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HEADER HYDROLASE 15-APR-16 5JD4
TITLE CRYSTAL STRUCTURE OF LAE6, AN ALPHA/BETA HYDROLASE ENZYME FROM THE
TITLE 2 METAGENOME OF LAKE ARREO, SPAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LAE6;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 77133;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P15TV LIC
KEYWDS ALPHA/BETA HYDROLASE, ESTERASE, METAGENOME, UNCULTURED BACTERIA,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.J.STOGIOS,X.XU,M.ALCAIDE,V.YIM,H.CUI,M.MARTINEZ-MARTINEZ,M.FERRER,
AUTHOR 2 A.SAVCHENKO
REVDAT 1 04-MAY-16 5JD4 0
JRNL AUTH M.MARTINEZ-MARTINEZ
JRNL TITL TO BE PUBLISHED
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.05 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.95
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.060
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.3
REMARK 3 NUMBER OF REFLECTIONS : 165467
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.130
REMARK 3 FREE R VALUE TEST SET COUNT : 1875
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 24.9542 - 4.8089 0.98 13980 161 0.1607 0.1758
REMARK 3 2 4.8089 - 3.8214 0.97 13790 158 0.1270 0.1701
REMARK 3 3 3.8214 - 3.3396 0.95 13526 156 0.1440 0.1805
REMARK 3 4 3.3396 - 3.0349 0.94 13466 158 0.1594 0.2135
REMARK 3 5 3.0349 - 2.8177 0.92 13112 153 0.1752 0.2291
REMARK 3 6 2.8177 - 2.6517 0.91 12976 149 0.1736 0.2146
REMARK 3 7 2.6517 - 2.5191 0.89 12724 150 0.1848 0.2368
REMARK 3 8 2.5191 - 2.4095 0.87 12489 126 0.1931 0.2603
REMARK 3 9 2.4095 - 2.3168 0.87 12280 148 0.2080 0.2666
REMARK 3 10 2.3168 - 2.2369 0.83 11881 142 0.2236 0.2734
REMARK 3 11 2.2369 - 2.1670 0.81 11670 120 0.2267 0.2888
REMARK 3 12 2.1670 - 2.1051 0.79 11206 143 0.2483 0.3230
REMARK 3 13 2.1051 - 2.0497 0.74 10492 111 0.2792 0.2995
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.870
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 : 0.003 20001
REMARK 3 ANGLE : 0.730 27117
REMARK 3 CHIRALITY : 0.028 2879
REMARK 3 PLANARITY : 0.004 3637
REMARK 3 DIHEDRAL : 11.888 7245
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 24
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID -1:12)
REMARK 3 ORIGIN FOR THE GROUP (A): 67.8775 91.8253 13.6766
REMARK 3 T TENSOR
REMARK 3 T11: 0.3244 T22: 0.4425
REMARK 3 T33: 0.3812 T12: 0.1028
REMARK 3 T13: -0.0574 T23: -0.1277
REMARK 3 L TENSOR
REMARK 3 L11: 8.6725 L22: 5.6968
REMARK 3 L33: 9.3047 L12: 6.7992
REMARK 3 L13: -7.5175 L23: -6.8546
REMARK 3 S TENSOR
REMARK 3 S11: -0.3626 S12: -1.3324 S13: -0.0307
REMARK 3 S21: 0.3838 S22: -0.0529 S23: -0.8586
REMARK 3 S31: -0.2159 S32: 1.0586 S33: 0.3466
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 13:77)
REMARK 3 ORIGIN FOR THE GROUP (A): 50.4382 77.1759 7.8238
REMARK 3 T TENSOR
REMARK 3 T11: 0.1692 T22: 0.3195
REMARK 3 T33: 0.2219 T12: -0.0117
REMARK 3 T13: 0.0793 T23: 0.0256
REMARK 3 L TENSOR
REMARK 3 L11: 1.9127 L22: 3.5898
REMARK 3 L33: 1.7713 L12: -0.4280
REMARK 3 L13: 0.0291 L23: 0.0972
REMARK 3 S TENSOR
REMARK 3 S11: -0.1147 S12: -0.2395 S13: -0.0790
REMARK 3 S21: 0.2674 S22: 0.1078 S23: -0.0442
REMARK 3 S31: 0.0768 S32: -0.0897 S33: 0.0115
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 78:315)
REMARK 3 ORIGIN FOR THE GROUP (A): 60.4785 76.4611 -3.6326
REMARK 3 T TENSOR
REMARK 3 T11: 0.1496 T22: 0.2058
REMARK 3 T33: 0.2422 T12: 0.0048
REMARK 3 T13: 0.0177 T23: -0.0204
REMARK 3 L TENSOR
REMARK 3 L11: 1.6362 L22: 1.5911
REMARK 3 L33: 1.3172 L12: -0.1918
REMARK 3 L13: -0.0502 L23: -0.0255
REMARK 3 S TENSOR
REMARK 3 S11: -0.0331 S12: -0.0200 S13: -0.1950
REMARK 3 S21: -0.0357 S22: 0.0327 S23: -0.1570
REMARK 3 S31: 0.1344 S32: -0.0034 S33: 0.0044
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN B AND RESID -1:55)
REMARK 3 ORIGIN FOR THE GROUP (A): 47.9677 96.4077 18.1624
REMARK 3 T TENSOR
REMARK 3 T11: 0.4652 T22: 0.2345
REMARK 3 T33: 0.2549 T12: 0.0049
REMARK 3 T13: -0.0340 T23: -0.0252
REMARK 3 L TENSOR
REMARK 3 L11: 3.0699 L22: 0.6617
REMARK 3 L33: 2.9495 L12: -0.5390
REMARK 3 L13: -0.7402 L23: -0.9945
REMARK 3 S TENSOR
REMARK 3 S11: 0.0557 S12: 0.3940 S13: 0.3281
REMARK 3 S21: -0.5708 S22: -0.0492 S23: 0.0321
REMARK 3 S31: 0.0990 S32: -0.2372 S33: -0.0067
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN B AND RESID 56:78)
REMARK 3 ORIGIN FOR THE GROUP (A): 36.0241 85.2869 37.6551
REMARK 3 T TENSOR
REMARK 3 T11: 0.2852 T22: 0.2988
REMARK 3 T33: 0.3522 T12: -0.1431
REMARK 3 T13: 0.0103 T23: 0.0456
REMARK 3 L TENSOR
REMARK 3 L11: 4.9731 L22: 8.3397
REMARK 3 L33: 1.2185 L12: -4.9298
REMARK 3 L13: -0.4094 L23: 1.8038
REMARK 3 S TENSOR
REMARK 3 S11: 0.0968 S12: -0.6080 S13: -0.5330
REMARK 3 S21: 0.2092 S22: -0.0926 S23: 0.6250
REMARK 3 S31: 0.2080 S32: -0.2986 S33: -0.0422
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN B AND RESID 79:315)
REMARK 3 ORIGIN FOR THE GROUP (A): 44.2633 101.0411 36.0433
REMARK 3 T TENSOR
REMARK 3 T11: 0.1802 T22: 0.1596
REMARK 3 T33: 0.2244 T12: -0.0115
REMARK 3 T13: -0.0005 T23: -0.0229
REMARK 3 L TENSOR
REMARK 3 L11: 1.6608 L22: 1.9028
REMARK 3 L33: 1.3333 L12: -0.1433
REMARK 3 L13: 0.0800 L23: 0.0070
REMARK 3 S TENSOR
REMARK 3 S11: -0.0217 S12: -0.0817 S13: 0.2140
REMARK 3 S21: -0.0634 S22: 0.0050 S23: 0.1654
REMARK 3 S31: -0.0584 S32: -0.1565 S33: 0.0107
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN C AND RESID -1:49)
REMARK 3 ORIGIN FOR THE GROUP (A): 103.1896 74.1444 15.7003
REMARK 3 T TENSOR
REMARK 3 T11: 0.2116 T22: 0.3859
REMARK 3 T33: 0.2443 T12: 0.0799
REMARK 3 T13: -0.0291 T23: 0.0108
REMARK 3 L TENSOR
REMARK 3 L11: 0.3278 L22: 7.9609
REMARK 3 L33: 4.2909 L12: 0.3424
REMARK 3 L13: -0.7582 L23: 2.4214
REMARK 3 S TENSOR
REMARK 3 S11: -0.0614 S12: -0.4716 S13: 0.3053
REMARK 3 S21: 0.3940 S22: 0.1017 S23: 0.5662
REMARK 3 S31: -0.0530 S32: 0.0454 S33: -0.0276
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN C AND RESID 50:77)
REMARK 3 ORIGIN FOR THE GROUP (A): 120.9167 79.6231 -4.5513
REMARK 3 T TENSOR
REMARK 3 T11: 0.1705 T22: 0.3670
REMARK 3 T33: 0.2251 T12: -0.0585
REMARK 3 T13: 0.0085 T23: 0.0192
REMARK 3 L TENSOR
REMARK 3 L11: 4.4752 L22: 9.6327
REMARK 3 L33: 2.0751 L12: 0.3283
REMARK 3 L13: 0.4894 L23: 0.8876
REMARK 3 S TENSOR
REMARK 3 S11: -0.1837 S12: 0.2424 S13: 0.1356
REMARK 3 S21: -0.3128 S22: 0.2319 S23: -0.1731
REMARK 3 S31: -0.2753 S32: 0.4360 S33: -0.0700
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN C AND RESID 78:315)
REMARK 3 ORIGIN FOR THE GROUP (A): 102.5133 79.2389 -3.9697
REMARK 3 T TENSOR
REMARK 3 T11: 0.1701 T22: 0.2133
REMARK 3 T33: 0.3041 T12: 0.0096
REMARK 3 T13: -0.0253 T23: 0.0347
REMARK 3 L TENSOR
REMARK 3 L11: 1.5880 L22: 1.3515
REMARK 3 L33: 1.1317 L12: -0.0148
REMARK 3 L13: 0.0948 L23: 0.3514
REMARK 3 S TENSOR
REMARK 3 S11: -0.0406 S12: 0.0100 S13: 0.2681
REMARK 3 S21: -0.0854 S22: -0.0007 S23: 0.1704
REMARK 3 S31: -0.1932 S32: -0.0204 S33: 0.0356
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN D AND RESID -1:56)
REMARK 3 ORIGIN FOR THE GROUP (A): 115.0651 60.0139 18.5509
REMARK 3 T TENSOR
REMARK 3 T11: 0.4753 T22: 0.2208
REMARK 3 T33: 0.3011 T12: 0.0059
REMARK 3 T13: 0.0025 T23: 0.0309
REMARK 3 L TENSOR
REMARK 3 L11: 3.8506 L22: 0.1044
REMARK 3 L33: 1.4802 L12: -0.4562
REMARK 3 L13: 0.4302 L23: 0.0388
REMARK 3 S TENSOR
REMARK 3 S11: 0.0997 S12: 0.4771 S13: -0.4279
REMARK 3 S21: -0.4119 S22: -0.0812 S23: -0.1271
REMARK 3 S31: -0.0434 S32: 0.0269 S33: -0.0020
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN D AND RESID 57:77)
REMARK 3 ORIGIN FOR THE GROUP (A): 126.8553 70.8185 37.3806
