HEADER HYDROLASE 30-SEP-15 5E1Q
TITLE MUTANT (D415G) GH97 ALPHA-GALACTOSIDASE IN COMPLEX WITH GAL-LAC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RETAINING ALPHA-GALACTOSIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 27-662;
COMPND 5 SYNONYM: BTGH97B,MELIBIASE;
COMPND 6 EC: 3.2.1.22;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACTEROIDES THETAIOTAOMICRON (STRAIN ATCC 29148
SOURCE 3 / DSM 2079 / NCTC 10582 / E50 / VPI-5482);
SOURCE 4 ORGANISM_TAXID: 226186;
SOURCE 5 STRAIN: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482;
SOURCE 6 GENE: BT_1871;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21 CODONPLUS RIL (DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PCOLD I
KEYWDS ALPHA-GALACTOSIDASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.MATSUNAGA,K.YAMASHITA,T.TAGAMI,M.YAO,M.OKUYAMA,A.KIMURA
REVDAT 6 08-NOV-23 5E1Q 1 HETSYN LINK
REVDAT 5 29-JUL-20 5E1Q 1 COMPND REMARK HET HETNAM
REVDAT 5 2 1 HETSYN FORMUL LINK SITE
REVDAT 5 3 1 ATOM
REVDAT 4 19-FEB-20 5E1Q 1 REMARK
REVDAT 3 05-APR-17 5E1Q 1 JRNL
REVDAT 2 01-FEB-17 5E1Q 1 JRNL
REVDAT 1 05-OCT-16 5E1Q 0
JRNL AUTH M.OKUYAMA,K.MATSUNAGA,K.I.WATANABE,K.YAMASHITA,T.TAGAMI,
JRNL AUTH 2 A.KIKUCHI,M.MA,P.KLAHAN,H.MORI,M.YAO,A.KIMURA
JRNL TITL EFFICIENT SYNTHESIS OF ALPHA-GALACTOSYL OLIGOSACCHARIDES
JRNL TITL 2 USING A MUTANT BACTEROIDES THETAIOTAOMICRON RETAINING
JRNL TITL 3 ALPHA-GALACTOSIDASE (BTGH97B).
JRNL REF FEBS J. V. 284 766 2017
JRNL REFN ISSN 1742-4658
JRNL PMID 28103425
JRNL DOI 10.1111/FEBS.14018
REMARK 2
REMARK 2 RESOLUTION. 1.94 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1690
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) : 1.94
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.44
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 106883
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2139
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 42.4509 - 4.7894 1.00 7437 152 0.1415 0.1811
REMARK 3 2 4.7894 - 3.8023 1.00 7165 146 0.1375 0.1610
REMARK 3 3 3.8023 - 3.3219 1.00 7126 145 0.1644 0.1999
REMARK 3 4 3.3219 - 3.0182 1.00 7034 143 0.1823 0.1927
REMARK 3 5 3.0182 - 2.8019 1.00 7032 143 0.2009 0.2245
REMARK 3 6 2.8019 - 2.6368 1.00 7024 145 0.2017 0.2589
REMARK 3 7 2.6368 - 2.5047 1.00 7012 142 0.2092 0.2825
REMARK 3 8 2.5047 - 2.3957 1.00 6991 143 0.2128 0.2725
REMARK 3 9 2.3957 - 2.3035 1.00 6993 143 0.2073 0.2472
REMARK 3 10 2.3035 - 2.2240 1.00 6941 142 0.2270 0.2666
REMARK 3 11 2.2240 - 2.1545 1.00 6974 143 0.2386 0.2910
REMARK 3 12 2.1545 - 2.0929 1.00 6925 141 0.2635 0.3498
REMARK 3 13 2.0929 - 2.0378 1.00 7000 143 0.2894 0.2930
REMARK 3 14 2.0378 - 1.9881 1.00 6936 141 0.3032 0.3725
REMARK 3 15 1.9881 - 1.9429 0.89 6154 127 0.3396 0.3725
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) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.350
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.05
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.77
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 : 0.008 10602
REMARK 3 ANGLE : 1.079 14379
REMARK 3 CHIRALITY : 0.045 1533
REMARK 3 PLANARITY : 0.006 1852
REMARK 3 DIHEDRAL : 12.343 3922
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 16
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 22 THROUGH 88 )
REMARK 3 ORIGIN FOR THE GROUP (A): -67.0258 110.8628 64.5607
REMARK 3 T TENSOR
REMARK 3 T11: 0.5660 T22: 0.3713
REMARK 3 T33: 0.2926 T12: -0.0454
REMARK 3 T13: 0.0404 T23: -0.0305
REMARK 3 L TENSOR
REMARK 3 L11: 1.3976 L22: 1.2752
REMARK 3 L33: 2.3323 L12: -0.4593
REMARK 3 L13: -0.4563 L23: 0.4310
REMARK 3 S TENSOR
REMARK 3 S11: 0.0507 S12: -0.1958 S13: 0.0794
REMARK 3 S21: 0.3385 S22: -0.1363 S23: 0.1947
REMARK 3 S31: -0.2646 S32: -0.2783 S33: 0.0806
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 89 THROUGH 142 )
REMARK 3 ORIGIN FOR THE GROUP (A): -59.8400 103.4537 64.4198
REMARK 3 T TENSOR
REMARK 3 T11: 0.5259 T22: 0.3213
REMARK 3 T33: 0.2870 T12: -0.0533
REMARK 3 T13: 0.0113 T23: 0.0283
