HEADER CYTOKINE 15-APR-11 3RJR
TITLE CRYSTAL STRUCTURE OF PRO-TGF BETA 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSFORMING GROWTH FACTOR BETA-1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: TGF-BETA-1, LATENCY-ASSOCIATED PEPTIDE, LAP;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIGS,SWINE,WILD BOAR;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 GENE: TGFB1;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: LEC 3.2.8.1;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1
KEYWDS TGF BETA, ACTIVATION, INTEGRIN, CYTOKINE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.H.ZHU,M.L.SHI,T.A.SPRINGER
REVDAT 4 29-JUL-20 3RJR 1 COMPND REMARK SEQADV HETNAM
REVDAT 4 2 1 LINK SITE ATOM
REVDAT 3 08-NOV-17 3RJR 1 REMARK
REVDAT 2 13-FEB-13 3RJR 1 JRNL VERSN
REVDAT 1 15-JUN-11 3RJR 0
JRNL AUTH M.SHI,J.ZHU,R.WANG,X.CHEN,L.MI,T.WALZ,T.A.SPRINGER
JRNL TITL LATENT TGF-BETA STRUCTURE AND ACTIVATION
JRNL REF NATURE V. 474 343 2011
JRNL REFN ISSN 0028-0836
JRNL PMID 21677751
JRNL DOI 10.1038/NATURE10152
REMARK 2
REMARK 2 RESOLUTION. 3.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_276
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.55
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.440
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 35267
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.275
REMARK 3 R VALUE (WORKING SET) : 0.274
REMARK 3 FREE R VALUE : 0.311
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.950
REMARK 3 FREE R VALUE TEST SET COUNT : 1040
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 46.5595 - 5.8312 0.99 4971 179 0.2459 0.2681
REMARK 3 2 5.8312 - 4.6298 0.99 4907 159 0.2500 0.3186
REMARK 3 3 4.6298 - 4.0449 0.99 4907 139 0.2565 0.2977
REMARK 3 4 4.0449 - 3.6753 0.99 4873 144 0.2912 0.3294
REMARK 3 5 3.6753 - 3.4119 0.99 4859 145 0.3207 0.3512
REMARK 3 6 3.4119 - 3.2108 0.98 4853 124 0.3366 0.3901
REMARK 3 7 3.2108 - 3.0500 0.98 4857 150 0.3668 0.4188
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 1.20
REMARK 3 K_SOL : 0.30
REMARK 3 B_SOL : 242.9
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.510
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 214.8
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -11.61110
REMARK 3 B22 (A**2) : -17.93140
REMARK 3 B33 (A**2) : -22.11040
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -4.76920
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 : 0.002 11236
REMARK 3 ANGLE : 0.488 15215
REMARK 3 CHIRALITY : 0.032 1690
REMARK 3 PLANARITY : 0.002 1939
REMARK 3 DIHEDRAL : 12.461 4211
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 40
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND RESID 1:30
REMARK 3 ORIGIN FOR THE GROUP (A): -84.6996 55.2195 -39.7024
REMARK 3 T TENSOR
REMARK 3 T11: 1.9445 T22: 0.7840
REMARK 3 T33: 1.6305 T12: 0.4269
REMARK 3 T13: -0.6968 T23: -0.3838
REMARK 3 L TENSOR
REMARK 3 L11: 0.2017 L22: 0.3906
REMARK 3 L33: 0.1301 L12: 0.2136
REMARK 3 L13: 0.1929 L23: 0.2850
REMARK 3 S TENSOR
REMARK 3 S11: -0.2655 S12: -0.7811 S13: -0.0349
REMARK 3 S21: 0.5686 S22: -0.1133 S23: -0.4492
REMARK 3 S31: -1.0960 S32: 0.0066 S33: -0.0002
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND RESID 31:61
REMARK 3 ORIGIN FOR THE GROUP (A): -87.8041 62.7726 -16.2105
REMARK 3 T TENSOR
REMARK 3 T11: 3.3288 T22: 1.7124
REMARK 3 T33: 0.9648 T12: 0.4194
REMARK 3 T13: -0.0795 T23: 0.2300
REMARK 3 L TENSOR
REMARK 3 L11: 0.0790 L22: 0.2226
REMARK 3 L33: 0.0237 L12: 0.3479
REMARK 3 L13: 0.2602 L23: -0.0323
REMARK 3 S TENSOR
REMARK 3 S11: 0.4059 S12: -1.2910 S13: 0.1329
REMARK 3 S21: 0.1988 S22: 0.2271 S23: 0.5414
REMARK 3 S31: -1.9573 S32: -0.2670 S33: 0.0003
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND RESID 62:116
REMARK 3 ORIGIN FOR THE GROUP (A): -85.7603 50.2919 1.1620
REMARK 3 T TENSOR
REMARK 3 T11: 1.3145 T22: 1.7773
REMARK 3 T33: 1.8771 T12: 0.3273
REMARK 3 T13: -0.2889 T23: -0.3080
REMARK 3 L TENSOR
REMARK 3 L11: -0.0122 L22: 0.8710
REMARK 3 L33: -0.1437 L12: 0.2869
REMARK 3 L13: 0.6086 L23: 0.2027
REMARK 3 S TENSOR
REMARK 3 S11: 0.4943 S12: -0.3724 S13: 0.2889
REMARK 3 S21: -0.2277 S22: -0.0288 S23: 0.7157
REMARK 3 S31: -0.0351 S32: -0.2523 S33: -0.0001
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND RESID 117:202
REMARK 3 ORIGIN FOR THE GROUP (A): -76.3851 43.8873 1.3589
REMARK 3 T TENSOR
REMARK 3 T11: 1.9685 T22: 1.7428
REMARK 3 T33: 0.8955 T12: -0.0288
REMARK 3 T13: 0.0205 T23: -0.0165
REMARK 3 L TENSOR
REMARK 3 L11: 0.1077 L22: 1.5521
REMARK 3 L33: 0.0606 L12: -0.3149
REMARK 3 L13: -0.0360 L23: 0.6051
REMARK 3 S TENSOR
REMARK 3 S11: -0.7440 S12: -0.2309 S13: 1.2277
REMARK 3 S21: -0.6345 S22: 0.1635 S23: -0.2493
REMARK 3 S31: 0.5087 S32: 0.2131 S33: -0.0001
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND RESID 203:227
REMARK 3 ORIGIN FOR THE GROUP (A): -70.1387 52.1929 6.9298
REMARK 3 T TENSOR
REMARK 3 T11: 2.5101 T22: 1.7650
REMARK 3 T33: 1.2361 T12: -0.3871
REMARK 3 T13: 0.0411 T23: -0.4831
REMARK 3 L TENSOR
REMARK 3 L11: 0.0835 L22: 0.2811
REMARK 3 L33: 0.2881 L12: 0.0751
REMARK 3 L13: -0.0138 L23: -0.1127
REMARK 3 S TENSOR
REMARK 3 S11: -1.2205 S12: 0.0306 S13: 0.0800
REMARK 3 S21: -0.7787 S22: -0.1389 S23: 0.3328
REMARK 3 S31: -0.2378 S32: 1.5903 S33: -0.0111
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN A AND RESID 228:263
REMARK 3 ORIGIN FOR THE GROUP (A): -80.2795 49.4094 -24.5551
REMARK 3 T TENSOR
REMARK 3 T11: 2.7190 T22: 1.1309
REMARK 3 T33: 1.5895 T12: 0.1987
REMARK 3 T13: -0.4321 T23: 0.1230
REMARK 3 L TENSOR
REMARK 3 L11: 0.0442 L22: 0.3989
REMARK 3 L33: -0.0526 L12: -0.3586
REMARK 3 L13: -0.0923 L23: -0.1950
REMARK 3 S TENSOR
REMARK 3 S11: 0.3612 S12: -0.3341 S13: 1.0817
REMARK 3 S21: 0.6895 S22: -0.4285 S23: 0.4315
REMARK 3 S31: -0.0623 S32: 0.8831 S33: -0.0000
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN A AND RESID 264:299
REMARK 3 ORIGIN FOR THE GROUP (A): -80.9383 57.0859 -33.3787
REMARK 3 T TENSOR
REMARK 3 T11: 2.8056 T22: 1.5360
REMARK 3 T33: 1.1763 T12: 0.4189
REMARK 3 T13: -0.2611 T23: 0.1678
REMARK 3 L TENSOR
REMARK 3 L11: 0.2803 L22: 0.5407
REMARK 3 L33: 0.6123 L12: 0.2245
REMARK 3 L13: 0.3048 L23: -0.6417
REMARK 3 S TENSOR
REMARK 3 S11: -0.1371 S12: -1.3340 S13: 0.0784
REMARK 3 S21: -0.6564 S22: 0.1235 S23: -0.7324
REMARK 3 S31: -0.9302 S32: 0.0254 S33: 0.0002
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN A AND RESID 300:313
