL ALA ARG ARG VAL ASN PRO ASN LEU
SEQRES 44 B 1528 TYR VAL VAL ALA GLN LEU PHE SER GLY SER GLU ALA MET
SEQRES 45 B 1528 ASP CYS LEU PHE VAL GLU ARG LEU GLY ILE SER SER LEU
SEQRES 46 B 1528 ILE ARG GLU ALA MET GLN ALA TRP SER GLU GLU GLU LEU
SEQRES 47 B 1528 SER ARG LEU VAL HIS ARG HIS GLY GLY ARG PRO ILE GLY
SEQRES 48 B 1528 SER TYR LYS PHE VAL PRO LEU ASP ASP PHE PRO TYR PRO
SEQRES 49 B 1528 ALA ASP VAL LYS ILE ASP GLU GLU TYR CYS ALA TYR ASN
SEQRES 50 B 1528 PRO ASP ASP HIS SER VAL LYS CYS VAL SER GLU ILE MET
SEQRES 51 B 1528 ILE PRO LYS THR LEU THR ALA THR PRO PRO HIS ALA LEU
SEQRES 52 B 1528 PHE MET ASP CYS THR HIS ASP ASN GLU THR PRO ASN GLN
SEQRES 53 B 1528 LYS ARG THR VAL GLU ASP THR LEU PRO ASN ALA ALA LEU
SEQRES 54 B 1528 VAL ALA PHE CYS SER SER ALA ILE GLY SER VAL TYR GLY
SEQRES 55 B 1528 TYR ASP GLU VAL PHE PRO GLN LEU LEU ASP LEU VAL GLN
SEQRES 56 B 1528 GLU LYS ARG THR TYR SER CYS ALA GLU ASN THR GLY ILE
SEQRES 57 B 1528 SER LYS VAL LYS THR LEU LEU ASN ASN MET ARG GLU GLU
SEQRES 58 B 1528 ILE ALA SER GLU ALA VAL ASP ILE GLU ASP SER GLU MET
SEQRES 59 B 1528 HIS VAL HIS HIS ASP GLY GLN TYR ILE THR PHE HIS ARG
SEQRES 60 B 1528 THR ASN ALA LYS ASN GLY LYS GLY TRP TYR LEU VAL ALA
SEQRES 61 B 1528 ARG THR LYS PHE HIS SER SER GLY ASP GLN MET LEU PRO
SEQRES 62 B 1528 ARG ILE LYS LEU SER GLN THR LYS ALA THR PHE LYS ALA
SEQRES 63 B 1528 ALA PHE SER LEU GLU ARG THR GLY ASP ALA PRO ILE SER
SEQRES 64 B 1528 ASP GLU ILE ILE GLU GLY ILE PRO THR LYS LEU ARG GLU
SEQRES 65 B 1528 LEU THR GLY PHE ASP ILE GLY PHE ASP GLU ASN THR LYS
SEQRES 66 B 1528 GLU THR SER ILE LEU LEU PRO GLN ASP PHE PRO GLN GLY
SEQRES 67 B 1528 SER ILE VAL ILE PHE GLU THR GLN GLN LEU GLY ILE ASP
SEQRES 68 B 1528 ASP SER LEU ASP HIS PHE ILE ARG SER GLY ALA ILE LYS
SEQRES 69 B 1528 ALA THR GLU LYS LEU SER LEU GLU SER ILE ASN TYR VAL
SEQRES 70 B 1528 LEU TYR ARG ALA GLU GLN GLU GLU TYR ASP TYR SER GLU
SEQRES 71 B 1528 GLY ARG SER GLY ALA TYR ASP ILE PRO ASP TYR GLY LYS
SEQRES 72 B 1528 PRO VAL TYR CYS GLY LEU GLN GLY TRP VAL SER ILE LEU
SEQRES 73 B 1528 ARG LYS ILE ILE PHE TYR ASN ASP LEU ALA HIS PRO LEU
SEQRES 74 B 1528 SER ASN ASN LEU ARG ASN GLY HIS TRP ALA VAL ASP TYR
SEQRES 75 B 1528 VAL VAL ASN ARG LEU ASP LEU TYR LYS ASP LYS GLU GLY
