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PDBsum entry 3t1e

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Hydrolase PDB id
3t1e
Jmol
Contents
Protein chains
447 a.a.
37 a.a.
HEADER    HYDROLASE                               21-JUL-11   3T1E
TITLE     THE STRUCTURE OF THE NEWCASTLE DISEASE VIRUS HEMAGGLUTININ-
TITLE    2 NEURAMINIDASE (HN) ECTODOMAIN REVEALS A 4-HELIX BUNDLE STALK
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: HEMAGGLUTININ-NEURAMINIDASE;
COMPND   3 CHAIN: A, B, E, F;
COMPND   4 FRAGMENT: NDV HN ECTODOMAIN;
COMPND   5 EC: 3.2.1.18;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: NEWCASTLE DISEASE VIRUS;
SOURCE   3 ORGANISM_COMMON: NDV;
SOURCE   4 ORGANISM_TAXID: 11177;
SOURCE   5 STRAIN: CHICKEN/AUSTRALIA-VICTORIA/32;
SOURCE   6 GENE: HN;
SOURCE   7 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   9 EXPRESSION_SYSTEM_CELL: HI5, SF PLUS
KEYWDS    BETA-PROPELLER, 4 HELIX BUNDLE, HEMAGGLUTININ, NEURAMINIDASE,
KEYWDS   2 MEMBRANE PROTEIN, ECTODOMAIN, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    P.YUAN,K.SWANSON,G.P.LESER,R.G.PATERSON,R.A.LAMB,T.S.JARDETZKY
REVDAT   3   21-SEP-11 3T1E    1       JRNL   REMARK
REVDAT   2   14-SEP-11 3T1E    1       JRNL
REVDAT   1   07-SEP-11 3T1E    0
JRNL        AUTH   P.YUAN,K.A.SWANSON,G.P.LESER,R.G.PATERSON,R.A.LAMB,
JRNL        AUTH 2 T.S.JARDETZKY
JRNL        TITL   STRUCTURE OF THE NEWCASTLE DISEASE VIRUS
JRNL        TITL 2 HEMAGGLUTININ-NEURAMINIDASE (HN) ECTODOMAIN REVEALS A
JRNL        TITL 3 FOUR-HELIX BUNDLE STALK.
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 108 14920 2011
JRNL        REFN                   ISSN 0027-8424
JRNL        PMID   21873198
JRNL        DOI    10.1073/PNAS.1111691108
REMARK   2
REMARK   2 RESOLUTION.    3.30 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.1_743)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK   3               : ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : ML
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.89
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9
REMARK   3   NUMBER OF REFLECTIONS             : 25011
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.251
REMARK   3   R VALUE            (WORKING SET) : 0.248
REMARK   3   FREE R VALUE                     : 0.310
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.950
REMARK   3   FREE R VALUE TEST SET COUNT      : 1239
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 48.8989 -  6.8601    0.99     2826   141  0.2606 0.3055
REMARK   3     2  6.8601 -  5.4473    1.00     2674   144  0.2697 0.3636
REMARK   3     3  5.4473 -  4.7594    1.00     2637   141  0.2241 0.2660
REMARK   3     4  4.7594 -  4.3245    1.00     2648   130  0.2134 0.2615
REMARK   3     5  4.3245 -  4.0147    1.00     2626   128  0.2330 0.3351
REMARK   3     6  4.0147 -  3.7781    1.00     2618   125  0.2384 0.3184
REMARK   3     7  3.7781 -  3.5890    1.00     2589   145  0.2496 0.2933
REMARK   3     8  3.5890 -  3.4328    1.00     2581   132  0.2618 0.3576
REMARK   3     9  3.4328 -  3.3010    1.00     2573   153  0.3084 0.3680
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.10
REMARK   3   SHRINKAGE RADIUS   : 0.83
REMARK   3   K_SOL              : 0.31
REMARK   3   B_SOL              : 125.74
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.930
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.450
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) : 5.87250
REMARK   3    B22 (A**2) : 5.87250
REMARK   3    B33 (A**2) : -11.74500
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -0.00000
REMARK   3    B23 (A**2) : 0.00000
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      :  0.005           7160
REMARK   3   ANGLE     :  1.001           9784
REMARK   3   CHIRALITY :  0.071           1103
REMARK   3   PLANARITY :  0.005           1307
REMARK   3   DIHEDRAL  : 13.831           2394
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 15
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 123:165)
REMARK   3    ORIGIN FOR THE GROUP (A): -28.0802 -62.1591  -6.7045
REMARK   3    T TENSOR
REMARK   3      T11:   0.9330 T22:   0.9709
REMARK   3      T33:   0.6280 T12:  -0.1435
REMARK   3      T13:  -0.2918 T23:  -0.0986
REMARK   3    L TENSOR
REMARK   3      L11:   6.6386 L22:   9.3797
REMARK   3      L33:   2.5207 L12:   0.9318
REMARK   3      L13:  -0.9323 L23:  -0.1055
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2577 S12:   0.1895 S13:   0.1829
REMARK   3      S21:  -1.7437 S22:  -0.0215 S23:   1.1284
REMARK   3      S31:   0.3458 S32:   0.5555 S33:   0.2557
REMARK   3   TLS GROUP : 2
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 166:191)
REMARK   3    ORIGIN FOR THE GROUP (A): -14.0358 -57.0892   5.2644
REMARK   3    T TENSOR
REMARK   3      T11:   0.8620 T22:   1.0840
REMARK   3      T33:   0.7374 T12:   0.1045
REMARK   3      T13:  -0.1023 T23:  -0.3225
REMARK   3    L TENSOR
REMARK   3      L11:   4.2208 L22:   9.2427
REMARK   3      L33:   4.7986 L12:  -1.5036
REMARK   3      L13:   4.1926 L23:  -3.3635
REMARK   3    S TENSOR
REMARK   3      S11:   1.4731 S12:   1.1956 S13:  -1.7814
REMARK   3      S21:  -0.7431 S22:  -0.4070 S23:  -0.1240
REMARK   3      S31:   1.4761 S32:   1.4095 S33:  -1.1577
REMARK   3   TLS GROUP : 3
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 192:212)
REMARK   3    ORIGIN FOR THE GROUP (A): -10.9324 -54.8128   7.1119
REMARK   3    T TENSOR
REMARK   3      T11:   0.7988 T22:   0.5448
REMARK   3      T33:   0.9553 T12:  -0.4027
REMARK   3      T13:  -0.2420 T23:  -0.4788
REMARK   3    L TENSOR
REMARK   3      L11:   7.5654 L22:   9.3721
REMARK   3      L33:   3.4776 L12:   1.7687
REMARK   3      L13:  -1.9136 L23:   1.9643
REMARK   3    S TENSOR
REMARK   3      S11:  -2.5386 S12:  -1.0390 S13:   2.2962
REMARK   3      S21:   0.5941 S22:  -0.0530 S23:  -2.9548
REMARK   3      S31:   0.6243 S32:   2.4551 S33:   0.4123
REMARK   3   TLS GROUP : 4
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 213:414)
REMARK   3    ORIGIN FOR THE GROUP (A): -23.3560 -63.0380  18.6313
REMARK   3    T TENSOR
REMARK   3      T11:   0.6207 T22:   0.8222
REMARK   3      T33:   0.5537 T12:  -0.0509
REMARK   3      T13:  -0.2054 T23:  -0.0551
REMARK   3    L TENSOR
REMARK   3      L11:   3.9976 L22:   4.2673
REMARK   3      L33:   2.9113 L12:   1.2029
REMARK   3      L13:  -1.5374 L23:  -1.1936
REMARK   3    S TENSOR
REMARK   3      S11:   0.1936 S12:  -1.1419 S13:   0.0393
REMARK   3      S21:   0.4723 S22:   0.0891 S23:  -0.1178
REMARK   3      S31:   0.2517 S32:   0.4832 S33:  -0.2495
REMARK   3   TLS GROUP : 5
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 123:165)
REMARK   3    ORIGIN FOR THE GROUP (A):   5.9561 -40.2226  -0.9933
REMARK   3    T TENSOR
REMARK   3      T11:   1.2482 T22:   1.0251
REMARK   3      T33:   1.5566 T12:  -0.1675
REMARK   3      T13:  -0.0241 T23:  -0.2749
REMARK   3    L TENSOR
REMARK   3      L11:   6.0712 L22:   3.5122
REMARK   3      L33:   3.5790 L12:   3.0366
REMARK   3      L13:  -0.5067 L23:   1.0414
REMARK   3    S TENSOR
REMARK   3      S11:   0.3399 S12:  -2.2841 S13:   1.4023
REMARK   3      S21:  -0.5143 S22:  -0.8029 S23:  -0.2077
REMARK   3      S31:  -1.4314 S32:   0.2455 S33:   0.3423
REMARK   3   TLS GROUP : 6
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 166:191)
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.1833 -51.0015 -13.0105
REMARK   3    T TENSOR
REMARK   3      T11:   0.7480 T22:   0.9174
REMARK   3      T33:   0.5067 T12:  -0.0555
REMARK   3      T13:  -0.1312 T23:  -0.0409
REMARK   3    L TENSOR
REMARK   3      L11:   8.8806 L22:   9.2663
REMARK   3      L33:   7.4427 L12:   2.0077
REMARK   3      L13:   0.8859 L23:   5.8805
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0215 S12:   1.0425 S13:  -0.6781
REMARK   3      S21:  -0.3197 S22:   1.2745 S23:  -0.9866
REMARK   3      S31:   0.5361 S32:   2.0493 S33:  -0.6617
REMARK   3   TLS GROUP : 7
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 192:212)
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.7478 -52.7210 -14.8517
REMARK   3    T TENSOR
REMARK   3      T11:   1.2345 T22:   1.1050
REMARK   3      T33:   1.2851 T12:  -0.3934
REMARK   3      T13:   0.2128 T23:  -0.1300
REMARK   3    L TENSOR
REMARK   3      L11:   4.6695 L22:   2.2300
REMARK   3      L33:   2.1705 L12:   0.9756
REMARK   3      L13:   2.5116 L23:   0.3412
REMARK   3    S TENSOR
REMARK   3      S11:   0.4533 S12:  -1.1126 S13:   0.0334
REMARK   3      S21:  -0.3795 S22:  -0.7457 S23:  -0.4397
REMARK   3      S31:   1.1510 S32:  -1.0053 S33:   0.8564
REMARK   3   TLS GROUP : 8
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 213:414)
REMARK   3    ORIGIN FOR THE GROUP (A):   3.5270 -44.7794 -26.4112
REMARK   3    T TENSOR
REMARK   3      T11:   1.3346 T22:   0.6639
REMARK   3      T33:   0.8761 T12:  -0.1758
REMARK   3      T13:   0.0566 T23:  -0.0127
REMARK   3    L TENSOR
REMARK   3      L11:   6.0492 L22:   2.5530
REMARK   3      L33:   3.5043 L12:   1.4653
REMARK   3      L13:  -1.9887 L23:  -1.9839
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1041 S12:   0.4861 S13:   0.5390
REMARK   3      S21:  -1.1332 S22:   0.2962 S23:  -0.1457
REMARK   3      S31:   0.3647 S32:   0.4498 S33:  -0.2180
REMARK   3   TLS GROUP : 9
REMARK   3    SELECTION: CHAIN E
REMARK   3    ORIGIN FOR THE GROUP (A): -46.4211 -55.0593   4.3081
REMARK   3    T TENSOR
REMARK   3      T11:   1.1107 T22:   0.8686
REMARK   3      T33:   1.3164 T12:   0.0039
REMARK   3      T13:  -0.3548 T23:   0.4754
REMARK   3    L TENSOR
REMARK   3      L11:   6.6748 L22:   3.7717
REMARK   3      L33:   4.0545 L12:   3.7930
REMARK   3      L13:  -2.7207 L23:  -0.2835
REMARK   3    S TENSOR
REMARK   3      S11:   0.4201 S12:  -0.7754 S13:  -1.0630
REMARK   3      S21:   0.8339 S22:   0.1835 S23:  -0.5287
REMARK   3      S31:   0.1624 S32:  -0.4867 S33:  -0.5846
REMARK   3   TLS GROUP : 10
REMARK   3    SELECTION: CHAIN F AND (RESSEQ 79:85)
REMARK   3    ORIGIN FOR THE GROUP (A): -65.9387 -67.5989  -7.7824
REMARK   3    T TENSOR
REMARK   3      T11:   2.0491 T22:   0.8954
REMARK   3      T33:   2.7525 T12:   0.1801
REMARK   3      T13:   0.2715 T23:  -0.1439
