HEADER IMMUNE SYSTEM 03-JUN-19 6P67
TITLE CRYSTAL STRUCTURE OF A COMPLEX OF HUMAN IL-7RALPHA WITH AN ANTI-IL-
TITLE 2 7RALPHA 2B8 FAB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTI-IL-7R 2B8 FAB HEAVY CHAIN;
COMPND 3 CHAIN: A, C, E, H;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: ANTI-IL-7R 2B8 FAB LIGHT CHAIN;
COMPND 7 CHAIN: B, D, F, L;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: INTERLEUKIN-7 RECEPTOR SUBUNIT ALPHA;
COMPND 11 CHAIN: G, I, J, K;
COMPND 12 SYNONYM: IL-7RA,CDW127;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: FREESTYLE HEK293F;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 11 ORGANISM_COMMON: MOUSE;
SOURCE 12 ORGANISM_TAXID: 10090;
SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 14 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 16 EXPRESSION_SYSTEM_VARIANT: FREESTYLE HEK293F;
SOURCE 17 MOL_ID: 3;
SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 19 ORGANISM_COMMON: HUMAN;
SOURCE 20 ORGANISM_TAXID: 9606;
SOURCE 21 GENE: IL7R;
SOURCE 22 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;
SOURCE 23 EXPRESSION_SYSTEM_TAXID: 7227;
SOURCE 24 EXPRESSION_SYSTEM_VARIANT: SCHNEIDER S2
KEYWDS INTERLEUKIN-7 RECEPTOR EXTRACELLULAR DOHMAIN, ANTIBODY 2B8 FAB
KEYWDS 2 FRAGMENT, PROTEIN POLYMER, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR S.T.R.WALSH,L.KASHI,C.L.KOHNHORST
REVDAT 6 13-MAR-24 6P67 1 SOURCE
REVDAT 5 11-OCT-23 6P67 1 HETSYN
REVDAT 4 29-JUL-20 6P67 1 COMPND SOURCE REMARK HETNAM
REVDAT 4 2 1 LINK SITE ATOM
REVDAT 3 01-JAN-20 6P67 1 JRNL
REVDAT 2 04-DEC-19 6P67 1 REMARK
REVDAT 1 04-SEP-19 6P67 0
JRNL AUTH J.A.HIXON,C.ANDREWS,L.KASHI,C.L.KOHNHORST,E.SENKEVITCH,
JRNL AUTH 2 K.CZARRA,J.T.BARATA,W.LI,J.P.SCHNEIDER,S.T.R.WALSH,S.K.DURUM
JRNL TITL NEW ANTI-IL-7R ALPHA MONOCLONAL ANTIBODIES SHOW EFFICACY
JRNL TITL 2 AGAINST T CELL ACUTE LYMPHOBLASTIC LEUKEMIA IN PRE-CLINICAL
JRNL TITL 3 MODELS.
JRNL REF LEUKEMIA V. 34 35 2020
JRNL REFN ESSN 1476-5551
JRNL PMID 31439943
JRNL DOI 10.1038/S41375-019-0531-8
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.16RC1_3535
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.77
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 70220
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.249
REMARK 3 R VALUE (WORKING SET) : 0.249
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.830
REMARK 3 FREE R VALUE TEST SET COUNT : 1985
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 43.7700 - 6.9800 0.99 4941 146 0.2074 0.1867
REMARK 3 2 6.9800 - 5.5400 1.00 4902 147 0.2340 0.2458
REMARK 3 3 5.5400 - 4.8400 1.00 4932 144 0.2090 0.2490
REMARK 3 4 4.8400 - 4.4000 1.00 4886 138 0.1980 0.2261
REMARK 3 5 4.4000 - 4.0900 1.00 4881 144 0.2106 0.2435
REMARK 3 6 4.0900 - 3.8500 0.99 4881 136 0.2503 0.2578
REMARK 3 7 3.8500 - 3.6500 0.99 4877 136 0.2628 0.2882
REMARK 3 8 3.6500 - 3.4900 0.99 4890 147 0.2928 0.3092
REMARK 3 9 3.4900 - 3.3600 0.99 4845 141 0.2885 0.2938
REMARK 3 10 3.3600 - 3.2400 0.99 4842 152 0.2979 0.3369
REMARK 3 11 3.2400 - 3.1400 0.99 4838 134 0.3272 0.3815
REMARK 3 12 3.1400 - 3.0500 0.99 4856 151 0.3490 0.3800
REMARK 3 13 3.0500 - 2.9700 0.99 4839 126 0.3977 0.4237
REMARK 3 14 2.9700 - 2.9000 0.99 4825 143 0.4444 0.4747
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) : 0.512
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.718
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 73.25
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 90.44
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 : 0.003 19796
REMARK 3 ANGLE : 0.660 26944
REMARK 3 CHIRALITY : 0.047 3064
REMARK 3 PLANARITY : 0.004 3407
REMARK 3 DIHEDRAL : 10.564 11730
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 3
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: (CHAIN 'A' AND (RESID 1 THROUGH 42 OR
REMARK 3 (RESID 43 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 44
REMARK 3 THROUGH 57 OR (RESID 58 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 59 THROUGH 61 OR (RESID 62 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 63 THROUGH 83 OR
REMARK 3 (RESID 84 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 85
REMARK 3 THROUGH 136 OR RESID 140 THROUGH 207 OR
REMARK 3 (RESID 208 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 209
REMARK 3 THROUGH 212 OR (RESID 213 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 214 THROUGH 223))
REMARK 3 SELECTION : (CHAIN 'C' AND ((RESID 1 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 2 THROUGH 12 OR (RESID 13 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 14 THROUGH 40 OR
REMARK 3 (RESID 41 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 42
REMARK 3 THROUGH 57 OR (RESID 58 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 59 THROUGH 61 OR (RESID 62 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 63 THROUGH 136 OR
REMARK 3 RESID 140 THROUGH 207 OR (RESID 208 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 209 THROUGH 212 OR
REMARK 3 (RESID 213 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 214
REMARK 3 THROUGH 223))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: (CHAIN 'A' AND (RESID 1 THROUGH 42 OR
REMARK 3 (RESID 43 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 44
REMARK 3 THROUGH 57 OR (RESID 58 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 59 THROUGH 61 OR (RESID 62 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 63 THROUGH 83 OR
REMARK 3 (RESID 84 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 85
REMARK 3 THROUGH 136 OR RESID 140 THROUGH 207 OR
REMARK 3 (RESID 208 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 209
REMARK 3 THROUGH 212 OR (RESID 213 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 214 THROUGH 223))
REMARK 3 SELECTION : (CHAIN 'E' AND (RESID 1 THROUGH 12 OR
REMARK 3 (RESID 13 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 14
REMARK 3 THROUGH 40 OR (RESID 41 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 42 OR (RESID 43 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 44 THROUGH 64 OR (RESID 65 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 66 THROUGH 223))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: (CHAIN 'A' AND (RESID 1 THROUGH 42 OR
REMARK 3 (RESID 43 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 44
REMARK 3 THROUGH 57 OR (RESID 58 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 59 THROUGH 61 OR (RESID 62 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 63 THROUGH 83 OR
REMARK 3 (RESID 84 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 85
REMARK 3 THROUGH 136 OR RESID 140 THROUGH 207 OR
REMARK 3 (RESID 208 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 209
REMARK 3 THROUGH 212 OR (RESID 213 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 214 THROUGH 223))
REMARK 3 SELECTION : (CHAIN 'H' AND (RESID 1 THROUGH 12 OR
REMARK 3 (RESID 13 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 14
REMARK 3 THROUGH 40 OR (RESID 41 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 42 OR (RESID 43 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 44 THROUGH 57 OR (RESID 58 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 59 THROUGH 61 OR
