HEADER IMMUNE SYSTEM 05-JUN-13 4L3E
TITLE THE COMPLEX BETWEEN HIGH AFFINITY TCR DMF5(ALPHA-D26Y,BETA-L98W) AND
TITLE 2 HUMAN CLASS I MHC HLA-A2 WITH THE BOUND MART-1(26-35)(A27L) PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, A-2 ALPHA CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 25-299;
COMPND 5 SYNONYM: MHC CLASS I ANTIGEN A*2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: BETA-2-MICROGLOBULIN;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: UNP RESIDUES 21-119;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: MELANOMA ANTIGEN RECOGNIZED BY T-CELLS 1;
COMPND 14 CHAIN: C;
COMPND 15 FRAGMENT: UNP RESIDUES 26-35;
COMPND 16 SYNONYM: MART-1, ANTIGEN LB39-AA, ANTIGEN SK29-AA, PROTEIN MELAN-A;
COMPND 17 ENGINEERED: YES;
COMPND 18 MUTATION: YES;
COMPND 19 MOL_ID: 4;
COMPND 20 MOLECULE: DMF5 ALPHA CHAIN;
COMPND 21 CHAIN: D;
COMPND 22 ENGINEERED: YES;
COMPND 23 MOL_ID: 5;
COMPND 24 MOLECULE: DMF5 BETA CHAIN;
COMPND 25 CHAIN: E;
COMPND 26 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: HLA-A, HLAA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: B2M, CDABP0092, HDCMA22P;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 MOL_ID: 3;
SOURCE 16 SYNTHETIC: YES;
SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 18 ORGANISM_COMMON: HUMAN;
SOURCE 19 ORGANISM_TAXID: 9606;
SOURCE 20 MOL_ID: 4;
SOURCE 21 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 22 ORGANISM_COMMON: HUMAN;
SOURCE 23 ORGANISM_TAXID: 9606;
SOURCE 24 GENE: TRAC, TCRA;
SOURCE 25 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 26 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 27 MOL_ID: 5;
SOURCE 28 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 29 ORGANISM_COMMON: HUMAN;
SOURCE 30 ORGANISM_TAXID: 9606;
SOURCE 31 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 32 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS RECEPTORS, MEMBRANE, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR L.M.HELLMAN
REVDAT 2 27-AUG-14 4L3E 1 JRNL
REVDAT 1 11-JUN-14 4L3E 0
JRNL AUTH B.G.PIERCE,L.M.HELLMAN,M.HOSSAIN,N.K.SINGH,C.W.VANDER KOOI,
JRNL AUTH 2 Z.WENG,B.M.BAKER
JRNL TITL COMPUTATIONAL DESIGN OF THE AFFINITY AND SPECIFICITY OF A
JRNL TITL 2 THERAPEUTIC T CELL RECEPTOR.
JRNL REF PLOS COMPUT.BIOL. V. 10 03478 2014
JRNL REFN ISSN 1553-734X
JRNL PMID 24550723
JRNL DOI 10.1371/JOURNAL.PCBI.1003478
REMARK 2
REMARK 2 RESOLUTION. 2.56 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.56
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.05
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.6
REMARK 3 NUMBER OF REFLECTIONS : 31816
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.231
REMARK 3 R VALUE (WORKING SET) : 0.229
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110
REMARK 3 FREE R VALUE TEST SET COUNT : 1625
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 20.0473 - 5.8097 0.99 2743 150 0.1852 0.2179
REMARK 3 2 5.8097 - 4.6300 0.99 2667 155 0.1857 0.2195
REMARK 3 3 4.6300 - 4.0502 0.99 2619 153 0.1902 0.2445
REMARK 3 4 4.0502 - 3.6824 0.99 2644 143 0.2236 0.2338
REMARK 3 5 3.6824 - 3.4199 0.99 2616 148 0.2416 0.2878
REMARK 3 6 3.4199 - 3.2191 0.98 2603 135 0.2680 0.3386
REMARK 3 7 3.2191 - 3.0585 0.98 2613 119 0.3047 0.3956
REMARK 3 8 3.0585 - 2.9258 0.96 2516 142 0.2868 0.3066
REMARK 3 9 2.9258 - 2.8135 0.93 2466 135 0.3311 0.3736
REMARK 3 10 2.8135 - 2.7166 0.89 2340 128 0.3484 0.4641
REMARK 3 11 2.7166 - 2.6319 0.86 2277 106 0.3542 0.3374
REMARK 3 12 2.6319 - 2.5570 0.80 2087 111 0.3755 0.4264
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.380
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 35.620
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 6782
REMARK 3 ANGLE : 1.151 9198
REMARK 3 CHIRALITY : 0.075 966
REMARK 3 PLANARITY : 0.005 1206
REMARK 3 DIHEDRAL : 16.591 2453
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 29
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: chain 'A' and (resid 1 through 84 )
REMARK 3 ORIGIN FOR THE GROUP (A): -41.0144 -22.3900 -6.0475
