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PDBsum entry 4fzh

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Hydrolase PDB id
4fzh
Jmol
Contents
Protein chains
486 a.a.
Ligands
NAG ×7
NAG-NAG ×4
HEADER    HYDROLASE                               06-JUL-12   4FZH
TITLE     STRUCTURE OF THE ULSTER STRAIN NEWCASTLE DISEASE VIRUS HEMAGGLUTININ-
TITLE    2 NEURAMINIDASE REVEALS AUTO-INHIBITORY INTERACTIONS ASSOCIATED WITH
TITLE    3 LOW VIRULENCE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: HEMAGGLUTININ-NEURAMINIDASE;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 FRAGMENT: HEAD DOMAIN UNP RESIDUES 124-616;
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: 11190;
SOURCE   5 STRAIN: CHICKEN/N. IRELAND/ULSTER/67;
SOURCE   6 GENE: HN;
SOURCE   7 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   8 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS    HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    P.YUAN,R.G.PATERSON,G.P.LESER,R.A.LAMB,T.S.JARDETZKY
REVDAT   1   05-SEP-12 4FZH    0
JRNL        AUTH   P.YUAN,R.G.PATERSON,G.P.LESER,R.A.LAMB,T.S.JARDETZKY
JRNL        TITL   STRUCTURE OF THE ULSTER STRAIN NEWCASTLE DISEASE VIRUS
JRNL        TITL 2 HEMAGGLUTININ-NEURAMINIDASE REVEALS AUTO-INHIBITORY
JRNL        TITL 3 INTERACTIONS ASSOCIATED WITH LOW VIRULENCE.
JRNL        REF    PLOS PATHOG.                  V.   8 02855 2012
JRNL        REFN                   ISSN 1553-7366
JRNL        PMID   22912577
JRNL        DOI    10.1371/JOURNAL.PPAT.1002855
REMARK   2
REMARK   2 RESOLUTION.    3.50 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) : 3.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.91
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1
REMARK   3   NUMBER OF REFLECTIONS             : 32817
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.239
REMARK   3   R VALUE            (WORKING SET) : 0.236
REMARK   3   FREE R VALUE                     : 0.304
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.060
REMARK   3   FREE R VALUE TEST SET COUNT      : 1662
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 46.9176 -  8.0026    0.94     2653   136  0.2240 0.2781
REMARK   3     2  8.0026 -  6.3569    0.99     2629   137  0.2106 0.2804
REMARK   3     3  6.3569 -  5.5548    1.00     2639   144  0.2498 0.3661
REMARK   3     4  5.5548 -  5.0476    1.00     2601   147  0.2060 0.2658
REMARK   3     5  5.0476 -  4.6862    0.99     2596   128  0.1866 0.2482
REMARK   3     6  4.6862 -  4.4101    1.00     2580   140  0.2077 0.2538
REMARK   3     7  4.4101 -  4.1894    1.00     2593   141  0.2371 0.3126
REMARK   3     8  4.1894 -  4.0071    1.00     2564   140  0.2707 0.3651
REMARK   3     9  4.0071 -  3.8529    1.00     2569   158  0.2896 0.3780
REMARK   3    10  3.8529 -  3.7200    1.00     2568   138  0.3054 0.3551
REMARK   3    11  3.7200 -  3.6037    1.00     2578   132  0.3117 0.3356
REMARK   3    12  3.6037 -  3.5008    1.00     2585   121  0.3493 0.4389
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              : 0.27
REMARK   3   B_SOL              : 87.58
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 1.050
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.780
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) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : 0.00000
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      :  0.006          15659
REMARK   3   ANGLE     :  1.040          21291
REMARK   3   CHIRALITY :  0.071           2400
REMARK   3   PLANARITY :  0.005           2735
REMARK   3   DIHEDRAL  : 15.401           5664
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 25
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: chain 'A' and (resseq 124:192)
REMARK   3    ORIGIN FOR THE GROUP (A): -31.0727  11.6002  15.2727
REMARK   3    T TENSOR
REMARK   3      T11:   0.4780 T22:   2.2035
REMARK   3      T33:   0.7659 T12:   0.1462
REMARK   3      T13:   0.2162 T23:  -0.4470
REMARK   3    L TENSOR
REMARK   3      L11:   2.3150 L22:   2.5115
REMARK   3      L33:   1.9107 L12:   1.2735
REMARK   3      L13:  -1.0237 L23:  -0.4922
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1606 S12:  -0.6292 S13:   0.2961
REMARK   3      S21:   0.4268 S22:   0.6404 S23:   0.5157
REMARK   3      S31:  -0.3167 S32:  -0.9782 S33:  -0.2548
REMARK   3   TLS GROUP : 2
REMARK   3    SELECTION: chain 'A' and (resseq 193:229)
REMARK   3    ORIGIN FOR THE GROUP (A): -25.0094  20.9551  10.9265
REMARK   3    T TENSOR
REMARK   3      T11:   0.4810 T22:   1.9502
REMARK   3      T33:   1.0560 T12:   0.0981
REMARK   3      T13:  -0.0265 T23:  -0.5739
REMARK   3    L TENSOR
REMARK   3      L11:   7.9856 L22:   3.3591
REMARK   3      L33:   5.5644 L12:   0.1560
REMARK   3      L13:  -6.5819 L23:  -0.8057
REMARK   3    S TENSOR
REMARK   3      S11:  -1.3375 S12:  -0.7672 S13:   0.3722
REMARK   3      S21:  -0.1343 S22:   0.7171 S23:   0.1602
REMARK   3      S31:  -0.2875 S32:   0.4006 S33:   0.1352
REMARK   3   TLS GROUP : 3
REMARK   3    SELECTION: chain 'A' and (resseq 230:300)
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.4520  16.6226  15.7058
REMARK   3    T TENSOR
REMARK   3      T11:   0.6709 T22:   1.5069
REMARK   3      T33:   1.0459 T12:   0.0720
REMARK   3      T13:  -0.2230 T23:  -0.4240
REMARK   3    L TENSOR
REMARK   3      L11:   1.4861 L22:   5.5131
REMARK   3      L33:   1.0204 L12:  -0.2695
REMARK   3      L13:   0.5807 L23:  -1.8645
REMARK   3    S TENSOR
REMARK   3      S11:  -0.3038 S12:  -0.9777 S13:   0.8312
REMARK   3      S21:   0.6110 S22:   0.2018 S23:  -1.6076
REMARK   3      S31:  -0.3924 S32:  -0.1069 S33:   0.1560
REMARK   3   TLS GROUP : 4
REMARK   3    SELECTION: chain 'A' and (resseq 301:459)
REMARK   3    ORIGIN FOR THE GROUP (A): -11.7224  -2.8531  17.0556
REMARK   3    T TENSOR
REMARK   3      T11:   0.4342 T22:   1.6078
REMARK   3      T33:   0.5085 T12:   0.1201
REMARK   3      T13:   0.1030 T23:  -0.1634
REMARK   3    L TENSOR
REMARK   3      L11:   3.0425 L22:   5.2258
REMARK   3      L33:   0.9357 L12:  -0.6117
REMARK   3      L13:  -0.3501 L23:   0.2789
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1619 S12:  -0.4651 S13:  -0.2306
REMARK   3      S21:   0.4297 S22:  -0.0858 S23:  -0.7622
REMARK   3      S31:   0.1148 S32:   0.0008 S33:   0.2006
REMARK   3   TLS GROUP : 5
REMARK   3    SELECTION: chain 'A' and (resseq 460:555)
REMARK   3    ORIGIN FOR THE GROUP (A): -29.0486   0.8903   9.5564
REMARK   3    T TENSOR
REMARK   3      T11:   0.3029 T22:   1.2318
REMARK   3      T33:   0.5617 T12:   0.0078
REMARK   3      T13:   0.0624 T23:  -0.3362
REMARK   3    L TENSOR
REMARK   3      L11:   6.2780 L22:   4.4336
REMARK   3      L33:   1.4794 L12:   0.0945
REMARK   3      L13:  -1.3813 L23:  -1.4236
REMARK   3    S TENSOR
REMARK   3      S11:   0.0145 S12:  -1.0656 S13:  -0.6591
REMARK   3      S21:   0.0481 S22:   0.4339 S23:   0.2525
REMARK   3      S31:   0.0039 S32:  -0.0321 S33:  -0.2876
REMARK   3   TLS GROUP : 6
REMARK   3    SELECTION: chain 'A' and (resseq 556:571)
REMARK   3    ORIGIN FOR THE GROUP (A): -37.7858   5.0094   9.3495
REMARK   3    T TENSOR
REMARK   3      T11:   0.4440 T22:   1.5337
REMARK   3      T33:   0.8269 T12:  -0.0776
REMARK   3      T13:   0.4495 T23:  -0.4060
REMARK   3    L TENSOR
REMARK   3      L11:   1.7800 L22:   2.4949
REMARK   3      L33:   5.6872 L12:  -1.2507
REMARK   3      L13:   2.2469 L23:   0.5577
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2824 S12:  -0.4674 S13:  -0.1126
REMARK   3      S21:   0.4557 S22:   0.1272 S23:   0.9845
REMARK   3      S31:   0.8192 S32:  -1.1653 S33:   0.2016
REMARK   3   TLS GROUP : 7
REMARK   3    SELECTION: chain 'A' and (resseq 578:615)
REMARK   3    ORIGIN FOR THE GROUP (A): -30.1404   2.3219 -10.3838
REMARK   3    T TENSOR
REMARK   3      T11:   0.6295 T22:   1.2037
REMARK   3      T33:   1.1227 T12:   0.1275
REMARK   3      T13:  -0.0029 T23:  -0.2875
REMARK   3    L TENSOR
REMARK   3      L11:   1.9942 L22:   5.6441
REMARK   3      L33:   5.7304 L12:   1.2226
REMARK   3      L13:   1.6831 L23:  -3.5598
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1474 S12:   0.3929 S13:   0.7132
REMARK   3      S21:  -1.1453 S22:   0.3846 S23:   1.0272
REMARK   3      S31:   1.5216 S32:  -0.2436 S33:  -0.1549
REMARK   3   TLS GROUP : 8
REMARK   3    SELECTION: chain 'B' and (resseq 124:192)
REMARK   3    ORIGIN FOR THE GROUP (A): -29.7864  37.0701  -0.6993
REMARK   3    T TENSOR
REMARK   3      T11:   0.7778 T22:   0.9949
REMARK   3      T33:   1.6857 T12:   0.1944
REMARK   3      T13:   0.1284 T23:  -0.6405
REMARK   3    L TENSOR
REMARK   3      L11:   4.2555 L22:   0.8263
REMARK   3      L33:   2.6193 L12:   0.0693
REMARK   3      L13:  -0.2610 L23:  -1.4691
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1143 S12:  -0.5339 S13:   0.9398
REMARK   3      S21:   0.3256 S22:  -0.2610 S23:  -0.3236
REMARK   3      S31:  -0.8918 S32:  -0.5484 S33:   0.1843
REMARK   3   TLS GROUP : 9