REMARK   3    L TENSOR
REMARK   3      L11:   5.5202 L22:   6.3264
REMARK   3      L33:   4.0558 L12:   3.2468
REMARK   3      L13:  -0.0489 L23:   1.1608
REMARK   3    S TENSOR
REMARK   3      S11:  -2.1492 S12:   0.1273 S13:  -2.1309
REMARK   3      S21:  -2.7939 S22:  -1.3363 S23:   0.7991
REMARK   3      S31:   2.5760 S32:   0.9358 S33:   2.4591
REMARK   3   TLS GROUP : 11
REMARK   3    SELECTION: CHAIN F AND (RESSEQ 86:115)
REMARK   3    ORIGIN FOR THE GROUP (A): -42.9252 -49.9842  -6.1088
REMARK   3    T TENSOR
REMARK   3      T11:   0.8395 T22:   0.6019
REMARK   3      T33:   1.3496 T12:   0.1728
REMARK   3      T13:  -0.0582 T23:  -0.0359
REMARK   3    L TENSOR
REMARK   3      L11:   8.7859 L22:   8.9632
REMARK   3      L33:   5.8163 L12:   6.5678
REMARK   3      L13:  -3.2050 L23:  -1.3357
REMARK   3    S TENSOR
REMARK   3      S11:   0.0652 S12:   2.1190 S13:  -1.1769
REMARK   3      S21:   1.0654 S22:   0.8806 S23:  -0.4271
REMARK   3      S31:   0.0977 S32:   0.2377 S33:  -0.7721
REMARK   3   TLS GROUP : 12
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 415:525)
REMARK   3    ORIGIN FOR THE GROUP (A): -25.1929 -75.6708   7.2756
REMARK   3    T TENSOR
REMARK   3      T11:   1.2089 T22:   0.4514
REMARK   3      T33:   0.7713 T12:  -0.0207
REMARK   3      T13:  -0.3259 T23:   0.1235
REMARK   3    L TENSOR
REMARK   3      L11:   3.5395 L22:   4.3549
REMARK   3      L33:   4.6896 L12:   0.1299
REMARK   3      L13:  -3.3054 L23:   0.9397
REMARK   3    S TENSOR
REMARK   3      S11:  -0.4571 S12:  -0.6114 S13:  -0.5855
REMARK   3      S21:   0.1660 S22:   0.3473 S23:  -0.3848
REMARK   3      S31:   1.5290 S32:   0.0333 S33:  -0.0472
REMARK   3   TLS GROUP : 13
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 526:569)
REMARK   3    ORIGIN FOR THE GROUP (A): -21.4702 -65.8023  -5.9953
REMARK   3    T TENSOR
REMARK   3      T11:   0.9528 T22:   0.4564
REMARK   3      T33:   0.8938 T12:  -0.1612
REMARK   3      T13:  -0.1325 T23:  -0.0191
REMARK   3    L TENSOR
REMARK   3      L11:   2.8724 L22:   2.5252
REMARK   3      L33:   7.1654 L12:  -2.3963
REMARK   3      L13:  -0.3074 L23:   0.6060
REMARK   3    S TENSOR
REMARK   3      S11:   0.3671 S12:   1.1228 S13:  -0.1217
REMARK   3      S21:  -0.6495 S22:   0.1902 S23:  -0.5528
REMARK   3      S31:   0.5249 S32:   0.8066 S33:  -0.6855
REMARK   3   TLS GROUP : 14
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 415:525)
REMARK   3    ORIGIN FOR THE GROUP (A):  16.0964 -48.1453 -15.1763
REMARK   3    T TENSOR
REMARK   3      T11:   0.6193 T22:   1.6261
REMARK   3      T33:   1.1656 T12:   0.0090
REMARK   3      T13:   0.3093 T23:  -0.3212
REMARK   3    L TENSOR
REMARK   3      L11:   1.5798 L22:   6.8056
REMARK   3      L33:   7.0696 L12:   0.6983
REMARK   3      L13:   2.8558 L23:  -4.7884
REMARK   3    S TENSOR
REMARK   3      S11:   0.1305 S12:   0.0547 S13:   0.1345
REMARK   3      S21:  -1.6824 S22:  -0.1425 S23:  -0.9407
REMARK   3      S31:   0.1063 S32:   1.9752 S33:  -0.1525
REMARK   3   TLS GROUP : 15
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 526:569)
REMARK   3    ORIGIN FOR THE GROUP (A):   5.7994 -47.6632  -1.7952
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0894 T22:   1.3076
REMARK   3      T33:   1.1591 T12:  -0.4711
REMARK   3      T13:   0.0312 T23:  -0.6124
REMARK   3    L TENSOR
REMARK   3      L11:   1.7937 L22:   8.7197
REMARK   3      L33:   5.0871 L12:   0.1671
REMARK   3      L13:   2.4692 L23:   1.0492
REMARK   3    S TENSOR
REMARK   3      S11:   0.7359 S12:  -0.9065 S13:   1.1350
REMARK   3      S21:   0.5515 S22:  -0.9173 S23:   0.1863
REMARK   3      S31:   1.7971 S32:   2.0000 S33:   0.1192
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 3T1E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUL-11.
REMARK 100 THE RCSB ID CODE IS RCSB066914.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 16-DEC-07
REMARK 200  TEMPERATURE           (KELVIN) : 77.2
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 21-ID-D
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97850
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25027
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.301
REMARK 200  RESOLUTION RANGE LOW       (A) : 105.409
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9
REMARK 200  DATA REDUNDANCY                : 23.800
REMARK 200  R MERGE                    (I) : 0.09500
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
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   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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 4000, 200 MM LI2SO4, 100 MM N-
REMARK 280  (2-ACETAMIDO) IMINODIACETIC ACID (ADA), PH 6.5, VAPOR DIFFUSION,
REMARK 280  HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4
REMARK 290       7555   Y,X,-Z
REMARK 290       8555   -Y,-X,-Z+1/2
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       83.66900
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       69.14600
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       69.14600
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      125.50350
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       69.14600
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       69.14600
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       41.83450
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       69.14600
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       69.14600
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      125.50350
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       69.14600
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       69.14600
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       41.83450
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       83.66900
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 300 REMARK: ALTHOUGH 4 CHAINS (A, B, E, AND F) ARE PRESENT IN THE PDB
REMARK 300 FILE, THEY DO NOT REPRESENT 4 INDEPENDENT COPIES OF THE ENTIRE
REMARK 300 PROTEIN. INSTEAD, CHAINS E AND F ARE N-TERMINAL SEGMENTS OF CHAINS
REMARK 300 A AND B. THE MOST LIKELY CONNECTIVITY IS CHAINS E-A AND CHAINS F-B.
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 71730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -107.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, 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   BIOMT1   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  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     ALA A    34
REMARK 465     MET A    35
REMARK 465     ALA A    36
REMARK 465     HIS A    37
REMARK 465     HIS A    38
REMARK 465     HIS A    39
REMARK 465     HIS A    40
REMARK 465     HIS A    41
REMARK 465     HIS A    42
REMARK 465     LEU A    43
REMARK 465     VAL A    44
REMARK 465     PRO A    45
REMARK 465     ARG A    46
REMARK 465     GLY A    47
REMARK 465     SER A    48
REMARK 465     GLU A    49
REMARK 465     ALA A    50
REMARK 465     SER A    51
REMARK 465     THR A    52
REMARK 465     PRO A    53
REMARK 465     GLY A    54
REMARK 465     ASP A    55
REMARK 465     LEU A    56
REMARK 465     VAL A    57
REMARK 465     SER A    58
REMARK 465     ILE A    59
REMARK 465     PRO A    60
REMARK 465     THR A    61
REMARK 465     ALA A    62
REMARK 465     ILE A    63
REMARK 465     SER A    64
REMARK 465     ARG A    65
REMARK 465     ALA A    66
REMARK 465     GLU A    67
REMARK 465     GLY A    68
REMARK 465     LYS A    69
REMARK 465     ILE A    70
REMARK 465     THR A    71
REMARK 465     SER A    72
REMARK 465     ALA A    73
REMARK 465     LEU A    74
REMARK 465     GLY A    75
REMARK 465     SER A    76
REMARK 465     ASN A    77
REMARK 465     GLN A    78
REMARK 465     ASP A    79
REMARK 465     VAL A    80
REMARK 465     VAL A    81
REMARK 465     ASP A    82
REMARK 465     ARG A    83
REMARK 465     ILE A    84
REMARK 465     TYR A    85
REMARK 465     LYS A    86
REMARK 465     GLN A    87
REMARK 465     VAL A    88
REMARK 465     ALA A    89
REMARK 465     LEU A    90
REMARK 465     GLU A    91
REMARK 465     SER A    92
REMARK 465     PRO A    93
REMARK 465     LEU A    94
REMARK 465     ALA A    95
REMARK 465     LEU A    96
REMARK 465     LEU A    97
REMARK 465     ASN A    98
REMARK 465     THR A    99
REMARK 465     GLU A   100
REMARK 465     SER A   101
REMARK 465     ILE A   102
REMARK 465     ILE A   103
REMARK 465     MET A   104
REMARK 465     ASN A   105
REMARK 465     ALA A   106
REMARK 465     ILE A   107
REMARK 465     THR A   108
REMARK 465     SER A   109
REMARK 465     LEU A   110
REMARK 465     SER A   111
REMARK 465     TYR A   112
REMARK 465     GLN A   113
REMARK 465     ILE A   114
REMARK 465     ASN A   115
REMARK 465     GLY A   116
REMARK 465     ALA A   117
REMARK 465     ALA A   118
REMARK 465     ASN A   119
REMARK 465     ASN A   120
REMARK 465     SER A   121
REMARK 465     GLY A   122
REMARK 465     VAL A   570
REMARK 465     ALA B    34
REMARK 465     MET B    35
REMARK 465     ALA B    36
REMARK 465     HIS B    37
REMARK 465     HIS B    38
REMARK 465     HIS B    39
REMARK 465     HIS B    40
REMARK 465     HIS B    41
REMARK 465     HIS B    42
REMARK 465     LEU B    43
REMARK 465     VAL B    44
REMARK 465     PRO B    45
REMARK 465     ARG B    46
REMARK 465     GLY B    47
REMARK 465     SER B    48
REMARK 465     GLU B    49
REMARK 465     ALA B    50
REMARK 465     SER B    51
REMARK 465     THR B    52
REMARK 465     PRO B    53
REMARK 465     GLY B    54
REMARK 465     ASP B    55
REMARK 465     LEU B    56
REMARK 465     VAL B    57
REMARK 465     SER B    58
REMARK 465     ILE B    59
REMARK 465     PRO B    60
REMARK 465     THR B    61
REMARK 465     ALA B    62
REMARK 465     ILE B    63
REMARK 465     SER B    64
REMARK 465     ARG B    65
REMARK 465     ALA B    66
REMARK 465     GLU B    67
REMARK 465     GLY B    68
REMARK 465     LYS B    69
REMARK 465     ILE B    70
REMARK 465     THR B    71
REMARK 465     SER B    72
REMARK 465     ALA B    73
REMARK 465     LEU B    74
REMARK 465     GLY B    75
REMARK 465     SER B    76
REMARK 465     ASN B    77
REMARK 465     GLN B    78
REMARK 465     ASP B    79
REMARK 465     VAL B    80
REMARK 465     VAL B    81