REMARK 3 T TENSOR
REMARK 3 T11: 0.2618 T22: 0.3266
REMARK 3 T33: 0.4674 T12: -0.1035
REMARK 3 T13: -0.0337 T23: -0.0103
REMARK 3 L TENSOR
REMARK 3 L11: 7.9825 L22: 4.7983
REMARK 3 L33: 2.2144 L12: -5.1593
REMARK 3 L13: 0.4045 L23: -1.4208
REMARK 3 S TENSOR
REMARK 3 S11: -0.0721 S12: -0.4654 S13: 0.3829
REMARK 3 S21: 0.2451 S22: -0.0674 S23: -0.5022
REMARK 3 S31: -0.1638 S32: 0.5208 S33: 0.1051
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN D AND RESID 78:315)
REMARK 3 ORIGIN FOR THE GROUP (A): 118.6833 55.4239 36.2116
REMARK 3 T TENSOR
REMARK 3 T11: 0.1912 T22: 0.1654
REMARK 3 T33: 0.3095 T12: -0.0008
REMARK 3 T13: -0.0154 T23: 0.0379
REMARK 3 L TENSOR
REMARK 3 L11: 1.4199 L22: 1.5831
REMARK 3 L33: 1.2866 L12: 0.1494
REMARK 3 L13: -0.4004 L23: 0.0171
REMARK 3 S TENSOR
REMARK 3 S11: -0.0407 S12: -0.0968 S13: -0.2688
REMARK 3 S21: -0.0078 S22: 0.0040 S23: -0.2256
REMARK 3 S31: 0.0951 S32: 0.2000 S33: 0.0273
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN E AND RESID -1:60)
REMARK 3 ORIGIN FOR THE GROUP (A): 70.8284 96.4656 65.8931
REMARK 3 T TENSOR
REMARK 3 T11: 0.4115 T22: 0.3737
REMARK 3 T33: 0.2469 T12: 0.0444
REMARK 3 T13: -0.0539 T23: -0.0424
REMARK 3 L TENSOR
REMARK 3 L11: 2.8871 L22: 2.2358
REMARK 3 L33: 3.8717 L12: -0.3419
REMARK 3 L13: -0.5505 L23: 1.4465
REMARK 3 S TENSOR
REMARK 3 S11: -0.1227 S12: -0.5588 S13: 0.2818
REMARK 3 S21: 0.5807 S22: 0.0854 S23: -0.0925
REMARK 3 S31: 0.0425 S32: 0.0049 S33: 0.0165
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN E AND RESID 61:77)
REMARK 3 ORIGIN FOR THE GROUP (A): 80.6713 84.9395 48.3604
REMARK 3 T TENSOR
REMARK 3 T11: 0.2779 T22: 0.3292
REMARK 3 T33: 0.3971 T12: 0.1025
REMARK 3 T13: -0.0092 T23: -0.0888
REMARK 3 L TENSOR
REMARK 3 L11: 4.6905 L22: 8.0083
REMARK 3 L33: 1.5280 L12: 5.4215
REMARK 3 L13: 0.0687 L23: -0.4504
REMARK 3 S TENSOR
REMARK 3 S11: 0.2265 S12: 0.3181 S13: -0.5065
REMARK 3 S21: 0.0687 S22: -0.1643 S23: -0.6681
REMARK 3 S31: 0.1985 S32: 0.1652 S33: -0.1142
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN E AND RESID 78:315)
REMARK 3 ORIGIN FOR THE GROUP (A): 73.3471 101.1432 49.2019
REMARK 3 T TENSOR
REMARK 3 T11: 0.2035 T22: 0.2230
REMARK 3 T33: 0.3363 T12: -0.0082
REMARK 3 T13: -0.0282 T23: -0.0666
REMARK 3 L TENSOR
REMARK 3 L11: 1.8132 L22: 1.5770
REMARK 3 L33: 1.5584 L12: -0.5456
REMARK 3 L13: 0.2651 L23: -0.2580
REMARK 3 S TENSOR
REMARK 3 S11: -0.0923 S12: -0.2344 S13: 0.4555
REMARK 3 S21: 0.1864 S22: 0.0298 S23: -0.3654
REMARK 3 S31: -0.1315 S32: 0.1795 S33: 0.0308
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (CHAIN F AND RESID -1:65)
REMARK 3 ORIGIN FOR THE GROUP (A): 96.2233 51.3428 -32.7772
REMARK 3 T TENSOR
REMARK 3 T11: 0.5202 T22: 0.5552
REMARK 3 T33: 0.3125 T12: 0.0695
REMARK 3 T13: -0.0366 T23: -0.0321
REMARK 3 L TENSOR
REMARK 3 L11: 2.0117 L22: 3.1082
REMARK 3 L33: 0.8661 L12: 0.9220
REMARK 3 L13: -0.1821 L23: -0.1479
REMARK 3 S TENSOR
REMARK 3 S11: 0.0129 S12: 0.6567 S13: 0.0038
REMARK 3 S21: -0.5453 S22: -0.0065 S23: 0.5083
REMARK 3 S31: -0.0427 S32: -0.0928 S33: -0.0179
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: (CHAIN F AND RESID 66:77)
REMARK 3 ORIGIN FOR THE GROUP (A): 108.1856 42.4701 -15.2119
REMARK 3 T TENSOR
REMARK 3 T11: 0.3955 T22: 0.2663
REMARK 3 T33: 0.3793 T12: 0.1091
REMARK 3 T13: -0.0418 T23: 0.0140
REMARK 3 L TENSOR
REMARK 3 L11: 8.6347 L22: 7.1611
REMARK 3 L33: 9.0143 L12: 6.8417
REMARK 3 L13: 5.5941 L23: 4.1035
REMARK 3 S TENSOR
REMARK 3 S11: 0.7075 S12: -0.1913 S13: -0.7745
REMARK 3 S21: 0.5853 S22: -0.2694 S23: -0.9311
REMARK 3 S31: 0.9900 S32: 0.2677 S33: -0.5283
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: (CHAIN F AND RESID 78:315)
REMARK 3 ORIGIN FOR THE GROUP (A): 91.2986 52.3712 -17.1912
REMARK 3 T TENSOR
REMARK 3 T11: 0.2214 T22: 0.2584
REMARK 3 T33: 0.3283 T12: 0.0039
REMARK 3 T13: -0.0753 T23: -0.0206
REMARK 3 L TENSOR
REMARK 3 L11: 1.5840 L22: 1.8574
REMARK 3 L33: 1.5692 L12: -0.4527
REMARK 3 L13: -0.1211 L23: 0.3310
REMARK 3 S TENSOR
REMARK 3 S11: 0.0276 S12: 0.2266 S13: -0.1658
REMARK 3 S21: -0.2262 S22: -0.1405 S23: 0.4579
REMARK 3 S31: 0.1450 S32: -0.1619 S33: 0.0689
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: (CHAIN G AND RESID -1:49)
REMARK 3 ORIGIN FOR THE GROUP (A): 94.2082 58.0730 69.0059
REMARK 3 T TENSOR
REMARK 3 T11: 0.6333 T22: 0.5490
REMARK 3 T33: 0.3588 T12: 0.0471
REMARK 3 T13: 0.0261 T23: 0.0729
REMARK 3 L TENSOR
REMARK 3 L11: 6.2567 L22: 0.1184
REMARK 3 L33: 3.1151 L12: 0.6736
REMARK 3 L13: -0.9994 L23: 0.0378
REMARK 3 S TENSOR
REMARK 3 S11: -0.0510 S12: -1.0808 S13: -0.7450
REMARK 3 S21: 0.5516 S22: 0.0267 S23: 0.1500
REMARK 3 S31: 0.1911 S32: 0.0095 S33: 0.0314
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: (CHAIN G AND RESID 50:78)
REMARK 3 ORIGIN FOR THE GROUP (A): 81.8381 72.2847 48.6605
REMARK 3 T TENSOR
REMARK 3 T11: 0.2510 T22: 0.2329
REMARK 3 T33: 0.3511 T12: 0.0757
REMARK 3 T13: 0.0306 T23: -0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 5.6506 L22: 5.3387
REMARK 3 L33: 3.0680 L12: 1.5184
REMARK 3 L13: 2.2158 L23: 1.7625
REMARK 3 S TENSOR
REMARK 3 S11: -0.1605 S12: -0.0785 S13: -0.0519
REMARK 3 S21: 0.1808 S22: -0.1600 S23: 0.4767
REMARK 3 S31: -0.2547 S32: -0.3646 S33: 0.2860
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: (CHAIN G AND RESID 79:315)
REMARK 3 ORIGIN FOR THE GROUP (A): 89.6474 55.3224 49.5487
REMARK 3 T TENSOR
REMARK 3 T11: 0.2373 T22: 0.2172
REMARK 3 T33: 0.3587 T12: -0.0202
REMARK 3 T13: 0.0558 T23: 0.0524
REMARK 3 L TENSOR
REMARK 3 L11: 1.8427 L22: 1.8854
REMARK 3 L33: 1.6336 L12: -0.4376
REMARK 3 L13: -0.4831 L23: 0.3132
REMARK 3 S TENSOR
REMARK 3 S11: -0.0865 S12: -0.2216 S13: -0.3792
REMARK 3 S21: 0.2661 S22: -0.0329 S23: 0.4075
REMARK 3 S31: 0.1523 S32: -0.2013 S33: 0.0588
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: (CHAIN H AND RESID -1:65)
REMARK 3 ORIGIN FOR THE GROUP (A): 66.3273 104.1133 -32.7426
REMARK 3 T TENSOR
REMARK 3 T11: 0.5650 T22: 0.5618
REMARK 3 T33: 0.3402 T12: 0.1377
REMARK 3 T13: 0.1081 T23: 0.0644
REMARK 3 L TENSOR
REMARK 3 L11: 1.0915 L22: 2.5640
REMARK 3 L33: 2.1571 L12: 0.2103
REMARK 3 L13: -0.4532 L23: 0.6277
REMARK 3 S TENSOR
REMARK 3 S11: 0.2191 S12: 0.6330 S13: 0.1643
REMARK 3 S21: -0.7640 S22: -0.1966 S23: -0.4972
REMARK 3 S31: 0.0164 S32: -0.0109 S33: -0.0621
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: (CHAIN H AND RESID 66:77)
REMARK 3 ORIGIN FOR THE GROUP (A): 54.6205 113.0435 -15.3595
REMARK 3 T TENSOR
REMARK 3 T11: 0.3337 T22: 0.2418
REMARK 3 T33: 0.4011 T12: 0.1156
REMARK 3 T13: 0.0702 T23: 0.0151
REMARK 3 L TENSOR
REMARK 3 L11: 7.6574 L22: 6.6630
REMARK 3 L33: 8.3821 L12: 5.1027
REMARK 3 L13: -2.9453 L23: -0.5045
REMARK 3 S TENSOR
REMARK 3 S11: 0.6660 S12: 0.1022 S13: 1.1521
REMARK 3 S21: 0.2770 S22: -0.0550 S23: 1.0639
REMARK 3 S31: -0.9815 S32: -0.3657 S33: -0.6466
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: (CHAIN H AND RESID 78:315)
REMARK 3 ORIGIN FOR THE GROUP (A): 71.4672 103.2290 -17.2303
REMARK 3 T TENSOR
REMARK 3 T11: 0.2276 T22: 0.2599
REMARK 3 T33: 0.4019 T12: 0.0068
REMARK 3 T13: 0.0905 T23: 0.0400
REMARK 3 L TENSOR
REMARK 3 L11: 1.4393 L22: 2.1079
REMARK 3 L33: 1.4105 L12: -0.3935
REMARK 3 L13: 0.0068 L23: -0.2503
REMARK 3 S TENSOR
REMARK 3 S11: 0.0596 S12: 0.2409 S13: 0.2508
REMARK 3 S21: -0.2829 S22: -0.1173 S23: -0.5972
REMARK 3 S31: -0.1319 S32: 0.1747 S33: 0.0204
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 5JD4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-APR-16.