REMARK 3 L TENSOR
REMARK 3 L11: 1.5083 L22: 0.7778
REMARK 3 L33: 2.2137 L12: -0.2740
REMARK 3 L13: -0.1969 L23: 0.6448
REMARK 3 S TENSOR
REMARK 3 S11: 0.0163 S12: -0.2462 S13: -0.1812
REMARK 3 S21: 0.4077 S22: -0.0919 S23: 0.0839
REMARK 3 S31: 0.0622 S32: -0.1207 S33: 0.0872
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 143 THROUGH 359 )
REMARK 3 ORIGIN FOR THE GROUP (A): -56.5479 96.0409 44.2139
REMARK 3 T TENSOR
REMARK 3 T11: 0.3491 T22: 0.1976
REMARK 3 T33: 0.2459 T12: -0.0795
REMARK 3 T13: -0.0117 T23: 0.0156
REMARK 3 L TENSOR
REMARK 3 L11: 0.9453 L22: 0.9888
REMARK 3 L33: 2.6273 L12: -0.4097
REMARK 3 L13: -0.6192 L23: 0.2354
REMARK 3 S TENSOR
REMARK 3 S11: -0.0362 S12: -0.0404 S13: -0.1462
REMARK 3 S21: 0.1855 S22: -0.1160 S23: 0.0867
REMARK 3 S31: 0.2831 S32: -0.0428 S33: 0.1337
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 360 THROUGH 407 )
REMARK 3 ORIGIN FOR THE GROUP (A): -39.9606 77.8484 42.8342
REMARK 3 T TENSOR
REMARK 3 T11: 0.7073 T22: 0.4380
REMARK 3 T33: 0.4038 T12: 0.1730
REMARK 3 T13: 0.0178 T23: 0.1049
REMARK 3 L TENSOR
REMARK 3 L11: 1.2992 L22: 1.8811
REMARK 3 L33: 2.4445 L12: -0.9724
REMARK 3 L13: -0.2947 L23: 0.7335
REMARK 3 S TENSOR
REMARK 3 S11: -0.3336 S12: -0.2027 S13: -0.3873
REMARK 3 S21: 0.2880 S22: 0.0059 S23: 0.0029
REMARK 3 S31: 0.9671 S32: 0.6281 S33: 0.3053
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 408 THROUGH 562 )
REMARK 3 ORIGIN FOR THE GROUP (A): -46.7352 97.5854 38.0378
REMARK 3 T TENSOR
REMARK 3 T11: 0.3310 T22: 0.2397
REMARK 3 T33: 0.2798 T12: -0.0232
REMARK 3 T13: -0.0146 T23: 0.0186
REMARK 3 L TENSOR
REMARK 3 L11: 0.5744 L22: 0.7831
REMARK 3 L33: 3.1569 L12: -0.0448
REMARK 3 L13: -0.4078 L23: -0.0719
REMARK 3 S TENSOR
REMARK 3 S11: -0.0108 S12: -0.1334 S13: -0.0165
REMARK 3 S21: 0.0927 S22: -0.0930 S23: 0.0069
REMARK 3 S31: 0.1603 S32: 0.3135 S33: 0.0963
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 563 THROUGH 662 )
REMARK 3 ORIGIN FOR THE GROUP (A): -37.5664 117.0702 36.8822
REMARK 3 T TENSOR
REMARK 3 T11: 0.6540 T22: 0.5259
REMARK 3 T33: 0.4101 T12: -0.2901
REMARK 3 T13: -0.0246 T23: -0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 0.3154 L22: 1.1828
REMARK 3 L33: 1.4740 L12: -0.2283
REMARK 3 L13: -0.4524 L23: -0.0008
REMARK 3 S TENSOR
REMARK 3 S11: 0.2007 S12: -0.2714 S13: 0.1708
REMARK 3 S21: 0.1937 S22: -0.0887 S23: -0.2148
REMARK 3 S31: -1.0088 S32: 0.7690 S33: -0.0639
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 22 THROUGH 63 )
REMARK 3 ORIGIN FOR THE GROUP (A): -39.2341 119.2202 85.2048
REMARK 3 T TENSOR
REMARK 3 T11: 0.9114 T22: 0.5493
REMARK 3 T33: 0.3710 T12: -0.2095
REMARK 3 T13: -0.0446 T23: 0.0264
REMARK 3 L TENSOR
REMARK 3 L11: 1.2477 L22: 1.3463
REMARK 3 L33: 1.4642 L12: -0.1916
REMARK 3 L13: 0.1928 L23: 0.1285
REMARK 3 S TENSOR
REMARK 3 S11: -0.0945 S12: 0.2566 S13: 0.1660
REMARK 3 S21: -0.4181 S22: 0.0934 S23: -0.0101
REMARK 3 S31: -0.9508 S32: 0.3597 S33: -0.0002
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 64 THROUGH 108 )
REMARK 3 ORIGIN FOR THE GROUP (A): -48.7784 108.7401 83.8359
REMARK 3 T TENSOR
REMARK 3 T11: 0.5024 T22: 0.4566
REMARK 3 T33: 0.3397 T12: -0.0121
REMARK 3 T13: -0.0505 T23: -0.0346
REMARK 3 L TENSOR
REMARK 3 L11: 0.8041 L22: 0.7403
REMARK 3 L33: 1.9734 L12: 0.3408
REMARK 3 L13: 0.4049 L23: -0.1100
REMARK 3 S TENSOR
REMARK 3 S11: -0.0794 S12: 0.3091 S13: -0.0980
REMARK 3 S21: -0.2398 S22: -0.0230 S23: 0.0047
REMARK 3 S31: -0.3819 S32: 0.1573 S33: 0.0713
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 109 THROUGH 142 )
REMARK 3 ORIGIN FOR THE GROUP (A): -40.2216 104.7447 82.1188
REMARK 3 T TENSOR
REMARK 3 T11: 0.4247 T22: 0.5846
REMARK 3 T33: 0.3228 T12: -0.0854
REMARK 3 T13: -0.0056 T23: -0.0460
REMARK 3 L TENSOR
REMARK 3 L11: 2.1689 L22: 2.0064
REMARK 3 L33: 2.3085 L12: -0.6295
REMARK 3 L13: -0.4858 L23: 0.2551
REMARK 3 S TENSOR
REMARK 3 S11: -0.0520 S12: 0.4416 S13: -0.2004
REMARK 3 S21: -0.3436 S22: 0.0188 S23: -0.0190
