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PDBsum entry 4fqx

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Immune system PDB id
4fqx
Jmol
Contents
Protein chains
186 a.a.
191 a.a.
180 a.a.
187 a.a.
Ligands
ASN-CYS-LEU-LYS-
LEU-ALA-THR
NAG-NAG
Waters ×124
HEADER    IMMUNE SYSTEM                           25-JUN-12   4FQX
TITLE     CRYSTAL STRUCTURE OF HLA-DM BOUND TO HLA-DR1
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DM ALPHA CHAIN;
COMPND   3 CHAIN: C;
COMPND   4 FRAGMENT: UNP RESIDUES 27-225;
COMPND   5 SYNONYM: MHC CLASS II ANTIGEN DMA, REALLY INTERESTING NEW GENE 6
COMPND   6 PROTEIN;
COMPND   7 ENGINEERED: YES;
COMPND   8 MOL_ID: 2;
COMPND   9 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DM BETA CHAIN;
COMPND  10 CHAIN: D;
COMPND  11 FRAGMENT: UNP RESIDUES 19-211;
COMPND  12 SYNONYM: MHC CLASS II ANTIGEN DMB, REALLY INTERESTING NEW GENE 7
COMPND  13 PROTEIN;
COMPND  14 ENGINEERED: YES;
COMPND  15 MOL_ID: 3;
COMPND  16 MOLECULE: SYNTHETIC PEPTIDE;
COMPND  17 CHAIN: E;
COMPND  18 ENGINEERED: YES;
COMPND  19 MOL_ID: 4;
COMPND  20 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN;
COMPND  21 CHAIN: A;
COMPND  22 FRAGMENT: UNP RESIDUES 26-216;
COMPND  23 SYNONYM: MHC CLASS II ANTIGEN DRA;
COMPND  24 ENGINEERED: YES;
COMPND  25 MOL_ID: 5;
COMPND  26 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DRB1-1 BETA CHAIN;
COMPND  27 CHAIN: B;
COMPND  28 FRAGMENT: UNP RESIDUES 30-221;
COMPND  29 SYNONYM: MHC CLASS II ANTIGEN DRB1*1, DR-1, DR1;
COMPND  30 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: DM ALPHA CHAIN, DMA, HLA CLASS II HISTOCOMPATIBILITY ANTIGEN,
SOURCE   6 HLA-DMA, RING6;
SOURCE   7 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: LEC3.2.8.1;
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PEE14.1;
SOURCE  12 MOL_ID: 2;
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  14 ORGANISM_COMMON: HUMAN;
SOURCE  15 ORGANISM_TAXID: 9606;
SOURCE  16 GENE: DM BETA CHAIN, DMB, HLA CLASS II HISTOCOMPATIBILITY ANTIGEN,
SOURCE  17 HLA-DMB, RING7;
SOURCE  18 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE  20 EXPRESSION_SYSTEM_STRAIN: LEC3.2.8.1;
SOURCE  21 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  22 EXPRESSION_SYSTEM_PLASMID: PEE14.1;
SOURCE  23 MOL_ID: 3;
SOURCE  24 SYNTHETIC: YES;
SOURCE  25 MOL_ID: 4;
SOURCE  26 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  27 ORGANISM_COMMON: HUMAN;
SOURCE  28 ORGANISM_TAXID: 9606;
SOURCE  29 GENE: HLA-DR1 ALPHA CHAIN, HLA-DRA, HLA-DRA1, MHC CLASS II MOLECULE;
SOURCE  30 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE  31 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE  32 MOL_ID: 5;
SOURCE  33 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  34 ORGANISM_COMMON: HUMAN;
SOURCE  35 ORGANISM_TAXID: 9606;
SOURCE  36 GENE: BETA CHAIN, HLA-DR1, HLA-DRB1, MHC CLASS II MOLECULE;
SOURCE  37 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE  38 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS    IMMUNE COMPLEX, PEPTIDE LOADING, PEPTIDE EDITING, ANTIGEN
KEYWDS   2 PRESENTATION, IMMUNE SYSTEM
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.K.SETHI,W.POS,K.W.WUCHERPFENNIG
REVDAT   1   09-JAN-13 4FQX    0
JRNL        AUTH   W.POS,D.K.SETHI,M.J.CALL,M.S.SCHULZE,A.K.ANDERS,J.PYRDOL,
JRNL        AUTH 2 K.W.WUCHERPFENNIG
JRNL        TITL   CRYSTAL STRUCTURE OF THE HLA-DM-HLA-DR1 COMPLEX DEFINES
JRNL        TITL 2 MECHANISMS FOR RAPID PEPTIDE SELECTION.
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 151  1557 2012
JRNL        REFN                   ISSN 0092-8674
JRNL        PMID   23260142
JRNL        DOI    10.1016/J.CELL.2012.11.025
REMARK   2
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8_1069)
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) : 2.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.14
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.1
REMARK   3   NUMBER OF REFLECTIONS             : 34135
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.196
REMARK   3   R VALUE            (WORKING SET) : 0.194
REMARK   3   FREE R VALUE                     : 0.240
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 1742
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 36.1448 -  5.9424    0.94     2805   143  0.1855 0.2139
REMARK   3     2  5.9424 -  4.7200    0.96     2717   166  0.1541 0.1946
REMARK   3     3  4.7200 -  4.1243    0.97     2707   150  0.1455 0.1797
REMARK   3     4  4.1243 -  3.7477    0.98     2720   142  0.1789 0.2447
REMARK   3     5  3.7477 -  3.4793    0.98     2696   140  0.1911 0.2427
REMARK   3     6  3.4793 -  3.2743    0.98     2748   139  0.2098 0.2544
REMARK   3     7  3.2743 -  3.1104    0.98     2714   144  0.2335 0.2816
REMARK   3     8  3.1104 -  2.9751    0.98     2700   144  0.2549 0.3030
REMARK   3     9  2.9751 -  2.8606    0.98     2712   142  0.2611 0.3329
REMARK   3    10  2.8606 -  2.7619    0.99     2674   154  0.2619 0.3394
REMARK   3    11  2.7619 -  2.6756    0.98     2691   154  0.2630 0.3312
REMARK   3    12  2.6756 -  2.5991    0.92     2509   124  0.2639 0.3240
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.11
REMARK   3   SHRINKAGE RADIUS   : 0.90
REMARK   3   K_SOL              : NULL
REMARK   3   B_SOL              : NULL
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.330
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.930
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 63.91
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  TWINNING INFORMATION.