REMARK 100 THE DEPOSITION ID IS D_1000220343.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 177343
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 24.952
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.9
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.07200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 21.6600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.09
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.60600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.520
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: BALBES
REMARK 200 STARTING MODEL: 1EVQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS PH 8.5, 0.2 M AMMONIUM
REMARK 280 SULFATE, 25% (W/V) PEG3350. CRYOPROTECTANT: 12% GLYCEROL AND
REMARK 280 PARATONE-N OIL., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E
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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, F
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: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, G
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 -20
REMARK 465 GLY A -19
REMARK 465 SER A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 GLY A -8
REMARK 465 ARG A -7
REMARK 465 GLU A -6
REMARK 465 ASN A -5
REMARK 465 LEU A -4
REMARK 465 TYR A -3
REMARK 465 PHE A -2
REMARK 465 MET B -20
REMARK 465 GLY B -19
REMARK 465 SER B -18
REMARK 465 SER B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 SER B -10
REMARK 465 SER B -9
REMARK 465 GLY B -8
REMARK 465 ARG B -7
REMARK 465 GLU B -6
REMARK 465 ASN B -5
REMARK 465 LEU B -4
REMARK 465 TYR B -3
REMARK 465 PHE B -2
REMARK 465 MET C -20
REMARK 465 GLY C -19
REMARK 465 SER C -18
REMARK 465 SER C -17
REMARK 465 HIS C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 SER C -10
REMARK 465 SER C -9
REMARK 465 GLY C -8
REMARK 465 ARG C -7
REMARK 465 GLU C -6
REMARK 465 ASN C -5
REMARK 465 LEU C -4
REMARK 465 TYR C -3
REMARK 465 PHE C -2
REMARK 465 MET D -20
REMARK 465 GLY D -19
REMARK 465 SER D -18
REMARK 465 SER D -17
REMARK 465 HIS D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 SER D -10
REMARK 465 SER D -9
REMARK 465 GLY D -8
REMARK 465 ARG D -7
REMARK 465 GLU D -6
REMARK 465 ASN D -5
REMARK 465 LEU D -4
REMARK 465 TYR D -3
REMARK 465 PHE D -2
REMARK 465 MET E -20
REMARK 465 GLY E -19
REMARK 465 SER E -18
REMARK 465 SER E -17
REMARK 465 HIS E -16
REMARK 465 HIS E -15
REMARK 465 HIS E -14
REMARK 465 HIS E -13
REMARK 465 HIS E -12
REMARK 465 HIS E -11
REMARK 465 SER E -10
REMARK 465 SER E -9
REMARK 465 GLY E -8
REMARK 465 ARG E -7
REMARK 465 GLU E -6
REMARK 465 ASN E -5
REMARK 465 LEU E -4
REMARK 465 TYR E -3
REMARK 465 PHE E -2
REMARK 465 MET F -20
REMARK 465 GLY F -19
REMARK 465 SER F -18
REMARK 465 SER F -17
REMARK 465 HIS F -16
REMARK 465 HIS F -15
REMARK 465 HIS F -14
REMARK 465 HIS F -13
REMARK 465 HIS F -12
REMARK 465 HIS F -11
REMARK 465 SER F -10
REMARK 465 SER F -9
REMARK 465 GLY F -8
REMARK 465 ARG F -7
REMARK 465 GLU F -6
REMARK 465 ASN F -5
REMARK 465 LEU F -4
REMARK 465 TYR F -3
REMARK 465 PHE F -2
REMARK 465 MET G -20
REMARK 465 GLY G -19
REMARK 465 SER G -18
REMARK 465 SER G -17
REMARK 465 HIS G -16
REMARK 465 HIS G -15
REMARK 465 HIS G -14
REMARK 465 HIS G -13
REMARK 465 HIS G -12
REMARK 465 HIS G -11
REMARK 465 SER G -10
REMARK 465 SER G -9
REMARK 465 GLY G -8
REMARK 465 ARG G -7
REMARK 465 GLU G -6
REMARK 465 ASN G -5
REMARK 465 LEU G -4
REMARK 465 TYR G -3
REMARK 465 PHE G -2
REMARK 465 MET H -20
REMARK 465 GLY H -19
REMARK 465 SER H -18
REMARK 465 SER H -17
REMARK 465 HIS H -16
REMARK 465 HIS H -15
REMARK 465 HIS H -14
REMARK 465 HIS H -13
REMARK 465 HIS H -12
REMARK 465 HIS H -11
REMARK 465 SER H -10
REMARK 465 SER H -9
REMARK 465 GLY H -8
REMARK 465 ARG H -7
REMARK 465 GLU H -6
REMARK 465 ASN H -5
REMARK 465 LEU H -4
REMARK 465 TYR H -3
REMARK 465 PHE H -2
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 SER A 161 OG
REMARK 470 SER B 161 OG
REMARK 470 SER C 161 OG
REMARK 470 SER D 161 OG
REMARK 470 SER E 161 OG
REMARK 470 SER F 161 OG
REMARK 470 SER G 161 OG
REMARK 470 SER H 161 OG
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 C 596 O HOH C 650 1.85
REMARK 500 ND2 ASN B 8 O HOH B 501 1.91
REMARK 500 O HOH H 695 O HOH H 707 1.92
REMARK 500 O HOH F 736 O HOH F 753 1.92
REMARK 500 NE ARG G 263 O3 GOL G 408 1.97
REMARK 500 O HOH A 672 O HOH A 778 2.10
REMARK 500 O HOH C 700 O HOH C 772 2.10
REMARK 500 O HOH G 718 O HOH G 740 2.14
REMARK 500 O HOH D 616 O HOH D 776 2.17
REMARK 500 O HOH D 653 O HOH D 698 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 ASN A 95 -165.78 -164.25
REMARK 500 SER A 161 -113.37 61.41
REMARK 500 TYR A 189 70.62 23.15
REMARK 500 PHE A 209 -66.75 68.18
REMARK 500 LEU A 291 44.26 -95.46
REMARK 500 ASN B 95 -164.95 -163.22
REMARK 500 SER B 161 -112.81 56.82
REMARK 500 TYR B 189 67.35 21.19
REMARK 500 PHE B 209 -67.64 65.95
REMARK 500 LEU B 291 40.63 -92.97
REMARK 500 ALA C 62 19.99 -142.64
REMARK 500 ASN C 95 -165.61 -162.11
REMARK 500 SER C 161 -117.07 59.39
REMARK 500 TYR C 189 67.11 23.48
REMARK 500 PHE C 209 -70.63 65.34
REMARK 500 ASP C 226 -1.23 81.35
REMARK 500 LEU C 291 45.60 -94.46
REMARK 500 ASN D 95 -163.56 -164.97
REMARK 500 SER D 161 -110.19 61.73
REMARK 500 TYR D 189 66.97 20.60
REMARK 500 PHE D 209 -66.17 67.73
REMARK 500 LEU D 291 42.15 -96.68
REMARK 500 ALA E 62 11.91 -141.72
REMARK 500 ASN E 95 -164.66 -166.90
REMARK 500 SER E 161 -114.60 58.85
REMARK 500 TYR E 189 65.66 21.15
REMARK 500 PHE E 209 -66.51 61.08
REMARK 500 ASP E 226 6.80 84.51
REMARK 500 LEU E 291 46.75 -88.72
REMARK 500 ASN F 95 -164.49 -168.12
REMARK 500 SER F 161 -115.07 54.80
REMARK 500 TYR F 189 66.40 22.30
REMARK 500 PHE F 209 -67.14 61.70
REMARK 500 LEU F 291 43.48 -92.73
REMARK 500 ASN G 95 -160.16 -165.42
REMARK 500 SER G 161 -114.30 60.06
REMARK 500 PHE G 184 147.01 -172.12
REMARK 500 TYR G 189 65.37 21.72
REMARK 500 SER G 198 176.51 -59.86
REMARK 500 PHE G 209 -67.09 61.56
REMARK 500 LEU G 291 42.38 -91.61
REMARK 500 GLU H 75 -73.53 -84.51
REMARK 500 PHE H 91 19.80 59.85
REMARK 500 ASN H 95 -162.55 -166.15
REMARK 500 SER H 161 -116.81 59.85
REMARK 500 TYR H 189 65.99 23.59
REMARK 500 PHE H 209 -65.50 60.30