REMARK 465     ASP B    82
REMARK 465     ARG B    83
REMARK 465     ILE B    84
REMARK 465     TYR B    85
REMARK 465     LYS B    86
REMARK 465     GLN B    87
REMARK 465     VAL B    88
REMARK 465     ALA B    89
REMARK 465     LEU B    90
REMARK 465     GLU B    91
REMARK 465     SER B    92
REMARK 465     PRO B    93
REMARK 465     LEU B    94
REMARK 465     ALA B    95
REMARK 465     LEU B    96
REMARK 465     LEU B    97
REMARK 465     ASN B    98
REMARK 465     THR B    99
REMARK 465     GLU B   100
REMARK 465     SER B   101
REMARK 465     ILE B   102
REMARK 465     ILE B   103
REMARK 465     MET B   104
REMARK 465     ASN B   105
REMARK 465     ALA B   106
REMARK 465     ILE B   107
REMARK 465     THR B   108
REMARK 465     SER B   109
REMARK 465     LEU B   110
REMARK 465     SER B   111
REMARK 465     TYR B   112
REMARK 465     GLN B   113
REMARK 465     ILE B   114
REMARK 465     ASN B   115
REMARK 465     GLY B   116
REMARK 465     ALA B   117
REMARK 465     ALA B   118
REMARK 465     ASN B   119
REMARK 465     ASN B   120
REMARK 465     SER B   121
REMARK 465     GLY B   122
REMARK 465     CYS B   123
REMARK 465     GLY B   124
REMARK 465     VAL B   570
REMARK 465     ALA E    34
REMARK 465     MET E    35
REMARK 465     ALA E    36
REMARK 465     HIS E    37
REMARK 465     HIS E    38
REMARK 465     HIS E    39
REMARK 465     HIS E    40
REMARK 465     HIS E    41
REMARK 465     HIS E    42
REMARK 465     LEU E    43
REMARK 465     VAL E    44
REMARK 465     PRO E    45
REMARK 465     ARG E    46
REMARK 465     GLY E    47
REMARK 465     SER E    48
REMARK 465     GLU E    49
REMARK 465     ALA E    50
REMARK 465     SER E    51
REMARK 465     THR E    52
REMARK 465     PRO E    53
REMARK 465     GLY E    54
REMARK 465     ASP E    55
REMARK 465     LEU E    56
REMARK 465     VAL E    57
REMARK 465     SER E    58
REMARK 465     ILE E    59
REMARK 465     PRO E    60
REMARK 465     THR E    61
REMARK 465     ALA E    62
REMARK 465     ILE E    63
REMARK 465     SER E    64
REMARK 465     ARG E    65
REMARK 465     ALA E    66
REMARK 465     GLU E    67
REMARK 465     GLY E    68
REMARK 465     LYS E    69
REMARK 465     ILE E    70
REMARK 465     THR E    71
REMARK 465     SER E    72
REMARK 465     ALA E    73
REMARK 465     LEU E    74
REMARK 465     GLY E    75
REMARK 465     SER E    76
REMARK 465     ASN E    77
REMARK 465     GLN E    78
REMARK 465     GLY E   116
REMARK 465     ALA E   117
REMARK 465     ALA E   118
REMARK 465     ASN E   119
REMARK 465     ASN E   120
REMARK 465     SER E   121
REMARK 465     GLY E   122
REMARK 465     CYS E   123
REMARK 465     GLY E   124
REMARK 465     ALA E   125
REMARK 465     PRO E   126
REMARK 465     VAL E   127
REMARK 465     HIS E   128
REMARK 465     ASP E   129
REMARK 465     PRO E   130
REMARK 465     ASP E   131
REMARK 465     TYR E   132
REMARK 465     ILE E   133
REMARK 465     GLY E   134
REMARK 465     GLY E   135
REMARK 465     ILE E   136
REMARK 465     GLY E   137
REMARK 465     LYS E   138
REMARK 465     GLU E   139
REMARK 465     LEU E   140
REMARK 465     ILE E   141
REMARK 465     VAL E   142
REMARK 465     ASP E   143
REMARK 465     ASP E   144
REMARK 465     THR E   145
REMARK 465     SER E   146
REMARK 465     ASP E   147
REMARK 465     VAL E   148
REMARK 465     THR E   149
REMARK 465     SER E   150
REMARK 465     PHE E   151
REMARK 465     TYR E   152
REMARK 465     PRO E   153
REMARK 465     SER E   154
REMARK 465     ALA E   155
REMARK 465     PHE E   156
REMARK 465     GLN E   157
REMARK 465     GLU E   158
REMARK 465     HIS E   159
REMARK 465     LEU E   160
REMARK 465     ASN E   161
REMARK 465     PHE E   162
REMARK 465     ILE E   163
REMARK 465     PRO E   164
REMARK 465     ALA E   165
REMARK 465     PRO E   166
REMARK 465     THR E   167
REMARK 465     THR E   168
REMARK 465     GLY E   169
REMARK 465     SER E   170
REMARK 465     GLY E   171
REMARK 465     CYS E   172
REMARK 465     THR E   173
REMARK 465     ARG E   174
REMARK 465     ILE E   175
REMARK 465     PRO E   176
REMARK 465     SER E   177
REMARK 465     PHE E   178
REMARK 465     ASP E   179
REMARK 465     MET E   180
REMARK 465     SER E   181
REMARK 465     ALA E   182
REMARK 465     THR E   183
REMARK 465     HIS E   184
REMARK 465     CYS E   185
REMARK 465     TYR E   186
REMARK 465     THR E   187
REMARK 465     HIS E   188
REMARK 465     ASN E   189
REMARK 465     VAL E   190
REMARK 465     ILE E   191
REMARK 465     PHE E   192
REMARK 465     SER E   193
REMARK 465     GLY E   194
REMARK 465     CYS E   195
REMARK 465     ARG E   196
REMARK 465     ASP E   197
REMARK 465     HIS E   198
REMARK 465     SER E   199
REMARK 465     HIS E   200
REMARK 465     SER E   201
REMARK 465     HIS E   202
REMARK 465     GLN E   203
REMARK 465     TYR E   204
REMARK 465     LEU E   205
REMARK 465     ALA E   206
REMARK 465     LEU E   207
REMARK 465     GLY E   208
REMARK 465     VAL E   209
REMARK 465     LEU E   210
REMARK 465     ARG E   211
REMARK 465     THR E   212
REMARK 465     SER E   213
REMARK 465     ALA E   214
REMARK 465     THR E   215
REMARK 465     GLY E   216
REMARK 465     ARG E   217
REMARK 465     VAL E   218
REMARK 465     PHE E   219
REMARK 465     PHE E   220
REMARK 465     SER E   221
REMARK 465     THR E   222
REMARK 465     LEU E   223
REMARK 465     ARG E   224
REMARK 465     SER E   225
REMARK 465     ILE E   226
REMARK 465     ASN E   227
REMARK 465     LEU E   228
REMARK 465     ASP E   229
REMARK 465     ASP E   230
REMARK 465     THR E   231
REMARK 465     GLN E   232
REMARK 465     ASN E   233
REMARK 465     ARG E   234
REMARK 465     LYS E   235
REMARK 465     SER E   236
REMARK 465     CYS E   237
REMARK 465     SER E   238
REMARK 465     VAL E   239
REMARK 465     SER E   240
REMARK 465     ALA E   241
REMARK 465     THR E   242
REMARK 465     PRO E   243
REMARK 465     LEU E   244
REMARK 465     GLY E   245
REMARK 465     CYS E   246
REMARK 465     ASP E   247
REMARK 465     MET E   248
REMARK 465     LEU E   249
REMARK 465     CYS E   250
REMARK 465     SER E   251
REMARK 465     LYS E   252
REMARK 465     VAL E   253
REMARK 465     THR E   254
REMARK 465     GLU E   255
REMARK 465     THR E   256
REMARK 465     GLU E   257
REMARK 465     GLU E   258
REMARK 465     GLU E   259
REMARK 465     ASP E   260
REMARK 465     TYR E   261
REMARK 465     ASN E   262
REMARK 465     SER E   263
REMARK 465     VAL E   264
REMARK 465     ILE E   265
REMARK 465     PRO E   266
REMARK 465     THR E   267
REMARK 465     SER E   268
REMARK 465     MET E   269
REMARK 465     VAL E   270
REMARK 465     HIS E   271
REMARK 465     GLY E   272
REMARK 465     ARG E   273
REMARK 465     LEU E   274
REMARK 465     GLY E   275
REMARK 465     PHE E   276
REMARK 465     ASP E   277
REMARK 465     GLY E   278
REMARK 465     GLN E   279
REMARK 465     TYR E   280
REMARK 465     HIS E   281
REMARK 465     GLU E   282
REMARK 465     LYS E   283
REMARK 465     ASP E   284
REMARK 465     LEU E   285
REMARK 465     ASP E   286
REMARK 465     VAL E   287
REMARK 465     THR E   288
REMARK 465     THR E   289
REMARK 465     LEU E   290
REMARK 465     PHE E   291
REMARK 465     GLY E   292
REMARK 465     ASP E   293
REMARK 465     TRP E   294
REMARK 465     VAL E   295
REMARK 465     ALA E   296
REMARK 465     ASN E   297
REMARK 465     TYR E   298
REMARK 465     PRO E   299
REMARK 465     GLY E   300
REMARK 465     VAL E   301
REMARK 465     GLY E   302
REMARK 465     GLY E   303
REMARK 465     GLY E   304
REMARK 465     SER E   305
REMARK 465     PHE E   306
REMARK 465     ILE E   307
REMARK 465     ASP E   308
REMARK 465     ASN E   309
REMARK 465     ARG E   310
REMARK 465     VAL E   311
REMARK 465     TRP E   312
REMARK 465     PHE E   313
REMARK 465     PRO E   314
REMARK 465     VAL E   315
REMARK 465     TYR E   316
REMARK 465     GLY E   317
REMARK 465     GLY E   318
REMARK 465     LEU E   319
REMARK 465     LYS E   320
REMARK 465     PRO E   321
REMARK 465     SER E   322
REMARK 465     SER E   323
REMARK 465     PRO E   324
REMARK 465     SER E   325
REMARK 465     ASP E   326
REMARK 465     THR E   327
REMARK 465     ALA E   328
REMARK 465     GLN E   329
REMARK 465     GLU E   330
REMARK 465     GLY E   331
REMARK 465     ARG E   332
REMARK 465     TYR E   333
REMARK 465     VAL E   334
REMARK 465     ILE E   335
REMARK 465     TYR E   336
REMARK 465     LYS E   337
REMARK 465     ARG E   338
REMARK 465     TYR E   339
REMARK 465     ASN E   340
REMARK 465     ASP E   341
REMARK 465     THR E   342
REMARK 465     CYS E   343
REMARK 465     PRO E   344
REMARK 465     ASP E   345
REMARK 465     GLU E   346
REMARK 465     GLN E   347
REMARK 465     ASP E   348
REMARK 465     TYR E   349
REMARK 465     GLN E   350
REMARK 465     ILE E   351
REMARK 465     ARG E   352
REMARK 465     MET E   353
REMARK 465     ALA E   354
REMARK 465     LYS E   355
REMARK 465     SER E   356
REMARK 465     SER E   357
REMARK 465     TYR E   358
REMARK 465     LYS E   359
REMARK 465     PRO E   360
REMARK 465     GLY E   361
REMARK 465     ARG E   362
REMARK 465     PHE E   363
REMARK 465     GLY E   364
REMARK 465     GLY E   365
REMARK 465     LYS E   366
REMARK 465     ARG E   367
REMARK 465     VAL E   368
REMARK 465     GLN E   369
REMARK 465     GLN E   370
REMARK 465     ALA E   371
REMARK 465     ILE E   372
REMARK 465     LEU E   373
REMARK 465     SER E   374
REMARK 465     ILE E   375
REMARK 465     LYS E   376
REMARK 465     VAL E   377
REMARK 465     SER E   378
REMARK 465     THR E   379
REMARK 465     SER E   380
REMARK 465     LEU E   381
REMARK 465     GLY E   382
REMARK 465     GLU E   383
REMARK 465     ASP E   384
REMARK 465     PRO E   385
REMARK 465     VAL E   386
REMARK 465     LEU E   387
REMARK 465     THR E   388
REMARK 465     ILE E   389
REMARK 465     PRO E   390
REMARK 465     PRO E   391
REMARK 465     ASN E   392
REMARK 465     THR E   393
REMARK 465     VAL E   394
REMARK 465     THR E   395
REMARK 465     LEU E   396
REMARK 465     MET E   397
REMARK 465     GLY E   398
REMARK 465     ALA E   399
REMARK 465     GLU E   400
REMARK 465     GLY E   401
REMARK 465     ARG E   402
REMARK 465     VAL E   403
REMARK 465     LEU E   404
