HEADER IMMUNE SYSTEM 28-JUL-12 4GBX
TITLE CRYSTAL STRUCTURE OF AN IMMUNE COMPLEX AT PH 6.5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DM ALPHA CHAIN;
COMPND 3 CHAIN: C;
COMPND 4 SYNONYM: MHC CLASS II ANTIGEN DMA, REALLY INTERESTING NEW GENE 6
COMPND 5 PROTEIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DM BETA CHAIN;
COMPND 10 CHAIN: D;
COMPND 11 SYNONYM: MHC CLASS II ANTIGEN DMB, REALLY INTERESTING NEW GENE 7
COMPND 12 PROTEIN;
COMPND 13 ENGINEERED: YES;
COMPND 14 MUTATION: YES;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN;
COMPND 17 CHAIN: A;
COMPND 18 SYNONYM: MHC CLASS II ANTIGEN DRA;
COMPND 19 ENGINEERED: YES;
COMPND 20 MUTATION: YES;
COMPND 21 MOL_ID: 4;
COMPND 22 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DRB1-1 BETA CHAIN;
COMPND 23 CHAIN: B;
COMPND 24 SYNONYM: MHC CLASS II ANTIGEN DRB1*1, DR-1, DR1;
COMPND 25 ENGINEERED: YES;
COMPND 26 MUTATION: YES;
COMPND 27 MOL_ID: 5;
COMPND 28 MOLECULE: SYNTHETIC PEPTIDE;
COMPND 29 CHAIN: E;
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: ALPHA CHAIN, DMA, HLA-DM, HLA-DMA, MHC CLASS II MOLECULE,
SOURCE 6 RING6;
SOURCE 7 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10029;
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: BETA CHAIN, DMB, HLA-DMB, MHC CLASS II MOLECULE HLA-DM, RING7;
SOURCE 17 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 19 EXPRESSION_SYSTEM_STRAIN: LEC3.2.8.1;
SOURCE 20 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 21 EXPRESSION_SYSTEM_PLASMID: PEE14.1;
SOURCE 22 MOL_ID: 3;
SOURCE 23 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 24 ORGANISM_COMMON: HUMAN;
SOURCE 25 ORGANISM_TAXID: 9606;
SOURCE 26 GENE: ALPHA CHAIN, HLA-DR1, HLA-DRA, HLA-DRA1, MHC CLASS II
SOURCE 27 MOLECULE;
SOURCE 28 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 29 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 30 MOL_ID: 4;
SOURCE 31 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 32 ORGANISM_COMMON: HUMAN;
SOURCE 33 ORGANISM_TAXID: 9606;
SOURCE 34 GENE: BETA CHAIN, HLA-DR1, HLA-DRB1, MHC CLASS II MOLECULE;
SOURCE 35 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 36 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 37 MOL_ID: 5;
SOURCE 38 SYNTHETIC: YES;
SOURCE 39 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 40 ORGANISM_COMMON: SYNTHETIC CONSTRUCT;
SOURCE 41 ORGANISM_TAXID: 32630
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 4GBX 1 COMPND REMARK SEQADV HETNAM
REVDAT 3 2 1 LINK SITE
REVDAT 2 15-NOV-17 4GBX 1 REMARK
REVDAT 1 16-JAN-13 4GBX 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. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8_1065
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.99
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 24550
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1227
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 36.9936 - 6.2315 0.98 2691 160 0.2030 0.2508
REMARK 3 2 6.2315 - 4.9499 0.99 2616 143 0.1906 0.2338
REMARK 3 3 4.9499 - 4.3253 1.00 2609 137 0.1492 0.1970
REMARK 3 4 4.3253 - 3.9303 1.00 2593 129 0.1772 0.2291
REMARK 3 5 3.9303 - 3.6489 1.00 2578 137 0.2101 0.2789
REMARK 3 6 3.6489 - 3.4339 1.00 2594 106 0.2036 0.2963
REMARK 3 7 3.4339 - 3.2621 1.00 2562 128 0.2229 0.2897