REMARK 3 S31: -0.3842 S32: 0.4864 S33: 0.0284
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 143 THROUGH 221 )
REMARK 3 ORIGIN FOR THE GROUP (A): -34.1823 108.7993 102.5217
REMARK 3 T TENSOR
REMARK 3 T11: 0.4304 T22: 0.5295
REMARK 3 T33: 0.3124 T12: -0.2060
REMARK 3 T13: -0.0442 T23: 0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 1.3089 L22: 0.8152
REMARK 3 L33: 2.0048 L12: 0.4495
REMARK 3 L13: -0.0146 L23: 0.2529
REMARK 3 S TENSOR
REMARK 3 S11: -0.0937 S12: 0.1191 S13: 0.0305
REMARK 3 S21: -0.1712 S22: 0.0306 S23: -0.2192
REMARK 3 S31: -0.7615 S32: 1.0040 S33: 0.0481
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 222 THROUGH 359 )
REMARK 3 ORIGIN FOR THE GROUP (A): -46.4211 93.7479 106.2966
REMARK 3 T TENSOR
REMARK 3 T11: 0.2587 T22: 0.2602
REMARK 3 T33: 0.2939 T12: -0.0208
REMARK 3 T13: -0.0211 T23: -0.0609
REMARK 3 L TENSOR
REMARK 3 L11: 0.6173 L22: 0.8224
REMARK 3 L33: 3.9978 L12: 0.0694
REMARK 3 L13: -0.1092 L23: -0.1962
REMARK 3 S TENSOR
REMARK 3 S11: -0.0465 S12: 0.1108 S13: -0.0996
REMARK 3 S21: -0.0777 S22: -0.0209 S23: -0.0400
REMARK 3 S31: 0.2940 S32: 0.1285 S33: 0.0517
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 360 THROUGH 407 )
REMARK 3 ORIGIN FOR THE GROUP (A): -53.4667 78.1155 110.1887
REMARK 3 T TENSOR
REMARK 3 T11: 0.7658 T22: 0.3262
REMARK 3 T33: 0.4812 T12: -0.1358
REMARK 3 T13: 0.0007 T23: -0.1109
REMARK 3 L TENSOR
REMARK 3 L11: 1.3628 L22: 1.2875
REMARK 3 L33: 2.1580 L12: 0.2847
REMARK 3 L13: 0.2942 L23: -0.6383
REMARK 3 S TENSOR
REMARK 3 S11: 0.0235 S12: 0.0643 S13: -0.4715
REMARK 3 S21: -0.1007 S22: -0.0924 S23: 0.0603
REMARK 3 S31: 1.3217 S32: -0.3094 S33: 0.0662
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 408 THROUGH 509 )
REMARK 3 ORIGIN FOR THE GROUP (A): -47.5127 97.1710 107.8512
REMARK 3 T TENSOR
REMARK 3 T11: 0.2704 T22: 0.2640
REMARK 3 T33: 0.2981 T12: 0.0153
REMARK 3 T13: 0.0079 T23: -0.0327
REMARK 3 L TENSOR
REMARK 3 L11: 0.8458 L22: 0.8747
REMARK 3 L33: 2.3410 L12: 0.0821
REMARK 3 L13: 0.4227 L23: -0.1494
REMARK 3 S TENSOR
REMARK 3 S11: -0.0659 S12: 0.1741 S13: -0.0806
REMARK 3 S21: -0.1138 S22: -0.0303 S23: -0.0043
REMARK 3 S31: -0.0053 S32: 0.0546 S33: 0.0997
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 510 THROUGH 562 )
REMARK 3 ORIGIN FOR THE GROUP (A): -54.0220 101.9775 123.8667
REMARK 3 T TENSOR
REMARK 3 T11: 0.2637 T22: 0.2635
REMARK 3 T33: 0.2991 T12: -0.0020
REMARK 3 T13: -0.0174 T23: -0.0370
REMARK 3 L TENSOR
REMARK 3 L11: 0.4721 L22: 1.0069
REMARK 3 L33: 2.2365 L12: -0.1453
REMARK 3 L13: -0.2126 L23: 0.0944
REMARK 3 S TENSOR
REMARK 3 S11: -0.0093 S12: 0.0335 S13: -0.0036
REMARK 3 S21: 0.0612 S22: -0.0812 S23: 0.0868
REMARK 3 S31: -0.0689 S32: -0.3222 S33: 0.0812
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 563 THROUGH 607 )
REMARK 3 ORIGIN FOR THE GROUP (A): -58.9566 114.9780 112.6002
REMARK 3 T TENSOR
REMARK 3 T11: 0.5315 T22: 0.4067
REMARK 3 T33: 0.4024 T12: 0.1633
REMARK 3 T13: -0.0668 T23: -0.0499
REMARK 3 L TENSOR
REMARK 3 L11: 2.3871 L22: 1.2353
REMARK 3 L33: 3.2285 L12: 0.0836
REMARK 3 L13: 0.3059 L23: -0.2323
REMARK 3 S TENSOR
REMARK 3 S11: -0.2520 S12: 0.1320 S13: 0.3968
REMARK 3 S21: -0.0250 S22: -0.0052 S23: 0.3159
REMARK 3 S31: -1.0010 S32: -0.6318 S33: 0.2544
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 608 THROUGH 662 )
REMARK 3 ORIGIN FOR THE GROUP (A): -65.0046 116.6947 122.0122
REMARK 3 T TENSOR
REMARK 3 T11: 0.5690 T22: 0.6499
REMARK 3 T33: 0.5007 T12: 0.2955
REMARK 3 T13: -0.0267 T23: -0.0849
REMARK 3 L TENSOR
REMARK 3 L11: 1.6775 L22: 1.5386
REMARK 3 L33: 0.8154 L12: -0.5182
REMARK 3 L13: 0.3562 L23: -1.0342
REMARK 3 S TENSOR
REMARK 3 S11: -0.1486 S12: 0.0876 S13: 0.2833
REMARK 3 S21: 0.0176 S22: -0.0581 S23: 0.3147
REMARK 3 S31: -0.7479 S32: -0.8867 S33: 0.1481
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN B
REMARK 3 ATOM PAIRS NUMBER : 6180
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5E1Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-OCT-15.