REMARK 465     THR E   405
REMARK 465     VAL E   406
REMARK 465     GLY E   407
REMARK 465     THR E   408
REMARK 465     SER E   409
REMARK 465     HIS E   410
REMARK 465     PHE E   411
REMARK 465     LEU E   412
REMARK 465     TYR E   413
REMARK 465     GLN E   414
REMARK 465     ARG E   415
REMARK 465     GLY E   416
REMARK 465     SER E   417
REMARK 465     SER E   418
REMARK 465     TYR E   419
REMARK 465     PHE E   420
REMARK 465     SER E   421
REMARK 465     PRO E   422
REMARK 465     ALA E   423
REMARK 465     LEU E   424
REMARK 465     LEU E   425
REMARK 465     TYR E   426
REMARK 465     PRO E   427
REMARK 465     MET E   428
REMARK 465     THR E   429
REMARK 465     VAL E   430
REMARK 465     ASN E   431
REMARK 465     ASN E   432
REMARK 465     ASN E   433
REMARK 465     THR E   434
REMARK 465     ALA E   435
REMARK 465     THR E   436
REMARK 465     LEU E   437
REMARK 465     HIS E   438
REMARK 465     SER E   439
REMARK 465     PRO E   440
REMARK 465     TYR E   441
REMARK 465     THR E   442
REMARK 465     PHE E   443
REMARK 465     ASN E   444
REMARK 465     ALA E   445
REMARK 465     PHE E   446
REMARK 465     THR E   447
REMARK 465     ARG E   448
REMARK 465     PRO E   449
REMARK 465     GLY E   450
REMARK 465     SER E   451
REMARK 465     VAL E   452
REMARK 465     PRO E   453
REMARK 465     CYS E   454
REMARK 465     GLN E   455
REMARK 465     ALA E   456
REMARK 465     SER E   457
REMARK 465     ALA E   458
REMARK 465     ARG E   459
REMARK 465     CYS E   460
REMARK 465     PRO E   461
REMARK 465     ASN E   462
REMARK 465     SER E   463
REMARK 465     CYS E   464
REMARK 465     VAL E   465
REMARK 465     THR E   466
REMARK 465     GLY E   467
REMARK 465     VAL E   468
REMARK 465     TYR E   469
REMARK 465     THR E   470
REMARK 465     ASP E   471
REMARK 465     PRO E   472
REMARK 465     TYR E   473
REMARK 465     PRO E   474
REMARK 465     LEU E   475
REMARK 465     VAL E   476
REMARK 465     PHE E   477
REMARK 465     HIS E   478
REMARK 465     ARG E   479
REMARK 465     ASN E   480
REMARK 465     HIS E   481
REMARK 465     THR E   482
REMARK 465     LEU E   483
REMARK 465     ARG E   484
REMARK 465     GLY E   485
REMARK 465     VAL E   486
REMARK 465     PHE E   487
REMARK 465     GLY E   488
REMARK 465     THR E   489
REMARK 465     MET E   490
REMARK 465     LEU E   491
REMARK 465     ASP E   492
REMARK 465     ASP E   493
REMARK 465     GLU E   494
REMARK 465     GLN E   495
REMARK 465     ALA E   496
REMARK 465     ARG E   497
REMARK 465     LEU E   498
REMARK 465     ASN E   499
REMARK 465     LEU E   500
REMARK 465     VAL E   501
REMARK 465     SER E   502
REMARK 465     ALA E   503
REMARK 465     VAL E   504
REMARK 465     PHE E   505
REMARK 465     ASP E   506
REMARK 465     ASN E   507
REMARK 465     ILE E   508
REMARK 465     SER E   509
REMARK 465     ARG E   510
REMARK 465     SER E   511
REMARK 465     ARG E   512
REMARK 465     ILE E   513
REMARK 465     THR E   514
REMARK 465     ARG E   515
REMARK 465     VAL E   516
REMARK 465     SER E   517
REMARK 465     SER E   518
REMARK 465     SER E   519
REMARK 465     ARG E   520
REMARK 465     THR E   521
REMARK 465     LYS E   522
REMARK 465     ALA E   523
REMARK 465     ALA E   524
REMARK 465     TYR E   525
REMARK 465     THR E   526
REMARK 465     THR E   527
REMARK 465     SER E   528
REMARK 465     THR E   529
REMARK 465     CYS E   530
REMARK 465     PHE E   531
REMARK 465     LYS E   532
REMARK 465     VAL E   533
REMARK 465     VAL E   534
REMARK 465     LYS E   535
REMARK 465     THR E   536
REMARK 465     ASN E   537
REMARK 465     LYS E   538
REMARK 465     THR E   539
REMARK 465     TYR E   540
REMARK 465     CYS E   541
REMARK 465     LEU E   542
REMARK 465     SER E   543
REMARK 465     ILE E   544
REMARK 465     ALA E   545
REMARK 465     GLU E   546
REMARK 465     ILE E   547
REMARK 465     SER E   548
REMARK 465     ASN E   549
REMARK 465     THR E   550
REMARK 465     LEU E   551
REMARK 465     PHE E   552
REMARK 465     GLY E   553
REMARK 465     GLU E   554
REMARK 465     PHE E   555
REMARK 465     ARG E   556
REMARK 465     ILE E   557
REMARK 465     VAL E   558
REMARK 465     PRO E   559
REMARK 465     LEU E   560
REMARK 465     LEU E   561
REMARK 465     VAL E   562
REMARK 465     GLU E   563
REMARK 465     ILE E   564
REMARK 465     LEU E   565
REMARK 465     LYS E   566
REMARK 465     ASP E   567
REMARK 465     ASP E   568
REMARK 465     GLY E   569
REMARK 465     VAL E   570
REMARK 465     ALA F    34
REMARK 465     MET F    35
REMARK 465     ALA F    36
REMARK 465     HIS F    37
REMARK 465     HIS F    38
REMARK 465     HIS F    39
REMARK 465     HIS F    40
REMARK 465     HIS F    41
REMARK 465     HIS F    42
REMARK 465     LEU F    43
REMARK 465     VAL F    44
REMARK 465     PRO F    45
REMARK 465     ARG F    46
REMARK 465     GLY F    47
REMARK 465     SER F    48
REMARK 465     GLU F    49
REMARK 465     ALA F    50
REMARK 465     SER F    51
REMARK 465     THR F    52
REMARK 465     PRO F    53
REMARK 465     GLY F    54
REMARK 465     ASP F    55
REMARK 465     LEU F    56
REMARK 465     VAL F    57
REMARK 465     SER F    58
REMARK 465     ILE F    59
REMARK 465     PRO F    60
REMARK 465     THR F    61
REMARK 465     ALA F    62
REMARK 465     ILE F    63
REMARK 465     SER F    64
REMARK 465     ARG F    65
REMARK 465     ALA F    66
REMARK 465     GLU F    67
REMARK 465     GLY F    68
REMARK 465     LYS F    69
REMARK 465     ILE F    70
REMARK 465     THR F    71
REMARK 465     SER F    72
REMARK 465     ALA F    73
REMARK 465     LEU F    74
REMARK 465     GLY F    75
REMARK 465     SER F    76
REMARK 465     ASN F    77
REMARK 465     GLN F    78
REMARK 465     GLY F   116
REMARK 465     ALA F   117
REMARK 465     ALA F   118
REMARK 465     ASN F   119
REMARK 465     ASN F   120
REMARK 465     SER F   121
REMARK 465     GLY F   122
REMARK 465     CYS F   123
REMARK 465     GLY F   124
REMARK 465     ALA F   125
REMARK 465     PRO F   126
REMARK 465     VAL F   127
REMARK 465     HIS F   128
REMARK 465     ASP F   129
REMARK 465     PRO F   130
REMARK 465     ASP F   131
REMARK 465     TYR F   132
REMARK 465     ILE F   133
REMARK 465     GLY F   134
REMARK 465     GLY F   135
REMARK 465     ILE F   136
REMARK 465     GLY F   137
REMARK 465     LYS F   138
REMARK 465     GLU F   139
REMARK 465     LEU F   140
REMARK 465     ILE F   141
REMARK 465     VAL F   142
REMARK 465     ASP F   143
REMARK 465     ASP F   144
REMARK 465     THR F   145
REMARK 465     SER F   146
REMARK 465     ASP F   147
REMARK 465     VAL F   148
REMARK 465     THR F   149
REMARK 465     SER F   150
REMARK 465     PHE F   151
REMARK 465     TYR F   152
REMARK 465     PRO F   153
REMARK 465     SER F   154
REMARK 465     ALA F   155
REMARK 465     PHE F   156
REMARK 465     GLN F   157
REMARK 465     GLU F   158
REMARK 465     HIS F   159
REMARK 465     LEU F   160
REMARK 465     ASN F   161
REMARK 465     PHE F   162
REMARK 465     ILE F   163
REMARK 465     PRO F   164
REMARK 465     ALA F   165
REMARK 465     PRO F   166
REMARK 465     THR F   167
REMARK 465     THR F   168
REMARK 465     GLY F   169
REMARK 465     SER F   170
REMARK 465     GLY F   171
REMARK 465     CYS F   172
REMARK 465     THR F   173
REMARK 465     ARG F   174
REMARK 465     ILE F   175
REMARK 465     PRO F   176
REMARK 465     SER F   177
REMARK 465     PHE F   178
REMARK 465     ASP F   179
REMARK 465     MET F   180
REMARK 465     SER F   181
REMARK 465     ALA F   182
REMARK 465     THR F   183
REMARK 465     HIS F   184
REMARK 465     CYS F   185
REMARK 465     TYR F   186
REMARK 465     THR F   187
REMARK 465     HIS F   188
REMARK 465     ASN F   189
REMARK 465     VAL F   190
REMARK 465     ILE F   191
REMARK 465     PHE F   192
REMARK 465     SER F   193
REMARK 465     GLY F   194
REMARK 465     CYS F   195
REMARK 465     ARG F   196
REMARK 465     ASP F   197
REMARK 465     HIS F   198
REMARK 465     SER F   199
REMARK 465     HIS F   200
REMARK 465     SER F   201
REMARK 465     HIS F   202
REMARK 465     GLN F   203
REMARK 465     TYR F   204
REMARK 465     LEU F   205
REMARK 465     ALA F   206
REMARK 465     LEU F   207
REMARK 465     GLY F   208
REMARK 465     VAL F   209
REMARK 465     LEU F   210
REMARK 465     ARG F   211
REMARK 465     THR F   212
REMARK 465     SER F   213
REMARK 465     ALA F   214
REMARK 465     THR F   215
REMARK 465     GLY F   216
REMARK 465     ARG F   217
REMARK 465     VAL F   218
REMARK 465     PHE F   219
REMARK 465     PHE F   220
REMARK 465     SER F   221
REMARK 465     THR F   222
REMARK 465     LEU F   223
REMARK 465     ARG F   224
REMARK 465     SER F   225
REMARK 465     ILE F   226
REMARK 465     ASN F   227
REMARK 465     LEU F   228
REMARK 465     ASP F   229
REMARK 465     ASP F   230
REMARK 465     THR F   231
REMARK 465     GLN F   232
REMARK 465     ASN F   233
REMARK 465     ARG F   234
REMARK 465     LYS F   235
REMARK 465     SER F   236
REMARK 465     CYS F   237
REMARK 465     SER F   238
REMARK 465     VAL F   239
REMARK 465     SER F   240
REMARK 465     ALA F   241
REMARK 465     THR F   242
REMARK 465     PRO F   243
REMARK 465     LEU F   244
REMARK 465     GLY F   245
REMARK 465     CYS F   246
REMARK 465     ASP F   247
REMARK 465     MET F   248
REMARK 465     LEU F   249
REMARK 465     CYS F   250
REMARK 465     SER F   251
REMARK 465     LYS F   252
REMARK 465     VAL F   253
REMARK 465     THR F   254
REMARK 465     GLU F   255
REMARK 465     THR F   256
REMARK 465     GLU F   257
REMARK 465     GLU F   258
REMARK 465     GLU F   259
REMARK 465     ASP F   260
REMARK 465     TYR F   261
REMARK 465     ASN F   262
REMARK 465     SER F   263
REMARK 465     VAL F   264
REMARK 465     ILE F   265
REMARK 465     PRO F   266
REMARK 465     THR F   267
REMARK 465     SER F   268
REMARK 465     MET F   269
REMARK 465     VAL F   270
REMARK 465     HIS F   271
REMARK 465     GLY F   272
REMARK 465     ARG F   273
REMARK 465     LEU F   274
REMARK 465     GLY F   275
REMARK 465     PHE F   276
REMARK 465     ASP F   277
REMARK 465     GLY F   278
REMARK 465     GLN F   279
REMARK 465     TYR F   280
REMARK 465     HIS F   281
REMARK 465     GLU F   282
REMARK 465     LYS F   283