REMARK 3 ORIGIN FOR THE GROUP (A): -62.1950 32.7115 -44.6607
REMARK 3 T TENSOR
REMARK 3 T11: 3.9869 T22: 1.8039
REMARK 3 T33: 1.9711 T12: 1.2569
REMARK 3 T13: -0.2783 T23: 0.3369
REMARK 3 L TENSOR
REMARK 3 L11: 0.0037 L22: 0.0016
REMARK 3 L33: 0.0031 L12: -0.0015
REMARK 3 L13: -0.0049 L23: -0.0023
REMARK 3 S TENSOR
REMARK 3 S11: -0.2822 S12: -0.1285 S13: -0.1447
REMARK 3 S21: -0.0210 S22: -0.1336 S23: -0.0203
REMARK 3 S31: -0.0532 S32: 0.0109 S33: -0.0001
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN A AND RESID 314:324
REMARK 3 ORIGIN FOR THE GROUP (A): -70.0183 33.6250 -39.9448
REMARK 3 T TENSOR
REMARK 3 T11: 2.1059 T22: 0.9243
REMARK 3 T33: 3.9801 T12: -0.1338
REMARK 3 T13: 0.5993 T23: 0.4107
REMARK 3 L TENSOR
REMARK 3 L11: -0.0070 L22: -0.0014
REMARK 3 L33: -0.0149 L12: 0.0127
REMARK 3 L13: -0.0136 L23: 0.0243
REMARK 3 S TENSOR
REMARK 3 S11: -0.3458 S12: -0.0400 S13: -0.0060
REMARK 3 S21: -0.2327 S22: -0.5981 S23: -0.7786
REMARK 3 S31: -0.3738 S32: 1.2158 S33: -0.0004
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN A AND RESID 325:361
REMARK 3 ORIGIN FOR THE GROUP (A): -83.8884 51.5010 -25.1319
REMARK 3 T TENSOR
REMARK 3 T11: 2.5278 T22: 0.7765
REMARK 3 T33: 0.5442 T12: 0.3234
REMARK 3 T13: -0.9686 T23: -0.2905
REMARK 3 L TENSOR
REMARK 3 L11: 1.7830 L22: 1.3698
REMARK 3 L33: 1.4357 L12: 1.3041
REMARK 3 L13: -0.7624 L23: -0.9653
REMARK 3 S TENSOR
REMARK 3 S11: -2.3457 S12: 0.3276 S13: 0.1892
REMARK 3 S21: -0.0793 S22: -0.8912 S23: -0.7051
REMARK 3 S31: -2.3661 S32: 0.7507 S33: -0.6705
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN B AND RESID 1:30
REMARK 3 ORIGIN FOR THE GROUP (A): -76.5441 22.4656 -43.3148
REMARK 3 T TENSOR
REMARK 3 T11: 1.4235 T22: 1.3523
REMARK 3 T33: 0.5432 T12: 0.3749
REMARK 3 T13: 0.1015 T23: 0.1448
REMARK 3 L TENSOR
REMARK 3 L11: 0.3836 L22: 1.8099
REMARK 3 L33: -0.5247 L12: -0.6959
REMARK 3 L13: 0.5516 L23: -0.9292
REMARK 3 S TENSOR
REMARK 3 S11: 1.2324 S12: 0.4092 S13: 2.2388
REMARK 3 S21: 0.1263 S22: -0.0049 S23: -0.0282
REMARK 3 S31: -0.6485 S32: -0.4496 S33: 0.0540
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN B AND RESID 31:61
REMARK 3 ORIGIN FOR THE GROUP (A): -61.2300 12.9337 -26.4307
REMARK 3 T TENSOR
REMARK 3 T11: 1.6999 T22: 1.5372
REMARK 3 T33: 0.8526 T12: -0.4745
REMARK 3 T13: 0.0711 T23: -0.2996
REMARK 3 L TENSOR
REMARK 3 L11: 0.7378 L22: 0.2152
REMARK 3 L33: 0.2145 L12: 0.7146
REMARK 3 L13: 0.0921 L23: -0.0729
REMARK 3 S TENSOR
REMARK 3 S11: 0.7355 S12: -0.2302 S13: 1.2386
REMARK 3 S21: 1.0330 S22: 0.7795 S23: -1.4293
REMARK 3 S31: 1.8087 S32: 0.6854 S33: 0.0006
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN B AND RESID 62:116
REMARK 3 ORIGIN FOR THE GROUP (A): -53.3864 23.5162 -9.7300
REMARK 3 T TENSOR
REMARK 3 T11: 1.1049 T22: 1.6017
REMARK 3 T33: 0.8237 T12: -0.1420
REMARK 3 T13: 0.0953 T23: -0.4312
REMARK 3 L TENSOR
REMARK 3 L11: 0.0461 L22: 0.5656
REMARK 3 L33: 0.1512 L12: 0.7583
REMARK 3 L13: -0.1996 L23: -0.3774
REMARK 3 S TENSOR
REMARK 3 S11: -0.0319 S12: 0.3529 S13: 0.0329
REMARK 3 S21: -0.8261 S22: 0.0339 S23: -1.0775
REMARK 3 S31: -1.3036 S32: 1.0347 S33: -0.0027
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN B AND RESID 117:200
REMARK 3 ORIGIN FOR THE GROUP (A): -61.0645 29.1959 -4.2023
REMARK 3 T TENSOR
REMARK 3 T11: 1.3227 T22: 1.4963
REMARK 3 T33: 0.9061 T12: -0.1977
REMARK 3 T13: -0.3220 T23: -0.2773
REMARK 3 L TENSOR
REMARK 3 L11: 0.6198 L22: 0.4100
REMARK 3 L33: 0.4917 L12: -0.8616
REMARK 3 L13: 0.6767 L23: 0.8733
REMARK 3 S TENSOR
REMARK 3 S11: -1.4615 S12: -0.4917 S13: 0.4526
REMARK 3 S21: 0.6235 S22: 0.6340 S23: 0.8702
REMARK 3 S31: 0.2669 S32: -0.3103 S33: -0.0033
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN B AND RESID 201:263
REMARK 3 ORIGIN FOR THE GROUP (A): -68.4017 25.2558 -14.7882
REMARK 3 T TENSOR
REMARK 3 T11: 0.8955 T22: 1.0172
REMARK 3 T33: 1.2443 T12: -0.5087
REMARK 3 T13: -0.0050 T23: 0.1363
REMARK 3 L TENSOR
REMARK 3 L11: 1.1930 L22: 0.0679
REMARK 3 L33: 0.7712 L12: -0.8383
REMARK 3 L13: 0.2453 L23: 1.4839
REMARK 3 S TENSOR
REMARK 3 S11: 0.1317 S12: 0.0259 S13: 0.1566
REMARK 3 S21: 0.2907 S22: 0.3824 S23: 0.8180
REMARK 3 S31: -0.1862 S32: -0.3311 S33: -0.0011
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN B AND RESID 264:274
REMARK 3 ORIGIN FOR THE GROUP (A): -79.0914 19.0512 -35.9327
REMARK 3 T TENSOR
REMARK 3 T11: 1.6558 T22: 1.1146
REMARK 3 T33: 0.9573 T12: -0.2251
REMARK 3 T13: -0.1855 T23: -0.1732
REMARK 3 L TENSOR
REMARK 3 L11: -0.1119 L22: 0.0545
REMARK 3 L33: -0.2030 L12: -0.0801
REMARK 3 L13: -0.0040 L23: 0.1826
REMARK 3 S TENSOR
REMARK 3 S11: 0.3416 S12: 0.4873 S13: -0.9237
REMARK 3 S21: 1.0435 S22: 0.2437 S23: -0.1156
REMARK 3 S31: 0.3934 S32: -0.5504 S33: 0.0003
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN B AND RESID 275:296
REMARK 3 ORIGIN FOR THE GROUP (A): -72.6041 17.1603 -36.3774
REMARK 3 T TENSOR
REMARK 3 T11: 1.6443 T22: 1.0635
REMARK 3 T33: 1.0219 T12: -0.0440
REMARK 3 T13: -0.3022 T23: -0.5569
REMARK 3 L TENSOR
REMARK 3 L11: 0.2436 L22: 0.4280
REMARK 3 L33: 0.1196 L12: 0.5682
REMARK 3 L13: 0.2591 L23: 0.0967
REMARK 3 S TENSOR
REMARK 3 S11: 0.5292 S12: 0.4165 S13: 0.0382
REMARK 3 S21: -1.1117 S22: 0.2298 S23: -0.3643
REMARK 3 S31: 0.4367 S32: 0.2556 S33: 0.0000
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN B AND RESID 297:311
REMARK 3 ORIGIN FOR THE GROUP (A): -95.6622 39.9690 -31.9919
REMARK 3 T TENSOR
REMARK 3 T11: 1.8264 T22: 2.5049
REMARK 3 T33: 2.1282 T12: -0.2497
REMARK 3 T13: -0.1999 T23: -0.0902
REMARK 3 L TENSOR
REMARK 3 L11: -0.0308 L22: -0.0035
REMARK 3 L33: 0.0238 L12: 0.0947
REMARK 3 L13: -0.0263 L23: -0.0627
REMARK 3 S TENSOR
REMARK 3 S11: -0.0323 S12: -0.2670 S13: -1.2834
REMARK 3 S21: -0.2140 S22: -0.7272 S23: 0.4804
REMARK 3 S31: 0.1794 S32: -0.5089 S33: -0.0004
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN B AND RESID 312:324
REMARK 3 ORIGIN FOR THE GROUP (A): -85.4423 42.9772 -32.7974
REMARK 3 T TENSOR
REMARK 3 T11: 2.1362 T22: 1.3175
REMARK 3 T33: 1.6361 T12: -0.6798
REMARK 3 T13: -0.1274 T23: 0.2879
REMARK 3 L TENSOR
REMARK 3 L11: -0.0127 L22: -0.0128
REMARK 3 L33: 0.0358 L12: 0.0471
REMARK 3 L13: -0.0693 L23: 0.0453
REMARK 3 S TENSOR
REMARK 3 S11: -0.0806 S12: -0.7964 S13: -0.6642
REMARK 3 S21: 0.0979 S22: -0.2519 S23: 0.3397
REMARK 3 S31: 0.7071 S32: -0.5010 S33: -0.0000
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN B AND RESID 325:361