REMARK 100 THE DEPOSITION ID IS D_1000214149.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-5A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 106969
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.940
REMARK 200 RESOLUTION RANGE LOW (A) : 48.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.94
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.5
REMARK 200 DATA REDUNDANCY IN SHELL : 7.30
REMARK 200 R MERGE FOR SHELL (I) : 0.99000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.310
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 3A24
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 6000, 0.1 M MES-NAOH (PH 6.2),
REMARK 280 3.9 MM BETA-LACTOSYL ALPHA-D-GALACTOPYRANOSIDE, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 288K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 30.31000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 118.53950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 50.31200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 118.53950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.31000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 50.31200
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
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, D
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 8
REMARK 465 ASN A 9
REMARK 465 HIS A 10
REMARK 465 LYS A 11
REMARK 465 VAL A 12
REMARK 465 HIS A 13
REMARK 465 HIS A 14
REMARK 465 HIS A 15
REMARK 465 HIS A 16
REMARK 465 HIS A 17
REMARK 465 HIS A 18
REMARK 465 ILE A 19
REMARK 465 GLU A 20
REMARK 465 MET B 8
REMARK 465 ASN B 9
REMARK 465 HIS B 10
REMARK 465 LYS B 11
REMARK 465 VAL B 12
REMARK 465 HIS B 13
REMARK 465 HIS B 14
REMARK 465 HIS B 15
REMARK 465 HIS B 16
REMARK 465 HIS B 17
REMARK 465 HIS B 18
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU B 20 CG CD OE1 OE2
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 HOH A 1109 O HOH A 1136 2.15
REMARK 500 O HOH A 1124 O HOH A 1167 2.16
REMARK 500 O HOH A 1199 O HOH A 1201 2.18
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 TYR A 92 -142.28 -148.96
REMARK 500 LYS A 110 24.60 83.10
REMARK 500 HIS A 245 106.22 -55.97
REMARK 500 ASP A 257 32.84 -92.36
REMARK 500 TRP A 316 19.04 56.87
REMARK 500 LEU A 357 -6.41 72.76
REMARK 500 ASP A 396 47.86 -142.68
REMARK 500 ASP A 420 30.58 -143.53
REMARK 500 GLU A 464 -112.24 -88.66
REMARK 500 TRP A 474 -13.73 -149.14
REMARK 500 ILE A 491 -84.46 -127.93
REMARK 500 THR A 501 65.96 61.80
REMARK 500 SER A 538 82.46 -151.08
REMARK 500 GLU A 579 -50.04 -127.24
REMARK 500 ASP A 598 -147.78 -83.52
REMARK 500 TYR B 92 -141.86 -146.17
REMARK 500 LYS B 110 25.87 82.07
REMARK 500 HIS B 245 106.40 -56.25
REMARK 500 ASP B 257 31.61 -89.69
REMARK 500 TRP B 316 18.61 58.05
REMARK 500 LEU B 357 -3.75 72.69
REMARK 500 ASP B 396 44.01 -141.42
REMARK 500 ASP B 420 31.82 -142.34
REMARK 500 GLU B 464 -113.01 -87.33
REMARK 500 TRP B 474 -13.63 -148.05
REMARK 500 ILE B 491 -83.23 -129.32
REMARK 500 THR B 501 66.11 61.74
REMARK 500 SER B 538 81.87 -152.62
REMARK 500 ASP B 598 -148.46 -82.81
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 CA A 701 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 174 OE2
REMARK 620 2 GLU A 464 OE1 73.5
REMARK 620 3 GLU A 464 OE2 73.1 50.8
REMARK 620 4 GLU A 470 OE2 82.4 127.5 77.9
REMARK 620 5 HOH A1107 O 77.6 72.0 120.8 146.1
REMARK 620 6 BGC C 1 O1 153.5 129.7 129.8 89.5 96.4
REMARK 620 7 BGC C 1 O2 92.4 140.9 158.5 84.7 69.3 61.6
REMARK 620 8 GLA C 2 O2 149.2 78.0 79.9 106.5 104.7 57.3 117.4
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 701 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 174 OE2
REMARK 620 2 GLU B 464 OE1 76.6
REMARK 620 3 GLU B 464 OE2 75.6 50.8
REMARK 620 4 GLU B 470 OE2 81.6 130.1 80.5
REMARK 620 5 HOH B 968 O 78.6 64.7 114.2 151.1
REMARK 620 6 BGC D 1 O1 153.6 126.5 127.6 89.6 98.9
REMARK 620 7 BGC D 1 O2 92.8 140.1 162.3 84.7 75.5 61.5
REMARK 620 8 GLA D 2 O2 146.4 72.7 74.5 108.1 100.0 60.1 119.7
REMARK 620 N 1 2 3 4 5 6 7
DBREF 5E1Q A 27 662 UNP Q8A6L0 AGAL_BACTN 27 662
DBREF 5E1Q B 27 662 UNP Q8A6L0 AGAL_BACTN 27 662
