HEADER PROTEIN TRANSPORT 30-APR-17 5VNM
TITLE CRYSTAL STRUCTURE OF SEC23A/SEC24A/SEC22 COMPLEXED WITH 4-
TITLE 2 PHENYLBUTYRIC ACID (15MM SOAKING)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN TRANSPORT PROTEIN SEC23A;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SEC23-RELATED PROTEIN A;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PROTEIN TRANSPORT PROTEIN SEC24A;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: UNP RESIDUES 346-1093;
COMPND 10 SYNONYM: SEC24-RELATED PROTEIN A;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: VESICLE-TRAFFICKING PROTEIN SEC22B;
COMPND 14 CHAIN: C;
COMPND 15 FRAGMENT: UNP RESIDUES 1-157;
COMPND 16 SYNONYM: ER-GOLGI SNARE OF 24 KDA,ERS24,SEC22 VESICLE-TRAFFICKING
COMPND 17 PROTEIN HOMOLOG B,SEC22 VESICLE-TRAFFICKING PROTEIN-LIKE 1,MSEC22B;
COMPND 18 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: SEC23A;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HI-5;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 GENE: SEC24A;
SOURCE 14 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 16 EXPRESSION_SYSTEM_CELL_LINE: HI-5;
SOURCE 17 MOL_ID: 3;
SOURCE 18 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 19 ORGANISM_COMMON: MOUSE;
SOURCE 20 ORGANISM_TAXID: 10090;
SOURCE 21 GENE: SEC22B, SEC22L1;
SOURCE 22 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 23 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS COPII, TRAFFICKING, P24, ER RETENTION, PROTEIN TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR W.MA,J.GOLDBERG
REVDAT 2 04-OCT-23 5VNM 1 REMARK
REVDAT 1 05-JUL-17 5VNM 0
JRNL AUTH W.MA,E.GOLDBERG,J.GOLDBERG
JRNL TITL ER RETENTION IS IMPOSED BY COPII PROTEIN SORTING AND
JRNL TITL 2 ATTENUATED BY 4-PHENYLBUTYRATE.
JRNL REF ELIFE V. 6 2017
JRNL REFN ESSN 2050-084X
JRNL PMID 28594326
JRNL DOI 10.7554/ELIFE.26624
REMARK 2
REMARK 2 RESOLUTION. 2.77 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.11.1_2575
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) : 2.77
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 130.61
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.2
REMARK 3 NUMBER OF REFLECTIONS : 43047
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.269
REMARK 3 R VALUE (WORKING SET) : 0.268
REMARK 3 FREE R VALUE : 0.297
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.570
REMARK 3 FREE R VALUE TEST SET COUNT : 1966
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
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) : 0.610
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 35.470
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 : 0.002 12709
REMARK 3 ANGLE : 0.553 17215
REMARK 3 CHIRALITY : 0.041 1946
REMARK 3 PLANARITY : 0.004 2225
REMARK 3 DIHEDRAL : 12.213 7740
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 20
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 38 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.6444-115.3005 -4.9739
REMARK 3 T TENSOR
REMARK 3 T11: 1.3188 T22: 0.9945
REMARK 3 T33: 0.6007 T12: 0.0358
REMARK 3 T13: 0.1421 T23: -0.2410
REMARK 3 L TENSOR
REMARK 3 L11: 3.0359 L22: 4.4134
REMARK 3 L33: 2.0230 L12: -0.0862
REMARK 3 L13: -1.4785 L23: -0.9864
REMARK 3 S TENSOR
REMARK 3 S11: -0.1517 S12: 0.8206 S13: -0.1679
REMARK 3 S21: -0.3516 S22: 0.0068 S23: -0.0576
REMARK 3 S31: 0.9850 S32: -0.8251 S33: 0.1627
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 39 THROUGH 107 )
REMARK 3 ORIGIN FOR THE GROUP (A): 40.4578 -94.3156 -9.2044
REMARK 3 T TENSOR
REMARK 3 T11: 1.4927 T22: 0.8529
REMARK 3 T33: 0.9648 T12: 0.1474
REMARK 3 T13: 0.2611 T23: -0.0252
REMARK 3 L TENSOR
REMARK 3 L11: 3.7940 L22: 2.7223
REMARK 3 L33: 1.7608 L12: 1.7908
REMARK 3 L13: -1.7107 L23: -2.1835
REMARK 3 S TENSOR
REMARK 3 S11: -0.4997 S12: 0.3832 S13: 0.4972
REMARK 3 S21: -0.9723 S22: 0.2091 S23: -0.5096
REMARK 3 S31: 0.3535 S32: 0.0583 S33: 0.2990
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 108 THROUGH 232 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.4684 -82.8126 20.7433
REMARK 3 T TENSOR
REMARK 3 T11: 0.4981 T22: 0.5295
REMARK 3 T33: 0.5863 T12: 0.1831
REMARK 3 T13: -0.0126 T23: -0.0229
REMARK 3 L TENSOR
REMARK 3 L11: 3.0674 L22: 3.2614
REMARK 3 L33: 2.4997 L12: -0.6249
REMARK 3 L13: -0.6593 L23: 1.0607
REMARK 3 S TENSOR
REMARK 3 S11: 0.2014 S12: 0.2535 S13: 0.4379
REMARK 3 S21: -0.4680 S22: -0.2423 S23: 0.0314
REMARK 3 S31: -0.3537 S32: -0.1849 S33: 0.0603
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 233 THROUGH 420 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.7515 -94.1116 19.6412