REMARK 3 ORIGIN FOR THE GROUP (A): -69.2170 24.8029 -30.5868
REMARK 3 T TENSOR
REMARK 3 T11: 1.0504 T22: 1.2699
REMARK 3 T33: 0.6984 T12: -0.0402
REMARK 3 T13: 0.0058 T23: -0.0299
REMARK 3 L TENSOR
REMARK 3 L11: 0.0482 L22: 0.8498
REMARK 3 L33: 0.6967 L12: 0.6153
REMARK 3 L13: 0.4763 L23: 0.2041
REMARK 3 S TENSOR
REMARK 3 S11: 0.5990 S12: -0.5086 S13: 0.7163
REMARK 3 S21: -0.3895 S22: -0.1331 S23: -0.4585
REMARK 3 S31: 0.8253 S32: -0.3071 S33: 0.0000
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN C AND RESID -1:49
REMARK 3 ORIGIN FOR THE GROUP (A): -40.1509 55.6674 71.9351
REMARK 3 T TENSOR
REMARK 3 T11: 1.2441 T22: 0.3947
REMARK 3 T33: 1.3973 T12: 0.1487
REMARK 3 T13: -0.3283 T23: -0.0483
REMARK 3 L TENSOR
REMARK 3 L11: 0.4014 L22: 1.2790
REMARK 3 L33: 0.4588 L12: 0.2768
REMARK 3 L13: -0.0383 L23: 1.6527
REMARK 3 S TENSOR
REMARK 3 S11: -0.2633 S12: 0.0735 S13: 0.6190
REMARK 3 S21: 1.3079 S22: -0.0266 S23: -0.4164
REMARK 3 S31: -2.0951 S32: 0.2279 S33: 0.0013
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN C AND RESID 50:100
REMARK 3 ORIGIN FOR THE GROUP (A): -44.2007 49.9031 41.3836
REMARK 3 T TENSOR
REMARK 3 T11: 1.0351 T22: 0.8068
REMARK 3 T33: 1.3587 T12: 0.0528
REMARK 3 T13: -0.0100 T23: 0.1850
REMARK 3 L TENSOR
REMARK 3 L11: 0.1381 L22: 0.4173
REMARK 3 L33: 0.4957 L12: -0.0684
REMARK 3 L13: -0.0687 L23: -0.2258
REMARK 3 S TENSOR
REMARK 3 S11: 0.4155 S12: -0.1869 S13: 0.5966
REMARK 3 S21: -0.5956 S22: 0.0520 S23: -1.3742
REMARK 3 S31: 1.0482 S32: -0.4398 S33: 0.0003
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN C AND RESID 101:142
REMARK 3 ORIGIN FOR THE GROUP (A): -46.1360 47.4090 38.4754
REMARK 3 T TENSOR
REMARK 3 T11: 1.1449 T22: 0.9829
REMARK 3 T33: 1.0975 T12: 0.0312
REMARK 3 T13: -0.0647 T23: 0.0117
REMARK 3 L TENSOR
REMARK 3 L11: 0.2015 L22: 1.6659
REMARK 3 L33: -0.0059 L12: 0.2876
REMARK 3 L13: 0.0128 L23: -0.2463
REMARK 3 S TENSOR
REMARK 3 S11: -0.3732 S12: 0.9671 S13: -0.2128
REMARK 3 S21: -0.3426 S22: 0.0907 S23: -0.6504
REMARK 3 S31: -0.5238 S32: 0.3274 S33: 0.0001
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN C AND RESID 143:200
REMARK 3 ORIGIN FOR THE GROUP (A): -49.1762 41.2225 34.5191
REMARK 3 T TENSOR
REMARK 3 T11: 1.5427 T22: 0.8805
REMARK 3 T33: 0.7728 T12: 0.1953
REMARK 3 T13: 0.3500 T23: 0.3341
REMARK 3 L TENSOR
REMARK 3 L11: 0.4835 L22: 1.2575
REMARK 3 L33: 2.3138 L12: 0.4700
REMARK 3 L13: 0.5335 L23: 0.9408
REMARK 3 S TENSOR
REMARK 3 S11: -0.2963 S12: 1.1114 S13: 0.4617
REMARK 3 S21: -0.7254 S22: -0.4956 S23: -0.1361
REMARK 3 S31: 0.5839 S32: -0.2260 S33: -0.3563
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN C AND RESID 201:240
REMARK 3 ORIGIN FOR THE GROUP (A): -48.0634 48.2205 37.7475
REMARK 3 T TENSOR
REMARK 3 T11: 1.0453 T22: 0.5924
REMARK 3 T33: 1.3315 T12: 0.3229
REMARK 3 T13: 0.4256 T23: 0.0394
REMARK 3 L TENSOR
REMARK 3 L11: 2.3027 L22: 0.2330
REMARK 3 L33: 2.3945 L12: 0.7900
REMARK 3 L13: 0.8855 L23: -1.2162
REMARK 3 S TENSOR
REMARK 3 S11: -1.8827 S12: -1.3934 S13: 1.5417
REMARK 3 S21: 0.3621 S22: 0.1302 S23: -1.3543
REMARK 3 S31: -0.9201 S32: -1.3335 S33: -0.0903
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN C AND RESID 251:263
REMARK 3 ORIGIN FOR THE GROUP (A): -61.8745 45.2496 74.1571
REMARK 3 T TENSOR
REMARK 3 T11: 0.7905 T22: 2.0089
REMARK 3 T33: 2.7489 T12: 0.5222
REMARK 3 T13: -0.1105 T23: 0.1091
REMARK 3 L TENSOR
REMARK 3 L11: 0.0045 L22: -0.0526
REMARK 3 L33: -0.0064 L12: 0.0174
REMARK 3 L13: -0.0134 L23: -0.0801
REMARK 3 S TENSOR
REMARK 3 S11: -0.2461 S12: -0.5337 S13: -0.3950
REMARK 3 S21: -0.0421 S22: -0.9146 S23: 0.1873
REMARK 3 S31: -0.7988 S32: -0.4384 S33: -0.0000
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN C AND RESID 264:274
REMARK 3 ORIGIN FOR THE GROUP (A): -49.6866 53.8699 72.5897
REMARK 3 T TENSOR
REMARK 3 T11: 1.5576 T22: 0.7447
REMARK 3 T33: 2.1068 T12: 0.4538
REMARK 3 T13: -0.8251 T23: -0.5898
REMARK 3 L TENSOR
REMARK 3 L11: 0.0922 L22: 0.0344
REMARK 3 L33: 0.2170 L12: -0.0278
REMARK 3 L13: 0.1290 L23: 0.0851
REMARK 3 S TENSOR
REMARK 3 S11: 0.0593 S12: -0.2398 S13: 0.0387
REMARK 3 S21: 0.3959 S22: 0.0536 S23: 0.4015
REMARK 3 S31: -0.7751 S32: 0.3497 S33: 0.0002
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN C AND RESID 275:298
REMARK 3 ORIGIN FOR THE GROUP (A): -44.8467 54.4327 70.4582
REMARK 3 T TENSOR
REMARK 3 T11: 0.8484 T22: -0.6881
REMARK 3 T33: 0.0687 T12: 0.1882
REMARK 3 T13: -0.1423 T23: -1.5098
REMARK 3 L TENSOR
REMARK 3 L11: 0.8847 L22: 0.8499
REMARK 3 L33: 2.0665 L12: -0.7108
REMARK 3 L13: -0.1831 L23: 0.4587
REMARK 3 S TENSOR
REMARK 3 S11: -2.0485 S12: -1.6560 S13: 2.8680
REMARK 3 S21: 2.2538 S22: 0.2404 S23: -1.0347
REMARK 3 S31: -1.7440 S32: 1.7293 S33: -1.6938
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN C AND RESID 299:314
REMARK 3 ORIGIN FOR THE GROUP (A): -62.4633 27.4699 85.4460
REMARK 3 T TENSOR
REMARK 3 T11: 1.4146 T22: 1.1865
REMARK 3 T33: 1.3869 T12: 0.5917
REMARK 3 T13: 0.6159 T23: 0.1167
REMARK 3 L TENSOR
REMARK 3 L11: -0.0205 L22: 0.0262
REMARK 3 L33: 0.0307 L12: -0.1072
REMARK 3 L13: 0.1371 L23: 0.0302
REMARK 3 S TENSOR
REMARK 3 S11: 1.7763 S12: 0.5078 S13: 1.5371
REMARK 3 S21: 0.6173 S22: -0.4929 S23: -0.7664
REMARK 3 S31: -0.6081 S32: -0.9318 S33: 0.0003
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN C AND RESID 315:361
REMARK 3 ORIGIN FOR THE GROUP (A): -45.9728 44.7803 65.5754
REMARK 3 T TENSOR
REMARK 3 T11: -4.8923 T22: -1.8958
REMARK 3 T33: -0.4432 T12: 3.5532
REMARK 3 T13: 1.7252 T23: -0.9553
REMARK 3 L TENSOR
REMARK 3 L11: 2.7438 L22: 5.0819
REMARK 3 L33: 5.5120 L12: 1.3742
REMARK 3 L13: -0.5641 L23: -4.4880
REMARK 3 S TENSOR
REMARK 3 S11: -6.3318 S12: 0.6154 S13: 2.4809
REMARK 3 S21: -0.1435 S22: -1.4502 S23: 0.1731
REMARK 3 S31: -4.5827 S32: 0.3692 S33: -7.1854
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN D AND RESID 1:36
REMARK 3 ORIGIN FOR THE GROUP (A): -53.6161 17.8719 78.3028
REMARK 3 T TENSOR
REMARK 3 T11: 0.5056 T22: 1.0325
REMARK 3 T33: 0.5721 T12: -0.0253
REMARK 3 T13: 0.1215 T23: 0.4750
REMARK 3 L TENSOR
REMARK 3 L11: 0.5338 L22: 1.4656
REMARK 3 L33: 0.7611 L12: 0.2225
REMARK 3 L13: 0.0887 L23: 0.3484
REMARK 3 S TENSOR
REMARK 3 S11: 1.0397 S12: -1.8659 S13: -0.1640
REMARK 3 S21: 1.3201 S22: -1.4039 S23: -0.6741
REMARK 3 S31: 0.4963 S32: 0.5556 S33: -0.2206
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: CHAIN D AND RESID 37:59