REMARK   3   FRACTION: NULL
REMARK   3   OPERATOR: NULL
REMARK   3
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3                 RMSD          COUNT
REMARK   3   BOND      :  0.009           6263
REMARK   3   ANGLE     :  1.188           8530
REMARK   3   CHIRALITY :  0.079            928
REMARK   3   PLANARITY :  0.006           1109
REMARK   3   DIHEDRAL  : 15.957           2252
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 18
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: (CHAIN C AND RESID 15:137 )
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.6200   8.4382 -12.9916
REMARK   3    T TENSOR
REMARK   3      T11:   0.7234 T22:   0.3916
REMARK   3      T33:   0.5557 T12:  -0.6064
REMARK   3      T13:  -0.2811 T23:   0.1957
REMARK   3    L TENSOR
REMARK   3      L11:   0.3078 L22:   0.2424
REMARK   3      L33:   0.4352 L12:   0.2333
REMARK   3      L13:  -0.0588 L23:  -0.1637
REMARK   3    S TENSOR
REMARK   3      S11:  -0.3899 S12:   0.1404 S13:   0.2782
REMARK   3      S21:   0.0321 S22:  -0.2790 S23:  -0.2093
REMARK   3      S31:  -0.9460 S32:   0.5463 S33:  -0.3460
REMARK   3   TLS GROUP : 2
REMARK   3    SELECTION: (CHAIN C AND RESID 138:147 )
REMARK   3    ORIGIN FOR THE GROUP (A):   0.2837  -7.8231 -27.2399
REMARK   3    T TENSOR
REMARK   3      T11:   0.4759 T22:   0.9878
REMARK   3      T33:   0.9446 T12:  -0.2702
REMARK   3      T13:   0.0715 T23:   0.0277
REMARK   3    L TENSOR
REMARK   3      L11:   0.0175 L22:   0.0052
REMARK   3      L33:  -0.0019 L12:  -0.0025
REMARK   3      L13:  -0.0124 L23:   0.0055
REMARK   3    S TENSOR
REMARK   3      S11:   0.0551 S12:   0.1532 S13:  -0.0389
REMARK   3      S21:  -0.0194 S22:   0.0152 S23:   0.0212
REMARK   3      S31:   0.0291 S32:   0.1059 S33:   0.0026
REMARK   3   TLS GROUP : 3
REMARK   3    SELECTION: (CHAIN C AND RESID 148:200 )
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.6157  -4.9859 -23.9651
REMARK   3    T TENSOR
REMARK   3      T11:   0.4184 T22:   0.5326
REMARK   3      T33:   0.4144 T12:  -0.1360
REMARK   3      T13:  -0.0055 T23:   0.1140
REMARK   3    L TENSOR
REMARK   3      L11:   0.1097 L22:   0.0735
REMARK   3      L33:   0.3766 L12:  -0.0718
REMARK   3      L13:   0.0804 L23:   0.0224
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1694 S12:   0.2642 S13:   0.1687
REMARK   3      S21:   0.0270 S22:  -0.1123 S23:  -0.2596
REMARK   3      S31:  -0.4956 S32:   0.2481 S33:  -0.2086
REMARK   3   TLS GROUP : 4
REMARK   3    SELECTION: (CHAIN D AND RESID 3:133 )
REMARK   3    ORIGIN FOR THE GROUP (A): -20.1527  14.2929 -13.2402
REMARK   3    T TENSOR
REMARK   3      T11:   1.1966 T22:   0.1094
REMARK   3      T33:   0.5380 T12:   0.0147
REMARK   3      T13:  -0.3621 T23:   0.1129
REMARK   3    L TENSOR
REMARK   3      L11:   0.3137 L22:   0.4312
REMARK   3      L33:   0.2542 L12:   0.1030
REMARK   3      L13:  -0.2064 L23:  -0.2320
REMARK   3    S TENSOR
REMARK   3      S11:  -0.3348 S12:   0.1020 S13:   0.2563
REMARK   3      S21:   0.1428 S22:  -0.0685 S23:   0.0595
REMARK   3      S31:  -0.8394 S32:  -0.2896 S33:  -0.1659
REMARK   3   TLS GROUP : 5
REMARK   3    SELECTION: (CHAIN D AND RESID 134:157 )
REMARK   3    ORIGIN FOR THE GROUP (A): -27.4693   3.6563 -30.9583
REMARK   3    T TENSOR
REMARK   3      T11:   0.6531 T22:   0.4677
REMARK   3      T33:   0.5298 T12:  -0.0558
REMARK   3      T13:  -0.1470 T23:   0.1089
REMARK   3    L TENSOR
REMARK   3      L11:   0.0320 L22:   0.0453
REMARK   3      L33:   0.0209 L12:  -0.0496
REMARK   3      L13:  -0.0337 L23:   0.0403
REMARK   3    S TENSOR
REMARK   3      S11:   0.1294 S12:  -0.0058 S13:  -0.0485
REMARK   3      S21:  -0.1113 S22:  -0.2038 S23:   0.2393
REMARK   3      S31:  -0.2445 S32:   0.0920 S33:   0.0002
REMARK   3   TLS GROUP : 6
REMARK   3    SELECTION: (CHAIN D AND RESID 158:193 )
REMARK   3    ORIGIN FOR THE GROUP (A): -30.6600   2.0788 -43.6638
REMARK   3    T TENSOR
REMARK   3      T11:   0.9649 T22:   0.4445
REMARK   3      T33:   0.4366 T12:  -0.1889
REMARK   3      T13:  -0.2859 T23:   0.1994
REMARK   3    L TENSOR
REMARK   3      L11:   0.5788 L22:   0.0837