SEQRES 76 B 1528 VAL ALA GLU VAL GLN GLU TRP LEU ARG SER ARG MET GLU
SEQRES 77 B 1528 ARG ILE LYS GLN LEU PRO SER TYR LEU VAL PRO SER PHE
SEQRES 78 B 1528 PHE ALA LEU VAL VAL GLY ILE MET TYR GLY CYS CYS ARG
SEQRES 79 B 1528 LEU ARG ALA MET GLN LEU MET SER ASP ASN VAL GLY LYS
SEQRES 80 B 1528 SER THR VAL PHE VAL GLN SER LEU ALA MET THR SER ILE
SEQRES 81 B 1528 GLN MET VAL SER ALA MET LYS SER THR SER ILE LEU PRO
SEQRES 82 B 1528 ASP GLN ASN ILE ALA ALA MET ALA ALA GLY LEU PRO HIS
SEQRES 83 B 1528 PHE SER THR ASN TYR MET ARG CYS TRP GLY ARG ASP VAL
SEQRES 84 B 1528 PHE ILE SER LEU ARG GLY LEU LEU LEU THR THR GLY ARG
SEQRES 85 B 1528 TYR GLU GLU ALA LYS GLU HIS ILE LEU ALA PHE ALA LYS
SEQRES 86 B 1528 THR LEU LYS HIS GLY LEU ILE PRO ASN LEU LEU ASP ALA
SEQRES 87 B 1528 GLY ARG ASN PRO ARG TYR ASN ALA ARG ASP ALA ALA TRP
SEQRES 88 B 1528 PHE PHE VAL GLN ALA ILE GLN ASP TYR VAL THR ILE VAL
SEQRES 89 B 1528 PRO GLY GLY VAL SER LEU LEU GLN GLU LYS VAL THR ARG
SEQRES 90 B 1528 ARG PHE PRO LEU ASP ASP GLU TYR ILE PRO TYR ASP ASP
SEQRES 91 B 1528 PRO LYS ALA PHE SER TYR SER SER THR ILE GLU GLU ILE
SEQRES 92 B 1528 ILE TYR GLU ILE LEU ASN ARG HIS ALA GLY GLY ILE LYS
SEQRES 93 B 1528 TYR ARG GLU ALA ASN ALA GLY PRO ASN LEU ASP ARG VAL
SEQRES 94 B 1528 MET LYS ASP GLU GLY PHE ASN VAL GLU VAL ASN VAL ASP
SEQRES 95 B 1528 TRP GLU THR GLY LEU ILE HIS GLY GLY SER GLN PHE ASN
SEQRES 96 B 1528 CYS GLY THR TRP MET ASP LYS MET GLY GLU SER GLU LYS
SEQRES 97 B 1528 ALA ASN SER VAL GLY VAL PRO GLY THR PRO ARG ASP GLY
SEQRES 98 B 1528 ALA ALA VAL GLU ILE ASN GLY LEU LEU LYS SER CYS LEU
SEQRES 99 B 1528 ARG PHE VAL LEU GLN LEU SER LYS ASP GLY LYS PHE LYS
SEQRES 100 B 1528 TYR THR GLU VAL THR LYS PRO ASP GLY SER LYS ILE SER
SEQRES 101 B 1528 LEU SER SER TRP ASN ASP LEU LEU GLN GLU ASN PHE GLU
SEQRES 102 B 1528 ARG CYS PHE TYR VAL PRO LYS ASN LYS GLU ASP ASP ASN
SEQRES 103 B 1528 LYS PHE GLU ILE ASP ALA THR ILE ILE ASN ARG ARG GLY
SEQRES 104 B 1528 ILE TYR LYS ASP LEU TYR ARG SER GLY LYS PRO TYR GLU
SEQRES 105 B 1528 ASP TYR GLN PHE ARG PRO ASN PHE THR ILE ALA MET VAL
SEQRES 106 B 1528 VAL ALA PRO GLU LEU PHE THR PRO ASP TYR ALA ALA GLY
SEQRES 107 B 1528 ALA ILE GLU LEU ALA ASP GLN VAL LEU ARG GLY PRO VAL
SEQRES 108 B 1528 GLY MET ARG THR LEU ASP PRO SER ASP TYR ASN TYR ARG