REMARK 3 T TENSOR
REMARK 3 T11: 0.4553 T22: 0.5958
REMARK 3 T33: 0.5493 T12: 0.2283
REMARK 3 T13: -0.0637 T23: -0.0759
REMARK 3 L TENSOR
REMARK 3 L11: 1.6590 L22: 3.7975
REMARK 3 L33: 3.3920 L12: 0.0168
REMARK 3 L13: -0.9492 L23: 0.5163
REMARK 3 S TENSOR
REMARK 3 S11: -0.2017 S12: 0.2840 S13: -0.1379
REMARK 3 S21: -0.3994 S22: -0.0267 S23: 0.2634
REMARK 3 S31: 0.4227 S32: -0.3524 S33: 0.1487
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 421 THROUGH 456 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.4817 -98.4266 -1.6732
REMARK 3 T TENSOR
REMARK 3 T11: 1.3123 T22: 1.0603
REMARK 3 T33: 0.8739 T12: 0.3241
REMARK 3 T13: -0.0150 T23: -0.0226
REMARK 3 L TENSOR
REMARK 3 L11: 3.4265 L22: 3.8247
REMARK 3 L33: 3.8365 L12: 0.7992
REMARK 3 L13: -1.9645 L23: -0.5674
REMARK 3 S TENSOR
REMARK 3 S11: -0.2674 S12: 0.7449 S13: 0.5302
REMARK 3 S21: -1.0965 S22: -0.5469 S23: 0.6707
REMARK 3 S31: 0.0525 S32: -1.3512 S33: 0.2248
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 457 THROUGH 518 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.1330-106.0659 -4.8750
REMARK 3 T TENSOR
REMARK 3 T11: 1.2035 T22: 1.0582
REMARK 3 T33: 0.5693 T12: 0.1906
REMARK 3 T13: 0.1508 T23: -0.0829
REMARK 3 L TENSOR
REMARK 3 L11: 1.7303 L22: 1.1712
REMARK 3 L33: 2.2219 L12: 0.2268
REMARK 3 L13: 0.4963 L23: -1.4211
REMARK 3 S TENSOR
REMARK 3 S11: -0.0581 S12: 0.6911 S13: -0.3152
REMARK 3 S21: -1.5569 S22: -0.0420 S23: -0.0741
REMARK 3 S31: 0.2593 S32: 0.1078 S33: 0.0209
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 519 THROUGH 646 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.6545-121.7678 10.2181
REMARK 3 T TENSOR
REMARK 3 T11: 1.0195 T22: 0.5835
REMARK 3 T33: 0.7019 T12: 0.0161
REMARK 3 T13: 0.0330 T23: -0.1581
REMARK 3 L TENSOR
REMARK 3 L11: 2.3018 L22: 2.5916
REMARK 3 L33: 3.6261 L12: 0.6147
REMARK 3 L13: -1.2073 L23: 0.8557
REMARK 3 S TENSOR
REMARK 3 S11: 0.0075 S12: 0.3366 S13: -0.4407
REMARK 3 S21: -0.4347 S22: -0.2107 S23: 0.3499
REMARK 3 S31: 0.5758 S32: -0.2060 S33: 0.2048
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 647 THROUGH 764 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.2967-122.7003 25.3721
REMARK 3 T TENSOR
REMARK 3 T11: 0.8161 T22: 0.5888
REMARK 3 T33: 0.8306 T12: 0.0067
REMARK 3 T13: 0.1842 T23: -0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 3.0922 L22: 4.4287
REMARK 3 L33: 4.6578 L12: -1.3101
REMARK 3 L13: 0.0307 L23: -0.0663
REMARK 3 S TENSOR
REMARK 3 S11: 0.1263 S12: -0.6448 S13: -0.0777
REMARK 3 S21: 0.4268 S22: -0.2440 S23: -0.0544
REMARK 3 S31: 0.3278 S32: -0.5395 S33: 0.2107
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 346 THROUGH 431 )
REMARK 3 ORIGIN FOR THE GROUP (A): -31.0281 -37.6340 51.8721
REMARK 3 T TENSOR
REMARK 3 T11: 0.7779 T22: 0.6207
REMARK 3 T33: 0.6692 T12: 0.2560
REMARK 3 T13: 0.0783 T23: 0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 3.5555 L22: 0.8897
REMARK 3 L33: 1.8894 L12: -0.2660
REMARK 3 L13: -0.2723 L23: 0.3880
REMARK 3 S TENSOR
REMARK 3 S11: -0.0541 S12: -0.5758 S13: -0.0367
REMARK 3 S21: 0.9294 S22: 0.1143 S23: 0.6453
REMARK 3 S31: -0.6564 S32: 0.3014 S33: -0.0902
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 432 THROUGH 707 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.3711 -59.8532 40.5538
REMARK 3 T TENSOR
REMARK 3 T11: 0.6234 T22: 0.4104
REMARK 3 T33: 0.5604 T12: 0.0942
REMARK 3 T13: 0.0098 T23: 0.0480
REMARK 3 L TENSOR
REMARK 3 L11: 3.6581 L22: 2.0261
REMARK 3 L33: 2.3568 L12: -0.5006
REMARK 3 L13: -0.6760 L23: -0.0460
REMARK 3 S TENSOR
REMARK 3 S11: 0.0507 S12: 0.0060 S13: -0.1663
REMARK 3 S21: -0.0092 S22: -0.0088 S23: 0.0120
REMARK 3 S31: 0.2336 S32: -0.0227 S33: -0.0307
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 708 THROUGH 780 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.3788 -51.0776 41.2761
REMARK 3 T TENSOR
REMARK 3 T11: 0.5085 T22: 0.4432
REMARK 3 T33: 0.5076 T12: 0.1516
REMARK 3 T13: -0.0696 T23: 0.0853
REMARK 3 L TENSOR
REMARK 3 L11: 1.4098 L22: 1.7190
REMARK 3 L33: 1.9232 L12: -1.0539
REMARK 3 L13: -1.5927 L23: 0.7304
REMARK 3 S TENSOR
REMARK 3 S11: -0.1462 S12: 0.3090 S13: -0.0269
REMARK 3 S21: 0.1179 S22: -0.0008 S23: -0.1307
REMARK 3 S31: 0.0572 S32: -0.0499 S33: 0.0803
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 781 THROUGH 839 )
REMARK 3 ORIGIN FOR THE GROUP (A): -33.3565 -46.9964 50.0991
REMARK 3 T TENSOR
REMARK 3 T11: 0.3710 T22: 0.6973
REMARK 3 T33: 0.6583 T12: 0.3176
REMARK 3 T13: 0.0320 T23: 0.1829
REMARK 3 L TENSOR
REMARK 3 L11: 2.8639 L22: 2.4040
REMARK 3 L33: 1.4601 L12: -1.5579