REMARK 3 8 3.2621 - 3.1201 1.00 2563 146 0.2667 0.2862
REMARK 3 9 3.1201 - 3.0001 1.00 2517 141 0.3113 0.3513
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) : 0.390
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.850
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 70.32
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 : 0.010 6323
REMARK 3 ANGLE : 1.295 8612
REMARK 3 CHIRALITY : 0.087 939
REMARK 3 PLANARITY : 0.007 1120
REMARK 3 DIHEDRAL : 16.830 2269
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 25
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 12 THROUGH 37 )
REMARK 3 ORIGIN FOR THE GROUP (A): -57.3588 12.0208 13.2840
REMARK 3 T TENSOR
REMARK 3 T11: 1.2116 T22: 0.5822
REMARK 3 T33: 1.1091 T12: 0.4933
REMARK 3 T13: -0.1332 T23: -0.1950
REMARK 3 L TENSOR
REMARK 3 L11: 0.4725 L22: 0.5339
REMARK 3 L33: 0.8619 L12: -0.2209
REMARK 3 L13: -0.3280 L23: -0.3722
REMARK 3 S TENSOR
REMARK 3 S11: -0.3064 S12: -0.2421 S13: 0.6189
REMARK 3 S21: 0.6483 S22: 0.1879 S23: 0.5803
REMARK 3 S31: -0.6608 S32: -0.1190 S33: 0.0784
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 38 THROUGH 54 )
REMARK 3 ORIGIN FOR THE GROUP (A): -65.1056 13.4398 17.8295
REMARK 3 T TENSOR
REMARK 3 T11: 1.3306 T22: 1.1434
REMARK 3 T33: 1.1682 T12: 0.5559
REMARK 3 T13: -0.0860 T23: -0.3919
REMARK 3 L TENSOR
REMARK 3 L11: 0.3075 L22: 1.0192
REMARK 3 L33: 1.0574 L12: -0.5595
REMARK 3 L13: 0.5243 L23: -0.9898
REMARK 3 S TENSOR
REMARK 3 S11: 0.0018 S12: 0.1667 S13: 0.1025
REMARK 3 S21: 0.2448 S22: 0.2689 S23: 0.2790
REMARK 3 S31: -0.2337 S32: -0.1609 S33: -0.2983
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 55 THROUGH 69 )
REMARK 3 ORIGIN FOR THE GROUP (A): -65.2016 19.0638 24.1041
REMARK 3 T TENSOR
REMARK 3 T11: 1.2046 T22: 1.0250
REMARK 3 T33: 1.4391 T12: 0.3685
REMARK 3 T13: -0.1384 T23: -0.2498
REMARK 3 L TENSOR
REMARK 3 L11: 0.2073 L22: 2.4148
REMARK 3 L33: 0.8046 L12: -0.6830
REMARK 3 L13: 0.4044 L23: -1.3975
REMARK 3 S TENSOR
REMARK 3 S11: 0.8427 S12: 0.1533 S13: 0.3061
REMARK 3 S21: 0.9483 S22: 0.6094 S23: 0.0189
REMARK 3 S31: -0.2574 S32: 0.2880 S33: -0.6249
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 70 THROUGH 130 )
REMARK 3 ORIGIN FOR THE GROUP (A): -60.0225 1.3947 12.3894
REMARK 3 T TENSOR
REMARK 3 T11: 0.5796 T22: 0.6914
REMARK 3 T33: 0.8283 T12: 0.3421
REMARK 3 T13: -0.0094 T23: -0.1340
REMARK 3 L TENSOR
REMARK 3 L11: 0.8457 L22: 1.3731
REMARK 3 L33: 0.4192 L12: -0.4754
REMARK 3 L13: 0.0968 L23: 0.1356
REMARK 3 S TENSOR
REMARK 3 S11: -0.2410 S12: -0.2936 S13: 0.7339
REMARK 3 S21: 0.1909 S22: -0.0664 S23: 0.3924
REMARK 3 S31: -0.5062 S32: -0.8202 S33: -0.0126
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 131 THROUGH 142 )
REMARK 3 ORIGIN FOR THE GROUP (A): -67.1955 -12.3916 24.9462
REMARK 3 T TENSOR
REMARK 3 T11: 0.7154 T22: 0.7623
REMARK 3 T33: 0.6381 T12: 0.1156
REMARK 3 T13: 0.2893 T23: -0.2639
REMARK 3 L TENSOR
REMARK 3 L11: 3.4144 L22: 1.8614
REMARK 3 L33: 1.3995 L12: 1.4419
REMARK 3 L13: 1.1957 L23: -0.6080
REMARK 3 S TENSOR
REMARK 3 S11: 0.1956 S12: -1.0395 S13: 0.1220
REMARK 3 S21: -0.1969 S22: -0.0565 S23: -0.1459
REMARK 3 S31: -0.3135 S32: -0.5949 S33: 0.1167
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 143 THROUGH 162 )