SEQRES 109 B 1528 PRO TYR TYR ASN ASN GLY GLU ASP SER ASP ASP PHE ALA
SEQRES 110 B 1528 THR SER LYS GLY ARG ASN TYR HIS GLN GLY PRO GLU TRP
SEQRES 111 B 1528 VAL TRP CYS TYR GLY TYR PHE ILE ARG ALA TYR HIS TYR
SEQRES 112 B 1528 PHE ASN PHE LEU THR ASN PRO LYS CYS GLN VAL GLU GLY
SEQRES 113 B 1528 SER ALA LYS LYS LEU LYS PRO SER SER TYR LEU TYR ARG
SEQRES 114 B 1528 LYS LEU TYR SER ARG LEU LEU LYS HIS ARG GLU TRP ILE
SEQRES 115 B 1528 GLU ASN SER PRO TRP ALA GLY LEU ALA GLU LEU THR ASN
SEQRES 116 B 1528 LYS ASP GLY GLU VAL CYS ASN ASP SER SER PRO THR GLN
SEQRES 117 B 1528 ALA TRP SER THR GLY CYS LEU LEU ASP LEU PHE TYR ASP
SEQRES 118 B 1528 LEU TRP ILE SER TYR GLU GLU
HET GLC C 1 12
HET GLC C 2 11
HET GLC C 3 11
HET GLC C 4 11
HET GLC D 1 12
HET GLC D 2 11
HET GLC D 3 11
HET GLC D 4 11
HET GLC D 5 11
HET GLC E 1 11
HET GLC E 2 11
HET GLC E 3 11
HET GLC E 4 11
HET GLC F 1 12
HET GLC F 2 11
HET GLC F 3 11
HET GLC G 1 12
HET GLC G 2 11
HET GLC G 3 11
HET GLC G 4 11
HET GLC G 5 11
HET GLC H 1 11
HET GLC H 2 11
HET GLC H 3 11
HET GLC H 4 11
HET GLC I 1 12
HET GLC I 2 11
HET GLC I 3 11
HET GLC I 4 11
HET GLC J 1 12
HET GLC J 2 11
HET GLC J 3 11
HET GLC J 4 11
HET GLC J 5 11
HET GLC K 1 11
HET GLC K 2 11
HET GLC K 3 11
HET GLC K 4 11
HET GLC L 1 12
HET GLC L 2 11
HET GLC L 3 11
HET GLC M 1 12
HET GLC M 2 11
HET GLC M 3 11
HET GLC M 4 11
HET GLC M 5 11
HETNAM GLC ALPHA-D-GLUCOPYRANOSE
HETSYN GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
FORMUL 3 GLC 46(C6 H12 O6)
HELIX 1 AA1 SER A 57 ARG A 61 5 5
HELIX 2 AA2 VAL A 152 MET A 156 5 5
HELIX 3 AA3 THR A 159 LYS A 173 1 15
HELIX 4 AA4 GLU A 209 ASN A 224 1 16
HELIX 5 AA5 HIS A 246 GLY A 250 5 5
HELIX 6 AA6 SER A 256 HIS A 258 5 3
HELIX 7 AA7 LEU A 259 ASP A 271 1 13
HELIX 8 AA8 ASP A 271 MET A 276 1 6
HELIX 9 AA9 THR A 287 VAL A 302 1 16
HELIX 10 AB1 ILE A 303 LYS A 307 5 5
HELIX 11 AB2 ASP A 315 LYS A 326 1 12
HELIX 12 AB3 ASP A 343 ALA A 355 1 13
HELIX 13 AB4 ASN A 372 HIS A 384 1 13
HELIX 14 AB5 GLY A 391 ARG A 430 1 40
HELIX 15 AB6 GLY A 507 ASP A 510 5 4
HELIX 16 AB7 SER A 511 ARG A 527 1 17
HELIX 17 AB8 ASN A 536 THR A 540 5 5
HELIX 18 AB9 PRO A 541 ASN A 556 1 16
HELIX 19 AC1 SER A 569 GLY A 581 1 13
HELIX 20 AC2 SER A 594 HIS A 605 1 12