REMARK   3      L33:   0.3230 L12:  -0.1952
REMARK   3      L13:  -0.4418 L23:   0.1519
REMARK   3    S TENSOR
REMARK   3      S11:  -0.3924 S12:   0.3025 S13:  -0.0355
REMARK   3      S21:  -0.0293 S22:  -0.3865 S23:  -0.0619
REMARK   3      S31:  -0.2515 S32:  -0.5354 S33:  -0.1850
REMARK   3   TLS GROUP : 7
REMARK   3    SELECTION: (CHAIN E AND RESID 87:93 )
REMARK   3    ORIGIN FOR THE GROUP (A): -26.6457 -11.6481  23.1359
REMARK   3    T TENSOR
REMARK   3      T11:   0.5087 T22:   0.5078
REMARK   3      T33:   0.6470 T12:  -0.0387
REMARK   3      T13:  -0.0301 T23:  -0.1008
REMARK   3    L TENSOR
REMARK   3      L11:   0.0043 L22:   0.0149
REMARK   3      L33:   0.0075 L12:   0.0001
REMARK   3      L13:   0.0062 L23:  -0.0036
REMARK   3    S TENSOR
REMARK   3      S11:   0.1870 S12:  -0.0532 S13:   0.1357
REMARK   3      S21:  -0.0193 S22:  -0.0328 S23:  -0.0876
REMARK   3      S31:  -0.0283 S32:  -0.0911 S33:   0.0006
REMARK   3   TLS GROUP : 8
REMARK   3    SELECTION: (CHAIN A AND RESID 2:45 )
REMARK   3    ORIGIN FOR THE GROUP (A): -23.3604 -12.2209   2.4233
REMARK   3    T TENSOR
REMARK   3      T11:   0.2640 T22:   0.3435
REMARK   3      T33:   0.3424 T12:   0.0074
REMARK   3      T13:  -0.0269 T23:   0.0041
REMARK   3    L TENSOR
REMARK   3      L11:   0.0019 L22:   0.0434
REMARK   3      L33:   0.0886 L12:  -0.0124
REMARK   3      L13:   0.0086 L23:  -0.0140
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1127 S12:  -0.1049 S13:   0.0480
REMARK   3      S21:   0.1202 S22:  -0.0153 S23:  -0.0043
REMARK   3      S31:  -0.2684 S32:   0.0467 S33:   0.0000
REMARK   3   TLS GROUP : 9
REMARK   3    SELECTION: (CHAIN A AND RESID 46:76 )
REMARK   3    ORIGIN FOR THE GROUP (A): -21.8755  -9.4083  10.2287
REMARK   3    T TENSOR
REMARK   3      T11:   0.4703 T22:   0.4307
REMARK   3      T33:   0.3632 T12:   0.0051
REMARK   3      T13:  -0.0550 T23:  -0.0149
REMARK   3    L TENSOR
REMARK   3      L11:   0.0691 L22:   0.0267
REMARK   3      L33:   0.0231 L12:   0.0026
REMARK   3      L13:  -0.0228 L23:   0.0180
REMARK   3    S TENSOR
REMARK   3      S11:   0.0491 S12:  -0.1471 S13:   0.1605
REMARK   3      S21:   0.0017 S22:  -0.0232 S23:   0.1635
REMARK   3      S31:  -0.4029 S32:  -0.0065 S33:  -0.0000
REMARK   3   TLS GROUP : 10
REMARK   3    SELECTION: (CHAIN A AND RESID 77:101 )
REMARK   3    ORIGIN FOR THE GROUP (A): -21.0661 -26.9340  -6.9073
REMARK   3    T TENSOR
REMARK   3      T11:   0.3118 T22:   0.3416
REMARK   3      T33:   0.3466 T12:   0.0024
REMARK   3      T13:  -0.0058 T23:   0.0154
REMARK   3    L TENSOR
REMARK   3      L11:   0.1797 L22:   0.0299
REMARK   3      L33:   0.0451 L12:   0.0538
REMARK   3      L13:  -0.0153 L23:   0.0365
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0770 S12:   0.1986 S13:  -0.0386
REMARK   3      S21:  -0.0425 S22:  -0.0376 S23:  -0.0087
REMARK   3      S31:   0.0664 S32:   0.0286 S33:   0.0001
REMARK   3   TLS GROUP : 11
REMARK   3    SELECTION: (CHAIN A AND RESID 102:154 )
REMARK   3    ORIGIN FOR THE GROUP (A): -17.3665 -22.5874  -8.1483
REMARK   3    T TENSOR
REMARK   3      T11:   0.2496 T22:   0.3337
REMARK   3      T33:   0.3221 T12:  -0.0086
REMARK   3      T13:  -0.0091 T23:   0.0132
REMARK   3    L TENSOR
REMARK   3      L11:   0.0606 L22:   0.0625
REMARK   3      L33:   0.0671 L12:  -0.0613
REMARK   3      L13:   0.0432 L23:  -0.0116
REMARK   3    S TENSOR
REMARK   3      S11:   0.1008 S12:   0.2278 S13:  -0.0013
REMARK   3      S21:  -0.0189 S22:  -0.0555 S23:   0.0935
REMARK   3      S31:  -0.1125 S32:  -0.1026 S33:   0.0000
REMARK   3   TLS GROUP : 12
REMARK   3    SELECTION: (CHAIN A AND RESID 155:181 )
REMARK   3    ORIGIN FOR THE GROUP (A): -13.8362 -31.3782 -13.7832
REMARK   3    T TENSOR
REMARK   3      T11:   0.4112 T22:   0.4241
REMARK   3      T33:   0.4473 T12:   0.0650
REMARK   3      T13:   0.0069 T23:   0.0245
REMARK   3    L TENSOR
REMARK   3      L11:   0.0722 L22:   0.1059
REMARK   3      L33:   0.0129 L12:   0.0057
REMARK   3      L13:   0.0265 L23:   0.0053
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0753 S12:   0.0891 S13:  -0.1977
REMARK   3      S21:   0.0752 S22:  -0.1009 S23:  -0.0054