REMARK 3 ORIGIN FOR THE GROUP (A): -60.2948 2.2041 18.6938
REMARK 3 T TENSOR
REMARK 3 T11: 0.6501 T22: 0.7613
REMARK 3 T33: 0.7371 T12: 0.3345
REMARK 3 T13: 0.0527 T23: -0.0381
REMARK 3 L TENSOR
REMARK 3 L11: 1.2524 L22: 1.9660
REMARK 3 L33: 1.0504 L12: 1.2335
REMARK 3 L13: 0.7885 L23: 0.7749
REMARK 3 S TENSOR
REMARK 3 S11: -0.8988 S12: -0.6552 S13: 0.2288
REMARK 3 S21: 0.6202 S22: 0.2557 S23: 0.1076
REMARK 3 S31: -0.5880 S32: -0.2241 S33: 0.1761
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 163 THROUGH 202 )
REMARK 3 ORIGIN FOR THE GROUP (A): -59.3138 -10.2817 27.7109
REMARK 3 T TENSOR
REMARK 3 T11: 0.4696 T22: 0.7771
REMARK 3 T33: 0.6018 T12: 0.1733
REMARK 3 T13: 0.1398 T23: -0.1410
REMARK 3 L TENSOR
REMARK 3 L11: 1.0697 L22: 1.3033
REMARK 3 L33: 2.9484 L12: 0.2325
REMARK 3 L13: 1.0863 L23: 0.0493
REMARK 3 S TENSOR
REMARK 3 S11: -0.0830 S12: -0.8845 S13: 0.4608
REMARK 3 S21: 0.2310 S22: -0.0264 S23: 0.2059
REMARK 3 S31: 0.3392 S32: -1.2370 S33: -0.0417
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 3 THROUGH 14 )
REMARK 3 ORIGIN FOR THE GROUP (A): -54.3710 12.9236 8.3687
REMARK 3 T TENSOR
REMARK 3 T11: 1.2695 T22: 0.6486
REMARK 3 T33: 1.0294 T12: 0.2829
REMARK 3 T13: -0.2910 T23: -0.1916
REMARK 3 L TENSOR
REMARK 3 L11: 0.2723 L22: 0.1652
REMARK 3 L33: 0.1243 L12: 0.1959
REMARK 3 L13: -0.1903 L23: -0.1324
REMARK 3 S TENSOR
REMARK 3 S11: -0.2651 S12: -0.1784 S13: 0.5988
REMARK 3 S21: 0.5183 S22: -0.0031 S23: -0.6361
REMARK 3 S31: -0.3258 S32: 0.0624 S33: 0.1454
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 15 THROUGH 28 )
REMARK 3 ORIGIN FOR THE GROUP (A): -49.4334 20.3955 10.6683
REMARK 3 T TENSOR
REMARK 3 T11: 1.9697 T22: 0.2154
REMARK 3 T33: 1.2188 T12: 0.0252
REMARK 3 T13: -0.4970 T23: -0.2133
REMARK 3 L TENSOR
REMARK 3 L11: -0.0020 L22: 0.4145
REMARK 3 L33: 0.2154 L12: 0.0723
REMARK 3 L13: -0.0439 L23: -0.3001
REMARK 3 S TENSOR
REMARK 3 S11: -0.3596 S12: -0.1652 S13: 1.0352
REMARK 3 S21: 0.3039 S22: -0.3223 S23: -0.2263
REMARK 3 S31: -0.9072 S32: -0.1007 S33: 0.4523
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 29 THROUGH 38 )
REMARK 3 ORIGIN FOR THE GROUP (A): -50.3056 12.5228 0.2704
REMARK 3 T TENSOR
REMARK 3 T11: 1.2550 T22: 0.6031
REMARK 3 T33: 0.8826 T12: 0.1370
REMARK 3 T13: -0.0256 T23: 0.0839
REMARK 3 L TENSOR
REMARK 3 L11: 3.4964 L22: 1.3276
REMARK 3 L33: 1.3990 L12: 2.1529
REMARK 3 L13: 0.0761 L23: -0.0129
REMARK 3 S TENSOR
REMARK 3 S11: 0.1035 S12: 0.3168 S13: 0.2712
REMARK 3 S21: 0.1408 S22: 0.1684 S23: 0.1451
REMARK 3 S31: -1.4216 S32: -0.2006 S33: -0.0381
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 39 THROUGH 65 )
REMARK 3 ORIGIN FOR THE GROUP (A): -50.3891 16.7006 -6.4171
REMARK 3 T TENSOR
REMARK 3 T11: 1.6598 T22: 0.8674
REMARK 3 T33: 1.3601 T12: -0.0686
REMARK 3 T13: -0.1623 T23: 0.3403
REMARK 3 L TENSOR
REMARK 3 L11: 1.1792 L22: 1.7275
REMARK 3 L33: 1.8471 L12: 1.3700
REMARK 3 L13: 0.2896 L23: 0.8403
REMARK 3 S TENSOR
REMARK 3 S11: 0.0090 S12: 0.6897 S13: 0.5031
REMARK 3 S21: 0.1307 S22: 0.2321 S23: -0.7991
REMARK 3 S31: -0.2887 S32: -0.1896 S33: -0.5676
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 66 THROUGH 91 )
REMARK 3 ORIGIN FOR THE GROUP (A): -55.0981 26.3620 12.8083