REMARK   3    SELECTION: chain 'B' and (resseq 193:459)
REMARK   3    ORIGIN FOR THE GROUP (A): -48.4660  40.0216  -5.8794
REMARK   3    T TENSOR
REMARK   3      T11:   0.6326 T22:   1.1344
REMARK   3      T33:   1.6811 T12:   0.1720
REMARK   3      T13:   0.0580 T23:  -0.3895
REMARK   3    L TENSOR
REMARK   3      L11:   3.8111 L22:   1.5008
REMARK   3      L33:   2.8545 L12:  -0.5520
REMARK   3      L13:   0.2228 L23:  -1.6041
REMARK   3    S TENSOR
REMARK   3      S11:  -0.4458 S12:  -0.1961 S13:   0.8905
REMARK   3      S21:   0.2942 S22:   0.2500 S23:   0.4291
REMARK   3      S31:  -0.2191 S32:  -0.8190 S33:   0.2059
REMARK   3   TLS GROUP : 10
REMARK   3    SELECTION: chain 'B' and (resseq 460:555)
REMARK   3    ORIGIN FOR THE GROUP (A): -31.7094  36.5994 -12.8091
REMARK   3    T TENSOR
REMARK   3      T11:   0.3678 T22:   0.8233
REMARK   3      T33:   1.2846 T12:   0.1431
REMARK   3      T13:   0.0052 T23:  -0.1855
REMARK   3    L TENSOR
REMARK   3      L11:   4.0171 L22:   2.2267
REMARK   3      L33:   3.2854 L12:   1.8983
REMARK   3      L13:   0.0939 L23:   0.0339
REMARK   3    S TENSOR
REMARK   3      S11:  -0.3918 S12:   0.7648 S13:   0.8717
REMARK   3      S21:  -0.1418 S22:   0.2132 S23:   0.2348
REMARK   3      S31:  -0.0403 S32:   0.0202 S33:   0.2256
REMARK   3   TLS GROUP : 11
REMARK   3    SELECTION: chain 'B' and (resseq 556:571)
REMARK   3    ORIGIN FOR THE GROUP (A): -22.9601  34.6591  -9.0915
REMARK   3    T TENSOR
REMARK   3      T11:   0.4992 T22:   1.0001
REMARK   3      T33:   1.2772 T12:   0.0365
REMARK   3      T13:   0.1102 T23:  -0.4725
REMARK   3    L TENSOR
REMARK   3      L11:   4.1787 L22:   6.8838
REMARK   3      L33:   9.4454 L12:   5.2279
REMARK   3      L13:  -3.5929 L23:  -2.9801
REMARK   3    S TENSOR
REMARK   3      S11:   0.8736 S12:  -1.0908 S13:  -0.3165
REMARK   3      S21:  -0.3236 S22:  -1.4145 S23:   0.4902
REMARK   3      S31:  -0.6307 S32:   0.8389 S33:   0.3657
REMARK   3   TLS GROUP : 12
REMARK   3    SELECTION: chain 'B' and (resseq 578:615)
REMARK   3    ORIGIN FOR THE GROUP (A): -30.2551  18.1357 -20.2885
REMARK   3    T TENSOR
REMARK   3      T11:   0.5987 T22:   1.0741
REMARK   3      T33:   1.2159 T12:   0.1487
REMARK   3      T13:   0.0198 T23:  -0.0028
REMARK   3    L TENSOR
REMARK   3      L11:   7.7509 L22:   6.7195
REMARK   3      L33:   7.3003 L12:   5.0339
REMARK   3      L13:  -0.6924 L23:  -2.8852
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0978 S12:  -0.0145 S13:   0.2815
REMARK   3      S21:  -1.4470 S22:  -0.2147 S23:  -1.5780
REMARK   3      S31:   0.6299 S32:   0.2784 S33:   0.1714
REMARK   3   TLS GROUP : 13
REMARK   3    SELECTION: chain 'C' and (resseq 124:192)
REMARK   3    ORIGIN FOR THE GROUP (A):   1.6124  45.4824  44.3325
REMARK   3    T TENSOR
REMARK   3      T11:   2.3419 T22:   1.3745
REMARK   3      T33:   0.9424 T12:   0.3453
REMARK   3      T13:  -1.4162 T23:  -0.0531
REMARK   3    L TENSOR
REMARK   3      L11:   0.7092 L22:   1.6043
REMARK   3      L33:   4.1526 L12:  -0.4745
REMARK   3      L13:  -0.2135 L23:  -0.5854
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0034 S12:  -0.9986 S13:   0.0988
REMARK   3      S21:   1.2736 S22:   0.2431 S23:  -0.2699
REMARK   3      S31:  -0.0501 S32:   0.1358 S33:   0.1316
REMARK   3   TLS GROUP : 14
REMARK   3    SELECTION: chain 'C' and (resseq 193:229)
REMARK   3    ORIGIN FOR THE GROUP (A):   4.0910  40.8089  33.5700
REMARK   3    T TENSOR
REMARK   3      T11:   2.1071 T22:   1.4840
REMARK   3      T33:   1.4259 T12:   0.4349
REMARK   3      T13:  -0.8762 T23:  -0.4274
REMARK   3    L TENSOR
REMARK   3      L11:   2.7836 L22:   1.7851
REMARK   3      L33:   1.5863 L12:  -0.6720
REMARK   3      L13:   1.6765 L23:   0.5827
REMARK   3    S TENSOR
REMARK   3      S11:   0.1607 S12:  -0.2089 S13:  -0.4791
REMARK   3      S21:   1.1828 S22:   1.1248 S23:  -0.3286
REMARK   3      S31:   0.3046 S32:   0.7212 S33:  -0.8094
REMARK   3   TLS GROUP : 15
REMARK   3    SELECTION: chain 'C' and (resseq 230:300)
REMARK   3    ORIGIN FOR THE GROUP (A): -10.7224  46.2782  23.5817
REMARK   3    T TENSOR
REMARK   3      T11:   1.8857 T22:   1.0445
REMARK   3      T33:   0.8938 T12:   0.1275
REMARK   3      T13:  -0.6256 T23:  -0.1114
REMARK   3    L TENSOR
REMARK   3      L11:   4.6091 L22:   7.1559
REMARK   3      L33:   0.3026 L12:  -2.7172
REMARK   3      L13:  -0.1612 L23:   1.1422
REMARK   3    S TENSOR
REMARK   3      S11:   0.3883 S12:   0.0703 S13:  -0.9341
REMARK   3      S21:   0.8212 S22:   0.3328 S23:   0.0779
REMARK   3      S31:   0.2573 S32:   0.3327 S33:  -0.6161
REMARK   3   TLS GROUP : 16
REMARK   3    SELECTION: chain 'C' and (resseq 301:423)
REMARK   3    ORIGIN FOR THE GROUP (A): -15.5762  61.1529  34.3508
REMARK   3    T TENSOR
REMARK   3      T11:   1.7985 T22:   1.4121
REMARK   3      T33:   0.7107 T12:   0.0755
REMARK   3      T13:  -0.3040 T23:   0.1219
REMARK   3    L TENSOR
REMARK   3      L11:   2.3151 L22:   4.5858
REMARK   3      L33:   0.2505 L12:  -1.5681
REMARK   3      L13:  -0.7197 L23:   0.4383
REMARK   3    S TENSOR
REMARK   3      S11:  -0.3447 S12:  -0.2378 S13:   0.2922
REMARK   3      S21:   1.2612 S22:   0.3871 S23:  -0.4428
REMARK   3      S31:   0.4681 S32:  -0.6054 S33:  -0.0333
REMARK   3   TLS GROUP : 17
REMARK   3    SELECTION: chain 'C' and (resseq 424:506)
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.2278  61.9768  43.5357
REMARK   3    T TENSOR
REMARK   3      T11:   2.3471 T22:   0.9811
REMARK   3      T33:   1.0062 T12:   0.2936
REMARK   3      T13:  -0.7655 T23:  -0.0689
REMARK   3    L TENSOR
REMARK   3      L11:   4.1176 L22:   1.5661
REMARK   3      L33:   5.4099 L12:  -1.4787
REMARK   3      L13:   2.3728 L23:   0.4139
REMARK   3    S TENSOR
REMARK   3      S11:  -0.3385 S12:  -1.2402 S13:   0.4022
REMARK   3      S21:  -0.1518 S22:   0.4597 S23:  -0.2349
REMARK   3      S31:   1.0251 S32:  -0.9482 S33:  -0.0839
REMARK   3   TLS GROUP : 18
REMARK   3    SELECTION: chain 'C' and (resseq 507:555)
REMARK   3    ORIGIN FOR THE GROUP (A):   6.4828  53.7349  44.7501
REMARK   3    T TENSOR
REMARK   3      T11:   2.2979 T22:   1.2454
REMARK   3      T33:   1.3588 T12:   0.2110
REMARK   3      T13:  -1.3827 T23:  -0.4824
REMARK   3    L TENSOR
REMARK   3      L11:   2.7572 L22:   1.1730
REMARK   3      L33:   2.4735 L12:   0.5475
REMARK   3      L13:   1.2244 L23:   0.1625
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0497 S12:  -1.1716 S13:  -0.0098
REMARK   3      S21:   0.6026 S22:   0.0699 S23:  -0.5157
REMARK   3      S31:  -0.6892 S32:   0.0176 S33:  -0.1037
REMARK   3   TLS GROUP : 19
REMARK   3    SELECTION: chain 'C' and (resseq 556:571)
REMARK   3    ORIGIN FOR THE GROUP (A):   8.0807  52.2700  50.1131
REMARK   3    T TENSOR
REMARK   3      T11:   2.8091 T22:   1.1678
REMARK   3      T33:   1.0981 T12:   0.6682
REMARK   3      T13:  -0.8990 T23:  -0.2562
REMARK   3    L TENSOR
REMARK   3      L11:   5.7393 L22:   2.1488
REMARK   3      L33:   9.6983 L12:  -0.2380
REMARK   3      L13:   3.7398 L23:   2.7475
REMARK   3    S TENSOR
REMARK   3      S11:  -0.3929 S12:  -0.7799 S13:   0.1813
REMARK   3      S21:   0.4823 S22:   0.9382 S23:   0.0530
REMARK   3      S31:  -1.5312 S32:  -0.5229 S33:  -0.0910
REMARK   3   TLS GROUP : 20
REMARK   3    SELECTION: chain 'C' and (resseq 578:615)
REMARK   3    ORIGIN FOR THE GROUP (A):  18.5978  65.2958  36.5536
REMARK   3    T TENSOR
REMARK   3      T11:   1.5662 T22:   0.9203
REMARK   3      T33:   2.0894 T12:   0.9530
REMARK   3      T13:  -0.9259 T23:  -0.2674
REMARK   3    L TENSOR
REMARK   3      L11:   4.6697 L22:   0.5713
REMARK   3      L33:   2.2845 L12:   0.0983
REMARK   3      L13:  -0.9383 L23:  -1.1238
REMARK   3    S TENSOR
REMARK   3      S11:   0.9701 S12:  -0.7345 S13:   0.4165
REMARK   3      S21:   1.4733 S22:   0.1463 S23:  -1.4057
REMARK   3      S31:   0.6119 S32:   1.2127 S33:  -0.1883
REMARK   3   TLS GROUP : 21
REMARK   3    SELECTION: chain 'D' and (resseq 124:192)
REMARK   3    ORIGIN FOR THE GROUP (A):  20.1669  31.0343  25.5072
REMARK   3    T TENSOR
REMARK   3      T11:   2.3290 T22:   1.5718
REMARK   3      T33:   2.2262 T12:   0.7327
REMARK   3      T13:  -1.1312 T23:  -0.3901
REMARK   3    L TENSOR
REMARK   3      L11:   0.1408 L22:   3.2925
REMARK   3      L33:   1.6479 L12:   0.3842
REMARK   3      L13:  -0.3968 L23:  -0.1519
REMARK   3    S TENSOR
REMARK   3      S11:   0.6082 S12:   0.3683 S13:  -0.6980
REMARK   3      S21:  -0.6868 S22:  -0.5841 S23:  -0.8254
REMARK   3      S31:   0.5970 S32:   0.4057 S33:  -0.0126
REMARK   3   TLS GROUP : 22
REMARK   3    SELECTION: chain 'D' and (resseq 193:459)
REMARK   3    ORIGIN FOR THE GROUP (A):  35.6088  26.7762  36.8947
REMARK   3    T TENSOR
REMARK   3      T11:   1.9293 T22:   1.2576
REMARK   3      T33:   2.3685 T12:   1.0606
REMARK   3      T13:  -1.4477 T23:  -0.3226
REMARK   3    L TENSOR
REMARK   3      L11:   1.7451 L22:   0.3302
REMARK   3      L33:   0.9659 L12:  -0.5293
REMARK   3      L13:  -0.2126 L23:   0.4740
