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PDBsum entry 4gs0

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Hydrolase/transferase PDB id
4gs0
Jmol
Contents
Protein chains
279 a.a.
258 a.a.
Ligands
UNK-UNK-FTY-UNK
Waters ×287
HEADER    HYDROLASE/TRANSFERASE                   27-AUG-12   4GS0
TITLE     CRYSTAL STRUCTURE OF SHP1 CATALYTIC DOMAIN WITH JAK1 ACTIVATION LOOP
TITLE    2 PEPTIDE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 6;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: PHOSPHATASE DOMAIN (UNP RESIDUES 242-528);
COMPND   5 SYNONYM: HEMATOPOIETIC CELL PROTEIN-TYROSINE PHOSPHATASE, PROTEIN-
COMPND   6 TYROSINE PHOSPHATASE 1C, PTP-1C, PROTEIN-TYROSINE PHOSPHATASE SHP-1,
COMPND   7 SH-PTP1;
COMPND   8 EC: 3.1.3.48;
COMPND   9 ENGINEERED: YES;
COMPND  10 MOL_ID: 2;
COMPND  11 MOLECULE: TYROSINE-PROTEIN KINASE JAK1;
COMPND  12 CHAIN: C;
COMPND  13 FRAGMENT: JAK1 ACTIVATION LOOP PHOPHOMIMETIC (UNP RESIDUES 1032-
COMPND  14 1037);
COMPND  15 SYNONYM: JANUS KINASE 1, JAK-1;
COMPND  16 EC: 2.7.10.2;
COMPND  17 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: HCP, PTP1C, PTPN6, SHP-1;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3);
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-32;
SOURCE  11 MOL_ID: 2;
SOURCE  12 SYNTHETIC: YES;
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  14 ORGANISM_COMMON: HUMAN;
SOURCE  15 ORGANISM_TAXID: 9606
KEYWDS    PROTEIN-PROTEIN COMPLEX, PHOSPHATASE DOMAIN, HYDROLASE, HYDROLASE-
KEYWDS   2 TRANSFERASE COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    N.L.ALICEA-VELAZQUEZ,J.JAKONCIC,T.J.BOGGON
REVDAT   3   06-MAR-13 4GS0    1       JRNL
REVDAT   2   23-JAN-13 4GS0    1       JRNL
REVDAT   1   19-DEC-12 4GS0    0
JRNL        AUTH   N.L.ALICEA-VELAZQUEZ,J.JAKONCIC,T.J.BOGGON
JRNL        TITL   STRUCTURE-GUIDED STUDIES OF THE SHP-1/JAK1 INTERACTION
JRNL        TITL 2 PROVIDE NEW INSIGHTS INTO PHOSPHATASE CATALYTIC DOMAIN
JRNL        TITL 3 SUBSTRATE RECOGNITION.
JRNL        REF    J.STRUCT.BIOL.                V. 181   243 2013
JRNL        REFN                   ISSN 1047-8477
JRNL        PMID   23296072
JRNL        DOI    10.1016/J.JSB.2012.12.009
REMARK   2
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.2_869)
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) : 1.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.02
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.980
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.4
REMARK   3   NUMBER OF REFLECTIONS             : 51204
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.163
REMARK   3   R VALUE            (WORKING SET) : 0.162
REMARK   3   FREE R VALUE                     : 0.195
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.110
REMARK   3   FREE R VALUE TEST SET COUNT      : 2618
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 43.0310 -  4.7905    1.00     2589   134  0.1762 0.1973
REMARK   3     2  4.7905 -  3.8031    0.99     2598   136  0.1360 0.1467
REMARK   3     3  3.8031 -  3.3226    0.98     2499   145  0.1457 0.1858
REMARK   3     4  3.3226 -  3.0189    0.98     2614   123  0.1523 0.1678
REMARK   3     5  3.0189 -  2.8026    0.98     2523   140  0.1614 0.1891
REMARK   3     6  2.8026 -  2.6374    0.99     2587   113  0.1658 0.2346
REMARK   3     7  2.6374 -  2.5053    0.99     2584   152  0.1565 0.2059
REMARK   3     8  2.5053 -  2.3962    0.98     2518   134  0.1562 0.2014
REMARK   3     9  2.3962 -  2.3040    0.98     2473   134  0.1554 0.1927
REMARK   3    10  2.3040 -  2.2245    0.99     2603   145  0.1513 0.2005
REMARK   3    11  2.2245 -  2.1549    0.99     2593   150  0.1576 0.1825
REMARK   3    12  2.1549 -  2.0933    0.99     2500   128  0.1581 0.2066
REMARK   3    13  2.0933 -  2.0382    0.98     2597   128  0.1642 0.2033