REMARK 3 T TENSOR
REMARK 3 T11: 1.7251 T22: 0.6481
REMARK 3 T33: 1.6807 T12: 0.3125
REMARK 3 T13: 0.1147 T23: -0.0102
REMARK 3 L TENSOR
REMARK 3 L11: 0.0777 L22: 0.0064
REMARK 3 L33: 0.0125 L12: -0.0243
REMARK 3 L13: 0.0341 L23: -0.0074
REMARK 3 S TENSOR
REMARK 3 S11: -0.2534 S12: -0.0623 S13: 0.9083
REMARK 3 S21: 1.1773 S22: 0.1043 S23: -0.2525
REMARK 3 S31: -0.0126 S32: 0.1177 S33: 0.4115
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 92 THROUGH 119 )
REMARK 3 ORIGIN FOR THE GROUP (A): -43.2496 -4.7582 39.1748
REMARK 3 T TENSOR
REMARK 3 T11: 0.8163 T22: 0.7798
REMARK 3 T33: 0.7087 T12: 0.2248
REMARK 3 T13: -0.1252 T23: -0.3836
REMARK 3 L TENSOR
REMARK 3 L11: 0.3507 L22: 1.0186
REMARK 3 L33: 1.5522 L12: 0.3109
REMARK 3 L13: -0.7179 L23: -0.4260
REMARK 3 S TENSOR
REMARK 3 S11: -0.2130 S12: -0.4982 S13: 0.4347
REMARK 3 S21: 0.6664 S22: -0.1078 S23: 0.4134
REMARK 3 S31: -0.4818 S32: 0.0315 S33: 0.3761
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 120 THROUGH 143 )
REMARK 3 ORIGIN FOR THE GROUP (A): -37.9724 1.7505 38.4501
REMARK 3 T TENSOR
REMARK 3 T11: 1.0010 T22: 0.7272
REMARK 3 T33: 0.8485 T12: -0.0418
REMARK 3 T13: -0.1346 T23: -0.2849
REMARK 3 L TENSOR
REMARK 3 L11: 0.9142 L22: 1.0021
REMARK 3 L33: 0.9453 L12: -0.6928
REMARK 3 L13: 0.6134 L23: -0.3907
REMARK 3 S TENSOR
REMARK 3 S11: 0.0264 S12: 0.0481 S13: 0.4191
REMARK 3 S21: -0.2956 S22: -0.0162 S23: -0.0983
REMARK 3 S31: -0.3882 S32: 0.5520 S33: -0.0611
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 144 THROUGH 157 )
REMARK 3 ORIGIN FOR THE GROUP (A): -49.4172 3.3027 28.3110
REMARK 3 T TENSOR
REMARK 3 T11: 0.7642 T22: 0.5219
REMARK 3 T33: 0.8625 T12: 0.1715
REMARK 3 T13: 0.1953 T23: -0.4529
REMARK 3 L TENSOR
REMARK 3 L11: 1.2029 L22: 4.3848
REMARK 3 L33: 3.9058 L12: 1.3502
REMARK 3 L13: 0.1240 L23: -0.4507
REMARK 3 S TENSOR
REMARK 3 S11: -0.6581 S12: -0.3744 S13: 0.4666
REMARK 3 S21: -0.1546 S22: 0.2116 S23: 0.5171
REMARK 3 S31: -0.0638 S32: 0.4861 S33: -0.0070
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 158 THROUGH 177 )
REMARK 3 ORIGIN FOR THE GROUP (A): -36.2669 -6.0806 45.1304
REMARK 3 T TENSOR
REMARK 3 T11: 1.1621 T22: 0.7797
REMARK 3 T33: 0.5210 T12: 0.2788
REMARK 3 T13: -0.1017 T23: -0.5411
REMARK 3 L TENSOR
REMARK 3 L11: 3.4419 L22: 1.8162
REMARK 3 L33: 2.2543 L12: 0.1464
REMARK 3 L13: 0.8729 L23: 1.2525
REMARK 3 S TENSOR
REMARK 3 S11: -0.3802 S12: -0.5305 S13: 0.1350
REMARK 3 S21: 0.7585 S22: -0.0196 S23: -0.1319
REMARK 3 S31: -0.4744 S32: 0.3269 S33: -0.2949
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 178 THROUGH 193 )
REMARK 3 ORIGIN FOR THE GROUP (A): -41.6171 3.9959 45.9340
REMARK 3 T TENSOR
REMARK 3 T11: 1.3966 T22: 0.9310
REMARK 3 T33: 0.8619 T12: 0.4061
REMARK 3 T13: -0.1897 T23: -0.7102
REMARK 3 L TENSOR
REMARK 3 L11: 1.4239 L22: 1.6215
REMARK 3 L33: 1.4604 L12: -0.8653
REMARK 3 L13: 0.8363 L23: -0.3156
REMARK 3 S TENSOR
REMARK 3 S11: -0.2831 S12: -0.5798 S13: 0.6719
REMARK 3 S21: 0.5704 S22: 0.0112 S23: -0.0047
REMARK 3 S31: 0.0121 S32: 0.0782 S33: -0.1775
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 45 )
REMARK 3 ORIGIN FOR THE GROUP (A): -46.2275 -13.1716 -1.6973
REMARK 3 T TENSOR
REMARK 3 T11: 0.2948 T22: 0.3199
REMARK 3 T33: 0.4582 T12: 0.0206