REMARK 3 (RESID 62 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 63
REMARK 3 THROUGH 64 OR (RESID 65 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 66 THROUGH 83 OR (RESID 84 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 85 THROUGH 136 OR
REMARK 3 RESID 140 THROUGH 207 OR (RESID 208 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 209 THROUGH 212 OR
REMARK 3 (RESID 213 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 214
REMARK 3 THROUGH 223))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: (CHAIN 'B' AND (RESID 1 THROUGH 212 OR
REMARK 3 (RESID 213 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB ))))
REMARK 3 SELECTION : (CHAIN 'D' AND (RESID 1 THROUGH 212 OR
REMARK 3 (RESID 213 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB ))))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: (CHAIN 'B' AND (RESID 1 THROUGH 212 OR
REMARK 3 (RESID 213 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB ))))
REMARK 3 SELECTION : CHAIN 'F'
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: (CHAIN 'B' AND (RESID 1 THROUGH 212 OR
REMARK 3 (RESID 213 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB ))))
REMARK 3 SELECTION : (CHAIN 'L' AND (RESID 1 THROUGH 212 OR
REMARK 3 (RESID 213 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB ))))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 3
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: (CHAIN 'G' AND ((RESID 17 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 18 THROUGH 26 OR (RESID 27 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 28 THROUGH 31 OR
REMARK 3 (RESID 32 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 33
REMARK 3 THROUGH 34 OR (RESID 35 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 36 THROUGH 38 OR (RESID 39
REMARK 3 THROUGH 41 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 42 OR
REMARK 3 (RESID 43 THROUGH 45 AND (NAME N OR NAME
REMARK 3 CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK 3 RESID 51 OR (RESID 52 THROUGH 53 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 54 THROUGH 56 OR
REMARK 3 (RESID 57 THROUGH 59 AND (NAME N OR NAME
REMARK 3 CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK 3 RESID 60 OR (RESID 61 AND (NAME N OR NAME
REMARK 3 CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK 3 RESID 62 OR (RESID 63 THROUGH 64 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 65 OR (RESID 66
REMARK 3 THROUGH 71 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 72 OR
REMARK 3 (RESID 73 THROUGH 75 AND (NAME N OR NAME
REMARK 3 CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK 3 RESID 76 OR (RESID 77 THROUGH 82 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 83 OR (RESID 84 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 85 OR (RESID 86
REMARK 3 THROUGH 87 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 88 OR
REMARK 3 (RESID 89 THROUGH 90 AND (NAME N OR NAME
REMARK 3 CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK 3 RESID 95 OR (RESID 96 AND (NAME N OR NAME
REMARK 3 CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK 3 RESID 97 THROUGH 100 OR (RESID 101
REMARK 3 THROUGH 103 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 104 THROUGH 105 OR (RESID 106 AND (NAME N
REMARK 3 OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK 3 )) OR RESID 107 OR (RESID 108 AND (NAME N
REMARK 3 OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK 3 )) OR RESID 109 THROUGH 135 OR (RESID 136
REMARK 3 THROUGH 138 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 139 THROUGH 149 OR (RESID 150 AND (NAME N
REMARK 3 OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK 3 )) OR RESID 151 OR (RESID 152 THROUGH 153
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR (RESID 154 AND (NAME N
REMARK 3 OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK 3 OR NAME CG )) OR (RESID 155 AND (NAME N
REMARK 3 OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK 3 )) OR RESID 156 OR (RESID 157 AND (NAME N
REMARK 3 OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK 3 )) OR RESID 158 THROUGH 166 OR (RESID 167
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 168 THROUGH 190
REMARK 3 OR (RESID 191 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 192 THROUGH 193 OR (RESID 194 AND (NAME N
REMARK 3 OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK 3 )) OR RESID 195 THROUGH 209 OR (RESID 210
REMARK 3 THROUGH 211 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 328))
REMARK 3 SELECTION : (CHAIN 'I' AND ((RESID 17 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 18 OR (RESID 19 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 20 THROUGH 26 OR (RESID 27 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 28 THROUGH 31 OR
REMARK 3 (RESID 32 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 33
REMARK 3 THROUGH 34 OR (RESID 35 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 36 THROUGH 38 OR (RESID 39
REMARK 3 THROUGH 41 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 42 OR
REMARK 3 (RESID 43 THROUGH 45 AND (NAME N OR NAME
REMARK 3 CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK 3 RESID 51 OR (RESID 52 THROUGH 53 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 54 THROUGH 56 OR
REMARK 3 (RESID 57 THROUGH 59 AND (NAME N OR NAME
REMARK 3 CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK 3 RESID 60 THROUGH 62 OR (RESID 63 THROUGH
REMARK 3 64 AND (NAME N OR NAME CA OR NAME C OR
REMARK 3 NAME O OR NAME CB )) OR RESID 65 THROUGH
REMARK 3 66 OR (RESID 67 THROUGH 71 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 72 OR (RESID 73 THROUGH 75 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 76 OR (RESID 77
REMARK 3 THROUGH 82 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 83 OR
REMARK 3 (RESID 84 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 85
REMARK 3 THROUGH 86 OR (RESID 87 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 88 OR (RESID 89 THROUGH 90 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 95 OR (RESID 96 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 97 THROUGH 98 OR
REMARK 3 (RESID 99 THROUGH 103 AND (NAME N OR NAME
REMARK 3 CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK 3 RESID 104 THROUGH 105 OR (RESID 106 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 107 OR (RESID 108 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 109 THROUGH 135 OR
REMARK 3 (RESID 136 THROUGH 138 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 139 THROUGH 140 OR (RESID 141
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 142 THROUGH 149
REMARK 3 OR (RESID 150 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 151 OR (RESID 152 THROUGH 153 AND (NAME N
REMARK 3 OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK 3 )) OR (RESID 154 AND (NAME N OR NAME CA
REMARK 3 OR NAME C OR NAME O OR NAME CB OR NAME CG
REMARK 3 )) OR (RESID 155 AND (NAME N OR NAME CA
REMARK 3 OR NAME C OR NAME O OR NAME CB )) OR
