HEADER IMMUNE SYSTEM 25-JUN-12 4FQX
TITLE CRYSTAL STRUCTURE OF HLA-DM BOUND TO HLA-DR1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DM ALPHA CHAIN;
COMPND 3 CHAIN: C;
COMPND 4 FRAGMENT: UNP RESIDUES 27-225;
COMPND 5 SYNONYM: MHC CLASS II ANTIGEN DMA, REALLY INTERESTING NEW GENE 6
COMPND 6 PROTEIN;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DM BETA CHAIN;
COMPND 10 CHAIN: D;
COMPND 11 FRAGMENT: UNP RESIDUES 19-211;
COMPND 12 SYNONYM: MHC CLASS II ANTIGEN DMB, REALLY INTERESTING NEW GENE 7
COMPND 13 PROTEIN;
COMPND 14 ENGINEERED: YES;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: SYNTHETIC PEPTIDE;
COMPND 17 CHAIN: E;
COMPND 18 ENGINEERED: YES;
COMPND 19 MOL_ID: 4;
COMPND 20 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN;
COMPND 21 CHAIN: A;
COMPND 22 FRAGMENT: UNP RESIDUES 26-216;
COMPND 23 SYNONYM: MHC CLASS II ANTIGEN DRA;
COMPND 24 ENGINEERED: YES;
COMPND 25 MOL_ID: 5;
COMPND 26 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DRB1-1 BETA CHAIN;
COMPND 27 CHAIN: B;
COMPND 28 FRAGMENT: UNP RESIDUES 30-221;
COMPND 29 SYNONYM: MHC CLASS II ANTIGEN DRB1*1, DR-1, DR1;
COMPND 30 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: DM ALPHA CHAIN, DMA, HLA CLASS II HISTOCOMPATIBILITY ANTIGEN,
SOURCE 6 HLA-DMA, RING6;
SOURCE 7 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: LEC3.2.8.1;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PEE14.1;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606;
SOURCE 16 GENE: DM BETA CHAIN, DMB, HLA CLASS II HISTOCOMPATIBILITY ANTIGEN,
SOURCE 17 HLA-DMB, RING7;
SOURCE 18 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 20 EXPRESSION_SYSTEM_STRAIN: LEC3.2.8.1;
SOURCE 21 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 22 EXPRESSION_SYSTEM_PLASMID: PEE14.1;
SOURCE 23 MOL_ID: 3;
SOURCE 24 SYNTHETIC: YES;
SOURCE 25 MOL_ID: 4;
SOURCE 26 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 27 ORGANISM_COMMON: HUMAN;
SOURCE 28 ORGANISM_TAXID: 9606;
SOURCE 29 GENE: HLA-DR1 ALPHA CHAIN, HLA-DRA, HLA-DRA1, MHC CLASS II MOLECULE;
SOURCE 30 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 31 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 32 MOL_ID: 5;
SOURCE 33 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 34 ORGANISM_COMMON: HUMAN;
SOURCE 35 ORGANISM_TAXID: 9606;
SOURCE 36 GENE: BETA CHAIN, HLA-DR1, HLA-DRB1, MHC CLASS II MOLECULE;
SOURCE 37 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 38 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS IMMUNE COMPLEX, PEPTIDE LOADING, PEPTIDE EDITING, ANTIGEN
KEYWDS 2 PRESENTATION, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR D.K.SETHI,W.POS,K.W.WUCHERPFENNIG
REVDAT 3 29-JUL-20 4FQX 1 COMPND REMARK SEQADV HETNAM
REVDAT 3 2 1 LINK SITE ATOM
REVDAT 2 15-NOV-17 4FQX 1 REMARK
REVDAT 1 09-JAN-13 4FQX 0
JRNL AUTH W.POS,D.K.SETHI,M.J.CALL,M.S.SCHULZE,A.K.ANDERS,J.PYRDOL,
JRNL AUTH 2 K.W.WUCHERPFENNIG
JRNL TITL CRYSTAL STRUCTURE OF THE HLA-DM-HLA-DR1 COMPLEX DEFINES
JRNL TITL 2 MECHANISMS FOR RAPID PEPTIDE SELECTION.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 151 1557 2012
JRNL REFN ISSN 0092-8674
JRNL PMID 23260142
JRNL DOI 10.1016/J.CELL.2012.11.025
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8_1069
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.14
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 34135
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1742
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 36.1448 - 5.9424 0.94 2805 143 0.1855 0.2139
REMARK 3 2 5.9424 - 4.7200 0.96 2717 166 0.1541 0.1946
REMARK 3 3 4.7200 - 4.1243 0.97 2707 150 0.1455 0.1797