SEQADV 5E1Q MET A 8 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q ASN A 9 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q HIS A 10 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q LYS A 11 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q VAL A 12 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q HIS A 13 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q HIS A 14 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q HIS A 15 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q HIS A 16 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q HIS A 17 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q HIS A 18 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q ILE A 19 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q GLU A 20 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q GLY A 21 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q ARG A 22 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q HIS A 23 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q MET A 24 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q GLU A 25 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q LEU A 26 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q GLY A 415 UNP Q8A6L0 ASP 415 ENGINEERED MUTATION
SEQADV 5E1Q MET B 8 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q ASN B 9 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q HIS B 10 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q LYS B 11 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q VAL B 12 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q HIS B 13 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q HIS B 14 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q HIS B 15 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q HIS B 16 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q HIS B 17 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q HIS B 18 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q ILE B 19 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q GLU B 20 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q GLY B 21 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q ARG B 22 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q HIS B 23 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q MET B 24 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q GLU B 25 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q LEU B 26 UNP Q8A6L0 EXPRESSION TAG
SEQADV 5E1Q GLY B 415 UNP Q8A6L0 ASP 415 ENGINEERED MUTATION
SEQRES 1 A 655 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS ILE GLU
SEQRES 2 A 655 GLY ARG HIS MET GLU LEU SER PRO ASP GLY ASN LEU LYS
SEQRES 3 A 655 THR THR ILE THR ILE GLY ASP ARG LEU THR TYR ASP ILE
SEQRES 4 A 655 THR CYS ASN GLY ARG GLN ILE LEU THR PRO SER PRO ILE
SEQRES 5 A 655 SER MET THR LEU ASP ASN GLY THR VAL TRP GLY GLU ASN
SEQRES 6 A 655 ALA LYS LEU SER GLY THR SER ARG LYS SER VAL ASP GLU
SEQRES 7 A 655 MET ILE PRO SER PRO PHE TYR ARG ALA SER GLU LEU ARG
SEQRES 8 A 655 ASN HIS TYR ASN GLY LEU THR LEU ARG PHE LYS LYS ASP
SEQRES 9 A 655 TRP ASN VAL GLU PHE ARG ALA TYR ASN ASP GLY ILE ALA
SEQRES 10 A 655 TYR ARG PHE VAL ASN GLN GLY LYS LYS PRO PHE ARG VAL
SEQRES 11 A 655 VAL THR GLU VAL SER ASP TYR CYS PHE PRO SER ASP MET
SEQRES 12 A 655 THR ALA SER VAL PRO TYR VAL LYS SER GLY LYS ASP GLY
SEQRES 13 A 655 ASP TYR ASN SER GLN PHE PHE ASN SER PHE GLU ASN THR
SEQRES 14 A 655 TYR THR THR ASP LYS LEU SER LYS LEU ASN LYS GLN ARG
SEQRES 15 A 655 LEU MET PHE LEU PRO LEU VAL VAL ASP ALA GLY ASP GLY
SEQRES 16 A 655 VAL LYS VAL CYS ILE THR GLU SER ASP LEU GLU ASN TYR
SEQRES 17 A 655 PRO GLY LEU TYR LEU SER ALA SER GLU GLY ALA ASN ARG
SEQRES 18 A 655 LEU SER SER MET HIS ALA PRO TYR PRO LYS ARG THR VAL
SEQRES 19 A 655 GLN GLY GLY HIS ASN GLN LEU GLN MET LEU VAL LYS GLU
SEQRES 20 A 655 HIS GLU ASP TYR ILE ALA LYS VAL ASP LYS PRO ARG ASN
SEQRES 21 A 655 PHE PRO TRP ARG ILE ALA VAL VAL THR THR THR ASP LYS
SEQRES 22 A 655 ASP LEU ALA ALA THR ASN LEU SER TYR LEU LEU GLY ALA
SEQRES 23 A 655 PRO SER ARG MET SER ASP LEU SER TRP ILE LYS PRO GLY
SEQRES 24 A 655 LYS VAL ALA TRP ASP TRP TRP ASN ASP TRP ASN LEU ASP
SEQRES 25 A 655 GLY VAL ASP PHE VAL THR GLY VAL ASN ASN PRO THR TYR
SEQRES 26 A 655 LYS ALA TYR ILE ASP PHE ALA SER ALA ASN GLY ILE GLU
SEQRES 27 A 655 TYR VAL ILE LEU ASP GLU GLY TRP ALA VAL ASN LEU GLN
SEQRES 28 A 655 ALA ASP LEU MET GLN VAL VAL LYS GLU ILE ASP LEU LYS
SEQRES 29 A 655 GLU LEU VAL ASP TYR ALA ALA SER LYS ASN VAL GLY ILE
SEQRES 30 A 655 ILE LEU TRP ALA GLY TYR HIS ALA PHE GLU ARG ASP MET
SEQRES 31 A 655 GLU ASN VAL CYS ARG HIS TYR ALA GLU MET GLY VAL LYS