REMARK 465     ASP F   284
REMARK 465     LEU F   285
REMARK 465     ASP F   286
REMARK 465     VAL F   287
REMARK 465     THR F   288
REMARK 465     THR F   289
REMARK 465     LEU F   290
REMARK 465     PHE F   291
REMARK 465     GLY F   292
REMARK 465     ASP F   293
REMARK 465     TRP F   294
REMARK 465     VAL F   295
REMARK 465     ALA F   296
REMARK 465     ASN F   297
REMARK 465     TYR F   298
REMARK 465     PRO F   299
REMARK 465     GLY F   300
REMARK 465     VAL F   301
REMARK 465     GLY F   302
REMARK 465     GLY F   303
REMARK 465     GLY F   304
REMARK 465     SER F   305
REMARK 465     PHE F   306
REMARK 465     ILE F   307
REMARK 465     ASP F   308
REMARK 465     ASN F   309
REMARK 465     ARG F   310
REMARK 465     VAL F   311
REMARK 465     TRP F   312
REMARK 465     PHE F   313
REMARK 465     PRO F   314
REMARK 465     VAL F   315
REMARK 465     TYR F   316
REMARK 465     GLY F   317
REMARK 465     GLY F   318
REMARK 465     LEU F   319
REMARK 465     LYS F   320
REMARK 465     PRO F   321
REMARK 465     SER F   322
REMARK 465     SER F   323
REMARK 465     PRO F   324
REMARK 465     SER F   325
REMARK 465     ASP F   326
REMARK 465     THR F   327
REMARK 465     ALA F   328
REMARK 465     GLN F   329
REMARK 465     GLU F   330
REMARK 465     GLY F   331
REMARK 465     ARG F   332
REMARK 465     TYR F   333
REMARK 465     VAL F   334
REMARK 465     ILE F   335
REMARK 465     TYR F   336
REMARK 465     LYS F   337
REMARK 465     ARG F   338
REMARK 465     TYR F   339
REMARK 465     ASN F   340
REMARK 465     ASP F   341
REMARK 465     THR F   342
REMARK 465     CYS F   343
REMARK 465     PRO F   344
REMARK 465     ASP F   345
REMARK 465     GLU F   346
REMARK 465     GLN F   347
REMARK 465     ASP F   348
REMARK 465     TYR F   349
REMARK 465     GLN F   350
REMARK 465     ILE F   351
REMARK 465     ARG F   352
REMARK 465     MET F   353
REMARK 465     ALA F   354
REMARK 465     LYS F   355
REMARK 465     SER F   356
REMARK 465     SER F   357
REMARK 465     TYR F   358
REMARK 465     LYS F   359
REMARK 465     PRO F   360
REMARK 465     GLY F   361
REMARK 465     ARG F   362
REMARK 465     PHE F   363
REMARK 465     GLY F   364
REMARK 465     GLY F   365
REMARK 465     LYS F   366
REMARK 465     ARG F   367
REMARK 465     VAL F   368
REMARK 465     GLN F   369
REMARK 465     GLN F   370
REMARK 465     ALA F   371
REMARK 465     ILE F   372
REMARK 465     LEU F   373
REMARK 465     SER F   374
REMARK 465     ILE F   375
REMARK 465     LYS F   376
REMARK 465     VAL F   377
REMARK 465     SER F   378
REMARK 465     THR F   379
REMARK 465     SER F   380
REMARK 465     LEU F   381
REMARK 465     GLY F   382
REMARK 465     GLU F   383
REMARK 465     ASP F   384
REMARK 465     PRO F   385
REMARK 465     VAL F   386
REMARK 465     LEU F   387
REMARK 465     THR F   388
REMARK 465     ILE F   389
REMARK 465     PRO F   390
REMARK 465     PRO F   391
REMARK 465     ASN F   392
REMARK 465     THR F   393
REMARK 465     VAL F   394
REMARK 465     THR F   395
REMARK 465     LEU F   396
REMARK 465     MET F   397
REMARK 465     GLY F   398
REMARK 465     ALA F   399
REMARK 465     GLU F   400
REMARK 465     GLY F   401
REMARK 465     ARG F   402
REMARK 465     VAL F   403
REMARK 465     LEU F   404
REMARK 465     THR F   405
REMARK 465     VAL F   406
REMARK 465     GLY F   407
REMARK 465     THR F   408
REMARK 465     SER F   409
REMARK 465     HIS F   410
REMARK 465     PHE F   411
REMARK 465     LEU F   412
REMARK 465     TYR F   413
REMARK 465     GLN F   414
REMARK 465     ARG F   415
REMARK 465     GLY F   416
REMARK 465     SER F   417
REMARK 465     SER F   418
REMARK 465     TYR F   419
REMARK 465     PHE F   420
REMARK 465     SER F   421
REMARK 465     PRO F   422
REMARK 465     ALA F   423
REMARK 465     LEU F   424
REMARK 465     LEU F   425
REMARK 465     TYR F   426
REMARK 465     PRO F   427
REMARK 465     MET F   428
REMARK 465     THR F   429
REMARK 465     VAL F   430
REMARK 465     ASN F   431
REMARK 465     ASN F   432
REMARK 465     ASN F   433
REMARK 465     THR F   434
REMARK 465     ALA F   435
REMARK 465     THR F   436
REMARK 465     LEU F   437
REMARK 465     HIS F   438
REMARK 465     SER F   439
REMARK 465     PRO F   440
REMARK 465     TYR F   441
REMARK 465     THR F   442
REMARK 465     PHE F   443
REMARK 465     ASN F   444
REMARK 465     ALA F   445
REMARK 465     PHE F   446
REMARK 465     THR F   447
REMARK 465     ARG F   448
REMARK 465     PRO F   449
REMARK 465     GLY F   450
REMARK 465     SER F   451
REMARK 465     VAL F   452
REMARK 465     PRO F   453
REMARK 465     CYS F   454
REMARK 465     GLN F   455
REMARK 465     ALA F   456
REMARK 465     SER F   457
REMARK 465     ALA F   458
REMARK 465     ARG F   459
REMARK 465     CYS F   460
REMARK 465     PRO F   461
REMARK 465     ASN F   462
REMARK 465     SER F   463
REMARK 465     CYS F   464
REMARK 465     VAL F   465
REMARK 465     THR F   466
REMARK 465     GLY F   467
REMARK 465     VAL F   468
REMARK 465     TYR F   469
REMARK 465     THR F   470
REMARK 465     ASP F   471
REMARK 465     PRO F   472
REMARK 465     TYR F   473
REMARK 465     PRO F   474
REMARK 465     LEU F   475
REMARK 465     VAL F   476
REMARK 465     PHE F   477
REMARK 465     HIS F   478
REMARK 465     ARG F   479
REMARK 465     ASN F   480
REMARK 465     HIS F   481
REMARK 465     THR F   482
REMARK 465     LEU F   483
REMARK 465     ARG F   484
REMARK 465     GLY F   485
REMARK 465     VAL F   486
REMARK 465     PHE F   487
REMARK 465     GLY F   488
REMARK 465     THR F   489
REMARK 465     MET F   490
REMARK 465     LEU F   491
REMARK 465     ASP F   492
REMARK 465     ASP F   493
REMARK 465     GLU F   494
REMARK 465     GLN F   495
REMARK 465     ALA F   496
REMARK 465     ARG F   497
REMARK 465     LEU F   498
REMARK 465     ASN F   499
REMARK 465     LEU F   500
REMARK 465     VAL F   501
REMARK 465     SER F   502
REMARK 465     ALA F   503
REMARK 465     VAL F   504
REMARK 465     PHE F   505
REMARK 465     ASP F   506
REMARK 465     ASN F   507
REMARK 465     ILE F   508
REMARK 465     SER F   509
REMARK 465     ARG F   510
REMARK 465     SER F   511
REMARK 465     ARG F   512
REMARK 465     ILE F   513
REMARK 465     THR F   514
REMARK 465     ARG F   515
REMARK 465     VAL F   516
REMARK 465     SER F   517
REMARK 465     SER F   518
REMARK 465     SER F   519
REMARK 465     ARG F   520
REMARK 465     THR F   521
REMARK 465     LYS F   522
REMARK 465     ALA F   523
REMARK 465     ALA F   524
REMARK 465     TYR F   525
REMARK 465     THR F   526
REMARK 465     THR F   527
REMARK 465     SER F   528
REMARK 465     THR F   529
REMARK 465     CYS F   530
REMARK 465     PHE F   531
REMARK 465     LYS F   532
REMARK 465     VAL F   533
REMARK 465     VAL F   534
REMARK 465     LYS F   535
REMARK 465     THR F   536
REMARK 465     ASN F   537
REMARK 465     LYS F   538
REMARK 465     THR F   539
REMARK 465     TYR F   540
REMARK 465     CYS F   541
REMARK 465     LEU F   542
REMARK 465     SER F   543
REMARK 465     ILE F   544
REMARK 465     ALA F   545
REMARK 465     GLU F   546
REMARK 465     ILE F   547
REMARK 465     SER F   548
REMARK 465     ASN F   549
REMARK 465     THR F   550
REMARK 465     LEU F   551
REMARK 465     PHE F   552
REMARK 465     GLY F   553
REMARK 465     GLU F   554
REMARK 465     PHE F   555
REMARK 465     ARG F   556
REMARK 465     ILE F   557
REMARK 465     VAL F   558
REMARK 465     PRO F   559
REMARK 465     LEU F   560
REMARK 465     LEU F   561
REMARK 465     VAL F   562
REMARK 465     GLU F   563
REMARK 465     ILE F   564
REMARK 465     LEU F   565
REMARK 465     LYS F   566
REMARK 465     ASP F   567
REMARK 465     ASP F   568
REMARK 465     GLY F   569
REMARK 465     VAL F   570
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     ILE A 133    CG1  CG2  CD1
REMARK 470     ILE A 136    CG1  CG2  CD1
REMARK 470     ILE A 141    CG1  CG2  CD1
REMARK 470     ASP A 143    CG   OD1  OD2
REMARK 470     THR A 145    OG1  CG2
REMARK 470     ILE A 163    CG1  CG2  CD1
REMARK 470     ILE A 175    CG1  CG2  CD1
REMARK 470     ARG A 196    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ASP A 197    CG   OD1  OD2
REMARK 470     LEU A 205    CG   CD1  CD2
REMARK 470     LEU A 223    CG   CD1  CD2
REMARK 470     SER A 225    OG
REMARK 470     LYS A 235    CG   CD   CE   NZ
REMARK 470     VAL A 239    CG1  CG2
REMARK 470     SER A 240    OG
REMARK 470     LEU A 244    CG   CD1  CD2
REMARK 470     VAL A 253    CG1  CG2
REMARK 470     THR A 254    OG1  CG2
REMARK 470     GLU A 258    CG   CD   OE1  OE2
REMARK 470     VAL A 264    CG1  CG2
REMARK 470     ILE A 265    CG1  CG2  CD1
REMARK 470     VAL A 270    CG1  CG2
REMARK 470     LYS A 283    CG   CD   CE   NZ
REMARK 470     VAL A 287    CG1  CG2
REMARK 470     VAL A 295    CG1  CG2
REMARK 470     ASN A 297    CG   OD1  ND2
REMARK 470     VAL A 301    CG1  CG2
REMARK 470     ILE A 307    CG1  CG2  CD1
REMARK 470     ASN A 309    CG   OD1  ND2
REMARK 470     VAL A 311    CG1  CG2
REMARK 470     VAL A 315    CG1  CG2
REMARK 470     LYS A 320    CG   CD   CE   NZ
REMARK 470     VAL A 334    CG1  CG2
REMARK 470     ILE A 335    CG1  CG2  CD1
REMARK 470     LYS A 337    CG   CD   CE   NZ
REMARK 470     ASP A 341    CG   OD1  OD2
REMARK 470     ILE A 351    CG1  CG2  CD1
REMARK 470     ARG A 352    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A 355    CG   CD   CE   NZ
REMARK 470     LYS A 359    CG   CD   CE   NZ
REMARK 470     ARG A 362    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A 366    CG   CD   CE   NZ
REMARK 470     ARG A 367    CG   CD   NE   CZ   NH1  NH2
REMARK 470     VAL A 368    CG1  CG2
REMARK 470     GLN A 369    CG   CD   OE1  NE2
REMARK 470     GLN A 370    CG   CD   OE1  NE2
REMARK 470     ILE A 372    CG1  CG2  CD1
REMARK 470     LEU A 373    CG   CD1  CD2
REMARK 470     ILE A 375    CG1  CG2  CD1
REMARK 470     LYS A 376    CG   CD   CE   NZ
REMARK 470     VAL A 377    CG1  CG2
REMARK 470     VAL A 386    CG1  CG2
REMARK 470     LEU A 387    CG   CD1  CD2
REMARK 470     ILE A 389    CG1  CG2  CD1
REMARK 470     THR A 393    OG1  CG2
REMARK 470     VAL A 394    CG1  CG2
REMARK 470     ARG A 402    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLN A 414    CG   CD   OE1  NE2