REMARK   3    14  2.0382 -  1.9885    0.98     2577   123  0.1780 0.2375
REMARK   3    15  1.9885 -  1.9433    0.99     2578   148  0.1877 0.2335
REMARK   3    16  1.9433 -  1.9019    0.99     2481   161  0.1964 0.2372
REMARK   3    17  1.9019 -  1.8639    0.99     2645   148  0.2180 0.2736
REMARK   3    18  1.8639 -  1.8287    1.00     2511   146  0.2427 0.2854
REMARK   3    19  1.8287 -  1.7961    0.94     2516   130  0.2613 0.3309
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 0.90
REMARK   3   SHRINKAGE RADIUS   : 0.60
REMARK   3   K_SOL              : 0.37
REMARK   3   B_SOL              : 49.98
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.420
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.270
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 23.30
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.87460
REMARK   3    B22 (A**2) : -0.87460
REMARK   3    B33 (A**2) : 1.74920
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      :  0.007           4555
REMARK   3   ANGLE     :  1.062           6195
REMARK   3   CHIRALITY :  0.074            672
REMARK   3   PLANARITY :  0.004            807
REMARK   3   DIHEDRAL  : 16.380           1760
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 21
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: chain 'A' and (resseq 243:257)
REMARK   3    ORIGIN FOR THE GROUP (A):  37.9094 -15.3626 -15.0191
REMARK   3    T TENSOR
REMARK   3      T11:   0.5384 T22:   0.2950
REMARK   3      T33:   0.5629 T12:  -0.0618
REMARK   3      T13:  -0.0415 T23:  -0.0763
REMARK   3    L TENSOR
REMARK   3      L11:   4.6001 L22:   3.9898
REMARK   3      L33:   2.7056 L12:   4.1593
REMARK   3      L13:  -2.4627 L23:  -2.7941
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2709 S12:   0.6287 S13:  -1.3000
REMARK   3      S21:   0.1481 S22:  -0.0384 S23:   0.3124
REMARK   3      S31:  -0.0683 S32:  -0.0695 S33:   0.2417
REMARK   3   TLS GROUP : 2
REMARK   3    SELECTION: chain 'A' and (resseq 258:273)
REMARK   3    ORIGIN FOR THE GROUP (A):  26.9136 -13.7176   5.9683
REMARK   3    T TENSOR
REMARK   3      T11:   0.3315 T22:   0.0933
REMARK   3      T33:   0.2131 T12:   0.1895
REMARK   3      T13:  -0.0048 T23:  -0.0451
REMARK   3    L TENSOR
REMARK   3      L11:   2.9805 L22:   4.3494
REMARK   3      L33:   3.9159 L12:  -0.4864
REMARK   3      L13:  -0.0142 L23:   1.8999
REMARK   3    S TENSOR
REMARK   3      S11:   0.0681 S12:   0.3509 S13:  -0.4390
REMARK   3      S21:  -0.3820 S22:  -0.0865 S23:   0.1150
REMARK   3      S31:   0.1599 S32:   0.1768 S33:  -0.0066
REMARK   3   TLS GROUP : 3
REMARK   3    SELECTION: chain 'A' and (resseq 274:320)
REMARK   3    ORIGIN FOR THE GROUP (A):  23.8798  -5.8761   1.7211
REMARK   3    T TENSOR
REMARK   3      T11:   0.2093 T22:   0.0975
REMARK   3      T33:   0.1627 T12:   0.0823
REMARK   3      T13:   0.0435 T23:  -0.0014
REMARK   3    L TENSOR
REMARK   3      L11:   3.4766 L22:   1.9284
REMARK   3      L33:   3.9946 L12:   0.8638
REMARK   3      L13:   1.2679 L23:  -0.2126
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0491 S12:   0.2605 S13:  -0.0611
REMARK   3      S21:  -0.2903 S22:   0.0234 S23:  -0.2274
REMARK   3      S31:   0.2063 S32:   0.1818 S33:   0.0141
REMARK   3   TLS GROUP : 4
REMARK   3    SELECTION: chain 'A' and (resseq 321:342)
REMARK   3    ORIGIN FOR THE GROUP (A):  20.0546   2.3220   6.6239
REMARK   3    T TENSOR
REMARK   3      T11:   0.2070 T22:   0.1204
REMARK   3      T33:   0.1840 T12:   0.0542
REMARK   3      T13:   0.0121 T23:  -0.0055
REMARK   3    L TENSOR
REMARK   3      L11:   0.9536 L22:   1.4683
REMARK   3      L33:   1.6875 L12:   0.3588
REMARK   3      L13:   0.6350 L23:  -0.4387
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0566 S12:  -0.0378 S13:   0.0838
REMARK   3      S21:  -0.0270 S22:  -0.0925 S23:  -0.0243