REMARK   3      S31:   0.3019 S32:   0.1355 S33:  -0.0003
REMARK   3   TLS GROUP : 13
REMARK   3    SELECTION: (CHAIN B AND RESID -5:17 )
REMARK   3    ORIGIN FOR THE GROUP (A): -21.0410 -25.0367  10.7711
REMARK   3    T TENSOR
REMARK   3      T11:   0.2198 T22:   0.3927
REMARK   3      T33:   0.2835 T12:   0.0607
REMARK   3      T13:  -0.0277 T23:   0.0452
REMARK   3    L TENSOR
REMARK   3      L11:   0.0169 L22:   0.0040
REMARK   3      L33:   0.0438 L12:  -0.0218
REMARK   3      L13:  -0.0118 L23:  -0.0511
REMARK   3    S TENSOR
REMARK   3      S11:   0.1264 S12:  -0.0054 S13:   0.1471
REMARK   3      S21:  -0.1808 S22:  -0.0320 S23:   0.0634
REMARK   3      S31:   0.0864 S32:  -0.1138 S33:   0.0003
REMARK   3   TLS GROUP : 14
REMARK   3    SELECTION: (CHAIN B AND RESID 18:84 )
REMARK   3    ORIGIN FOR THE GROUP (A): -37.7612 -12.4817  14.4692
REMARK   3    T TENSOR
REMARK   3      T11:   0.2653 T22:   0.4028
REMARK   3      T33:   0.3886 T12:   0.1386
REMARK   3      T13:   0.0188 T23:  -0.0015
REMARK   3    L TENSOR
REMARK   3      L11:   0.1372 L22:   0.1989
REMARK   3      L33:   0.1419 L12:   0.1184
REMARK   3      L13:   0.0647 L23:   0.0384
REMARK   3    S TENSOR
REMARK   3      S11:   0.1022 S12:  -0.0536 S13:   0.1929
REMARK   3      S21:   0.1788 S22:  -0.0567 S23:  -0.0772
REMARK   3      S31:  -0.1003 S32:  -0.3849 S33:   0.0041
REMARK   3   TLS GROUP : 15
REMARK   3    SELECTION: (CHAIN B AND RESID 85:97 )
REMARK   3    ORIGIN FOR THE GROUP (A): -34.0170  -4.6354 -12.0245
REMARK   3    T TENSOR
REMARK   3      T11:   0.2624 T22:   0.2274
REMARK   3      T33:   0.5071 T12:   0.0616
REMARK   3      T13:  -0.0035 T23:   0.1127
REMARK   3    L TENSOR
REMARK   3      L11:   0.2695 L22:   0.1374
REMARK   3      L33:   0.1088 L12:   0.1834
REMARK   3      L13:  -0.1693 L23:  -0.1181
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1417 S12:   0.2438 S13:  -0.0714
REMARK   3      S21:  -0.2025 S22:  -0.0448 S23:  -0.0276
REMARK   3      S31:   0.0042 S32:  -0.0974 S33:  -0.0118
REMARK   3   TLS GROUP : 16
REMARK   3    SELECTION: (CHAIN B AND RESID 98:144 )
REMARK   3    ORIGIN FOR THE GROUP (A): -38.4544 -23.5370 -26.0701
REMARK   3    T TENSOR
REMARK   3      T11:   0.2540 T22:   0.3079
REMARK   3      T33:   0.2637 T12:  -0.0666
REMARK   3      T13:  -0.0257 T23:   0.0085
REMARK   3    L TENSOR
REMARK   3      L11:   0.0679 L22:   0.0820
REMARK   3      L33:   0.0611 L12:   0.0089
REMARK   3      L13:   0.0174 L23:  -0.0736
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2140 S12:   0.1602 S13:   0.1141
REMARK   3      S21:   0.0103 S22:   0.1641 S23:   0.0296
REMARK   3      S31:  -0.1654 S32:  -0.0466 S33:   0.0000
REMARK   3   TLS GROUP : 17
REMARK   3    SELECTION: (CHAIN B AND RESID 145:170 )
REMARK   3    ORIGIN FOR THE GROUP (A): -33.9992 -24.8818 -23.4770
REMARK   3    T TENSOR
REMARK   3      T11:   0.4172 T22:   0.3090
REMARK   3      T33:   0.3803 T12:  -0.0449
REMARK   3      T13:  -0.0052 T23:   0.0170
REMARK   3    L TENSOR
REMARK   3      L11:   0.1290 L22:   0.1088
REMARK   3      L33:   0.0781 L12:  -0.0556
REMARK   3      L13:  -0.0854 L23:  -0.0454
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0297 S12:  -0.0419 S13:   0.0473
REMARK   3      S21:  -0.2784 S22:   0.0948 S23:  -0.1856
REMARK   3      S31:   0.0853 S32:   0.0644 S33:   0.0000
REMARK   3   TLS GROUP : 18
REMARK   3    SELECTION: (CHAIN B AND RESID 171:190 )
REMARK   3    ORIGIN FOR THE GROUP (A): -39.5034 -17.5744 -30.1457
REMARK   3    T TENSOR
REMARK   3      T11:   0.4012 T22:   0.4736
REMARK   3      T33:   0.4154 T12:  -0.0083
REMARK   3      T13:  -0.0498 T23:   0.0656
REMARK   3    L TENSOR
REMARK   3      L11:   0.0103 L22:   0.0415
REMARK   3      L33:   0.0386 L12:  -0.0004
REMARK   3      L13:   0.0325 L23:  -0.0251
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1842 S12:   0.4443 S13:   0.1161
REMARK   3      S21:  -0.2934 S22:  -0.0445 S23:   0.1303
REMARK   3      S31:   0.0918 S32:  -0.0992 S33:   0.0000
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 4FQX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUL-12.