REMARK 3 ORIGIN FOR THE GROUP (A): -65.6700 9.1782 58.4109
REMARK 3 T TENSOR
REMARK 3 T11: 1.6774 T22: 0.9649
REMARK 3 T33: 0.6371 T12: 0.0450
REMARK 3 T13: -0.3305 T23: 0.1885
REMARK 3 L TENSOR
REMARK 3 L11: 0.0026 L22: 0.0573
REMARK 3 L33: 0.1389 L12: -0.0227
REMARK 3 L13: 0.0742 L23: -0.2315
REMARK 3 S TENSOR
REMARK 3 S11: 0.4650 S12: 1.0687 S13: -0.2223
REMARK 3 S21: -0.7993 S22: -0.8065 S23: 1.5629
REMARK 3 S31: 1.4696 S32: -0.3748 S33: -0.0042
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: CHAIN D AND RESID 60:73
REMARK 3 ORIGIN FOR THE GROUP (A): -61.0878 31.3895 59.0000
REMARK 3 T TENSOR
REMARK 3 T11: 2.3481 T22: 2.0234
REMARK 3 T33: 0.6937 T12: 1.0822
REMARK 3 T13: 0.0838 T23: -0.6593
REMARK 3 L TENSOR
REMARK 3 L11: 0.0761 L22: 0.0060
REMARK 3 L33: -0.0231 L12: 0.0413
REMARK 3 L13: -0.0025 L23: 0.0280
REMARK 3 S TENSOR
REMARK 3 S11: -0.2943 S12: 0.3625 S13: -0.2317
REMARK 3 S21: 1.2996 S22: 0.3642 S23: -0.3131
REMARK 3 S31: -0.6725 S32: 0.1999 S33: 0.0003
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: CHAIN D AND RESID 74:137
REMARK 3 ORIGIN FOR THE GROUP (A): -70.8127 21.2767 43.7745
REMARK 3 T TENSOR
REMARK 3 T11: 0.8030 T22: 0.9090
REMARK 3 T33: 0.7312 T12: 0.1661
REMARK 3 T13: -0.1881 T23: -0.1455
REMARK 3 L TENSOR
REMARK 3 L11: 1.0775 L22: 1.6288
REMARK 3 L33: 0.4089 L12: 0.5810
REMARK 3 L13: -1.1930 L23: 0.0789
REMARK 3 S TENSOR
REMARK 3 S11: -0.0426 S12: 0.0089 S13: -0.5402
REMARK 3 S21: -0.3924 S22: 0.1595 S23: 0.8478
REMARK 3 S31: 0.2265 S32: -0.2363 S33: 0.0000
REMARK 3 TLS GROUP : 35
REMARK 3 SELECTION: CHAIN D AND RESID 138:200
REMARK 3 ORIGIN FOR THE GROUP (A): -66.6467 29.5934 38.5411
REMARK 3 T TENSOR
REMARK 3 T11: 1.2179 T22: 0.8063
REMARK 3 T33: 0.9426 T12: 0.0744
REMARK 3 T13: -0.4162 T23: -0.0868
REMARK 3 L TENSOR
REMARK 3 L11: 0.5485 L22: 0.5212
REMARK 3 L33: -0.1820 L12: -0.3684
REMARK 3 L13: -0.3477 L23: -1.2151
REMARK 3 S TENSOR
REMARK 3 S11: -0.6008 S12: 0.4774 S13: 0.2981
REMARK 3 S21: -0.5234 S22: 0.1530 S23: -0.3306
REMARK 3 S31: -0.1465 S32: 0.0956 S33: -0.0002
REMARK 3 TLS GROUP : 36
REMARK 3 SELECTION: CHAIN D AND RESID 201:223
REMARK 3 ORIGIN FOR THE GROUP (A): -60.9472 25.1284 26.2959
REMARK 3 T TENSOR
REMARK 3 T11: 0.9545 T22: 0.7752
REMARK 3 T33: 1.3495 T12: 0.5192
REMARK 3 T13: -0.1899 T23: -0.5095
REMARK 3 L TENSOR
REMARK 3 L11: 0.3264 L22: 0.1832
REMARK 3 L33: 1.1398 L12: -0.4758
REMARK 3 L13: 0.3105 L23: 0.0260
REMARK 3 S TENSOR
REMARK 3 S11: -0.4273 S12: 2.6128 S13: -0.3880
REMARK 3 S21: 0.0774 S22: 1.1162 S23: -0.1447
REMARK 3 S31: -0.6079 S32: 1.9009 S33: 0.0027
REMARK 3 TLS GROUP : 37
REMARK 3 SELECTION: CHAIN D AND RESID 224:255
REMARK 3 ORIGIN FOR THE GROUP (A): -64.5293 22.1308 58.7252
REMARK 3 T TENSOR
REMARK 3 T11: 0.3608 T22: 0.5244
REMARK 3 T33: 0.3042 T12: 0.3009
REMARK 3 T13: -0.1162 T23: 0.1631
REMARK 3 L TENSOR
REMARK 3 L11: 1.0551 L22: 1.1777
REMARK 3 L33: 1.1617 L12: -0.7435
REMARK 3 L13: 0.6287 L23: -0.5132
REMARK 3 S TENSOR
REMARK 3 S11: 0.2392 S12: -2.5746 S13: 0.2169
REMARK 3 S21: -0.2190 S22: 0.2935 S23: -0.4533
REMARK 3 S31: 0.5230 S32: 0.1464 S33: 0.0695
REMARK 3 TLS GROUP : 38
REMARK 3 SELECTION: CHAIN D AND RESID 256:275
REMARK 3 ORIGIN FOR THE GROUP (A): -43.4262 17.6306 70.6728
REMARK 3 T TENSOR
REMARK 3 T11: 0.2096 T22: 0.2997
REMARK 3 T33: 1.0551 T12: 0.4774
REMARK 3 T13: 0.1058 T23: 0.2303
REMARK 3 L TENSOR
REMARK 3 L11: -0.0204 L22: 0.2694
REMARK 3 L33: 0.2931 L12: -0.0385
REMARK 3 L13: 0.2398 L23: 0.0219
REMARK 3 S TENSOR
REMARK 3 S11: -0.2439 S12: -0.8349 S13: -2.6919
REMARK 3 S21: 0.1650 S22: -0.1681 S23: -2.4304
REMARK 3 S31: -1.0949 S32: 2.0252 S33: 0.0412
REMARK 3 TLS GROUP : 39
REMARK 3 SELECTION: CHAIN D AND RESID 276:324
REMARK 3 ORIGIN FOR THE GROUP (A): -44.1364 27.3606 70.1682
REMARK 3 T TENSOR
REMARK 3 T11: 0.2920 T22: 0.6306
REMARK 3 T33: 0.9859 T12: 0.3727
REMARK 3 T13: -0.1258 T23: 0.1338
REMARK 3 L TENSOR
REMARK 3 L11: 1.1854 L22: 1.5431
REMARK 3 L33: 1.2295 L12: -0.9663
REMARK 3 L13: 0.2243 L23: 0.6003
REMARK 3 S TENSOR
REMARK 3 S11: -0.6094 S12: -0.1770 S13: 0.1667
REMARK 3 S21: -0.1646 S22: 0.5301 S23: -0.7809
REMARK 3 S31: 0.2850 S32: 0.4977 S33: -0.3859
REMARK 3 TLS GROUP : 40
REMARK 3 SELECTION: CHAIN D AND RESID 325:361
REMARK 3 ORIGIN FOR THE GROUP (A): -57.9149 21.6597 66.2035
REMARK 3 T TENSOR
REMARK 3 T11: 0.3035 T22: 0.4543
REMARK 3 T33: 0.5608 T12: 0.0289
REMARK 3 T13: 0.0458 T23: -0.0758
REMARK 3 L TENSOR
REMARK 3 L11: 0.9412 L22: 1.3020
REMARK 3 L33: 1.1865 L12: -1.3594
REMARK 3 L13: -0.7381 L23: 0.9284
REMARK 3 S TENSOR
REMARK 3 S11: -0.5377 S12: -0.1991 S13: -0.0718
REMARK 3 S21: 0.0027 S22: -0.0078 S23: -0.3049
REMARK 3 S31: 0.3959 S32: -0.3684 S33: -1.1269
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 2
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESID 26:60 OR RESID 75:190
REMARK 3 OR RESID 216:239 OR RESID 264:295 OR
REMARK 3 RESID 328:360)
REMARK 3 SELECTION : CHAIN B AND (RESID 26:60 OR RESID 75:190
REMARK 3 OR RESID 216:239 OR RESID 264:295 OR
REMARK 3 RESID 328:360)
REMARK 3 ATOM PAIRS NUMBER : 1945
REMARK 3 RMSD : 0.002
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESID 26:60 OR RESID 75:190
REMARK 3 OR RESID 216:239 OR RESID 264:295 OR
REMARK 3 RESID 328:360)
REMARK 3 SELECTION : CHAIN C AND (RESID 26:60 OR RESID 75:190
REMARK 3 OR RESID 216:239 OR RESID 264:295 OR
REMARK 3 RESID 328:360)
REMARK 3 ATOM PAIRS NUMBER : 1945
REMARK 3 RMSD : 0.004
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESID 26:60 OR RESID 75:190
REMARK 3 OR RESID 216:239 OR RESID 264:295 OR
REMARK 3 RESID 328:360)
REMARK 3 SELECTION : CHAIN D AND (RESID 26:60 OR RESID 75:190
REMARK 3 OR RESID 216:239 OR RESID 264:295 OR
REMARK 3 RESID 328:360)
REMARK 3 ATOM PAIRS NUMBER : 1945
REMARK 3 RMSD : 0.004
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND RESID 193:208
REMARK 3 SELECTION : CHAIN B AND RESID 193:208
REMARK 3 ATOM PAIRS NUMBER : 124
REMARK 3 RMSD : 0.009
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN A AND RESID 193:208
REMARK 3 SELECTION : CHAIN C AND RESID 193:208
REMARK 3 ATOM PAIRS NUMBER : 124
REMARK 3 RMSD : 0.004
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN A AND RESID 193:208
REMARK 3 SELECTION : CHAIN D AND RESID 193:208
REMARK 3 ATOM PAIRS NUMBER : 124
REMARK 3 RMSD : 0.004
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3RJR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-APR-11.