REMARK 3 4 4.1243 - 3.7477 0.98 2720 142 0.1789 0.2447
REMARK 3 5 3.7477 - 3.4793 0.98 2696 140 0.1911 0.2427
REMARK 3 6 3.4793 - 3.2743 0.98 2748 139 0.2098 0.2544
REMARK 3 7 3.2743 - 3.1104 0.98 2714 144 0.2335 0.2816
REMARK 3 8 3.1104 - 2.9751 0.98 2700 144 0.2549 0.3030
REMARK 3 9 2.9751 - 2.8606 0.98 2712 142 0.2611 0.3329
REMARK 3 10 2.8606 - 2.7619 0.99 2674 154 0.2619 0.3394
REMARK 3 11 2.7619 - 2.6756 0.98 2691 154 0.2630 0.3312
REMARK 3 12 2.6756 - 2.5991 0.92 2509 124 0.2639 0.3240
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.330
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.930
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 63.91
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 6263
REMARK 3 ANGLE : 1.188 8530
REMARK 3 CHIRALITY : 0.079 928
REMARK 3 PLANARITY : 0.006 1109
REMARK 3 DIHEDRAL : 15.957 2252
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 18
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN C AND RESID 15:137 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.6200 8.4382 -12.9916
REMARK 3 T TENSOR
REMARK 3 T11: 0.7234 T22: 0.3916
REMARK 3 T33: 0.5557 T12: -0.6064
REMARK 3 T13: -0.2811 T23: 0.1957
REMARK 3 L TENSOR
REMARK 3 L11: 0.3078 L22: 0.2424
REMARK 3 L33: 0.4352 L12: 0.2333
REMARK 3 L13: -0.0588 L23: -0.1637
REMARK 3 S TENSOR
REMARK 3 S11: -0.3899 S12: 0.1404 S13: 0.2782
REMARK 3 S21: 0.0321 S22: -0.2790 S23: -0.2093
REMARK 3 S31: -0.9460 S32: 0.5463 S33: -0.3460
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN C AND RESID 138:147 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.2837 -7.8231 -27.2399
REMARK 3 T TENSOR
REMARK 3 T11: 0.4759 T22: 0.9878
REMARK 3 T33: 0.9446 T12: -0.2702
REMARK 3 T13: 0.0715 T23: 0.0277
REMARK 3 L TENSOR
REMARK 3 L11: 0.0175 L22: 0.0052
REMARK 3 L33: -0.0019 L12: -0.0025
REMARK 3 L13: -0.0124 L23: 0.0055
REMARK 3 S TENSOR
REMARK 3 S11: 0.0551 S12: 0.1532 S13: -0.0389
REMARK 3 S21: -0.0194 S22: 0.0152 S23: 0.0212
REMARK 3 S31: 0.0291 S32: 0.1059 S33: 0.0026
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ( CHAIN C AND RESID 148:200 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.6157 -4.9859 -23.9651
REMARK 3 T TENSOR
REMARK 3 T11: 0.4184 T22: 0.5326
REMARK 3 T33: 0.4144 T12: -0.1360
REMARK 3 T13: -0.0055 T23: 0.1140
REMARK 3 L TENSOR
REMARK 3 L11: 0.1097 L22: 0.0735
REMARK 3 L33: 0.3766 L12: -0.0718
REMARK 3 L13: 0.0804 L23: 0.0224
REMARK 3 S TENSOR
REMARK 3 S11: -0.1694 S12: 0.2642 S13: 0.1687
REMARK 3 S21: 0.0270 S22: -0.1123 S23: -0.2596
REMARK 3 S31: -0.4956 S32: 0.2481 S33: -0.2086
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: ( CHAIN D AND RESID 3:133 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.1527 14.2929 -13.2402
REMARK 3 T TENSOR
REMARK 3 T11: 1.1966 T22: 0.1094
REMARK 3 T33: 0.5380 T12: 0.0147
REMARK 3 T13: -0.3621 T23: 0.1129
REMARK 3 L TENSOR
REMARK 3 L11: 0.3137 L22: 0.4312
REMARK 3 L33: 0.2542 L12: 0.1030
REMARK 3 L13: -0.2064 L23: -0.2320
REMARK 3 S TENSOR
REMARK 3 S11: -0.3348 S12: 0.1020 S13: 0.2563
REMARK 3 S21: 0.1428 S22: -0.0685 S23: 0.0595
REMARK 3 S31: -0.8394 S32: -0.2896 S33: -0.1659
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: ( CHAIN D AND RESID 134:157 )
REMARK 3 ORIGIN FOR THE GROUP (A): -27.4693 3.6563 -30.9583
REMARK 3 T TENSOR
REMARK 3 T11: 0.6531 T22: 0.4677
REMARK 3 T33: 0.5298 T12: -0.0558
REMARK 3 T13: -0.1470 T23: 0.1089
REMARK 3 L TENSOR
REMARK 3 L11: 0.0320 L22: 0.0453
REMARK 3 L33: 0.0209 L12: -0.0496
REMARK 3 L13: -0.0337 L23: 0.0403
REMARK 3 S TENSOR
REMARK 3 S11: 0.1294 S12: -0.0058 S13: -0.0485
REMARK 3 S21: -0.1113 S22: -0.2038 S23: 0.2393
REMARK 3 S31: -0.2445 S32: 0.0920 S33: 0.0002