HELIX 21 AC3 ASN A 637 HIS A 641 5 5
HELIX 22 AC4 THR A 673 ARG A 678 1 6
HELIX 23 AC5 THR A 679 GLU A 681 5 3
HELIX 24 AC6 ASP A 682 PHE A 692 1 11
HELIX 25 AC7 ILE A 728 SER A 744 1 17
HELIX 26 AC8 SER A 873 ARG A 879 1 7
HELIX 27 AC9 GLY A 881 GLU A 887 1 7
HELIX 28 AD1 GLU A 892 TYR A 899 1 8
HELIX 29 AD2 ALA A 901 SER A 909 1 9
HELIX 30 AD3 GLY A 928 ASN A 943 1 16
HELIX 31 AD4 HIS A 947 GLY A 956 1 10
HELIX 32 AD5 HIS A 957 LEU A 967 1 11
HELIX 33 AD6 ASP A 968 LYS A 971 5 4
HELIX 34 AD7 GLY A 975 LYS A 991 1 17
HELIX 35 AD8 PRO A 994 TYR A 996 5 3
HELIX 36 AD9 LEU A 997 MET A 1021 1 25
HELIX 37 AE1 SER A 1022 LYS A 1027 1 6
HELIX 38 AE2 THR A 1029 MET A 1042 1 14
HELIX 39 AE3 THR A 1069 ARG A 1073 5 5
HELIX 40 AE4 TRP A 1075 LEU A 1088 1 14
HELIX 41 AE5 ARG A 1092 LYS A 1105 1 14
HELIX 42 AE6 ARG A 1127 VAL A 1144 1 18
HELIX 43 AE7 GLY A 1146 LEU A 1151 5 6
HELIX 44 AE8 ILE A 1180 GLY A 1193 1 14
HELIX 45 AE9 VAL A 1264 LYS A 1282 1 19
HELIX 46 AF1 SER A 1300 TYR A 1317 1 18
HELIX 47 AF2 ASN A 1321 GLU A 1329 5 9
HELIX 48 AF3 LYS A 1349 TYR A 1354 5 6
HELIX 49 AF4 ASN A 1359 ALA A 1367 1 9
HELIX 50 AF5 PRO A 1368 PHE A 1371 5 4
HELIX 51 AF6 THR A 1372 GLN A 1385 1 14
HELIX 52 AF7 THR A 1418 GLN A 1426 5 9
HELIX 53 AF8 VAL A 1431 ASN A 1449 1 19
HELIX 54 AF9 SER A 1457 LYS A 1459 5 3
HELIX 55 AG1 SER A 1464 ARG A 1474 1 11
HELIX 56 AG2 LEU A 1475 ASN A 1484 1 10
HELIX 57 AG3 ASN A 1495 GLU A 1499 5 5
HELIX 58 AG4 ALA A 1509 GLU A 1527 1 19
HELIX 59 AG5 SER B 57 ARG B 61 5 5
HELIX 60 AG6 VAL B 152 MET B 156 5 5
HELIX 61 AG7 THR B 159 LYS B 173 1 15
HELIX 62 AG8 GLU B 209 ASN B 224 1 16
HELIX 63 AG9 HIS B 246 GLY B 250 5 5
HELIX 64 AH1 SER B 256 HIS B 258 5 3
HELIX 65 AH2 LEU B 259 ASP B 271 1 13
HELIX 66 AH3 ASP B 271 MET B 276 1 6
HELIX 67 AH4 THR B 287 VAL B 302 1 16
HELIX 68 AH5 ILE B 303 LYS B 307 5 5
HELIX 69 AH6 ASP B 315 LYS B 326 1 12
HELIX 70 AH7 ASP B 343 ALA B 355 1 13
HELIX 71 AH8 ASN B 372 HIS B 384 1 13
HELIX 72 AH9 GLY B 391 ARG B 430 1 40
HELIX 73 AI1 GLY B 507 ASP B 510 5 4
HELIX 74 AI2 SER B 511 ARG B 527 1 17
HELIX 75 AI3 ASN B 536 THR B 540 5 5
HELIX 76 AI4 PRO B 541 ASN B 556 1 16
HELIX 77 AI5 SER B 569 GLY B 581 1 13
HELIX 78 AI6 SER B 594 HIS B 605 1 12