REMARK 470     ARG A 448    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LEU A 475    CG   CD1  CD2
REMARK 470     VAL A 476    CG1  CG2
REMARK 470     VAL A 486    CG1  CG2
REMARK 470     ARG A 497    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ASN A 499    CG   OD1  ND2
REMARK 470     LEU A 500    CG   CD1  CD2
REMARK 470     ASN A 507    CG   OD1  ND2
REMARK 470     ILE A 508    CG1  CG2  CD1
REMARK 470     SER A 509    OG
REMARK 470     ARG A 510    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG A 512    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG A 520    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A 535    CG   CD   CE   NZ
REMARK 470     ILE A 547    CG1  CG2  CD1
REMARK 470     LEU A 551    CG   CD1  CD2
REMARK 470     GLU A 554    CG   CD   OE1  OE2
REMARK 470     PHE A 555    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 566    CG   CD   CE   NZ
REMARK 470     ILE B 133    CG1  CG2  CD1
REMARK 470     ILE B 136    CG1  CG2  CD1
REMARK 470     LEU B 140    CG   CD1  CD2
REMARK 470     ILE B 141    CG1  CG2  CD1
REMARK 470     ASP B 143    CG   OD1  OD2
REMARK 470     THR B 145    OG1  CG2
REMARK 470     ILE B 163    CG1  CG2  CD1
REMARK 470     ILE B 175    CG1  CG2  CD1
REMARK 470     ARG B 196    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ASP B 197    CG   OD1  OD2
REMARK 470     LEU B 205    CG   CD1  CD2
REMARK 470     LEU B 223    CG   CD1  CD2
REMARK 470     SER B 225    OG
REMARK 470     LYS B 235    CG   CD   CE   NZ
REMARK 470     VAL B 239    CG1  CG2
REMARK 470     SER B 240    OG
REMARK 470     LEU B 244    CG   CD1  CD2
REMARK 470     VAL B 253    CG1  CG2
REMARK 470     THR B 254    OG1  CG2
REMARK 470     GLU B 258    CG   CD   OE1  OE2
REMARK 470     VAL B 264    CG1  CG2
REMARK 470     ILE B 265    CG1  CG2  CD1
REMARK 470     VAL B 270    CG1  CG2
REMARK 470     LYS B 283    CG   CD   CE   NZ
REMARK 470     VAL B 287    CG1  CG2
REMARK 470     VAL B 295    CG1  CG2
REMARK 470     ASN B 297    CG   OD1  ND2
REMARK 470     VAL B 301    CG1  CG2
REMARK 470     ILE B 307    CG1  CG2  CD1
REMARK 470     VAL B 311    CG1  CG2
REMARK 470     VAL B 315    CG1  CG2
REMARK 470     LYS B 320    CG   CD   CE   NZ
REMARK 470     VAL B 334    CG1  CG2
REMARK 470     ILE B 335    CG1  CG2  CD1
REMARK 470     LYS B 337    CG   CD   CE   NZ
REMARK 470     ASP B 341    CG   OD1  OD2
REMARK 470     ILE B 351    CG1  CG2  CD1
REMARK 470     ARG B 352    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS B 355    CG   CD   CE   NZ
REMARK 470     LYS B 359    CG   CD   CE   NZ
REMARK 470     ARG B 362    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS B 366    CG   CD   CE   NZ
REMARK 470     ARG B 367    CG   CD   NE   CZ   NH1  NH2
REMARK 470     VAL B 368    CG1  CG2
REMARK 470     GLN B 369    CG   CD   OE1  NE2
REMARK 470     GLN B 370    CG   CD   OE1  NE2
REMARK 470     ILE B 372    CG1  CG2  CD1
REMARK 470     LEU B 373    CG   CD1  CD2
REMARK 470     ILE B 375    CG1  CG2  CD1
REMARK 470     LYS B 376    CG   CD   CE   NZ
REMARK 470     VAL B 377    CG1  CG2
REMARK 470     VAL B 386    CG1  CG2
REMARK 470     LEU B 387    CG   CD1  CD2
REMARK 470     ILE B 389    CG1  CG2  CD1
REMARK 470     THR B 393    OG1  CG2
REMARK 470     VAL B 394    CG1  CG2
REMARK 470     ARG B 402    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLN B 414    CG   CD   OE1  NE2
REMARK 470     ARG B 448    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG B 459    CG   CD   NE   CZ   NH1  NH2
REMARK 470     VAL B 476    CG1  CG2
REMARK 470     VAL B 486    CG1  CG2
REMARK 470     ARG B 497    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LEU B 500    CG   CD1  CD2
REMARK 470     ASN B 507    CG   OD1  ND2
REMARK 470     ILE B 508    CG1  CG2  CD1
REMARK 470     SER B 509    OG
REMARK 470     ARG B 510    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG B 512    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG B 520    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS B 535    CG   CD   CE   NZ
REMARK 470     ILE B 547    CG1  CG2  CD1
REMARK 470     LEU B 551    CG   CD1  CD2
REMARK 470     GLU B 554    CG   CD   OE1  OE2
REMARK 470     PHE B 555    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS B 566    CG   CD   CE   NZ
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    ASP B   147     OG   SER B   150              1.98
REMARK 500   O    HIS B   198     ND2  ASN B   233              2.01
REMARK 500   SG   CYS B   185     CB   CYS B   246              2.05
REMARK 500   NE2  HIS B   198     O    VAL B   253              2.09
REMARK 500   O    ASP B   260     OG   SER B   263              2.10
REMARK 500   O    MET B   353     N    SER B   356              2.10
REMARK 500   N    THR B   256     OE2  GLU B   259              2.16
REMARK 500   OG1  THR A   242     OD1  ASP A   247              2.17
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 472   C   -  N   -  CA  ANGL. DEV. =  10.9 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    PHE A 162      -60.62    -97.17
REMARK 500    SER A 181      -84.60   -126.98
REMARK 500    ASP A 197       73.82     55.12
REMARK 500    LYS A 235      -76.57   -108.37
REMARK 500    PRO A 266     -177.73    -64.01
REMARK 500    THR A 289      -64.40   -105.96
REMARK 500    VAL A 301      -16.09     68.83
REMARK 500    TYR A 339      -73.92    -61.26
REMARK 500    VAL A 394      -62.51   -106.22
REMARK 500    ASN A 431      -77.27    -90.97
REMARK 500    ASN A 432      -80.11   -125.80
REMARK 500    PRO A 453       45.91    -89.91
REMARK 500    ARG A 459      -62.21    -99.01
REMARK 500    LEU A 475      -72.54   -117.41
REMARK 500    ARG A 484      -60.74    -91.54
REMARK 500    ASP A 493      159.49    175.50
REMARK 500    GLU A 554      -73.02    -56.69
REMARK 500    ASP A 568       -4.11     72.90
REMARK 500    ILE B 136      -72.49    -84.98
REMARK 500    LEU B 140      -70.12    -90.09
REMARK 500    SER B 170      -65.07    -91.82
REMARK 500    ILE B 175       70.31     57.04
REMARK 500    SER B 181      -83.24   -127.23
REMARK 500    ASP B 197       70.56     59.73
REMARK 500    LYS B 235      -78.33   -100.33
REMARK 500    VAL B 301      -11.60     69.52
REMARK 500    ASN B 309       -3.39     67.78
REMARK 500    TYR B 339      -72.18    -59.96
REMARK 500    TYR B 349      -61.93    -97.06
REMARK 500    ASN B 432     -118.57     46.65
REMARK 500    ALA B 445      -14.05     66.27
REMARK 500    PRO B 453       48.93    -91.04
REMARK 500    LEU B 475      -74.62   -125.00
REMARK 500    HIS B 481        0.33     84.91
REMARK 500    ASP B 493      159.78    176.72
REMARK 500    GLN B 495      -61.58   -127.32
REMARK 500    ALA B 524      -60.99   -126.85
REMARK 500    GLU B 554      -75.64    -81.33
REMARK 500    ASP B 567      -70.90    -74.07
REMARK 500    VAL E  80      -16.59     68.72
REMARK 500    LEU E  90      -61.35   -122.63
REMARK 500    VAL F  81      -57.36   -127.31
REMARK 500    LEU F  90      -74.16   -114.48
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    PHE B 363        24.2      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AUTHORS STATE THAT THE RESIDUE AT THIS POSITION IS ALA ACCORDING TO
REMARK 999 THE CRYSTAL STRUCTURE.
DBREF  3T1E A   49   570  UNP    P12554   HN_NDVA         49    570
DBREF  3T1E B   49   570  UNP    P12554   HN_NDVA         49    570
DBREF  3T1E E   49   570  UNP    P12554   HN_NDVA         49    570
DBREF  3T1E F   49   570  UNP    P12554   HN_NDVA         49    570
SEQADV 3T1E ALA A   34  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E MET A   35  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E ALA A   36  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E HIS A   37  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E HIS A   38  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E HIS A   39  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E HIS A   40  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E HIS A   41  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E HIS A   42  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E LEU A   43  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E VAL A   44  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E PRO A   45  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E ARG A   46  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E GLY A   47  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E SER A   48  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E ALA A  328  UNP  P12554    GLY   328 SEE REMARK 999
SEQADV 3T1E ALA B   34  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E MET B   35  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E ALA B   36  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E HIS B   37  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E HIS B   38  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E HIS B   39  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E HIS B   40  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E HIS B   41  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E HIS B   42  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E LEU B   43  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E VAL B   44  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E PRO B   45  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E ARG B   46  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E GLY B   47  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E SER B   48  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E ALA B  328  UNP  P12554    GLY   328 SEE REMARK 999