REMARK   3    S TENSOR
REMARK   3      S11:   0.0049 S12:   0.1831 S13:  -0.3574
REMARK   3      S21:   0.3947 S22:   0.1982 S23:  -0.7782
REMARK   3      S31:   0.2632 S32:   0.8303 S33:  -0.0290
REMARK   3   TLS GROUP : 23
REMARK   3    SELECTION: chain 'D' and (resseq 460:555)
REMARK   3    ORIGIN FOR THE GROUP (A):  30.5365  36.5129  22.0024
REMARK   3    T TENSOR
REMARK   3      T11:   1.5333 T22:   1.4813
REMARK   3      T33:   2.3557 T12:   0.6344
REMARK   3      T13:  -0.6708 T23:  -0.4946
REMARK   3    L TENSOR
REMARK   3      L11:   0.8996 L22:   2.2355
REMARK   3      L33:   0.9746 L12:   0.3820
REMARK   3      L13:  -0.1798 L23:  -1.4125
REMARK   3    S TENSOR
REMARK   3      S11:   0.1767 S12:   0.3313 S13:  -0.3191
REMARK   3      S21:   0.7061 S22:   0.3344 S23:  -1.4865
REMARK   3      S31:   0.2931 S32:   1.1311 S33:  -0.4900
REMARK   3   TLS GROUP : 24
REMARK   3    SELECTION: chain 'D' and (resseq 556:571)
REMARK   3    ORIGIN FOR THE GROUP (A):  22.1630  38.2618  17.3037
REMARK   3    T TENSOR
REMARK   3      T11:   1.7462 T22:   1.7629
REMARK   3      T33:   2.3843 T12:   0.3417
REMARK   3      T13:  -0.5888 T23:  -0.1078
REMARK   3    L TENSOR
REMARK   3      L11:   4.1816 L22:   7.1621
REMARK   3      L33:   7.1419 L12:  -5.4813
REMARK   3      L13:  -5.4631 L23:   7.1520
REMARK   3    S TENSOR
REMARK   3      S11:   0.6680 S12:   1.7171 S13:   1.3078
REMARK   3      S21:  -1.2359 S22:  -0.9404 S23:  -0.7474
REMARK   3      S31:  -2.2522 S32:  -2.6688 S33:   0.4645
REMARK   3   TLS GROUP : 25
REMARK   3    SELECTION: chain 'D' and (resseq 578:615)
REMARK   3    ORIGIN FOR THE GROUP (A):  30.6017  56.1943  25.6525
REMARK   3    T TENSOR
REMARK   3      T11:   1.5776 T22:   1.8864
REMARK   3      T33:   2.5769 T12:   0.6562
REMARK   3      T13:  -0.5699 T23:  -0.3607
REMARK   3    L TENSOR
REMARK   3      L11:   1.1582 L22:   3.1993
REMARK   3      L33:   4.5752 L12:   0.7076
REMARK   3      L13:  -0.8268 L23:   2.8310
REMARK   3    S TENSOR
REMARK   3      S11:   0.2182 S12:  -0.2180 S13:   0.9745
REMARK   3      S21:  -1.1225 S22:   0.0176 S23:  -1.4143
REMARK   3      S31:  -0.1747 S32:   0.0162 S33:  -0.1850
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 4FZH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUL-12.
REMARK 100 THE RCSB ID CODE IS RCSB073546.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 16-FEB-11
REMARK 200  TEMPERATURE           (KELVIN) : 77.2
REMARK 200  PH                             : 7.5
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-E
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97916
REMARK 200  MONOCHROMATOR                  : CRYO-COOLED DOUBLE CRYSTAL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33126
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.913
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
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: CCP4, PHASER FOR MR
REMARK 200 STARTING MODEL: PDB ENTRY 1E8T
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 54.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 17% PEG 8000, 200 MM MGCL2, 100 MM
REMARK 280  TRIS, PH 7.5, EVAPORATION, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+1/3
REMARK 290       3555   -X+Y,-X,Z+2/3
REMARK 290       4555   Y,X,-Z
REMARK 290       5555   X-Y,-Y,-Z+2/3
REMARK 290       6555   -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       94.97133
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      189.94267
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      189.94267
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       94.97133
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5460 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET A    81
REMARK 465     GLY A    82
REMARK 465     ILE A    83
REMARK 465     LEU A    84
REMARK 465     PRO A    85
REMARK 465     SER A    86
REMARK 465     PRO A    87
REMARK 465     GLY A    88
REMARK 465     MET A    89
REMARK 465     PRO A    90
REMARK 465     ALA A    91
REMARK 465     LEU A    92
REMARK 465     LEU A    93
REMARK 465     SER A    94
REMARK 465     LEU A    95
REMARK 465     VAL A    96
REMARK 465     SER A    97
REMARK 465     LEU A    98
REMARK 465     LEU A    99
REMARK 465     SER A   100
REMARK 465     VAL A   101
REMARK 465     LEU A   102
REMARK 465     LEU A   103
REMARK 465     MET A   104
REMARK 465     GLY A   105
REMARK 465     CYS A   106
REMARK 465     VAL A   107
REMARK 465     ALA A   108
REMARK 465     GLU A   109
REMARK 465     THR A   110
REMARK 465     GLY A   111
REMARK 465     HIS A   112
REMARK 465     HIS A   113
REMARK 465     HIS A   114
REMARK 465     HIS A   115
REMARK 465     HIS A   116
REMARK 465     HIS A   117
REMARK 465     LEU A   118
REMARK 465     VAL A   119
REMARK 465     PRO A   120
REMARK 465     ARG A   121
REMARK 465     GLY A   122
REMARK 465     SER A   123
REMARK 465     ARG A   572
REMARK 465     GLU A   573
REMARK 465     ALA A   574
REMARK 465     ARG A   575
REMARK 465     ALA A   576
REMARK 465     GLY A   577
REMARK 465     PRO A   616
REMARK 465     MET B    81
REMARK 465     GLY B    82
REMARK 465     ILE B    83
REMARK 465     LEU B    84
REMARK 465     PRO B    85
REMARK 465     SER B    86
REMARK 465     PRO B    87
REMARK 465     GLY B    88
REMARK 465     MET B    89
REMARK 465     PRO B    90
REMARK 465     ALA B    91
REMARK 465     LEU B    92
REMARK 465     LEU B    93
REMARK 465     SER B    94
REMARK 465     LEU B    95
REMARK 465     VAL B    96
REMARK 465     SER B    97
REMARK 465     LEU B    98
REMARK 465     LEU B    99
REMARK 465     SER B   100
REMARK 465     VAL B   101
REMARK 465     LEU B   102
REMARK 465     LEU B   103
REMARK 465     MET B   104
REMARK 465     GLY B   105
REMARK 465     CYS B   106
REMARK 465     VAL B   107
REMARK 465     ALA B   108
REMARK 465     GLU B   109
REMARK 465     THR B   110
REMARK 465     GLY B   111
REMARK 465     HIS B   112
REMARK 465     HIS B   113
REMARK 465     HIS B   114
REMARK 465     HIS B   115
REMARK 465     HIS B   116
REMARK 465     HIS B   117
REMARK 465     LEU B   118
REMARK 465     VAL B   119
REMARK 465     PRO B   120
REMARK 465     ARG B   121
REMARK 465     GLY B   122
REMARK 465     SER B   123
REMARK 465     ARG B   572
REMARK 465     GLU B   573
REMARK 465     ALA B   574
REMARK 465     ARG B   575
REMARK 465     ALA B   576
REMARK 465     GLY B   577
REMARK 465     PRO B   616
REMARK 465     MET C    81
REMARK 465     GLY C    82
REMARK 465     ILE C    83
REMARK 465     LEU C    84
REMARK 465     PRO C    85
REMARK 465     SER C    86
REMARK 465     PRO C    87
REMARK 465     GLY C    88
REMARK 465     MET C    89
REMARK 465     PRO C    90
REMARK 465     ALA C    91
REMARK 465     LEU C    92
REMARK 465     LEU C    93
REMARK 465     SER C    94
REMARK 465     LEU C    95
REMARK 465     VAL C    96
REMARK 465     SER C    97
REMARK 465     LEU C    98
REMARK 465     LEU C    99
REMARK 465     SER C   100
REMARK 465     VAL C   101
REMARK 465     LEU C   102
REMARK 465     LEU C   103
REMARK 465     MET C   104
REMARK 465     GLY C   105
REMARK 465     CYS C   106
REMARK 465     VAL C   107
REMARK 465     ALA C   108
REMARK 465     GLU C   109
REMARK 465     THR C   110
REMARK 465     GLY C   111
REMARK 465     HIS C   112
REMARK 465     HIS C   113
REMARK 465     HIS C   114
REMARK 465     HIS C   115
REMARK 465     HIS C   116
REMARK 465     HIS C   117
REMARK 465     LEU C   118
REMARK 465     VAL C   119
REMARK 465     PRO C   120
REMARK 465     ARG C   121
REMARK 465     GLY C   122
REMARK 465     SER C   123
REMARK 465     ARG C   572
REMARK 465     GLU C   573
REMARK 465     ALA C   574
REMARK 465     ARG C   575
REMARK 465     ALA C   576
REMARK 465     GLY C   577
REMARK 465     PRO C   616
REMARK 465     MET D    81
REMARK 465     GLY D    82
REMARK 465     ILE D    83
REMARK 465     LEU D    84
REMARK 465     PRO D    85
REMARK 465     SER D    86
REMARK 465     PRO D    87
REMARK 465     GLY D    88
REMARK 465     MET D    89
REMARK 465     PRO D    90
REMARK 465     ALA D    91
REMARK 465     LEU D    92
REMARK 465     LEU D    93
REMARK 465     SER D    94
REMARK 465     LEU D    95
REMARK 465     VAL D    96
REMARK 465     SER D    97
REMARK 465     LEU D    98
REMARK 465     LEU D    99
REMARK 465     SER D   100
REMARK 465     VAL D   101
REMARK 465     LEU D   102
REMARK 465     LEU D   103
REMARK 465     MET D   104
REMARK 465     GLY D   105
REMARK 465     CYS D   106
REMARK 465     VAL D   107
REMARK 465     ALA D   108
REMARK 465     GLU D   109
REMARK 465     THR D   110
REMARK 465     GLY D   111
REMARK 465     HIS D   112
REMARK 465     HIS D   113
REMARK 465     HIS D   114
REMARK 465     HIS D   115
REMARK 465     HIS D   116
REMARK 465     HIS D   117
REMARK 465     LEU D   118
REMARK 465     VAL D   119
REMARK 465     PRO D   120
REMARK 465     ARG D   121
REMARK 465     GLY D   122
REMARK 465     SER D   123
REMARK 465     ARG D   572
REMARK 465     GLU D   573