HELIX 79 AI7 THR B 673 ARG B 678 1 6
HELIX 80 AI8 THR B 679 GLU B 681 5 3
HELIX 81 AI9 ASP B 682 PHE B 692 1 11
HELIX 82 AJ1 ILE B 728 SER B 744 1 17
HELIX 83 AJ2 ASP B 872 ARG B 879 1 8
HELIX 84 AJ3 GLY B 881 GLU B 887 1 7
HELIX 85 AJ4 GLU B 892 TYR B 899 1 8
HELIX 86 AJ5 ALA B 901 SER B 909 1 9
HELIX 87 AJ6 GLY B 928 ASN B 943 1 16
HELIX 88 AJ7 HIS B 947 GLY B 956 1 10
HELIX 89 AJ8 HIS B 957 LEU B 967 1 11
HELIX 90 AJ9 ASP B 968 LYS B 971 5 4
HELIX 91 AK1 GLY B 975 GLN B 992 1 18
HELIX 92 AK2 PRO B 994 TYR B 996 5 3
HELIX 93 AK3 LEU B 997 MET B 1021 1 25
HELIX 94 AK4 SER B 1022 LYS B 1027 1 6
HELIX 95 AK5 THR B 1029 MET B 1042 1 14
HELIX 96 AK6 THR B 1069 ARG B 1073 5 5
HELIX 97 AK7 TRP B 1075 LEU B 1087 1 13
HELIX 98 AK8 ARG B 1092 LYS B 1105 1 14
HELIX 99 AK9 ARG B 1127 VAL B 1144 1 18
HELIX 100 AL1 GLY B 1146 LEU B 1151 5 6
HELIX 101 AL2 ILE B 1180 GLY B 1193 1 14
HELIX 102 AL3 VAL B 1264 LYS B 1282 1 19
HELIX 103 AL4 SER B 1300 TYR B 1317 1 18
HELIX 104 AL5 ASN B 1321 GLU B 1329 5 9
HELIX 105 AL6 LYS B 1349 TYR B 1354 5 6
HELIX 106 AL7 ASN B 1359 ALA B 1367 1 9
HELIX 107 AL8 PRO B 1368 PHE B 1371 5 4
HELIX 108 AL9 THR B 1372 VAL B 1386 1 15
HELIX 109 AM1 THR B 1418 GLN B 1426 5 9
HELIX 110 AM2 VAL B 1431 ASN B 1449 1 19
HELIX 111 AM3 SER B 1457 LYS B 1459 5 3
HELIX 112 AM4 SER B 1464 ARG B 1474 1 11
HELIX 113 AM5 LEU B 1475 ASN B 1484 1 10
HELIX 114 AM6 ASN B 1495 GLU B 1499 5 5
HELIX 115 AM7 ALA B 1509 GLU B 1527 1 19
SHEET 1 AA1 4 ASP A 95 ILE A 101 0
SHEET 2 AA1 4 TYR A 47 ILE A 53 -1 N TYR A 47 O ILE A 101
SHEET 3 AA1 4 THR A 6 ARG A 10 1 N LEU A 9 O LYS A 50
SHEET 4 AA1 4 LYS A 653 THR A 654 1 O LYS A 653 N LEU A 8
SHEET 1 AA2 4 THR A 29 LEU A 30 0
SHEET 2 AA2 4 PHE A 126 VAL A 130 1 O VAL A 129 N LEU A 30
SHEET 3 AA2 4 THR A 106 LYS A 114 -1 N PHE A 109 O PHE A 126
SHEET 4 AA2 4 LEU A 64 THR A 67 -1 N TRP A 66 O TYR A 110
SHEET 1 AA3 4 THR A 29 LEU A 30 0
SHEET 2 AA3 4 PHE A 126 VAL A 130 1 O VAL A 129 N LEU A 30
SHEET 3 AA3 4 THR A 106 LYS A 114 -1 N PHE A 109 O PHE A 126
SHEET 4 AA3 4 LEU A 120 THR A 122 -1 O GLU A 121 N PHE A 113
SHEET 1 AA4 9 ALA A 147 VAL A 151 0
SHEET 2 AA4 9 MET A 177 PHE A 180 1 O HIS A 179 N VAL A 151
SHEET 3 AA4 9 LEU A 226 ILE A 231 1 O LEU A 226 N ILE A 178