REMARK 100 THE DEPOSITION ID IS D_1000065017.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-NOV-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934, 0.97932, 0.97956,
REMARK 200 0.95667
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35401
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.050
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.04700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> 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 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 7% PEG 3350, 17% ISOPROPANOL, 0.1M NA
REMARK 280 CITRATE PH 5.6, VAPOR DIFFUSION, TEMPERATURE 293K, VAPOR
REMARK 280 DIFFUSION
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 63.47000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 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 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: 10270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 GLY A -1
REMARK 465 SER A 63
REMARK 465 VAL A 64
REMARK 465 GLU A 65
REMARK 465 PRO A 66
REMARK 465 GLU A 67
REMARK 465 PRO A 68
REMARK 465 GLU A 69
REMARK 465 GLY A 209
REMARK 465 PHE A 210
REMARK 465 ASN A 211
REMARK 465 SER A 212
REMARK 465 GLY A 213
REMARK 465 ARG A 214
REMARK 465 ARG A 215
REMARK 465 LEU A 242
REMARK 465 HIS A 243
REMARK 465 SER A 244
REMARK 465 SER A 245
REMARK 465 ARG A 246
REMARK 465 HIS A 247
REMARK 465 ARG A 248
REMARK 465 ARG A 249
REMARK 465 GLY B -1
REMARK 465 PRO B 0
REMARK 465 SER B 63
REMARK 465 VAL B 64
REMARK 465 GLU B 65
REMARK 465 PRO B 66
REMARK 465 GLU B 67
REMARK 465 PRO B 68
REMARK 465 GLU B 69
REMARK 465 GLY B 209
REMARK 465 PHE B 210
REMARK 465 ASN B 211
REMARK 465 SER B 212
REMARK 465 GLY B 213
REMARK 465 ARG B 214
REMARK 465 ARG B 215
REMARK 465 HIS B 243
REMARK 465 SER B 244
REMARK 465 SER B 245
REMARK 465 ARG B 246
REMARK 465 HIS B 247
REMARK 465 ARG B 248
REMARK 465 ARG B 249
REMARK 465 ILE B 300
REMARK 465 TRP B 301
REMARK 465 SER B 302
REMARK 465 LEU B 303
REMARK 465 ASP B 304
REMARK 465 THR B 305
REMARK 465 GLN B 306
REMARK 465 TYR B 307
REMARK 465 SER B 308
REMARK 465 LYS B 309
REMARK 465 SER C 63
REMARK 465 VAL C 64
REMARK 465 GLU C 65
REMARK 465 PRO C 66
REMARK 465 GLU C 67
REMARK 465 GLY C 209
REMARK 465 PHE C 210
REMARK 465 ASN C 211
REMARK 465 SER C 212
REMARK 465 GLY C 213
REMARK 465 ARG C 214
REMARK 465 ARG C 215
REMARK 465 LEU C 242
REMARK 465 HIS C 243
REMARK 465 SER C 244
REMARK 465 SER C 245
REMARK 465 ARG C 246
REMARK 465 HIS C 247
REMARK 465 ARG C 248
REMARK 465 ARG C 249
REMARK 465 GLY D -1
REMARK 465 SER D 63
REMARK 465 VAL D 64
REMARK 465 GLU D 65
REMARK 465 PRO D 66
REMARK 465 GLU D 67
REMARK 465 PRO D 68
REMARK 465 GLY D 209
REMARK 465 PHE D 210
REMARK 465 ASN D 211
REMARK 465 SER D 212
REMARK 465 GLY D 213
REMARK 465 ARG D 214
REMARK 465 ARG D 215
REMARK 465 HIS D 243
REMARK 465 SER D 244
REMARK 465 SER D 245
REMARK 465 ARG D 246
REMARK 465 HIS D 247
REMARK 465 ARG D 248
REMARK 465 ARG D 249
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 PRO A 0 N CB CG 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 ND2 ASN C 53 C2 NAG F 1 2.05
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 LYS A 96 -169.92 -74.66
REMARK 500 TYR A 145 -79.13 -58.82
REMARK 500 LEU A 153 -68.75 -123.14
REMARK 500 PRO A 160 104.14 -58.12
REMARK 500 PRO A 164 89.16 -63.99
REMARK 500 ALA A 184 43.26 -87.89
REMARK 500 LYS A 199 137.95 -176.73
REMARK 500 ALA A 219 -165.28 -165.51
REMARK 500 LEU A 269 111.20 -168.25
REMARK 500 ASN A 291 -176.03 57.90
REMARK 500 ALA A 321 160.64 67.58
REMARK 500 SER A 322 -36.78 71.37
REMARK 500 ALA A 323 -23.90 68.54
REMARK 500 LYS B 96 -169.87 -74.71
REMARK 500 TYR B 145 -79.12 -58.80
REMARK 500 LEU B 153 -68.92 -123.18
REMARK 500 PRO B 160 104.16 -58.18
REMARK 500 PRO B 164 89.17 -64.02
REMARK 500 ALA B 184 43.29 -87.96
REMARK 500 LYS B 199 137.96 -176.75
REMARK 500 ALA B 219 -165.23 -165.52
REMARK 500 LEU B 269 111.28 -168.17
REMARK 500 ASN B 291 -175.92 58.06
REMARK 500 PRO B 298 157.29 -48.99
REMARK 500 ASN B 318 63.64 -156.87
REMARK 500 ALA B 323 -9.08 -57.12
REMARK 500 CYS B 327 90.86 -66.35
REMARK 500 PRO C 0 -74.58 -44.41
REMARK 500 PRO C 70 -178.03 -64.32
REMARK 500 TYR C 74 -58.17 -29.44
REMARK 500 LYS C 96 -169.76 -74.74
REMARK 500 TYR C 145 -79.18 -58.76
REMARK 500 LEU C 153 -68.95 -123.24
REMARK 500 PRO C 160 104.12 -58.15
REMARK 500 PRO C 164 89.17 -64.05
REMARK 500 ALA C 184 43.19 -87.90
REMARK 500 LYS C 199 137.95 -176.66
REMARK 500 ALA C 219 -165.28 -165.50
REMARK 500 LEU C 269 111.23 -168.06
REMARK 500 ASN C 291 -176.11 58.06
REMARK 500 CYS C 297 77.20 -119.16
REMARK 500 TYR C 299 129.17 -35.83
REMARK 500 THR C 305 173.09 -59.49
REMARK 500 GLN C 306 71.28 58.93
REMARK 500 TYR C 314 46.35 -96.84
REMARK 500 ALA C 323 -1.41 63.51
REMARK 500 ALA C 324 112.12 -169.43
REMARK 500 PRO D 70 -112.83 -87.48
REMARK 500 TYR D 74 -76.03 -57.93
REMARK 500 LYS D 96 -169.85 -74.74
REMARK 500
REMARK 500 THIS ENTRY HAS 64 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE AUTHORS SEQUENCE CORRESPONDS TO REFERENCE SEQUENCE NP_999180.1
DBREF 3RJR A 1 361 UNP P07200 TGFB1_PIG 30 390
DBREF 3RJR B 1 361 UNP P07200 TGFB1_PIG 30 390
DBREF 3RJR C 1 361 UNP P07200 TGFB1_PIG 30 390
DBREF 3RJR D 1 361 UNP P07200 TGFB1_PIG 30 390
SEQADV 3RJR GLY A -1 UNP P07200 EXPRESSION TAG
SEQADV 3RJR PRO A 0 UNP P07200 EXPRESSION TAG