SEQRES 32 A 655 GLY PHE LYS VAL GLY PHE MET ASP ARG ASP ASP GLN GLU
SEQRES 33 A 655 MET THR ALA PHE ASN TYR ARG ALA ALA GLU MET CYS ALA
SEQRES 34 A 655 LYS TYR LYS LEU ILE LEU ASP LEU HIS GLY THR HIS LYS
SEQRES 35 A 655 PRO ALA GLY LEU ASN ARG THR TYR PRO ASN VAL LEU ASN
SEQRES 36 A 655 PHE GLU GLY VAL ASN GLY LEU GLU GLN MET LYS TRP SER
SEQRES 37 A 655 SER PRO SER VAL ASP GLN VAL LYS TYR ASP VAL MET ILE
SEQRES 38 A 655 PRO PHE ILE ARG GLN VAL SER GLY PRO MET ASP TYR THR
SEQRES 39 A 655 GLN GLY ALA MET ARG ASN ALA SER LYS GLY ASN TYR TYR
SEQRES 40 A 655 PRO CYS TYR SER GLU PRO MET SER GLN GLY THR ARG CYS
SEQRES 41 A 655 ARG GLN LEU ALA LEU TYR VAL VAL PHE GLU SER PRO PHE
SEQRES 42 A 655 ASN MET LEU CYS ASP THR PRO SER ASN TYR MET ARG GLU
SEQRES 43 A 655 PRO GLU SER THR ALA PHE ILE ALA GLU ILE PRO THR VAL
SEQRES 44 A 655 TRP ASP GLU SER ILE VAL LEU ASP GLY LYS MET GLY GLU
SEQRES 45 A 655 TYR ILE VAL THR ALA ARG ARG LYS GLY ASP VAL TRP TYR
SEQRES 46 A 655 VAL GLY GLY ILE THR ASP TRP SER ALA ARG ASP ILE GLU
SEQRES 47 A 655 VAL ASP CYS SER PHE LEU GLY ASP LYS SER TYR HIS ALA
SEQRES 48 A 655 THR LEU PHE LYS ASP GLY VAL ASN ALA HIS ARG ALA GLY
SEQRES 49 A 655 ARG ASP TYR LYS CYS GLU SER PHE PRO ILE LYS LYS ASP
SEQRES 50 A 655 GLY LYS LEU LYS VAL HIS LEU ALA PRO GLY GLY GLY PHE
SEQRES 51 A 655 ALA LEU LYS ILE LYS
SEQRES 1 B 655 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS ILE GLU
SEQRES 2 B 655 GLY ARG HIS MET GLU LEU SER PRO ASP GLY ASN LEU LYS
SEQRES 3 B 655 THR THR ILE THR ILE GLY ASP ARG LEU THR TYR ASP ILE
SEQRES 4 B 655 THR CYS ASN GLY ARG GLN ILE LEU THR PRO SER PRO ILE
SEQRES 5 B 655 SER MET THR LEU ASP ASN GLY THR VAL TRP GLY GLU ASN
SEQRES 6 B 655 ALA LYS LEU SER GLY THR SER ARG LYS SER VAL ASP GLU
SEQRES 7 B 655 MET ILE PRO SER PRO PHE TYR ARG ALA SER GLU LEU ARG
SEQRES 8 B 655 ASN HIS TYR ASN GLY LEU THR LEU ARG PHE LYS LYS ASP
SEQRES 9 B 655 TRP ASN VAL GLU PHE ARG ALA TYR ASN ASP GLY ILE ALA
SEQRES 10 B 655 TYR ARG PHE VAL ASN GLN GLY LYS LYS PRO PHE ARG VAL
SEQRES 11 B 655 VAL THR GLU VAL SER ASP TYR CYS PHE PRO SER ASP MET
SEQRES 12 B 655 THR ALA SER VAL PRO TYR VAL LYS SER GLY LYS ASP GLY
SEQRES 13 B 655 ASP TYR ASN SER GLN PHE PHE ASN SER PHE GLU ASN THR
SEQRES 14 B 655 TYR THR THR ASP LYS LEU SER LYS LEU ASN LYS GLN ARG
SEQRES 15 B 655 LEU MET PHE LEU PRO LEU VAL VAL ASP ALA GLY ASP GLY
SEQRES 16 B 655 VAL LYS VAL CYS ILE THR GLU SER ASP LEU GLU ASN TYR
SEQRES 17 B 655 PRO GLY LEU TYR LEU SER ALA SER GLU GLY ALA ASN ARG
SEQRES 18 B 655 LEU SER SER MET HIS ALA PRO TYR PRO LYS ARG THR VAL
SEQRES 19 B 655 GLN GLY GLY HIS ASN GLN LEU GLN MET LEU VAL LYS GLU
SEQRES 20 B 655 HIS GLU ASP TYR ILE ALA LYS VAL ASP LYS PRO ARG ASN
SEQRES 21 B 655 PHE PRO TRP ARG ILE ALA VAL VAL THR THR THR ASP LYS
SEQRES 22 B 655 ASP LEU ALA ALA THR ASN LEU SER TYR LEU LEU GLY ALA
SEQRES 23 B 655 PRO SER ARG MET SER ASP LEU SER TRP ILE LYS PRO GLY
SEQRES 24 B 655 LYS VAL ALA TRP ASP TRP TRP ASN ASP TRP ASN LEU ASP
SEQRES 25 B 655 GLY VAL ASP PHE VAL THR GLY VAL ASN ASN PRO THR TYR
SEQRES 26 B 655 LYS ALA TYR ILE ASP PHE ALA SER ALA ASN GLY ILE GLU
SEQRES 27 B 655 TYR VAL ILE LEU ASP GLU GLY TRP ALA VAL ASN LEU GLN
SEQRES 28 B 655 ALA ASP LEU MET GLN VAL VAL LYS GLU ILE ASP LEU LYS
SEQRES 29 B 655 GLU LEU VAL ASP TYR ALA ALA SER LYS ASN VAL GLY ILE
SEQRES 30 B 655 ILE LEU TRP ALA GLY TYR HIS ALA PHE GLU ARG ASP MET
SEQRES 31 B 655 GLU ASN VAL CYS ARG HIS TYR ALA GLU MET GLY VAL LYS
SEQRES 32 B 655 GLY PHE LYS VAL GLY PHE MET ASP ARG ASP ASP GLN GLU
SEQRES 33 B 655 MET THR ALA PHE ASN TYR ARG ALA ALA GLU MET CYS ALA
SEQRES 34 B 655 LYS TYR LYS LEU ILE LEU ASP LEU HIS GLY THR HIS LYS
SEQRES 35 B 655 PRO ALA GLY LEU ASN ARG THR TYR PRO ASN VAL LEU ASN
SEQRES 36 B 655 PHE GLU GLY VAL ASN GLY LEU GLU GLN MET LYS TRP SER
SEQRES 37 B 655 SER PRO SER VAL ASP GLN VAL LYS TYR ASP VAL MET ILE
SEQRES 38 B 655 PRO PHE ILE ARG GLN VAL SER GLY PRO MET ASP TYR THR
SEQRES 39 B 655 GLN GLY ALA MET ARG ASN ALA SER LYS GLY ASN TYR TYR
SEQRES 40 B 655 PRO CYS TYR SER GLU PRO MET SER GLN GLY THR ARG CYS
SEQRES 41 B 655 ARG GLN LEU ALA LEU TYR VAL VAL PHE GLU SER PRO PHE
SEQRES 42 B 655 ASN MET LEU CYS ASP THR PRO SER ASN TYR MET ARG GLU
SEQRES 43 B 655 PRO GLU SER THR ALA PHE ILE ALA GLU ILE PRO THR VAL
SEQRES 44 B 655 TRP ASP GLU SER ILE VAL LEU ASP GLY LYS MET GLY GLU
SEQRES 45 B 655 TYR ILE VAL THR ALA ARG ARG LYS GLY ASP VAL TRP TYR