REMARK 3 L13: 0.3011 L23: -0.0395
REMARK 3 S TENSOR
REMARK 3 S11: -0.1277 S12: -0.2932 S13: -0.4943
REMARK 3 S21: 0.8407 S22: -0.1093 S23: 0.8417
REMARK 3 S31: -0.0353 S32: -0.0654 S33: -0.0050
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 840 THROUGH 1016 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.4198 -28.2423 40.8283
REMARK 3 T TENSOR
REMARK 3 T11: 0.6829 T22: 0.4816
REMARK 3 T33: 0.5633 T12: 0.0802
REMARK 3 T13: 0.0003 T23: 0.1406
REMARK 3 L TENSOR
REMARK 3 L11: 3.1740 L22: 1.1005
REMARK 3 L33: 1.5250 L12: 0.2611
REMARK 3 L13: 0.1328 L23: 0.3530
REMARK 3 S TENSOR
REMARK 3 S11: -0.0741 S12: 0.2142 S13: 0.4395
REMARK 3 S21: -0.2817 S22: -0.0615 S23: 0.0197
REMARK 3 S31: -0.4666 S32: 0.1115 S33: 0.1668
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1017 THROUGH 1093 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.3211 -26.2635 41.3527
REMARK 3 T TENSOR
REMARK 3 T11: 0.7466 T22: 0.7445
REMARK 3 T33: 0.6420 T12: -0.0271
REMARK 3 T13: 0.0590 T23: 0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 4.8834 L22: 1.6818
REMARK 3 L33: 1.6515 L12: 0.8745
REMARK 3 L13: 1.4956 L23: -0.8643
REMARK 3 S TENSOR
REMARK 3 S11: 0.2301 S12: 0.7311 S13: 0.4395
REMARK 3 S21: -0.6015 S22: -0.3832 S23: -0.2809
REMARK 3 S31: -0.1454 S32: 0.2964 S33: 0.0861
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 29 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.4896 -81.0521 52.4093
REMARK 3 T TENSOR
REMARK 3 T11: 0.9572 T22: 0.7630
REMARK 3 T33: 0.8290 T12: -0.0522
REMARK 3 T13: 0.2160 T23: 0.1745
REMARK 3 L TENSOR
REMARK 3 L11: 2.2120 L22: 3.0051
REMARK 3 L33: 3.2897 L12: -0.6479
REMARK 3 L13: 1.1286 L23: 0.8793
REMARK 3 S TENSOR
REMARK 3 S11: 0.2031 S12: 0.5891 S13: -0.0401
REMARK 3 S21: -0.5799 S22: -0.1263 S23: 0.2003
REMARK 3 S31: -0.7780 S32: 0.3503 S33: -0.0798
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 30 THROUGH 50 )
REMARK 3 ORIGIN FOR THE GROUP (A): -27.7008 -85.7459 55.0860
REMARK 3 T TENSOR
REMARK 3 T11: 1.0748 T22: 0.8633
REMARK 3 T33: 0.9128 T12: 0.1575
REMARK 3 T13: 0.2695 T23: 0.0768
REMARK 3 L TENSOR
REMARK 3 L11: 3.6014 L22: 7.9596
REMARK 3 L33: 2.0424 L12: 1.9054
REMARK 3 L13: -0.4051 L23: -1.8449
REMARK 3 S TENSOR
REMARK 3 S11: -0.1647 S12: 0.5528 S13: 0.3832
REMARK 3 S21: 0.2915 S22: -0.6193 S23: 0.1350
REMARK 3 S31: 0.0144 S32: -1.0920 S33: 0.7796
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 51 THROUGH 80 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.6388 -91.9369 52.9864
REMARK 3 T TENSOR
REMARK 3 T11: 1.4821 T22: 0.8226
REMARK 3 T33: 1.2430 T12: 0.0228
REMARK 3 T13: 0.4574 T23: -0.0392
REMARK 3 L TENSOR
REMARK 3 L11: 6.8241 L22: 6.5394
REMARK 3 L33: 7.2188 L12: -0.7077
REMARK 3 L13: -1.0719 L23: 2.0744
REMARK 3 S TENSOR
REMARK 3 S11: -0.8721 S12: 0.9008 S13: -1.7877
REMARK 3 S21: -0.4735 S22: -0.5814 S23: -0.6457
REMARK 3 S31: 1.9906 S32: -0.4187 S33: 1.1422
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 81 THROUGH 112 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.0914 -83.5092 61.8766
REMARK 3 T TENSOR
REMARK 3 T11: 1.1196 T22: 0.8554
REMARK 3 T33: 1.0677 T12: 0.1508
REMARK 3 T13: 0.3259 T23: 0.2706
REMARK 3 L TENSOR
REMARK 3 L11: 3.6815 L22: 6.4136
REMARK 3 L33: 8.2514 L12: 1.5854
REMARK 3 L13: -0.3924 L23: 0.2059
REMARK 3 S TENSOR
REMARK 3 S11: 0.2376 S12: 0.0013 S13: -0.1261
REMARK 3 S21: 0.7930 S22: 0.1490 S23: -1.0800
REMARK 3 S31: -0.2101 S32: 0.9287 S33: -0.1345
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 113 THROUGH 149 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.9676 -86.2363 51.2446
REMARK 3 T TENSOR
REMARK 3 T11: 0.8484 T22: 1.0033
REMARK 3 T33: 1.1050 T12: 0.0437
REMARK 3 T13: 0.2434 T23: 0.0964
REMARK 3 L TENSOR
REMARK 3 L11: 4.4957 L22: 3.0980
REMARK 3 L33: 8.1385 L12: -3.3744
REMARK 3 L13: -2.4537 L23: -0.1213
REMARK 3 S TENSOR
REMARK 3 S11: -0.5944 S12: 0.2860 S13: -0.6340
REMARK 3 S21: 0.1266 S22: 0.8141 S23: -0.0019
REMARK 3 S31: 0.6919 S32: 0.4686 S33: -0.2737
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 150 THROUGH 157 )
REMARK 3 ORIGIN FOR THE GROUP (A): -31.2040 -94.3787 50.9163
REMARK 3 T TENSOR
REMARK 3 T11: 1.9083 T22: 1.3057
REMARK 3 T33: 1.2989 T12: -0.1915
REMARK 3 T13: 0.2646 T23: 0.0135
REMARK 3 L TENSOR
REMARK 3 L11: 4.1267 L22: 6.0282
REMARK 3 L33: 4.7730 L12: -1.4070
REMARK 3 L13: -1.2171 L23: 1.4924
REMARK 3 S TENSOR
REMARK 3 S11: 0.0459 S12: 0.3962 S13: -1.0671
REMARK 3 S21: -0.0879 S22: 0.9007 S23: 0.4315
REMARK 3 S31: 0.6386 S32: -0.6061 S33: -0.7962
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 5VNM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAY-17.