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: ( CHAIN D AND RESID 158:193 )
REMARK 3 ORIGIN FOR THE GROUP (A): -30.6600 2.0788 -43.6638
REMARK 3 T TENSOR
REMARK 3 T11: 0.9649 T22: 0.4445
REMARK 3 T33: 0.4366 T12: -0.1889
REMARK 3 T13: -0.2859 T23: 0.1994
REMARK 3 L TENSOR
REMARK 3 L11: 0.5788 L22: 0.0837
REMARK 3 L33: 0.3230 L12: -0.1952
REMARK 3 L13: -0.4418 L23: 0.1519
REMARK 3 S TENSOR
REMARK 3 S11: -0.3924 S12: 0.3025 S13: -0.0355
REMARK 3 S21: -0.0293 S22: -0.3865 S23: -0.0619
REMARK 3 S31: -0.2515 S32: -0.5354 S33: -0.1850
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: ( CHAIN E AND RESID 87:93 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.6457 -11.6481 23.1359
REMARK 3 T TENSOR
REMARK 3 T11: 0.5087 T22: 0.5078
REMARK 3 T33: 0.6470 T12: -0.0387
REMARK 3 T13: -0.0301 T23: -0.1008
REMARK 3 L TENSOR
REMARK 3 L11: 0.0043 L22: 0.0149
REMARK 3 L33: 0.0075 L12: 0.0001
REMARK 3 L13: 0.0062 L23: -0.0036
REMARK 3 S TENSOR
REMARK 3 S11: 0.1870 S12: -0.0532 S13: 0.1357
REMARK 3 S21: -0.0193 S22: -0.0328 S23: -0.0876
REMARK 3 S31: -0.0283 S32: -0.0911 S33: 0.0006
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: ( CHAIN A AND RESID 2:45 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.3604 -12.2209 2.4233
REMARK 3 T TENSOR
REMARK 3 T11: 0.2640 T22: 0.3435
REMARK 3 T33: 0.3424 T12: 0.0074
REMARK 3 T13: -0.0269 T23: 0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 0.0019 L22: 0.0434
REMARK 3 L33: 0.0886 L12: -0.0124
REMARK 3 L13: 0.0086 L23: -0.0140
REMARK 3 S TENSOR
REMARK 3 S11: -0.1127 S12: -0.1049 S13: 0.0480
REMARK 3 S21: 0.1202 S22: -0.0153 S23: -0.0043
REMARK 3 S31: -0.2684 S32: 0.0467 S33: 0.0000
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: ( CHAIN A AND RESID 46:76 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.8755 -9.4083 10.2287
REMARK 3 T TENSOR
REMARK 3 T11: 0.4703 T22: 0.4307
REMARK 3 T33: 0.3632 T12: 0.0051
REMARK 3 T13: -0.0550 T23: -0.0149
REMARK 3 L TENSOR
REMARK 3 L11: 0.0691 L22: 0.0267
REMARK 3 L33: 0.0231 L12: 0.0026
REMARK 3 L13: -0.0228 L23: 0.0180
REMARK 3 S TENSOR
REMARK 3 S11: 0.0491 S12: -0.1471 S13: 0.1605
REMARK 3 S21: 0.0017 S22: -0.0232 S23: 0.1635
REMARK 3 S31: -0.4029 S32: -0.0065 S33: -0.0000
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: ( CHAIN A AND RESID 77:101 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.0661 -26.9340 -6.9073
REMARK 3 T TENSOR
REMARK 3 T11: 0.3118 T22: 0.3416
REMARK 3 T33: 0.3466 T12: 0.0024
REMARK 3 T13: -0.0058 T23: 0.0154
REMARK 3 L TENSOR
REMARK 3 L11: 0.1797 L22: 0.0299
REMARK 3 L33: 0.0451 L12: 0.0538
REMARK 3 L13: -0.0153 L23: 0.0365
REMARK 3 S TENSOR
REMARK 3 S11: -0.0770 S12: 0.1986 S13: -0.0386
REMARK 3 S21: -0.0425 S22: -0.0376 S23: -0.0087
REMARK 3 S31: 0.0664 S32: 0.0286 S33: 0.0001
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: ( CHAIN A AND RESID 102:154 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.3665 -22.5874 -8.1483
REMARK 3 T TENSOR
REMARK 3 T11: 0.2496 T22: 0.3337
REMARK 3 T33: 0.3221 T12: -0.0086
REMARK 3 T13: -0.0091 T23: 0.0132
REMARK 3 L TENSOR
REMARK 3 L11: 0.0606 L22: 0.0625
REMARK 3 L33: 0.0671 L12: -0.0613
REMARK 3 L13: 0.0432 L23: -0.0116
REMARK 3 S TENSOR
REMARK 3 S11: 0.1008 S12: 0.2278 S13: -0.0013
REMARK 3 S21: -0.0189 S22: -0.0555 S23: 0.0935
REMARK 3 S31: -0.1125 S32: -0.1026 S33: 0.0000
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: ( CHAIN A AND RESID 155:181 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.8362 -31.3782 -13.7832
REMARK 3 T TENSOR
REMARK 3 T11: 0.4112 T22: 0.4241
REMARK 3 T33: 0.4473 T12: 0.0650
REMARK 3 T13: 0.0069 T23: 0.0245
REMARK 3 L TENSOR
REMARK 3 L11: 0.0722 L22: 0.1059