REMARK   3      S31:  -0.0548 S32:   0.0050 S33:   0.1375
REMARK   3   TLS GROUP : 5
REMARK   3    SELECTION: chain 'A' and (resseq 343:359)
REMARK   3    ORIGIN FOR THE GROUP (A):   8.1775   0.6233   7.1912
REMARK   3    T TENSOR
REMARK   3      T11:   0.1902 T22:   0.1380
REMARK   3      T33:   0.2029 T12:   0.0533
REMARK   3      T13:  -0.0012 T23:  -0.0404
REMARK   3    L TENSOR
REMARK   3      L11:   7.6334 L22:   4.0235
REMARK   3      L33:   8.5655 L12:   4.0680
REMARK   3      L13:  -5.3347 L23:  -4.0902
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0700 S12:  -0.2667 S13:  -0.0252
REMARK   3      S21:  -0.1223 S22:  -0.0734 S23:   0.2383
REMARK   3      S31:   0.1356 S32:  -0.2891 S33:   0.1228
REMARK   3   TLS GROUP : 6
REMARK   3    SELECTION: chain 'A' and (resseq 360:386)
REMARK   3    ORIGIN FOR THE GROUP (A):  12.7726  11.3520  11.9460
REMARK   3    T TENSOR
REMARK   3      T11:   0.2032 T22:   0.1469
REMARK   3      T33:   0.2531 T12:   0.1119
REMARK   3      T13:  -0.0269 T23:  -0.0645
REMARK   3    L TENSOR
REMARK   3      L11:   0.7431 L22:   1.6300
REMARK   3      L33:   0.5579 L12:  -0.7658
REMARK   3      L13:  -0.0500 L23:  -0.2475
REMARK   3    S TENSOR
REMARK   3      S11:   0.0015 S12:  -0.0970 S13:   0.2609
REMARK   3      S21:   0.1150 S22:  -0.1507 S23:   0.4638
REMARK   3      S31:  -0.1849 S32:  -0.3036 S33:   0.0301
REMARK   3   TLS GROUP : 7
REMARK   3    SELECTION: chain 'A' and (resseq 387:441)
REMARK   3    ORIGIN FOR THE GROUP (A):   7.5810   7.7904   0.6191
REMARK   3    T TENSOR
REMARK   3      T11:   0.2169 T22:   0.1316
REMARK   3      T33:   0.2285 T12:   0.0999
REMARK   3      T13:   0.0003 T23:  -0.0010
REMARK   3    L TENSOR
REMARK   3      L11:   3.4218 L22:   2.2741
REMARK   3      L33:   2.1327 L12:   1.7796
REMARK   3      L13:   1.6652 L23:   0.6693
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1067 S12:  -0.0751 S13:   0.4099
REMARK   3      S21:  -0.1386 S22:  -0.0801 S23:   0.3790
REMARK   3      S31:  -0.2353 S32:  -0.2021 S33:   0.1581
REMARK   3   TLS GROUP : 8
REMARK   3    SELECTION: chain 'A' and (resseq 442:501)
REMARK   3    ORIGIN FOR THE GROUP (A):  10.9162  -5.0236  -8.7671
REMARK   3    T TENSOR
REMARK   3      T11:   0.2424 T22:   0.1471
REMARK   3      T33:   0.1300 T12:   0.0508
REMARK   3      T13:   0.0023 T23:   0.0150
REMARK   3    L TENSOR
REMARK   3      L11:   3.4692 L22:   2.5540
REMARK   3      L33:   3.5905 L12:   0.1863
REMARK   3      L13:   0.3312 L23:   0.3989
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0022 S12:   0.5082 S13:   0.0679
REMARK   3      S21:  -0.3668 S22:  -0.0059 S23:   0.0263
REMARK   3      S31:   0.1831 S32:  -0.1153 S33:  -0.0162
REMARK   3   TLS GROUP : 9
REMARK   3    SELECTION: chain 'A' and (resseq 502:527)
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.8285  -2.9716 -15.4756
REMARK   3    T TENSOR
REMARK   3      T11:   0.2558 T22:   0.2815
REMARK   3      T33:   0.1489 T12:  -0.0372
REMARK   3      T13:   0.0007 T23:   0.0267
REMARK   3    L TENSOR
REMARK   3      L11:   4.8445 L22:   9.2310
REMARK   3      L33:   2.9519 L12:  -2.6492
REMARK   3      L13:   2.3559 L23:  -4.6389
REMARK   3    S TENSOR
REMARK   3      S11:   0.0977 S12:   0.6799 S13:   0.0157
REMARK   3      S21:  -0.5418 S22:   0.1783 S23:   0.3532
REMARK   3      S31:   0.3334 S32:  -0.3064 S33:  -0.2916
REMARK   3   TLS GROUP : 10
REMARK   3    SELECTION: chain 'B' and (resseq 260:273)
REMARK   3    ORIGIN FOR THE GROUP (A):  18.4956  11.5997  28.2490
REMARK   3    T TENSOR
REMARK   3      T11:   0.2429 T22:   0.0753
REMARK   3      T33:   0.1972 T12:   0.2266
REMARK   3      T13:  -0.0659 T23:  -0.0815
REMARK   3    L TENSOR
REMARK   3      L11:   3.0619 L22:   4.7396
REMARK   3      L33:   3.4432 L12:  -1.7837