REMARK 3 T TENSOR
REMARK 3 T11: 0.2406 T22: -0.0216
REMARK 3 T33: 0.2766 T12: 0.1900
REMARK 3 T13: 0.0685 T23: -0.1219
REMARK 3 L TENSOR
REMARK 3 L11: 1.1255 L22: 0.9602
REMARK 3 L33: 1.5430 L12: -0.5613
REMARK 3 L13: 0.2193 L23: 0.0672
REMARK 3 S TENSOR
REMARK 3 S11: 0.1768 S12: 0.3791 S13: -0.1218
REMARK 3 S21: -0.0594 S22: -0.1501 S23: 0.2262
REMARK 3 S31: 0.5911 S32: 0.3051 S33: 0.0615
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain 'A' and (resid 85 through 137 )
REMARK 3 ORIGIN FOR THE GROUP (A): -38.9297 -7.2728 -2.5562
REMARK 3 T TENSOR
REMARK 3 T11: 0.2154 T22: 0.0787
REMARK 3 T33: 0.6339 T12: -0.0885
REMARK 3 T13: 0.1088 T23: 0.0420
REMARK 3 L TENSOR
REMARK 3 L11: 1.0297 L22: 1.3033
REMARK 3 L33: 1.6414 L12: -0.3164
REMARK 3 L13: 0.5125 L23: 0.5421
REMARK 3 S TENSOR
REMARK 3 S11: 0.0953 S12: 0.2670 S13: 0.2738
REMARK 3 S21: -0.2068 S22: -0.1415 S23: -0.1018
REMARK 3 S31: -0.3741 S32: 0.4031 S33: 0.1673
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: chain 'A' and (resid 138 through 185 )
REMARK 3 ORIGIN FOR THE GROUP (A): -30.9482 -12.6320 -8.5695
REMARK 3 T TENSOR
REMARK 3 T11: 0.1931 T22: 0.3670
REMARK 3 T33: 0.4378 T12: -0.0201
REMARK 3 T13: 0.0876 T23: 0.0159
REMARK 3 L TENSOR
REMARK 3 L11: 1.6813 L22: 1.1715
REMARK 3 L33: 0.9716 L12: -0.4985
REMARK 3 L13: 0.8997 L23: -0.5524
REMARK 3 S TENSOR
REMARK 3 S11: 0.2610 S12: 0.6871 S13: 0.3008
REMARK 3 S21: -0.2420 S22: -0.0754 S23: -0.3374
REMARK 3 S31: -0.0258 S32: 0.6029 S33: -0.2650
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: chain 'A' and (resid 186 through 242 )
REMARK 3 ORIGIN FOR THE GROUP (A): -53.8529 -1.8446 -31.4016
REMARK 3 T TENSOR
REMARK 3 T11: 0.7760 T22: 0.7234
REMARK 3 T33: 0.8633 T12: 0.1262
REMARK 3 T13: 0.0408 T23: 0.5304
REMARK 3 L TENSOR
REMARK 3 L11: 1.2468 L22: 1.1529
REMARK 3 L33: 1.0503 L12: -0.7815
REMARK 3 L13: 0.8386 L23: 0.0328
REMARK 3 S TENSOR
REMARK 3 S11: -0.1317 S12: 0.3803 S13: 0.8579
REMARK 3 S21: -0.3551 S22: 0.1128 S23: 0.2923
REMARK 3 S31: -0.8137 S32: -0.1338 S33: 0.1253
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: chain 'A' and (resid 243 through 262 )
REMARK 3 ORIGIN FOR THE GROUP (A): -55.8335 4.4773 -36.0393
REMARK 3 T TENSOR
REMARK 3 T11: 1.0374 T22: 0.8852
REMARK 3 T33: 1.1143 T12: 0.0913
REMARK 3 T13: 0.0572 T23: 0.6465
REMARK 3 L TENSOR
REMARK 3 L11: 0.0639 L22: 0.2434
REMARK 3 L33: 0.2428 L12: -0.1209
REMARK 3 L13: -0.1209 L23: 0.2430
REMARK 3 S TENSOR
REMARK 3 S11: -0.1323 S12: 0.4808 S13: 0.4662
REMARK 3 S21: -0.4181 S22: 0.0177 S23: 0.0969
REMARK 3 S31: -0.7425 S32: -0.1151 S33: -0.0336
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: chain 'A' and (resid 263 through 275 )
REMARK 3 ORIGIN FOR THE GROUP (A): -45.4108 -1.4982 -39.3532
REMARK 3 T TENSOR
REMARK 3 T11: 0.8161 T22: 0.9792
REMARK 3 T33: 1.0880 T12: -0.0631
REMARK 3 T13: 0.1520 T23: 0.5346
REMARK 3 L TENSOR
REMARK 3 L11: 1.3105 L22: 2.4567
REMARK 3 L33: 1.2136 L12: -0.2269
REMARK 3 L13: -0.3192 L23: -0.0492
REMARK 3 S TENSOR
REMARK 3 S11: 0.0425 S12: 0.3724 S13: 0.3842
REMARK 3 S21: -0.4109 S22: -0.0459 S23: 0.1111
REMARK 3 S31: -0.4777 S32: -0.1112 S33: -0.0120
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: chain 'B' and (resid 0 through 5 )
REMARK 3 ORIGIN FOR THE GROUP (A): -58.4355 -6.5435 -4.9737
REMARK 3 T TENSOR
REMARK 3 T11: 0.2501 T22: 0.2135
REMARK 3 T33: 0.6466 T12: 0.0234
REMARK 3 T13: -0.1188 T23: 0.0936
REMARK 3 L TENSOR
REMARK 3 L11: 9.5479 L22: 8.5334
REMARK 3 L33: 9.7306 L12: 3.3828
REMARK 3 L13: 5.6889 L23: 6.9252
REMARK 3 S TENSOR
REMARK 3 S11: -0.3016 S12: -0.1424 S13: 0.3512
REMARK 3 S21: 0.1024 S22: -0.0129 S23: -0.9298
REMARK 3 S31: -0.5346 S32: 0.6169 S33: 0.3033
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: chain 'B' and (resid 6 through 19 )
REMARK 3 ORIGIN FOR THE GROUP (A): -58.0644 -17.3793 -30.3657
REMARK 3 T TENSOR
REMARK 3 T11: 0.5367 T22: 0.3295
REMARK 3 T33: 0.2750 T12: 0.1355
REMARK 3 T13: -0.0851 T23: 0.1424
REMARK 3 L TENSOR
REMARK 3 L11: 3.2129 L22: 3.4920