REMARK 465     ALA D   574
REMARK 465     ARG D   575
REMARK 465     ALA D   576
REMARK 465     GLY D   577
REMARK 465     PRO D   616
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 578    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LEU A 579    CG   CD1  CD2
REMARK 470     SER A 580    OG
REMARK 470     GLN A 581    CG   CD   OE1  NE2
REMARK 470     LEU A 582    CG   CD1  CD2
REMARK 470     ARG A 583    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG B 578    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LEU B 579    CG   CD1  CD2
REMARK 470     SER B 580    OG
REMARK 470     GLN B 581    CG   CD   OE1  NE2
REMARK 470     LEU B 582    CG   CD1  CD2
REMARK 470     ARG B 583    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG C 578    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LEU C 579    CG   CD1  CD2
REMARK 470     SER C 580    OG
REMARK 470     GLN C 581    CG   CD   OE1  NE2
REMARK 470     LEU C 582    CG   CD1  CD2
REMARK 470     ARG C 583    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG D 578    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LEU D 579    CG   CD1  CD2
REMARK 470     SER D 580    OG
REMARK 470     GLN D 581    CG   CD   OE1  NE2
REMARK 470     LEU D 582    CG   CD1  CD2
REMARK 470     ARG D 583    CG   CD   NE   CZ   NH1  NH2
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   OG   SER D   239     O    GLY D   303              1.75
REMARK 500   OG   SER D   452     OG1  THR D   467              1.89
REMARK 500   OD2  ASP A   261     OG   SER A   264              1.97
REMARK 500   O    GLY D   468     NH2  ARG D   498              2.02
REMARK 500   N    SER B   519     O    LYS B   587              2.02
REMARK 500   OH   TYR D   337     O    VAL D   395              2.04
REMARK 500   OE2  GLU B   331     NH2  ARG B   368              2.06
REMARK 500   OD2  ASP C   261     OG   SER C   264              2.06
REMARK 500   O    ASP B   147     OG   SER B   150              2.07
REMARK 500   O    ASP A   147     OG   SER A   150              2.08
REMARK 500   OG1  THR C   490     OG   SER C   503              2.09
REMARK 500   OH   TYR D   470     OD2  ASP D   472              2.11
REMARK 500   ND2  ASN B   341     C2   NAG B   701              2.11
REMARK 500   ND2  ASN C   433     C2   NAG C   701              2.12
REMARK 500   OE1  GLN D   233     NZ   LYS D   253              2.15
REMARK 500   OD1  ASP C   494     NH2  ARG C   605              2.15
REMARK 500   OE2  GLU C   331     NH2  ARG C   368              2.15
REMARK 500   N    SER D   519     O    LYS D   587              2.17
REMARK 500   NH2  ARG B   416     O    GLY B   468              2.19
REMARK 500   OG1  THR B   188     O    TYR B   205              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   NH2  ARG B   353     OE2  GLU C   609     4455     2.14
REMARK 500   NH2  ARG A   353     OE2  GLU A   609     4555     2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    ILE A 127     -143.35     51.99
REMARK 500    THR A 167      -57.89   -121.54
REMARK 500    SER A 170      -79.27   -122.43
REMARK 500    ILE A 175       70.32     59.23
REMARK 500    THR A 183      -65.59   -103.43
REMARK 500    VAL A 302     -106.82     57.49
REMARK 500    ASN A 341       -7.60     65.98
REMARK 500    VAL A 395      -70.16   -124.18
REMARK 500    SER A 418       -8.22    -57.23
REMARK 500    SER A 419     -163.46   -127.10
REMARK 500    LYS A 434      -13.01     68.93
REMARK 500    HIS A 482       -5.47     83.87
REMARK 500    ASP A 494      157.95    174.79
REMARK 500    GLN A 496      -73.18   -102.57
REMARK 500    ILE A 509      -60.90    -99.43
REMARK 500    SER A 520     -142.89     48.27
REMARK 500    ALA A 525     -158.87   -155.67
REMARK 500    THR A 551     -115.36     53.26
REMARK 500    PHE A 553        2.89     84.71
REMARK 500    GLU A 555      -14.91     79.18
REMARK 500    SER A 580       36.33     73.02
REMARK 500    PRO A 593     -159.97    -84.98
REMARK 500    ILE A 594      -22.74     93.22
REMARK 500    CYS A 596      -42.44   -142.37
REMARK 500    ASP A 597       -0.67     82.23
REMARK 500    ALA A 598     -142.52     58.71
REMARK 500    GLN A 601       -8.93    -56.57
REMARK 500    SER A 614     -164.48   -166.90
REMARK 500    ILE B 127     -142.00     53.57
REMARK 500    SER B 170      -75.57   -119.05
REMARK 500    ILE B 175       66.10     63.43
REMARK 500    ASP B 231     -179.73    -68.44
REMARK 500    VAL B 302     -109.21     61.37
REMARK 500    ASN B 310       20.00     57.26
REMARK 500    ARG B 339      -73.61    -57.95
REMARK 500    TYR B 340     -159.52   -166.31
REMARK 500    ASP B 385       62.72     60.71
REMARK 500    VAL B 395      -70.58   -120.30
REMARK 500    ALA B 400     -179.75   -170.38
REMARK 500    SER B 418       -8.19    -55.58
REMARK 500    TYR B 420       -8.58    -59.13
REMARK 500    LYS B 434      -10.48     64.99
REMARK 500    THR B 467     -161.98   -160.13
REMARK 500    LEU B 476      -62.69   -130.29
REMARK 500    ARG B 485      -54.18   -123.16
REMARK 500    ASP B 494      158.41    176.53
REMARK 500    GLN B 496      -62.43   -103.39
REMARK 500    ASN B 500       72.40     50.53
REMARK 500    ASP B 507     -169.22   -127.00
REMARK 500    ILE B 509      -61.57   -106.76
REMARK 500
REMARK 500 THIS ENTRY HAS     119 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 ALA A  613     SER A  614                 -145.17
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    ILE A 594        24.8      L          L   OUTSIDE RANGE
REMARK 500    ILE B 594        23.6      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 704
DBREF  4FZH A  124   616  UNP    P12558   HN_NDVU        124    616
DBREF  4FZH B  124   616  UNP    P12558   HN_NDVU        124    616
DBREF  4FZH C  124   616  UNP    P12558   HN_NDVU        124    616
DBREF  4FZH D  124   616  UNP    P12558   HN_NDVU        124    616
SEQADV 4FZH MET A   81  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH GLY A   82  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH ILE A   83  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH LEU A   84  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH PRO A   85  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH SER A   86  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH PRO A   87  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH GLY A   88  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH MET A   89  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH PRO A   90  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH ALA A   91  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH LEU A   92  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH LEU A   93  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH SER A   94  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH LEU A   95  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH VAL A   96  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH SER A   97  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH LEU A   98  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH LEU A   99  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH SER A  100  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH VAL A  101  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH LEU A  102  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH LEU A  103  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH MET A  104  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH GLY A  105  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH CYS A  106  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH VAL A  107  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH ALA A  108  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH GLU A  109  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH THR A  110  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH GLY A  111  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH HIS A  112  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH HIS A  113  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH HIS A  114  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH HIS A  115  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH HIS A  116  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH HIS A  117  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH LEU A  118  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH VAL A  119  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH PRO A  120  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH ARG A  121  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH GLY A  122  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH SER A  123  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH MET B   81  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH GLY B   82  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH ILE B   83  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH LEU B   84  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH PRO B   85  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH SER B   86  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH PRO B   87  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH GLY B   88  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH MET B   89  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH PRO B   90  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH ALA B   91  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH LEU B   92  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH LEU B   93  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH SER B   94  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH LEU B   95  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH VAL B   96  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH SER B   97  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH LEU B   98  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH LEU B   99  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH SER B  100  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH VAL B  101  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH LEU B  102  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH LEU B  103  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH MET B  104  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH GLY B  105  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH CYS B  106  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH VAL B  107  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH ALA B  108  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH GLU B  109  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH THR B  110  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH GLY B  111  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH HIS B  112  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH HIS B  113  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH HIS B  114  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH HIS B  115  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH HIS B  116  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH HIS B  117  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH LEU B  118  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH VAL B  119  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH PRO B  120  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH ARG B  121  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH GLY B  122  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH SER B  123  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH MET C   81  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH GLY C   82  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH ILE C   83  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH LEU C   84  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH PRO C   85  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH SER C   86  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH PRO C   87  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH GLY C   88  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH MET C   89  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH PRO C   90  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH ALA C   91  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH LEU C   92  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH LEU C   93  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH SER C   94  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH LEU C   95  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH VAL C   96  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH SER C   97  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH LEU C   98  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH LEU C   99  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH SER C  100  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH VAL C  101  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH LEU C  102  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH LEU C  103  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH MET C  104  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH GLY C  105  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH CYS C  106  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH VAL C  107  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH ALA C  108  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH GLU C  109  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH THR C  110  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH GLY C  111  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH HIS C  112  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH HIS C  113  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH HIS C  114  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH HIS C  115  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH HIS C  116  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH HIS C  117  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH LEU C  118  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH VAL C  119  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH PRO C  120  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH ARG C  121  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH GLY C  122  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH SER C  123  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH MET D   81  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH GLY D   82  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH ILE D   83  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH LEU D   84  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH PRO D   85  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH SER D   86  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH PRO D   87  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH GLY D   88  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH MET D   89  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH PRO D   90  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH ALA D   91  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH LEU D   92  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH LEU D   93  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH SER D   94  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH LEU D   95  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH VAL D   96  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH SER D   97  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH LEU D   98  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH LEU D   99  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH SER D  100  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH VAL D  101  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH LEU D  102  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH LEU D  103  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH MET D  104  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH GLY D  105  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH CYS D  106  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH VAL D  107  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH ALA D  108  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH GLU D  109  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH THR D  110  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH GLY D  111  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH HIS D  112  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH HIS D  113  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH HIS D  114  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH HIS D  115  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH HIS D  116  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH HIS D  117  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH LEU D  118  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH VAL D  119  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH PRO D  120  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH ARG D  121  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH GLY D  122  UNP  P12558              EXPRESSION TAG
SEQADV 4FZH SER D  123  UNP  P12558              EXPRESSION TAG
SEQRES   1 A  536  MET GLY ILE LEU PRO SER PRO GLY MET PRO ALA LEU LEU
SEQRES   2 A  536  SER LEU VAL SER LEU LEU SER VAL LEU LEU MET GLY CYS
SEQRES   3 A  536  VAL ALA GLU THR GLY HIS HIS HIS HIS HIS HIS LEU VAL
SEQRES   4 A  536  PRO ARG GLY SER GLY ALA PRO ILE HIS ASP PRO ASP TYR
SEQRES   5 A  536  ILE GLY GLY ILE GLY LYS GLU LEU ILE VAL ASP ASP ALA
SEQRES   6 A  536  SER ASP VAL THR SER PHE TYR PRO SER ALA PHE GLN GLU
SEQRES   7 A  536  HIS LEU ASN PHE ILE PRO ALA PRO THR THR GLY SER GLY
SEQRES   8 A  536  CYS THR ARG ILE PRO SER PHE ASP MET SER ALA THR HIS