REMARK 100 THE DEPOSITION ID IS D_1000227723.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUL-15
REMARK 200 TEMPERATURE (KELVIN) : 77
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.987
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43047
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.765
REMARK 200 RESOLUTION RANGE LOW (A) : 130.608
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 2NUT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM HEPES PH 7.8, 0.5M NAAC AND 12%
REMARK 280 PEG4K, VAPOR DIFFUSION, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 74.59150
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.40000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 74.59150
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 48.40000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 LEU A 206
REMARK 465 SER A 207
REMARK 465 LYS A 208
REMARK 465 VAL A 209
REMARK 465 PRO A 210
REMARK 465 LEU A 211
REMARK 465 THR A 212
REMARK 465 GLN A 213
REMARK 465 ALA A 214
REMARK 465 THR A 215
REMARK 465 ARG A 216
REMARK 465 GLY A 217
REMARK 465 PRO A 218
REMARK 465 GLN A 219
REMARK 465 VAL A 220
REMARK 465 GLN A 221
REMARK 465 GLN A 222
REMARK 465 ASN A 465
REMARK 465 GLN A 466
REMARK 465 HIS A 467
REMARK 465 ASN A 468
REMARK 465 ALA A 469
REMARK 465 PRO A 470
REMARK 465 ILE A 471
REMARK 465 PRO A 472
REMARK 465 GLN A 473
REMARK 465 GLY A 474
REMARK 465 GLU A 538
REMARK 465 GLY A 539
REMARK 465 PRO A 540
REMARK 465 TRP A 667
REMARK 465 ARG A 668
REMARK 465 LYS A 669
REMARK 465 SER A 670
REMARK 465 GLY A 671
REMARK 465 TYR A 672
REMARK 465 GLN A 673
REMARK 465 ASP A 674
REMARK 465 MET A 675
REMARK 465 PRO A 676
REMARK 465 GLU A 677
REMARK 465 TYR A 678
REMARK 465 PRO A 724
REMARK 465 SER A 725
REMARK 465 GLN A 726
REMARK 465 THR A 727
REMARK 465 HIS A 728
REMARK 465 ASN A 729
REMARK 465 ASN A 730
REMARK 465 MET A 731
REMARK 465 TYR A 732
REMARK 465 ALA A 733
REMARK 465 TRP A 734
REMARK 465 GLY A 735
REMARK 465 GLN A 736
REMARK 465 GLU A 737
REMARK 465 SER A 738
REMARK 465 GLY A 739
REMARK 465 ALA A 740
REMARK 465 PRO A 741
REMARK 465 ILE A 742
REMARK 465 LEU A 743
REMARK 465 THR A 744
REMARK 465 ASP A 745
REMARK 465 TYR B 467
REMARK 465 ASN B 468
REMARK 465 PRO B 469
REMARK 465 LEU B 470
REMARK 465 THR B 471
REMARK 465 ARG B 472
REMARK 465 VAL B 473
REMARK 465 TYR B 474
REMARK 465 GLY B 475
REMARK 465 ASP B 663
REMARK 465 ILE B 664
REMARK 465 HIS B 665
REMARK 465 LEU B 883
REMARK 465 SER B 884
REMARK 465 ASN B 885
REMARK 465 GLN B 886
REMARK 465 GLN B 887
REMARK 465 GLU C 24
REMARK 465 GLN C 25
REMARK 465 SER C 26
REMARK 465 GLY C 27
REMARK 465 ARG C 28
REMARK 465 ARG C 133
REMARK 465 ASN C 134
REMARK 465 LEU C 135
REMARK 465 GLY C 136
REMARK 465 SER C 137
REMARK 465 ILE C 138
REMARK 465 ASN C 139
REMARK 465 THR C 140
REMARK 465 GLU C 141
REMARK 465 LEU C 142
REMARK 465 GLN C 143
REMARK 465 ASP C 144
REMARK 465 VAL C 145
REMARK 465 GLN C 146
REMARK 465 ARG C 147
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 ARG A 33 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 746 CG OD1 OD2
REMARK 470 ARG B 769 CG CD NE CZ NH1 NH2
REMARK 470 MET C 1 CG SD CE
REMARK 470 VAL C 2 CG1 CG2
REMARK 470 LEU C 3 CG CD1 CD2
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 LEU B 958 N ILE B 960 1.54
REMARK 500 OG SER B 551 OE1 GLU B 611 1.86
REMARK 500 O HOH B 1208 O HOH B 1225 1.92
REMARK 500 OE1 GLN B 1089 O HOH B 1201 2.02
REMARK 500 OE2 GLU B 815 O HOH B 1202 2.04
REMARK 500 OG SER B 712 O HOH B 1203 2.06
REMARK 500 OH TYR B 719 O HOH B 1204 2.11
REMARK 500 OD2 ASP B 839 O HOH B 1205 2.11
REMARK 500 O PRO B 969 O HOH B 1206 2.13
REMARK 500 OD2 ASP B 950 O HOH B 1207 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO B 477 C - N - CA ANGL. DEV. = 17.5 DEGREES
REMARK 500 PRO B 477 C - N - CD ANGL. DEV. = -16.6 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 CYS A 66 -70.98 -68.37
REMARK 500 ASN A 105 89.66 -172.10
REMARK 500 SER A 116 77.66 61.59
REMARK 500 CYS A 138 78.10 -104.12
REMARK 500 CYS A 180 49.05 -87.55
REMARK 500 GLU A 181 -117.75 58.57
REMARK 500 SER A 226 145.92 -170.67
REMARK 500 SER A 263 59.00 -102.50
REMARK 500 ASN A 281 61.25 64.08
REMARK 500 ALA A 321 86.24 -155.86
REMARK 500 ASN A 378 49.65 -96.08
REMARK 500 ASP A 393 -158.96 -100.22
REMARK 500 PRO A 422 90.18 -68.15
REMARK 500 PRO A 453 8.90 -65.39
REMARK 500 ARG A 476 102.09 -161.08
REMARK 500 THR A 508 40.67 -152.95
REMARK 500 ASP A 611 -166.91 -74.21
REMARK 500 ASP A 645 38.89 -95.66