REMARK 3 T13: -0.0330 T23: 0.0352
REMARK 3 L TENSOR
REMARK 3 L11: 0.2182 L22: 1.9953
REMARK 3 L33: 2.0287 L12: 0.3184
REMARK 3 L13: -0.6229 L23: -0.1285
REMARK 3 S TENSOR
REMARK 3 S11: -0.1716 S12: 0.2724 S13: 0.4560
REMARK 3 S21: 0.0245 S22: 0.0786 S23: 0.0578
REMARK 3 S31: -0.1329 S32: -0.2394 S33: 0.1278
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 46 THROUGH 58 )
REMARK 3 ORIGIN FOR THE GROUP (A): -45.9742 -1.2785 3.6464
REMARK 3 T TENSOR
REMARK 3 T11: 0.8852 T22: 0.1910
REMARK 3 T33: 1.2346 T12: -0.1900
REMARK 3 T13: -0.1875 T23: 0.0083
REMARK 3 L TENSOR
REMARK 3 L11: 0.5846 L22: 0.1616
REMARK 3 L33: 2.6534 L12: -0.2914
REMARK 3 L13: 1.1778 L23: -0.6465
REMARK 3 S TENSOR
REMARK 3 S11: -0.3106 S12: -0.0753 S13: 0.9729
REMARK 3 S21: -0.5635 S22: -0.1997 S23: 0.2486
REMARK 3 S31: -0.8805 S32: -0.1021 S33: 0.2245
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 59 THROUGH 154 )
REMARK 3 ORIGIN FOR THE GROUP (A): -49.7612 -23.9534 3.0823
REMARK 3 T TENSOR
REMARK 3 T11: 0.2123 T22: 0.3951
REMARK 3 T33: 0.3028 T12: 0.0099
REMARK 3 T13: -0.0456 T23: 0.0376
REMARK 3 L TENSOR
REMARK 3 L11: 1.7120 L22: 1.1619
REMARK 3 L33: 1.7948 L12: 0.0209
REMARK 3 L13: -0.7969 L23: 0.2742
REMARK 3 S TENSOR
REMARK 3 S11: -0.0708 S12: 0.1411 S13: 0.3090
REMARK 3 S21: 0.0344 S22: 0.0684 S23: 0.0667
REMARK 3 S31: 0.0601 S32: -0.0937 S33: 0.0144
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 155 THROUGH 182 )
REMARK 3 ORIGIN FOR THE GROUP (A): -54.9050 -33.2905 13.5626
REMARK 3 T TENSOR
REMARK 3 T11: 0.3875 T22: 0.4671
REMARK 3 T33: 0.3856 T12: -0.1114
REMARK 3 T13: 0.0457 T23: 0.0467
REMARK 3 L TENSOR
REMARK 3 L11: 1.9140 L22: 1.7159
REMARK 3 L33: 6.5355 L12: 0.2316
REMARK 3 L13: -1.0285 L23: 1.9773
REMARK 3 S TENSOR
REMARK 3 S11: 0.1351 S12: -0.1906 S13: -0.2586
REMARK 3 S21: 0.3773 S22: 0.0375 S23: -0.0758
REMARK 3 S31: 0.8634 S32: -0.6821 S33: -0.1210
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'B' AND (RESID -5 THROUGH 32 )
REMARK 3 ORIGIN FOR THE GROUP (A): -40.7443 -20.3999 -8.4580
REMARK 3 T TENSOR
REMARK 3 T11: 0.2816 T22: 0.3870
REMARK 3 T33: 0.3361 T12: -0.0431
REMARK 3 T13: 0.0275 T23: 0.0319
REMARK 3 L TENSOR
REMARK 3 L11: 2.6249 L22: 2.0519
REMARK 3 L33: 2.1965 L12: 1.4222
REMARK 3 L13: 1.8487 L23: 1.8496
REMARK 3 S TENSOR
REMARK 3 S11: 0.0356 S12: 0.2369 S13: 0.1772
REMARK 3 S21: 0.1870 S22: -0.0257 S23: 0.0230
REMARK 3 S31: -0.0616 S32: 0.2300 S33: -0.0007
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 33 THROUGH 122 )
REMARK 3 ORIGIN FOR THE GROUP (A): -33.3798 -14.4841 -2.3340
REMARK 3 T TENSOR
REMARK 3 T11: 0.3345 T22: 0.3967
REMARK 3 T33: 0.4444 T12: -0.1337
REMARK 3 T13: -0.0029 T23: 0.0612
REMARK 3 L TENSOR
REMARK 3 L11: 1.6752 L22: 0.2745
REMARK 3 L33: 2.9536 L12: -0.6405
REMARK 3 L13: -0.2169 L23: 0.0720
REMARK 3 S TENSOR
REMARK 3 S11: -0.0217 S12: 0.3674 S13: 0.3858
REMARK 3 S21: -0.0847 S22: -0.0354 S23: -0.2038
REMARK 3 S31: -0.3799 S32: 0.2469 S33: 0.0639
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 123 THROUGH 190 )
REMARK 3 ORIGIN FOR THE GROUP (A): -30.1004 -24.3689 26.4315
REMARK 3 T TENSOR
REMARK 3 T11: 0.4458 T22: 0.4369
REMARK 3 T33: 0.3847 T12: 0.1141
REMARK 3 T13: -0.0371 T23: -0.0725
REMARK 3 L TENSOR
REMARK 3 L11: 2.3582 L22: 1.1324