REMARK 3 L33: 0.0129 L12: 0.0057
REMARK 3 L13: 0.0265 L23: 0.0053
REMARK 3 S TENSOR
REMARK 3 S11: -0.0753 S12: 0.0891 S13: -0.1977
REMARK 3 S21: 0.0752 S22: -0.1009 S23: -0.0054
REMARK 3 S31: 0.3019 S32: 0.1355 S33: -0.0003
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: ( CHAIN B AND RESID -5:17 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.0410 -25.0367 10.7711
REMARK 3 T TENSOR
REMARK 3 T11: 0.2198 T22: 0.3927
REMARK 3 T33: 0.2835 T12: 0.0607
REMARK 3 T13: -0.0277 T23: 0.0452
REMARK 3 L TENSOR
REMARK 3 L11: 0.0169 L22: 0.0040
REMARK 3 L33: 0.0438 L12: -0.0218
REMARK 3 L13: -0.0118 L23: -0.0511
REMARK 3 S TENSOR
REMARK 3 S11: 0.1264 S12: -0.0054 S13: 0.1471
REMARK 3 S21: -0.1808 S22: -0.0320 S23: 0.0634
REMARK 3 S31: 0.0864 S32: -0.1138 S33: 0.0003
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: ( CHAIN B AND RESID 18:84 )
REMARK 3 ORIGIN FOR THE GROUP (A): -37.7612 -12.4817 14.4692
REMARK 3 T TENSOR
REMARK 3 T11: 0.2653 T22: 0.4028
REMARK 3 T33: 0.3886 T12: 0.1386
REMARK 3 T13: 0.0188 T23: -0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 0.1372 L22: 0.1989
REMARK 3 L33: 0.1419 L12: 0.1184
REMARK 3 L13: 0.0647 L23: 0.0384
REMARK 3 S TENSOR
REMARK 3 S11: 0.1022 S12: -0.0536 S13: 0.1929
REMARK 3 S21: 0.1788 S22: -0.0567 S23: -0.0772
REMARK 3 S31: -0.1003 S32: -0.3849 S33: 0.0041
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: ( CHAIN B AND RESID 85:97 )
REMARK 3 ORIGIN FOR THE GROUP (A): -34.0170 -4.6354 -12.0245
REMARK 3 T TENSOR
REMARK 3 T11: 0.2624 T22: 0.2274
REMARK 3 T33: 0.5071 T12: 0.0616
REMARK 3 T13: -0.0035 T23: 0.1127
REMARK 3 L TENSOR
REMARK 3 L11: 0.2695 L22: 0.1374
REMARK 3 L33: 0.1088 L12: 0.1834
REMARK 3 L13: -0.1693 L23: -0.1181
REMARK 3 S TENSOR
REMARK 3 S11: -0.1417 S12: 0.2438 S13: -0.0714
REMARK 3 S21: -0.2025 S22: -0.0448 S23: -0.0276
REMARK 3 S31: 0.0042 S32: -0.0974 S33: -0.0118
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: ( CHAIN B AND RESID 98:144 )
REMARK 3 ORIGIN FOR THE GROUP (A): -38.4544 -23.5370 -26.0701
REMARK 3 T TENSOR
REMARK 3 T11: 0.2540 T22: 0.3079
REMARK 3 T33: 0.2637 T12: -0.0666
REMARK 3 T13: -0.0257 T23: 0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 0.0679 L22: 0.0820
REMARK 3 L33: 0.0611 L12: 0.0089
REMARK 3 L13: 0.0174 L23: -0.0736
REMARK 3 S TENSOR
REMARK 3 S11: -0.2140 S12: 0.1602 S13: 0.1141
REMARK 3 S21: 0.0103 S22: 0.1641 S23: 0.0296
REMARK 3 S31: -0.1654 S32: -0.0466 S33: 0.0000
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: ( CHAIN B AND RESID 145:170 )
REMARK 3 ORIGIN FOR THE GROUP (A): -33.9992 -24.8818 -23.4770
REMARK 3 T TENSOR
REMARK 3 T11: 0.4172 T22: 0.3090
REMARK 3 T33: 0.3803 T12: -0.0449
REMARK 3 T13: -0.0052 T23: 0.0170
REMARK 3 L TENSOR
REMARK 3 L11: 0.1290 L22: 0.1088
REMARK 3 L33: 0.0781 L12: -0.0556
REMARK 3 L13: -0.0854 L23: -0.0454
REMARK 3 S TENSOR
REMARK 3 S11: -0.0297 S12: -0.0419 S13: 0.0473
REMARK 3 S21: -0.2784 S22: 0.0948 S23: -0.1856
REMARK 3 S31: 0.0853 S32: 0.0644 S33: 0.0000
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: ( CHAIN B AND RESID 171:190 )
REMARK 3 ORIGIN FOR THE GROUP (A): -39.5034 -17.5744 -30.1457
REMARK 3 T TENSOR
REMARK 3 T11: 0.4012 T22: 0.4736
REMARK 3 T33: 0.4154 T12: -0.0083
REMARK 3 T13: -0.0498 T23: 0.0656
REMARK 3 L TENSOR
REMARK 3 L11: 0.0103 L22: 0.0415
REMARK 3 L33: 0.0386 L12: -0.0004
REMARK 3 L13: 0.0325 L23: -0.0251
REMARK 3 S TENSOR
REMARK 3 S11: -0.1842 S12: 0.4443 S13: 0.1161
REMARK 3 S21: -0.2934 S22: -0.0445 S23: 0.1303
REMARK 3 S31: 0.0918 S32: -0.0992 S33: 0.0000
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4FQX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUL-12.