SHEET 4 AA4 9 GLY A 531 ILE A 534 1 O ARG A 533 N THR A 229
SHEET 5 AA4 9 TYR A 560 ALA A 563 1 O TYR A 560 N PHE A 532
SHEET 6 AA4 9 SER A 584 GLU A 588 1 O ILE A 586 N ALA A 563
SHEET 7 AA4 9 ALA A 662 MET A 665 1 O MET A 665 N ARG A 587
SHEET 8 AA4 9 ALA A 696 VAL A 700 1 O ALA A 696 N PHE A 664
SHEET 9 AA4 9 ALA A 147 VAL A 151 1 N MET A 148 O SER A 699
SHEET 1 AA5 2 GLN A 184 ARG A 186 0
SHEET 2 AA5 2 ILE A 195 PHE A 201 -1 O GLU A 200 N HIS A 185
SHEET 1 AA6 4 HIS A 235 ALA A 237 0
SHEET 2 AA6 4 ILE A 494 LYS A 501 -1 O VAL A 500 N THR A 236
SHEET 3 AA6 4 GLU A 462 TRP A 470 -1 N TRP A 470 O ILE A 494
SHEET 4 AA6 4 PHE A 452 LYS A 456 -1 N THR A 453 O LEU A 465
SHEET 1 AA7 2 THR A 719 TYR A 720 0
SHEET 2 AA7 2 ILE A 822 ILE A 823 1 O ILE A 823 N THR A 719
SHEET 1 AA8 6 HIS A 755 ASP A 759 0
SHEET 2 AA8 6 TYR A 762 HIS A 766 -1 O TYR A 762 N ASP A 759
SHEET 3 AA8 6 LYS A 774 ARG A 781 -1 O ALA A 780 N ILE A 763
SHEET 4 AA8 6 SER A 859 GLN A 867 -1 O PHE A 863 N TYR A 777
SHEET 5 AA8 6 THR A 800 ARG A 812 -1 N ALA A 806 O ILE A 862
SHEET 6 AA8 6 THR A 828 GLU A 832 -1 O ARG A 831 N SER A 809
SHEET 1 AA9 3 ILE A 795 LEU A 797 0
SHEET 2 AA9 3 GLU A 846 LEU A 850 -1 O ILE A 849 N ILE A 795
SHEET 3 AA9 3 ASP A 837 ASP A 841 -1 N ASP A 841 O GLU A 846
SHEET 1 AB1 2 VAL A1043 SER A1044 0
SHEET 2 AB1 2 ALA A1059 MET A1060 -1 O ALA A1059 N SER A1044
SHEET 1 AB2 2 GLY A1063 LEU A1064 0
SHEET 2 AB2 2 THR A1507 GLN A1508 -1 O THR A1507 N LEU A1064
SHEET 1 AB3 2 LYS A1154 ARG A1157 0
SHEET 2 AB3 2 TYR A1176 THR A1179 -1 O TYR A1176 N ARG A1157
SHEET 1 AB4 3 ILE A1195 ARG A1198 0
SHEET 2 AB4 3 ASN A1216 VAL A1221 -1 O VAL A1217 N TYR A1197
SHEET 3 AB4 3 ILE A1228 GLY A1230 -1 O HIS A1229 N ASN A1220
SHEET 1 AB5 2 ALA A1262 ALA A1263 0
SHEET 2 AB5 2 LEU A1344 TYR A1345 -1 O TYR A1345 N ALA A1262
SHEET 1 AB6 3 MET A1393 ARG A1394 0
SHEET 2 AB6 3 GLU A1429 TRP A1430 -1 O TRP A1430 N MET A1393
SHEET 3 AB6 3 LEU A1493 THR A1494 -1 O THR A1494 N GLU A1429
SHEET 1 AB7 2 GLN A1453 GLU A1455 0
SHEET 2 AB7 2 LEU A1461 PRO A1463 -1 O LYS A1462 N VAL A1454
SHEET 1 AB8 4 ASP B 95 ILE B 101 0
SHEET 2 AB8 4 TYR B 47 ILE B 53 -1 N TYR B 47 O ILE B 101
SHEET 3 AB8 4 THR B 6 ARG B 10 1 N LEU B 9 O LYS B 50
SHEET 4 AB8 4 LYS B 653 THR B 654 1 O LYS B 653 N LEU B 8