REMARK 500 LEU H 291 46.60 -91.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 822 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH B 815 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH B 816 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH B 817 DISTANCE = 6.95 ANGSTROMS
REMARK 525 HOH C 835 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH C 836 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH C 837 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH C 838 DISTANCE = 6.37 ANGSTROMS
REMARK 525 HOH C 839 DISTANCE = 6.49 ANGSTROMS
REMARK 525 HOH C 841 DISTANCE = 7.83 ANGSTROMS
REMARK 525 HOH D 798 DISTANCE = 6.07 ANGSTROMS
REMARK 525 HOH D 801 DISTANCE = 6.93 ANGSTROMS
REMARK 525 HOH D 803 DISTANCE = 7.22 ANGSTROMS
REMARK 525 HOH E 783 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH F 802 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH F 804 DISTANCE = 6.26 ANGSTROMS
REMARK 525 HOH F 805 DISTANCE = 7.14 ANGSTROMS
REMARK 525 HOH G 780 DISTANCE = 6.77 ANGSTROMS
REMARK 525 HOH H 758 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH H 759 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH H 760 DISTANCE = 6.92 ANGSTROMS
REMARK 525 HOH H 761 DISTANCE = 7.10 ANGSTROMS
REMARK 525 HOH H 762 DISTANCE = 7.16 ANGSTROMS
REMARK 525 HOH H 763 DISTANCE = 7.38 ANGSTROMS
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 PE3 A 406
REMARK 610 PE3 D 408
REMARK 610 PE3 H 405
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PE3 A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BAM A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BAM B 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BAM C 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PE3 D 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BAM D 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL E 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL E 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL E 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL E 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BAM E 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL F 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL F 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL F 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL F 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BAM F 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 G 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL G 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL G 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL G 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL G 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL G 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL G 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL G 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BAM G 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL H 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL H 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PE3 H 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BAM H 406
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5JD3 RELATED DB: PDB
REMARK 900 RELATED ID: 5JD5 RELATED DB: PDB
REMARK 900 RELATED ID: 5JD6 RELATED DB: PDB
DBREF 5JD4 A -20 315 PDB 5JD4 5JD4 -20 315
DBREF 5JD4 B -20 315 PDB 5JD4 5JD4 -20 315
DBREF 5JD4 C -20 315 PDB 5JD4 5JD4 -20 315
DBREF 5JD4 D -20 315 PDB 5JD4 5JD4 -20 315
DBREF 5JD4 E -20 315 PDB 5JD4 5JD4 -20 315
DBREF 5JD4 F -20 315 PDB 5JD4 5JD4 -20 315
DBREF 5JD4 G -20 315 PDB 5JD4 5JD4 -20 315
DBREF 5JD4 H -20 315 PDB 5JD4 5JD4 -20 315
SEQRES 1 A 336 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 336 ARG GLU ASN LEU TYR PHE GLN GLY MET LEU LEU PRO GLU
SEQRES 3 A 336 THR ARG ASN LEU LEU ASP LEU MET ASP ALA ALA THR ARG
SEQRES 4 A 336 GLY GLY ARG PRO ARG LEU GLU THR LEU PRO HIS ALA VAL
SEQRES 5 A 336 GLY ARG LYS ALA VAL ASP LYS MET SER GLU ASP GLY GLU
SEQRES 6 A 336 ALA ASP PRO PRO GLU VAL ALA GLU VAL ALA ASN GLY GLY
SEQRES 7 A 336 PHE ALA GLY PRO ALA SER GLU ILE ARG PHE ARG ARG TYR
SEQRES 8 A 336 ARG PRO LEU GLY GLU ALA ALA GLY LEU LEU PRO THR LEU
SEQRES 9 A 336 ILE TYR TYR HIS GLY GLY GLY PHE VAL ILE GLY ASN ILE
SEQRES 10 A 336 GLU THR HIS ASP SER THR CYS ARG ARG LEU ALA ASN LYS
SEQRES 11 A 336 SER ARG CYS GLN VAL ILE SER ILE ASP TYR ARG LEU ALA
SEQRES 12 A 336 PRO GLU HIS PRO PHE PRO ALA PRO ILE ASP ASP GLY ILE
SEQRES 13 A 336 ALA ALA PHE ARG HIS ILE ARG ASP ASN ALA GLU SER PHE
SEQRES 14 A 336 GLY ALA ASP ALA ALA ARG LEU ALA VAL GLY GLY ASP SER
SEQRES 15 A 336 ALA GLY GLY ALA MET ALA ALA VAL VAL CYS GLN ALA CYS
SEQRES 16 A 336 ARG ASP ALA GLY GLU THR GLY PRO ALA PHE GLN MET LEU
SEQRES 17 A 336 ILE TYR PRO ALA THR ASP SER SER ARG GLU SER ALA SER
SEQRES 18 A 336 ARG VAL ALA PHE ALA GLU GLY TYR PHE LEU SER LYS ALA
SEQRES 19 A 336 LEU MET ASP TRP PHE TRP GLU ALA TYR VAL PRO GLU ASP
SEQRES 20 A 336 THR ASP LEU THR ASP LEU ARG LEU SER PRO LEU LEU ALA
SEQRES 21 A 336 THR ASP PHE THR GLY LEU PRO PRO ALA PHE VAL LEU THR
SEQRES 22 A 336 ALA GLY TYR ASP PRO LEU ARG ASP GLU GLY ARG ALA TYR
SEQRES 23 A 336 ALA ASP ARG LEU ILE GLU ALA GLY ILE LYS THR THR TYR
SEQRES 24 A 336 VAL ASN TYR PRO GLY THR ILE HIS GLY PHE PHE SER LEU
SEQRES 25 A 336 THR ARG PHE LEU SER GLN GLY LEU LYS ALA ASN ASP GLU
SEQRES 26 A 336 ALA ALA ALA VAL MET GLY ALA HIS PHE GLY THR
SEQRES 1 B 336 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 336 ARG GLU ASN LEU TYR PHE GLN GLY MET LEU LEU PRO GLU
SEQRES 3 B 336 THR ARG ASN LEU LEU ASP LEU MET ASP ALA ALA THR ARG
SEQRES 4 B 336 GLY GLY ARG PRO ARG LEU GLU THR LEU PRO HIS ALA VAL
SEQRES 5 B 336 GLY ARG LYS ALA VAL ASP LYS MET SER GLU ASP GLY GLU
SEQRES 6 B 336 ALA ASP PRO PRO GLU VAL ALA GLU VAL ALA ASN GLY GLY
SEQRES 7 B 336 PHE ALA GLY PRO ALA SER GLU ILE ARG PHE ARG ARG TYR
SEQRES 8 B 336 ARG PRO LEU GLY GLU ALA ALA GLY LEU LEU PRO THR LEU
SEQRES 9 B 336 ILE TYR TYR HIS GLY GLY GLY PHE VAL ILE GLY ASN ILE
SEQRES 10 B 336 GLU THR HIS ASP SER THR CYS ARG ARG LEU ALA ASN LYS
SEQRES 11 B 336 SER ARG CYS GLN VAL ILE SER ILE ASP TYR ARG LEU ALA
SEQRES 12 B 336 PRO GLU HIS PRO PHE PRO ALA PRO ILE ASP ASP GLY ILE
SEQRES 13 B 336 ALA ALA PHE ARG HIS ILE ARG ASP ASN ALA GLU SER PHE
SEQRES 14 B 336 GLY ALA ASP ALA ALA ARG LEU ALA VAL GLY GLY ASP SER
SEQRES 15 B 336 ALA GLY GLY ALA MET ALA ALA VAL VAL CYS GLN ALA CYS