REMARK 3 L33: 2.3923 L12: 0.2653
REMARK 3 L13: 0.0257 L23: 1.0498
REMARK 3 S TENSOR
REMARK 3 S11: -0.1694 S12: -0.2569 S13: -0.0044
REMARK 3 S21: 0.6530 S22: 0.1783 S23: -0.1159
REMARK 3 S31: 0.3322 S32: 0.6716 S33: -0.0285
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 84 THROUGH 93 )
REMARK 3 ORIGIN FOR THE GROUP (A): -41.1958 -9.1352 -16.2979
REMARK 3 T TENSOR
REMARK 3 T11: 0.3780 T22: 0.7789
REMARK 3 T33: 0.7923 T12: -0.1606
REMARK 3 T13: -0.0689 T23: 0.0815
REMARK 3 L TENSOR
REMARK 3 L11: 2.3628 L22: 1.1996
REMARK 3 L33: 1.8222 L12: -0.6023
REMARK 3 L13: 0.0268 L23: -1.3853
REMARK 3 S TENSOR
REMARK 3 S11: -0.4075 S12: 0.1375 S13: -0.1205
REMARK 3 S21: 0.2034 S22: -0.1106 S23: -0.2699
REMARK 3 S31: -0.4061 S32: -0.1190 S33: 0.5898
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 4GBX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUL-12.
REMARK 100 THE DEPOSITION ID IS D_1000073991.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-APR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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) : 0.978
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 : 27191
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.87500
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 (%): 62.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES, 6% PEG 20000, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K, PH 6.5
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 33.08350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 71.55350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 63.01600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 71.55350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.08350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 63.01600
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
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: 5570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 VAL C 1
REMARK 465 PRO C 2
REMARK 465 GLU C 3
REMARK 465 ALA C 4
REMARK 465 PRO C 5
REMARK 465 THR C 6
REMARK 465 PRO C 7
REMARK 465 MET C 8
REMARK 465 TRP C 9
REMARK 465 PRO C 10
REMARK 465 ASP C 11
REMARK 465 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 ILE A 1
REMARK 465 LYS A 2
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 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 GLN C 14 CG CD OE1 NE2
REMARK 470 LEU C 56 CG CD1 CD2
REMARK 470 GLN C 64 CG CD OE1 NE2
REMARK 470 PHE C 145 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP D 15 CG OD1 OD2
REMARK 470 LYS D 20 CG CD CE NZ
REMARK 470 ASN D 74 CG OD1 ND2
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 ND2 ASN A 118 O5 NAG A 201 2.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NZ LYS C 89 O GLY D 169 2354 2.17
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 C 55 -143.18 -74.01
REMARK 500 LEU C 56 79.37 -114.82
REMARK 500 PRO C 57 61.11 -115.09
REMARK 500 GLU C 58 44.84 39.89
REMARK 500 ALA C 60 86.36 53.62
REMARK 500 ALA C 63 -131.97 55.83
REMARK 500 ASP C 68 84.78 -150.53
REMARK 500 ASP C 183 20.26 -153.49
REMARK 500 LEU D 33 -61.03 -102.77
REMARK 500 MET D 43 58.18 -96.40
REMARK 500 GLU D 47 -139.02 50.13
REMARK 500 LEU D 62 157.89 80.34
REMARK 500 ASN D 63 -8.00 67.53