REMARK 100 THE RCSB ID CODE IS RCSB073243.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 20-APR-12
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 5.5
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) : 0.979
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200  DATA SCALING SOFTWARE          : HKL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34280
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3
REMARK 200  DATA REDUNDANCY                : 3.400
REMARK 200  R MERGE                    (I) : 0.05900
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 10.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30
REMARK 200  R MERGE FOR SHELL          (I) : 0.53300
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   (%): 59.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       33.09500
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       69.20800
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       60.82450
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       69.20800
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       33.09500
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       60.82450
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 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: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -68.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, A, B, E
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6460 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 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     VAL C     1
REMARK 465     PRO C     2
REMARK 465     GLU C     3
REMARK 465     ALA C     4
REMARK 465     PRO C     5
REMARK 465     THR C     6
REMARK 465     PRO C     7
REMARK 465     MET C     8
REMARK 465     TRP C     9
REMARK 465     PRO C    10
REMARK 465     ASP C    11
REMARK 465     ASP C    12
REMARK 465     LEU C    13
REMARK 465     GLN C    14
REMARK 465     VAL C   201
REMARK 465     PRO C   202
REMARK 465     ARG C   203
REMARK 465     GLY D     1
REMARK 465     GLY D     2
REMARK 465     GLY D   194
REMARK 465     CYS D   195
REMARK 465     LEU D   196
REMARK 465     VAL D   197
REMARK 465     PRO D   198
REMARK 465     ARG D   199
REMARK 465     GLY E    84
REMARK 465     LYS E    85
REMARK 465     GLN E    86
REMARK 465     LYS E    94
REMARK 465     ILE A     1
REMARK 465     ALA A   182
REMARK 465     PRO A   183
REMARK 465     SER A   184
REMARK 465     PRO A   185
REMARK 465     LEU A   186
REMARK 465     PRO A   187
REMARK 465     GLU A   188
REMARK 465     THR A   189
REMARK 465     THR A   190
REMARK 465     GLU A   191
REMARK 465     LYS B   105
REMARK 465     THR B   106
REMARK 465     GLN B   107
REMARK 465     PRO B   108
REMARK 465     LEU B   109
REMARK 465     GLN B   110
REMARK 465     HIS B   111
REMARK 465     HIS B   112
REMARK 465     ASN B   113
REMARK 465     ARG B   191
REMARK 465     SER B   192
REMARK 465     SER B   193
REMARK 465     GLY B   194
REMARK 465     GLY B   195
REMARK 465     GLY B   196
REMARK 465     SER B   197
REMARK 465     LEU B   198
REMARK 465     PRO B   199
REMARK 465     ALA B   200
REMARK 465     THR B   201
REMARK 465     GLY B   202
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     PHE C 145    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     GLU A 141    CG   CD   OE1  OE2
REMARK 470     LYS B  65    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   NH1  ARG D   110     OE2  GLU B   187              2.10
REMARK 500   ND2  ASN A   118     O5   NAG A   201              2.17
REMARK 500   O    GLN D    70     ND2  ASN D    74              2.18
REMARK 500   OE2  GLU C   181     NH1  ARG C   184              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    ASN C  50       36.32     38.27
REMARK 500    PHE C 127      117.43   -175.36
REMARK 500    GLU C 143      -64.48    -25.62
REMARK 500    ASP C 183       19.55   -153.13
REMARK 500    LEU D  13     -159.76    -86.51
REMARK 500    ASP D  21      173.19    177.79
REMARK 500    LYS D  30       -0.91     68.70
REMARK 500    GLN D  84      -46.28   -140.25
REMARK 500    PRO D 124     -170.55    -69.49
REMARK 500    HIS D 145       74.08     44.25
REMARK 500    ASP B   2       75.64     64.96
REMARK 500    ASN B  19       76.09     48.29
REMARK 500    ASN B  33     -101.47     51.00
REMARK 500    TYR B  78      -63.50   -105.68
REMARK 500    THR B  90     -151.03    -71.22
REMARK 500    PRO B 165      150.35    -48.11
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 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 202