REMARK 3 L33: 3.8748 L12: 0.1271
REMARK 3 L13: 0.2752 L23: 1.4480
REMARK 3 S TENSOR
REMARK 3 S11: 0.0443 S12: 0.7956 S13: -0.0350
REMARK 3 S21: -0.7967 S22: -0.0110 S23: 0.0434
REMARK 3 S31: 0.3545 S32: 0.1329 S33: -0.0648
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: chain 'B' and (resid 20 through 41 )
REMARK 3 ORIGIN FOR THE GROUP (A): -59.2358 -17.8990 -17.2638
REMARK 3 T TENSOR
REMARK 3 T11: 0.2590 T22: 0.0817
REMARK 3 T33: 0.3105 T12: 0.1660
REMARK 3 T13: -0.0129 T23: 0.1274
REMARK 3 L TENSOR
REMARK 3 L11: 0.1720 L22: 0.3252
REMARK 3 L33: 0.5661 L12: 0.1675
REMARK 3 L13: 0.0104 L23: 0.2920
REMARK 3 S TENSOR
REMARK 3 S11: 0.1435 S12: 0.1281 S13: -0.0820
REMARK 3 S21: -0.1586 S22: -0.0145 S23: 0.0714
REMARK 3 S31: 0.2028 S32: 0.0514 S33: 0.0006
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: chain 'B' and (resid 42 through 51 )
REMARK 3 ORIGIN FOR THE GROUP (A): -64.0235 -26.9674 -19.9566
REMARK 3 T TENSOR
REMARK 3 T11: 0.3624 T22: 0.1992
REMARK 3 T33: 0.1870 T12: 0.0460
REMARK 3 T13: -0.1013 T23: -0.0441
REMARK 3 L TENSOR
REMARK 3 L11: 3.7933 L22: 1.4735
REMARK 3 L33: 3.2511 L12: 0.1663
REMARK 3 L13: 2.4738 L23: -0.0202
REMARK 3 S TENSOR
REMARK 3 S11: 0.2145 S12: -0.0466 S13: -0.4498
REMARK 3 S21: -0.0312 S22: 0.0275 S23: 0.0280
REMARK 3 S31: 0.4725 S32: -0.0547 S33: -0.2002
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: chain 'B' and (resid 52 through 71 )
REMARK 3 ORIGIN FOR THE GROUP (A): -52.1513 -16.5755 -15.7364
REMARK 3 T TENSOR
REMARK 3 T11: 0.2715 T22: 0.0165
REMARK 3 T33: 0.3237 T12: 0.0139
REMARK 3 T13: 0.0703 T23: 0.0596
REMARK 3 L TENSOR
REMARK 3 L11: 2.1463 L22: 2.5939
REMARK 3 L33: 3.7726 L12: -0.0188
REMARK 3 L13: 1.9107 L23: 0.8034
REMARK 3 S TENSOR
REMARK 3 S11: 0.0654 S12: 0.1296 S13: -0.1312
REMARK 3 S21: -0.3439 S22: 0.0999 S23: -0.0673
REMARK 3 S31: 0.0634 S32: 0.0907 S33: 0.0190
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: chain 'B' and (resid 72 through 77 )
REMARK 3 ORIGIN FOR THE GROUP (A): -69.3626 -22.3871 -34.2150
REMARK 3 T TENSOR
REMARK 3 T11: 0.8004 T22: 0.5439
REMARK 3 T33: 0.6618 T12: 0.0115
REMARK 3 T13: -0.3147 T23: 0.0202
REMARK 3 L TENSOR
REMARK 3 L11: 2.5673 L22: 2.7844
REMARK 3 L33: 4.1219 L12: 0.0319
REMARK 3 L13: 2.9945 L23: -1.2754
REMARK 3 S TENSOR
REMARK 3 S11: 0.1904 S12: 0.8101 S13: 0.0469
REMARK 3 S21: -1.0580 S22: 0.0026 S23: 0.7159
REMARK 3 S31: -0.1237 S32: -0.5971 S33: -0.2072
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: chain 'B' and (resid 78 through 90 )
REMARK 3 ORIGIN FOR THE GROUP (A): -66.9549 -14.8389 -13.2856
REMARK 3 T TENSOR
REMARK 3 T11: 0.2588 T22: 0.0440
REMARK 3 T33: 0.4153 T12: 0.0849
REMARK 3 T13: -0.0585 T23: 0.0584
REMARK 3 L TENSOR
REMARK 3 L11: 0.4104 L22: 0.8603
REMARK 3 L33: 1.3922 L12: 0.1217
REMARK 3 L13: 0.5313 L23: 0.4382
REMARK 3 S TENSOR
REMARK 3 S11: 0.0656 S12: 0.0298 S13: -0.1000
REMARK 3 S21: -0.0895 S22: -0.0594 S23: 0.0310
REMARK 3 S31: -0.0864 S32: -0.0310 S33: 0.0127
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: chain 'B' and (resid 91 through 99 )
REMARK 3 ORIGIN FOR THE GROUP (A): -65.7078 -12.6303 -27.7693
REMARK 3 T TENSOR
REMARK 3 T11: 0.4573 T22: 0.3430
REMARK 3 T33: 0.4609 T12: 0.1770
REMARK 3 T13: -0.0560 T23: 0.2223
REMARK 3 L TENSOR
REMARK 3 L11: 3.6796 L22: 4.3175
REMARK 3 L33: 4.7338 L12: -1.6964
REMARK 3 L13: 0.9733 L23: 1.0831
REMARK 3 S TENSOR
REMARK 3 S11: 0.1281 S12: 0.5736 S13: 0.4048
REMARK 3 S21: -0.7165 S22: -0.2791 S23: -0.2877
REMARK 3 S31: -0.3800 S32: 0.2708 S33: 0.1649
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: chain 'C' and (resid 1 through 10 )
REMARK 3 ORIGIN FOR THE GROUP (A): -33.1214 -16.8293 1.1018
REMARK 3 T TENSOR
REMARK 3 T11: 0.1392 T22: 0.1058
REMARK 3 T33: 0.2140 T12: -0.0026
REMARK 3 T13: 0.0997 T23: -0.0440
REMARK 3 L TENSOR
REMARK 3 L11: 1.4054 L22: 0.7727
REMARK 3 L33: 0.7055 L12: 0.1547
REMARK 3 L13: 0.5429 L23: -0.4618
REMARK 3 S TENSOR
REMARK 3 S11: 0.2359 S12: 0.1653 S13: -0.0262
REMARK 3 S21: -0.0372 S22: -0.0912 S23: 0.1485