SEQRES 46 B 655 VAL GLY GLY ILE THR ASP TRP SER ALA ARG ASP ILE GLU
SEQRES 47 B 655 VAL ASP CYS SER PHE LEU GLY ASP LYS SER TYR HIS ALA
SEQRES 48 B 655 THR LEU PHE LYS ASP GLY VAL ASN ALA HIS ARG ALA GLY
SEQRES 49 B 655 ARG ASP TYR LYS CYS GLU SER PHE PRO ILE LYS LYS ASP
SEQRES 50 B 655 GLY LYS LEU LYS VAL HIS LEU ALA PRO GLY GLY GLY PHE
SEQRES 51 B 655 ALA LEU LYS ILE LYS
HET BGC C 1 12
HET GLA C 2 11
HET GAL C 3 11
HET BGC D 1 12
HET GLA D 2 11
HET GAL D 3 11
HET CA A 701 1
HET GOL A 704 6
HET CA B 701 1
HET GOL B 704 6
HET GOL B 705 6
HETNAM BGC BETA-D-GLUCOPYRANOSE
HETNAM GLA ALPHA-D-GALACTOPYRANOSE
HETNAM GAL BETA-D-GALACTOPYRANOSE
HETNAM CA CALCIUM ION
HETNAM GOL GLYCEROL
HETSYN BGC BETA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
HETSYN GLA ALPHA-D-GALACTOSE; D-GALACTOSE; GALACTOSE; ALPHA D-
HETSYN 2 GLA GALACTOSE
HETSYN GAL BETA-D-GALACTOSE; D-GALACTOSE; GALACTOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 BGC 2(C6 H12 O6)
FORMUL 3 GLA 2(C6 H12 O6)
FORMUL 3 GAL 2(C6 H12 O6)
FORMUL 5 CA 2(CA 2+)
FORMUL 6 GOL 3(C3 H8 O3)
FORMUL 10 HOH *763(H2 O)
HELIX 1 AA1 ASP A 164 PHE A 170 1 7
HELIX 2 AA2 SER A 183 LEU A 185 5 3
HELIX 3 AA3 GLY A 244 LEU A 248 5 5
HELIX 4 AA4 THR A 278 THR A 285 1 8
HELIX 5 AA5 ASN A 286 LEU A 291 1 6
HELIX 6 AA6 ASN A 328 ASN A 342 1 15
HELIX 7 AA7 ASP A 369 SER A 379 1 11
HELIX 8 AA8 TYR A 390 ARG A 395 1 6
HELIX 9 AA9 ASP A 396 GLY A 408 1 13
HELIX 10 AB1 ASP A 421 TYR A 438 1 18
HELIX 11 AB2 GLY A 452 TYR A 457 1 6
HELIX 12 AB3 GLY A 468 TRP A 474 5 7
HELIX 13 AB4 ASP A 480 ILE A 488 1 9
HELIX 14 AB5 PRO A 489 SER A 495 5 7
HELIX 15 AB6 THR A 525 PHE A 536 1 12
HELIX 16 AB7 THR A 546 ARG A 552 1 7
HELIX 17 AB8 GLU A 553 ILE A 563 1 11
HELIX 18 AB9 ASP B 164 PHE B 170 1 7
HELIX 19 AC1 SER B 183 LEU B 185 5 3
HELIX 20 AC2 GLY B 244 LEU B 248 5 5
HELIX 21 AC3 THR B 278 THR B 285 1 8
HELIX 22 AC4 ASN B 286 GLY B 292 1 7
HELIX 23 AC5 ASN B 328 ASN B 342 1 15
HELIX 24 AC6 ASP B 369 SER B 379 1 11
HELIX 25 AC7 TYR B 390 ARG B 395 1 6
HELIX 26 AC8 ASP B 396 GLY B 408 1 13
HELIX 27 AC9 ASP B 421 TYR B 438 1 18
HELIX 28 AD1 GLY B 452 TYR B 457 1 6
HELIX 29 AD2 GLY B 468 TRP B 474 5 7
HELIX 30 AD3 ASP B 480 VAL B 486 1 7
HELIX 31 AD4 MET B 487 GLY B 496 5 10
HELIX 32 AD5 THR B 525 PHE B 536 1 12
HELIX 33 AD6 THR B 546 ARG B 552 1 7
HELIX 34 AD7 GLU B 553 ILE B 563 1 11
SHEET 1 AA1 5 ARG A 22 LEU A 26 0
SHEET 2 AA1 5 LEU A 32 ILE A 38 -1 O ILE A 36 N HIS A 23
SHEET 3 AA1 5 LEU A 42 CYS A 48 -1 O THR A 47 N LYS A 33
SHEET 4 AA1 5 ARG A 51 LEU A 63 -1 O SER A 57 N TYR A 44
SHEET 5 AA1 5 VAL A 68 TRP A 69 -1 O TRP A 69 N MET A 61
SHEET 1 AA2 6 ARG A 22 LEU A 26 0
SHEET 2 AA2 6 LEU A 32 ILE A 38 -1 O ILE A 36 N HIS A 23
SHEET 3 AA2 6 LEU A 42 CYS A 48 -1 O THR A 47 N LYS A 33
SHEET 4 AA2 6 ARG A 51 LEU A 63 -1 O SER A 57 N TYR A 44
SHEET 5 AA2 6 PHE A 135 SER A 142 -1 O VAL A 138 N THR A 62
SHEET 6 AA2 6 ALA A 260 VAL A 262 -1 O VAL A 262 N PHE A 135
SHEET 1 AA318 THR A 178 LYS A 181 0
SHEET 2 AA318 THR A 151 VAL A 154 -1 N ALA A 152 O ASP A 180
SHEET 3 AA318 LEU A 195 GLY A 200 -1 O VAL A 196 N SER A 153
SHEET 4 AA318 VAL A 203 SER A 210 -1 O VAL A 205 N VAL A 197
SHEET 5 AA318 TRP A 270 THR A 276 -1 O ILE A 272 N THR A 208
SHEET 6 AA318 GLY A 122 ASN A 129 -1 N TYR A 125 O ARG A 271
SHEET 7 AA318 TRP A 112 TYR A 119 -1 N TYR A 119 O GLY A 122
SHEET 8 AA318 GLU A 96 PHE A 108 -1 N LEU A 104 O PHE A 116
SHEET 9 AA318 LEU A 75 PRO A 88 -1 N GLU A 85 O ASN A 99
SHEET 10 AA318 LEU B 75 PRO B 88 -1 O SER B 76 N MET A 86
SHEET 11 AA318 GLU B 96 PHE B 108 -1 O LEU B 97 N ILE B 87
SHEET 12 AA318 TRP B 112 TYR B 119 -1 O PHE B 116 N LEU B 104
SHEET 13 AA318 GLY B 122 ASN B 129 -1 O GLY B 122 N TYR B 119
SHEET 14 AA318 TRP B 270 THR B 276 -1 O ARG B 271 N TYR B 125
SHEET 15 AA318 VAL B 203 SER B 210 -1 N CYS B 206 O VAL B 274
SHEET 16 AA318 LEU B 195 GLY B 200 -1 N VAL B 197 O VAL B 205
SHEET 17 AA318 THR B 151 VAL B 154 -1 N SER B 153 O VAL B 196
SHEET 18 AA318 THR B 178 LYS B 181 -1 O THR B 178 N VAL B 154
SHEET 1 AA410 ARG A 266 ASN A 267 0
SHEET 2 AA410 GLY A 122 ASN A 129 -1 N ASN A 129 O ARG A 266
SHEET 3 AA410 TRP A 112 TYR A 119 -1 N TYR A 119 O GLY A 122
SHEET 4 AA410 GLU A 96 PHE A 108 -1 N LEU A 104 O PHE A 116
SHEET 5 AA410 LEU A 75 PRO A 88 -1 N GLU A 85 O ASN A 99
SHEET 6 AA410 LEU B 75 PRO B 88 -1 O SER B 76 N MET A 86
SHEET 7 AA410 GLU B 96 PHE B 108 -1 O LEU B 97 N ILE B 87