DBREF  4FQX C    1   199  UNP    P28067   DMA_HUMAN       27    225
DBREF  4FQX D    1   193  UNP    P28068   DMB_HUMAN       19    211
DBREF  4FQX A    1   191  UNP    P01903   DRA_HUMAN       26    216
DBREF  4FQX B    1   192  UNP    P04229   2B11_HUMAN      30    221
DBREF  4FQX E   84    94  PDB    4FQX     4FQX            84     94
SEQADV 4FQX GLN C  136  UNP  P28067    HIS   162 VARIANT
SEQADV 4FQX HIS C  137  UNP  P28067    ASP   163 VARIANT
SEQADV 4FQX ASP C  165  UNP  P28067    ASN   191 ENGINEERED MUTATION
SEQADV 4FQX LEU C  200  UNP  P28067              EXPRESSION TAG
SEQADV 4FQX VAL C  201  UNP  P28067              EXPRESSION TAG
SEQADV 4FQX PRO C  202  UNP  P28067              EXPRESSION TAG
SEQADV 4FQX ARG C  203  UNP  P28067              EXPRESSION TAG
SEQADV 4FQX SER D   46  UNP  P28068    CYS    64 ENGINEERED MUTATION
SEQADV 4FQX ASP D   92  UNP  P28068    ASN   110 ENGINEERED MUTATION
SEQADV 4FQX GLY D  194  UNP  P28068              EXPRESSION TAG
SEQADV 4FQX CYS D  195  UNP  P28068              EXPRESSION TAG
SEQADV 4FQX LEU D  196  UNP  P28068              EXPRESSION TAG
SEQADV 4FQX VAL D  197  UNP  P28068              EXPRESSION TAG
SEQADV 4FQX PRO D  198  UNP  P28068              EXPRESSION TAG
SEQADV 4FQX ARG D  199  UNP  P28068              EXPRESSION TAG
SEQADV 4FQX CYS A   65  UNP  P01903    VAL    90 ENGINEERED MUTATION
SEQADV 4FQX VAL B   -5  UNP  P04229              EXPRESSION TAG
SEQADV 4FQX LEU B   -4  UNP  P04229              EXPRESSION TAG
SEQADV 4FQX PHE B   -3  UNP  P04229              EXPRESSION TAG
SEQADV 4FQX GLN B   -2  UNP  P04229              EXPRESSION TAG
SEQADV 4FQX GLY B   -1  UNP  P04229              EXPRESSION TAG
SEQADV 4FQX PRO B    0  UNP  P04229              EXPRESSION TAG
SEQADV 4FQX SER B   30  UNP  P04229    CYS    59 ENGINEERED MUTATION
SEQADV 4FQX SER B  193  UNP  P04229              EXPRESSION TAG
SEQADV 4FQX GLY B  194  UNP  P04229              EXPRESSION TAG
SEQADV 4FQX GLY B  195  UNP  P04229              EXPRESSION TAG
SEQADV 4FQX GLY B  196  UNP  P04229              EXPRESSION TAG
SEQADV 4FQX SER B  197  UNP  P04229              EXPRESSION TAG
SEQADV 4FQX LEU B  198  UNP  P04229              EXPRESSION TAG
SEQADV 4FQX PRO B  199  UNP  P04229              EXPRESSION TAG
SEQADV 4FQX ALA B  200  UNP  P04229              EXPRESSION TAG
SEQADV 4FQX THR B  201  UNP  P04229              EXPRESSION TAG
SEQADV 4FQX GLY B  202  UNP  P04229              EXPRESSION TAG
SEQRES   1 C  203  VAL PRO GLU ALA PRO THR PRO MET TRP PRO ASP ASP LEU
SEQRES   2 C  203  GLN ASN HIS THR PHE LEU HIS THR VAL TYR CYS GLN ASP
SEQRES   3 C  203  GLY SER PRO SER VAL GLY LEU SER GLU ALA TYR ASP GLU
SEQRES   4 C  203  ASP GLN LEU PHE PHE PHE ASP PHE SER GLN ASN THR ARG
SEQRES   5 C  203  VAL PRO ARG LEU PRO GLU PHE ALA ASP TRP ALA GLN GLU
SEQRES   6 C  203  GLN GLY ASP ALA PRO ALA ILE LEU PHE ASP LYS GLU PHE
SEQRES   7 C  203  CYS GLU TRP MET ILE GLN GLN ILE GLY PRO LYS LEU ASP
SEQRES   8 C  203  GLY LYS ILE PRO VAL SER ARG GLY PHE PRO ILE ALA GLU
SEQRES   9 C  203  VAL PHE THR LEU LYS PRO LEU GLU PHE GLY LYS PRO ASN
SEQRES  10 C  203  THR LEU VAL CYS PHE VAL SER ASN LEU PHE PRO PRO MET
SEQRES  11 C  203  LEU THR VAL ASN TRP GLN HIS HIS SER VAL PRO VAL GLU
SEQRES  12 C  203  GLY PHE GLY PRO THR PHE VAL SER ALA VAL ASP GLY LEU
SEQRES  13 C  203  SER PHE GLN ALA PHE SER TYR LEU ASP PHE THR PRO GLU
SEQRES  14 C  203  PRO SER ASP ILE PHE SER CYS ILE VAL THR HIS GLU ILE
SEQRES  15 C  203  ASP ARG TYR THR ALA ILE ALA TYR TRP VAL PRO ARG ASN
SEQRES  16 C  203  ALA LEU PRO SER LEU VAL PRO ARG
SEQRES   1 D  199  GLY GLY PHE VAL ALA HIS VAL GLU SER THR CYS LEU LEU
SEQRES   2 D  199  ASP ASP ALA GLY THR PRO LYS ASP PHE THR TYR CYS ILE
SEQRES   3 D  199  SER PHE ASN LYS ASP LEU LEU THR CYS TRP ASP PRO GLU
SEQRES   4 D  199  GLU ASN LYS MET ALA PRO SER GLU PHE GLY VAL LEU ASN
SEQRES   5 D  199  SER LEU ALA ASN VAL LEU SER GLN HIS LEU ASN GLN LYS
SEQRES   6 D  199  ASP THR LEU MET GLN ARG LEU ARG ASN GLY LEU GLN ASN
SEQRES   7 D  199  CYS ALA THR HIS THR GLN PRO PHE TRP GLY SER LEU THR
SEQRES   8 D  199  ASP ARG THR ARG PRO PRO SER VAL GLN VAL ALA LYS THR
SEQRES   9 D  199  THR PRO PHE ASN THR ARG GLU PRO VAL MET LEU ALA CYS
SEQRES  10 D  199  TYR VAL TRP GLY PHE TYR PRO ALA GLU VAL THR ILE THR
SEQRES  11 D  199  TRP ARG LYS ASN GLY LYS LEU VAL MET PRO HIS SER SER
SEQRES  12 D  199  ALA HIS LYS THR ALA GLN PRO ASN GLY ASP TRP THR TYR
SEQRES  13 D  199  GLN THR LEU SER HIS LEU ALA LEU THR PRO SER TYR GLY