REMARK   3      L13:  -0.9470 L23:   0.8546
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2016 S12:  -0.1546 S13:   0.2377
REMARK   3      S21:   0.3061 S22:  -0.0677 S23:   0.0833
REMARK   3      S31:  -0.1462 S32:  -0.0719 S33:   0.1017
REMARK   3   TLS GROUP : 11
REMARK   3    SELECTION: chain 'B' and (resseq 274:290)
REMARK   3    ORIGIN FOR THE GROUP (A):  21.4496   6.7282  33.1096
REMARK   3    T TENSOR
REMARK   3      T11:   0.2681 T22:   0.2059
REMARK   3      T33:   0.1571 T12:   0.1621
REMARK   3      T13:  -0.0571 T23:  -0.0271
REMARK   3    L TENSOR
REMARK   3      L11:   2.3923 L22:   4.4374
REMARK   3      L33:   3.3574 L12:  -0.1691
REMARK   3      L13:  -1.3964 L23:   1.6276
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1378 S12:  -0.1688 S13:   0.4847
REMARK   3      S21:   0.1789 S22:   0.0833 S23:  -0.1500
REMARK   3      S31:  -0.2290 S32:  -0.3016 S33:   0.0048
REMARK   3   TLS GROUP : 12
REMARK   3    SELECTION: chain 'B' and (resseq 291:320)
REMARK   3    ORIGIN FOR THE GROUP (A):  29.0460   7.4417  34.4015
REMARK   3    T TENSOR
REMARK   3      T11:   0.1997 T22:   0.1490
REMARK   3      T33:   0.1888 T12:   0.0890
REMARK   3      T13:  -0.0549 T23:  -0.0589
REMARK   3    L TENSOR
REMARK   3      L11:   2.8759 L22:   2.7321
REMARK   3      L33:   5.8957 L12:   0.3695
REMARK   3      L13:   0.2536 L23:  -1.1803
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0186 S12:  -0.2890 S13:   0.3430
REMARK   3      S21:   0.3170 S22:  -0.1054 S23:  -0.1865
REMARK   3      S31:  -0.3197 S32:   0.4324 S33:   0.1050
REMARK   3   TLS GROUP : 13
REMARK   3    SELECTION: chain 'B' and (resseq 321:342)
REMARK   3    ORIGIN FOR THE GROUP (A):  28.9033  -1.3908  29.6148
REMARK   3    T TENSOR
REMARK   3      T11:   0.1895 T22:   0.1425
REMARK   3      T33:   0.1822 T12:   0.0879
REMARK   3      T13:  -0.0081 T23:  -0.0203
REMARK   3    L TENSOR
REMARK   3      L11:   0.9859 L22:   0.6726
REMARK   3      L33:   1.3817 L12:  -0.1146
REMARK   3      L13:  -0.1860 L23:  -0.1857
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1785 S12:  -0.0700 S13:   0.1242
REMARK   3      S21:   0.0012 S22:   0.0890 S23:  -0.0209
REMARK   3      S31:  -0.1423 S32:  -0.0959 S33:   0.0738
REMARK   3   TLS GROUP : 14
REMARK   3    SELECTION: chain 'B' and (resseq 343:359)
REMARK   3    ORIGIN FOR THE GROUP (A):  22.1857 -10.5965  34.1342
REMARK   3    T TENSOR
REMARK   3      T11:   0.2459 T22:   0.2376
REMARK   3      T33:   0.2623 T12:   0.0801
REMARK   3      T13:  -0.0182 T23:  -0.0328
REMARK   3    L TENSOR
REMARK   3      L11:   1.5687 L22:   5.3947
REMARK   3      L33:   3.8568 L12:   2.8060
REMARK   3      L13:   1.0454 L23:   0.8198
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1372 S12:  -0.2805 S13:   0.5211
REMARK   3      S21:  -0.0880 S22:  -0.0404 S23:   0.7165
REMARK   3      S31:   0.2204 S32:  -0.5481 S33:   0.1273
REMARK   3   TLS GROUP : 15
REMARK   3    SELECTION: chain 'B' and (resseq 360:386)
REMARK   3    ORIGIN FOR THE GROUP (A):  30.9597 -13.6062  25.5289
REMARK   3    T TENSOR
REMARK   3      T11:   0.2517 T22:   0.1464
REMARK   3      T33:   0.1793 T12:   0.0541
REMARK   3      T13:   0.0267 T23:  -0.0325
REMARK   3    L TENSOR
REMARK   3      L11:   3.2204 L22:   2.8753
REMARK   3      L33:   1.5279 L12:  -1.5701
REMARK   3      L13:  -0.5437 L23:  -0.1108
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0952 S12:  -0.0074 S13:  -0.3659
REMARK   3      S21:   0.0660 S22:  -0.0324 S23:   0.0382
REMARK   3      S31:   0.3387 S32:  -0.0083 S33:   0.1108
REMARK   3   TLS GROUP : 16
REMARK   3    SELECTION: chain 'B' and (resseq 387:399)
REMARK   3    ORIGIN FOR THE GROUP (A):  32.4698 -16.1082  34.0719
REMARK   3    T TENSOR
REMARK   3      T11:   0.3157 T22:   0.1168
REMARK   3      T33:   0.2014 T12:   0.0908