REMARK 100 THE DEPOSITION ID IS D_1000073243.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-APR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-E
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34280
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.05900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.53300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 33.09500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.20800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 60.82450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 69.20800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.09500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 60.82450
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -68.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, E, A, B, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6460 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, A, B, 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 VAL C 1
REMARK 465 PRO C 2
REMARK 465 GLU C 3
REMARK 465 ALA C 4
REMARK 465 PRO C 5
REMARK 465 THR C 6
REMARK 465 PRO C 7
REMARK 465 MET C 8
REMARK 465 TRP C 9
REMARK 465 PRO C 10
REMARK 465 ASP C 11
REMARK 465 ASP C 12
REMARK 465 LEU C 13
REMARK 465 GLN C 14
REMARK 465 VAL C 201
REMARK 465 PRO C 202
REMARK 465 ARG C 203
REMARK 465 GLY D 1
REMARK 465 GLY D 2
REMARK 465 GLY D 194
REMARK 465 CYS D 195
REMARK 465 LEU D 196
REMARK 465 VAL D 197
REMARK 465 PRO D 198
REMARK 465 ARG D 199
REMARK 465 GLY E 84
REMARK 465 LYS E 85
REMARK 465 GLN E 86
REMARK 465 LYS E 94
REMARK 465 ILE A 1
REMARK 465 ALA A 182
REMARK 465 PRO A 183
REMARK 465 SER A 184
REMARK 465 PRO A 185
REMARK 465 LEU A 186
REMARK 465 PRO A 187
REMARK 465 GLU A 188
REMARK 465 THR A 189
REMARK 465 THR A 190
REMARK 465 GLU A 191
REMARK 465 LYS B 105
REMARK 465 THR B 106
REMARK 465 GLN B 107
REMARK 465 PRO B 108
REMARK 465 LEU B 109
REMARK 465 GLN B 110
REMARK 465 HIS B 111
REMARK 465 HIS B 112
REMARK 465 ASN B 113
REMARK 465 ARG B 191
REMARK 465 SER B 192
REMARK 465 SER B 193
REMARK 465 GLY B 194
REMARK 465 GLY B 195
REMARK 465 GLY B 196
REMARK 465 SER B 197
REMARK 465 LEU B 198
REMARK 465 PRO B 199
REMARK 465 ALA B 200
REMARK 465 THR B 201
REMARK 465 GLY B 202
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 PHE C 145 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 141 CG CD OE1 OE2
REMARK 470 LYS B 65 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NH1 ARG D 110 OE2 GLU B 187 2.10
REMARK 500 ND2 ASN A 118 O5 NAG F 1 2.17
REMARK 500 O GLN D 70 ND2 ASN D 74 2.18
REMARK 500 OE2 GLU C 181 NH1 ARG C 184 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN C 50 36.32 38.27
REMARK 500 PHE C 127 117.43 -175.36
REMARK 500 GLU C 143 -64.48 -25.62
REMARK 500 ASP C 183 19.55 -153.13
REMARK 500 LEU D 13 -159.76 -86.51
REMARK 500 ASP D 21 173.19 177.79
REMARK 500 LYS D 30 -0.91 68.70
REMARK 500 GLN D 84 -46.28 -140.25
REMARK 500 PRO D 124 -170.55 -69.49
REMARK 500 HIS D 145 74.08 44.25
REMARK 500 ASP B 2 75.64 64.96
REMARK 500 ASN B 19 76.09 48.29
REMARK 500 ASN B 33 -101.47 51.00
REMARK 500 TYR B 78 -63.50 -105.68
REMARK 500 THR B 90 -151.03 -71.22
REMARK 500 PRO B 165 150.35 -48.11
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4FQX C 1 199 UNP P28067 DMA_HUMAN 27 225
DBREF 4FQX D 1 193 UNP P28068 DMB_HUMAN 19 211
DBREF 4FQX A 1 191 UNP P01903 DRA_HUMAN 26 216
DBREF 4FQX B 1 192 UNP P04229 2B11_HUMAN 30 221
DBREF 4FQX E 84 94 PDB 4FQX 4FQX 84 94
SEQADV 4FQX GLN C 136 UNP P28067 HIS 162 VARIANT