REMARK 500 ALA A 665 8.93 -69.10
REMARK 500 GLU B 356 -71.35 -63.05
REMARK 500 ARG B 357 16.13 56.82
REMARK 500 ASN B 358 39.11 -145.06
REMARK 500 SER B 433 -73.19 -100.02
REMARK 500 LEU B 445 -74.51 -117.43
REMARK 500 GLN B 447 -8.67 72.63
REMARK 500 GLU B 463 49.72 -81.56
REMARK 500 PRO B 493 -166.91 -77.67
REMARK 500 ASN B 539 -147.71 -95.77
REMARK 500 ASP B 550 -86.11 -135.85
REMARK 500 ASP B 575 80.00 -155.88
REMARK 500 GLU B 582 -65.25 -109.79
REMARK 500 ASN B 583 35.01 -98.87
REMARK 500 ALA B 615 68.45 -101.97
REMARK 500 SER B 660 -161.57 -77.35
REMARK 500 ALA B 661 53.69 -94.94
REMARK 500 LEU B 692 56.12 -110.97
REMARK 500 GLU B 746 62.86 31.68
REMARK 500 ARG B 769 -109.76 -88.35
REMARK 500 LEU B 795 46.34 -91.28
REMARK 500 ASP B 797 -72.57 -60.28
REMARK 500 ALA B 858 -73.62 -129.76
REMARK 500 THR B 914 -73.54 -118.33
REMARK 500 ASN B 951 46.25 -155.70
REMARK 500 GLU B 955 14.14 -148.38
REMARK 500 ASN B 959 -22.81 -16.00
REMARK 500 SER B 961 -102.85 50.65
REMARK 500 LEU B 978 -177.83 -69.20
REMARK 500 ASN B 999 34.55 -86.82
REMARK 500 GLN B1019 -70.29 -61.94
REMARK 500 ILE B1055 -18.53 -49.31
REMARK 500
REMARK 500 THIS ENTRY HAS 59 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 801 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 61 SG
REMARK 620 2 CYS A 66 SG 141.6
REMARK 620 3 CYS A 85 SG 107.1 98.5
REMARK 620 4 CYS A 88 SG 110.9 89.8 103.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1101 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 431 SG
REMARK 620 2 CYS B 434 SG 123.0
REMARK 620 3 CYS B 452 SG 107.2 104.8
REMARK 620 4 CYS B 455 SG 103.7 104.8 113.7
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLT B 1102
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5VNE RELATED DB: PDB
REMARK 900 RELATED ID: 5VNF RELATED DB: PDB
REMARK 900 RELATED ID: 5VNG RELATED DB: PDB
REMARK 900 RELATED ID: 5VNH RELATED DB: PDB
REMARK 900 RELATED ID: 5VNI RELATED DB: PDB
REMARK 900 RELATED ID: 5VNJ RELATED DB: PDB
REMARK 900 RELATED ID: 5VNK RELATED DB: PDB
REMARK 900 RELATED ID: 5VNL RELATED DB: PDB
REMARK 900 RELATED ID: 5VNN RELATED DB: PDB
REMARK 900 RELATED ID: 5VNO RELATED DB: PDB
DBREF 5VNM A 1 764 UNP Q15436 SC23A_HUMAN 1 764
DBREF 5VNM B 346 1093 UNP O95486 SC24A_HUMAN 346 1093
DBREF 5VNM C 1 157 UNP O08547 SC22B_MOUSE 1 157
SEQADV 5VNM ALA B 1056 UNP O95486 ARG 1056 CONFLICT
SEQRES 1 A 764 MET THR THR TYR LEU GLU PHE ILE GLN GLN ASN GLU GLU
SEQRES 2 A 764 ARG ASP GLY VAL ARG PHE SER TRP ASN VAL TRP PRO SER
SEQRES 3 A 764 SER ARG LEU GLU ALA THR ARG MET VAL VAL PRO VAL ALA
SEQRES 4 A 764 ALA LEU PHE THR PRO LEU LYS GLU ARG PRO ASP LEU PRO
SEQRES 5 A 764 PRO ILE GLN TYR GLU PRO VAL LEU CYS SER ARG THR THR
SEQRES 6 A 764 CYS ARG ALA VAL LEU ASN PRO LEU CYS GLN VAL ASP TYR
SEQRES 7 A 764 ARG ALA LYS LEU TRP ALA CYS ASN PHE CYS TYR GLN ARG
SEQRES 8 A 764 ASN GLN PHE PRO PRO SER TYR ALA GLY ILE SER GLU LEU
SEQRES 9 A 764 ASN GLN PRO ALA GLU LEU LEU PRO GLN PHE SER SER ILE
SEQRES 10 A 764 GLU TYR VAL VAL LEU ARG GLY PRO GLN MET PRO LEU ILE
SEQRES 11 A 764 PHE LEU TYR VAL VAL ASP THR CYS MET GLU ASP GLU ASP
SEQRES 12 A 764 LEU GLN ALA LEU LYS GLU SER MET GLN MET SER LEU SER
SEQRES 13 A 764 LEU LEU PRO PRO THR ALA LEU VAL GLY LEU ILE THR PHE
SEQRES 14 A 764 GLY ARG MET VAL GLN VAL HIS GLU LEU GLY CYS GLU GLY
SEQRES 15 A 764 ILE SER LYS SER TYR VAL PHE ARG GLY THR LYS ASP LEU
SEQRES 16 A 764 SER ALA LYS GLN LEU GLN GLU MET LEU GLY LEU SER LYS
SEQRES 17 A 764 VAL PRO LEU THR GLN ALA THR ARG GLY PRO GLN VAL GLN
SEQRES 18 A 764 GLN PRO PRO PRO SER ASN ARG PHE LEU GLN PRO VAL GLN
SEQRES 19 A 764 LYS ILE ASP MET ASN LEU THR ASP LEU LEU GLY GLU LEU
SEQRES 20 A 764 GLN ARG ASP PRO TRP PRO VAL PRO GLN GLY LYS ARG PRO
SEQRES 21 A 764 LEU ARG SER SER GLY VAL ALA LEU SER ILE ALA VAL GLY
SEQRES 22 A 764 LEU LEU GLU CYS THR PHE PRO ASN THR GLY ALA ARG ILE
SEQRES 23 A 764 MET MET PHE ILE GLY GLY PRO ALA THR GLN GLY PRO GLY
SEQRES 24 A 764 MET VAL VAL GLY ASP GLU LEU LYS THR PRO ILE ARG SER
SEQRES 25 A 764 TRP HIS ASP ILE ASP LYS ASP ASN ALA LYS TYR VAL LYS
SEQRES 26 A 764 LYS GLY THR LYS HIS PHE GLU ALA LEU ALA ASN ARG ALA
SEQRES 27 A 764 ALA THR THR GLY HIS VAL ILE ASP ILE TYR ALA CYS ALA
SEQRES 28 A 764 LEU ASP GLN THR GLY LEU LEU GLU MET LYS CYS CYS PRO
SEQRES 29 A 764 ASN LEU THR GLY GLY TYR MET VAL MET GLY ASP SER PHE
SEQRES 30 A 764 ASN THR SER LEU PHE LYS GLN THR PHE GLN ARG VAL PHE
SEQRES 31 A 764 THR LYS ASP MET HIS GLY GLN PHE LYS MET GLY PHE GLY
SEQRES 32 A 764 GLY THR LEU GLU ILE LYS THR SER ARG GLU ILE LYS ILE
SEQRES 33 A 764 SER GLY ALA ILE GLY PRO CYS VAL SER LEU ASN SER LYS