REMARK 3 S31: -0.0398 S32: 0.1363 S33: -0.0659
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: chain 'D' and (resid 1 through 13 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.1821 -32.1003 3.3384
REMARK 3 T TENSOR
REMARK 3 T11: 0.5213 T22: 1.1986
REMARK 3 T33: 0.5320 T12: 0.3257
REMARK 3 T13: -0.0388 T23: -0.3007
REMARK 3 L TENSOR
REMARK 3 L11: 5.3450 L22: 1.0923
REMARK 3 L33: 0.9634 L12: 0.6751
REMARK 3 L13: 2.2222 L23: 0.0835
REMARK 3 S TENSOR
REMARK 3 S11: 0.3918 S12: 0.5443 S13: -0.8032
REMARK 3 S21: -0.3621 S22: -0.1826 S23: -0.0906
REMARK 3 S31: 0.0863 S32: -0.1065 S33: -0.3311
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: chain 'D' and (resid 14 through 31 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.0535 -24.5308 -0.6541
REMARK 3 T TENSOR
REMARK 3 T11: 0.2449 T22: 1.0262
REMARK 3 T33: 0.4282 T12: 0.3052
REMARK 3 T13: 0.1277 T23: -0.1847
REMARK 3 L TENSOR
REMARK 3 L11: 0.3315 L22: 0.0065
REMARK 3 L33: 0.2198 L12: -0.0200
REMARK 3 L13: -0.0107 L23: -0.0419
REMARK 3 S TENSOR
REMARK 3 S11: 0.1483 S12: 0.2178 S13: 0.0354
REMARK 3 S21: -0.0122 S22: 0.0181 S23: -0.1636
REMARK 3 S31: 0.0386 S32: 0.3044 S33: -0.0455
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: chain 'D' and (resid 32 through 65 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.5996 -19.4657 7.0976
REMARK 3 T TENSOR
REMARK 3 T11: 0.1039 T22: 0.9785
REMARK 3 T33: 0.3286 T12: 0.2361
REMARK 3 T13: 0.1385 T23: -0.1587
REMARK 3 L TENSOR
REMARK 3 L11: 0.8346 L22: 0.3030
REMARK 3 L33: 0.1849 L12: -0.2922
REMARK 3 L13: -0.1489 L23: 0.0953
REMARK 3 S TENSOR
REMARK 3 S11: 0.1283 S12: 0.0246 S13: 0.3888
REMARK 3 S21: 0.0669 S22: 0.0472 S23: -0.2700
REMARK 3 S31: -0.0002 S32: 0.1272 S33: -0.0925
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: chain 'D' and (resid 66 through 96 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.8094 -23.4219 4.6006
REMARK 3 T TENSOR
REMARK 3 T11: 0.2336 T22: 1.1009
REMARK 3 T33: 0.3544 T12: 0.2117
REMARK 3 T13: 0.0288 T23: -0.1584
REMARK 3 L TENSOR
REMARK 3 L11: 0.6018 L22: 0.3274
REMARK 3 L33: 0.5691 L12: -0.1002
REMARK 3 L13: -0.2926 L23: -0.0875
REMARK 3 S TENSOR
REMARK 3 S11: 0.0996 S12: -0.0061 S13: 0.2567
REMARK 3 S21: 0.0236 S22: -0.0907 S23: -0.2059
REMARK 3 S31: -0.0158 S32: 0.4818 S33: -0.1424
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: chain 'D' and (resid 97 through 116 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.8011 -28.9033 13.3694
REMARK 3 T TENSOR
REMARK 3 T11: 0.3203 T22: 1.2691
REMARK 3 T33: 0.5211 T12: 0.1532
REMARK 3 T13: 0.0523 T23: 0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 4.4048 L22: 2.0722
REMARK 3 L33: 0.5464 L12: -1.0368
REMARK 3 L13: 1.4342 L23: -0.7184
REMARK 3 S TENSOR
REMARK 3 S11: 0.2097 S12: -0.3375 S13: -0.1137
REMARK 3 S21: 0.1052 S22: -0.2958 S23: -0.7616
REMARK 3 S31: 0.0186 S32: 0.6595 S33: 0.0624
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: chain 'D' and (resid 117 through 130 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.7525 -43.9527 37.7905
REMARK 3 T TENSOR
REMARK 3 T11: 0.7432 T22: 1.7643
REMARK 3 T33: 0.9585 T12: 0.2127
REMARK 3 T13: 0.0039 T23: 0.2156
REMARK 3 L TENSOR
REMARK 3 L11: 5.9128 L22: 1.8585
REMARK 3 L33: 0.9650 L12: 0.4856
REMARK 3 L13: 1.0667 L23: 1.2730
REMARK 3 S TENSOR
REMARK 3 S11: 0.1646 S12: -0.9184 S13: -0.5414
REMARK 3 S21: 0.4484 S22: -0.1039 S23: 0.0207
REMARK 3 S31: 0.3113 S32: 0.3300 S33: 0.0106
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: chain 'D' and (resid 131 through 140 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.4175 -36.1562 22.6840
REMARK 3 T TENSOR
REMARK 3 T11: 0.4941 T22: 1.6255
REMARK 3 T33: 0.6114 T12: 0.1540
REMARK 3 T13: 0.0082 T23: -0.0773
REMARK 3 L TENSOR
REMARK 3 L11: 1.8384 L22: 1.9651
REMARK 3 L33: 9.0446 L12: -1.4910
REMARK 3 L13: 0.7661 L23: -2.1488
REMARK 3 S TENSOR
REMARK 3 S11: -0.0723 S12: -0.1312 S13: -0.1826
REMARK 3 S21: -0.2268 S22: -0.0215 S23: -0.0667
REMARK 3 S31: -0.2197 S32: 0.3909 S33: 0.0691