REMARK   3      T13:   0.0311 T23:  -0.0062
REMARK   3    L TENSOR
REMARK   3      L11:   6.0284 L22:   6.8034
REMARK   3      L33:   6.3261 L12:   3.3093
REMARK   3      L13:  -3.2021 L23:  -4.3490
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1840 S12:  -0.3651 S13:  -0.5569
REMARK   3      S21:   0.2619 S22:  -0.0391 S23:  -0.0423
REMARK   3      S31:   0.5747 S32:   0.2149 S33:   0.2910
REMARK   3   TLS GROUP : 17
REMARK   3    SELECTION: chain 'B' and (resseq 400:414)
REMARK   3    ORIGIN FOR THE GROUP (A):  38.1821  -9.2909  30.6977
REMARK   3    T TENSOR
REMARK   3      T11:   0.2105 T22:   0.1837
REMARK   3      T33:   0.1939 T12:   0.0915
REMARK   3      T13:  -0.0326 T23:  -0.0399
REMARK   3    L TENSOR
REMARK   3      L11:   3.4300 L22:   2.3848
REMARK   3      L33:   6.2370 L12:   1.1095
REMARK   3      L13:  -2.4209 L23:  -2.7205
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1443 S12:  -0.3798 S13:  -0.2053
REMARK   3      S21:   0.0375 S22:  -0.2151 S23:  -0.4594
REMARK   3      S31:   0.1877 S32:   0.8092 S33:   0.3757
REMARK   3   TLS GROUP : 18
REMARK   3    SELECTION: chain 'B' and (resseq 415:441)
REMARK   3    ORIGIN FOR THE GROUP (A):  25.2651 -14.0822  46.0181
REMARK   3    T TENSOR
REMARK   3      T11:   0.2797 T22:   0.2740
REMARK   3      T33:   0.1758 T12:   0.0703
REMARK   3      T13:  -0.0119 T23:   0.0409
REMARK   3    L TENSOR
REMARK   3      L11:   6.2345 L22:   4.4108
REMARK   3      L33:   5.2291 L12:   1.4865
REMARK   3      L13:  -2.0624 L23:  -0.4575
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1307 S12:  -0.3101 S13:  -0.7538
REMARK   3      S21:   0.1416 S22:   0.1123 S23:   0.1026
REMARK   3      S31:   0.3870 S32:  -0.4524 S33:   0.0136
REMARK   3   TLS GROUP : 19
REMARK   3    SELECTION: chain 'B' and (resseq 442:457)
REMARK   3    ORIGIN FOR THE GROUP (A):  31.1523  -4.2651  39.0525
REMARK   3    T TENSOR
REMARK   3      T11:   0.2077 T22:   0.1784
REMARK   3      T33:   0.1461 T12:   0.0919
REMARK   3      T13:  -0.0071 T23:  -0.0009
REMARK   3    L TENSOR
REMARK   3      L11:   0.0677 L22:   4.1507
REMARK   3      L33:   4.1826 L12:   0.3379
REMARK   3      L13:   0.3714 L23:  -0.4684
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2078 S12:  -0.2625 S13:  -0.2437
REMARK   3      S21:   0.2102 S22:   0.0335 S23:  -0.3234
REMARK   3      S31:  -0.1172 S32:   0.1878 S33:   0.1513
REMARK   3   TLS GROUP : 20
REMARK   3    SELECTION: chain 'B' and (resseq 458:523)
REMARK   3    ORIGIN FOR THE GROUP (A):  23.5317  -4.0000  53.8696
REMARK   3    T TENSOR
REMARK   3      T11:   0.4524 T22:   0.4998
REMARK   3      T33:   0.1170 T12:   0.2233
REMARK   3      T13:   0.0390 T23:  -0.0438
REMARK   3    L TENSOR
REMARK   3      L11:   1.9677 L22:   2.9914
REMARK   3      L33:   0.1464 L12:   0.0743
REMARK   3      L13:  -0.1501 L23:  -0.5901
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1664 S12:  -0.8655 S13:  -0.0347
REMARK   3      S21:   1.0301 S22:   0.1528 S23:  -0.0599
REMARK   3      S31:  -0.6567 S32:  -0.6727 S33:   0.0244
REMARK   3   TLS GROUP : 21
REMARK   3    SELECTION: chain 'C'
REMARK   3    ORIGIN FOR THE GROUP (A):  10.7162  -1.8188  35.9366
REMARK   3    T TENSOR
REMARK   3      T11:   0.4603 T22:   1.1042
REMARK   3      T33:   0.3060 T12:   0.0123
REMARK   3      T13:   0.0126 T23:   0.1458
REMARK   3    L TENSOR
REMARK   3      L11:   3.8862 L22:   4.5204
REMARK   3      L33:   4.1674 L12:  -4.0851
REMARK   3      L13:   4.0230 L23:  -4.2512
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0928 S12:  -0.1013 S13:  -0.0715
REMARK   3      S21:  -0.3566 S22:   0.2557 S23:   0.2051
REMARK   3      S31:   0.2562 S32:  -0.7790 S33:  -0.4607
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 4GS0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-SEP-12.