SHEET 1 AB9 4 THR B 29 LEU B 30 0
SHEET 2 AB9 4 PHE B 126 VAL B 130 1 O VAL B 129 N LEU B 30
SHEET 3 AB9 4 THR B 106 LYS B 114 -1 N PHE B 109 O PHE B 126
SHEET 4 AB9 4 LEU B 64 THR B 67 -1 N TRP B 66 O TYR B 110
SHEET 1 AC1 4 THR B 29 LEU B 30 0
SHEET 2 AC1 4 PHE B 126 VAL B 130 1 O VAL B 129 N LEU B 30
SHEET 3 AC1 4 THR B 106 LYS B 114 -1 N PHE B 109 O PHE B 126
SHEET 4 AC1 4 LEU B 120 THR B 122 -1 O GLU B 121 N PHE B 113
SHEET 1 AC2 9 ALA B 147 VAL B 151 0
SHEET 2 AC2 9 MET B 177 PHE B 180 1 O HIS B 179 N VAL B 151
SHEET 3 AC2 9 LEU B 226 ILE B 231 1 O LEU B 226 N ILE B 178
SHEET 4 AC2 9 GLY B 531 ILE B 534 1 O ARG B 533 N THR B 229
SHEET 5 AC2 9 TYR B 560 ALA B 563 1 O TYR B 560 N PHE B 532
SHEET 6 AC2 9 SER B 584 GLU B 588 1 O ILE B 586 N ALA B 563
SHEET 7 AC2 9 ALA B 662 MET B 665 1 O MET B 665 N ARG B 587
SHEET 8 AC2 9 ALA B 696 VAL B 700 1 O ALA B 696 N PHE B 664
SHEET 9 AC2 9 ALA B 147 VAL B 151 1 N MET B 148 O SER B 699
SHEET 1 AC3 2 GLN B 184 ARG B 186 0
SHEET 2 AC3 2 ILE B 195 PHE B 201 -1 O GLU B 200 N HIS B 185
SHEET 1 AC4 4 HIS B 235 ALA B 237 0
SHEET 2 AC4 4 ILE B 494 LYS B 501 -1 O VAL B 500 N THR B 236
SHEET 3 AC4 4 GLU B 462 TRP B 470 -1 N TRP B 470 O ILE B 494
SHEET 4 AC4 4 PHE B 452 LYS B 456 -1 N THR B 453 O LEU B 465
SHEET 1 AC5 2 THR B 719 TYR B 720 0
SHEET 2 AC5 2 ILE B 822 ILE B 823 1 O ILE B 823 N THR B 719
SHEET 1 AC6 6 MET B 754 ASP B 759 0
SHEET 2 AC6 6 TYR B 762 ARG B 767 -1 O TYR B 762 N ASP B 759
SHEET 3 AC6 6 LYS B 774 ARG B 781 -1 O TRP B 776 N ARG B 767
SHEET 4 AC6 6 SER B 859 GLN B 867 -1 O PHE B 863 N TYR B 777
SHEET 5 AC6 6 THR B 800 ARG B 812 -1 N ALA B 806 O ILE B 862
SHEET 6 AC6 6 THR B 828 GLU B 832 -1 O ARG B 831 N SER B 809
SHEET 1 AC7 3 ILE B 795 LEU B 797 0
SHEET 2 AC7 3 GLU B 846 LEU B 850 -1 O THR B 847 N LEU B 797
SHEET 3 AC7 3 ASP B 837 ASP B 841 -1 N ASP B 841 O GLU B 846
SHEET 1 AC8 2 VAL B1043 SER B1044 0
SHEET 2 AC8 2 ALA B1059 MET B1060 -1 O ALA B1059 N SER B1044
SHEET 1 AC9 2 GLY B1063 LEU B1064 0
SHEET 2 AC9 2 THR B1507 GLN B1508 -1 O THR B1507 N LEU B1064
SHEET 1 AD1 2 LYS B1154 ARG B1157 0
SHEET 2 AD1 2 TYR B1176 THR B1179 -1 O TYR B1176 N ARG B1157
SHEET 1 AD2 3 ILE B1195 ARG B1198 0
SHEET 2 AD2 3 ASN B1216 VAL B1221 -1 O VAL B1217 N TYR B1197