SEQRES 34 A 764 GLY PRO CYS VAL SER GLU ASN GLU ILE GLY THR GLY GLY
SEQRES 35 A 764 THR CYS GLN TRP LYS ILE CYS GLY LEU SER PRO THR THR
SEQRES 36 A 764 THR LEU ALA ILE TYR PHE GLU VAL VAL ASN GLN HIS ASN
SEQRES 37 A 764 ALA PRO ILE PRO GLN GLY GLY ARG GLY ALA ILE GLN PHE
SEQRES 38 A 764 VAL THR GLN TYR GLN HIS SER SER GLY GLN ARG ARG ILE
SEQRES 39 A 764 ARG VAL THR THR ILE ALA ARG ASN TRP ALA ASP ALA GLN
SEQRES 40 A 764 THR GLN ILE GLN ASN ILE ALA ALA SER PHE ASP GLN GLU
SEQRES 41 A 764 ALA ALA ALA ILE LEU MET ALA ARG LEU ALA ILE TYR ARG
SEQRES 42 A 764 ALA GLU THR GLU GLU GLY PRO ASP VAL LEU ARG TRP LEU
SEQRES 43 A 764 ASP ARG GLN LEU ILE ARG LEU CYS GLN LYS PHE GLY GLU
SEQRES 44 A 764 TYR HIS LYS ASP ASP PRO SER SER PHE ARG PHE SER GLU
SEQRES 45 A 764 THR PHE SER LEU TYR PRO GLN PHE MET PHE HIS LEU ARG
SEQRES 46 A 764 ARG SER SER PHE LEU GLN VAL PHE ASN ASN SER PRO ASP
SEQRES 47 A 764 GLU SER SER TYR TYR ARG HIS HIS PHE MET ARG GLN ASP
SEQRES 48 A 764 LEU THR GLN SER LEU ILE MET ILE GLN PRO ILE LEU TYR
SEQRES 49 A 764 ALA TYR SER PHE SER GLY PRO PRO GLU PRO VAL LEU LEU
SEQRES 50 A 764 ASP SER SER SER ILE LEU ALA ASP ARG ILE LEU LEU MET
SEQRES 51 A 764 ASP THR PHE PHE GLN ILE LEU ILE TYR HIS GLY GLU THR
SEQRES 52 A 764 ILE ALA GLN TRP ARG LYS SER GLY TYR GLN ASP MET PRO
SEQRES 53 A 764 GLU TYR GLU ASN PHE ARG HIS LEU LEU GLN ALA PRO VAL
SEQRES 54 A 764 ASP ASP ALA GLN GLU ILE LEU HIS SER ARG PHE PRO MET
SEQRES 55 A 764 PRO ARG TYR ILE ASP THR GLU HIS GLY GLY SER GLN ALA
SEQRES 56 A 764 ARG PHE LEU LEU SER LYS VAL ASN PRO SER GLN THR HIS
SEQRES 57 A 764 ASN ASN MET TYR ALA TRP GLY GLN GLU SER GLY ALA PRO
SEQRES 58 A 764 ILE LEU THR ASP ASP VAL SER LEU GLN VAL PHE MET ASP
SEQRES 59 A 764 HIS LEU LYS LYS LEU ALA VAL SER SER ALA
SEQRES 1 B 748 GLU GLY LEU ARG VAL VAL ASN LEU LEU GLN GLU ARG ASN
SEQRES 2 B 748 MET LEU PRO SER THR PRO LEU LYS PRO PRO VAL PRO ASN
SEQRES 3 B 748 LEU HIS GLU ASP ILE GLN LYS LEU ASN CYS ASN PRO GLU
SEQRES 4 B 748 LEU PHE ARG CYS THR LEU THR SER ILE PRO GLN THR GLN
SEQRES 5 B 748 ALA LEU LEU ASN LYS ALA LYS LEU PRO LEU GLY LEU LEU
SEQRES 6 B 748 LEU HIS PRO PHE LYS ASP LEU VAL GLN LEU PRO VAL VAL
SEQRES 7 B 748 THR SER SER THR ILE VAL ARG CYS ARG SER CYS ARG THR
SEQRES 8 B 748 TYR ILE ASN PRO PHE VAL SER PHE LEU ASP GLN ARG ARG
SEQRES 9 B 748 TRP LYS CYS ASN LEU CYS TYR ARG VAL ASN ASP VAL PRO
SEQRES 10 B 748 GLU GLU PHE LEU TYR ASN PRO LEU THR ARG VAL TYR GLY
SEQRES 11 B 748 GLU PRO HIS ARG ARG PRO GLU VAL GLN ASN ALA THR ILE
SEQRES 12 B 748 GLU PHE MET ALA PRO SER GLU TYR MET LEU ARG PRO PRO
SEQRES 13 B 748 GLN PRO PRO VAL TYR LEU PHE VAL PHE ASP VAL SER HIS
SEQRES 14 B 748 ASN ALA VAL GLU THR GLY TYR LEU ASN SER VAL CYS GLN
SEQRES 15 B 748 SER LEU LEU ASP ASN LEU ASP LEU LEU PRO GLY ASN THR
SEQRES 16 B 748 ARG THR LYS ILE GLY PHE ILE THR PHE ASP SER THR ILE
SEQRES 17 B 748 HIS PHE TYR GLY LEU GLN GLU SER LEU SER GLN PRO GLN
SEQRES 18 B 748 MET LEU ILE VAL SER ASP ILE GLU ASP VAL PHE ILE PRO
SEQRES 19 B 748 MET PRO GLU ASN LEU LEU VAL ASN LEU ASN GLU SER LYS
SEQRES 20 B 748 GLU LEU VAL GLN ASP LEU LEU LYS THR LEU PRO GLN MET
SEQRES 21 B 748 PHE THR LYS THR LEU GLU THR GLN SER ALA LEU GLY PRO
SEQRES 22 B 748 ALA LEU GLN ALA ALA PHE LYS LEU MET SER PRO THR GLY
SEQRES 23 B 748 GLY ARG MET SER VAL PHE GLN THR GLN LEU PRO THR LEU
SEQRES 24 B 748 GLY VAL GLY ALA LEU LYS PRO ARG GLU GLU PRO ASN HIS
SEQRES 25 B 748 ARG SER SER ALA LYS ASP ILE HIS MET THR PRO SER THR
SEQRES 26 B 748 ASP PHE TYR LYS LYS LEU ALA LEU ASP CYS SER GLY GLN
SEQRES 27 B 748 GLN VAL ALA VAL ASP LEU PHE LEU LEU SER GLY GLN TYR
SEQRES 28 B 748 SER ASP LEU ALA SER LEU GLY CYS ILE SER ARG TYR SER
SEQRES 29 B 748 ALA GLY SER VAL TYR TYR TYR PRO SER TYR HIS HIS GLN
SEQRES 30 B 748 HIS ASN PRO VAL GLN VAL GLN LYS LEU GLN LYS GLU LEU
SEQRES 31 B 748 GLN ARG TYR LEU THR ARG LYS ILE GLY PHE GLU ALA VAL
SEQRES 32 B 748 MET ARG ILE ARG CYS THR LYS GLY LEU SER ILE HIS THR
SEQRES 33 B 748 PHE HIS GLY ASN PHE PHE VAL ARG SER THR ASP LEU LEU
SEQRES 34 B 748 SER LEU PRO ASN VAL ASN PRO ASP ALA GLY TYR ALA VAL
SEQRES 35 B 748 GLN MET SER VAL GLU GLU SER LEU THR ASP THR GLN LEU
SEQRES 36 B 748 VAL SER PHE GLN SER ALA LEU LEU TYR THR SER SER LYS
SEQRES 37 B 748 GLY GLU ARG ARG ILE ARG VAL HIS THR LEU CYS LEU PRO
SEQRES 38 B 748 VAL VAL SER THR LEU ASN ASP VAL PHE LEU GLY ALA ASP
SEQRES 39 B 748 VAL GLN ALA ILE SER GLY LEU LEU ALA ASN MET ALA VAL
SEQRES 40 B 748 ASP ARG SER MET THR ALA SER LEU SER ASP ALA ARG ASP
SEQRES 41 B 748 ALA LEU VAL ASN ALA VAL ILE ASP SER LEU SER ALA TYR