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: chain 'D' and (resid 141 through 150 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.6913 -48.0306 19.4869
REMARK 3 T TENSOR
REMARK 3 T11: 0.7058 T22: 1.3299
REMARK 3 T33: 0.8895 T12: -0.0452
REMARK 3 T13: 0.0627 T23: -0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 1.3360 L22: 6.2257
REMARK 3 L33: 1.2676 L12: 0.8227
REMARK 3 L13: 1.3004 L23: 0.9243
REMARK 3 S TENSOR
REMARK 3 S11: -0.1298 S12: -0.0341 S13: -0.2718
REMARK 3 S21: -0.4289 S22: 0.5503 S23: 0.7739
REMARK 3 S31: 0.3829 S32: -0.4710 S33: -0.3914
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: chain 'D' and (resid 151 through 165 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.8400 -31.4401 25.4267
REMARK 3 T TENSOR
REMARK 3 T11: 0.5502 T22: 1.5356
REMARK 3 T33: 0.6768 T12: -0.0349
REMARK 3 T13: -0.0508 T23: 0.1073
REMARK 3 L TENSOR
REMARK 3 L11: 1.9070 L22: 0.5876
REMARK 3 L33: 3.1084 L12: -0.1128
REMARK 3 L13: -0.3300 L23: -1.3108
REMARK 3 S TENSOR
REMARK 3 S11: -0.1720 S12: -0.0319 S13: 0.0733
REMARK 3 S21: -0.3087 S22: -0.0926 S23: -0.1578
REMARK 3 S31: -0.0499 S32: 0.3204 S33: 0.1933
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: chain 'D' and (resid 166 through 184 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.6661 -43.7371 28.2357
REMARK 3 T TENSOR
REMARK 3 T11: 0.6851 T22: 1.7681
REMARK 3 T33: 0.9025 T12: 0.2294
REMARK 3 T13: -0.1629 T23: 0.1294
REMARK 3 L TENSOR
REMARK 3 L11: 2.2644 L22: 0.9311
REMARK 3 L33: 1.6971 L12: -1.1038
REMARK 3 L13: -0.1221 L23: 0.4603
REMARK 3 S TENSOR
REMARK 3 S11: 0.1132 S12: -0.2800 S13: -0.8746
REMARK 3 S21: -0.0773 S22: -0.0587 S23: -0.5599
REMARK 3 S31: 0.3245 S32: 0.3442 S33: -0.0524
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: chain 'D' and (resid 185 through 199 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.3600 -42.4998 21.9785
REMARK 3 T TENSOR
REMARK 3 T11: 0.5884 T22: 1.7718
REMARK 3 T33: 0.8595 T12: 0.0940
REMARK 3 T13: 0.0810 T23: -0.1044
REMARK 3 L TENSOR
REMARK 3 L11: 0.8268 L22: 1.8109
REMARK 3 L33: 3.5908 L12: 1.1861
REMARK 3 L13: 1.7230 L23: 2.4693
REMARK 3 S TENSOR
REMARK 3 S11: 0.1350 S12: 0.0526 S13: -0.1740
REMARK 3 S21: -0.3888 S22: 0.0646 S23: -0.0492
REMARK 3 S31: -0.0034 S32: 0.3207 S33: -0.1531
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: chain 'E' and (resid 4 through 115 )
REMARK 3 ORIGIN FOR THE GROUP (A): -27.6378 -32.7342 17.0485
REMARK 3 T TENSOR
REMARK 3 T11: 0.4047 T22: 0.0940
REMARK 3 T33: 0.3579 T12: 0.1821
REMARK 3 T13: -0.1400 T23: -0.2961
REMARK 3 L TENSOR
REMARK 3 L11: 1.3759 L22: 0.9126
REMARK 3 L33: 1.2388 L12: -0.5295
REMARK 3 L13: 0.1600 L23: 0.3649
REMARK 3 S TENSOR
REMARK 3 S11: 0.3593 S12: -0.0273 S13: -0.5831
REMARK 3 S21: 0.0526 S22: 0.0825 S23: -0.0626
REMARK 3 S31: 0.6193 S32: 0.4416 S33: -0.0334
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: chain 'E' and (resid 116 through 215 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.2434 -37.5362 33.8021
REMARK 3 T TENSOR
REMARK 3 T11: 0.5816 T22: 1.1904
REMARK 3 T33: 0.4930 T12: 0.0800
REMARK 3 T13: -0.1491 T23: -0.0038
REMARK 3 L TENSOR
REMARK 3 L11: 2.7960 L22: 2.5827
REMARK 3 L33: 1.1270 L12: 0.5145
REMARK 3 L13: -0.0026 L23: -0.7628
REMARK 3 S TENSOR
REMARK 3 S11: 0.0938 S12: -0.0127 S13: -0.4364
REMARK 3 S21: 0.0149 S22: -0.0200 S23: -0.2149
REMARK 3 S31: 0.0143 S32: 0.9106 S33: -0.1295
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: chain 'E' and (resid 216 through 245 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.3687 -42.9264 40.5451
REMARK 3 T TENSOR
REMARK 3 T11: 0.5458 T22: 0.9166
REMARK 3 T33: 0.4554 T12: 0.0557
REMARK 3 T13: -0.0888 T23: 0.1301
REMARK 3 L TENSOR
REMARK 3 L11: 3.8796 L22: 5.0462
REMARK 3 L33: 3.2790 L12: 1.2116
REMARK 3 L13: 1.2631 L23: 0.1147
REMARK 3 S TENSOR
REMARK 3 S11: 0.1062 S12: -0.3412 S13: -0.4769
REMARK 3 S21: 0.4571 S22: 0.2194 S23: 0.7014
REMARK 3 S31: -0.0130 S32: -0.0944 S33: -0.3836
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 4L3E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUN-13.