REMARK 3 RESID 156 OR (RESID 157 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 158 THROUGH 166 OR (RESID 167
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 168 THROUGH 190
REMARK 3 OR (RESID 191 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 192 THROUGH 193 OR (RESID 194 AND (NAME N
REMARK 3 OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK 3 )) OR RESID 195 THROUGH 209 OR (RESID 210
REMARK 3 THROUGH 211 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 316))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: (CHAIN 'G' AND ((RESID 17 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 18 THROUGH 26 OR (RESID 27 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 28 THROUGH 31 OR
REMARK 3 (RESID 32 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 33
REMARK 3 THROUGH 34 OR (RESID 35 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 36 THROUGH 38 OR (RESID 39
REMARK 3 THROUGH 41 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 42 OR
REMARK 3 (RESID 43 THROUGH 45 AND (NAME N OR NAME
REMARK 3 CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK 3 RESID 51 OR (RESID 52 THROUGH 53 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 54 THROUGH 56 OR
REMARK 3 (RESID 57 THROUGH 59 AND (NAME N OR NAME
REMARK 3 CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK 3 RESID 60 OR (RESID 61 AND (NAME N OR NAME
REMARK 3 CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK 3 RESID 62 OR (RESID 63 THROUGH 64 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 65 OR (RESID 66
REMARK 3 THROUGH 71 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 72 OR
REMARK 3 (RESID 73 THROUGH 75 AND (NAME N OR NAME
REMARK 3 CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK 3 RESID 76 OR (RESID 77 THROUGH 82 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 83 OR (RESID 84 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 85 OR (RESID 86
REMARK 3 THROUGH 87 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 88 OR
REMARK 3 (RESID 89 THROUGH 90 AND (NAME N OR NAME
REMARK 3 CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK 3 RESID 95 OR (RESID 96 AND (NAME N OR NAME
REMARK 3 CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK 3 RESID 97 THROUGH 100 OR (RESID 101
REMARK 3 THROUGH 103 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 104 THROUGH 105 OR (RESID 106 AND (NAME N
REMARK 3 OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK 3 )) OR RESID 107 OR (RESID 108 AND (NAME N
REMARK 3 OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK 3 )) OR RESID 109 THROUGH 135 OR (RESID 136
REMARK 3 THROUGH 138 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 139 THROUGH 149 OR (RESID 150 AND (NAME N
REMARK 3 OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK 3 )) OR RESID 151 OR (RESID 152 THROUGH 153
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR (RESID 154 AND (NAME N
REMARK 3 OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK 3 OR NAME CG )) OR (RESID 155 AND (NAME N
REMARK 3 OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK 3 )) OR RESID 156 OR (RESID 157 AND (NAME N
REMARK 3 OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK 3 )) OR RESID 158 THROUGH 166 OR (RESID 167
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 168 THROUGH 190
REMARK 3 OR (RESID 191 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 192 THROUGH 193 OR (RESID 194 AND (NAME N
REMARK 3 OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK 3 )) OR RESID 195 THROUGH 209 OR (RESID 210
REMARK 3 THROUGH 211 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 328))
REMARK 3 SELECTION : (CHAIN 'J' AND (RESID 17 THROUGH 18 OR
REMARK 3 (RESID 19 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 20
REMARK 3 THROUGH 26 OR (RESID 27 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 28 THROUGH 34 OR (RESID 35 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 36 THROUGH 38 OR
REMARK 3 (RESID 39 THROUGH 41 AND (NAME N OR NAME
REMARK 3 CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK 3 RESID 42 OR (RESID 43 THROUGH 45 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 51 THROUGH 57 OR
REMARK 3 (RESID 58 THROUGH 59 AND (NAME N OR NAME
REMARK 3 CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK 3 RESID 60 OR (RESID 61 AND (NAME N OR NAME
REMARK 3 CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK 3 RESID 62 OR (RESID 63 THROUGH 64 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 65 OR (RESID 66
REMARK 3 THROUGH 71 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 72
REMARK 3 THROUGH 90 OR RESID 95 THROUGH 101 OR
REMARK 3 (RESID 102 THROUGH 103 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 104 THROUGH 105 OR (RESID 106
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 107 THROUGH 190
REMARK 3 OR (RESID 191 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 192 THROUGH 209 OR (RESID 210 THROUGH 211
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 315))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: (CHAIN 'G' AND ((RESID 17 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 18 THROUGH 26 OR (RESID 27 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 28 THROUGH 31 OR
REMARK 3 (RESID 32 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 33
REMARK 3 THROUGH 34 OR (RESID 35 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 36 THROUGH 38 OR (RESID 39
REMARK 3 THROUGH 41 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 42 OR
REMARK 3 (RESID 43 THROUGH 45 AND (NAME N OR NAME
REMARK 3 CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK 3 RESID 51 OR (RESID 52 THROUGH 53 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 54 THROUGH 56 OR
REMARK 3 (RESID 57 THROUGH 59 AND (NAME N OR NAME
REMARK 3 CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK 3 RESID 60 OR (RESID 61 AND (NAME N OR NAME
REMARK 3 CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK 3 RESID 62 OR (RESID 63 THROUGH 64 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 65 OR (RESID 66
REMARK 3 THROUGH 71 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 72 OR
REMARK 3 (RESID 73 THROUGH 75 AND (NAME N OR NAME
REMARK 3 CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK 3 RESID 76 OR (RESID 77 THROUGH 82 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 83 OR (RESID 84 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 85 OR (RESID 86
REMARK 3 THROUGH 87 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 88 OR
REMARK 3 (RESID 89 THROUGH 90 AND (NAME N OR NAME
REMARK 3 CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK 3 RESID 95 OR (RESID 96 AND (NAME N OR NAME
REMARK 3 CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK 3 RESID 97 THROUGH 100 OR (RESID 101
REMARK 3 THROUGH 103 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 104 THROUGH 105 OR (RESID 106 AND (NAME N
REMARK 3 OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK 3 )) OR RESID 107 OR (RESID 108 AND (NAME N
REMARK 3 OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK 3 )) OR RESID 109 THROUGH 135 OR (RESID 136