SEQADV 3RJR SER A 4 UNP P07200 CYS 33 ENGINEERED MUTATION
SEQADV 3RJR VAL A 85 UNP P07200 LEU 114 SEE REMARK 999
SEQADV 3RJR GLN A 147 UNP P07200 ASN 176 ENGINEERED MUTATION
SEQADV 3RJR GLY B -1 UNP P07200 EXPRESSION TAG
SEQADV 3RJR PRO B 0 UNP P07200 EXPRESSION TAG
SEQADV 3RJR SER B 4 UNP P07200 CYS 33 ENGINEERED MUTATION
SEQADV 3RJR VAL B 85 UNP P07200 LEU 114 SEE REMARK 999
SEQADV 3RJR GLN B 147 UNP P07200 ASN 176 ENGINEERED MUTATION
SEQADV 3RJR GLY C -1 UNP P07200 EXPRESSION TAG
SEQADV 3RJR PRO C 0 UNP P07200 EXPRESSION TAG
SEQADV 3RJR SER C 4 UNP P07200 CYS 33 ENGINEERED MUTATION
SEQADV 3RJR VAL C 85 UNP P07200 LEU 114 SEE REMARK 999
SEQADV 3RJR GLN C 147 UNP P07200 ASN 176 ENGINEERED MUTATION
SEQADV 3RJR GLY D -1 UNP P07200 EXPRESSION TAG
SEQADV 3RJR PRO D 0 UNP P07200 EXPRESSION TAG
SEQADV 3RJR SER D 4 UNP P07200 CYS 33 ENGINEERED MUTATION
SEQADV 3RJR VAL D 85 UNP P07200 LEU 114 SEE REMARK 999
SEQADV 3RJR GLN D 147 UNP P07200 ASN 176 ENGINEERED MUTATION
SEQRES 1 A 363 GLY PRO LEU SER THR SER LYS THR ILE ASP MET GLU LEU
SEQRES 2 A 363 VAL LYS ARG LYS ARG ILE GLU ALA ILE ARG GLY GLN ILE
SEQRES 3 A 363 LEU SER LYS LEU ARG LEU ALA SER PRO PRO SER GLN GLY
SEQRES 4 A 363 ASP VAL PRO PRO GLY PRO LEU PRO GLU ALA VAL LEU ALA
SEQRES 5 A 363 LEU TYR ASN SER THR ARG ASP ARG VAL ALA GLY GLU SER
SEQRES 6 A 363 VAL GLU PRO GLU PRO GLU PRO GLU ALA ASP TYR TYR ALA
SEQRES 7 A 363 LYS GLU VAL THR ARG VAL LEU MET VAL GLU SER GLY ASN
SEQRES 8 A 363 GLN ILE TYR ASP LYS PHE LYS GLY THR PRO HIS SER LEU
SEQRES 9 A 363 TYR MET LEU PHE ASN THR SER GLU LEU ARG GLU ALA VAL
SEQRES 10 A 363 PRO GLU PRO VAL LEU LEU SER ARG ALA GLU LEU ARG LEU
SEQRES 11 A 363 LEU ARG LEU LYS LEU LYS VAL GLU GLN HIS VAL GLU LEU
SEQRES 12 A 363 TYR GLN LYS TYR SER GLN ASP SER TRP ARG TYR LEU SER
SEQRES 13 A 363 ASN ARG LEU LEU ALA PRO SER ASP SER PRO GLU TRP LEU
SEQRES 14 A 363 SER PHE ASP VAL THR GLY VAL VAL ARG GLN TRP LEU THR
SEQRES 15 A 363 ARG ARG GLU ALA ILE GLU GLY PHE ARG LEU SER ALA HIS
SEQRES 16 A 363 CYS SER CYS ASP SER LYS ASP ASN THR LEU HIS VAL GLU
SEQRES 17 A 363 ILE ASN GLY PHE ASN SER GLY ARG ARG GLY ASP LEU ALA
SEQRES 18 A 363 THR ILE HIS GLY MET ASN ARG PRO PHE LEU LEU LEU MET
SEQRES 19 A 363 ALA THR PRO LEU GLU ARG ALA GLN HIS LEU HIS SER SER
SEQRES 20 A 363 ARG HIS ARG ARG ALA LEU ASP THR ASN TYR CYS PHE SER
SEQRES 21 A 363 SER THR GLU LYS ASN CYS CYS VAL ARG GLN LEU TYR ILE
SEQRES 22 A 363 ASP PHE ARG LYS ASP LEU GLY TRP LYS TRP ILE HIS GLU
SEQRES 23 A 363 PRO LYS GLY TYR HIS ALA ASN PHE CYS LEU GLY PRO CYS
SEQRES 24 A 363 PRO TYR ILE TRP SER LEU ASP THR GLN TYR SER LYS VAL
SEQRES 25 A 363 LEU ALA LEU TYR ASN GLN HIS ASN PRO GLY ALA SER ALA
SEQRES 26 A 363 ALA PRO CYS CYS VAL PRO GLN ALA LEU GLU PRO LEU PRO
SEQRES 27 A 363 ILE VAL TYR TYR VAL GLY ARG LYS PRO LYS VAL GLU GLN
SEQRES 28 A 363 LEU SER ASN MET ILE VAL ARG SER CYS LYS CYS SER
SEQRES 1 B 363 GLY PRO LEU SER THR SER LYS THR ILE ASP MET GLU LEU
SEQRES 2 B 363 VAL LYS ARG LYS ARG ILE GLU ALA ILE ARG GLY GLN ILE
SEQRES 3 B 363 LEU SER LYS LEU ARG LEU ALA SER PRO PRO SER GLN GLY
SEQRES 4 B 363 ASP VAL PRO PRO GLY PRO LEU PRO GLU ALA VAL LEU ALA
SEQRES 5 B 363 LEU TYR ASN SER THR ARG ASP ARG VAL ALA GLY GLU SER
SEQRES 6 B 363 VAL GLU PRO GLU PRO GLU PRO GLU ALA ASP TYR TYR ALA
SEQRES 7 B 363 LYS GLU VAL THR ARG VAL LEU MET VAL GLU SER GLY ASN
SEQRES 8 B 363 GLN ILE TYR ASP LYS PHE LYS GLY THR PRO HIS SER LEU
SEQRES 9 B 363 TYR MET LEU PHE ASN THR SER GLU LEU ARG GLU ALA VAL
SEQRES 10 B 363 PRO GLU PRO VAL LEU LEU SER ARG ALA GLU LEU ARG LEU
SEQRES 11 B 363 LEU ARG LEU LYS LEU LYS VAL GLU GLN HIS VAL GLU LEU
SEQRES 12 B 363 TYR GLN LYS TYR SER GLN ASP SER TRP ARG TYR LEU SER
SEQRES 13 B 363 ASN ARG LEU LEU ALA PRO SER ASP SER PRO GLU TRP LEU
SEQRES 14 B 363 SER PHE ASP VAL THR GLY VAL VAL ARG GLN TRP LEU THR
SEQRES 15 B 363 ARG ARG GLU ALA ILE GLU GLY PHE ARG LEU SER ALA HIS
SEQRES 16 B 363 CYS SER CYS ASP SER LYS ASP ASN THR LEU HIS VAL GLU
SEQRES 17 B 363 ILE ASN GLY PHE ASN SER GLY ARG ARG GLY ASP LEU ALA
SEQRES 18 B 363 THR ILE HIS GLY MET ASN ARG PRO PHE LEU LEU LEU MET
SEQRES 19 B 363 ALA THR PRO LEU GLU ARG ALA GLN HIS LEU HIS SER SER
SEQRES 20 B 363 ARG HIS ARG ARG ALA LEU ASP THR ASN TYR CYS PHE SER
SEQRES 21 B 363 SER THR GLU LYS ASN CYS CYS VAL ARG GLN LEU TYR ILE
SEQRES 22 B 363 ASP PHE ARG LYS ASP LEU GLY TRP LYS TRP ILE HIS GLU
SEQRES 23 B 363 PRO LYS GLY TYR HIS ALA ASN PHE CYS LEU GLY PRO CYS
SEQRES 24 B 363 PRO TYR ILE TRP SER LEU ASP THR GLN TYR SER LYS VAL
SEQRES 25 B 363 LEU ALA LEU TYR ASN GLN HIS ASN PRO GLY ALA SER ALA
SEQRES 26 B 363 ALA PRO CYS CYS VAL PRO GLN ALA LEU GLU PRO LEU PRO
SEQRES 27 B 363 ILE VAL TYR TYR VAL GLY ARG LYS PRO LYS VAL GLU GLN
SEQRES 28 B 363 LEU SER ASN MET ILE VAL ARG SER CYS LYS CYS SER
SEQRES 1 C 363 GLY PRO LEU SER THR SER LYS THR ILE ASP MET GLU LEU
SEQRES 2 C 363 VAL LYS ARG LYS ARG ILE GLU ALA ILE ARG GLY GLN ILE
SEQRES 3 C 363 LEU SER LYS LEU ARG LEU ALA SER PRO PRO SER GLN GLY
SEQRES 4 C 363 ASP VAL PRO PRO GLY PRO LEU PRO GLU ALA VAL LEU ALA
SEQRES 5 C 363 LEU TYR ASN SER THR ARG ASP ARG VAL ALA GLY GLU SER
SEQRES 6 C 363 VAL GLU PRO GLU PRO GLU PRO GLU ALA ASP TYR TYR ALA
SEQRES 7 C 363 LYS GLU VAL THR ARG VAL LEU MET VAL GLU SER GLY ASN
SEQRES 8 C 363 GLN ILE TYR ASP LYS PHE LYS GLY THR PRO HIS SER LEU
SEQRES 9 C 363 TYR MET LEU PHE ASN THR SER GLU LEU ARG GLU ALA VAL