REMARK 100 THE RCSB ID CODE IS RCSB074563.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 16-FEB-12
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 24-ID-C
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795
REMARK 200  MONOCHROMATOR                  : SI(111)
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : PIXEL
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 51289
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.796
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     (%) : 98.6
REMARK 200  DATA REDUNDANCY                : 3.900
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.08600
REMARK 200   FOR THE DATA SET  : 13.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.66900
REMARK 200   FOR SHELL         : 2.000
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: PDB ENTRY 1FPR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 38.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M CALCIUM ACETATE, 13% PEG3350, PH
REMARK 280  8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
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
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       86.03733
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      172.07467
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET A   221
REMARK 465     HIS A   222
REMARK 465     HIS A   223
REMARK 465     HIS A   224
REMARK 465     HIS A   225
REMARK 465     HIS A   226
REMARK 465     HIS A   227
REMARK 465     GLY A   228
REMARK 465     SER A   229
REMARK 465     LEU A   230
REMARK 465     VAL A   231
REMARK 465     PRO A   232
REMARK 465     ARG A   233
REMARK 465     SER A   234
REMARK 465     GLU A   235
REMARK 465     ASN A   236
REMARK 465     LEU A   237
REMARK 465     TYR A   238
REMARK 465     PHE A   239
REMARK 465     GLN A   240
REMARK 465     GLY A   241
REMARK 465     SER A   242
REMARK 465     GLY A   313
REMARK 465     PRO A   314
REMARK 465     ASP A   315
REMARK 465     GLU A   316
REMARK 465     ASN A   317
REMARK 465     ALA A   318
REMARK 465     SER A   528
REMARK 465     MET B   221
REMARK 465     HIS B   222
REMARK 465     HIS B   223
REMARK 465     HIS B   224
REMARK 465     HIS B   225
REMARK 465     HIS B   226
REMARK 465     HIS B   227
REMARK 465     GLY B   228
REMARK 465     SER B   229
REMARK 465     LEU B   230
REMARK 465     VAL B   231
REMARK 465     PRO B   232
REMARK 465     ARG B   233
REMARK 465     SER B   234
REMARK 465     GLU B   235
REMARK 465     ASN B   236
REMARK 465     LEU B   237
REMARK 465     TYR B   238
REMARK 465     PHE B   239
REMARK 465     GLN B   240
REMARK 465     GLY B   241
REMARK 465     SER B   242
REMARK 465     GLY B   243
REMARK 465     PHE B   244
REMARK 465     TRP B   245
REMARK 465     GLU B   246
REMARK 465     GLU B   247
REMARK 465     PHE B   248
REMARK 465     GLU B   249
REMARK 465     SER B   250
REMARK 465     LEU B   251
REMARK 465     GLN B   252
REMARK 465     LYS B   253
REMARK 465     GLN B   254
REMARK 465     GLU B   255
REMARK 465     VAL B   256
REMARK 465     LYS B   257
REMARK 465     ASN B   258
REMARK 465     LEU B   259
REMARK 465     GLY B   313
REMARK 465     PRO B   314
REMARK 465     ASP B   315
REMARK 465     GLU B   316
REMARK 465     ASN B   317
REMARK 465     ALA B   318
REMARK 465     GLU B   524
REMARK 465     VAL B   525
REMARK 465     LEU B   526
REMARK 465     GLN B   527
REMARK 465     SER B   528
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     HIS B 260    CG   ND1  CD2  CE1  NE2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480   M RES C SSEQI ATOMS
REMARK 480     GLN B  489   CD
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 A   454     O    HOH A   726              1.99
REMARK 500   OG1  THR A   320     O    HOH A   691              2.15
REMARK 500   OE1  GLN A   500     O    HOH A   741              2.15
REMARK 500   OE1  GLN A   310     O    HOH A   737              2.16
REMARK 500   OG1  THR B   320     O    HOH B   712              2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    CYS A 453     -124.69   -129.69
REMARK 500    SER A 454      -64.46    -94.40
REMARK 500    VAL A 499       91.37     67.62
REMARK 500    ASP B 404      -35.66   -134.32
REMARK 500    CYS B 453     -121.80   -131.06
REMARK 500    SER B 454      -61.31    -96.97
REMARK 500    ILE B 457      -34.08   -132.57
REMARK 500    VAL B 499      103.31     69.21
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE OF CHAIN F IS KE(FTY)(FTY)TV. DUE TO UNCERTAINTY IN
REMARK 999 SEQUENCE REGISTRATION, MUCH OF CHAIN F AS BUILT IS LABELLED UNK
DBREF  4GS0 A  243   528  UNP    P29350   PTN6_HUMAN     243    528
DBREF  4GS0 B  243   528  UNP    P29350   PTN6_HUMAN     243    528
DBREF  4GS0 C    1     4  UNP    P23458   JAK1_HUMAN    1033   1036