REMARK 3 THROUGH 138 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 139 THROUGH 149 OR (RESID 150 AND (NAME N
REMARK 3 OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK 3 )) OR RESID 151 OR (RESID 152 THROUGH 153
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR (RESID 154 AND (NAME N
REMARK 3 OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK 3 OR NAME CG )) OR (RESID 155 AND (NAME N
REMARK 3 OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK 3 )) OR RESID 156 OR (RESID 157 AND (NAME N
REMARK 3 OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK 3 )) OR RESID 158 THROUGH 166 OR (RESID 167
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 168 THROUGH 190
REMARK 3 OR (RESID 191 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 192 THROUGH 193 OR (RESID 194 AND (NAME N
REMARK 3 OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK 3 )) OR RESID 195 THROUGH 209 OR (RESID 210
REMARK 3 THROUGH 211 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 328))
REMARK 3 SELECTION : (CHAIN 'K' AND (RESID 17 THROUGH 18 OR
REMARK 3 (RESID 19 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 20
REMARK 3 THROUGH 43 OR (RESID 44 THROUGH 45 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 51 OR (RESID 52
REMARK 3 THROUGH 53 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 54
REMARK 3 THROUGH 56 OR (RESID 57 THROUGH 59 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 60 THROUGH 63 OR
REMARK 3 (RESID 64 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 65 OR
REMARK 3 (RESID 66 THROUGH 71 AND (NAME N OR NAME
REMARK 3 CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK 3 RESID 72 OR (RESID 73 THROUGH 75 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 76 OR (RESID 77
REMARK 3 THROUGH 82 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 83
REMARK 3 THROUGH 85 OR (RESID 86 THROUGH 87 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 88 OR (RESID 89
REMARK 3 THROUGH 90 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 95
REMARK 3 THROUGH 149 OR (RESID 150 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 151 THROUGH 153 OR (RESID 154
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB OR NAME CG )) OR RESID 155
REMARK 3 THROUGH 156 OR (RESID 157 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 158 THROUGH 312))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6P67 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JUN-19.
REMARK 100 THE DEPOSITION ID IS D_1000241897.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-APR-17
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 : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.03320
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70309
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.4100
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 (%) : 98.7
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.080
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: 3DI3 FOR IL-7R AND 6P4Y FOR 2B8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 17% PEG 3350, 10% MPD, 0.2 LITHIUM
REMARK 280 SULFATE, 0.1 M IMIDAZOLE PH 6.5, 20% GLYCEROL, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 109.84000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, K
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 APPLY THE FOLLOWING TO CHAINS: C, D, J, O
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 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, I, N
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, L, M
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 ASP A 224
REMARK 465 LYS A 225
REMARK 465 CYS B 214
REMARK 465 ASP C 224
REMARK 465 LYS C 225
REMARK 465 CYS D 214
REMARK 465 SER E 137
REMARK 465 THR E 138
REMARK 465 SER E 139
REMARK 465 ASP E 224
REMARK 465 LYS E 225
REMARK 465 CYS F 214
REMARK 465 GLY G -3
REMARK 465 SER G -2
REMARK 465 HIS G -1
REMARK 465 MET G 0
REMARK 465 GLU G 1
REMARK 465 SER G 2
REMARK 465 GLY G 3
REMARK 465 TYR G 4
REMARK 465 ALA G 5
REMARK 465 GLN G 6
REMARK 465 ASN G 7
REMARK 465 GLY G 8
REMARK 465 ASP G 9
REMARK 465 LEU G 10
REMARK 465 GLU G 11
REMARK 465 ASP G 12
REMARK 465 ALA G 13
REMARK 465 GLU G 14
REMARK 465 LEU G 15
REMARK 465 ASP G 16
REMARK 465 ASN G 212
REMARK 465 ASN G 213
REMARK 465 SER G 214
REMARK 465 SER G 215
REMARK 465 GLY G 216
REMARK 465 GLU G 217
REMARK 465 MET G 218
REMARK 465 ASP G 219
REMARK 465 ASP H 224
REMARK 465 LYS H 225
REMARK 465 GLY I -3
REMARK 465 SER I -2
REMARK 465 HIS I -1
REMARK 465 MET I 0
REMARK 465 GLU I 1
REMARK 465 SER I 2
REMARK 465 GLY I 3
REMARK 465 TYR I 4
REMARK 465 ALA I 5
REMARK 465 GLN I 6
REMARK 465 ASN I 7
REMARK 465 GLY I 8
REMARK 465 ASP I 9
REMARK 465 LEU I 10
REMARK 465 GLU I 11
REMARK 465 ASP I 12
REMARK 465 ALA I 13
REMARK 465 GLU I 14
REMARK 465 LEU I 15
REMARK 465 ASP I 16
REMARK 465 THR I 46
REMARK 465 THR I 47
REMARK 465 ASN I 212
REMARK 465 ASN I 213
REMARK 465 SER I 214
REMARK 465 SER I 215
REMARK 465 GLY I 216
REMARK 465 GLU I 217
REMARK 465 MET I 218
REMARK 465 ASP I 219
REMARK 465 GLY J -3
REMARK 465 SER J -2
REMARK 465 HIS J -1
REMARK 465 MET J 0
REMARK 465 GLU J 1
REMARK 465 SER J 2
REMARK 465 GLY J 3
REMARK 465 TYR J 4
REMARK 465 ALA J 5
REMARK 465 GLN J 6
REMARK 465 ASN J 7
REMARK 465 GLY J 8
REMARK 465 ASP J 9
REMARK 465 LEU J 10
REMARK 465 GLU J 11
REMARK 465 ASP J 12
REMARK 465 ALA J 13
REMARK 465 GLU J 14
REMARK 465 LEU J 15
REMARK 465 ASP J 16
REMARK 465 ASN J 212
REMARK 465 ASN J 213
REMARK 465 SER J 214
REMARK 465 SER J 215
REMARK 465 GLY J 216
REMARK 465 GLU J 217
REMARK 465 MET J 218
REMARK 465 ASP J 219
REMARK 465 GLY K -3
REMARK 465 SER K -2
REMARK 465 HIS K -1
REMARK 465 MET K 0
REMARK 465 GLU K 1
REMARK 465 SER K 2
REMARK 465 GLY K 3
REMARK 465 TYR K 4
REMARK 465 ALA K 5
REMARK 465 GLN K 6
REMARK 465 ASN K 7
REMARK 465 GLY K 8
REMARK 465 ASP K 9
REMARK 465 LEU K 10
REMARK 465 GLU K 11
REMARK 465 ASP K 12
REMARK 465 ALA K 13
REMARK 465 GLU K 14
REMARK 465 LEU K 15
REMARK 465 ASP K 16
REMARK 465 ASN K 48
REMARK 465 LEU K 49
REMARK 465 GLU K 50
REMARK 465 VAL K 91
REMARK 465 GLY K 92
REMARK 465 GLU K 93
REMARK 465 LYS K 94
REMARK 465 ASN K 212
REMARK 465 ASN K 213
REMARK 465 SER K 214
REMARK 465 SER K 215
REMARK 465 GLY K 216
REMARK 465 GLU K 217
REMARK 465 MET K 218
REMARK 465 ASP K 219
REMARK 465 CYS L 214
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 GLU A 1 CG CD OE1 OE2
REMARK 470 LYS A 13 CG CD CE NZ
REMARK 470 HIS A 41 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 65 CG CD CE NZ
REMARK 470 LYS A 67 CG CD CE NZ
REMARK 470 LYS A 136 CG CD CE NZ
REMARK 470 LYS C 43 CG CD CE NZ
REMARK 470 LYS C 65 CG CD CE NZ
REMARK 470 LYS C 67 CG CD CE NZ
REMARK 470 ARG C 84 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 136 CG CD CE NZ
REMARK 470 GLU E 1 CG CD OE1 OE2
REMARK 470 ASN E 58 CG OD1 ND2
REMARK 470 GLN E 62 CG CD OE1 NE2
REMARK 470 LYS E 67 CG CD CE NZ
REMARK 470 ARG E 84 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 136 CG CD CE NZ
REMARK 470 LYS E 208 CG CD CE NZ
REMARK 470 LYS E 213 CG CD CE NZ
REMARK 470 GLU F 213 CG CD OE1 OE2
REMARK 470 SER G 19 OG
REMARK 470 ASN G 48 CG OD1 ND2