SEQRES   9 A  536  TYR CYS TYR THR HIS ASN VAL ILE LEU SER GLY CYS ARG
SEQRES  10 A  536  ASP HIS SER HIS SER HIS GLN TYR LEU ALA LEU GLY VAL
SEQRES  11 A  536  LEU ARG THR SER ALA THR GLY ARG VAL PHE PHE SER THR
SEQRES  12 A  536  LEU HIS SER ILE ASN LEU ASP ASP THR GLN ASN ARG LYS
SEQRES  13 A  536  SER CYS SER VAL SER ALA THR PRO LEU GLY CYS ASP MET
SEQRES  14 A  536  LEU CYS SER LYS VAL THR GLU THR GLU GLU GLU ASP TYR
SEQRES  15 A  536  ASN SER ALA VAL PRO THR SER MET VAL HIS GLY ARG LEU
SEQRES  16 A  536  GLY PHE ASP GLY GLN TYR HIS GLU LYS ASP LEU ASP VAL
SEQRES  17 A  536  THR THR LEU PHE GLU ASP TRP VAL ALA ASN TYR PRO GLY
SEQRES  18 A  536  VAL GLY GLY GLY SER PHE ILE ASP ASN ARG VAL TRP PHE
SEQRES  19 A  536  PRO VAL TYR GLY GLY LEU LYS PRO ASN SER PRO SER ASP
SEQRES  20 A  536  THR ALA GLN GLU GLY LYS TYR VAL ILE TYR LYS ARG TYR
SEQRES  21 A  536  ASN ASP THR CYS PRO ASP GLU GLN ASP TYR GLN ILE ARG
SEQRES  22 A  536  MET ALA LYS SER SER TYR LYS PRO GLY ARG PHE GLY GLY
SEQRES  23 A  536  LYS ARG VAL GLN GLN ALA ILE LEU SER ILE LYS VAL SER
SEQRES  24 A  536  THR SER LEU GLY GLU ASP PRO VAL LEU THR VAL PRO PRO
SEQRES  25 A  536  ASN THR VAL THR LEU MET GLY ALA GLU GLY ARG VAL LEU
SEQRES  26 A  536  THR VAL GLY THR SER HIS PHE LEU TYR GLN ARG GLY SER
SEQRES  27 A  536  SER TYR PHE SER PRO ALA LEU LEU TYR PRO MET THR VAL
SEQRES  28 A  536  SER ASN LYS THR ALA THR LEU HIS SER PRO TYR THR PHE
SEQRES  29 A  536  ASP ALA PHE THR ARG PRO GLY SER VAL PRO CYS GLN ALA
SEQRES  30 A  536  SER ALA ARG CYS PRO ASN SER CYS VAL THR GLY VAL TYR
SEQRES  31 A  536  THR ASP PRO TYR PRO LEU VAL PHE TYR ARG ASN HIS THR
SEQRES  32 A  536  LEU ARG GLY VAL PHE GLY THR MET LEU ASP ASP LYS GLN
SEQRES  33 A  536  ALA ARG LEU ASN PRO VAL SER ALA VAL PHE ASP SER ILE
SEQRES  34 A  536  SER ARG SER ARG ILE THR ARG VAL SER SER SER SER THR
SEQRES  35 A  536  LYS ALA ALA TYR THR THR SER THR CYS PHE LYS VAL VAL
SEQRES  36 A  536  LYS THR ASN LYS THR TYR CYS LEU SER ILE ALA GLU ILE
SEQRES  37 A  536  SER ASN THR LEU PHE GLY GLU PHE ARG ILE VAL PRO LEU
SEQRES  38 A  536  LEU VAL GLU ILE LEU LYS ASP ASP GLY VAL ARG GLU ALA
SEQRES  39 A  536  ARG ALA GLY ARG LEU SER GLN LEU ARG GLU GLY TRP LYS
SEQRES  40 A  536  ASP ASP ILE VAL SER PRO ILE PHE CYS ASP ALA LYS ASN
SEQRES  41 A  536  GLN THR GLU TYR ARG ARG GLU LEU GLU SER TYR ALA ALA
SEQRES  42 A  536  SER TRP PRO
SEQRES   1 B  536  MET GLY ILE LEU PRO SER PRO GLY MET PRO ALA LEU LEU
SEQRES   2 B  536  SER LEU VAL SER LEU LEU SER VAL LEU LEU MET GLY CYS
SEQRES   3 B  536  VAL ALA GLU THR GLY HIS HIS HIS HIS HIS HIS LEU VAL
SEQRES   4 B  536  PRO ARG GLY SER GLY ALA PRO ILE HIS ASP PRO ASP TYR
SEQRES   5 B  536  ILE GLY GLY ILE GLY LYS GLU LEU ILE VAL ASP ASP ALA
SEQRES   6 B  536  SER ASP VAL THR SER PHE TYR PRO SER ALA PHE GLN GLU
SEQRES   7 B  536  HIS LEU ASN PHE ILE PRO ALA PRO THR THR GLY SER GLY
SEQRES   8 B  536  CYS THR ARG ILE PRO SER PHE ASP MET SER ALA THR HIS
SEQRES   9 B  536  TYR CYS TYR THR HIS ASN VAL ILE LEU SER GLY CYS ARG
SEQRES  10 B  536  ASP HIS SER HIS SER HIS GLN TYR LEU ALA LEU GLY VAL
SEQRES  11 B  536  LEU ARG THR SER ALA THR GLY ARG VAL PHE PHE SER THR
SEQRES  12 B  536  LEU HIS SER ILE ASN LEU ASP ASP THR GLN ASN ARG LYS
SEQRES  13 B  536  SER CYS SER VAL SER ALA THR PRO LEU GLY CYS ASP MET
SEQRES  14 B  536  LEU CYS SER LYS VAL THR GLU THR GLU GLU GLU ASP TYR
SEQRES  15 B  536  ASN SER ALA VAL PRO THR SER MET VAL HIS GLY ARG LEU
SEQRES  16 B  536  GLY PHE ASP GLY GLN TYR HIS GLU LYS ASP LEU ASP VAL
SEQRES  17 B  536  THR THR LEU PHE GLU ASP TRP VAL ALA ASN TYR PRO GLY
SEQRES  18 B  536  VAL GLY GLY GLY SER PHE ILE ASP ASN ARG VAL TRP PHE
SEQRES  19 B  536  PRO VAL TYR GLY GLY LEU LYS PRO ASN SER PRO SER ASP
SEQRES  20 B  536  THR ALA GLN GLU GLY LYS TYR VAL ILE TYR LYS ARG TYR
SEQRES  21 B  536  ASN ASP THR CYS PRO ASP GLU GLN ASP TYR GLN ILE ARG
SEQRES  22 B  536  MET ALA LYS SER SER TYR LYS PRO GLY ARG PHE GLY GLY
SEQRES  23 B  536  LYS ARG VAL GLN GLN ALA ILE LEU SER ILE LYS VAL SER
SEQRES  24 B  536  THR SER LEU GLY GLU ASP PRO VAL LEU THR VAL PRO PRO
SEQRES  25 B  536  ASN THR VAL THR LEU MET GLY ALA GLU GLY ARG VAL LEU
SEQRES  26 B  536  THR VAL GLY THR SER HIS PHE LEU TYR GLN ARG GLY SER
SEQRES  27 B  536  SER TYR PHE SER PRO ALA LEU LEU TYR PRO MET THR VAL
SEQRES  28 B  536  SER ASN LYS THR ALA THR LEU HIS SER PRO TYR THR PHE
SEQRES  29 B  536  ASP ALA PHE THR ARG PRO GLY SER VAL PRO CYS GLN ALA
SEQRES  30 B  536  SER ALA ARG CYS PRO ASN SER CYS VAL THR GLY VAL TYR
SEQRES  31 B  536  THR ASP PRO TYR PRO LEU VAL PHE TYR ARG ASN HIS THR
SEQRES  32 B  536  LEU ARG GLY VAL PHE GLY THR MET LEU ASP ASP LYS GLN
SEQRES  33 B  536  ALA ARG LEU ASN PRO VAL SER ALA VAL PHE ASP SER ILE
SEQRES  34 B  536  SER ARG SER ARG ILE THR ARG VAL SER SER SER SER THR
SEQRES  35 B  536  LYS ALA ALA TYR THR THR SER THR CYS PHE LYS VAL VAL
SEQRES  36 B  536  LYS THR ASN LYS THR TYR CYS LEU SER ILE ALA GLU ILE
SEQRES  37 B  536  SER ASN THR LEU PHE GLY GLU PHE ARG ILE VAL PRO LEU
SEQRES  38 B  536  LEU VAL GLU ILE LEU LYS ASP ASP GLY VAL ARG GLU ALA
SEQRES  39 B  536  ARG ALA GLY ARG LEU SER GLN LEU ARG GLU GLY TRP LYS
SEQRES  40 B  536  ASP ASP ILE VAL SER PRO ILE PHE CYS ASP ALA LYS ASN
SEQRES  41 B  536  GLN THR GLU TYR ARG ARG GLU LEU GLU SER TYR ALA ALA
SEQRES  42 B  536  SER TRP PRO
SEQRES   1 C  536  MET GLY ILE LEU PRO SER PRO GLY MET PRO ALA LEU LEU
SEQRES   2 C  536  SER LEU VAL SER LEU LEU SER VAL LEU LEU MET GLY CYS
SEQRES   3 C  536  VAL ALA GLU THR GLY HIS HIS HIS HIS HIS HIS LEU VAL
SEQRES   4 C  536  PRO ARG GLY SER GLY ALA PRO ILE HIS ASP PRO ASP TYR
SEQRES   5 C  536  ILE GLY GLY ILE GLY LYS GLU LEU ILE VAL ASP ASP ALA
SEQRES   6 C  536  SER ASP VAL THR SER PHE TYR PRO SER ALA PHE GLN GLU
SEQRES   7 C  536  HIS LEU ASN PHE ILE PRO ALA PRO THR THR GLY SER GLY
SEQRES   8 C  536  CYS THR ARG ILE PRO SER PHE ASP MET SER ALA THR HIS
SEQRES   9 C  536  TYR CYS TYR THR HIS ASN VAL ILE LEU SER GLY CYS ARG
SEQRES  10 C  536  ASP HIS SER HIS SER HIS GLN TYR LEU ALA LEU GLY VAL
SEQRES  11 C  536  LEU ARG THR SER ALA THR GLY ARG VAL PHE PHE SER THR
SEQRES  12 C  536  LEU HIS SER ILE ASN LEU ASP ASP THR GLN ASN ARG LYS
SEQRES  13 C  536  SER CYS SER VAL SER ALA THR PRO LEU GLY CYS ASP MET
SEQRES  14 C  536  LEU CYS SER LYS VAL THR GLU THR GLU GLU GLU ASP TYR
SEQRES  15 C  536  ASN SER ALA VAL PRO THR SER MET VAL HIS GLY ARG LEU
SEQRES  16 C  536  GLY PHE ASP GLY GLN TYR HIS GLU LYS ASP LEU ASP VAL
SEQRES  17 C  536  THR THR LEU PHE GLU ASP TRP VAL ALA ASN TYR PRO GLY
SEQRES  18 C  536  VAL GLY GLY GLY SER PHE ILE ASP ASN ARG VAL TRP PHE
SEQRES  19 C  536  PRO VAL TYR GLY GLY LEU LYS PRO ASN SER PRO SER ASP
SEQRES  20 C  536  THR ALA GLN GLU GLY LYS TYR VAL ILE TYR LYS ARG TYR
SEQRES  21 C  536  ASN ASP THR CYS PRO ASP GLU GLN ASP TYR GLN ILE ARG
SEQRES  22 C  536  MET ALA LYS SER SER TYR LYS PRO GLY ARG PHE GLY GLY
SEQRES  23 C  536  LYS ARG VAL GLN GLN ALA ILE LEU SER ILE LYS VAL SER
SEQRES  24 C  536  THR SER LEU GLY GLU ASP PRO VAL LEU THR VAL PRO PRO
SEQRES  25 C  536  ASN THR VAL THR LEU MET GLY ALA GLU GLY ARG VAL LEU
SEQRES  26 C  536  THR VAL GLY THR SER HIS PHE LEU TYR GLN ARG GLY SER
SEQRES  27 C  536  SER TYR PHE SER PRO ALA LEU LEU TYR PRO MET THR VAL
SEQRES  28 C  536  SER ASN LYS THR ALA THR LEU HIS SER PRO TYR THR PHE
SEQRES  29 C  536  ASP ALA PHE THR ARG PRO GLY SER VAL PRO CYS GLN ALA
SEQRES  30 C  536  SER ALA ARG CYS PRO ASN SER CYS VAL THR GLY VAL TYR
SEQRES  31 C  536  THR ASP PRO TYR PRO LEU VAL PHE TYR ARG ASN HIS THR
SEQRES  32 C  536  LEU ARG GLY VAL PHE GLY THR MET LEU ASP ASP LYS GLN
SEQRES  33 C  536  ALA ARG LEU ASN PRO VAL SER ALA VAL PHE ASP SER ILE
SEQRES  34 C  536  SER ARG SER ARG ILE THR ARG VAL SER SER SER SER THR
SEQRES  35 C  536  LYS ALA ALA TYR THR THR SER THR CYS PHE LYS VAL VAL
SEQRES  36 C  536  LYS THR ASN LYS THR TYR CYS LEU SER ILE ALA GLU ILE
SEQRES  37 C  536  SER ASN THR LEU PHE GLY GLU PHE ARG ILE VAL PRO LEU
SEQRES  38 C  536  LEU VAL GLU ILE LEU LYS ASP ASP GLY VAL ARG GLU ALA
SEQRES  39 C  536  ARG ALA GLY ARG LEU SER GLN LEU ARG GLU GLY TRP LYS
SEQRES  40 C  536  ASP ASP ILE VAL SER PRO ILE PHE CYS ASP ALA LYS ASN
SEQRES  41 C  536  GLN THR GLU TYR ARG ARG GLU LEU GLU SER TYR ALA ALA
SEQRES  42 C  536  SER TRP PRO
SEQRES   1 D  536  MET GLY ILE LEU PRO SER PRO GLY MET PRO ALA LEU LEU
SEQRES   2 D  536  SER LEU VAL SER LEU LEU SER VAL LEU LEU MET GLY CYS
SEQRES   3 D  536  VAL ALA GLU THR GLY HIS HIS HIS HIS HIS HIS LEU VAL
SEQRES   4 D  536  PRO ARG GLY SER GLY ALA PRO ILE HIS ASP PRO ASP TYR
SEQRES   5 D  536  ILE GLY GLY ILE GLY LYS GLU LEU ILE VAL ASP ASP ALA
SEQRES   6 D  536  SER ASP VAL THR SER PHE TYR PRO SER ALA PHE GLN GLU
SEQRES   7 D  536  HIS LEU ASN PHE ILE PRO ALA PRO THR THR GLY SER GLY
SEQRES   8 D  536  CYS THR ARG ILE PRO SER PHE ASP MET SER ALA THR HIS
SEQRES   9 D  536  TYR CYS TYR THR HIS ASN VAL ILE LEU SER GLY CYS ARG
SEQRES  10 D  536  ASP HIS SER HIS SER HIS GLN TYR LEU ALA LEU GLY VAL