SEQRES  14 D  199  ASP THR TYR THR CYS VAL VAL GLU HIS ILE GLY ALA PRO
SEQRES  15 D  199  GLU PRO ILE LEU ARG ASP TRP THR PRO GLY LEU GLY CYS
SEQRES  16 D  199  LEU VAL PRO ARG
SEQRES   1 E   11  GLY LYS GLN ASN CYS LEU LYS LEU ALA THR LYS
SEQRES   1 A  191  ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR
SEQRES   2 A  191  LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE
SEQRES   3 A  191  ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS
SEQRES   4 A  191  GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA
SEQRES   5 A  191  SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA CYS
SEQRES   6 A  191  ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN
SEQRES   7 A  191  TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL
SEQRES   8 A  191  LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL
SEQRES   9 A  191  LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL
SEQRES  10 A  191  ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR
SEQRES  11 A  191  GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS
SEQRES  12 A  191  LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER
SEQRES  13 A  191  THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES  14 A  191  LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP ALA
SEQRES  15 A  191  PRO SER PRO LEU PRO GLU THR THR GLU
SEQRES   1 B  208  VAL LEU PHE GLN GLY PRO GLY ASP THR ARG PRO ARG PHE
SEQRES   2 B  208  LEU TRP GLN LEU LYS PHE GLU CYS HIS PHE PHE ASN GLY
SEQRES   3 B  208  THR GLU ARG VAL ARG LEU LEU GLU ARG SER ILE TYR ASN
SEQRES   4 B  208  GLN GLU GLU SER VAL ARG PHE ASP SER ASP VAL GLY GLU
SEQRES   5 B  208  TYR ARG ALA VAL THR GLU LEU GLY ARG PRO ASP ALA GLU
SEQRES   6 B  208  TYR TRP ASN SER GLN LYS ASP LEU LEU GLU GLN ARG ARG
SEQRES   7 B  208  ALA ALA VAL ASP THR TYR CYS ARG HIS ASN TYR GLY VAL
SEQRES   8 B  208  GLY GLU SER PHE THR VAL GLN ARG ARG VAL GLU PRO LYS
SEQRES   9 B  208  VAL THR VAL TYR PRO SER LYS THR GLN PRO LEU GLN HIS
SEQRES  10 B  208  HIS ASN LEU LEU VAL CYS SER VAL SER GLY PHE TYR PRO
SEQRES  11 B  208  GLY SER ILE GLU VAL ARG TRP PHE ARG ASN GLY GLN GLU
SEQRES  12 B  208  GLU LYS ALA GLY VAL VAL SER THR GLY LEU ILE GLN ASN
SEQRES  13 B  208  GLY ASP TRP THR PHE GLN THR LEU VAL MET LEU GLU THR
SEQRES  14 B  208  VAL PRO ARG SER GLY GLU VAL TYR THR CYS GLN VAL GLU
SEQRES  15 B  208  HIS PRO SER VAL THR SER PRO LEU THR VAL GLU TRP ARG
SEQRES  16 B  208  ALA ARG SER SER GLY GLY GLY SER LEU PRO ALA THR GLY
MODRES 4FQX ASN A  118  ASN  GLYCOSYLATION SITE
HET    NAG  A 201      14
HET    NAG  A 202      14
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
FORMUL   6  NAG    2(C8 H15 N O6)
FORMUL   7  HOH   *124(H2 O)
HELIX    1   1 LEU C   56  GLU C   65  5                                  10
HELIX    2   2 ASP C   68  ASP C   91  1                                  24
HELIX    3   3 LEU D   51  ASN D   63  1                                  13
HELIX    4   4 LYS D   65  GLN D   70  1                                   6
HELIX    5   5 ASN D   74  THR D   83  1                                  10
HELIX    6   6 SER D   89  ARG D   93  5                                   5
HELIX    7   7 LEU A   45  GLU A   47  5                                   3
HELIX    8   8 PHE A   48  ALA A   56  1                                   9
HELIX    9   9 GLY A   58  SER A   77  1                                  20
HELIX   10  10 THR B   51  LEU B   53  5                                   3
HELIX   11  11 GLY B   54  SER B   63  1                                  10
HELIX   12  12 GLN B   64  ALA B   73  1                                  10
HELIX   13  13 ALA B   73  TYR B   78  1                                   6
HELIX   14  14 TYR B   78  VAL B   85  1                                   8
SHEET    1   A 8 THR C  51  PRO C  54  0
SHEET    2   A 8 ASP C  40  ASP C  46 -1  N  ASP C  46   O  THR C  51
SHEET    3   A 8 VAL C  31  TYR C  37 -1  N  GLU C  35   O  LEU C  42
SHEET    4   A 8 PHE C  18  GLN C  25 -1  N  TYR C  23   O  GLY C  32
SHEET    5   A 8 VAL D   4  CYS D  11 -1  O  VAL D   7   N  VAL C  22
SHEET    6   A 8 PHE D  22  PHE D  28 -1  O  CYS D  25   N  GLU D   8
SHEET    7   A 8 ASP D  31  ASP D  37 -1  O  TRP D  36   N  TYR D  24
SHEET    8   A 8 LYS D  42  PRO D  45 -1  O  ALA D  44   N  CYS D  35
SHEET    1   B 9 VAL C  96  ARG C  98  0
SHEET    2   B 9 GLU A  40  TRP A  43  1  O  THR A  41   N  ARG C  98
SHEET    3   B 9 ASP A  29  ASP A  35 -1  N  HIS A  33   O  VAL A  42
SHEET    4   B 9 SER A  19  PHE A  26 -1  N  PHE A  26   O  ASP A  29