SEQADV 3T1E ALA E   34  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E MET E   35  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E ALA E   36  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E HIS E   37  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E HIS E   38  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E HIS E   39  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E HIS E   40  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E HIS E   41  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E HIS E   42  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E LEU E   43  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E VAL E   44  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E PRO E   45  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E ARG E   46  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E GLY E   47  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E SER E   48  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E ALA E  328  UNP  P12554    GLY   328 SEE REMARK 999
SEQADV 3T1E ALA F   34  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E MET F   35  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E ALA F   36  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E HIS F   37  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E HIS F   38  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E HIS F   39  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E HIS F   40  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E HIS F   41  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E HIS F   42  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E LEU F   43  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E VAL F   44  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E PRO F   45  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E ARG F   46  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E GLY F   47  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E SER F   48  UNP  P12554              EXPRESSION TAG
SEQADV 3T1E ALA F  328  UNP  P12554    GLY   328 SEE REMARK 999
SEQRES   1 A  537  ALA MET ALA HIS HIS HIS HIS HIS HIS LEU VAL PRO ARG
SEQRES   2 A  537  GLY SER GLU ALA SER THR PRO GLY ASP LEU VAL SER ILE
SEQRES   3 A  537  PRO THR ALA ILE SER ARG ALA GLU GLY LYS ILE THR SER
SEQRES   4 A  537  ALA LEU GLY SER ASN GLN ASP VAL VAL ASP ARG ILE TYR
SEQRES   5 A  537  LYS GLN VAL ALA LEU GLU SER PRO LEU ALA LEU LEU ASN
SEQRES   6 A  537  THR GLU SER ILE ILE MET ASN ALA ILE THR SER LEU SER
SEQRES   7 A  537  TYR GLN ILE ASN GLY ALA ALA ASN ASN SER GLY CYS GLY
SEQRES   8 A  537  ALA PRO VAL HIS ASP PRO ASP TYR ILE GLY GLY ILE GLY
SEQRES   9 A  537  LYS GLU LEU ILE VAL ASP ASP THR SER ASP VAL THR SER
SEQRES  10 A  537  PHE TYR PRO SER ALA PHE GLN GLU HIS LEU ASN PHE ILE
SEQRES  11 A  537  PRO ALA PRO THR THR GLY SER GLY CYS THR ARG ILE PRO
SEQRES  12 A  537  SER PHE ASP MET SER ALA THR HIS CYS TYR THR HIS ASN
SEQRES  13 A  537  VAL ILE PHE SER GLY CYS ARG ASP HIS SER HIS SER HIS
SEQRES  14 A  537  GLN TYR LEU ALA LEU GLY VAL LEU ARG THR SER ALA THR
SEQRES  15 A  537  GLY ARG VAL PHE PHE SER THR LEU ARG SER ILE ASN LEU
SEQRES  16 A  537  ASP ASP THR GLN ASN ARG LYS SER CYS SER VAL SER ALA
SEQRES  17 A  537  THR PRO LEU GLY CYS ASP MET LEU CYS SER LYS VAL THR
SEQRES  18 A  537  GLU THR GLU GLU GLU ASP TYR ASN SER VAL ILE PRO THR
SEQRES  19 A  537  SER MET VAL HIS GLY ARG LEU GLY PHE ASP GLY GLN TYR
SEQRES  20 A  537  HIS GLU LYS ASP LEU ASP VAL THR THR LEU PHE GLY ASP
SEQRES  21 A  537  TRP VAL ALA ASN TYR PRO GLY VAL GLY GLY GLY SER PHE
SEQRES  22 A  537  ILE ASP ASN ARG VAL TRP PHE PRO VAL TYR GLY GLY LEU
SEQRES  23 A  537  LYS PRO SER SER PRO SER ASP THR ALA GLN GLU GLY ARG
SEQRES  24 A  537  TYR VAL ILE TYR LYS ARG TYR ASN ASP THR CYS PRO ASP
SEQRES  25 A  537  GLU GLN ASP TYR GLN ILE ARG MET ALA LYS SER SER TYR
SEQRES  26 A  537  LYS PRO GLY ARG PHE GLY GLY LYS ARG VAL GLN GLN ALA
SEQRES  27 A  537  ILE LEU SER ILE LYS VAL SER THR SER LEU GLY GLU ASP
SEQRES  28 A  537  PRO VAL LEU THR ILE PRO PRO ASN THR VAL THR LEU MET
SEQRES  29 A  537  GLY ALA GLU GLY ARG VAL LEU THR VAL GLY THR SER HIS
SEQRES  30 A  537  PHE LEU TYR GLN ARG GLY SER SER TYR PHE SER PRO ALA
SEQRES  31 A  537  LEU LEU TYR PRO MET THR VAL ASN ASN ASN THR ALA THR
SEQRES  32 A  537  LEU HIS SER PRO TYR THR PHE ASN ALA PHE THR ARG PRO
SEQRES  33 A  537  GLY SER VAL PRO CYS GLN ALA SER ALA ARG CYS PRO ASN
SEQRES  34 A  537  SER CYS VAL THR GLY VAL TYR THR ASP PRO TYR PRO LEU
SEQRES  35 A  537  VAL PHE HIS ARG ASN HIS THR LEU ARG GLY VAL PHE GLY
SEQRES  36 A  537  THR MET LEU ASP ASP GLU GLN ALA ARG LEU ASN LEU VAL
SEQRES  37 A  537  SER ALA VAL PHE ASP ASN ILE SER ARG SER ARG ILE THR
SEQRES  38 A  537  ARG VAL SER SER SER ARG THR LYS ALA ALA TYR THR THR
SEQRES  39 A  537  SER THR CYS PHE LYS VAL VAL LYS THR ASN LYS THR TYR
SEQRES  40 A  537  CYS LEU SER ILE ALA GLU ILE SER ASN THR LEU PHE GLY
SEQRES  41 A  537  GLU PHE ARG ILE VAL PRO LEU LEU VAL GLU ILE LEU LYS
SEQRES  42 A  537  ASP ASP GLY VAL
SEQRES   1 B  537  ALA MET ALA HIS HIS HIS HIS HIS HIS LEU VAL PRO ARG
SEQRES   2 B  537  GLY SER GLU ALA SER THR PRO GLY ASP LEU VAL SER ILE
SEQRES   3 B  537  PRO THR ALA ILE SER ARG ALA GLU GLY LYS ILE THR SER
SEQRES   4 B  537  ALA LEU GLY SER ASN GLN ASP VAL VAL ASP ARG ILE TYR
SEQRES   5 B  537  LYS GLN VAL ALA LEU GLU SER PRO LEU ALA LEU LEU ASN
SEQRES   6 B  537  THR GLU SER ILE ILE MET ASN ALA ILE THR SER LEU SER
SEQRES   7 B  537  TYR GLN ILE ASN GLY ALA ALA ASN ASN SER GLY CYS GLY
SEQRES   8 B  537  ALA PRO VAL HIS ASP PRO ASP TYR ILE GLY GLY ILE GLY
SEQRES   9 B  537  LYS GLU LEU ILE VAL ASP ASP THR SER ASP VAL THR SER
SEQRES  10 B  537  PHE TYR PRO SER ALA PHE GLN GLU HIS LEU ASN PHE ILE
SEQRES  11 B  537  PRO ALA PRO THR THR GLY SER GLY CYS THR ARG ILE PRO
SEQRES  12 B  537  SER PHE ASP MET SER ALA THR HIS CYS TYR THR HIS ASN
SEQRES  13 B  537  VAL ILE PHE SER GLY CYS ARG ASP HIS SER HIS SER HIS
SEQRES  14 B  537  GLN TYR LEU ALA LEU GLY VAL LEU ARG THR SER ALA THR
SEQRES  15 B  537  GLY ARG VAL PHE PHE SER THR LEU ARG SER ILE ASN LEU
SEQRES  16 B  537  ASP ASP THR GLN ASN ARG LYS SER CYS SER VAL SER ALA
SEQRES  17 B  537  THR PRO LEU GLY CYS ASP MET LEU CYS SER LYS VAL THR
SEQRES  18 B  537  GLU THR GLU GLU GLU ASP TYR ASN SER VAL ILE PRO THR
SEQRES  19 B  537  SER MET VAL HIS GLY ARG LEU GLY PHE ASP GLY GLN TYR
SEQRES  20 B  537  HIS GLU LYS ASP LEU ASP VAL THR THR LEU PHE GLY ASP
SEQRES  21 B  537  TRP VAL ALA ASN TYR PRO GLY VAL GLY GLY GLY SER PHE
SEQRES  22 B  537  ILE ASP ASN ARG VAL TRP PHE PRO VAL TYR GLY GLY LEU
SEQRES  23 B  537  LYS PRO SER SER PRO SER ASP THR ALA GLN GLU GLY ARG
SEQRES  24 B  537  TYR VAL ILE TYR LYS ARG TYR ASN ASP THR CYS PRO ASP
SEQRES  25 B  537  GLU GLN ASP TYR GLN ILE ARG MET ALA LYS SER SER TYR
SEQRES  26 B  537  LYS PRO GLY ARG PHE GLY GLY LYS ARG VAL GLN GLN ALA
SEQRES  27 B  537  ILE LEU SER ILE LYS VAL SER THR SER LEU GLY GLU ASP
SEQRES  28 B  537  PRO VAL LEU THR ILE PRO PRO ASN THR VAL THR LEU MET
SEQRES  29 B  537  GLY ALA GLU GLY ARG VAL LEU THR VAL GLY THR SER HIS
SEQRES  30 B  537  PHE LEU TYR GLN ARG GLY SER SER TYR PHE SER PRO ALA
SEQRES  31 B  537  LEU LEU TYR PRO MET THR VAL ASN ASN ASN THR ALA THR
SEQRES  32 B  537  LEU HIS SER PRO TYR THR PHE ASN ALA PHE THR ARG PRO
SEQRES  33 B  537  GLY SER VAL PRO CYS GLN ALA SER ALA ARG CYS PRO ASN
SEQRES  34 B  537  SER CYS VAL THR GLY VAL TYR THR ASP PRO TYR PRO LEU
SEQRES  35 B  537  VAL PHE HIS ARG ASN HIS THR LEU ARG GLY VAL PHE GLY
SEQRES  36 B  537  THR MET LEU ASP ASP GLU GLN ALA ARG LEU ASN LEU VAL
SEQRES  37 B  537  SER ALA VAL PHE ASP ASN ILE SER ARG SER ARG ILE THR
SEQRES  38 B  537  ARG VAL SER SER SER ARG THR LYS ALA ALA TYR THR THR
SEQRES  39 B  537  SER THR CYS PHE LYS VAL VAL LYS THR ASN LYS THR TYR
SEQRES  40 B  537  CYS LEU SER ILE ALA GLU ILE SER ASN THR LEU PHE GLY
SEQRES  41 B  537  GLU PHE ARG ILE VAL PRO LEU LEU VAL GLU ILE LEU LYS
SEQRES  42 B  537  ASP ASP GLY VAL
SEQRES   1 E  537  ALA MET ALA HIS HIS HIS HIS HIS HIS LEU VAL PRO ARG
SEQRES   2 E  537  GLY SER GLU ALA SER THR PRO GLY ASP LEU VAL SER ILE
SEQRES   3 E  537  PRO THR ALA ILE SER ARG ALA GLU GLY LYS ILE THR SER
SEQRES   4 E  537  ALA LEU GLY SER ASN GLN ASP VAL VAL ASP ARG ILE TYR
SEQRES   5 E  537  LYS GLN VAL ALA LEU GLU SER PRO LEU ALA LEU LEU ASN
SEQRES   6 E  537  THR GLU SER ILE ILE MET ASN ALA ILE THR SER LEU SER
SEQRES   7 E  537  TYR GLN ILE ASN GLY ALA ALA ASN ASN SER GLY CYS GLY
SEQRES   8 E  537  ALA PRO VAL HIS ASP PRO ASP TYR ILE GLY GLY ILE GLY
SEQRES   9 E  537  LYS GLU LEU ILE VAL ASP ASP THR SER ASP VAL THR SER
SEQRES  10 E  537  PHE TYR PRO SER ALA PHE GLN GLU HIS LEU ASN PHE ILE
SEQRES  11 E  537  PRO ALA PRO THR THR GLY SER GLY CYS THR ARG ILE PRO
SEQRES  12 E  537  SER PHE ASP MET SER ALA THR HIS CYS TYR THR HIS ASN
SEQRES  13 E  537  VAL ILE PHE SER GLY CYS ARG ASP HIS SER HIS SER HIS
SEQRES  14 E  537  GLN TYR LEU ALA LEU GLY VAL LEU ARG THR SER ALA THR
SEQRES  15 E  537  GLY ARG VAL PHE PHE SER THR LEU ARG SER ILE ASN LEU
SEQRES  16 E  537  ASP ASP THR GLN ASN ARG LYS SER CYS SER VAL SER ALA
SEQRES  17 E  537  THR PRO LEU GLY CYS ASP MET LEU CYS SER LYS VAL THR
SEQRES  18 E  537  GLU THR GLU GLU GLU ASP TYR ASN SER VAL ILE PRO THR
SEQRES  19 E  537  SER MET VAL HIS GLY ARG LEU GLY PHE ASP GLY GLN TYR
SEQRES  20 E  537  HIS GLU LYS ASP LEU ASP VAL THR THR LEU PHE GLY ASP
SEQRES  21 E  537  TRP VAL ALA ASN TYR PRO GLY VAL GLY GLY GLY SER PHE
SEQRES  22 E  537  ILE ASP ASN ARG VAL TRP PHE PRO VAL TYR GLY GLY LEU
SEQRES  23 E  537  LYS PRO SER SER PRO SER ASP THR ALA GLN GLU GLY ARG
SEQRES  24 E  537  TYR VAL ILE TYR LYS ARG TYR ASN ASP THR CYS PRO ASP
SEQRES  25 E  537  GLU GLN ASP TYR GLN ILE ARG MET ALA LYS SER SER TYR
SEQRES  26 E  537  LYS PRO GLY ARG PHE GLY GLY LYS ARG VAL GLN GLN ALA
SEQRES  27 E  537  ILE LEU SER ILE LYS VAL SER THR SER LEU GLY GLU ASP
SEQRES  28 E  537  PRO VAL LEU THR ILE PRO PRO ASN THR VAL THR LEU MET
SEQRES  29 E  537  GLY ALA GLU GLY ARG VAL LEU THR VAL GLY THR SER HIS
SEQRES  30 E  537  PHE LEU TYR GLN ARG GLY SER SER TYR PHE SER PRO ALA
SEQRES  31 E  537  LEU LEU TYR PRO MET THR VAL ASN ASN ASN THR ALA THR
SEQRES  32 E  537  LEU HIS SER PRO TYR THR PHE ASN ALA PHE THR ARG PRO
SEQRES  33 E  537  GLY SER VAL PRO CYS GLN ALA SER ALA ARG CYS PRO ASN
SEQRES  34 E  537  SER CYS VAL THR GLY VAL TYR THR ASP PRO TYR PRO LEU
SEQRES  35 E  537  VAL PHE HIS ARG ASN HIS THR LEU ARG GLY VAL PHE GLY
SEQRES  36 E  537  THR MET LEU ASP ASP GLU GLN ALA ARG LEU ASN LEU VAL
SEQRES  37 E  537  SER ALA VAL PHE ASP ASN ILE SER ARG SER ARG ILE THR
SEQRES  38 E  537  ARG VAL SER SER SER ARG THR LYS ALA ALA TYR THR THR