REMARK 470 GLU G 59 CG CD OE1 OE2
REMARK 470 LYS G 67 CD CE NZ
REMARK 470 GLN G 69 CG CD OE1 NE2
REMARK 470 GLU G 70 CG CD OE1 OE2
REMARK 470 LYS G 78 CG CD CE NZ
REMARK 470 LYS G 94 CG CD CE NZ
REMARK 470 LYS G 99 CG CD CE NZ
REMARK 470 LYS G 100 CG CD CE NZ
REMARK 470 LYS G 141 CG CD CE NZ
REMARK 470 LYS G 194 CD CE NZ
REMARK 470 GLU H 1 CG CD OE1 OE2
REMARK 470 LYS H 67 CG CD CE NZ
REMARK 470 LYS H 136 CG CD CE NZ
REMARK 470 ASN I 48 CG OD1 ND2
REMARK 470 GLU I 59 CG CD OE1 OE2
REMARK 470 LYS I 61 CG CD CE NZ
REMARK 470 ARG I 66 CG CD NE CZ NH1 NH2
REMARK 470 LYS I 67 CD CE NZ
REMARK 470 GLU I 70 CG CD OE1 OE2
REMARK 470 LEU I 80 CG CD1 CD2
REMARK 470 ILE I 82 CG1 CG2 CD1
REMARK 470 ASN I 86 CG OD1 ND2
REMARK 470 LYS I 90 CG CD CE NZ
REMARK 470 LYS I 94 CG CD CE NZ
REMARK 470 ILE I 211 CG1 CG2 CD1
REMARK 470 ASP J 17 CG OD1 OD2
REMARK 470 GLN J 32 CG CD OE1 NE2
REMARK 470 GLU J 40 CG CD OE1 OE2
REMARK 470 ASP J 41 CG OD1 OD2
REMARK 470 VAL J 44 CG1 CG2
REMARK 470 ASN J 45 CG OD1 ND2
REMARK 470 THR J 47 OG1 CG2
REMARK 470 ASN J 48 CG OD1 ND2
REMARK 470 GLU J 50 CG CD OE1 OE2
REMARK 470 GLU J 52 CG CD OE1 OE2
REMARK 470 ILE J 53 CG1 CG2 CD1
REMARK 470 LEU J 57 CG CD1 CD2
REMARK 470 ASN J 64 CG OD1 ND2
REMARK 470 LYS J 67 CG CD CE NZ
REMARK 470 GLN J 69 CG CD OE1 NE2
REMARK 470 PHE J 73 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE J 74 CG1 CG2 CD1
REMARK 470 GLU J 75 CG CD OE1 OE2
REMARK 470 LYS J 77 CG CD CE NZ
REMARK 470 LYS J 78 CG CD CE NZ
REMARK 470 PHE J 79 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU J 80 CG CD1 CD2
REMARK 470 LEU J 81 CG CD1 CD2
REMARK 470 ILE J 82 CG1 CG2 CD1
REMARK 470 LYS J 84 CG CD CE NZ
REMARK 470 ASN J 86 CG OD1 ND2
REMARK 470 ILE J 87 CG1 CG2 CD1
REMARK 470 VAL J 89 CG1 CG2
REMARK 470 LYS J 90 CG CD CE NZ
REMARK 470 VAL J 91 CG1 CG2
REMARK 470 GLU J 93 CG CD OE1 OE2
REMARK 470 LYS J 94 CG CD CE NZ
REMARK 470 LEU J 96 CG CD1 CD2
REMARK 470 LYS J 99 CG CD CE NZ
REMARK 470 LYS J 100 CG CD CE NZ
REMARK 470 ILE J 101 CG1 CG2 CD1
REMARK 470 LEU J 103 CG CD1 CD2
REMARK 470 LYS J 108 CG CD CE NZ
REMARK 470 GLN J 136 CG CD OE1 NE2
REMARK 470 LYS J 137 CG CD CE NZ
REMARK 470 LYS J 138 CG CD CE NZ
REMARK 470 LYS J 141 CG CD CE NZ
REMARK 470 ARG J 150 CG CD NE CZ NH1 NH2
REMARK 470 GLU J 152 CG CD OE1 OE2
REMARK 470 LYS J 153 CG CD CE NZ
REMARK 470 ASP J 154 OD1 OD2
REMARK 470 GLU J 155 CG CD OE1 OE2
REMARK 470 LYS J 157 CG CD CE NZ
REMARK 470 LYS J 167 CG CD CE NZ
REMARK 470 LYS J 194 CG CD CE NZ
REMARK 470 ASP K 17 CG OD1 OD2
REMARK 470 GLU K 27 CG CD OE1 OE2
REMARK 470 GLN K 32 CG CD OE1 NE2
REMARK 470 LEU K 35 CG CD1 CD2
REMARK 470 PHE K 39 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU K 40 CG CD OE1 OE2
REMARK 470 ASP K 41 CG OD1 OD2
REMARK 470 ASP K 43 CG OD1 OD2
REMARK 470 ASN K 45 CG OD1 ND2
REMARK 470 THR K 47 OG1 CG2
REMARK 470 VAL K 58 CG1 CG2
REMARK 470 GLU K 59 CG CD OE1 OE2
REMARK 470 LYS K 61 CG CD CE NZ
REMARK 470 LEU K 63 CG CD1 CD2
REMARK 470 LYS K 67 CG CD CE NZ
REMARK 470 LEU K 68 CG CD1 CD2
REMARK 470 GLN K 69 CG CD OE1 NE2
REMARK 470 ILE K 71 CG1 CG2 CD1
REMARK 470 GLU K 75 CG CD OE1 OE2
REMARK 470 LYS K 78 CG CD CE NZ
REMARK 470 LEU K 80 CG CD1 CD2
REMARK 470 LEU K 81 CG CD1 CD2
REMARK 470 LYS K 84 CG CD CE NZ
REMARK 470 ILE K 87 CG1 CG2 CD1
REMARK 470 LYS K 90 CG CD CE NZ
REMARK 470 LEU K 96 CG CD1 CD2
REMARK 470 LYS K 99 CG CD CE NZ
REMARK 470 LYS K 100 CG CD CE NZ
REMARK 470 ILE K 101 CG1 CG2 CD1
REMARK 470 ASP K 102 CG OD1 OD2
REMARK 470 LEU K 103 CG CD1 CD2
REMARK 470 ILE K 106 CG1 CG2 CD1
REMARK 470 LYS K 108 CG CD CE NZ
REMARK 470 GLN K 136 CG CD OE1 NE2
REMARK 470 LYS K 137 CG CD CE NZ
REMARK 470 LYS K 138 CG CD CE NZ
REMARK 470 LYS K 141 CG CD CE NZ
REMARK 470 GLU K 152 CG CD OE1 OE2
REMARK 470 LYS K 153 CG CD CE NZ
REMARK 470 GLU K 155 CG CD OE1 OE2
REMARK 470 LYS K 167 CG CD CE NZ
REMARK 470 HIS K 191 CG ND1 CD2 CE1 NE2
REMARK 470 LYS K 194 CG CD CE NZ
REMARK 470 GLU K 210 CG CD OE1 OE2
REMARK 470 ILE K 211 CG1 CG2 CD1
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 O4 NAG N 2 O5 BMA N 3 2.15
REMARK 500 O ASP H 90 N ALA H 92 2.16
REMARK 500 O4 NAG N 1 O5 NAG N 2 2.18
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 O SER H 179 O4 NAG I 301 2646 1.99
REMARK 500 OD2 ASP E 103 OH TYR I 204 1554 2.00
REMARK 500 OH TYR G 204 OD2 ASP H 103 1554 2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG F 18 NE - CZ - NH1 ANGL. DEV. = -4.0 DEGREES
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 A 55 -91.64 -140.57
REMARK 500 TYR A 60 123.02 52.05
REMARK 500 LEU A 83 -86.06 -98.97
REMARK 500 ASP A 90 -75.30 -73.30
REMARK 500 SER A 91 56.63 -60.84
REMARK 500 SER A 105 -78.00 -36.31
REMARK 500 SER A 137 68.01 -106.40
REMARK 500 ASP A 151 76.85 55.08
REMARK 500 SER B 30 -135.62 53.68
REMARK 500 ALA B 51 -47.33 70.69
REMARK 500 HIS B 91 52.13 -103.03
REMARK 500 ASN B 138 70.23 53.25
REMARK 500 ASN C 55 -93.00 -139.83
REMARK 500 TYR C 60 127.32 27.23
REMARK 500 LYS C 65 51.34 -93.17
REMARK 500 ARG C 84 73.79 52.67
REMARK 500 GLU C 89 2.26 -68.65
REMARK 500 SER C 91 74.48 24.89
REMARK 500 ASP C 103 86.07 72.32
REMARK 500 SER C 105 11.15 81.80
REMARK 500 ASP C 151 76.24 54.30
REMARK 500 SER D 30 -136.25 53.32
REMARK 500 THR D 32 79.97 -100.62
REMARK 500 ALA D 51 -47.89 70.39
REMARK 500 HIS D 91 52.16 -103.18
REMARK 500 HIS E 41 29.69 48.48
REMARK 500 LYS E 43 -81.86 -131.33
REMARK 500 ASN E 55 -88.15 -141.75
REMARK 500 LYS E 65 51.66 -91.32
REMARK 500 ARG E 84 72.41 42.23
REMARK 500 ASP E 90 -88.18 -67.11
REMARK 500 SER E 91 70.62 -56.36
REMARK 500 ASP E 103 75.00 75.18
REMARK 500 SER E 105 8.49 83.80
REMARK 500 ASP E 151 75.34 55.67
REMARK 500 THR E 198 -73.41 -107.88
REMARK 500 SER F 30 -136.42 53.61
REMARK 500 THR F 32 79.72 -100.38
REMARK 500 ALA F 51 -47.25 70.85
REMARK 500 HIS F 91 51.82 -103.40
REMARK 500 THR G 47 -129.00 51.42
REMARK 500 ALA G 56 73.19 40.15
REMARK 500 VAL G 60 98.78 -41.55
REMARK 500 LYS G 61 -142.96 -151.41
REMARK 500 GLN G 69 -177.17 57.94
REMARK 500 GLU G 70 45.14 -68.98
REMARK 500 LEU G 81 -20.79 -147.73
REMARK 500 LYS G 94 173.67 63.79
REMARK 500 SER G 165 -158.53 -80.70
REMARK 500 ASP G 190 52.31 -146.46
REMARK 500
REMARK 500 THIS ENTRY HAS 90 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 FUC G 304
DBREF 6P67 A 1 225 PDB 6P67 6P67 1 225
DBREF 6P67 B 1 214 PDB 6P67 6P67 1 214
DBREF 6P67 C 1 225 PDB 6P67 6P67 1 225
DBREF 6P67 D 1 214 PDB 6P67 6P67 1 214
DBREF 6P67 E 1 225 PDB 6P67 6P67 1 225
DBREF 6P67 F 1 214 PDB 6P67 6P67 1 214
DBREF 6P67 G 1 219 UNP P16871 IL7RA_HUMAN 21 239
DBREF 6P67 H 1 225 PDB 6P67 6P67 1 225
DBREF 6P67 I 1 219 UNP P16871 IL7RA_HUMAN 21 239
DBREF 6P67 J 1 219 UNP P16871 IL7RA_HUMAN 21 239
DBREF 6P67 K 1 219 UNP P16871 IL7RA_HUMAN 21 239
DBREF 6P67 L 1 214 PDB 6P67 6P67 1 214
SEQADV 6P67 GLY G -3 UNP P16871 EXPRESSION TAG
SEQADV 6P67 SER G -2 UNP P16871 EXPRESSION TAG
SEQADV 6P67 HIS G -1 UNP P16871 EXPRESSION TAG
SEQADV 6P67 MET G 0 UNP P16871 EXPRESSION TAG
SEQADV 6P67 THR G 46 UNP P16871 ILE 66 CONFLICT
SEQADV 6P67 GLY I -3 UNP P16871 EXPRESSION TAG
SEQADV 6P67 SER I -2 UNP P16871 EXPRESSION TAG