SEQRES 16 B 336 ARG ASP ALA GLY GLU THR GLY PRO ALA PHE GLN MET LEU
SEQRES 17 B 336 ILE TYR PRO ALA THR ASP SER SER ARG GLU SER ALA SER
SEQRES 18 B 336 ARG VAL ALA PHE ALA GLU GLY TYR PHE LEU SER LYS ALA
SEQRES 19 B 336 LEU MET ASP TRP PHE TRP GLU ALA TYR VAL PRO GLU ASP
SEQRES 20 B 336 THR ASP LEU THR ASP LEU ARG LEU SER PRO LEU LEU ALA
SEQRES 21 B 336 THR ASP PHE THR GLY LEU PRO PRO ALA PHE VAL LEU THR
SEQRES 22 B 336 ALA GLY TYR ASP PRO LEU ARG ASP GLU GLY ARG ALA TYR
SEQRES 23 B 336 ALA ASP ARG LEU ILE GLU ALA GLY ILE LYS THR THR TYR
SEQRES 24 B 336 VAL ASN TYR PRO GLY THR ILE HIS GLY PHE PHE SER LEU
SEQRES 25 B 336 THR ARG PHE LEU SER GLN GLY LEU LYS ALA ASN ASP GLU
SEQRES 26 B 336 ALA ALA ALA VAL MET GLY ALA HIS PHE GLY THR
SEQRES 1 C 336 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 336 ARG GLU ASN LEU TYR PHE GLN GLY MET LEU LEU PRO GLU
SEQRES 3 C 336 THR ARG ASN LEU LEU ASP LEU MET ASP ALA ALA THR ARG
SEQRES 4 C 336 GLY GLY ARG PRO ARG LEU GLU THR LEU PRO HIS ALA VAL
SEQRES 5 C 336 GLY ARG LYS ALA VAL ASP LYS MET SER GLU ASP GLY GLU
SEQRES 6 C 336 ALA ASP PRO PRO GLU VAL ALA GLU VAL ALA ASN GLY GLY
SEQRES 7 C 336 PHE ALA GLY PRO ALA SER GLU ILE ARG PHE ARG ARG TYR
SEQRES 8 C 336 ARG PRO LEU GLY GLU ALA ALA GLY LEU LEU PRO THR LEU
SEQRES 9 C 336 ILE TYR TYR HIS GLY GLY GLY PHE VAL ILE GLY ASN ILE
SEQRES 10 C 336 GLU THR HIS ASP SER THR CYS ARG ARG LEU ALA ASN LYS
SEQRES 11 C 336 SER ARG CYS GLN VAL ILE SER ILE ASP TYR ARG LEU ALA
SEQRES 12 C 336 PRO GLU HIS PRO PHE PRO ALA PRO ILE ASP ASP GLY ILE
SEQRES 13 C 336 ALA ALA PHE ARG HIS ILE ARG ASP ASN ALA GLU SER PHE
SEQRES 14 C 336 GLY ALA ASP ALA ALA ARG LEU ALA VAL GLY GLY ASP SER
SEQRES 15 C 336 ALA GLY GLY ALA MET ALA ALA VAL VAL CYS GLN ALA CYS
SEQRES 16 C 336 ARG ASP ALA GLY GLU THR GLY PRO ALA PHE GLN MET LEU
SEQRES 17 C 336 ILE TYR PRO ALA THR ASP SER SER ARG GLU SER ALA SER
SEQRES 18 C 336 ARG VAL ALA PHE ALA GLU GLY TYR PHE LEU SER LYS ALA
SEQRES 19 C 336 LEU MET ASP TRP PHE TRP GLU ALA TYR VAL PRO GLU ASP
SEQRES 20 C 336 THR ASP LEU THR ASP LEU ARG LEU SER PRO LEU LEU ALA
SEQRES 21 C 336 THR ASP PHE THR GLY LEU PRO PRO ALA PHE VAL LEU THR
SEQRES 22 C 336 ALA GLY TYR ASP PRO LEU ARG ASP GLU GLY ARG ALA TYR
SEQRES 23 C 336 ALA ASP ARG LEU ILE GLU ALA GLY ILE LYS THR THR TYR
SEQRES 24 C 336 VAL ASN TYR PRO GLY THR ILE HIS GLY PHE PHE SER LEU
SEQRES 25 C 336 THR ARG PHE LEU SER GLN GLY LEU LYS ALA ASN ASP GLU
SEQRES 26 C 336 ALA ALA ALA VAL MET GLY ALA HIS PHE GLY THR
SEQRES 1 D 336 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 336 ARG GLU ASN LEU TYR PHE GLN GLY MET LEU LEU PRO GLU
SEQRES 3 D 336 THR ARG ASN LEU LEU ASP LEU MET ASP ALA ALA THR ARG
SEQRES 4 D 336 GLY GLY ARG PRO ARG LEU GLU THR LEU PRO HIS ALA VAL
SEQRES 5 D 336 GLY ARG LYS ALA VAL ASP LYS MET SER GLU ASP GLY GLU
SEQRES 6 D 336 ALA ASP PRO PRO GLU VAL ALA GLU VAL ALA ASN GLY GLY
SEQRES 7 D 336 PHE ALA GLY PRO ALA SER GLU ILE ARG PHE ARG ARG TYR
SEQRES 8 D 336 ARG PRO LEU GLY GLU ALA ALA GLY LEU LEU PRO THR LEU
SEQRES 9 D 336 ILE TYR TYR HIS GLY GLY GLY PHE VAL ILE GLY ASN ILE
SEQRES 10 D 336 GLU THR HIS ASP SER THR CYS ARG ARG LEU ALA ASN LYS
SEQRES 11 D 336 SER ARG CYS GLN VAL ILE SER ILE ASP TYR ARG LEU ALA
SEQRES 12 D 336 PRO GLU HIS PRO PHE PRO ALA PRO ILE ASP ASP GLY ILE
SEQRES 13 D 336 ALA ALA PHE ARG HIS ILE ARG ASP ASN ALA GLU SER PHE
SEQRES 14 D 336 GLY ALA ASP ALA ALA ARG LEU ALA VAL GLY GLY ASP SER
SEQRES 15 D 336 ALA GLY GLY ALA MET ALA ALA VAL VAL CYS GLN ALA CYS
SEQRES 16 D 336 ARG ASP ALA GLY GLU THR GLY PRO ALA PHE GLN MET LEU
SEQRES 17 D 336 ILE TYR PRO ALA THR ASP SER SER ARG GLU SER ALA SER
SEQRES 18 D 336 ARG VAL ALA PHE ALA GLU GLY TYR PHE LEU SER LYS ALA
SEQRES 19 D 336 LEU MET ASP TRP PHE TRP GLU ALA TYR VAL PRO GLU ASP
SEQRES 20 D 336 THR ASP LEU THR ASP LEU ARG LEU SER PRO LEU LEU ALA
SEQRES 21 D 336 THR ASP PHE THR GLY LEU PRO PRO ALA PHE VAL LEU THR
SEQRES 22 D 336 ALA GLY TYR ASP PRO LEU ARG ASP GLU GLY ARG ALA TYR
SEQRES 23 D 336 ALA ASP ARG LEU ILE GLU ALA GLY ILE LYS THR THR TYR
SEQRES 24 D 336 VAL ASN TYR PRO GLY THR ILE HIS GLY PHE PHE SER LEU
SEQRES 25 D 336 THR ARG PHE LEU SER GLN GLY LEU LYS ALA ASN ASP GLU
SEQRES 26 D 336 ALA ALA ALA VAL MET GLY ALA HIS PHE GLY THR
SEQRES 1 E 336 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 E 336 ARG GLU ASN LEU TYR PHE GLN GLY MET LEU LEU PRO GLU
SEQRES 3 E 336 THR ARG ASN LEU LEU ASP LEU MET ASP ALA ALA THR ARG
SEQRES 4 E 336 GLY GLY ARG PRO ARG LEU GLU THR LEU PRO HIS ALA VAL
SEQRES 5 E 336 GLY ARG LYS ALA VAL ASP LYS MET SER GLU ASP GLY GLU
SEQRES 6 E 336 ALA ASP PRO PRO GLU VAL ALA GLU VAL ALA ASN GLY GLY
SEQRES 7 E 336 PHE ALA GLY PRO ALA SER GLU ILE ARG PHE ARG ARG TYR
SEQRES 8 E 336 ARG PRO LEU GLY GLU ALA ALA GLY LEU LEU PRO THR LEU
SEQRES 9 E 336 ILE TYR TYR HIS GLY GLY GLY PHE VAL ILE GLY ASN ILE
SEQRES 10 E 336 GLU THR HIS ASP SER THR CYS ARG ARG LEU ALA ASN LYS
SEQRES 11 E 336 SER ARG CYS GLN VAL ILE SER ILE ASP TYR ARG LEU ALA
SEQRES 12 E 336 PRO GLU HIS PRO PHE PRO ALA PRO ILE ASP ASP GLY ILE
SEQRES 13 E 336 ALA ALA PHE ARG HIS ILE ARG ASP ASN ALA GLU SER PHE
SEQRES 14 E 336 GLY ALA ASP ALA ALA ARG LEU ALA VAL GLY GLY ASP SER
SEQRES 15 E 336 ALA GLY GLY ALA MET ALA ALA VAL VAL CYS GLN ALA CYS
SEQRES 16 E 336 ARG ASP ALA GLY GLU THR GLY PRO ALA PHE GLN MET LEU
SEQRES 17 E 336 ILE TYR PRO ALA THR ASP SER SER ARG GLU SER ALA SER
SEQRES 18 E 336 ARG VAL ALA PHE ALA GLU GLY TYR PHE LEU SER LYS ALA
SEQRES 19 E 336 LEU MET ASP TRP PHE TRP GLU ALA TYR VAL PRO GLU ASP
SEQRES 20 E 336 THR ASP LEU THR ASP LEU ARG LEU SER PRO LEU LEU ALA
SEQRES 21 E 336 THR ASP PHE THR GLY LEU PRO PRO ALA PHE VAL LEU THR
SEQRES 22 E 336 ALA GLY TYR ASP PRO LEU ARG ASP GLU GLY ARG ALA TYR
SEQRES 23 E 336 ALA ASP ARG LEU ILE GLU ALA GLY ILE LYS THR THR TYR
SEQRES 24 E 336 VAL ASN TYR PRO GLY THR ILE HIS GLY PHE PHE SER LEU
SEQRES 25 E 336 THR ARG PHE LEU SER GLN GLY LEU LYS ALA ASN ASP GLU
SEQRES 26 E 336 ALA ALA ALA VAL MET GLY ALA HIS PHE GLY THR
SEQRES 1 F 336 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 F 336 ARG GLU ASN LEU TYR PHE GLN GLY MET LEU LEU PRO GLU
SEQRES 3 F 336 THR ARG ASN LEU LEU ASP LEU MET ASP ALA ALA THR ARG
SEQRES 4 F 336 GLY GLY ARG PRO ARG LEU GLU THR LEU PRO HIS ALA VAL
SEQRES 5 F 336 GLY ARG LYS ALA VAL ASP LYS MET SER GLU ASP GLY GLU