SEQRES  11 D  536  LEU ARG THR SER ALA THR GLY ARG VAL PHE PHE SER THR
SEQRES  12 D  536  LEU HIS SER ILE ASN LEU ASP ASP THR GLN ASN ARG LYS
SEQRES  13 D  536  SER CYS SER VAL SER ALA THR PRO LEU GLY CYS ASP MET
SEQRES  14 D  536  LEU CYS SER LYS VAL THR GLU THR GLU GLU GLU ASP TYR
SEQRES  15 D  536  ASN SER ALA VAL PRO THR SER MET VAL HIS GLY ARG LEU
SEQRES  16 D  536  GLY PHE ASP GLY GLN TYR HIS GLU LYS ASP LEU ASP VAL
SEQRES  17 D  536  THR THR LEU PHE GLU ASP TRP VAL ALA ASN TYR PRO GLY
SEQRES  18 D  536  VAL GLY GLY GLY SER PHE ILE ASP ASN ARG VAL TRP PHE
SEQRES  19 D  536  PRO VAL TYR GLY GLY LEU LYS PRO ASN SER PRO SER ASP
SEQRES  20 D  536  THR ALA GLN GLU GLY LYS TYR VAL ILE TYR LYS ARG TYR
SEQRES  21 D  536  ASN ASP THR CYS PRO ASP GLU GLN ASP TYR GLN ILE ARG
SEQRES  22 D  536  MET ALA LYS SER SER TYR LYS PRO GLY ARG PHE GLY GLY
SEQRES  23 D  536  LYS ARG VAL GLN GLN ALA ILE LEU SER ILE LYS VAL SER
SEQRES  24 D  536  THR SER LEU GLY GLU ASP PRO VAL LEU THR VAL PRO PRO
SEQRES  25 D  536  ASN THR VAL THR LEU MET GLY ALA GLU GLY ARG VAL LEU
SEQRES  26 D  536  THR VAL GLY THR SER HIS PHE LEU TYR GLN ARG GLY SER
SEQRES  27 D  536  SER TYR PHE SER PRO ALA LEU LEU TYR PRO MET THR VAL
SEQRES  28 D  536  SER ASN LYS THR ALA THR LEU HIS SER PRO TYR THR PHE
SEQRES  29 D  536  ASP ALA PHE THR ARG PRO GLY SER VAL PRO CYS GLN ALA
SEQRES  30 D  536  SER ALA ARG CYS PRO ASN SER CYS VAL THR GLY VAL TYR
SEQRES  31 D  536  THR ASP PRO TYR PRO LEU VAL PHE TYR ARG ASN HIS THR
SEQRES  32 D  536  LEU ARG GLY VAL PHE GLY THR MET LEU ASP ASP LYS GLN
SEQRES  33 D  536  ALA ARG LEU ASN PRO VAL SER ALA VAL PHE ASP SER ILE
SEQRES  34 D  536  SER ARG SER ARG ILE THR ARG VAL SER SER SER SER THR
SEQRES  35 D  536  LYS ALA ALA TYR THR THR SER THR CYS PHE LYS VAL VAL
SEQRES  36 D  536  LYS THR ASN LYS THR TYR CYS LEU SER ILE ALA GLU ILE
SEQRES  37 D  536  SER ASN THR LEU PHE GLY GLU PHE ARG ILE VAL PRO LEU
SEQRES  38 D  536  LEU VAL GLU ILE LEU LYS ASP ASP GLY VAL ARG GLU ALA
SEQRES  39 D  536  ARG ALA GLY ARG LEU SER GLN LEU ARG GLU GLY TRP LYS
SEQRES  40 D  536  ASP ASP ILE VAL SER PRO ILE PHE CYS ASP ALA LYS ASN
SEQRES  41 D  536  GLN THR GLU TYR ARG ARG GLU LEU GLU SER TYR ALA ALA
SEQRES  42 D  536  SER TRP PRO
MODRES 4FZH ASN B  433  ASN  GLYCOSYLATION SITE
MODRES 4FZH ASN A  433  ASN  GLYCOSYLATION SITE
MODRES 4FZH ASN D  481  ASN  GLYCOSYLATION SITE
MODRES 4FZH ASN A  481  ASN  GLYCOSYLATION SITE
MODRES 4FZH ASN D  341  ASN  GLYCOSYLATION SITE
MODRES 4FZH ASN C  481  ASN  GLYCOSYLATION SITE
MODRES 4FZH ASN D  433  ASN  GLYCOSYLATION SITE
MODRES 4FZH ASN C  433  ASN  GLYCOSYLATION SITE
MODRES 4FZH ASN A  341  ASN  GLYCOSYLATION SITE
MODRES 4FZH ASN B  341  ASN  GLYCOSYLATION SITE
MODRES 4FZH ASN B  481  ASN  GLYCOSYLATION SITE
HET    NAG  A 701      14
HET    NAG  A 702      14
HET    NAG  A 703      14
HET    NAG  A 704      14
HET    NAG  B 701      14
HET    NAG  B 702      14
HET    NAG  B 703      14
HET    NAG  B 704      14
HET    NAG  C 701      14
HET    NAG  C 702      14
HET    NAG  C 703      14
HET    NAG  D 701      14
HET    NAG  D 702      14
HET    NAG  D 703      14
HET    NAG  D 704      14
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
FORMUL   5  NAG    15(C8 H15 N O6)
HELIX    1   1 ASP A  147  THR A  149  5                                   3
HELIX    2   2 THR A  257  SER A  264  1                                   8
HELIX    3   3 ASP A  287  PHE A  292  1                                   6
HELIX    4   4 SER A  324  GLU A  331  1                                   8
HELIX    5   5 GLU A  347  TYR A  359  1                                  13
HELIX    6   6 LYS A  360  GLY A  365  5                                   6
HELIX    7   7 THR A  602  TYR A  611  1                                  10
HELIX    8   8 ASP B  147  THR B  149  5                                   3
HELIX    9   9 THR B  257  ASN B  263  1                                   7
HELIX   10  10 ASP B  287  PHE B  292  1                                   6
HELIX   11  11 SER B  324  GLU B  331  1                                   8
HELIX   12  12 GLU B  347  SER B  358  1                                  12
HELIX   13  13 TYR B  359  LYS B  360  5                                   2
HELIX   14  14 PRO B  361  GLY B  365  5                                   5
HELIX   15  15 GLU B  603  SER B  610  1                                   8
HELIX   16  16 ASP C  147  THR C  149  5                                   3
HELIX   17  17 THR C  257  ASN C  263  1                                   7
HELIX   18  18 ASP C  287  PHE C  292  1                                   6
HELIX   19  19 GLU C  347  SER C  358  1                                  12
HELIX   20  20 TYR C  359  LYS C  360  5                                   2
HELIX   21  21 PRO C  361  GLY C  365  5                                   5
HELIX   22  22 GLU C  603  TYR C  611  1                                   9
HELIX   23  23 ASP D  147  THR D  149  5                                   3
HELIX   24  24 THR D  257  ASN D  263  1                                   7
HELIX   25  25 ASP D  287  GLU D  293  1                                   7
HELIX   26  26 GLU D  347  SER D  358  1                                  12
HELIX   27  27 TYR D  359  LYS D  360  5                                   2
HELIX   28  28 PRO D  361  GLY D  365  5                                   5
HELIX   29  29 THR D  602  ALA D  612  1                                  11
SHEET    1   A 5 ILE A 141  VAL A 142  0
SHEET    2   A 5 TYR A 474  PHE A 478  1  O  PHE A 478   N  ILE A 141
SHEET    3   A 5 LEU A 484  LEU A 492 -1  O  PHE A 488   N  TYR A 474
SHEET    4   A 5 PRO A 501  ASP A 507 -1  O  PHE A 506   N  VAL A 487
SHEET    5   A 5 THR A 515  ARG A 516 -1  O  THR A 515   N  SER A 503
SHEET    1   B 4 PHE A 151  PRO A 153  0
SHEET    2   B 4 ARG A 557  LYS A 567 -1  O  LEU A 566   N  TYR A 152
SHEET    3   B 4 LYS A 539  ILE A 548 -1  N  CYS A 542   O  VAL A 563
SHEET    4   B 4 ALA A 524  VAL A 534 -1  N  PHE A 532   O  TYR A 541
SHEET    1   C 4 THR A 173  MET A 180  0
SHEET    2   C 4 TYR A 185  ILE A 192 -1  O  CYS A 186   N  ASP A 179
SHEET    3   C 4 SER A 202  THR A 213 -1  O  ALA A 207   N  TYR A 187
SHEET    4   C 4 VAL A 219  LEU A 229 -1  O  LEU A 229   N  GLN A 204
SHEET    1   D 4 ARG A 235  THR A 243  0
SHEET    2   D 4 GLY A 246  LYS A 253 -1  O  LEU A 250   N  SER A 239
SHEET    3   D 4 MET A 270  GLY A 276 -1  O  VAL A 271   N  CYS A 251
SHEET    4   D 4 TYR A 281  LEU A 286 -1  O  LYS A 284   N  HIS A 272
SHEET    1   E 3 TRP A 295  PRO A 300  0
SHEET    2   E 3 ARG A 311  LEU A 320 -1  O  TYR A 317   N  TYR A 299
SHEET    3   E 3 SER A 306  ILE A 308 -1  N  SER A 306   O  TRP A 313
SHEET    1   F 4 TRP A 295  PRO A 300  0
SHEET    2   F 4 ARG A 311  LEU A 320 -1  O  TYR A 317   N  TYR A 299
SHEET    3   F 4 VAL A 369  ILE A 376 -1  O  LEU A 374   N  PHE A 314
SHEET    4   F 4 VAL A 387  THR A 389 -1  O  THR A 389   N  ILE A 373
SHEET    1   G 4 GLY A 402  VAL A 407  0
SHEET    2   G 4 SER A 410  GLN A 415 -1  O  TYR A 414   N  ARG A 403
SHEET    3   G 4 ALA A 424  SER A 432 -1  O  TYR A 427   N  LEU A 413
SHEET    4   G 4 THR A 435  LEU A 438 -1  O  THR A 437   N  THR A 430
SHEET    1   H 4 GLY A 402  VAL A 407  0
SHEET    2   H 4 SER A 410  GLN A 415 -1  O  TYR A 414   N  ARG A 403
SHEET    3   H 4 ALA A 424  SER A 432 -1  O  TYR A 427   N  LEU A 413
SHEET    4   H 4 TYR A 442  PHE A 444 -1  O  TYR A 442   N  LEU A 426
SHEET    1   I 5 ILE B 141  VAL B 142  0
SHEET    2   I 5 TYR B 474  PHE B 478  1  O  PHE B 478   N  ILE B 141
SHEET    3   I 5 LEU B 484  LEU B 492 -1  O  PHE B 488   N  TYR B 474
SHEET    4   I 5 PRO B 501  ASP B 507 -1  O  PHE B 506   N  VAL B 487
SHEET    5   I 5 ARG B 511  ARG B 516 -1  O  THR B 515   N  SER B 503
SHEET    1   J 2 PHE B 151  TYR B 152  0
SHEET    2   J 2 LEU B 566  LYS B 567 -1  O  LEU B 566   N  TYR B 152
SHEET    1   K 4 THR B 173  MET B 180  0
SHEET    2   K 4 TYR B 185  ILE B 192 -1  O  ASN B 190   N  ARG B 174
SHEET    3   K 4 SER B 202  GLY B 209 -1  O  HIS B 203   N  VAL B 191
SHEET    4   K 4 THR B 223  LEU B 229 -1  O  LEU B 224   N  LEU B 208
SHEET    1   L 2 ARG B 212  THR B 213  0
SHEET    2   L 2 VAL B 219  PHE B 220 -1  O  PHE B 220   N  ARG B 212
SHEET    1   M 4 ARG B 235  THR B 243  0
SHEET    2   M 4 GLY B 246  LYS B 253 -1  O  ASP B 248   N  SER B 241
SHEET    3   M 4 MET B 270  LEU B 275 -1  O  VAL B 271   N  CYS B 251
SHEET    4   M 4 TYR B 281  LYS B 284 -1  O  LYS B 284   N  HIS B 272
SHEET    1   N 3 ASN B 298  PRO B 300  0
SHEET    2   N 3 ARG B 311  GLY B 318 -1  O  TYR B 317   N  TYR B 299
SHEET    3   N 3 PHE B 307  ILE B 308 -1  N  ILE B 308   O  ARG B 311
SHEET    1   O 4 ASN B 298  PRO B 300  0
SHEET    2   O 4 ARG B 311  GLY B 318 -1  O  TYR B 317   N  TYR B 299
SHEET    3   O 4 GLN B 370  LYS B 377 -1  O  ALA B 372   N  VAL B 316
SHEET    4   O 4 VAL B 387  THR B 389 -1  O  VAL B 387   N  SER B 375
SHEET    1   P 4 GLY B 402  VAL B 407  0