REMARK 500 MET D 69 -18.00 -41.79
REMARK 500 THR D 158 -178.79 -178.23
REMARK 500 GLU D 177 73.51 -111.94
REMARK 500 ASP A 27 15.41 51.09
REMARK 500 ARG A 100 -4.17 80.57
REMARK 500 PRO A 115 72.19 -65.23
REMARK 500 ASN A 124 73.63 42.55
REMARK 500 GLN B -2 -88.75 -123.12
REMARK 500 ASN B 19 73.30 41.92
REMARK 500 ASN B 33 -105.41 51.99
REMARK 500 VAL B 85 -71.14 -61.50
REMARK 500 TRP B 153 34.89 80.22
REMARK 500 HIS B 177 142.26 -170.53
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4GBX C 1 199 UNP P28067 DMA_HUMAN 27 225
DBREF 4GBX D 1 193 UNP P28068 DMB_HUMAN 19 211
DBREF 4GBX A 1 191 UNP P01903 DRA_HUMAN 26 216
DBREF 4GBX B 1 191 UNP P04229 2B11_HUMAN 30 220
DBREF 4GBX E 84 93 PDB 4GBX 4GBX 84 93
SEQADV 4GBX GLN C 136 UNP P28067 HIS 162 VARIANT
SEQADV 4GBX HIS C 137 UNP P28067 ASP 163 VARIANT
SEQADV 4GBX ASP C 165 UNP P28067 ASN 191 ENGINEERED MUTATION
SEQADV 4GBX LEU C 200 UNP P28067 EXPRESSION TAG
SEQADV 4GBX VAL C 201 UNP P28067 EXPRESSION TAG
SEQADV 4GBX PRO C 202 UNP P28067 EXPRESSION TAG
SEQADV 4GBX ARG C 203 UNP P28067 EXPRESSION TAG
SEQADV 4GBX SER D 46 UNP P28068 CYS 64 ENGINEERED MUTATION
SEQADV 4GBX ASP D 92 UNP P28068 ASN 110 ENGINEERED MUTATION
SEQADV 4GBX GLY D 194 UNP P28068 EXPRESSION TAG
SEQADV 4GBX CYS D 195 UNP P28068 EXPRESSION TAG
SEQADV 4GBX LEU D 196 UNP P28068 EXPRESSION TAG
SEQADV 4GBX VAL D 197 UNP P28068 EXPRESSION TAG
SEQADV 4GBX PRO D 198 UNP P28068 EXPRESSION TAG
SEQADV 4GBX ARG D 199 UNP P28068 EXPRESSION TAG
SEQADV 4GBX CYS A 65 UNP P01903 VAL 90 ENGINEERED MUTATION
SEQADV 4GBX VAL B -5 UNP P04229 EXPRESSION TAG
SEQADV 4GBX LEU B -4 UNP P04229 EXPRESSION TAG
SEQADV 4GBX PHE B -3 UNP P04229 EXPRESSION TAG
SEQADV 4GBX GLN B -2 UNP P04229 EXPRESSION TAG
SEQADV 4GBX GLY B -1 UNP P04229 EXPRESSION TAG
SEQADV 4GBX PRO B 0 UNP P04229 EXPRESSION TAG
SEQADV 4GBX SER B 30 UNP P04229 CYS 59 ENGINEERED MUTATION
SEQADV 4GBX SER B 192 UNP P04229 EXPRESSION TAG
SEQADV 4GBX SER B 193 UNP P04229 EXPRESSION TAG
SEQADV 4GBX GLY B 194 UNP P04229 EXPRESSION TAG
SEQADV 4GBX GLY B 195 UNP P04229 EXPRESSION TAG
SEQADV 4GBX GLY B 196 UNP P04229 EXPRESSION TAG
SEQADV 4GBX SER B 197 UNP P04229 EXPRESSION TAG
SEQADV 4GBX LEU B 198 UNP P04229 EXPRESSION TAG
SEQADV 4GBX PRO B 199 UNP P04229 EXPRESSION TAG
SEQADV 4GBX ALA B 200 UNP P04229 EXPRESSION TAG
SEQADV 4GBX THR B 201 UNP P04229 EXPRESSION TAG
SEQADV 4GBX 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 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
SEQRES 1 E 10 GLY LYS GLN ASN CYS LEU LYS LEU ALA THR
MODRES 4GBX ASN A 78 ASN GLYCOSYLATION SITE
MODRES 4GBX ASN C 15 ASN GLYCOSYLATION SITE
MODRES 4GBX ASN A 118 ASN GLYCOSYLATION SITE
HET NAG C 301 14
HET NAG A 201 14
HET NAG A 202 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
FORMUL 6 NAG 3(C8 H15 N O6)
FORMUL 9 HOH *56(H2 O)
HELIX 1 1 ASP C 68 ILE C 86 1 19
HELIX 2 2 ILE C 86 ASP C 91 1 6
HELIX 3 3 LEU D 51 HIS D 61 1 11
HELIX 4 4 LYS D 65 GLY D 75 1 11
HELIX 5 5 GLY D 75 ARG D 93 1 19
HELIX 6 6 LEU A 45 GLN A 57 1 13
HELIX 7 7 GLY A 58 SER A 77 1 20
HELIX 8 8 THR B 51 LEU B 53 5 3
HELIX 9 9 GLY B 54 GLN B 64 1 11
HELIX 10 10 GLN B 64 TYR B 78 1 15
HELIX 11 11 TYR B 78 GLY B 86 1 9
HELIX 12 12 GLY B 86 VAL B 91 1 6