SEQADV 4GS0 MET A  221  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 HIS A  222  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 HIS A  223  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 HIS A  224  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 HIS A  225  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 HIS A  226  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 HIS A  227  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 GLY A  228  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 SER A  229  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 LEU A  230  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 VAL A  231  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 PRO A  232  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 ARG A  233  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 SER A  234  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 GLU A  235  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 ASN A  236  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 LEU A  237  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 TYR A  238  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 PHE A  239  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 GLN A  240  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 GLY A  241  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 SER A  242  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 MET B  221  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 HIS B  222  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 HIS B  223  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 HIS B  224  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 HIS B  225  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 HIS B  226  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 HIS B  227  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 GLY B  228  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 SER B  229  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 LEU B  230  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 VAL B  231  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 PRO B  232  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 ARG B  233  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 SER B  234  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 GLU B  235  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 ASN B  236  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 LEU B  237  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 TYR B  238  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 PHE B  239  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 GLN B  240  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 GLY B  241  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 SER B  242  UNP  P29350              EXPRESSION TAG
SEQADV 4GS0 UNK C    1  UNP  P23458    GLU  1033 SEE REMARK 999
SEQADV 4GS0 UNK C    2  UNP  P23458    TYR  1034 SEE REMARK 999
SEQADV 4GS0 UNK C    4  UNP  P23458    THR  1036 SEE REMARK 999
SEQRES   1 A  308  MET HIS HIS HIS HIS HIS HIS GLY SER LEU VAL PRO ARG
SEQRES   2 A  308  SER GLU ASN LEU TYR PHE GLN GLY SER GLY PHE TRP GLU
SEQRES   3 A  308  GLU PHE GLU SER LEU GLN LYS GLN GLU VAL LYS ASN LEU
SEQRES   4 A  308  HIS GLN ARG LEU GLU GLY GLN ARG PRO GLU ASN LYS GLY
SEQRES   5 A  308  LYS ASN ARG TYR LYS ASN ILE LEU PRO PHE ASP HIS SER
SEQRES   6 A  308  ARG VAL ILE LEU GLN GLY ARG ASP SER ASN ILE PRO GLY
SEQRES   7 A  308  SER ASP TYR ILE ASN ALA ASN TYR ILE LYS ASN GLN LEU
SEQRES   8 A  308  LEU GLY PRO ASP GLU ASN ALA LYS THR TYR ILE ALA SER
SEQRES   9 A  308  GLN GLY CYS LEU GLU ALA THR VAL ASN ASP PHE TRP GLN
SEQRES  10 A  308  MET ALA TRP GLN GLU ASN SER ARG VAL ILE VAL MET THR
SEQRES  11 A  308  THR ARG GLU VAL GLU LYS GLY ARG ASN LYS CYS VAL PRO
SEQRES  12 A  308  TYR TRP PRO GLU VAL GLY MET GLN ARG ALA TYR GLY PRO
SEQRES  13 A  308  TYR SER VAL THR ASN CYS GLY GLU HIS ASP THR THR GLU
SEQRES  14 A  308  TYR LYS LEU ARG THR LEU GLN VAL SER PRO LEU ASP ASN
SEQRES  15 A  308  GLY ASP LEU ILE ARG GLU ILE TRP HIS TYR GLN TYR LEU
SEQRES  16 A  308  SER TRP PRO ASP HIS GLY VAL PRO SER GLU PRO GLY GLY
SEQRES  17 A  308  VAL LEU SER PHE LEU ASP GLN ILE ASN GLN ARG GLN GLU
SEQRES  18 A  308  SER LEU PRO HIS ALA GLY PRO ILE ILE VAL HIS CYS SER
SEQRES  19 A  308  ALA GLY ILE GLY ARG THR GLY THR ILE ILE VAL ILE ASP
SEQRES  20 A  308  MET LEU MET GLU ASN ILE SER THR LYS GLY LEU ASP CYS
SEQRES  21 A  308  ASP ILE ASP ILE GLN LYS THR ILE GLN MET VAL ARG ALA
SEQRES  22 A  308  GLN ARG SER GLY MET VAL GLN THR GLU ALA GLN TYR LYS
SEQRES  23 A  308  PHE ILE TYR VAL ALA ILE ALA GLN PHE ILE GLU THR THR
SEQRES  24 A  308  LYS LYS LYS LEU GLU VAL LEU GLN SER
SEQRES   1 B  308  MET HIS HIS HIS HIS HIS HIS GLY SER LEU VAL PRO ARG
SEQRES   2 B  308  SER GLU ASN LEU TYR PHE GLN GLY SER GLY PHE TRP GLU
SEQRES   3 B  308  GLU PHE GLU SER LEU GLN LYS GLN GLU VAL LYS ASN LEU
SEQRES   4 B  308  HIS GLN ARG LEU GLU GLY GLN ARG PRO GLU ASN LYS GLY