SHEET 3 AD2 3 ILE B1228 GLY B1230 -1 O HIS B1229 N ASN B1220
SHEET 1 AD3 2 ALA B1262 ALA B1263 0
SHEET 2 AD3 2 LEU B1344 TYR B1345 -1 O TYR B1345 N ALA B1262
SHEET 1 AD4 3 MET B1393 ARG B1394 0
SHEET 2 AD4 3 GLU B1429 TRP B1430 -1 O TRP B1430 N MET B1393
SHEET 3 AD4 3 LEU B1493 THR B1494 -1 O THR B1494 N GLU B1429
SHEET 1 AD5 2 GLN B1453 GLU B1455 0
SHEET 2 AD5 2 LEU B1461 PRO B1463 -1 O LYS B1462 N VAL B1454
LINK O4 GLC C 1 C1 GLC C 2 1555 1555 1.45
LINK O4 GLC C 2 C1 GLC C 3 1555 1555 1.47
LINK O4 GLC C 3 C1 GLC C 4 1555 1555 1.49
LINK O4 GLC D 1 C1 GLC D 2 1555 1555 1.47
LINK O4 GLC D 2 C1 GLC D 3 1555 1555 1.47
LINK O4 GLC D 3 C1 GLC D 4 1555 1555 1.42
LINK O4 GLC D 4 C1 GLC D 5 1555 1555 1.47
LINK O4 GLC E 1 C1 GLC E 2 1555 1555 1.47
LINK O4 GLC E 2 C1 GLC E 3 1555 1555 1.43
LINK O4 GLC E 3 C1 GLC E 4 1555 1555 1.43
LINK O4 GLC F 1 C1 GLC F 2 1555 1555 1.47
LINK O4 GLC F 2 C1 GLC F 3 1555 1555 1.47
LINK O4 GLC G 1 C1 GLC G 2 1555 1555 1.48
LINK O4 GLC G 2 C1 GLC G 3 1555 1555 1.43
LINK O4 GLC G 3 C1 GLC G 4 1555 1555 1.44
LINK O4 GLC G 4 C1 GLC G 5 1555 1555 1.44
LINK O4 GLC H 1 C1 GLC H 2 1555 1555 1.44
LINK O4 GLC H 2 C1 GLC H 3 1555 1555 1.46
LINK O4 GLC H 3 C1 GLC H 4 1555 1555 1.46
LINK O4 GLC I 1 C1 GLC I 2 1555 1555 1.45
LINK O4 GLC I 2 C1 GLC I 3 1555 1555 1.45
LINK O4 GLC I 3 C1 GLC I 4 1555 1555 1.48
LINK O4 GLC J 1 C1 GLC J 2 1555 1555 1.49
LINK O4 GLC J 2 C1 GLC J 3 1555 1555 1.45
LINK O4 GLC J 3 C1 GLC J 4 1555 1555 1.44
LINK O4 GLC J 4 C1 GLC J 5 1555 1555 1.43
LINK O4 GLC K 1 C1 GLC K 2 1555 1555 1.49
LINK O4 GLC K 2 C1 GLC K 3 1555 1555 1.49
LINK O4 GLC K 3 C1 GLC K 4 1555 1555 1.45
LINK O4 GLC L 1 C1 GLC L 2 1555 1555 1.44
LINK O4 GLC L 2 C1 GLC L 3 1555 1555 1.47
LINK O4 GLC M 1 C1 GLC M 2 1555 1555 1.45
LINK O4 GLC M 2 C1 GLC M 3 1555 1555 1.44
LINK O4 GLC M 3 C1 GLC M 4 1555 1555 1.44
LINK O4 GLC M 4 C1 GLC M 5 1555 1555 1.46
CISPEP 1 LEU A 1064 PRO A 1065 0 -0.56
CISPEP 2 LEU B 1064 PRO B 1065 0 6.54
CRYST1 158.070 202.010 135.240 90.00 101.32 90.00 C 1 2 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.006326 0.000000 0.001266 0.00000
SCALE2 0.000000 0.004950 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007541 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