SHEET 1 A 7 THR C 51 PRO C 54 0
SHEET 2 A 7 ASP C 40 ASP C 46 -1 N PHE C 44 O VAL C 53
SHEET 3 A 7 VAL C 31 TYR C 37 -1 N LEU C 33 O PHE C 45
SHEET 4 A 7 THR C 17 GLN C 25 -1 N THR C 21 O SER C 34
SHEET 5 A 7 VAL D 4 LEU D 13 -1 O ALA D 5 N CYS C 24
SHEET 6 A 7 PRO D 19 PHE D 28 -1 O LYS D 20 N LEU D 12
SHEET 7 A 7 LEU D 32 THR D 34 -1 O THR D 34 N ILE D 26
SHEET 1 B 9 VAL C 96 SER C 97 0
SHEET 2 B 9 GLU A 40 TRP A 43 1 O THR A 41 N VAL C 96
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 ALA A 10 O MET A 23
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 LEU B 27 N GLU B 14
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 PHE C 166 N ASN C 117
SHEET 4 C 4 PHE C 145 VAL C 153 -1 N SER C 151 O GLN C 159
SHEET 1 D 4 VAL C 140 VAL C 142 0
SHEET 2 D 4 LEU C 131 HIS C 137 -1 N TRP C 135 O VAL C 142
SHEET 3 D 4 PHE C 174 HIS C 180 -1 O ILE C 177 N ASN C 134
SHEET 4 D 4 THR C 186 TRP C 191 -1 O ALA C 189 N CYS C 176
SHEET 1 E 4 SER D 98 LYS D 103 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 ILE D 129 LYS D 133 -1 N LYS D 133 O LYS D 136
SHEET 3 F 4 TYR D 172 VAL D 176 -1 O THR D 173 N ARG D 132
SHEET 4 F 4 ILE D 185 TRP D 189 -1 O TRP D 189 N TYR D 172
SHEET 1 G 4 GLU A 88 THR A 93 0
SHEET 2 G 4 ASN A 103 PHE A 112 -1 O ILE A 106 N LEU A 92
SHEET 3 G 4 PHE A 145 PHE A 153 -1 O LEU A 151 N LEU A 105
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 ILE A 106 N LEU A 92
SHEET 3 H 4 PHE A 145 PHE A 153 -1 O LEU A 151 N LEU A 105
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 TYR A 161 GLU A 166 -1 O ARG A 164 N THR A 120
SHEET 4 I 4 LEU A 174 TRP A 178 -1 O TRP A 178 N TYR A 161
SHEET 1 J 4 LYS B 98 PRO B 103 0
SHEET 2 J 4 ASN B 113 PHE B 122 -1 O VAL B 116 N TYR B 102
SHEET 3 J 4 PHE B 155 THR B 163 -1 O VAL B 159 N CYS B 117
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 PRO B 103 0
SHEET 2 K 4 ASN B 113 PHE B 122 -1 O VAL B 116 N TYR B 102
SHEET 3 K 4 PHE B 155 THR B 163 -1 O VAL B 159 N CYS B 117
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 138 0
SHEET 2 L 4 GLU B 128 ARG B 133 -1 N ARG B 133 O GLN B 136
SHEET 3 L 4 VAL B 170 GLU B 176 -1 O THR B 172 N PHE B 132
SHEET 4 L 4 LEU B 184 ARG B 189 -1 O LEU B 184 N VAL B 175
SSBOND 1 CYS C 24 CYS C 79 1555 1555 2.03
SSBOND 2 CYS C 121 CYS C 176 1555 1555 2.02
SSBOND 3 CYS D 11 CYS D 79 1555 1555 2.03
SSBOND 4 CYS D 25 CYS D 35 1555 1555 2.01
SSBOND 5 CYS D 117 CYS D 174 1555 1555 2.02
SSBOND 6 CYS A 65 CYS E 88 1555 1555 2.06
SSBOND 7 CYS A 107 CYS A 163 1555 1555 2.06
SSBOND 8 CYS B 15 CYS B 79 1555 1555 2.06
SSBOND 9 CYS B 117 CYS B 173 1555 1555 2.04
LINK ND2 ASN C 15 C1 NAG C 301 1555 1555 1.50
LINK ND2 ASN A 78 C1 NAG A 202 1555 1555 1.50
LINK ND2 ASN A 118 C1 NAG A 201 1555 1555 1.54
CISPEP 1 SER C 28 PRO C 29 0 -1.40
CISPEP 2 PHE C 127 PRO C 128 0 0.95
CISPEP 3 TYR D 123 PRO D 124 0 -3.10
CISPEP 4 ASN A 15 PRO A 16 0 -0.45
CISPEP 5 GLN A 57 GLY A 58 0 -3.59
CISPEP 6 THR A 113 PRO A 114 0 -5.53
CISPEP 7 TYR B 123 PRO B 124 0 9.43
CRYST1 66.167 126.032 143.107 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 0.015113 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007934 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006988 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