SHEET 8 AA410 TRP B 112 TYR B 119 -1 O PHE B 116 N LEU B 104
SHEET 9 AA410 GLY B 122 ASN B 129 -1 O GLY B 122 N TYR B 119
SHEET 10 AA410 ARG B 266 ASN B 267 -1 O ARG B 266 N ASN B 129
SHEET 1 AA5 3 TYR A 144 CYS A 145 0
SHEET 2 AA5 3 ARG A 228 HIS A 233 -1 O LEU A 229 N TYR A 144
SHEET 3 AA5 3 LEU A 218 SER A 221 -1 N SER A 221 O SER A 230
SHEET 1 AA6 2 PRO A 237 GLY A 243 0
SHEET 2 AA6 2 GLN A 249 HIS A 255 -1 O LEU A 251 N VAL A 241
SHEET 1 AA7 2 GLY A 306 ALA A 309 0
SHEET 2 AA7 2 PHE A 540 LEU A 543 1 O LEU A 543 N VAL A 308
SHEET 1 AA8 5 TYR A 346 LEU A 349 0
SHEET 2 AA8 5 GLY A 383 GLY A 389 1 O ILE A 385 N LEU A 349
SHEET 3 AA8 5 GLY A 411 GLY A 415 1 O LYS A 413 N ALA A 388
SHEET 4 AA8 5 ILE A 441 LEU A 444 1 O ASP A 443 N VAL A 414
SHEET 5 AA8 5 VAL A 460 PHE A 463 1 O ASN A 462 N LEU A 444
SHEET 1 AA9 2 ASN A 507 ALA A 508 0
SHEET 2 AA9 2 SER A 522 GLN A 523 1 O SER A 522 N ALA A 508
SHEET 1 AB1 6 GLU A 569 LYS A 576 0
SHEET 2 AB1 6 TYR A 580 LYS A 587 -1 O ALA A 584 N ILE A 571
SHEET 3 AB1 6 VAL A 590 THR A 597 -1 O TYR A 592 N ARG A 585
SHEET 4 AB1 6 GLY A 656 LYS A 662 -1 O LEU A 659 N VAL A 593
SHEET 5 AB1 6 TYR A 616 ASP A 623 -1 N HIS A 617 O LYS A 662
SHEET 6 AB1 6 TYR A 634 ILE A 641 -1 O ILE A 641 N TYR A 616
SHEET 1 AB2 2 ARG A 602 ASP A 607 0
SHEET 2 AB2 2 LYS A 646 LEU A 651 -1 O LEU A 651 N ARG A 602
SHEET 1 AB3 5 ARG B 22 LEU B 26 0
SHEET 2 AB3 5 LEU B 32 ILE B 38 -1 O ILE B 36 N HIS B 23
SHEET 3 AB3 5 LEU B 42 CYS B 48 -1 O THR B 47 N LYS B 33
SHEET 4 AB3 5 ARG B 51 LEU B 63 -1 O SER B 57 N TYR B 44
SHEET 5 AB3 5 VAL B 68 TRP B 69 -1 O TRP B 69 N MET B 61
SHEET 1 AB4 6 ARG B 22 LEU B 26 0
SHEET 2 AB4 6 LEU B 32 ILE B 38 -1 O ILE B 36 N HIS B 23
SHEET 3 AB4 6 LEU B 42 CYS B 48 -1 O THR B 47 N LYS B 33
SHEET 4 AB4 6 ARG B 51 LEU B 63 -1 O SER B 57 N TYR B 44
SHEET 5 AB4 6 PHE B 135 SER B 142 -1 O THR B 139 N THR B 62
SHEET 6 AB4 6 ALA B 260 VAL B 262 -1 O VAL B 262 N PHE B 135
SHEET 1 AB5 3 TYR B 144 CYS B 145 0
SHEET 2 AB5 3 ARG B 228 HIS B 233 -1 O LEU B 229 N TYR B 144
SHEET 3 AB5 3 LEU B 218 SER B 221 -1 N TYR B 219 O MET B 232
SHEET 1 AB6 2 PRO B 237 GLY B 243 0
SHEET 2 AB6 2 GLN B 249 HIS B 255 -1 O GLU B 254 N LYS B 238
SHEET 1 AB7 2 GLY B 306 ALA B 309 0
SHEET 2 AB7 2 PHE B 540 LEU B 543 1 O LEU B 543 N VAL B 308
SHEET 1 AB8 5 TYR B 346 LEU B 349 0
SHEET 2 AB8 5 GLY B 383 GLY B 389 1 O ILE B 385 N LEU B 349
SHEET 3 AB8 5 GLY B 411 GLY B 415 1 O LYS B 413 N ALA B 388
SHEET 4 AB8 5 ILE B 441 LEU B 444 1 O ASP B 443 N VAL B 414
SHEET 5 AB8 5 VAL B 460 PHE B 463 1 O ASN B 462 N LEU B 444
SHEET 1 AB9 2 ASN B 507 ALA B 508 0
SHEET 2 AB9 2 SER B 522 GLN B 523 1 O SER B 522 N ALA B 508
SHEET 1 AC1 6 GLU B 569 LYS B 576 0
SHEET 2 AC1 6 TYR B 580 LYS B 587 -1 O ALA B 584 N ILE B 571
SHEET 3 AC1 6 VAL B 590 THR B 597 -1 O GLY B 594 N THR B 583
SHEET 4 AC1 6 GLY B 656 LYS B 662 -1 O ILE B 661 N TRP B 591
SHEET 5 AC1 6 TYR B 616 ASP B 623 -1 N PHE B 621 O ALA B 658
SHEET 6 AC1 6 TYR B 634 ILE B 641 -1 O PHE B 639 N ALA B 618
SHEET 1 AC2 2 ARG B 602 ASP B 607 0
SHEET 2 AC2 2 LYS B 646 LEU B 651 -1 O VAL B 649 N ILE B 604
LINK O1 BGC C 1 C1 GLA C 2 1555 1555 1.42
LINK O4 BGC C 1 C1 GAL C 3 1555 1555 1.42
LINK O1 BGC D 1 C1 GLA D 2 1555 1555 1.43
LINK O4 BGC D 1 C1 GAL D 3 1555 1555 1.42
LINK OE2 GLU A 174 CA CA A 701 1555 1555 2.40
LINK OE1 GLU A 464 CA CA A 701 1555 1555 2.66
LINK OE2 GLU A 464 CA CA A 701 1555 1555 2.46
LINK OE2 GLU A 470 CA CA A 701 1555 1555 2.30
LINK CA CA A 701 O HOH A1107 1555 1555 2.72
LINK CA CA A 701 O1 BGC C 1 1555 1555 3.04
LINK CA CA A 701 O2 BGC C 1 1555 1555 2.55
LINK CA CA A 701 O2 GLA C 2 1555 1555 2.25
LINK OE2 GLU B 174 CA CA B 701 1555 1555 2.34
LINK OE1 GLU B 464 CA CA B 701 1555 1555 2.73
LINK OE2 GLU B 464 CA CA B 701 1555 1555 2.34
LINK OE2 GLU B 470 CA CA B 701 1555 1555 2.29
LINK CA CA B 701 O HOH B 968 1555 1555 2.39
LINK CA CA B 701 O1 BGC D 1 1555 1555 3.04
LINK CA CA B 701 O2 BGC D 1 1555 1555 2.49
LINK CA CA B 701 O2 GLA D 2 1555 1555 2.37
CISPEP 1 LEU A 193 PRO A 194 0 -2.86
CISPEP 2 LEU B 193 PRO B 194 0 -2.16
CRYST1 60.620 100.624 237.079 90.00 90.00 90.00 P 21 21 21 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 0.016496 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009938 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004218 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