SEQRES   5 B  308  LYS ASN ARG TYR LYS ASN ILE LEU PRO PHE ASP HIS SER
SEQRES   6 B  308  ARG VAL ILE LEU GLN GLY ARG ASP SER ASN ILE PRO GLY
SEQRES   7 B  308  SER ASP TYR ILE ASN ALA ASN TYR ILE LYS ASN GLN LEU
SEQRES   8 B  308  LEU GLY PRO ASP GLU ASN ALA LYS THR TYR ILE ALA SER
SEQRES   9 B  308  GLN GLY CYS LEU GLU ALA THR VAL ASN ASP PHE TRP GLN
SEQRES  10 B  308  MET ALA TRP GLN GLU ASN SER ARG VAL ILE VAL MET THR
SEQRES  11 B  308  THR ARG GLU VAL GLU LYS GLY ARG ASN LYS CYS VAL PRO
SEQRES  12 B  308  TYR TRP PRO GLU VAL GLY MET GLN ARG ALA TYR GLY PRO
SEQRES  13 B  308  TYR SER VAL THR ASN CYS GLY GLU HIS ASP THR THR GLU
SEQRES  14 B  308  TYR LYS LEU ARG THR LEU GLN VAL SER PRO LEU ASP ASN
SEQRES  15 B  308  GLY ASP LEU ILE ARG GLU ILE TRP HIS TYR GLN TYR LEU
SEQRES  16 B  308  SER TRP PRO ASP HIS GLY VAL PRO SER GLU PRO GLY GLY
SEQRES  17 B  308  VAL LEU SER PHE LEU ASP GLN ILE ASN GLN ARG GLN GLU
SEQRES  18 B  308  SER LEU PRO HIS ALA GLY PRO ILE ILE VAL HIS CYS SER
SEQRES  19 B  308  ALA GLY ILE GLY ARG THR GLY THR ILE ILE VAL ILE ASP
SEQRES  20 B  308  MET LEU MET GLU ASN ILE SER THR LYS GLY LEU ASP CYS
SEQRES  21 B  308  ASP ILE ASP ILE GLN LYS THR ILE GLN MET VAL ARG ALA
SEQRES  22 B  308  GLN ARG SER GLY MET VAL GLN THR GLU ALA GLN TYR LYS
SEQRES  23 B  308  PHE ILE TYR VAL ALA ILE ALA GLN PHE ILE GLU THR THR
SEQRES  24 B  308  LYS LYS LYS LEU GLU VAL LEU GLN SER
SEQRES   1 C    4  UNK UNK FTY UNK
MODRES 4GS0 FTY C    3  TYR  DEOXY-DIFLUOROMETHELENE-PHOSPHOTYROSINE
HET    FTY  C   3      18
HETNAM     FTY DEOXY-DIFLUOROMETHELENE-PHOSPHOTYROSINE
FORMUL   3  FTY    C10 H12 F2 N O5 P
FORMUL   4  HOH   *287(H2 O)
HELIX    1   1 GLY A  243  ASN A  258  1                                  16
HELIX    2   2 LEU A  259  GLN A  261  5                                   3
HELIX    3   3 LEU A  263  ASN A  274  5                                  12
HELIX    4   4 PHE A  282  ARG A  286  5                                   5
HELIX    5   5 LEU A  328  ALA A  330  5                                   3
HELIX    6   6 THR A  331  ASN A  343  1                                  13
HELIX    7   7 PRO A  426  SER A  442  1                                  17
HELIX    8   8 GLY A  458  GLY A  477  1                                  20
HELIX    9   9 ASP A  483  ALA A  493  1                                  11
HELIX   10  10 THR A  501  LEU A  526  1                                  26
HELIX   11  11 LEU B  263  ASN B  274  5                                  12
HELIX   12  12 PHE B  282  HIS B  284  5                                   3
HELIX   13  13 LEU B  328  ALA B  330  5                                   3
HELIX   14  14 THR B  331  ASN B  343  1                                  13
HELIX   15  15 PRO B  426  SER B  442  1                                  17
HELIX   16  16 GLY B  458  GLY B  477  1                                  20
HELIX   17  17 ASP B  483  ALA B  493  1                                  11
HELIX   18  18 THR B  501  LEU B  523  1                                  23
SHEET    1   A 8 ALA A 304  ILE A 307  0
SHEET    2   A 8 TYR A 321  SER A 324 -1  O  TYR A 321   N  ILE A 307
SHEET    3   A 8 ILE A 449  HIS A 452  1  O  VAL A 451   N  ILE A 322
SHEET    4   A 8 VAL A 346  MET A 349  1  N  VAL A 348   O  ILE A 450
SHEET    5   A 8 ARG A 407  TYR A 414  1  O  TYR A 412   N  ILE A 347
SHEET    6   A 8 TYR A 390  PRO A 399 -1  N  ARG A 393   O  HIS A 411
SHEET    7   A 8 TYR A 377  ASP A 386 -1  N  SER A 378   O  SER A 398
SHEET    8   A 8 GLN A 371  TYR A 374 -1  N  TYR A 374   O  TYR A 377
SHEET    1   B 2 VAL A 354  GLU A 355  0
SHEET    2   B 2 ARG A 358  ASN A 359 -1  O  ARG A 358   N  GLU A 355
SHEET    1   C 9 ARG B 286  ILE B 288  0
SHEET    2   C 9 TYR B 301  ILE B 307 -1  O  ALA B 304   N  VAL B 287
SHEET    3   C 9 TYR B 321  SER B 324 -1  O  ALA B 323   N  ASN B 305
SHEET    4   C 9 ILE B 449  HIS B 452  1  O  VAL B 451   N  ILE B 322
SHEET    5   C 9 VAL B 346  MET B 349  1  N  VAL B 348   O  ILE B 450
SHEET    6   C 9 ARG B 407  TYR B 414  1  O  TYR B 412   N  MET B 349
SHEET    7   C 9 TYR B 390  PRO B 399 -1  N  LYS B 391   O  GLN B 413
SHEET    8   C 9 TYR B 377  ASP B 386 -1  N  SER B 378   O  SER B 398
SHEET    9   C 9 GLN B 371  TYR B 374 -1  N  TYR B 374   O  TYR B 377
SHEET    1   D 2 VAL B 354  GLU B 355  0
SHEET    2   D 2 ARG B 358  ASN B 359 -1  O  ARG B 358   N  GLU B 355
LINK         C   UNK C   2                 N   FTY C   3     1555   1555  1.33
LINK         C   FTY C   3                 N   UNK C   4     1555   1555  1.33
CRYST1   43.935   43.935  258.112  90.00  90.00 120.00 P 31          6
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      0.022761  0.013141  0.000000        0.00000
SCALE2      0.000000  0.026282  0.000000        0.00000
SCALE3      0.000000  0.000000  0.003874        0.00000
      
PROCHECK
Go to PROCHECK summary
 References