SEQRES 6 F 336 ALA ASP PRO PRO GLU VAL ALA GLU VAL ALA ASN GLY GLY
SEQRES 7 F 336 PHE ALA GLY PRO ALA SER GLU ILE ARG PHE ARG ARG TYR
SEQRES 8 F 336 ARG PRO LEU GLY GLU ALA ALA GLY LEU LEU PRO THR LEU
SEQRES 9 F 336 ILE TYR TYR HIS GLY GLY GLY PHE VAL ILE GLY ASN ILE
SEQRES 10 F 336 GLU THR HIS ASP SER THR CYS ARG ARG LEU ALA ASN LYS
SEQRES 11 F 336 SER ARG CYS GLN VAL ILE SER ILE ASP TYR ARG LEU ALA
SEQRES 12 F 336 PRO GLU HIS PRO PHE PRO ALA PRO ILE ASP ASP GLY ILE
SEQRES 13 F 336 ALA ALA PHE ARG HIS ILE ARG ASP ASN ALA GLU SER PHE
SEQRES 14 F 336 GLY ALA ASP ALA ALA ARG LEU ALA VAL GLY GLY ASP SER
SEQRES 15 F 336 ALA GLY GLY ALA MET ALA ALA VAL VAL CYS GLN ALA CYS
SEQRES 16 F 336 ARG ASP ALA GLY GLU THR GLY PRO ALA PHE GLN MET LEU
SEQRES 17 F 336 ILE TYR PRO ALA THR ASP SER SER ARG GLU SER ALA SER
SEQRES 18 F 336 ARG VAL ALA PHE ALA GLU GLY TYR PHE LEU SER LYS ALA
SEQRES 19 F 336 LEU MET ASP TRP PHE TRP GLU ALA TYR VAL PRO GLU ASP
SEQRES 20 F 336 THR ASP LEU THR ASP LEU ARG LEU SER PRO LEU LEU ALA
SEQRES 21 F 336 THR ASP PHE THR GLY LEU PRO PRO ALA PHE VAL LEU THR
SEQRES 22 F 336 ALA GLY TYR ASP PRO LEU ARG ASP GLU GLY ARG ALA TYR
SEQRES 23 F 336 ALA ASP ARG LEU ILE GLU ALA GLY ILE LYS THR THR TYR
SEQRES 24 F 336 VAL ASN TYR PRO GLY THR ILE HIS GLY PHE PHE SER LEU
SEQRES 25 F 336 THR ARG PHE LEU SER GLN GLY LEU LYS ALA ASN ASP GLU
SEQRES 26 F 336 ALA ALA ALA VAL MET GLY ALA HIS PHE GLY THR
SEQRES 1 G 336 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 G 336 ARG GLU ASN LEU TYR PHE GLN GLY MET LEU LEU PRO GLU
SEQRES 3 G 336 THR ARG ASN LEU LEU ASP LEU MET ASP ALA ALA THR ARG
SEQRES 4 G 336 GLY GLY ARG PRO ARG LEU GLU THR LEU PRO HIS ALA VAL
SEQRES 5 G 336 GLY ARG LYS ALA VAL ASP LYS MET SER GLU ASP GLY GLU
SEQRES 6 G 336 ALA ASP PRO PRO GLU VAL ALA GLU VAL ALA ASN GLY GLY
SEQRES 7 G 336 PHE ALA GLY PRO ALA SER GLU ILE ARG PHE ARG ARG TYR
SEQRES 8 G 336 ARG PRO LEU GLY GLU ALA ALA GLY LEU LEU PRO THR LEU
SEQRES 9 G 336 ILE TYR TYR HIS GLY GLY GLY PHE VAL ILE GLY ASN ILE
SEQRES 10 G 336 GLU THR HIS ASP SER THR CYS ARG ARG LEU ALA ASN LYS
SEQRES 11 G 336 SER ARG CYS GLN VAL ILE SER ILE ASP TYR ARG LEU ALA
SEQRES 12 G 336 PRO GLU HIS PRO PHE PRO ALA PRO ILE ASP ASP GLY ILE
SEQRES 13 G 336 ALA ALA PHE ARG HIS ILE ARG ASP ASN ALA GLU SER PHE
SEQRES 14 G 336 GLY ALA ASP ALA ALA ARG LEU ALA VAL GLY GLY ASP SER
SEQRES 15 G 336 ALA GLY GLY ALA MET ALA ALA VAL VAL CYS GLN ALA CYS
SEQRES 16 G 336 ARG ASP ALA GLY GLU THR GLY PRO ALA PHE GLN MET LEU
SEQRES 17 G 336 ILE TYR PRO ALA THR ASP SER SER ARG GLU SER ALA SER
SEQRES 18 G 336 ARG VAL ALA PHE ALA GLU GLY TYR PHE LEU SER LYS ALA
SEQRES 19 G 336 LEU MET ASP TRP PHE TRP GLU ALA TYR VAL PRO GLU ASP
SEQRES 20 G 336 THR ASP LEU THR ASP LEU ARG LEU SER PRO LEU LEU ALA
SEQRES 21 G 336 THR ASP PHE THR GLY LEU PRO PRO ALA PHE VAL LEU THR
SEQRES 22 G 336 ALA GLY TYR ASP PRO LEU ARG ASP GLU GLY ARG ALA TYR
SEQRES 23 G 336 ALA ASP ARG LEU ILE GLU ALA GLY ILE LYS THR THR TYR
SEQRES 24 G 336 VAL ASN TYR PRO GLY THR ILE HIS GLY PHE PHE SER LEU
SEQRES 25 G 336 THR ARG PHE LEU SER GLN GLY LEU LYS ALA ASN ASP GLU
SEQRES 26 G 336 ALA ALA ALA VAL MET GLY ALA HIS PHE GLY THR
SEQRES 1 H 336 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 H 336 ARG GLU ASN LEU TYR PHE GLN GLY MET LEU LEU PRO GLU
SEQRES 3 H 336 THR ARG ASN LEU LEU ASP LEU MET ASP ALA ALA THR ARG
SEQRES 4 H 336 GLY GLY ARG PRO ARG LEU GLU THR LEU PRO HIS ALA VAL
SEQRES 5 H 336 GLY ARG LYS ALA VAL ASP LYS MET SER GLU ASP GLY GLU
SEQRES 6 H 336 ALA ASP PRO PRO GLU VAL ALA GLU VAL ALA ASN GLY GLY
SEQRES 7 H 336 PHE ALA GLY PRO ALA SER GLU ILE ARG PHE ARG ARG TYR
SEQRES 8 H 336 ARG PRO LEU GLY GLU ALA ALA GLY LEU LEU PRO THR LEU
SEQRES 9 H 336 ILE TYR TYR HIS GLY GLY GLY PHE VAL ILE GLY ASN ILE
SEQRES 10 H 336 GLU THR HIS ASP SER THR CYS ARG ARG LEU ALA ASN LYS
SEQRES 11 H 336 SER ARG CYS GLN VAL ILE SER ILE ASP TYR ARG LEU ALA
SEQRES 12 H 336 PRO GLU HIS PRO PHE PRO ALA PRO ILE ASP ASP GLY ILE
SEQRES 13 H 336 ALA ALA PHE ARG HIS ILE ARG ASP ASN ALA GLU SER PHE
SEQRES 14 H 336 GLY ALA ASP ALA ALA ARG LEU ALA VAL GLY GLY ASP SER
SEQRES 15 H 336 ALA GLY GLY ALA MET ALA ALA VAL VAL CYS GLN ALA CYS
SEQRES 16 H 336 ARG ASP ALA GLY GLU THR GLY PRO ALA PHE GLN MET LEU
SEQRES 17 H 336 ILE TYR PRO ALA THR ASP SER SER ARG GLU SER ALA SER
SEQRES 18 H 336 ARG VAL ALA PHE ALA GLU GLY TYR PHE LEU SER LYS ALA
SEQRES 19 H 336 LEU MET ASP TRP PHE TRP GLU ALA TYR VAL PRO GLU ASP
SEQRES 20 H 336 THR ASP LEU THR ASP LEU ARG LEU SER PRO LEU LEU ALA
SEQRES 21 H 336 THR ASP PHE THR GLY LEU PRO PRO ALA PHE VAL LEU THR
SEQRES 22 H 336 ALA GLY TYR ASP PRO LEU ARG ASP GLU GLY ARG ALA TYR
SEQRES 23 H 336 ALA ASP ARG LEU ILE GLU ALA GLY ILE LYS THR THR TYR
SEQRES 24 H 336 VAL ASN TYR PRO GLY THR ILE HIS GLY PHE PHE SER LEU
SEQRES 25 H 336 THR ARG PHE LEU SER GLN GLY LEU LYS ALA ASN ASP GLU
SEQRES 26 H 336 ALA ALA ALA VAL MET GLY ALA HIS PHE GLY THR
HET SO4 A 401 5
HET SO4 A 402 5
HET GOL A 403 6
HET CL A 404 1
HET GOL A 405 6
HET PE3 A 406 12
HET BAM A 407 9
HET SO4 B 401 5
HET SO4 B 402 5
HET GOL B 403 6
HET CL B 404 1
HET GOL B 405 6
HET GOL B 406 6
HET GOL B 407 6
HET BAM B 408 9
HET SO4 C 401 5
HET SO4 C 402 5
HET GOL C 403 6
HET GOL C 404 6
HET CL C 405 1
HET BAM C 406 9
HET SO4 D 401 5
HET GOL D 402 6
HET CL D 403 1
HET GOL D 404 6
HET GOL D 405 6
HET GOL D 406 6
HET CL D 407 1
HET PE3 D 408 13
HET BAM D 409 9
HET CL E 401 1
HET GOL E 402 6
HET GOL E 403 6
HET GOL E 404 6
HET GOL E 405 6
HET BAM E 406 9
HET GOL F 401 6
HET GOL F 402 6
HET GOL F 403 6
HET CL F 404 1
HET BAM F 405 9
HET SO4 G 401 5
HET GOL G 402 6
HET GOL G 403 6
HET CL G 404 1
HET GOL G 405 6
HET GOL G 406 6
HET GOL G 407 6
HET GOL G 408 6
HET BAM G 409 9
HET SO4 H 401 5
HET SO4 H 402 5
HET GOL H 403 6
HET GOL H 404 6
HET PE3 H 405 7
HET BAM H 406 9
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETNAM CL CHLORIDE ION
HETNAM PE3 3,6,9,12,15,18,21,24,27,30,33,36,39-
HETNAM 2 PE3 TRIDECAOXAHENTETRACONTANE-1,41-DIOL
HETNAM BAM BENZAMIDINE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN PE3 POLYETHYLENE GLYCOL
FORMUL 9 SO4 10(O4 S 2-)
FORMUL 11 GOL 27(C3 H8 O3)
FORMUL 12 CL 8(CL 1-)
FORMUL 14 PE3 3(C28 H58 O15)
FORMUL 15 BAM 8(C7 H9 N2 1+)
FORMUL 65 HOH *2409(H2 O)
HELIX 1 AA1 LEU A 3 GLY A 20 1 18