SEQRES 42 B 748 ARG SER SER VAL LEU SER ASN GLN GLN PRO GLY LEU MET
SEQRES 43 B 748 VAL PRO PHE SER LEU ARG LEU PHE PRO LEU PHE VAL LEU
SEQRES 44 B 748 ALA LEU LEU LYS GLN LYS SER PHE GLN THR GLY THR ASN
SEQRES 45 B 748 ALA ARG LEU ASP GLU ARG ILE PHE ALA MET CYS GLN VAL
SEQRES 46 B 748 LYS ASN GLN PRO LEU VAL TYR LEU MET LEU THR THR HIS
SEQRES 47 B 748 PRO SER LEU TYR ARG VAL ASP ASN LEU SER ASP GLU GLY
SEQRES 48 B 748 ALA LEU ASN ILE SER ASP ARG THR ILE PRO GLN PRO PRO
SEQRES 49 B 748 ILE LEU GLN LEU SER VAL GLU LYS LEU SER ARG ASP GLY
SEQRES 50 B 748 ALA PHE LEU MET ASP ALA GLY SER VAL LEU MET LEU TRP
SEQRES 51 B 748 VAL GLY LYS ASN CYS THR GLN ASN PHE LEU SER GLN VAL
SEQRES 52 B 748 LEU GLY VAL GLN ASN TYR ALA SER ILE PRO GLN PRO MET
SEQRES 53 B 748 THR ASP LEU PRO GLU LEU ASP THR PRO GLU SER ALA ARG
SEQRES 54 B 748 ILE ILE ALA PHE ILE SER TRP LEU ARG GLU GLN ARG PRO
SEQRES 55 B 748 PHE PHE PRO ILE LEU TYR VAL ILE ALA ASP GLU SER PRO
SEQRES 56 B 748 MET LYS ALA ASN PHE LEU GLN ASN MET ILE GLU ASP ARG
SEQRES 57 B 748 THR GLU SER ALA LEU SER TYR TYR GLU PHE LEU LEU HIS
SEQRES 58 B 748 ILE GLN GLN GLN VAL ASN LYS
SEQRES 1 C 157 MET VAL LEU LEU THR MET ILE ALA ARG VAL ALA ASP GLY
SEQRES 2 C 157 LEU PRO LEU ALA ALA SER MET GLN GLU ASP GLU GLN SER
SEQRES 3 C 157 GLY ARG ASP LEU GLN GLN TYR GLN SER GLN ALA LYS GLN
SEQRES 4 C 157 LEU PHE ARG LYS LEU ASN GLU GLN SER PRO THR ARG CYS
SEQRES 5 C 157 THR LEU GLU ALA GLY ALA MET THR PHE HIS TYR ILE ILE
SEQRES 6 C 157 GLU GLN GLY VAL CYS TYR LEU VAL LEU CYS GLU ALA ALA
SEQRES 7 C 157 PHE PRO LYS LYS LEU ALA PHE ALA TYR LEU GLU ASP LEU
SEQRES 8 C 157 HIS SER GLU PHE ASP GLU GLN HIS GLY LYS LYS VAL PRO
SEQRES 9 C 157 THR VAL SER ARG PRO TYR SER PHE ILE GLU PHE ASP THR
SEQRES 10 C 157 PHE ILE GLN LYS THR LYS LYS LEU TYR ILE ASP SER ARG
SEQRES 11 C 157 ALA ARG ARG ASN LEU GLY SER ILE ASN THR GLU LEU GLN
SEQRES 12 C 157 ASP VAL GLN ARG ILE MET VAL ALA ASN ILE GLU GLU VAL
SEQRES 13 C 157 LEU
HET ZN A 801 1
HET ZN B1101 1
HET CLT B1102 12
HETNAM ZN ZINC ION
HETNAM CLT 4-PHENYL-BUTANOIC ACID
HETSYN CLT GAMMA-PHENYL-BUTYRIC ACID
FORMUL 4 ZN 2(ZN 2+)
FORMUL 6 CLT C10 H12 O2
FORMUL 7 HOH *40(H2 O)
HELIX 1 AA1 THR A 3 GLY A 16 1 14
HELIX 2 AA2 SER A 27 THR A 32 1 6
HELIX 3 AA3 PRO A 95 ALA A 99 5 5
HELIX 4 AA4 LEU A 111 SER A 115 5 5
HELIX 5 AA5 GLU A 140 SER A 156 1 17
HELIX 6 AA6 SER A 196 GLY A 205 1 10
HELIX 7 AA7 VAL A 233 LEU A 247 1 15
HELIX 8 AA8 SER A 263 PHE A 279 1 17
HELIX 9 AA9 SER A 312 LYS A 318 1 7
HELIX 10 AB1 TYR A 323 GLY A 342 1 20
HELIX 11 AB2 GLY A 356 LYS A 361 1 6
HELIX 12 AB3 LYS A 361 THR A 367 1 7
HELIX 13 AB4 THR A 379 VAL A 389 1 11
HELIX 14 AB5 ASP A 505 GLN A 507 5 3
HELIX 15 AB6 THR A 508 SER A 516 1 9
HELIX 16 AB7 ASP A 518 GLU A 535 1 18
HELIX 17 AB8 VAL A 542 GLY A 558 1 17
HELIX 18 AB9 LEU A 576 SER A 587 1 12
HELIX 19 AC1 SER A 596 MET A 608 1 13
HELIX 20 AC2 ASP A 611 GLN A 620 1 10
HELIX 21 AC3 ASP A 638 ILE A 642 5 5
HELIX 22 AC4 ASN A 680 ARG A 699 1 20
HELIX 23 AC5 GLY A 712 GLN A 714 5 3
HELIX 24 AC6 ALA A 715 VAL A 722 1 8
HELIX 25 AC7 SER A 748 VAL A 761 1 14
HELIX 26 AC8 LEU B 353 ARG B 357 1 5
HELIX 27 AC9 HIS B 373 LYS B 378 1 6
HELIX 28 AD1 THR B 396 LYS B 404 1 9
HELIX 29 AD2 ARG B 480 GLN B 484 5 5
HELIX 30 AD3 PRO B 493 MET B 497 5 5
HELIX 31 AD4 SER B 513 GLY B 520 1 8
HELIX 32 AD5 GLY B 520 ASN B 532 1 13
HELIX 33 AD6 SER B 591 LEU B 602 1 12
HELIX 34 AD7 PRO B 603 MET B 605 5 3
HELIX 35 AD8 ALA B 615 SER B 628 1 14
HELIX 36 AD9 ASP B 671 GLN B 683 1 13
HELIX 37 AE1 ASP B 698 GLY B 703 1 6
HELIX 38 AE2 GLY B 703 TYR B 708 1 6
HELIX 39 AE3 ASN B 724 ARG B 741 1 18
HELIX 40 AE4 THR B 830 GLY B 837 1 8
HELIX 41 AE5 ASP B 839 ALA B 858 1 20
HELIX 42 AE6 SER B 859 SER B 880 1 22
HELIX 43 AE7 SER B 895 ARG B 897 5 3
HELIX 44 AE8 LEU B 898 GLN B 909 1 12
HELIX 45 AE9 ARG B 919 GLN B 933 1 15
HELIX 46 AF1 PRO B 934 HIS B 943 1 10
HELIX 47 AF2 SER B 974 LEU B 978 5 5
HELIX 48 AF3 THR B 1001 VAL B 1008 1 8
HELIX 49 AF4 ASN B 1013 ILE B 1017 5 5
HELIX 50 AF5 THR B 1029 GLN B 1045 1 17
HELIX 51 AF6 PHE B 1065 MET B 1069 5 5
HELIX 52 AF7 SER B 1079 ASN B 1092 1 14
HELIX 53 AF8 LEU C 30 LEU C 44 1 15
HELIX 54 AF9 PRO C 80 GLY C 100 1 21
HELIX 55 AG1 LYS C 102 VAL C 106 5 5
HELIX 56 AG2 PHE C 112 GLU C 114 5 3
HELIX 57 AG3 PHE C 115 LYS C 124 1 10
HELIX 58 AG4 ILE C 153 LEU C 157 1 5
SHEET 1 AA1 2 VAL A 23 TRP A 24 0
SHEET 2 AA1 2 ASN A 502 TRP A 503 1 O ASN A 502 N TRP A 24
SHEET 1 AA2 4 ALA A 39 PHE A 42 0
SHEET 2 AA2 4 LEU A 457 VAL A 463 -1 O ILE A 459 N ALA A 40