SEQADV 4FQX HIS C 137 UNP P28067 ASP 163 VARIANT
SEQADV 4FQX ASP C 165 UNP P28067 ASN 191 ENGINEERED MUTATION
SEQADV 4FQX LEU C 200 UNP P28067 EXPRESSION TAG
SEQADV 4FQX VAL C 201 UNP P28067 EXPRESSION TAG
SEQADV 4FQX PRO C 202 UNP P28067 EXPRESSION TAG
SEQADV 4FQX ARG C 203 UNP P28067 EXPRESSION TAG
SEQADV 4FQX SER D 46 UNP P28068 CYS 64 ENGINEERED MUTATION
SEQADV 4FQX ASP D 92 UNP P28068 ASN 110 ENGINEERED MUTATION
SEQADV 4FQX GLY D 194 UNP P28068 EXPRESSION TAG
SEQADV 4FQX CYS D 195 UNP P28068 EXPRESSION TAG
SEQADV 4FQX LEU D 196 UNP P28068 EXPRESSION TAG
SEQADV 4FQX VAL D 197 UNP P28068 EXPRESSION TAG
SEQADV 4FQX PRO D 198 UNP P28068 EXPRESSION TAG
SEQADV 4FQX ARG D 199 UNP P28068 EXPRESSION TAG
SEQADV 4FQX CYS A 65 UNP P01903 VAL 90 ENGINEERED MUTATION
SEQADV 4FQX VAL B -5 UNP P04229 EXPRESSION TAG
SEQADV 4FQX LEU B -4 UNP P04229 EXPRESSION TAG
SEQADV 4FQX PHE B -3 UNP P04229 EXPRESSION TAG
SEQADV 4FQX GLN B -2 UNP P04229 EXPRESSION TAG
SEQADV 4FQX GLY B -1 UNP P04229 EXPRESSION TAG
SEQADV 4FQX PRO B 0 UNP P04229 EXPRESSION TAG
SEQADV 4FQX SER B 30 UNP P04229 CYS 59 ENGINEERED MUTATION
SEQADV 4FQX SER B 193 UNP P04229 EXPRESSION TAG
SEQADV 4FQX GLY B 194 UNP P04229 EXPRESSION TAG
SEQADV 4FQX GLY B 195 UNP P04229 EXPRESSION TAG
SEQADV 4FQX GLY B 196 UNP P04229 EXPRESSION TAG
SEQADV 4FQX SER B 197 UNP P04229 EXPRESSION TAG
SEQADV 4FQX LEU B 198 UNP P04229 EXPRESSION TAG
SEQADV 4FQX PRO B 199 UNP P04229 EXPRESSION TAG
SEQADV 4FQX ALA B 200 UNP P04229 EXPRESSION TAG
SEQADV 4FQX THR B 201 UNP P04229 EXPRESSION TAG
SEQADV 4FQX GLY B 202 UNP P04229 EXPRESSION TAG
SEQRES 1 C 203 VAL PRO GLU ALA PRO THR PRO MET TRP PRO ASP ASP LEU
SEQRES 2 C 203 GLN ASN HIS THR PHE LEU HIS THR VAL TYR CYS GLN ASP
SEQRES 3 C 203 GLY SER PRO SER VAL GLY LEU SER GLU ALA TYR ASP GLU
SEQRES 4 C 203 ASP GLN LEU PHE PHE PHE ASP PHE SER GLN ASN THR ARG
SEQRES 5 C 203 VAL PRO ARG LEU PRO GLU PHE ALA ASP TRP ALA GLN GLU
SEQRES 6 C 203 GLN GLY ASP ALA PRO ALA ILE LEU PHE ASP LYS GLU PHE
SEQRES 7 C 203 CYS GLU TRP MET ILE GLN GLN ILE GLY PRO LYS LEU ASP
SEQRES 8 C 203 GLY LYS ILE PRO VAL SER ARG GLY PHE PRO ILE ALA GLU
SEQRES 9 C 203 VAL PHE THR LEU LYS PRO LEU GLU PHE GLY LYS PRO ASN
SEQRES 10 C 203 THR LEU VAL CYS PHE VAL SER ASN LEU PHE PRO PRO MET
SEQRES 11 C 203 LEU THR VAL ASN TRP GLN HIS HIS SER VAL PRO VAL GLU
SEQRES 12 C 203 GLY PHE GLY PRO THR PHE VAL SER ALA VAL ASP GLY LEU
SEQRES 13 C 203 SER PHE GLN ALA PHE SER TYR LEU ASP PHE THR PRO GLU
SEQRES 14 C 203 PRO SER ASP ILE PHE SER CYS ILE VAL THR HIS GLU ILE
SEQRES 15 C 203 ASP ARG TYR THR ALA ILE ALA TYR TRP VAL PRO ARG ASN
SEQRES 16 C 203 ALA LEU PRO SER LEU VAL PRO ARG
SEQRES 1 D 199 GLY GLY PHE VAL ALA HIS VAL GLU SER THR CYS LEU LEU
SEQRES 2 D 199 ASP ASP ALA GLY THR PRO LYS ASP PHE THR TYR CYS ILE
SEQRES 3 D 199 SER PHE ASN LYS ASP LEU LEU THR CYS TRP ASP PRO GLU
SEQRES 4 D 199 GLU ASN LYS MET ALA PRO SER GLU PHE GLY VAL LEU ASN
SEQRES 5 D 199 SER LEU ALA ASN VAL LEU SER GLN HIS LEU ASN GLN LYS
SEQRES 6 D 199 ASP THR LEU MET GLN ARG LEU ARG ASN GLY LEU GLN ASN
SEQRES 7 D 199 CYS ALA THR HIS THR GLN PRO PHE TRP GLY SER LEU THR
SEQRES 8 D 199 ASP ARG THR ARG PRO PRO SER VAL GLN VAL ALA LYS THR
SEQRES 9 D 199 THR PRO PHE ASN THR ARG GLU PRO VAL MET LEU ALA CYS
SEQRES 10 D 199 TYR VAL TRP GLY PHE TYR PRO ALA GLU VAL THR ILE THR
SEQRES 11 D 199 TRP ARG LYS ASN GLY LYS LEU VAL MET PRO HIS SER SER
SEQRES 12 D 199 ALA HIS LYS THR ALA GLN PRO ASN GLY ASP TRP THR TYR