REMARK 100 THE RCSB ID CODE IS RCSB080130.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-NOV-12
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : ROSENBAUM-ROCK DOUBLE-CRYSTAL
REMARK 200 SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31904
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.557
REMARK 200 RESOLUTION RANGE LOW (A) : 20.047
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.7400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.56
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.43800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> 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: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG3350, 0.1 M TRIS-HCL, 0.25 M
REMARK 280 MAGNESIUM CHLORIDE, PH 8, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 113.52000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.65800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 113.52000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 24.65800
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, 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 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 OD1 ASP E 41 OG SER E 90 2.01
REMARK 500 O PRO A 250 NE2 GLN A 253 2.15
REMARK 500 OE2 GLU E 130 NH1 ARG E 243 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ARG A 17 -128.61 -117.53
REMARK 500 GLU A 19 93.88 61.40
REMARK 500 ASP A 29 -111.85 55.44
REMARK 500 ALA A 40 -177.24 -60.80
REMARK 500 HIS A 188 -169.72 -162.85
REMARK 500 ASP A 196 -70.38 55.24
REMARK 500 PRO A 210 -167.05 -77.71
REMARK 500 GLN A 226 -124.82 -72.01
REMARK 500 ASP A 227 96.55 -47.22
REMARK 500 PRO B 32 -169.93 -74.04
REMARK 500 TRP B 60 -1.66 85.13
REMARK 500 ASP B 98 52.54 -93.40
REMARK 500 SER D 81 33.46 -80.37
REMARK 500 LYS D 125 64.25 -67.25
REMARK 500 SER D 126 -155.19 100.21
REMARK 500 LYS D 129 102.81 -59.13
REMARK 500 SER D 146 75.10 -63.17
REMARK 500 LYS D 147 -131.45 -96.03
REMARK 500 SER D 175 28.92 -167.08
REMARK 500 ASN D 176 -134.71 51.06
REMARK 500 ASP D 179 43.28 -108.50
REMARK 500 ALA D 185 -51.68 -151.78
REMARK 500 PRO D 192 -166.25 -60.98
REMARK 500 GLU D 193 -84.48 -74.37
REMARK 500 LEU E 42 44.94 -56.12
REMARK 500 ILE E 49 -78.88 -89.96
REMARK 500 SER E 68 -169.38 -67.28
REMARK 500 VAL E 69 154.10 167.82
REMARK 500 PHE E 77 69.02 -154.74
REMARK 500 ALA E 82 -83.47 -72.79
REMARK 500 ASP E 154 42.12 -83.41
REMARK 500 PRO E 177 164.80 -45.53
REMARK 500 PRO E 182 45.44 -75.40
REMARK 500 ALA E 183 -52.88 -159.97
REMARK 500 PRO E 231 68.67 -69.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3QDG RELATED DB: PDB
REMARK 900 RELATED ID: 3QDJ RELATED DB: PDB
REMARK 900 RELATED ID: 3QDM RELATED DB: PDB
REMARK 900 RELATED ID: 3QEQ RELATED DB: PDB
REMARK 900 RELATED ID: 3QEU RELATED DB: PDB
DBREF 4L3E A 1 275 UNP P01892 1A02_HUMAN 25 299
DBREF 4L3E B 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 4L3E C 1 10 UNP Q16655 MAR1_HUMAN 26 35
DBREF 4L3E D 1 199 PDB 4L3E 4L3E 1 199
DBREF 4L3E E 4 245 PDB 4L3E 4L3E 4 245
SEQADV 4L3E MET B 0 UNP P61769 INITIATING METHIONINE
SEQADV 4L3E LEU C 2 UNP Q16655 ALA 27 ENGINEERED MUTATION
SEQRES 1 A 275 GLY SER HIS SER MET ARG TYR PHE PHE THR SER VAL SER
SEQRES 2 A 275 ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE ALA VAL GLY
SEQRES 3 A 275 TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP
SEQRES 4 A 275 ALA ALA SER GLN ARG MET GLU PRO ARG ALA PRO TRP ILE
SEQRES 5 A 275 GLU GLN GLU GLY PRO GLU TYR TRP ASP GLY GLU THR ARG
SEQRES 6 A 275 LYS VAL LYS ALA HIS SER GLN THR HIS ARG VAL ASP LEU
SEQRES 7 A 275 GLY THR LEU ARG GLY TYR TYR ASN GLN SER GLU ALA GLY
SEQRES 8 A 275 SER HIS THR VAL GLN ARG MET TYR GLY CYS ASP VAL GLY
SEQRES 9 A 275 SER ASP TRP ARG PHE LEU ARG GLY TYR HIS GLN TYR ALA
SEQRES 10 A 275 TYR ASP GLY LYS ASP TYR ILE ALA LEU LYS GLU ASP LEU
SEQRES 11 A 275 ARG SER TRP THR ALA ALA ASP MET ALA ALA GLN THR THR
SEQRES 12 A 275 LYS HIS LYS TRP GLU ALA ALA HIS VAL ALA GLU GLN LEU
SEQRES 13 A 275 ARG ALA TYR LEU GLU GLY THR CYS VAL GLU TRP LEU ARG
SEQRES 14 A 275 ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG THR
SEQRES 15 A 275 ASP ALA PRO LYS THR HIS MET THR HIS HIS ALA VAL SER