SEQRES 10 C 363 PRO GLU PRO VAL LEU LEU SER ARG ALA GLU LEU ARG LEU
SEQRES 11 C 363 LEU ARG LEU LYS LEU LYS VAL GLU GLN HIS VAL GLU LEU
SEQRES 12 C 363 TYR GLN LYS TYR SER GLN ASP SER TRP ARG TYR LEU SER
SEQRES 13 C 363 ASN ARG LEU LEU ALA PRO SER ASP SER PRO GLU TRP LEU
SEQRES 14 C 363 SER PHE ASP VAL THR GLY VAL VAL ARG GLN TRP LEU THR
SEQRES 15 C 363 ARG ARG GLU ALA ILE GLU GLY PHE ARG LEU SER ALA HIS
SEQRES 16 C 363 CYS SER CYS ASP SER LYS ASP ASN THR LEU HIS VAL GLU
SEQRES 17 C 363 ILE ASN GLY PHE ASN SER GLY ARG ARG GLY ASP LEU ALA
SEQRES 18 C 363 THR ILE HIS GLY MET ASN ARG PRO PHE LEU LEU LEU MET
SEQRES 19 C 363 ALA THR PRO LEU GLU ARG ALA GLN HIS LEU HIS SER SER
SEQRES 20 C 363 ARG HIS ARG ARG ALA LEU ASP THR ASN TYR CYS PHE SER
SEQRES 21 C 363 SER THR GLU LYS ASN CYS CYS VAL ARG GLN LEU TYR ILE
SEQRES 22 C 363 ASP PHE ARG LYS ASP LEU GLY TRP LYS TRP ILE HIS GLU
SEQRES 23 C 363 PRO LYS GLY TYR HIS ALA ASN PHE CYS LEU GLY PRO CYS
SEQRES 24 C 363 PRO TYR ILE TRP SER LEU ASP THR GLN TYR SER LYS VAL
SEQRES 25 C 363 LEU ALA LEU TYR ASN GLN HIS ASN PRO GLY ALA SER ALA
SEQRES 26 C 363 ALA PRO CYS CYS VAL PRO GLN ALA LEU GLU PRO LEU PRO
SEQRES 27 C 363 ILE VAL TYR TYR VAL GLY ARG LYS PRO LYS VAL GLU GLN
SEQRES 28 C 363 LEU SER ASN MET ILE VAL ARG SER CYS LYS CYS SER
SEQRES 1 D 363 GLY PRO LEU SER THR SER LYS THR ILE ASP MET GLU LEU
SEQRES 2 D 363 VAL LYS ARG LYS ARG ILE GLU ALA ILE ARG GLY GLN ILE
SEQRES 3 D 363 LEU SER LYS LEU ARG LEU ALA SER PRO PRO SER GLN GLY
SEQRES 4 D 363 ASP VAL PRO PRO GLY PRO LEU PRO GLU ALA VAL LEU ALA
SEQRES 5 D 363 LEU TYR ASN SER THR ARG ASP ARG VAL ALA GLY GLU SER
SEQRES 6 D 363 VAL GLU PRO GLU PRO GLU PRO GLU ALA ASP TYR TYR ALA
SEQRES 7 D 363 LYS GLU VAL THR ARG VAL LEU MET VAL GLU SER GLY ASN
SEQRES 8 D 363 GLN ILE TYR ASP LYS PHE LYS GLY THR PRO HIS SER LEU
SEQRES 9 D 363 TYR MET LEU PHE ASN THR SER GLU LEU ARG GLU ALA VAL
SEQRES 10 D 363 PRO GLU PRO VAL LEU LEU SER ARG ALA GLU LEU ARG LEU
SEQRES 11 D 363 LEU ARG LEU LYS LEU LYS VAL GLU GLN HIS VAL GLU LEU
SEQRES 12 D 363 TYR GLN LYS TYR SER GLN ASP SER TRP ARG TYR LEU SER
SEQRES 13 D 363 ASN ARG LEU LEU ALA PRO SER ASP SER PRO GLU TRP LEU
SEQRES 14 D 363 SER PHE ASP VAL THR GLY VAL VAL ARG GLN TRP LEU THR
SEQRES 15 D 363 ARG ARG GLU ALA ILE GLU GLY PHE ARG LEU SER ALA HIS
SEQRES 16 D 363 CYS SER CYS ASP SER LYS ASP ASN THR LEU HIS VAL GLU
SEQRES 17 D 363 ILE ASN GLY PHE ASN SER GLY ARG ARG GLY ASP LEU ALA
SEQRES 18 D 363 THR ILE HIS GLY MET ASN ARG PRO PHE LEU LEU LEU MET
SEQRES 19 D 363 ALA THR PRO LEU GLU ARG ALA GLN HIS LEU HIS SER SER
SEQRES 20 D 363 ARG HIS ARG ARG ALA LEU ASP THR ASN TYR CYS PHE SER
SEQRES 21 D 363 SER THR GLU LYS ASN CYS CYS VAL ARG GLN LEU TYR ILE
SEQRES 22 D 363 ASP PHE ARG LYS ASP LEU GLY TRP LYS TRP ILE HIS GLU
SEQRES 23 D 363 PRO LYS GLY TYR HIS ALA ASN PHE CYS LEU GLY PRO CYS
SEQRES 24 D 363 PRO TYR ILE TRP SER LEU ASP THR GLN TYR SER LYS VAL
SEQRES 25 D 363 LEU ALA LEU TYR ASN GLN HIS ASN PRO GLY ALA SER ALA
SEQRES 26 D 363 ALA PRO CYS CYS VAL PRO GLN ALA LEU GLU PRO LEU PRO
SEQRES 27 D 363 ILE VAL TYR TYR VAL GLY ARG LYS PRO LYS VAL GLU GLN
SEQRES 28 D 363 LEU SER ASN MET ILE VAL ARG SER CYS LYS CYS SER
MODRES 3RJR ASN B 53 ASN GLYCOSYLATION SITE
MODRES 3RJR ASN C 107 ASN GLYCOSYLATION SITE
MODRES 3RJR ASN A 53 ASN GLYCOSYLATION SITE
MODRES 3RJR ASN D 107 ASN GLYCOSYLATION SITE
MODRES 3RJR ASN D 53 ASN GLYCOSYLATION SITE
MODRES 3RJR ASN C 53 ASN GLYCOSYLATION SITE
HET NAG E 1 14
HET NAG E 2 14
HET NAG F 1 14
HET NAG F 2 14
HET NAG A3053 14
HET NAG C3107 14
HET NAG D3053 14
HET NAG D3107 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
FORMUL 5 NAG 8(C8 H15 N O6)
HELIX 1 1 PRO A 0 ARG A 29 1 30
HELIX 2 2 PRO A 45 ASP A 57 1 13
HELIX 3 3 ASN A 107 VAL A 115 1 9
HELIX 4 4 VAL A 171 ARG A 181 1 11
HELIX 5 5 PRO A 235 HIS A 241 1 7
HELIX 6 6 PHE A 273 GLY A 278 1 6
HELIX 7 7 TYR A 307 TYR A 314 1 8
HELIX 8 8 LEU B 1 ARG B 29 1 29
HELIX 9 9 PRO B 45 ASP B 57 1 13
HELIX 10 10 PRO B 70 TYR B 75 1 6
HELIX 11 11 ASN B 107 VAL B 115 1 9
HELIX 12 12 VAL B 171 ARG B 181 1 11
HELIX 13 13 PRO B 235 HIS B 241 1 7
HELIX 14 14 ASP B 252 PHE B 257 1 6
HELIX 15 15 PHE B 273 GLY B 278 1 6
HELIX 16 16 LEU C 1 ARG C 29 1 29
HELIX 17 17 PRO C 45 ASP C 57 1 13
HELIX 18 18 ASN C 107 VAL C 115 1 9
HELIX 19 19 VAL C 171 ARG C 181 1 11
HELIX 20 20 PRO C 235 GLN C 240 1 6
HELIX 21 21 ASP C 252 PHE C 257 1 6
HELIX 22 22 PHE C 273 GLY C 278 1 6
HELIX 23 23 TYR C 299 LEU C 303 5 5
HELIX 24 24 GLN C 306 TYR C 314 1 9
HELIX 25 25 PRO D 0 ARG D 29 1 30
HELIX 26 26 PRO D 45 ASP D 57 1 13
HELIX 27 27 ASN D 107 VAL D 115 1 9
HELIX 28 28 VAL D 171 ARG D 181 1 11
HELIX 29 29 PRO D 235 HIS D 241 1 7
HELIX 30 30 ASP D 252 PHE D 257 1 6
HELIX 31 31 PHE D 273 GLY D 278 1 6
HELIX 32 32 GLN D 306 LEU D 313 1 8
HELIX 33 33 TYR D 314 HIS D 317 5 4
SHEET 1 A 8 ALA A 60 GLU A 62 0
SHEET 2 A 8 TRP A 166 ASP A 170 1 O TRP A 166 N ALA A 60
SHEET 3 A 8 ARG A 123 LEU A 129 -1 N LEU A 128 O LEU A 167
SHEET 4 A 8 PHE A 228 ALA A 233 -1 O PHE A 228 N ARG A 127
SHEET 5 A 8 LYS A 77 LEU A 83 -1 N THR A 80 O LEU A 231
SHEET 6 A 8 LYS B 344 VAL B 355 -1 O VAL B 347 N VAL A 79
SHEET 7 A 8 LEU B 332 VAL B 341 -1 N GLU B 333 O ILE B 354
SHEET 8 A 8 ILE B 282 GLU B 284 -1 N GLU B 284 O VAL B 338
SHEET 1 B 4 SER A 101 PHE A 106 0