HELIX 2 AA2 ARG A 23 LEU A 27 5 5
HELIX 3 AA3 PRO A 28 GLU A 44 1 17
HELIX 4 AA4 ILE A 96 THR A 98 5 3
HELIX 5 AA5 HIS A 99 ARG A 111 1 13
HELIX 6 AA6 PRO A 128 ASN A 144 1 17
HELIX 7 AA7 ALA A 145 PHE A 148 5 4
HELIX 8 AA8 SER A 161 GLY A 178 1 18
HELIX 9 AA9 SER A 198 PHE A 204 1 7
HELIX 10 AB1 SER A 211 VAL A 223 1 13
HELIX 11 AB2 SER A 235 ALA A 239 5 5
HELIX 12 AB3 LEU A 258 ALA A 272 1 15
HELIX 13 AB4 LEU A 295 GLY A 314 1 20
HELIX 14 AB5 LEU B 3 GLY B 20 1 18
HELIX 15 AB6 ARG B 23 LEU B 27 5 5
HELIX 16 AB7 PRO B 28 GLU B 44 1 17
HELIX 17 AB8 ILE B 96 THR B 98 5 3
HELIX 18 AB9 HIS B 99 ARG B 111 1 13
HELIX 19 AC1 PRO B 128 ASN B 144 1 17
HELIX 20 AC2 ALA B 145 PHE B 148 5 4
HELIX 21 AC3 SER B 161 GLY B 178 1 18
HELIX 22 AC4 SER B 198 PHE B 204 1 7
HELIX 23 AC5 SER B 211 VAL B 223 1 13
HELIX 24 AC6 SER B 235 ALA B 239 5 5
HELIX 25 AC7 LEU B 258 ALA B 272 1 15
HELIX 26 AC8 LEU B 295 GLY B 314 1 20
HELIX 27 AC9 LEU C 3 GLY C 20 1 18
HELIX 28 AD1 ARG C 23 LEU C 27 5 5
HELIX 29 AD2 PRO C 28 GLU C 44 1 17
HELIX 30 AD3 ILE C 96 THR C 98 5 3
HELIX 31 AD4 HIS C 99 ARG C 111 1 13
HELIX 32 AD5 PRO C 128 ASN C 144 1 17
HELIX 33 AD6 ALA C 145 PHE C 148 5 4
HELIX 34 AD7 SER C 161 ALA C 177 1 17
HELIX 35 AD8 SER C 198 PHE C 204 1 7
HELIX 36 AD9 SER C 211 VAL C 223 1 13
HELIX 37 AE1 SER C 235 ALA C 239 5 5
HELIX 38 AE2 LEU C 258 ALA C 272 1 15
HELIX 39 AE3 LEU C 295 PHE C 313 1 19
HELIX 40 AE4 LEU D 3 GLY D 20 1 18
HELIX 41 AE5 ARG D 23 LEU D 27 5 5
HELIX 42 AE6 PRO D 28 GLU D 44 1 17
HELIX 43 AE7 ILE D 96 THR D 98 5 3
HELIX 44 AE8 HIS D 99 ARG D 111 1 13
HELIX 45 AE9 PRO D 128 ASN D 144 1 17
HELIX 46 AF1 ALA D 145 PHE D 148 5 4
HELIX 47 AF2 SER D 161 ALA D 177 1 17
HELIX 48 AF3 SER D 198 PHE D 204 1 7
HELIX 49 AF4 SER D 211 VAL D 223 1 13
HELIX 50 AF5 SER D 235 ALA D 239 5 5
HELIX 51 AF6 LEU D 258 ALA D 272 1 15
HELIX 52 AF7 LEU D 295 PHE D 313 1 19
HELIX 53 AF8 LEU E 3 GLY E 19 1 17
HELIX 54 AF9 ARG E 23 LEU E 27 5 5
HELIX 55 AG1 PRO E 28 GLU E 44 1 17
HELIX 56 AG2 ILE E 96 THR E 98 5 3
HELIX 57 AG3 HIS E 99 ARG E 111 1 13
HELIX 58 AG4 PRO E 128 ASN E 144 1 17
HELIX 59 AG5 ALA E 145 PHE E 148 5 4
HELIX 60 AG6 SER E 161 GLY E 178 1 18
HELIX 61 AG7 SER E 198 PHE E 204 1 7
HELIX 62 AG8 SER E 211 VAL E 223 1 13
HELIX 63 AG9 SER E 235 ALA E 239 5 5
HELIX 64 AH1 LEU E 258 ALA E 272 1 15
HELIX 65 AH2 LEU E 295 GLY E 314 1 20
HELIX 66 AH3 LEU F 3 GLY F 20 1 18
HELIX 67 AH4 ARG F 23 LEU F 27 5 5
HELIX 68 AH5 PRO F 28 GLU F 44 1 17
HELIX 69 AH6 ILE F 96 THR F 98 5 3
HELIX 70 AH7 HIS F 99 ARG F 111 1 13
HELIX 71 AH8 PRO F 128 ASN F 144 1 17
HELIX 72 AH9 ALA F 145 PHE F 148 5 4
HELIX 73 AI1 SER F 161 GLY F 178 1 18
HELIX 74 AI2 SER F 198 PHE F 204 1 7
HELIX 75 AI3 SER F 211 VAL F 223 1 13
HELIX 76 AI4 SER F 235 ALA F 239 5 5
HELIX 77 AI5 LEU F 258 ALA F 272 1 15
HELIX 78 AI6 LEU F 295 GLY F 314 1 20
HELIX 79 AI7 LEU G 3 GLY G 20 1 18
HELIX 80 AI8 ARG G 23 LEU G 27 5 5
HELIX 81 AI9 PRO G 28 GLU G 44 1 17
HELIX 82 AJ1 ILE G 96 THR G 98 5 3
HELIX 83 AJ2 HIS G 99 ARG G 111 1 13
HELIX 84 AJ3 PRO G 128 ASN G 144 1 17
HELIX 85 AJ4 ALA G 145 PHE G 148 5 4
HELIX 86 AJ5 SER G 161 ALA G 177 1 17
HELIX 87 AJ6 SER G 198 PHE G 204 1 7
HELIX 88 AJ7 SER G 211 VAL G 223 1 13
HELIX 89 AJ8 SER G 235 ALA G 239 5 5
HELIX 90 AJ9 LEU G 258 ALA G 272 1 15
HELIX 91 AK1 LEU G 295 PHE G 313 1 19
HELIX 92 AK2 LEU H 3 GLY H 20 1 18
HELIX 93 AK3 ARG H 23 LEU H 27 5 5
HELIX 94 AK4 PRO H 28 GLU H 44 1 17
HELIX 95 AK5 ILE H 96 THR H 98 5 3
HELIX 96 AK6 HIS H 99 ARG H 111 1 13
HELIX 97 AK7 PRO H 128 ASN H 144 1 17
HELIX 98 AK8 ALA H 145 PHE H 148 5 4
HELIX 99 AK9 SER H 161 GLY H 178 1 18
HELIX 100 AL1 SER H 198 PHE H 204 1 7
HELIX 101 AL2 SER H 211 VAL H 223 1 13
HELIX 102 AL3 SER H 235 ALA H 239 5 5
HELIX 103 AL4 LEU H 258 ALA H 272 1 15
HELIX 104 AL5 LEU H 295 GLY H 314 1 20
SHEET 1 AA116 GLU A 52 ALA A 59 0
SHEET 2 AA116 GLU A 64 ARG A 71 -1 O ILE A 65 N PHE A 58
SHEET 3 AA116 GLN A 113 ASP A 118 -1 O VAL A 114 N TYR A 70
SHEET 4 AA116 LEU A 80 TYR A 86 1 N LEU A 83 O GLN A 113
SHEET 5 AA116 ALA A 150 ASP A 160 1 O ALA A 156 N THR A 82
SHEET 6 AA116 PHE A 184 ILE A 188 1 O ILE A 188 N GLY A 159
SHEET 7 AA116 ALA A 248 ALA A 253 1 O PHE A 249 N LEU A 187
SHEET 8 AA116 THR A 276 TYR A 281 1 O THR A 277 N VAL A 250
SHEET 9 AA116 THR H 276 TYR H 281 -1 O TYR H 278 N TYR A 278
SHEET 10 AA116 ALA H 248 ALA H 253 1 N VAL H 250 O THR H 277
SHEET 11 AA116 PHE H 184 ILE H 188 1 N LEU H 187 O PHE H 249
SHEET 12 AA116 ALA H 150 ASP H 160 1 N GLY H 159 O ILE H 188
SHEET 13 AA116 LEU H 80 TYR H 86 1 N THR H 82 O ALA H 156
SHEET 14 AA116 GLN H 113 ASP H 118 1 O ILE H 115 N TYR H 85
SHEET 15 AA116 GLU H 64 ARG H 71 -1 N TYR H 70 O VAL H 114
SHEET 16 AA116 GLU H 52 ALA H 59 -1 N GLY H 56 O PHE H 67
SHEET 1 AA232 GLU B 52 ALA B 59 0
SHEET 2 AA232 GLU B 64 ARG B 71 -1 O ILE B 65 N PHE B 58
SHEET 3 AA232 GLN B 113 ASP B 118 -1 O ASP B 118 N ARG B 66
SHEET 4 AA232 LEU B 80 TYR B 86 1 N LEU B 83 O GLN B 113
SHEET 5 AA232 ALA B 150 ASP B 160 1 O ALA B 156 N THR B 82
SHEET 6 AA232 PHE B 184 ILE B 188 1 O MET B 186 N VAL B 157
SHEET 7 AA232 ALA B 248 ALA B 253 1 O PHE B 249 N LEU B 187
SHEET 8 AA232 THR B 276 TYR B 281 1 O THR B 277 N VAL B 250
SHEET 9 AA232 THR E 276 TYR E 281 -1 O TYR E 278 N TYR B 278
SHEET 10 AA232 ALA E 248 ALA E 253 1 N VAL E 250 O THR E 277
SHEET 11 AA232 PHE E 184 ILE E 188 1 N LEU E 187 O PHE E 249
SHEET 12 AA232 ALA E 150 ASP E 160 1 N GLY E 159 O ILE E 188
SHEET 13 AA232 LEU E 80 TYR E 86 1 N THR E 82 O ALA E 156
SHEET 14 AA232 GLN E 113 ASP E 118 1 O GLN E 113 N LEU E 83
SHEET 15 AA232 GLU E 64 ARG E 71 -1 N TYR E 70 O VAL E 114
SHEET 16 AA232 GLU E 52 ALA E 59 -1 N PHE E 58 O ILE E 65
SHEET 17 AA232 GLU G 52 ALA G 59 -1 O ASN G 55 N VAL E 53
SHEET 18 AA232 GLU G 64 ARG G 71 -1 O ILE G 65 N PHE G 58
SHEET 19 AA232 GLN G 113 ASP G 118 -1 O VAL G 114 N TYR G 70
SHEET 20 AA232 LEU G 80 TYR G 86 1 N LEU G 83 O GLN G 113
SHEET 21 AA232 ALA G 150 ASP G 160 1 O ALA G 156 N ILE G 84
SHEET 22 AA232 PHE G 184 ILE G 188 1 O ILE G 188 N GLY G 159
SHEET 23 AA232 ALA G 248 ALA G 253 1 O PHE G 249 N LEU G 187
SHEET 24 AA232 THR G 276 TYR G 281 1 O THR G 277 N VAL G 250
SHEET 25 AA232 THR D 276 TYR D 281 -1 N TYR D 278 O TYR G 278
SHEET 26 AA232 ALA D 248 ALA D 253 1 N VAL D 250 O THR D 277