SHEET    2   P 4 SER B 410  GLN B 415 -1  O  TYR B 414   N  ARG B 403
SHEET    3   P 4 ALA B 424  SER B 432 -1  O  TYR B 427   N  LEU B 413
SHEET    4   P 4 THR B 435  LEU B 438 -1  O  THR B 437   N  THR B 430
SHEET    1   Q 4 GLY B 402  VAL B 407  0
SHEET    2   Q 4 SER B 410  GLN B 415 -1  O  TYR B 414   N  ARG B 403
SHEET    3   Q 4 ALA B 424  SER B 432 -1  O  TYR B 427   N  LEU B 413
SHEET    4   Q 4 TYR B 442  PHE B 444 -1  O  TYR B 442   N  LEU B 426
SHEET    1   R 3 ALA B 524  VAL B 534  0
SHEET    2   R 3 LYS B 539  ILE B 548 -1  O  ILE B 545   N  THR B 528
SHEET    3   R 3 ARG B 557  GLU B 564 -1  O  LEU B 561   N  SER B 544
SHEET    1   S 5 ILE C 141  VAL C 142  0
SHEET    2   S 5 TYR C 474  PHE C 478  1  O  LEU C 476   N  ILE C 141
SHEET    3   S 5 LEU C 484  LEU C 492 -1  O  ARG C 485   N  VAL C 477
SHEET    4   S 5 PRO C 501  PHE C 506 -1  O  VAL C 502   N  MET C 491
SHEET    5   S 5 THR C 515  ARG C 516 -1  O  THR C 515   N  SER C 503
SHEET    1   T 2 PHE C 151  TYR C 152  0
SHEET    2   T 2 LEU C 566  LYS C 567 -1  O  LEU C 566   N  TYR C 152
SHEET    1   U 4 THR C 173  MET C 180  0
SHEET    2   U 4 TYR C 185  ILE C 192 -1  O  ASN C 190   N  ARG C 174
SHEET    3   U 4 SER C 202  THR C 213 -1  O  HIS C 203   N  VAL C 191
SHEET    4   U 4 VAL C 219  LEU C 229 -1  O  ILE C 227   N  LEU C 206
SHEET    1   V 4 ARG C 235  THR C 243  0
SHEET    2   V 4 GLY C 246  LYS C 253 -1  O  LEU C 250   N  SER C 239
SHEET    3   V 4 SER C 269  LEU C 275 -1  O  LEU C 275   N  CYS C 247
SHEET    4   V 4 TYR C 281  LYS C 284 -1  O  LYS C 284   N  HIS C 272
SHEET    1   W 3 TRP C 295  PRO C 300  0
SHEET    2   W 3 ARG C 311  LEU C 320 -1  O  TYR C 317   N  TYR C 299
SHEET    3   W 3 PHE C 307  ILE C 308 -1  N  ILE C 308   O  ARG C 311
SHEET    1   X 4 TRP C 295  PRO C 300  0
SHEET    2   X 4 ARG C 311  LEU C 320 -1  O  TYR C 317   N  TYR C 299
SHEET    3   X 4 VAL C 369  ILE C 376 -1  O  ALA C 372   N  VAL C 316
SHEET    4   X 4 PRO C 386  THR C 389 -1  O  VAL C 387   N  SER C 375
SHEET    1   Y 4 GLY C 402  VAL C 407  0
SHEET    2   Y 4 SER C 410  GLN C 415 -1  O  PHE C 412   N  LEU C 405
SHEET    3   Y 4 ALA C 424  SER C 432 -1  O  TYR C 427   N  LEU C 413
SHEET    4   Y 4 THR C 435  LEU C 438 -1  O  THR C 437   N  THR C 430
SHEET    1   Z 4 GLY C 402  VAL C 407  0
SHEET    2   Z 4 SER C 410  GLN C 415 -1  O  PHE C 412   N  LEU C 405
SHEET    3   Z 4 ALA C 424  SER C 432 -1  O  TYR C 427   N  LEU C 413
SHEET    4   Z 4 TYR C 442  PHE C 444 -1  O  TYR C 442   N  LEU C 426
SHEET    1  AA 4 THR C 471  ASP C 472  0
SHEET    2  AA 4 ALA C 524  VAL C 534  1  O  THR C 527   N  ASP C 472
SHEET    3  AA 4 LYS C 539  SER C 549 -1  O  LEU C 543   N  THR C 530
SHEET    4  AA 4 PHE C 556  GLU C 564 -1  O  VAL C 563   N  CYS C 542
SHEET    1  AB 5 ILE D 141  VAL D 142  0
SHEET    2  AB 5 TYR D 474  PHE D 478  1  O  PHE D 478   N  ILE D 141
SHEET    3  AB 5 LEU D 484  LEU D 492 -1  O  GLY D 486   N  VAL D 477
SHEET    4  AB 5 PRO D 501  PHE D 506 -1  O  PHE D 506   N  VAL D 487
SHEET    5  AB 5 THR D 515  ARG D 516 -1  O  THR D 515   N  SER D 503
SHEET    1  AC 5 PHE D 151  PRO D 153  0
SHEET    2  AC 5 ARG D 557  LYS D 567 -1  O  LEU D 566   N  TYR D 152
SHEET    3  AC 5 LYS D 539  ILE D 548 -1  N  ALA D 546   O  VAL D 559
SHEET    4  AC 5 ALA D 524  VAL D 534 -1  N  PHE D 532   O  TYR D 541
SHEET    5  AC 5 THR D 471  ASP D 472  1  N  ASP D 472   O  THR D 527
SHEET    1  AD 4 CYS D 172  MET D 180  0
SHEET    2  AD 4 TYR D 185  ILE D 192 -1  O  ASN D 190   N  ARG D 174
SHEET    3  AD 4 SER D 202  THR D 213 -1  O  ALA D 207   N  TYR D 187
SHEET    4  AD 4 VAL D 219  LEU D 229 -1  O  SER D 222   N  VAL D 210
SHEET    1  AE 4 LYS D 236  THR D 243  0
SHEET    2  AE 4 GLY D 246  LYS D 253 -1  O  ASP D 248   N  SER D 241
SHEET    3  AE 4 SER D 269  LEU D 275 -1  O  LEU D 275   N  CYS D 247
SHEET    4  AE 4 TYR D 281  ASP D 285 -1  O  LYS D 284   N  HIS D 272
SHEET    1  AF 3 TRP D 295  PRO D 300  0
SHEET    2  AF 3 ARG D 311  LEU D 320 -1  O  TYR D 317   N  TYR D 299
SHEET    3  AF 3 SER D 306  ILE D 308 -1  N  SER D 306   O  TRP D 313
SHEET    1  AG 4 TRP D 295  PRO D 300  0
SHEET    2  AG 4 ARG D 311  LEU D 320 -1  O  TYR D 317   N  TYR D 299
SHEET    3  AG 4 ARG D 368  LYS D 377 -1  O  LEU D 374   N  PHE D 314
SHEET    4  AG 4 GLU D 384  THR D 389 -1  O  VAL D 387   N  SER D 375
SHEET    1  AH 4 GLY D 402  VAL D 407  0
SHEET    2  AH 4 SER D 410  GLN D 415 -1  O  PHE D 412   N  LEU D 405
SHEET    3  AH 4 ALA D 424  SER D 432 -1  O  MET D 429   N  HIS D 411
SHEET    4  AH 4 THR D 435  LEU D 438 -1  O  THR D 437   N  THR D 430
SHEET    1  AI 4 GLY D 402  VAL D 407  0
SHEET    2  AI 4 SER D 410  GLN D 415 -1  O  PHE D 412   N  LEU D 405
SHEET    3  AI 4 ALA D 424  SER D 432 -1  O  MET D 429   N  HIS D 411
SHEET    4  AI 4 TYR D 442  PHE D 444 -1  O  TYR D 442   N  LEU D 426
SSBOND   1 CYS A  172    CYS A  196                          1555   1555  2.04
SSBOND   2 CYS A  186    CYS A  247                          1555   1555  2.03
SSBOND   3 CYS A  238    CYS A  251                          1555   1555  1.95
SSBOND   4 CYS A  344    CYS A  461                          1555   1555  2.03
SSBOND   5 CYS A  455    CYS A  465                          1555   1555  2.03
SSBOND   6 CYS A  531    CYS A  542                          1555   1555  2.03
SSBOND   7 CYS A  596    CYS B  596                          1555   1555  2.06
SSBOND   8 CYS B  172    CYS B  196                          1555   1555  2.04
SSBOND   9 CYS B  186    CYS B  247                          1555   1555  2.03
SSBOND  10 CYS B  238    CYS B  251                          1555   1555  2.03
SSBOND  11 CYS B  344    CYS B  461                          1555   1555  2.03
SSBOND  12 CYS B  455    CYS B  465                          1555   1555  2.03
SSBOND  13 CYS B  531    CYS B  542                          1555   1555  2.03
SSBOND  14 CYS C  172    CYS C  196                          1555   1555  2.04
SSBOND  15 CYS C  186    CYS C  247                          1555   1555  2.03
SSBOND  16 CYS C  238    CYS C  251                          1555   1555  1.98
SSBOND  17 CYS C  344    CYS C  461                          1555   1555  2.03
SSBOND  18 CYS C  455    CYS C  465                          1555   1555  2.03
SSBOND  19 CYS C  531    CYS C  542                          1555   1555  2.03
SSBOND  20 CYS C  596    CYS D  596                          1555   1555  2.06
SSBOND  21 CYS D  172    CYS D  196                          1555   1555  2.04
SSBOND  22 CYS D  186    CYS D  247                          1555   1555  2.03
SSBOND  23 CYS D  238    CYS D  251                          1555   1555  1.96
SSBOND  24 CYS D  344    CYS D  461                          1555   1555  2.03
SSBOND  25 CYS D  455    CYS D  465                          1555   1555  2.04
SSBOND  26 CYS D  531    CYS D  542                          1555   1555  2.03
LINK         ND2 ASN B 433                 C1  NAG B 702     1555   1555  1.44
LINK         ND2 ASN A 433                 C1  NAG A 702     1555   1555  1.44
LINK         ND2 ASN D 481                 C1  NAG D 703     1555   1555  1.44
LINK         ND2 ASN A 481                 C1  NAG A 703     1555   1555  1.44
LINK         ND2 ASN D 341                 C1  NAG D 701     1555   1555  1.44
LINK         ND2 ASN C 481                 C1  NAG C 702     1555   1555  1.44
LINK         ND2 ASN D 433                 C1  NAG D 702     1555   1555  1.44
LINK         O4  NAG D 703                 C1  NAG D 704     1555   1555  1.44
LINK         ND2 ASN C 433                 C1  NAG C 701     1555   1555  1.44
LINK         ND2 ASN A 341                 C1  NAG A 701     1555   1555  1.44
LINK         ND2 ASN B 341                 C1  NAG B 701     1555   1555  1.44
LINK         O4  NAG C 702                 C1  NAG C 703     1555   1555  1.44
LINK         O4  NAG B 703                 C1  NAG B 704     1555   1555  1.44
LINK         ND2 ASN B 481                 C1  NAG B 703     1555   1555  1.44
LINK         O4  NAG A 703                 C1  NAG A 704     1555   1555  1.44
SITE     1 AC1  2 TYR A 340  ASN A 341
SITE     1 AC2  2 ASN A 433  LYS A 434
SITE     1 AC3  3 TYR A 479  ASN A 481  NAG A 704
SITE     1 AC4  2 TYR A 479  NAG A 703
SITE     1 AC5  1 ASN B 341
SITE     1 AC6  1 ASN B 433
SITE     1 AC7  4 TYR B 479  ASN B 481  THR B 483  NAG B 704
SITE     1 AC8  1 NAG B 703
SITE     1 AC9  1 ASN C 433
SITE     1 BC1  4 TYR C 479  ASN C 481  THR C 483  NAG C 703
SITE     1 BC2  2 TYR C 479  NAG C 702
SITE     1 BC3  1 ASN D 341
SITE     1 BC4  1 ASN D 433
SITE     1 BC5  3 ASN D 481  THR D 483  NAG D 704
SITE     1 BC6  2 TYR D 479  NAG D 703
CRYST1  124.606  124.606  284.914  90.00  90.00 120.00 P 31 2 1     24
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      0.008025  0.004633  0.000000        0.00000
SCALE2      0.000000  0.009267  0.000000        0.00000
SCALE3      0.000000  0.000000  0.003510        0.00000
      
PROCHECK
Go to PROCHECK summary
 References