SHEET 2 B 4 GLU A 186 ALA A 192 -1 O LEU A 190 N LEU A 102
SHEET 3 B 4 GLN A 137 LYS A 144 -1 N TYR A 142 O ARG A 189
SHEET 4 B 4 TRP A 150 LEU A 158 -1 O SER A 154 N LEU A 141
SHEET 1 C 4 CYS A 194 LYS A 199 0
SHEET 2 C 4 THR A 202 ILE A 207 -1 O HIS A 204 N ASP A 197
SHEET 3 C 4 THR D 202 ILE D 207 -1 O VAL D 205 N LEU A 203
SHEET 4 C 4 CYS D 194 LYS D 199 -1 N ASP D 197 O HIS D 204
SHEET 1 D 2 CYS A 265 ARG A 267 0
SHEET 2 D 2 PHE A 292 LEU A 294 -1 O PHE A 292 N ARG A 267
SHEET 1 E 2 TYR A 270 ASP A 272 0
SHEET 2 E 2 GLY A 287 HIS A 289 -1 O TYR A 288 N ILE A 271
SHEET 1 F 7 ILE A 282 GLU A 284 0
SHEET 2 F 7 LEU A 332 VAL A 341 -1 O VAL A 338 N GLU A 284
SHEET 3 F 7 LYS A 344 VAL A 355 -1 O ILE A 354 N GLU A 333
SHEET 4 F 7 LYS B 77 LEU B 83 -1 O VAL B 79 N VAL A 347
SHEET 5 F 7 PHE B 228 ALA B 233 -1 O LEU B 231 N THR B 80
SHEET 6 F 7 ARG B 123 LEU B 129 -1 N ARG B 127 O PHE B 228
SHEET 7 F 7 TRP B 166 ASP B 170 -1 O LEU B 167 N LEU B 128
SHEET 1 G 2 CYS A 326 PRO A 329 0
SHEET 2 G 2 CYS A 358 SER A 361 -1 O LYS A 359 N VAL A 328
SHEET 1 H 4 SER B 101 PHE B 106 0
SHEET 2 H 4 GLU B 186 ALA B 192 -1 O LEU B 190 N LEU B 102
SHEET 3 H 4 GLN B 137 LYS B 144 -1 N TYR B 142 O ARG B 189
SHEET 4 H 4 TRP B 150 LEU B 158 -1 O SER B 154 N LEU B 141
SHEET 1 I 4 CYS B 194 LYS B 199 0
SHEET 2 I 4 THR B 202 ILE B 207 -1 O HIS B 204 N ASP B 197
SHEET 3 I 4 THR C 202 ILE C 207 -1 O LEU C 203 N VAL B 205
SHEET 4 I 4 CYS C 194 LYS C 199 -1 N ASP C 197 O HIS C 204
SHEET 1 J 2 CYS B 265 ARG B 267 0
SHEET 2 J 2 PHE B 292 LEU B 294 -1 O PHE B 292 N ARG B 267
SHEET 1 K 2 TYR B 270 ASP B 272 0
SHEET 2 K 2 GLY B 287 HIS B 289 -1 O TYR B 288 N ILE B 271
SHEET 1 L 2 VAL B 328 PRO B 329 0
SHEET 2 L 2 CYS B 358 LYS B 359 -1 O LYS B 359 N VAL B 328
SHEET 1 M 8 ALA C 60 GLU C 62 0
SHEET 2 M 8 TRP C 166 ASP C 170 1 O TRP C 166 N ALA C 60
SHEET 3 M 8 ARG C 123 LEU C 129 -1 N LEU C 128 O LEU C 167
SHEET 4 M 8 PHE C 228 ALA C 233 -1 O PHE C 228 N ARG C 127
SHEET 5 M 8 LYS C 77 LEU C 83 -1 N THR C 80 O LEU C 231
SHEET 6 M 8 LYS D 344 VAL D 355 -1 O VAL D 347 N VAL C 79
SHEET 7 M 8 LEU D 332 VAL D 341 -1 N GLU D 333 O ILE D 354
SHEET 8 M 8 ILE D 282 GLU D 284 -1 N GLU D 284 O VAL D 338
SHEET 1 N 4 SER C 101 PHE C 106 0
SHEET 2 N 4 GLU C 186 ALA C 192 -1 O LEU C 190 N LEU C 102
SHEET 3 N 4 GLN C 137 LYS C 144 -1 N TYR C 142 O ARG C 189
SHEET 4 N 4 TRP C 150 LEU C 158 -1 O SER C 154 N LEU C 141
SHEET 1 O 2 CYS C 265 ARG C 267 0
SHEET 2 O 2 PHE C 292 LEU C 294 -1 O PHE C 292 N ARG C 267
SHEET 1 P 2 TYR C 270 ASP C 272 0
SHEET 2 P 2 GLY C 287 HIS C 289 -1 O TYR C 288 N ILE C 271
SHEET 1 Q 8 ILE C 282 GLU C 284 0
SHEET 2 Q 8 LEU C 332 VAL C 341 -1 O VAL C 338 N GLU C 284
SHEET 3 Q 8 LYS C 344 VAL C 355 -1 O ILE C 354 N GLU C 333
SHEET 4 Q 8 LYS D 77 LEU D 83 -1 O VAL D 79 N VAL C 347
SHEET 5 Q 8 PHE D 228 ALA D 233 -1 O LEU D 231 N THR D 80
SHEET 6 Q 8 ARG D 123 LEU D 129 -1 N ARG D 127 O PHE D 228
SHEET 7 Q 8 TRP D 166 ASP D 170 -1 O LEU D 167 N LEU D 128
SHEET 8 Q 8 ALA D 60 GLU D 62 1 N ALA D 60 O TRP D 166
SHEET 1 R 2 CYS C 327 PRO C 329 0
SHEET 2 R 2 CYS C 358 CYS C 360 -1 O LYS C 359 N VAL C 328
SHEET 1 S 4 SER D 101 PHE D 106 0
SHEET 2 S 4 GLU D 186 ALA D 192 -1 O LEU D 190 N LEU D 102
SHEET 3 S 4 GLN D 137 LYS D 144 -1 N TYR D 142 O ARG D 189
SHEET 4 S 4 TRP D 150 LEU D 158 -1 O SER D 154 N LEU D 141
SHEET 1 T 2 CYS D 265 ARG D 267 0
SHEET 2 T 2 PHE D 292 LEU D 294 -1 O PHE D 292 N ARG D 267
SHEET 1 U 2 TYR D 270 ASP D 272 0
SHEET 2 U 2 GLY D 287 HIS D 289 -1 O TYR D 288 N ILE D 271
SHEET 1 V 2 CYS D 326 PRO D 329 0
SHEET 2 V 2 CYS D 358 SER D 361 -1 O LYS D 359 N VAL D 328
SSBOND 1 CYS A 194 CYS B 196 1555 1555 2.03
SSBOND 2 CYS A 196 CYS B 194 1555 1555 2.03
SSBOND 3 CYS A 256 CYS A 265 1555 1555 2.03
SSBOND 4 CYS A 264 CYS A 327 1555 1555 2.03
SSBOND 5 CYS A 293 CYS A 358 1555 1555 2.03
SSBOND 6 CYS A 297 CYS A 360 1555 1555 2.03
SSBOND 7 CYS A 326 CYS B 326 1555 1555 2.03
SSBOND 8 CYS B 256 CYS B 265 1555 1555 2.03
SSBOND 9 CYS B 264 CYS B 327 1555 1555 2.03
SSBOND 10 CYS B 293 CYS B 358 1555 1555 2.03
SSBOND 11 CYS B 297 CYS B 360 1555 1555 2.03
SSBOND 12 CYS C 194 CYS D 196 1555 1555 2.03
SSBOND 13 CYS C 196 CYS D 194 1555 1555 2.02
SSBOND 14 CYS C 256 CYS C 265 1555 1555 2.03
SSBOND 15 CYS C 264 CYS C 327 1555 1555 2.03
SSBOND 16 CYS C 293 CYS C 358 1555 1555 2.03
SSBOND 17 CYS C 297 CYS C 360 1555 1555 2.03
SSBOND 18 CYS C 326 CYS D 326 1555 1555 2.03
SSBOND 19 CYS D 256 CYS D 265 1555 1555 2.03
SSBOND 20 CYS D 264 CYS D 327 1555 1555 2.03
SSBOND 21 CYS D 293 CYS D 358 1555 1555 2.03
SSBOND 22 CYS D 297 CYS D 360 1555 1555 2.03
LINK ND2 ASN A 53 C1 NAG A3053 1555 1555 1.44
LINK ND2 ASN B 53 C1 NAG E 1 1555 1555 1.44
LINK ND2 ASN C 53 C1 NAG F 1 1555 1555 1.44
LINK ND2 ASN C 107 C1 NAG C3107 1555 1555 1.44
LINK ND2 ASN D 53 C1 NAG D3053 1555 1555 1.44
LINK ND2 ASN D 107 C1 NAG D3107 1555 1555 1.44
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44
CISPEP 1 GLU A 284 PRO A 285 0 -0.14
CISPEP 2 GLU B 284 PRO B 285 0 -0.11
CISPEP 3 GLU C 284 PRO C 285 0 -0.21
CISPEP 4 GLU D 284 PRO D 285 0 -0.19
CRYST1 54.690 126.940 137.930 90.00 96.72 90.00 P 1 21 1 8
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 0.018285 0.000000 0.002154 0.00000
SCALE2 0.000000 0.007878 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007300 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