SEQRES 13 D 199 GLN THR LEU SER HIS LEU ALA LEU THR PRO SER TYR GLY
SEQRES 14 D 199 ASP THR TYR THR CYS VAL VAL GLU HIS ILE GLY ALA PRO
SEQRES 15 D 199 GLU PRO ILE LEU ARG ASP TRP THR PRO GLY LEU GLY CYS
SEQRES 16 D 199 LEU VAL PRO ARG
SEQRES 1 E 11 GLY LYS GLN ASN CYS LEU LYS LEU ALA THR LYS
SEQRES 1 A 191 ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR
SEQRES 2 A 191 LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE
SEQRES 3 A 191 ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS
SEQRES 4 A 191 GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA
SEQRES 5 A 191 SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA CYS
SEQRES 6 A 191 ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN
SEQRES 7 A 191 TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL
SEQRES 8 A 191 LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL
SEQRES 9 A 191 LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL
SEQRES 10 A 191 ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR
SEQRES 11 A 191 GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS
SEQRES 12 A 191 LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER
SEQRES 13 A 191 THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES 14 A 191 LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP ALA
SEQRES 15 A 191 PRO SER PRO LEU PRO GLU THR THR GLU
SEQRES 1 B 208 VAL LEU PHE GLN GLY PRO GLY ASP THR ARG PRO ARG PHE
SEQRES 2 B 208 LEU TRP GLN LEU LYS PHE GLU CYS HIS PHE PHE ASN GLY
SEQRES 3 B 208 THR GLU ARG VAL ARG LEU LEU GLU ARG SER ILE TYR ASN
SEQRES 4 B 208 GLN GLU GLU SER VAL ARG PHE ASP SER ASP VAL GLY GLU
SEQRES 5 B 208 TYR ARG ALA VAL THR GLU LEU GLY ARG PRO ASP ALA GLU
SEQRES 6 B 208 TYR TRP ASN SER GLN LYS ASP LEU LEU GLU GLN ARG ARG
SEQRES 7 B 208 ALA ALA VAL ASP THR TYR CYS ARG HIS ASN TYR GLY VAL
SEQRES 8 B 208 GLY GLU SER PHE THR VAL GLN ARG ARG VAL GLU PRO LYS
SEQRES 9 B 208 VAL THR VAL TYR PRO SER LYS THR GLN PRO LEU GLN HIS
SEQRES 10 B 208 HIS ASN LEU LEU VAL CYS SER VAL SER GLY PHE TYR PRO
SEQRES 11 B 208 GLY SER ILE GLU VAL ARG TRP PHE ARG ASN GLY GLN GLU
SEQRES 12 B 208 GLU LYS ALA GLY VAL VAL SER THR GLY LEU ILE GLN ASN
SEQRES 13 B 208 GLY ASP TRP THR PHE GLN THR LEU VAL MET LEU GLU THR
SEQRES 14 B 208 VAL PRO ARG SER GLY GLU VAL TYR THR CYS GLN VAL GLU
SEQRES 15 B 208 HIS PRO SER VAL THR SER PRO LEU THR VAL GLU TRP ARG
SEQRES 16 B 208 ALA ARG SER SER GLY GLY GLY SER LEU PRO ALA THR GLY
MODRES 4FQX ASN A 118 ASN GLYCOSYLATION SITE
HET NAG F 1 14
HET NAG F 2 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
FORMUL 6 NAG 2(C8 H15 N O6)
FORMUL 7 HOH *124(H2 O)
HELIX 1 1 LEU C 56 GLU C 65 5 10
HELIX 2 2 ASP C 68 ASP C 91 1 24
HELIX 3 3 LEU D 51 ASN D 63 1 13
HELIX 4 4 LYS D 65 GLN D 70 1 6
HELIX 5 5 ASN D 74 THR D 83 1 10
HELIX 6 6 SER D 89 ARG D 93 5 5
HELIX 7 7 LEU A 45 GLU A 47 5 3
HELIX 8 8 PHE A 48 ALA A 56 1 9
HELIX 9 9 GLY A 58 SER A 77 1 20
HELIX 10 10 THR B 51 LEU B 53 5 3
HELIX 11 11 GLY B 54 SER B 63 1 10
HELIX 12 12 GLN B 64 ALA B 73 1 10
HELIX 13 13 ALA B 73 TYR B 78 1 6
HELIX 14 14 TYR B 78 VAL B 85 1 8
SHEET 1 A 8 THR C 51 PRO C 54 0
SHEET 2 A 8 ASP C 40 ASP C 46 -1 N ASP C 46 O THR C 51
SHEET 3 A 8 VAL C 31 TYR C 37 -1 N GLU C 35 O LEU C 42
SHEET 4 A 8 PHE C 18 GLN C 25 -1 N TYR C 23 O GLY C 32
SHEET 5 A 8 VAL D 4 CYS D 11 -1 O VAL D 7 N VAL C 22
SHEET 6 A 8 PHE D 22 PHE D 28 -1 O CYS D 25 N GLU D 8
SHEET 7 A 8 ASP D 31 ASP D 37 -1 O TRP D 36 N TYR D 24
SHEET 8 A 8 LYS D 42 PRO D 45 -1 O ALA D 44 N CYS D 35
SHEET 1 B 9 VAL C 96 ARG C 98 0