SHEET 3 AA2 4 ILE A 414 ILE A 420 -1 N LYS A 415 O GLU A 462
SHEET 4 AA2 4 VAL A 433 GLY A 439 1 O SER A 434 N ILE A 416
SHEET 1 AA3 3 GLN A 75 ASP A 77 0
SHEET 2 AA3 3 LEU A 82 ALA A 84 -1 O ALA A 84 N GLN A 75
SHEET 3 AA3 3 ARG A 91 GLN A 93 -1 O ASN A 92 N TRP A 83
SHEET 1 AA4 6 ILE A 117 VAL A 121 0
SHEET 2 AA4 6 ARG A 492 ILE A 499 -1 O VAL A 496 N ILE A 117
SHEET 3 AA4 6 ILE A 479 GLN A 486 -1 N THR A 483 O ARG A 495
SHEET 4 AA4 6 GLY A 401 THR A 410 -1 N PHE A 402 O GLN A 486
SHEET 5 AA4 6 GLN A 445 LEU A 451 -1 O ILE A 448 N GLY A 404
SHEET 6 AA4 6 VAL A 424 SER A 425 -1 N VAL A 424 O LYS A 447
SHEET 1 AA5 8 GLN A 231 PRO A 232 0
SHEET 2 AA5 8 LEU A 163 PHE A 169 -1 N VAL A 164 O GLN A 231
SHEET 3 AA5 8 MET A 172 HIS A 176 -1 O GLN A 174 N THR A 168
SHEET 4 AA5 8 SER A 186 ARG A 190 -1 O TYR A 187 N VAL A 175
SHEET 5 AA5 8 GLN B 566 VAL B 570 1 O ILE B 569 N VAL A 188
SHEET 6 AA5 8 ILE B 553 GLY B 557 -1 N PHE B 555 O LEU B 568
SHEET 7 AA5 8 LYS B 543 PHE B 549 -1 N THR B 548 O HIS B 554
SHEET 8 AA5 8 VAL B 586 ASN B 587 -1 O VAL B 586 N ILE B 544
SHEET 1 AA614 MET A 371 GLY A 374 0
SHEET 2 AA614 VAL A 344 CYS A 350 1 N ALA A 349 O VAL A 372
SHEET 3 AA614 ALA A 284 ILE A 290 1 N ILE A 286 O VAL A 344
SHEET 4 AA614 ILE A 130 ASP A 136 1 N VAL A 134 O MET A 287
SHEET 5 AA614 LEU A 163 PHE A 169 1 O ILE A 167 N VAL A 135
SHEET 6 AA614 MET A 172 HIS A 176 -1 O GLN A 174 N THR A 168
SHEET 7 AA614 SER A 186 ARG A 190 -1 O TYR A 187 N VAL A 175
SHEET 8 AA614 GLN B 566 VAL B 570 1 O ILE B 569 N VAL A 188
SHEET 9 AA614 ILE B 553 GLY B 557 -1 N PHE B 555 O LEU B 568
SHEET 10 AA614 LYS B 543 PHE B 549 -1 N THR B 548 O HIS B 554
SHEET 11 AA614 VAL B 505 ASP B 511 1 N PHE B 510 O ILE B 547
SHEET 12 AA614 GLY B 632 GLN B 638 1 O SER B 635 N VAL B 509
SHEET 13 AA614 VAL B 685 LEU B 691 1 O PHE B 690 N VAL B 636
SHEET 14 AA614 VAL B 713 TYR B 715 1 O TYR B 714 N LEU B 689
SHEET 1 AA7 2 GLU A 559 HIS A 561 0
SHEET 2 AA7 2 ASP A 564 ARG A 569 -1 O ARG A 569 N GLU A 559
SHEET 1 AA8 5 GLU A 633 PRO A 634 0
SHEET 2 AA8 5 ILE A 622 TYR A 626 -1 N ALA A 625 O GLU A 633
SHEET 3 AA8 5 ILE A 647 THR A 652 -1 O ILE A 647 N TYR A 626
SHEET 4 AA8 5 GLN A 655 HIS A 660 -1 O LEU A 657 N MET A 650
SHEET 5 AA8 5 ARG A 704 GLU A 709 1 O ILE A 706 N ILE A 658
SHEET 1 AA9 2 VAL B 350 ASN B 352 0
SHEET 2 AA9 2 MET B 891 PRO B 893 -1 O VAL B 892 N VAL B 351
SHEET 1 AB1 4 PHE B 386 CYS B 388 0
SHEET 2 AB1 4 GLY B 408 LEU B 411 -1 O LEU B 410 N ARG B 387
SHEET 3 AB1 4 TYR B 785 VAL B 791 -1 O TYR B 785 N LEU B 411
SHEET 4 AB1 4 LEU B 757 HIS B 763 -1 N HIS B 760 O GLN B 788
SHEET 1 AB2 4 ILE B 393 PRO B 394 0
SHEET 2 AB2 4 ARG B 816 VAL B 828 1 O PRO B 826 N ILE B 393
SHEET 3 AB2 4 THR B 487 MET B 491 -1 N PHE B 490 O ILE B 818
SHEET 4 AB2 4 VAL B 422 VAL B 423 1 N VAL B 423 O GLU B 489
SHEET 1 AB3 5 ILE B 393 PRO B 394 0
SHEET 2 AB3 5 ARG B 816 VAL B 828 1 O PRO B 826 N ILE B 393
SHEET 3 AB3 5 LEU B 800 THR B 810 -1 N VAL B 801 O LEU B 825
SHEET 4 AB3 5 GLY B 744 CYS B 753 -1 N ARG B 752 O GLN B 804
SHEET 5 AB3 5 LEU B 774 VAL B 779 -1 O LEU B 776 N ALA B 747
SHEET 1 AB4 3 SER B 443 PHE B 444 0
SHEET 2 AB4 3 ARG B 449 LYS B 451 -1 O LYS B 451 N SER B 443
SHEET 3 AB4 3 VAL B 458 ASP B 460 -1 O ASN B 459 N TRP B 450
SHEET 1 AB5 3 SER B 945 ARG B 948 0
SHEET 2 AB5 3 ALA B 983 ASP B 987 -1 O ASP B 987 N SER B 945
SHEET 3 AB5 3 LEU B 992 VAL B 996 -1 O TRP B 995 N PHE B 984
SHEET 1 AB6 6 PRO C 15 SER C 19 0
SHEET 2 AB6 6 THR C 5 ARG C 9 -1 N ILE C 7 O LEU C 16
SHEET 3 AB6 6 VAL C 69 GLU C 76 -1 O CYS C 70 N ALA C 8
SHEET 4 AB6 6 MET C 59 GLU C 66 -1 N HIS C 62 O VAL C 73
SHEET 5 AB6 6 ARG C 51 ALA C 56 -1 N ALA C 56 O MET C 59
SHEET 6 AB6 6 VAL C 150 ASN C 152 1 O ALA C 151 N THR C 53
LINK SG CYS A 61 ZN ZN A 801 1555 1555 2.45
LINK SG CYS A 66 ZN ZN A 801 1555 1555 2.36
LINK SG CYS A 85 ZN ZN A 801 1555 1555 2.36
LINK SG CYS A 88 ZN ZN A 801 1555 1555 2.32
LINK SG CYS B 431 ZN ZN B1101 1555 1555 2.29
LINK SG CYS B 434 ZN ZN B1101 1555 1555 2.30
LINK SG CYS B 452 ZN ZN B1101 1555 1555 2.33
LINK SG CYS B 455 ZN ZN B1101 1555 1555 2.26
SITE 1 AC1 4 CYS A 61 CYS A 66 CYS A 85 CYS A 88
SITE 1 AC2 4 CYS B 431 CYS B 434 CYS B 452 CYS B 455
SITE 1 AC3 7 TYR B 437 VAL B 748 ARG B 750 ARG B 752
SITE 2 AC3 7 ALA B 806 LEU B 808 ILE B 818
CRYST1 149.183 96.800 130.609 90.00 90.22 90.00 C 1 2 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.006703 0.000000 0.000026 0.00000
SCALE2 0.000000 0.010331 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007656 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