SEQRES 16 A 275 ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU SER PHE
SEQRES 17 A 275 TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP GLY
SEQRES 18 A 275 GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR ARG
SEQRES 19 A 275 PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA VAL
SEQRES 20 A 275 VAL VAL PRO SER GLY GLN GLU GLN ARG TYR THR CYS HIS
SEQRES 21 A 275 VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU ARG
SEQRES 22 A 275 TRP GLU
SEQRES 1 B 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG
SEQRES 2 B 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS
SEQRES 3 B 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP
SEQRES 4 B 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS
SEQRES 5 B 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU
SEQRES 6 B 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU
SEQRES 7 B 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO
SEQRES 8 B 100 LYS ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 C 10 GLU LEU ALA GLY ILE GLY ILE LEU THR VAL
SEQRES 1 D 199 LYS GLU VAL GLU GLN ASN SER GLY PRO LEU SER VAL PRO
SEQRES 2 D 199 GLU GLY ALA ILE ALA SER LEU ASN CYS THR TYR SER TYR
SEQRES 3 D 199 ARG GLY SER GLN SER PHE PHE TRP TYR ARG GLN TYR SER
SEQRES 4 D 199 GLY LYS SER PRO GLU LEU ILE MET PHE ILE TYR SER ASN
SEQRES 5 D 199 GLY ASP LYS GLU ASP GLY ARG PHE THR ALA GLN LEU ASN
SEQRES 6 D 199 LYS ALA SER GLN TYR VAL SER LEU LEU ILE ARG ASP SER
SEQRES 7 D 199 GLN PRO SER ASP SER ALA THR TYR LEU CYS ALA VAL ASN
SEQRES 8 D 199 PHE GLY GLY GLY LYS LEU ILE PHE GLY GLN GLY THR GLU
SEQRES 9 D 199 LEU SER VAL LYS PRO ASN ILE GLN ASN PRO ASP PRO ALA
SEQRES 10 D 199 VAL TYR GLN LEU ARG ASP SER LYS SER SER ASP LYS SER
SEQRES 11 D 199 VAL CYS LEU PHE THR ASP PHE ASP SER GLN THR ASN VAL
SEQRES 12 D 199 SER GLN SER LYS ASP SER ASP VAL TYR ILE THR ASP LYS
SEQRES 13 D 199 CYS VAL LEU ASP MET ARG SER MET ASP PHE LYS SER ASN
SEQRES 14 D 199 SER ALA VAL ALA TRP SER ASN LYS SER ASP PHE ALA CYS
SEQRES 15 D 199 ALA ASN ALA PHE ASN ASN SER ILE ILE PRO GLU ASP THR
SEQRES 16 D 199 PHE PHE PRO SER
SEQRES 1 E 242 ILE ALA GLY ILE THR GLN ALA PRO THR SER GLN ILE LEU
SEQRES 2 E 242 ALA ALA GLY ARG ARG MET THR LEU ARG CYS THR GLN ASP
SEQRES 3 E 242 MET ARG HIS ASN ALA MET TYR TRP TYR ARG GLN ASP LEU
SEQRES 4 E 242 GLY LEU GLY LEU ARG LEU ILE HIS TYR SER ASN THR ALA
SEQRES 5 E 242 GLY THR THR GLY LYS GLY GLU VAL PRO ASP GLY TYR SER
SEQRES 6 E 242 VAL SER ARG ALA ASN THR ASP ASP PHE PRO LEU THR LEU
SEQRES 7 E 242 ALA SER ALA VAL PRO SER GLN THR SER VAL TYR PHE CYS
SEQRES 8 E 242 ALA SER SER TRP SER PHE GLY THR GLU ALA PHE PHE GLY
SEQRES 9 E 242 GLN GLY THR ARG LEU THR VAL VAL GLU ASP LEU ASN LYS
SEQRES 10 E 242 VAL PHE PRO PRO GLU VAL ALA VAL PHE GLU PRO SER GLU
SEQRES 11 E 242 ALA GLU ILE SER HIS THR GLN LYS ALA THR LEU VAL CYS
SEQRES 12 E 242 LEU ALA THR GLY PHE TYR PRO ASP HIS VAL GLU LEU SER
SEQRES 13 E 242 TRP TRP VAL ASN GLY LYS GLU VAL HIS SER GLY VAL CYS
SEQRES 14 E 242 THR ASP PRO GLN PRO LEU LYS GLU GLN PRO ALA LEU ASN
SEQRES 15 E 242 ASP SER ARG TYR ALA LEU SER SER ARG LEU ARG VAL SER
SEQRES 16 E 242 ALA THR PHE TRP GLN ASP PRO ARG ASN HIS PHE ARG CYS
SEQRES 17 E 242 GLN VAL GLN PHE TYR GLY LEU SER GLU ASN ASP GLU TRP
SEQRES 18 E 242 THR GLN ASP ARG ALA LYS PRO VAL THR GLN ILE VAL SER
SEQRES 19 E 242 ALA GLU ALA TRP GLY ARG ALA ASP
FORMUL 6 HOH *12(H2 O)
HELIX 1 1 ALA A 49 GLU A 53 5 5
HELIX 2 2 GLY A 56 TYR A 85 1 30
HELIX 3 3 ASP A 137 ALA A 150 1 14
HELIX 4 4 HIS A 151 GLY A 162 1 12
HELIX 5 5 GLY A 162 GLY A 175 1 14
HELIX 6 6 GLY A 175 GLN A 180 1 6
HELIX 7 7 GLN D 79 SER D 83 5 5
HELIX 8 8 VAL E 85 THR E 89 5 5
HELIX 9 9 ASP E 117 VAL E 121 5 5
HELIX 10 10 SER E 132 GLN E 140 1 9
HELIX 11 11 ALA E 199 ASP E 204 1 6
SHEET 1 A 8 GLU A 46 PRO A 47 0
SHEET 2 A 8 THR A 31 ASP A 37 -1 N ARG A 35 O GLU A 46
SHEET 3 A 8 ARG A 21 VAL A 28 -1 N ALA A 24 O PHE A 36
SHEET 4 A 8 HIS A 3 VAL A 12 -1 N ARG A 6 O TYR A 27
SHEET 5 A 8 THR A 94 VAL A 103 -1 O VAL A 95 N SER A 11
SHEET 6 A 8 PHE A 109 TYR A 118 -1 O LEU A 110 N ASP A 102
SHEET 7 A 8 LYS A 121 LEU A 126 -1 O TYR A 123 N TYR A 116
SHEET 8 A 8 TRP A 133 ALA A 135 -1 O THR A 134 N ALA A 125
SHEET 1 B 4 LYS A 186 ALA A 193 0