SHEET 2 B 9 GLU A 40 TRP A 43 1 O THR A 41 N ARG C 98
SHEET 3 B 9 ASP A 29 ASP A 35 -1 N HIS A 33 O VAL A 42
SHEET 4 B 9 SER A 19 PHE A 26 -1 N PHE A 26 O ASP A 29
SHEET 5 B 9 HIS A 5 ASN A 15 -1 N LEU A 14 O SER A 19
SHEET 6 B 9 PHE B 7 PHE B 18 -1 O CYS B 15 N ILE A 7
SHEET 7 B 9 ARG B 23 TYR B 32 -1 O ARG B 23 N PHE B 18
SHEET 8 B 9 GLU B 35 ASP B 41 -1 O GLU B 35 N TYR B 32
SHEET 9 B 9 TYR B 47 ALA B 49 -1 O ARG B 48 N ARG B 39
SHEET 1 C 4 ILE C 102 THR C 107 0
SHEET 2 C 4 ASN C 117 LEU C 126 -1 O SER C 124 N ILE C 102
SHEET 3 C 4 SER C 157 PHE C 166 -1 O ALA C 160 N VAL C 123
SHEET 4 C 4 THR C 148 VAL C 153 -1 N SER C 151 O GLN C 159
SHEET 1 D 4 VAL C 140 PRO C 141 0
SHEET 2 D 4 LEU C 131 HIS C 137 -1 N HIS C 137 O VAL C 140
SHEET 3 D 4 PHE C 174 HIS C 180 -1 O THR C 179 N THR C 132
SHEET 4 D 4 THR C 186 TRP C 191 -1 O ALA C 187 N VAL C 178
SHEET 1 E 4 SER D 98 THR D 104 0
SHEET 2 E 4 VAL D 113 PHE D 122 -1 O ALA D 116 N ALA D 102
SHEET 3 E 4 TYR D 156 LEU D 164 -1 O SER D 160 N CYS D 117
SHEET 4 E 4 GLN D 149 PRO D 150 -1 N GLN D 149 O GLN D 157
SHEET 1 F 4 LYS D 136 VAL D 138 0
SHEET 2 F 4 THR D 128 LYS D 133 -1 N LYS D 133 O LYS D 136
SHEET 3 F 4 TYR D 172 GLU D 177 -1 O GLU D 177 N THR D 128
SHEET 4 F 4 ILE D 185 TRP D 189 -1 O ARG D 187 N CYS D 174
SHEET 1 G 4 GLU A 88 THR A 93 0
SHEET 2 G 4 ASN A 103 PHE A 112 -1 O ASP A 110 N GLU A 88
SHEET 3 G 4 PHE A 145 PHE A 153 -1 O PHE A 153 N ASN A 103
SHEET 4 G 4 SER A 133 GLU A 134 -1 N SER A 133 O TYR A 150
SHEET 1 H 4 GLU A 88 THR A 93 0
SHEET 2 H 4 ASN A 103 PHE A 112 -1 O ASP A 110 N GLU A 88
SHEET 3 H 4 PHE A 145 PHE A 153 -1 O PHE A 153 N ASN A 103
SHEET 4 H 4 LEU A 138 PRO A 139 -1 N LEU A 138 O ARG A 146
SHEET 1 I 4 LYS A 126 PRO A 127 0
SHEET 2 I 4 ASN A 118 ARG A 123 -1 N ARG A 123 O LYS A 126
SHEET 3 I 4 VAL A 160 GLU A 166 -1 O ASP A 162 N LEU A 122
SHEET 4 I 4 LEU A 174 GLU A 179 -1 O TRP A 178 N TYR A 161
SHEET 1 J 4 LYS B 98 TYR B 102 0
SHEET 2 J 4 LEU B 115 PHE B 122 -1 O VAL B 116 N TYR B 102
SHEET 3 J 4 PHE B 155 LEU B 161 -1 O LEU B 161 N LEU B 115
SHEET 4 J 4 VAL B 142 SER B 144 -1 N VAL B 143 O MET B 160
SHEET 1 K 4 LYS B 98 TYR B 102 0
SHEET 2 K 4 LEU B 115 PHE B 122 -1 O VAL B 116 N TYR B 102
SHEET 3 K 4 PHE B 155 LEU B 161 -1 O LEU B 161 N LEU B 115
SHEET 4 K 4 ILE B 148 GLN B 149 -1 N ILE B 148 O GLN B 156
SHEET 1 L 4 GLN B 136 GLU B 137 0
SHEET 2 L 4 GLU B 128 ARG B 133 -1 N ARG B 133 O GLN B 136
SHEET 3 L 4 TYR B 171 GLU B 176 -1 O GLN B 174 N ARG B 130
SHEET 4 L 4 LEU B 184 TRP B 188 -1 O LEU B 184 N VAL B 175
SSBOND 1 CYS C 24 CYS C 79 1555 1555 2.04
SSBOND 2 CYS C 121 CYS C 176 1555 1555 2.03
SSBOND 3 CYS D 11 CYS D 79 1555 1555 2.03
SSBOND 4 CYS D 25 CYS D 35 1555 1555 2.04
SSBOND 5 CYS D 117 CYS D 174 1555 1555 2.02
SSBOND 6 CYS E 88 CYS A 65 1555 1555 2.04
SSBOND 7 CYS A 107 CYS A 163 1555 1555 2.04
SSBOND 8 CYS B 15 CYS B 79 1555 1555 2.09
SSBOND 9 CYS B 117 CYS B 173 1555 1555 2.03
LINK ND2 ASN A 118 C1 NAG F 1 1555 1555 1.45
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.46
CISPEP 1 SER C 28 PRO C 29 0 0.48
CISPEP 2 PHE C 127 PRO C 128 0 0.16
CISPEP 3 TYR D 123 PRO D 124 0 -0.53
CISPEP 4 ASN A 15 PRO A 16 0 3.46
CISPEP 5 THR A 113 PRO A 114 0 -4.02
CISPEP 6 TYR B 123 PRO B 124 0 3.04
CRYST1 66.190 121.649 138.416 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.015108 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008220 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007225 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