SHEET    5   B 9 HIS A   5  ASN A  15 -1  N  LEU A  14   O  SER A  19
SHEET    6   B 9 PHE B   7  PHE B  18 -1  O  CYS B  15   N  ILE A   7
SHEET    7   B 9 ARG B  23  TYR B  32 -1  O  ARG B  23   N  PHE B  18
SHEET    8   B 9 GLU B  35  ASP B  41 -1  O  GLU B  35   N  TYR B  32
SHEET    9   B 9 TYR B  47  ALA B  49 -1  O  ARG B  48   N  ARG B  39
SHEET    1   C 4 ILE C 102  THR C 107  0
SHEET    2   C 4 ASN C 117  LEU C 126 -1  O  SER C 124   N  ILE C 102
SHEET    3   C 4 SER C 157  PHE C 166 -1  O  ALA C 160   N  VAL C 123
SHEET    4   C 4 THR C 148  VAL C 153 -1  N  SER C 151   O  GLN C 159
SHEET    1   D 4 VAL C 140  PRO C 141  0
SHEET    2   D 4 LEU C 131  HIS C 137 -1  N  HIS C 137   O  VAL C 140
SHEET    3   D 4 PHE C 174  HIS C 180 -1  O  THR C 179   N  THR C 132
SHEET    4   D 4 THR C 186  TRP C 191 -1  O  ALA C 187   N  VAL C 178
SHEET    1   E 4 SER D  98  THR D 104  0
SHEET    2   E 4 VAL D 113  PHE D 122 -1  O  ALA D 116   N  ALA D 102
SHEET    3   E 4 TYR D 156  LEU D 164 -1  O  SER D 160   N  CYS D 117
SHEET    4   E 4 GLN D 149  PRO D 150 -1  N  GLN D 149   O  GLN D 157
SHEET    1   F 4 LYS D 136  VAL D 138  0
SHEET    2   F 4 THR D 128  LYS D 133 -1  N  LYS D 133   O  LYS D 136
SHEET    3   F 4 TYR D 172  GLU D 177 -1  O  GLU D 177   N  THR D 128
SHEET    4   F 4 ILE D 185  TRP D 189 -1  O  ARG D 187   N  CYS D 174
SHEET    1   G 4 GLU A  88  THR A  93  0
SHEET    2   G 4 ASN A 103  PHE A 112 -1  O  ASP A 110   N  GLU A  88
SHEET    3   G 4 PHE A 145  PHE A 153 -1  O  PHE A 153   N  ASN A 103
SHEET    4   G 4 SER A 133  GLU A 134 -1  N  SER A 133   O  TYR A 150
SHEET    1   H 4 GLU A  88  THR A  93  0
SHEET    2   H 4 ASN A 103  PHE A 112 -1  O  ASP A 110   N  GLU A  88
SHEET    3   H 4 PHE A 145  PHE A 153 -1  O  PHE A 153   N  ASN A 103
SHEET    4   H 4 LEU A 138  PRO A 139 -1  N  LEU A 138   O  ARG A 146
SHEET    1   I 4 LYS A 126  PRO A 127  0
SHEET    2   I 4 ASN A 118  ARG A 123 -1  N  ARG A 123   O  LYS A 126
SHEET    3   I 4 VAL A 160  GLU A 166 -1  O  ASP A 162   N  LEU A 122
SHEET    4   I 4 LEU A 174  GLU A 179 -1  O  TRP A 178   N  TYR A 161
SHEET    1   J 4 LYS B  98  TYR B 102  0
SHEET    2   J 4 LEU B 115  PHE B 122 -1  O  VAL B 116   N  TYR B 102
SHEET    3   J 4 PHE B 155  LEU B 161 -1  O  LEU B 161   N  LEU B 115
SHEET    4   J 4 VAL B 142  SER B 144 -1  N  VAL B 143   O  MET B 160
SHEET    1   K 4 LYS B  98  TYR B 102  0
SHEET    2   K 4 LEU B 115  PHE B 122 -1  O  VAL B 116   N  TYR B 102
SHEET    3   K 4 PHE B 155  LEU B 161 -1  O  LEU B 161   N  LEU B 115
SHEET    4   K 4 ILE B 148  GLN B 149 -1  N  ILE B 148   O  GLN B 156
SHEET    1   L 4 GLN B 136  GLU B 137  0
SHEET    2   L 4 GLU B 128  ARG B 133 -1  N  ARG B 133   O  GLN B 136
SHEET    3   L 4 TYR B 171  GLU B 176 -1  O  GLN B 174   N  ARG B 130
SHEET    4   L 4 LEU B 184  TRP B 188 -1  O  LEU B 184   N  VAL B 175
SSBOND   1 CYS C   24    CYS C   79                          1555   1555  2.04
SSBOND   2 CYS C  121    CYS C  176                          1555   1555  2.03
SSBOND   3 CYS D   11    CYS D   79                          1555   1555  2.03
SSBOND   4 CYS D   25    CYS D   35                          1555   1555  2.04
SSBOND   5 CYS D  117    CYS D  174                          1555   1555  2.02
SSBOND   6 CYS E   88    CYS A   65                          1555   1555  2.04
SSBOND   7 CYS A  107    CYS A  163                          1555   1555  2.04
SSBOND   8 CYS B   15    CYS B   79                          1555   1555  2.09
SSBOND   9 CYS B  117    CYS B  173                          1555   1555  2.03
LINK         ND2 ASN A 118                 C1  NAG A 201     1555   1555  1.45
LINK         O4  NAG A 201                 C1  NAG A 202     1555   1555  1.46
CISPEP   1 SER C   28    PRO C   29          0         0.48
CISPEP   2 PHE C  127    PRO C  128          0         0.16
CISPEP   3 TYR D  123    PRO D  124          0        -0.53
CISPEP   4 ASN A   15    PRO A   16          0         3.46
CISPEP   5 THR A  113    PRO A  114          0        -4.02
CISPEP   6 TYR B  123    PRO B  124          0         3.04
SITE     1 AC1  5 ASN A 118  GLU A 166  TRP A 168  NAG A 202
SITE     2 AC1  5 HOH A 307
SITE     1 AC2  2 NAG A 201  GLY B   1
CRYST1   66.190  121.649  138.416  90.00  90.00  90.00 P 21 21 21    4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.015108  0.000000  0.000000        0.00000
SCALE2      0.000000  0.008220  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007225        0.00000
      
PROCHECK
Go to PROCHECK summary
 References