SHEET 27 AA232 PHE D 184 ILE D 188 1 N LEU D 187 O PHE D 249
SHEET 28 AA232 ALA D 150 ASP D 160 1 N VAL D 157 O MET D 186
SHEET 29 AA232 LEU D 80 TYR D 86 1 N THR D 82 O ALA D 156
SHEET 30 AA232 GLN D 113 ASP D 118 1 O GLN D 113 N LEU D 83
SHEET 31 AA232 GLU D 64 ARG D 71 -1 N TYR D 70 O VAL D 114
SHEET 32 AA232 GLU D 52 ALA D 59 -1 N PHE D 58 O ILE D 65
SHEET 1 AA316 GLU C 52 ALA C 59 0
SHEET 2 AA316 GLU C 64 ARG C 71 -1 O ILE C 65 N PHE C 58
SHEET 3 AA316 GLN C 113 ASP C 118 -1 O ASP C 118 N ARG C 66
SHEET 4 AA316 LEU C 80 TYR C 86 1 N LEU C 83 O GLN C 113
SHEET 5 AA316 ALA C 150 ASP C 160 1 O ALA C 156 N THR C 82
SHEET 6 AA316 PHE C 184 ILE C 188 1 O ILE C 188 N GLY C 159
SHEET 7 AA316 ALA C 248 ALA C 253 1 O PHE C 249 N LEU C 187
SHEET 8 AA316 THR C 276 TYR C 281 1 O THR C 277 N VAL C 250
SHEET 9 AA316 THR F 276 TYR F 281 -1 O TYR F 278 N TYR C 278
SHEET 10 AA316 ALA F 248 ALA F 253 1 N VAL F 250 O THR F 277
SHEET 11 AA316 PHE F 184 ILE F 188 1 N LEU F 187 O PHE F 249
SHEET 12 AA316 ALA F 150 ASP F 160 1 N GLY F 159 O ILE F 188
SHEET 13 AA316 LEU F 80 TYR F 86 1 N ILE F 84 O ALA F 156
SHEET 14 AA316 GLN F 113 ASP F 118 1 O GLN F 113 N LEU F 83
SHEET 15 AA316 GLU F 64 ARG F 71 -1 N TYR F 70 O VAL F 114
SHEET 16 AA316 GLU F 52 ALA F 59 -1 N PHE F 58 O ILE F 65
CISPEP 1 ALA A 122 PRO A 123 0 1.07
CISPEP 2 PHE A 127 PRO A 128 0 5.01
CISPEP 3 ALA B 122 PRO B 123 0 3.15
CISPEP 4 PHE B 127 PRO B 128 0 1.87
CISPEP 5 ALA C 122 PRO C 123 0 2.37
CISPEP 6 PHE C 127 PRO C 128 0 1.90
CISPEP 7 ALA D 122 PRO D 123 0 2.65
CISPEP 8 PHE D 127 PRO D 128 0 3.41
CISPEP 9 ALA E 122 PRO E 123 0 3.02
CISPEP 10 PHE E 127 PRO E 128 0 3.50
CISPEP 11 ALA F 122 PRO F 123 0 2.29
CISPEP 12 PHE F 127 PRO F 128 0 2.67
CISPEP 13 ALA G 122 PRO G 123 0 1.88
CISPEP 14 PHE G 127 PRO G 128 0 2.62
CISPEP 15 ALA H 122 PRO H 123 0 2.71
CISPEP 16 PHE H 127 PRO H 128 0 3.72
SITE 1 AC1 5 LYS A 275 HIS A 312 HOH A 552 GLN H 297
SITE 2 AC1 5 LYS H 300
SITE 1 AC2 7 ARG A 263 ASP A 267 ILE A 270 TYR A 278
SITE 2 AC2 7 ARG H 263 ASP H 267 ILE H 270
SITE 1 AC3 5 GLN A -1 LEU A 10 ASP A 11 ASP A 14
SITE 2 AC3 5 GLY A 207
SITE 1 AC4 1 HIS A 29
SITE 1 AC5 8 GLU A 52 ARG A 69 ARG A 71 GLY A 78
SITE 2 AC5 8 HOH A 501 HOH A 533 ARG C 69 SER C 147
SITE 1 AC6 4 ARG A 105 LEU A 299 HOH A 562 GLY B 19
SITE 1 AC7 7 GLY A 89 GLY A 90 SER A 161 ALA A 162
SITE 2 AC7 7 LEU A 210 MET A 215 HIS A 286
SITE 1 AC8 5 GLN B 297 LYS B 300 HOH B 539 LYS E 275
SITE 2 AC8 5 HIS E 312
SITE 1 AC9 5 LYS B 275 HIS B 312 HOH B 529 GLN E 297
SITE 2 AC9 5 LYS E 300
SITE 1 AD1 4 GLU B 25 LEU B 27 CL B 404 HOH B 614
SITE 1 AD2 2 HIS B 29 GOL B 403
SITE 1 AD3 5 GLN B -1 ASP B 11 GLY B 207 HOH B 516
SITE 2 AD3 5 HOH B 659
SITE 1 AD4 7 ARG B 69 ARG B 71 GLY B 78 SER B 147
SITE 2 AD4 7 ARG D 69 GLU D 146 SER D 147
SITE 1 AD5 3 ARG B 21 PRO B 22 ALA B 35
SITE 1 AD6 6 GLY B 88 GLY B 89 GLY B 90 SER B 161
SITE 2 AD6 6 ALA B 162 HIS B 286
SITE 1 AD7 5 LYS C 275 HIS C 312 HOH C 505 GLN F 297
SITE 2 AD7 5 LYS F 300
SITE 1 AD8 6 GLN C 297 LYS C 300 HOH C 508 HOH C 571
SITE 2 AD8 6 LYS F 275 HIS F 312
SITE 1 AD9 7 ASN A 55 ARG A 66 GLU C 49 VAL C 50
SITE 2 AD9 7 VAL C 53 ARG C 104 HOH C 516
SITE 1 AE1 6 ALA C 62 ARG C 120 ALA C 129 ASP C 132
SITE 2 AE1 6 HOH C 503 HOH C 559
SITE 1 AE2 7 GLY C 88 GLY C 89 GLY C 90 SER C 161
SITE 2 AE2 7 ALA C 162 LEU C 210 HIS C 286
SITE 1 AE3 6 LYS D 275 HIS D 312 HOH D 522 HOH D 613
SITE 2 AE3 6 GLN G 297 LYS G 300
SITE 1 AE4 3 ARG D 21 PRO D 22 MET D 39
SITE 1 AE5 3 HIS D 29 GOL D 404 HOH D 555
SITE 1 AE6 9 GLU D 25 LEU D 27 PRO D 28 HIS D 29
SITE 2 AE6 9 TRP D 217 CL D 403 HOH D 541 HOH D 555
SITE 3 AE6 9 HOH D 736
SITE 1 AE7 5 GLN D -1 ARG D 7 LEU D 10 ASP D 11
SITE 2 AE7 5 GLY D 207
SITE 1 AE8 5 ALA D 62 ARG D 120 ALA D 129 ASP D 132
SITE 2 AE8 5 HOH D 595
SITE 1 AE9 4 ASP D 231 LEU D 232 HOH D 750 HOH D 785
SITE 1 AF1 9 ALA C 45 THR C 292 ARG C 293 HOH C 565
SITE 2 AF1 9 LEU D 12 ARG D 21 MET D 39 PHE D 209
SITE 3 AF1 9 HOH D 647
SITE 1 AF2 7 GLY D 89 GLY D 90 SER D 161 ALA D 162
SITE 2 AF2 7 LEU D 210 MET D 215 HIS D 286
SITE 1 AF3 1 HIS E 29
SITE 1 AF4 8 GLU E 49 VAL E 50 VAL E 53 ARG E 104
SITE 2 AF4 8 HOH E 600 ASN G 55 GLY G 56 ARG G 66
SITE 1 AF5 2 ARG E 105 LYS E 109
SITE 1 AF6 7 ASN E 55 GLY E 56 ARG E 66 PHE E 67
SITE 2 AF6 7 ARG E 68 ILE E 96 GLU E 97
SITE 1 AF7 5 GLN E -1 ARG E 7 ASP E 11 GLY E 207
SITE 2 AF7 5 HOH E 647
SITE 1 AF8 5 GLY E 89 GLY E 90 SER E 161 ALA E 162
SITE 2 AF8 5 HIS E 286
SITE 1 AF9 7 ARG C 263 ASP C 267 ILE C 270 ARG F 263
SITE 2 AF9 7 ASP F 267 ILE F 270 TYR F 278
SITE 1 AG1 4 GLU F 49 VAL F 50 VAL F 53 ARG F 104
SITE 1 AG2 3 GLY F 207 HOH F 506 HOH F 636
SITE 1 AG3 2 ARG F 105 HOH F 673
SITE 1 AG4 8 GLY F 88 GLY F 89 GLY F 90 SER F 161
SITE 2 AG4 8 ALA F 162 MET F 215 HIS F 286 HOH F 790
SITE 1 AG5 6 GLN D 297 LYS D 300 LYS G 275 HIS G 312
SITE 2 AG5 6 HOH G 557 HOH G 583
SITE 1 AG6 6 ASN E 55 ARG E 66 GLU G 49 VAL G 50
SITE 2 AG6 6 VAL G 53 ARG G 104
SITE 1 AG7 2 ARG G 105 LYS G 109
SITE 1 AG8 1 HIS G 29
SITE 1 AG9 5 GLN G -1 LEU G 2 ASP G 11 GLY G 207
SITE 2 AG9 5 HOH G 511
SITE 1 AH1 5 LEU E 79 GLU E 146 LEU G 79 GLU G 146
SITE 2 AH1 5 HOH G 594
SITE 1 AH2 5 ILE D 270 ARG G 259 ASP G 260 ARG G 263
SITE 2 AH2 5 HOH G 647
SITE 1 AH3 6 ARG D 263 ASP D 267 ARG G 263 ASP G 267
SITE 2 AH3 6 ILE G 270 TYR G 278
SITE 1 AH4 6 GLY G 88 GLY G 89 GLY G 90 SER G 161
SITE 2 AH4 6 ALA G 162 HIS G 286
SITE 1 AH5 5 GLN A 297 LYS A 300 LYS H 275 HIS H 312
SITE 2 AH5 5 HOH H 548
SITE 1 AH6 2 ARG H 105 GOL H 403
SITE 1 AH7 7 GLY A 314 HOH A 528 SER H 296 LEU H 299
SITE 2 AH7 7 SO4 H 402 HOH H 583 HOH H 632
SITE 1 AH8 5 ARG H 175 LEU H 232 ALA H 239 THR H 240
SITE 2 AH8 5 ASP H 241
SITE 1 AH9 5 ILE A 270 ARG H 259 ASP H 260 ARG H 263
SITE 2 AH9 5 ASN H 280
SITE 1 AI1 6 GLY H 89 GLY H 90 SER H 161 ALA H 162
SITE 2 AI1 6 MET H 215 HIS H 286
CRYST1 90.275 90.098 110.760 68.02 79.60 67.57 P 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 0.011077 -0.004573 -0.000528 0.00000
SCALE2 0.000000 0.012008 -0.004282 0.00000
SCALE3 0.000000 0.000000 0.009746 0.00000
TER 2409 THR A 315
TER 4818 THR B 315
TER 7232 THR C 315
TER 9636 THR D 315
TER 12046 THR E 315
TER 14450 THR F 315
TER 16866 THR G 315
TER 19270 THR H 315
MASTER 1113 0 56 104 64 0 96 621957 8 316 208
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