SHEET 2 B 4 GLU A 198 PHE A 208 -1 O THR A 200 N HIS A 192
SHEET 3 B 4 PHE A 241 PRO A 250 -1 O ALA A 245 N CYS A 203
SHEET 4 B 4 GLU A 229 LEU A 230 -1 N GLU A 229 O ALA A 246
SHEET 1 C 4 LYS A 186 ALA A 193 0
SHEET 2 C 4 GLU A 198 PHE A 208 -1 O THR A 200 N HIS A 192
SHEET 3 C 4 PHE A 241 PRO A 250 -1 O ALA A 245 N CYS A 203
SHEET 4 C 4 ARG A 234 PRO A 235 -1 N ARG A 234 O GLN A 242
SHEET 1 D 4 GLU A 222 ASP A 223 0
SHEET 2 D 4 THR A 214 ARG A 219 -1 N ARG A 219 O GLU A 222
SHEET 3 D 4 TYR A 257 GLN A 262 -1 O GLN A 262 N THR A 214
SHEET 4 D 4 LEU A 270 LEU A 272 -1 O LEU A 270 N VAL A 261
SHEET 1 E 4 LYS B 6 SER B 11 0
SHEET 2 E 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10
SHEET 3 E 4 PHE B 62 PHE B 70 -1 O TYR B 66 N CYS B 25
SHEET 4 E 4 GLU B 50 HIS B 51 -1 N GLU B 50 O TYR B 67
SHEET 1 F 4 LYS B 6 SER B 11 0
SHEET 2 F 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10
SHEET 3 F 4 PHE B 62 PHE B 70 -1 O TYR B 66 N CYS B 25
SHEET 4 F 4 SER B 55 PHE B 56 -1 N SER B 55 O TYR B 63
SHEET 1 G 4 GLU B 44 ARG B 45 0
SHEET 2 G 4 ILE B 35 LYS B 41 -1 N LYS B 41 O GLU B 44
SHEET 3 G 4 TYR B 78 HIS B 84 -1 O ALA B 79 N LEU B 40
SHEET 4 G 4 LYS B 91 LYS B 94 -1 O LYS B 91 N VAL B 82
SHEET 1 H 5 VAL D 3 GLN D 5 0
SHEET 2 H 5 ALA D 18 TYR D 24 -1 O THR D 23 N GLU D 4
SHEET 3 H 5 TYR D 70 ILE D 75 -1 O LEU D 73 N LEU D 20
SHEET 4 H 5 PHE D 60 ASN D 65 -1 N ASN D 65 O TYR D 70
SHEET 5 H 5 GLY D 53 ASP D 57 -1 N ASP D 57 O PHE D 60
SHEET 1 I 5 LEU D 10 PRO D 13 0
SHEET 2 I 5 THR D 103 LYS D 108 1 O GLU D 104 N LEU D 10
SHEET 3 I 5 THR D 85 ASN D 91 -1 N TYR D 86 O THR D 103
SHEET 4 I 5 PHE D 32 GLN D 37 -1 N PHE D 33 O ALA D 89
SHEET 5 I 5 GLU D 44 ILE D 49 -1 O ILE D 46 N TRP D 34
SHEET 1 J 4 LEU D 10 PRO D 13 0
SHEET 2 J 4 THR D 103 LYS D 108 1 O GLU D 104 N LEU D 10
SHEET 3 J 4 THR D 85 ASN D 91 -1 N TYR D 86 O THR D 103
SHEET 4 J 4 LEU D 97 PHE D 99 -1 O ILE D 98 N VAL D 90
SHEET 1 K 3 TYR D 152 ILE D 153 0
SHEET 2 K 3 PHE D 166 TRP D 174 -1 O TRP D 174 N TYR D 152
SHEET 3 K 3 CYS D 157 MET D 161 -1 N LEU D 159 O SER D 168
SHEET 1 L 8 TYR D 152 ILE D 153 0
SHEET 2 L 8 PHE D 166 TRP D 174 -1 O TRP D 174 N TYR D 152
SHEET 3 L 8 VAL D 131 THR D 135 -1 N CYS D 132 O ALA D 173
SHEET 4 L 8 ALA D 117 ASP D 123 -1 N ALA D 117 O THR D 135
SHEET 5 L 8 GLU E 125 GLU E 130 -1 O GLU E 130 N ARG D 122
SHEET 6 L 8 LYS E 141 PHE E 151 -1 O THR E 149 N GLU E 125
SHEET 7 L 8 TYR E 189 SER E 198 -1 O LEU E 191 N ALA E 148
SHEET 8 L 8 VAL E 171 THR E 173 -1 N CYS E 172 O ARG E 194
SHEET 1 M 4 ILE E 7 ALA E 10 0
SHEET 2 M 4 MET E 22 GLN E 28 -1 O THR E 27 N THR E 8
SHEET 3 M 4 LEU E 79 LEU E 81 -1 O LEU E 79 N LEU E 24
SHEET 4 M 4 TYR E 67 VAL E 69 -1 N SER E 68 O THR E 80
SHEET 1 N 6 SER E 13 ALA E 17 0
SHEET 2 N 6 THR E 110 VAL E 115 1 O VAL E 115 N LEU E 16
SHEET 3 N 6 SER E 90 SER E 97 -1 N TYR E 92 O THR E 110
SHEET 4 N 6 ALA E 34 GLN E 40 -1 N ALA E 34 O SER E 97
SHEET 5 N 6 LEU E 46 SER E 52 -1 O ILE E 49 N TRP E 37
SHEET 6 N 6 GLY E 59 LYS E 60 -1 O GLY E 59 N TYR E 51
SHEET 1 O 4 SER E 13 ALA E 17 0
SHEET 2 O 4 THR E 110 VAL E 115 1 O VAL E 115 N LEU E 16
SHEET 3 O 4 SER E 90 SER E 97 -1 N TYR E 92 O THR E 110
SHEET 4 O 4 PHE E 105 PHE E 106 -1 O PHE E 105 N SER E 96
SHEET 1 P 4 LYS E 165 VAL E 167 0
SHEET 2 P 4 VAL E 156 VAL E 162 -1 N VAL E 162 O LYS E 165
SHEET 3 P 4 HIS E 208 PHE E 215 -1 O GLN E 214 N GLU E 157
SHEET 4 P 4 GLN E 234 TRP E 241 -1 O GLN E 234 N PHE E 215
SSBOND 1 CYS A 101 CYS A 164 1555 1555 2.05
SSBOND 2 CYS A 203 CYS A 259 1555 1555 2.04
SSBOND 3 CYS B 25 CYS B 80 1555 1555 2.03
SSBOND 4 CYS D 22 CYS D 88 1555 1555 2.04
SSBOND 5 CYS D 157 CYS E 172 1555 1555 2.10
SSBOND 6 CYS E 26 CYS E 94 1555 1555 2.03
SSBOND 7 CYS E 146 CYS E 211 1555 1555 2.01
CISPEP 1 TYR A 209 PRO A 210 0 -0.11
CISPEP 2 HIS B 31 PRO B 32 0 -0.25
CISPEP 3 GLY D 8 PRO D 9 0 -2.84
CISPEP 4 ALA E 10 PRO E 11 0 -1.57
CISPEP 5 TYR E 152 PRO E 153 0 0.23
CRYST1 227.040 49.316 92.894 90.00 94.82 90.00 C 1 2 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.004405 0.000000 0.000371 0.00000
SCALE2 0.000000 0.020277 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010803 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