SEQRES  39 E  537  SER THR CYS PHE LYS VAL VAL LYS THR ASN LYS THR TYR
SEQRES  40 E  537  CYS LEU SER ILE ALA GLU ILE SER ASN THR LEU PHE GLY
SEQRES  41 E  537  GLU PHE ARG ILE VAL PRO LEU LEU VAL GLU ILE LEU LYS
SEQRES  42 E  537  ASP ASP GLY VAL
SEQRES   1 F  537  ALA MET ALA HIS HIS HIS HIS HIS HIS LEU VAL PRO ARG
SEQRES   2 F  537  GLY SER GLU ALA SER THR PRO GLY ASP LEU VAL SER ILE
SEQRES   3 F  537  PRO THR ALA ILE SER ARG ALA GLU GLY LYS ILE THR SER
SEQRES   4 F  537  ALA LEU GLY SER ASN GLN ASP VAL VAL ASP ARG ILE TYR
SEQRES   5 F  537  LYS GLN VAL ALA LEU GLU SER PRO LEU ALA LEU LEU ASN
SEQRES   6 F  537  THR GLU SER ILE ILE MET ASN ALA ILE THR SER LEU SER
SEQRES   7 F  537  TYR GLN ILE ASN GLY ALA ALA ASN ASN SER GLY CYS GLY
SEQRES   8 F  537  ALA PRO VAL HIS ASP PRO ASP TYR ILE GLY GLY ILE GLY
SEQRES   9 F  537  LYS GLU LEU ILE VAL ASP ASP THR SER ASP VAL THR SER
SEQRES  10 F  537  PHE TYR PRO SER ALA PHE GLN GLU HIS LEU ASN PHE ILE
SEQRES  11 F  537  PRO ALA PRO THR THR GLY SER GLY CYS THR ARG ILE PRO
SEQRES  12 F  537  SER PHE ASP MET SER ALA THR HIS CYS TYR THR HIS ASN
SEQRES  13 F  537  VAL ILE PHE SER GLY CYS ARG ASP HIS SER HIS SER HIS
SEQRES  14 F  537  GLN TYR LEU ALA LEU GLY VAL LEU ARG THR SER ALA THR
SEQRES  15 F  537  GLY ARG VAL PHE PHE SER THR LEU ARG SER ILE ASN LEU
SEQRES  16 F  537  ASP ASP THR GLN ASN ARG LYS SER CYS SER VAL SER ALA
SEQRES  17 F  537  THR PRO LEU GLY CYS ASP MET LEU CYS SER LYS VAL THR
SEQRES  18 F  537  GLU THR GLU GLU GLU ASP TYR ASN SER VAL ILE PRO THR
SEQRES  19 F  537  SER MET VAL HIS GLY ARG LEU GLY PHE ASP GLY GLN TYR
SEQRES  20 F  537  HIS GLU LYS ASP LEU ASP VAL THR THR LEU PHE GLY ASP
SEQRES  21 F  537  TRP VAL ALA ASN TYR PRO GLY VAL GLY GLY GLY SER PHE
SEQRES  22 F  537  ILE ASP ASN ARG VAL TRP PHE PRO VAL TYR GLY GLY LEU
SEQRES  23 F  537  LYS PRO SER SER PRO SER ASP THR ALA GLN GLU GLY ARG
SEQRES  24 F  537  TYR VAL ILE TYR LYS ARG TYR ASN ASP THR CYS PRO ASP
SEQRES  25 F  537  GLU GLN ASP TYR GLN ILE ARG MET ALA LYS SER SER TYR
SEQRES  26 F  537  LYS PRO GLY ARG PHE GLY GLY LYS ARG VAL GLN GLN ALA
SEQRES  27 F  537  ILE LEU SER ILE LYS VAL SER THR SER LEU GLY GLU ASP
SEQRES  28 F  537  PRO VAL LEU THR ILE PRO PRO ASN THR VAL THR LEU MET
SEQRES  29 F  537  GLY ALA GLU GLY ARG VAL LEU THR VAL GLY THR SER HIS
SEQRES  30 F  537  PHE LEU TYR GLN ARG GLY SER SER TYR PHE SER PRO ALA
SEQRES  31 F  537  LEU LEU TYR PRO MET THR VAL ASN ASN ASN THR ALA THR
SEQRES  32 F  537  LEU HIS SER PRO TYR THR PHE ASN ALA PHE THR ARG PRO
SEQRES  33 F  537  GLY SER VAL PRO CYS GLN ALA SER ALA ARG CYS PRO ASN
SEQRES  34 F  537  SER CYS VAL THR GLY VAL TYR THR ASP PRO TYR PRO LEU
SEQRES  35 F  537  VAL PHE HIS ARG ASN HIS THR LEU ARG GLY VAL PHE GLY
SEQRES  36 F  537  THR MET LEU ASP ASP GLU GLN ALA ARG LEU ASN LEU VAL
SEQRES  37 F  537  SER ALA VAL PHE ASP ASN ILE SER ARG SER ARG ILE THR
SEQRES  38 F  537  ARG VAL SER SER SER ARG THR LYS ALA ALA TYR THR THR
SEQRES  39 F  537  SER THR CYS PHE LYS VAL VAL LYS THR ASN LYS THR TYR
SEQRES  40 F  537  CYS LEU SER ILE ALA GLU ILE SER ASN THR LEU PHE GLY
SEQRES  41 F  537  GLU PHE ARG ILE VAL PRO LEU LEU VAL GLU ILE LEU LYS
SEQRES  42 F  537  ASP ASP GLY VAL
HELIX    1   1 ASP A  129  ILE A  133  5                                   5
HELIX    2   2 ASP A  147  PHE A  151  5                                   5
HELIX    3   3 THR A  256  TYR A  261  1                                   6
HELIX    4   4 SER A  323  ALA A  328  1                                   6
HELIX    5   5 GLU A  346  SER A  357  1                                  12
HELIX    6   6 TYR A  358  LYS A  359  5                                   2
HELIX    7   7 PRO A  360  GLY A  364  5                                   5
HELIX    8   8 ASP B  129  ILE B  133  5                                   5
HELIX    9   9 ASP B  147  THR B  149  5                                   3
HELIX   10  10 THR B  256  TYR B  261  1                                   6
HELIX   11  11 ASP B  286  GLY B  292  1                                   7
HELIX   12  12 SER B  323  ALA B  328  1                                   6
HELIX   13  13 GLU B  346  TYR B  358  1                                  13
HELIX   14  14 PRO B  360  GLY B  364  5                                   5
HELIX   15  15 VAL E   80  LYS E   86  1                                   7
HELIX   16  16 GLN E   87  LEU E   90  5                                   4
HELIX   17  17 GLU E   91  TYR E  112  1                                  22
HELIX   18  18 VAL F   81  TYR F   85  5                                   5
HELIX   19  19 LEU F   90  TYR F  112  1                                  23
SHEET    1   A 2 ILE A 141  VAL A 142  0
SHEET    2   A 2 VAL A 476  PHE A 477  1  O  PHE A 477   N  ILE A 141
SHEET    1   B 5 TYR A 152  PRO A 153  0
SHEET    2   B 5 GLY A 553  LEU A 565 -1  O  LEU A 565   N  TYR A 152
SHEET    3   B 5 LYS A 538  ASN A 549 -1  N  ASN A 549   O  GLY A 553
SHEET    4   B 5 LYS A 522  VAL A 533 -1  N  THR A 527   O  ILE A 544
SHEET    5   B 5 TYR A 469  THR A 470  1  N  TYR A 469   O  THR A 526
SHEET    1   C 4 CYS A 172  MET A 180  0
SHEET    2   C 4 HIS A 184  ILE A 191 -1  O  CYS A 185   N  ASP A 179
SHEET    3   C 4 HIS A 202  THR A 212 -1  O  GLY A 208   N  HIS A 184
SHEET    4   C 4 VAL A 218  LEU A 228 -1  O  ARG A 224   N  LEU A 207
SHEET    1   D 4 SER A 238  THR A 242  0
SHEET    2   D 4 GLY A 245  SER A 251 -1  O  ASP A 247   N  SER A 240
SHEET    3   D 4 MET A 269  LEU A 274 -1  O  GLY A 272   N  MET A 248
SHEET    4   D 4 TYR A 280  LEU A 285 -1  O  LEU A 285   N  MET A 269
SHEET    1   E 3 TRP A 294  PRO A 299  0
SHEET    2   E 3 ARG A 310  LEU A 319 -1  O  TYR A 316   N  TYR A 298
SHEET    3   E 3 SER A 305  ILE A 307 -1  N  ILE A 307   O  ARG A 310
SHEET    1   F 4 TRP A 294  PRO A 299  0
SHEET    2   F 4 ARG A 310  LEU A 319 -1  O  TYR A 316   N  TYR A 298
SHEET    3   F 4 VAL A 368  LYS A 376 -1  O  ALA A 371   N  VAL A 315
SHEET    4   F 4 GLU A 383  THR A 388 -1  O  THR A 388   N  ILE A 372
SHEET    1   G 4 GLY A 401  VAL A 406  0
SHEET    2   G 4 SER A 409  GLN A 414 -1  O  PHE A 411   N  LEU A 404
SHEET    3   G 4 PRO A 422  VAL A 430 -1  O  MET A 428   N  HIS A 410
SHEET    4   G 4 ALA A 435  LEU A 437 -1  O  THR A 436   N  THR A 429
SHEET    1   H 4 GLY A 401  VAL A 406  0
SHEET    2   H 4 SER A 409  GLN A 414 -1  O  PHE A 411   N  LEU A 404
SHEET    3   H 4 PRO A 422  VAL A 430 -1  O  MET A 428   N  HIS A 410
SHEET    4   H 4 TYR A 441  THR A 447 -1  O  TYR A 441   N  LEU A 425
SHEET    1   I 4 TYR A 473  PRO A 474  0
SHEET    2   I 4 VAL A 486  LEU A 491 -1  O  PHE A 487   N  TYR A 473
SHEET    3   I 4 LEU A 500  PHE A 505 -1  O  PHE A 505   N  VAL A 486
SHEET    4   I 4 THR A 514  ARG A 515 -1  O  THR A 514   N  SER A 502
SHEET    1   J 5 ILE B 141  VAL B 142  0
SHEET    2   J 5 TYR B 473  PHE B 477  1  O  PHE B 477   N  ILE B 141
SHEET    3   J 5 LEU B 483  LEU B 491 -1  O  PHE B 487   N  TYR B 473
SHEET    4   J 5 LEU B 500  ASP B 506 -1  O  VAL B 501   N  MET B 490
SHEET    5   J 5 THR B 514  ARG B 515 -1  O  THR B 514   N  SER B 502
SHEET    1   K 5 PHE B 151  PRO B 153  0
SHEET    2   K 5 GLY B 553  LYS B 566 -1  O  LEU B 565   N  TYR B 152
SHEET    3   K 5 LYS B 538  ASN B 549 -1  N  ASN B 549   O  GLY B 553
SHEET    4   K 5 LYS B 522  VAL B 533 -1  N  THR B 527   O  ILE B 544
SHEET    5   K 5 TYR B 469  THR B 470  1  N  TYR B 469   O  THR B 526
SHEET    1   L 4 CYS B 172  MET B 180  0
SHEET    2   L 4 HIS B 184  PHE B 192 -1  O  CYS B 185   N  ASP B 179
SHEET    3   L 4 ARG B 196  THR B 212 -1  O  GLY B 208   N  HIS B 184
SHEET    4   L 4 VAL B 218  LEU B 228 -1  O  ARG B 224   N  LEU B 207
SHEET    1   M 4 ARG B 234  THR B 242  0
SHEET    2   M 4 GLY B 245  LYS B 252 -1  O  ASP B 247   N  SER B 240
SHEET    3   M 4 SER B 268  LEU B 274 -1  O  GLY B 272   N  MET B 248
SHEET    4   M 4 TYR B 280  LEU B 285 -1  O  LEU B 285   N  MET B 269
SHEET    1   N 3 TRP B 294  PRO B 299  0
SHEET    2   N 3 ARG B 310  LEU B 319 -1  O  TYR B 316   N  TYR B 298
SHEET    3   N 3 SER B 305  ILE B 307 -1  N  SER B 305   O  TRP B 312
SHEET    1   O 4 TRP B 294  PRO B 299  0
SHEET    2   O 4 ARG B 310  LEU B 319 -1  O  TYR B 316   N  TYR B 298
SHEET    3   O 4 ALA B 371  LYS B 376 -1  O  ALA B 371   N  VAL B 315
SHEET    4   O 4 GLU B 383  THR B 388 -1  O  THR B 388   N  ILE B 372
SHEET    1   P 4 VAL B 403  VAL B 406  0
SHEET    2   P 4 SER B 409  TYR B 413 -1  O  PHE B 411   N  LEU B 404
SHEET    3   P 4 PRO B 422  ASN B 431 -1  O  TYR B 426   N  LEU B 412
SHEET    4   P 4 THR B 434  LEU B 437 -1  O  THR B 434   N  ASN B 431
SHEET    1   Q 4 VAL B 403  VAL B 406  0
SHEET    2   Q 4 SER B 409  TYR B 413 -1  O  PHE B 411   N  LEU B 404
SHEET    3   Q 4 PRO B 422  ASN B 431 -1  O  TYR B 426   N  LEU B 412
SHEET    4   Q 4 TYR B 441  THR B 447 -1  O  TYR B 441   N  LEU B 425
SSBOND   1 CYS A  172    CYS A  195                          1555   1555  2.02
SSBOND   2 CYS A  185    CYS A  246                          1555   1555  2.03
SSBOND   3 CYS A  237    CYS A  250                          1555   1555  2.03
SSBOND   4 CYS A  343    CYS A  460                          1555   1555  2.03
SSBOND   5 CYS A  454    CYS A  464                          1555   1555  2.03
SSBOND   6 CYS A  530    CYS A  541                          1555   1555  2.03
SSBOND   7 CYS B  172    CYS B  195                          1555   1555  2.03
SSBOND   8 CYS B  185    CYS B  246                          1555   1555  2.01
SSBOND   9 CYS B  237    CYS B  250                          1555   1555  2.04
SSBOND  10 CYS B  343    CYS B  460                          1555   1555  2.03
SSBOND  11 CYS B  454    CYS B  464                          1555   1555  2.03
SSBOND  12 CYS B  530    CYS B  541                          1555   1555  2.03
CISPEP   1 VAL A  452    PRO A  453          0       -10.02
CISPEP   2 VAL B  452    PRO B  453          0       -12.82
CRYST1  138.292  138.292  167.338  90.00  90.00  90.00 P 43 21 2    32
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      0.007231  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007231  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005976        0.00000
      
PROCHECK
Go to PROCHECK summary
 References