SEQADV 6P67 HIS I -1 UNP P16871 EXPRESSION TAG
SEQADV 6P67 MET I 0 UNP P16871 EXPRESSION TAG
SEQADV 6P67 THR I 46 UNP P16871 ILE 66 CONFLICT
SEQADV 6P67 GLY J -3 UNP P16871 EXPRESSION TAG
SEQADV 6P67 SER J -2 UNP P16871 EXPRESSION TAG
SEQADV 6P67 HIS J -1 UNP P16871 EXPRESSION TAG
SEQADV 6P67 MET J 0 UNP P16871 EXPRESSION TAG
SEQADV 6P67 THR J 46 UNP P16871 ILE 66 CONFLICT
SEQADV 6P67 GLY K -3 UNP P16871 EXPRESSION TAG
SEQADV 6P67 SER K -2 UNP P16871 EXPRESSION TAG
SEQADV 6P67 HIS K -1 UNP P16871 EXPRESSION TAG
SEQADV 6P67 MET K 0 UNP P16871 EXPRESSION TAG
SEQADV 6P67 THR K 46 UNP P16871 ILE 66 CONFLICT
SEQRES 1 A 225 GLU VAL GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS
SEQRES 2 A 225 PRO GLY ALA SER VAL LYS MET SER CYS LYS ALA SER GLY
SEQRES 3 A 225 TYR THR PHE SER ASP TYR TYR MET HIS TRP VAL LYS GLN
SEQRES 4 A 225 SER HIS GLY LYS SER LEU GLU TRP ILE GLY TYR ILE TYR
SEQRES 5 A 225 PRO ASP ASN GLY GLY ASN GLY TYR ASN GLN LYS PHE LYS
SEQRES 6 A 225 GLY LYS ALA THR LEU THR VAL ASP LYS SER SER SER THR
SEQRES 7 A 225 VAL TYR MET GLU LEU ARG SER LEU THR SER GLU ASP SER
SEQRES 8 A 225 ALA LEU TYR TYR CYS ALA ARG GLY THR TYR TYR ASP GLY
SEQRES 9 A 225 SER TYR PHE ASP TYR TRP GLY GLN GLY THR THR LEU THR
SEQRES 10 A 225 VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO
SEQRES 11 A 225 LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA
SEQRES 12 A 225 ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO
SEQRES 13 A 225 VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY
SEQRES 14 A 225 VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU
SEQRES 15 A 225 TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER
SEQRES 16 A 225 LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS
SEQRES 17 A 225 PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS
SEQRES 18 A 225 SER CYS ASP LYS
SEQRES 1 B 214 ASP ILE VAL MET THR GLN SER HIS LYS PHE MET SER THR
SEQRES 2 B 214 LEU VAL GLY ASP ARG VAL SER ILE THR CYS LYS ALA SER
SEQRES 3 B 214 GLN ASP VAL SER THR THR VAL ALA TRP TYR GLN GLN LYS
SEQRES 4 B 214 PRO GLY GLN SER PRO LYS LEU LEU ILE TYR SER ALA SER
SEQRES 5 B 214 TYR ARG TYR THR GLY VAL PRO ASP ARG PHE THR GLY SER
SEQRES 6 B 214 GLY SER GLY THR ASP PHE THR PHE THR ILE SER SER VAL
SEQRES 7 B 214 GLN ALA GLU ASP LEU ALA VAL TYR TYR CYS GLN GLN HIS
SEQRES 8 B 214 TYR SER ILE PRO ARG THR PHE GLY GLY GLY THR LYS LEU
SEQRES 9 B 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE
SEQRES 10 B 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA
SEQRES 11 B 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU
SEQRES 12 B 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER
SEQRES 13 B 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS
SEQRES 14 B 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER
SEQRES 15 B 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU
SEQRES 16 B 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER
SEQRES 17 B 214 PHE ASN ARG GLY GLU CYS
SEQRES 1 C 225 GLU VAL GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS
SEQRES 2 C 225 PRO GLY ALA SER VAL LYS MET SER CYS LYS ALA SER GLY
SEQRES 3 C 225 TYR THR PHE SER ASP TYR TYR MET HIS TRP VAL LYS GLN
SEQRES 4 C 225 SER HIS GLY LYS SER LEU GLU TRP ILE GLY TYR ILE TYR
SEQRES 5 C 225 PRO ASP ASN GLY GLY ASN GLY TYR ASN GLN LYS PHE LYS
SEQRES 6 C 225 GLY LYS ALA THR LEU THR VAL ASP LYS SER SER SER THR
SEQRES 7 C 225 VAL TYR MET GLU LEU ARG SER LEU THR SER GLU ASP SER
SEQRES 8 C 225 ALA LEU TYR TYR CYS ALA ARG GLY THR TYR TYR ASP GLY
SEQRES 9 C 225 SER TYR PHE ASP TYR TRP GLY GLN GLY THR THR LEU THR
SEQRES 10 C 225 VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO
SEQRES 11 C 225 LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA
SEQRES 12 C 225 ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO
SEQRES 13 C 225 VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY
SEQRES 14 C 225 VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU
SEQRES 15 C 225 TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER
SEQRES 16 C 225 LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS
SEQRES 17 C 225 PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS
SEQRES 18 C 225 SER CYS ASP LYS
SEQRES 1 D 214 ASP ILE VAL MET THR GLN SER HIS LYS PHE MET SER THR
SEQRES 2 D 214 LEU VAL GLY ASP ARG VAL SER ILE THR CYS LYS ALA SER
SEQRES 3 D 214 GLN ASP VAL SER THR THR VAL ALA TRP TYR GLN GLN LYS
SEQRES 4 D 214 PRO GLY GLN SER PRO LYS LEU LEU ILE TYR SER ALA SER
SEQRES 5 D 214 TYR ARG TYR THR GLY VAL PRO ASP ARG PHE THR GLY SER
SEQRES 6 D 214 GLY SER GLY THR ASP PHE THR PHE THR ILE SER SER VAL
SEQRES 7 D 214 GLN ALA GLU ASP LEU ALA VAL TYR TYR CYS GLN GLN HIS
SEQRES 8 D 214 TYR SER ILE PRO ARG THR PHE GLY GLY GLY THR LYS LEU
SEQRES 9 D 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE
SEQRES 10 D 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA
SEQRES 11 D 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU
SEQRES 12 D 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER
SEQRES 13 D 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS
SEQRES 14 D 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER
SEQRES 15 D 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU
SEQRES 16 D 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER
SEQRES 17 D 214 PHE ASN ARG GLY GLU CYS
SEQRES 1 E 225 GLU VAL GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS
SEQRES 2 E 225 PRO GLY ALA SER VAL LYS MET SER CYS LYS ALA SER GLY
SEQRES 3 E 225 TYR THR PHE SER ASP TYR TYR MET HIS TRP VAL LYS GLN
SEQRES 4 E 225 SER HIS GLY LYS SER LEU GLU TRP ILE GLY TYR ILE TYR
SEQRES 5 E 225 PRO ASP ASN GLY GLY ASN GLY TYR ASN GLN LYS PHE LYS
SEQRES 6 E 225 GLY LYS ALA THR LEU THR VAL ASP LYS SER SER SER THR
SEQRES 7 E 225 VAL TYR MET GLU LEU ARG SER LEU THR SER GLU ASP SER
SEQRES 8 E 225 ALA LEU TYR TYR CYS ALA ARG GLY THR TYR TYR ASP GLY
SEQRES 9 E 225 SER TYR PHE ASP TYR TRP GLY GLN GLY THR THR LEU THR
SEQRES 10 E 225 VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO
SEQRES 11 E 225 LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA
SEQRES 12 E 225 ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO
SEQRES 13 E 225 VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY
SEQRES 14 E 225 VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU
SEQRES 15 E 225 TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER
SEQRES 16 E 225 LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS
SEQRES 17 E 225 PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS
SEQRES 18 E 225 SER CYS ASP LYS
SEQRES 1 F 214 ASP ILE VAL MET THR GLN SER HIS LYS PHE MET SER THR
SEQRES 2 F 214 LEU VAL GLY ASP ARG VAL SER ILE THR CYS LYS ALA SER
SEQRES 3 F 214 GLN ASP VAL SER THR THR VAL ALA TRP TYR GLN GLN LYS
SEQRES 4 F 214 PRO GLY GLN SER PRO LYS LEU LEU ILE TYR SER ALA SER
SEQRES 5 F 214 TYR ARG TYR THR GLY VAL PRO ASP ARG PHE THR GLY SER
SEQRES 6 F 214 GLY SER GLY THR ASP PHE THR PHE THR ILE SER SER VAL
SEQRES 7 F 214 GLN ALA GLU ASP LEU ALA VAL TYR TYR CYS GLN GLN HIS
SEQRES 8 F 214 TYR SER ILE PRO ARG THR PHE GLY GLY GLY THR LYS LEU
SEQRES 9 F 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE
SEQRES 10 F 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA
SEQRES 11 F 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU
SEQRES 12 F 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER
SEQRES 13 F 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS
SEQRES 14 F 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER
SEQRES 15 F 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU
SEQRES 16 F 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER
SEQRES 17 F 214 PHE ASN ARG GLY GLU CYS
SEQRES 1 G 223 GLY SER HIS MET GLU SER GLY TYR ALA GLN ASN GLY ASP
SEQRES 2 G 223 LEU GLU ASP ALA GLU LEU ASP ASP TYR SER PHE SER CYS
SEQRES 3 G 223 TYR SER GLN LEU GLU VAL ASN GLY SER GLN HIS SER LEU
SEQRES 4 G 223 THR CYS ALA PHE GLU ASP PRO ASP VAL ASN THR THR ASN
SEQRES 5 G 223 LEU GLU PHE GLU ILE CYS GLY ALA LEU VAL GLU VAL LYS
SEQRES 6 G 223 CYS LEU ASN PHE ARG LYS LEU GLN GLU ILE TYR PHE ILE
SEQRES 7 G 223 GLU THR LYS LYS PHE LEU LEU ILE GLY LYS SER ASN ILE
SEQRES 8 G 223 CYS VAL LYS VAL GLY GLU LYS SER LEU THR CYS LYS LYS
SEQRES 9 G 223 ILE ASP LEU THR THR ILE VAL LYS PRO GLU ALA PRO PHE
SEQRES 10 G 223 ASP LEU SER VAL VAL TYR ARG GLU GLY ALA ASN ASP PHE
SEQRES 11 G 223 VAL VAL THR PHE ASN THR SER HIS LEU GLN LYS LYS TYR
SEQRES 12 G 223 VAL LYS VAL LEU MET HIS ASP VAL ALA TYR ARG GLN GLU
SEQRES 13 G 223 LYS ASP GLU ASN LYS TRP THR HIS VAL ASN LEU SER SER
SEQRES 14 G 223 THR LYS LEU THR LEU LEU GLN ARG LYS LEU GLN PRO ALA
SEQRES 15 G 223 ALA MET TYR GLU ILE LYS VAL ARG SER ILE PRO ASP HIS
SEQRES 16 G 223 TYR PHE LYS GLY PHE TRP SER GLU TRP SER PRO SER TYR
SEQRES 17 G 223 TYR PHE ARG THR PRO GLU ILE ASN ASN SER SER GLY GLU
SEQRES 18 G 223 MET ASP
SEQRES 1 H 225 GLU VAL GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS
SEQRES 2 H 225 PRO GLY ALA SER VAL LYS MET SER CYS LYS ALA SER GLY
SEQRES 3 H 225 TYR THR PHE SER ASP TYR TYR MET HIS TRP VAL LYS GLN
SEQRES 4 H 225 SER HIS GLY LYS SER LEU GLU TRP ILE GLY TYR ILE TYR
SEQRES 5 H 225 PRO ASP ASN GLY GLY ASN GLY TYR ASN GLN LYS PHE LYS
SEQRES 6 H 225 GLY LYS ALA THR LEU THR VAL ASP LYS SER SER SER THR
SEQRES 7 H 225 VAL TYR MET GLU LEU ARG SER LEU THR SER GLU ASP SER
SEQRES 8 H 225 ALA LEU TYR TYR CYS ALA ARG GLY THR TYR TYR ASP GLY
SEQRES 9 H 225 SER TYR PHE ASP TYR TRP GLY GLN GLY THR THR LEU THR
SEQRES 10 H 225 VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO
SEQRES 11 H 225 LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA
SEQRES 12 H 225 ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO
SEQRES 13 H 225 VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY
SEQRES 14 H 225 VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU
SEQRES 15 H 225 TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER
SEQRES 16 H 225 LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS
SEQRES 17 H 225 PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS
SEQRES 18 H 225 SER CYS ASP LYS
SEQRES 1 I 223 GLY SER HIS MET GLU SER GLY TYR ALA GLN ASN GLY ASP
SEQRES 2 I 223 LEU GLU ASP ALA GLU LEU ASP ASP TYR SER PHE SER CYS
SEQRES 3 I 223 TYR SER GLN LEU GLU VAL ASN GLY SER GLN HIS SER LEU
SEQRES 4 I 223 THR CYS ALA PHE GLU ASP PRO ASP VAL ASN THR THR ASN
SEQRES 5 I 223 LEU GLU PHE GLU ILE CYS GLY ALA LEU VAL GLU VAL LYS
SEQRES 6 I 223 CYS LEU ASN PHE ARG LYS LEU GLN GLU ILE TYR PHE ILE
SEQRES 7 I 223 GLU THR LYS LYS PHE LEU LEU ILE GLY LYS SER ASN ILE
SEQRES 8 I 223 CYS VAL LYS VAL GLY GLU LYS SER LEU THR CYS LYS LYS
SEQRES 9 I 223 ILE ASP LEU THR THR ILE VAL LYS PRO GLU ALA PRO PHE
SEQRES 10 I 223 ASP LEU SER VAL VAL TYR ARG GLU GLY ALA ASN ASP PHE
SEQRES 11 I 223 VAL VAL THR PHE ASN THR SER HIS LEU GLN LYS LYS TYR
SEQRES 12 I 223 VAL LYS VAL LEU MET HIS ASP VAL ALA TYR ARG GLN GLU
SEQRES 13 I 223 LYS ASP GLU ASN LYS TRP THR HIS VAL ASN LEU SER SER
SEQRES 14 I 223 THR LYS LEU THR LEU LEU GLN ARG LYS LEU GLN PRO ALA
SEQRES 15 I 223 ALA MET TYR GLU ILE LYS VAL ARG SER ILE PRO ASP HIS
SEQRES 16 I 223 TYR PHE LYS GLY PHE TRP SER GLU TRP SER PRO SER TYR
SEQRES 17 I 223 TYR PHE ARG THR PRO GLU ILE ASN ASN SER SER GLY GLU
SEQRES 18 I 223 MET ASP
SEQRES 1 J 223 GLY SER HIS MET GLU SER GLY TYR ALA GLN ASN GLY ASP
SEQRES 2 J 223 LEU GLU ASP ALA GLU LEU ASP ASP TYR SER PHE SER CYS
SEQRES 3 J 223 TYR SER GLN LEU GLU VAL ASN GLY SER GLN HIS SER LEU
SEQRES 4 J 223 THR CYS ALA PHE GLU ASP PRO ASP VAL ASN THR THR ASN
SEQRES 5 J 223 LEU GLU PHE GLU ILE CYS GLY ALA LEU VAL GLU VAL LYS
SEQRES 6 J 223 CYS LEU ASN PHE ARG LYS LEU GLN GLU ILE TYR PHE ILE
SEQRES 7 J 223 GLU THR LYS LYS PHE LEU LEU ILE GLY LYS SER ASN ILE
SEQRES 8 J 223 CYS VAL LYS VAL GLY GLU LYS SER LEU THR CYS LYS LYS
SEQRES 9 J 223 ILE ASP LEU THR THR ILE VAL LYS PRO GLU ALA PRO PHE
SEQRES 10 J 223 ASP LEU SER VAL VAL TYR ARG GLU GLY ALA ASN ASP PHE
SEQRES 11 J 223 VAL VAL THR PHE ASN THR SER HIS LEU GLN LYS LYS TYR
SEQRES 12 J 223 VAL LYS VAL LEU MET HIS ASP VAL ALA TYR ARG GLN GLU
SEQRES 13 J 223 LYS ASP GLU ASN LYS TRP THR HIS VAL ASN LEU SER SER
SEQRES 14 J 223 THR LYS LEU THR LEU LEU GLN ARG LYS LEU GLN PRO ALA
SEQRES 15 J 223 ALA MET TYR GLU ILE LYS VAL ARG SER ILE PRO ASP HIS
SEQRES 16 J 223 TYR PHE LYS GLY PHE TRP SER GLU TRP SER PRO SER TYR
SEQRES 17 J 223 TYR PHE ARG THR PRO GLU ILE ASN ASN SER SER GLY GLU
SEQRES 18 J 223 MET ASP
SEQRES 1 K 223 GLY SER HIS MET GLU SER GLY TYR ALA GLN ASN GLY ASP
SEQRES 2 K 223 LEU GLU ASP ALA GLU LEU ASP ASP TYR SER PHE SER CYS
SEQRES 3 K 223 TYR SER GLN LEU GLU VAL ASN GLY SER GLN HIS SER LEU
SEQRES 4 K 223 THR CYS ALA PHE GLU ASP PRO ASP VAL ASN THR THR ASN
SEQRES 5 K 223 LEU GLU PHE GLU ILE CYS GLY ALA LEU VAL GLU VAL LYS
SEQRES 6 K 223 CYS LEU ASN PHE ARG LYS LEU GLN GLU ILE TYR PHE ILE
SEQRES 7 K 223 GLU THR LYS LYS PHE LEU LEU ILE GLY LYS SER ASN ILE
SEQRES 8 K 223 CYS VAL LYS VAL GLY GLU LYS SER LEU THR CYS LYS LYS
SEQRES 9 K 223 ILE ASP LEU THR THR ILE VAL LYS PRO GLU ALA PRO PHE
SEQRES 10 K 223 ASP LEU SER VAL VAL TYR ARG GLU GLY ALA ASN ASP PHE
SEQRES 11 K 223 VAL VAL THR PHE ASN THR SER HIS LEU GLN LYS LYS TYR
SEQRES 12 K 223 VAL LYS VAL LEU MET HIS ASP VAL ALA TYR ARG GLN GLU
SEQRES 13 K 223 LYS ASP GLU ASN LYS TRP THR HIS VAL ASN LEU SER SER
SEQRES 14 K 223 THR LYS LEU THR LEU LEU GLN ARG LYS LEU GLN PRO ALA
SEQRES 15 K 223 ALA MET TYR GLU ILE LYS VAL ARG SER ILE PRO ASP HIS
SEQRES 16 K 223 TYR PHE LYS GLY PHE TRP SER GLU TRP SER PRO SER TYR
SEQRES 17 K 223 TYR PHE ARG THR PRO GLU ILE ASN ASN SER SER GLY GLU
SEQRES 18 K 223 MET ASP
SEQRES 1 L 214 ASP ILE VAL MET THR GLN SER HIS LYS PHE MET SER THR
SEQRES 2 L 214 LEU VAL GLY ASP ARG VAL SER ILE THR CYS LYS ALA SER
SEQRES 3 L 214 GLN ASP VAL SER THR THR VAL ALA TRP TYR GLN GLN LYS
SEQRES 4 L 214 PRO GLY GLN SER PRO LYS LEU LEU ILE TYR SER ALA SER
SEQRES 5 L 214 TYR ARG TYR THR GLY VAL PRO ASP ARG PHE THR GLY SER
SEQRES 6 L 214 GLY SER GLY THR ASP PHE THR PHE THR ILE SER SER VAL
SEQRES 7 L 214 GLN ALA GLU ASP LEU ALA VAL TYR TYR CYS GLN GLN HIS
SEQRES 8 L 214 TYR SER ILE PRO ARG THR PHE GLY GLY GLY THR LYS LEU
SEQRES 9 L 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE
SEQRES 10 L 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA
SEQRES 11 L 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU
SEQRES 12 L 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER
SEQRES 13 L 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS
SEQRES 14 L 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER
SEQRES 15 L 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU
SEQRES 16 L 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER
SEQRES 17 L 214 PHE ASN ARG GLY GLU CYS
HET NAG M 1 14
HET NAG M 2 14
HET BMA M 3 11
HET NAG N 1 14
HET NAG N 2 14
HET BMA N 3 11
HET NAG O 1 14
HET NAG O 2 14
HET FUC G 304 10
HET NAG G 305 14
HET NAG I 301 14
HET NAG J 303 14
HET NAG K 301 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUC FUCOSE; FUCOSE
FORMUL 13 NAG 10(C8 H15 N O6)
FORMUL 13 BMA 2(C6 H12 O6)
FORMUL 16 FUC C6 H12 O5
HELIX 1 AA1 THR A 28 TYR A 32 5 5
HELIX 2 AA2 SER A 163 ALA A 165 5 3
HELIX 3 AA3 SER A 194 GLY A 197 5 4
HELIX 4 AA4 GLN B 79 LEU B 83 5 5
HELIX 5 AA5 SER B 121 GLY B 128 1 8
HELIX 6 AA6 LYS B 183 HIS B 189 1 7
HELIX 7 AA7 THR C 28 TYR C 32 5 5
HELIX 8 AA8 SER C 163 ALA C 165 5 3
HELIX 9 AA9 SER C 194 GLY C 197 5 4
HELIX 10 AB1 GLN D 79 LEU D 83 5 5
HELIX 11 AB2 SER D 121 GLY D 128 1 8
HELIX 12 AB3 LYS D 183 HIS D 189 1 7
HELIX 13 AB4 THR E 28 TYR E 32 5 5
HELIX 14 AB5 SER E 163 ALA E 165 5 3
HELIX 15 AB6 SER E 194 THR E 198 5 5
HELIX 16 AB7 GLN F 79 LEU F 83 5 5
HELIX 17 AB8 SER F 121 GLY F 128 1 8
HELIX 18 AB9 LYS F 183 LYS F 188 1 6
HELIX 19 AC1 ASP G 102 ILE G 106 5 5
HELIX 20 AC2 THR H 28 TYR H 32 5 5
HELIX 21 AC3 TYR H 60 PHE H 64 5 5
HELIX 22 AC4 SER H 163 ALA H 165 5 3
HELIX 23 AC5 SER H 194 GLY H 197 5 4
HELIX 24 AC6 THR I 104 ILE I 106 5 3
HELIX 25 AC7 ARG I 173 LEU I 175 5 3
HELIX 26 AC8 ASN J 45 LEU J 49 5 5
HELIX 27 AC9 ASP J 102 ILE J 106 5 5
HELIX 28 AD1 THR K 104 ILE K 106 5 3
HELIX 29 AD2 THR K 132 LYS K 137 5 6
HELIX 30 AD3 GLN L 79 LEU L 83 5 5
HELIX 31 AD4 SER L 121 GLY L 128 1 8
HELIX 32 AD5 LYS L 183 HIS L 189 1 7
SHEET 1 AA1 4 GLN A 3 GLN A 6 0
SHEET 2 AA1 4 VAL A 18 SER A 25 -1 O LYS A 23 N GLN A 5
SHEET 3 AA1 4 SER A 77 GLU A 82 -1 O TYR A 80 N MET A 20
SHEET 4 AA1 4 LYS A 67 VAL A 72 -1 N ALA A 68 O MET A 81
SHEET 1 AA2 5 GLU A 10 VAL A 12 0
SHEET 2 AA2 5 THR A 114 VAL A 118 1 O THR A 115 N GLU A 10
SHEET 3 AA2 5 ALA A 92 GLY A 99 -1 N TYR A 94 O THR A 114
SHEET 4 AA2 5 MET A 34 SER A 40 -1 N HIS A 35 O ALA A 97
SHEET 5 AA2 5 LEU A 45 ILE A 51 -1 O GLU A 46 N LYS A 38
SHEET 1 AA3 4 GLU A 10 VAL A 12 0
SHEET 2 AA3 4 THR A 114 VAL A 118 1 O THR A 115 N GLU A 10
SHEET 3 AA3 4 ALA A 92 GLY A 99 -1 N TYR A 94 O THR A 114
SHEET 4 AA3 4 PHE A 107 TRP A 110 -1 O TYR A 109 N ARG A 98
SHEET 1 AA4 4 SER A 127 LEU A 131 0
SHEET 2 AA4 4 THR A 142 TYR A 152 -1 O LYS A 150 N SER A 127
SHEET 3 AA4 4 TYR A 183 PRO A 192 -1 O TYR A 183 N TYR A 152
SHEET 4 AA4 4 VAL A 170 THR A 172 -1 N HIS A 171 O VAL A 188
SHEET 1 AA5 4 SER A 127 LEU A 131 0
SHEET 2 AA5 4 THR A 142 TYR A 152 -1 O LYS A 150 N SER A 127
SHEET 3 AA5 4 TYR A 183 PRO A 192 -1 O TYR A 183 N TYR A 152
SHEET 4 AA5 4 VAL A 176 LEU A 177 -1 N VAL A 176 O SER A 184
SHEET 1 AA6 3 THR A 158 TRP A 161 0
SHEET 2 AA6 3 TYR A 201 HIS A 207 -1 O ASN A 206 N THR A 158
SHEET 3 AA6 3 THR A 212 VAL A 218 -1 O THR A 212 N HIS A 207
SHEET 1 AA7 4 MET B 4 GLN B 6 0
SHEET 2 AA7 4 VAL B 19 ALA B 25 -1 O LYS B 24 N THR B 5
SHEET 3 AA7 4 ASP B 70 ILE B 75 -1 O PHE B 73 N ILE B 21
SHEET 4 AA7 4 PHE B 62 SER B 67 -1 N THR B 63 O THR B 74
SHEET 1 AA8 6 PHE B 10 LEU B 14 0
SHEET 2 AA8 6 THR B 102 LYS B 107 1 O LYS B 107 N THR B 13
SHEET 3 AA8 6 ALA B 84 GLN B 90 -1 N ALA B 84 O LEU B 104
SHEET 4 AA8 6 VAL B 33 GLN B 38 -1 N ALA B 34 O GLN B 89
SHEET 5 AA8 6 LYS B 45 TYR B 49 -1 O LYS B 45 N GLN B 37
SHEET 6 AA8 6 TYR B 53 ARG B 54 -1 O TYR B 53 N TYR B 49
SHEET 1 AA9 4 PHE B 10 LEU B 14 0
SHEET 2 AA9 4 THR B 102 LYS B 107 1 O LYS B 107 N THR B 13
SHEET 3 AA9 4 ALA B 84 GLN B 90 -1 N ALA B 84 O LEU B 104
SHEET 4 AA9 4 THR B 97 PHE B 98 -1 O THR B 97 N GLN B 90
SHEET 1 AB1 4 SER B 114 PHE B 118 0
SHEET 2 AB1 4 THR B 129 PHE B 139 -1 O VAL B 133 N PHE B 118
SHEET 3 AB1 4 TYR B 173 SER B 182 -1 O LEU B 175 N LEU B 136
SHEET 4 AB1 4 SER B 159 VAL B 163 -1 N GLN B 160 O THR B 178
SHEET 1 AB2 4 ALA B 153 LEU B 154 0
SHEET 2 AB2 4 ALA B 144 VAL B 150 -1 N VAL B 150 O ALA B 153
SHEET 3 AB2 4 VAL B 191 HIS B 198 -1 O ALA B 193 N LYS B 149
SHEET 4 AB2 4 VAL B 205 ASN B 210 -1 O VAL B 205 N VAL B 196
SHEET 1 AB3 4 GLN C 3 GLN C 6 0
SHEET 2 AB3 4 VAL C 18 SER C 25 -1 O LYS C 23 N GLN C 5
SHEET 3 AB3 4 SER C 77 GLU C 82 -1 O TYR C 80 N MET C 20
SHEET 4 AB3 4 LYS C 67 VAL C 72 -1 N LEU C 70 O VAL C 79
SHEET 1 AB4 5 GLU C 10 VAL C 12 0
SHEET 2 AB4 5 THR C 114 VAL C 118 1 O THR C 115 N GLU C 10
SHEET 3 AB4 5 ALA C 92 GLY C 99 -1 N TYR C 94 O THR C 114
SHEET 4 AB4 5 MET C 34 SER C 40 -1 N VAL C 37 O TYR C 95
SHEET 5 AB4 5 SER C 44 ILE C 51 -1 O GLU C 46 N LYS C 38
SHEET 1 AB5 4 GLU C 10 VAL C 12 0
SHEET 2 AB5 4 THR C 114 VAL C 118 1 O THR C 115 N GLU C 10
SHEET 3 AB5 4 ALA C 92 GLY C 99 -1 N TYR C 94 O THR C 114
SHEET 4 AB5 4 PHE C 107 TRP C 110 -1 O TYR C 109 N ARG C 98
SHEET 1 AB6 4 SER C 127 LEU C 131 0
SHEET 2 AB6 4 THR C 142 TYR C 152 -1 O LYS C 150 N SER C 127
SHEET 3 AB6 4 TYR C 183 PRO C 192 -1 O TYR C 183 N TYR C 152
SHEET 4 AB6 4 VAL C 170 THR C 172 -1 N HIS C 171 O VAL C 188
SHEET 1 AB7 4 SER C 127 LEU C 131 0
SHEET 2 AB7 4 THR C 142 TYR C 152 -1 O LYS C 150 N SER C 127
SHEET 3 AB7 4 TYR C 183 PRO C 192 -1 O TYR C 183 N TYR C 152
SHEET 4 AB7 4 VAL C 176 LEU C 177 -1 N VAL C 176 O SER C 184
SHEET 1 AB8 3 THR C 158 TRP C 161 0
SHEET 2 AB8 3 TYR C 201 HIS C 207 -1 O ASN C 206 N THR C 158
SHEET 3 AB8 3 THR C 212 VAL C 218 -1 O VAL C 218 N TYR C 201
SHEET 1 AB9 4 MET D 4 GLN D 6 0
SHEET 2 AB9 4 VAL D 19 ALA D 25 -1 O LYS D 24 N THR D 5
SHEET 3 AB9 4 ASP D 70 ILE D 75 -1 O ILE D 75 N VAL D 19
SHEET 4 AB9 4 PHE D 62 SER D 67 -1 N THR D 63 O THR D 74
SHEET 1 AC1 6 PHE D 10 LEU D 14 0
SHEET 2 AC1 6 THR D 102 LYS D 107 1 O LYS D 107 N THR D 13
SHEET 3 AC1 6 VAL D 85 GLN D 90 -1 N TYR D 86 O THR D 102
SHEET 4 AC1 6 VAL D 33 GLN D 38 -1 N ALA D 34 O GLN D 89
SHEET 5 AC1 6 LYS D 45 TYR D 49 -1 O LYS D 45 N GLN D 37
SHEET 6 AC1 6 TYR D 53 ARG D 54 -1 O TYR D 53 N TYR D 49
SHEET 1 AC2 4 PHE D 10 LEU D 14 0
SHEET 2 AC2 4 THR D 102 LYS D 107 1 O LYS D 107 N THR D 13
SHEET 3 AC2 4 VAL D 85 GLN D 90 -1 N TYR D 86 O THR D 102
SHEET 4 AC2 4 THR D 97 PHE D 98 -1 O THR D 97 N GLN D 90
SHEET 1 AC3 4 SER D 114 PHE D 118 0
SHEET 2 AC3 4 THR D 129 PHE D 139 -1 O VAL D 133 N PHE D 118
SHEET 3 AC3 4 TYR D 173 SER D 182 -1 O LEU D 179 N VAL D 132
SHEET 4 AC3 4 SER D 159 VAL D 163 -1 N GLN D 160 O THR D 178
SHEET 1 AC4 4 ALA D 153 LEU D 154 0
SHEET 2 AC4 4 ALA D 144 VAL D 150 -1 N VAL D 150 O ALA D 153
SHEET 3 AC4 4 VAL D 191 HIS D 198 -1 O ALA D 193 N LYS D 149
SHEET 4 AC4 4 VAL D 205 ASN D 210 -1 O VAL D 205 N VAL D 196
SHEET 1 AC5 4 GLN E 3 GLN E 6 0
SHEET 2 AC5 4 VAL E 18 SER E 25 -1 O LYS E 23 N GLN E 5
SHEET 3 AC5 4 SER E 77 GLU E 82 -1 O TYR E 80 N MET E 20
SHEET 4 AC5 4 LYS E 67 VAL E 72 -1 N ALA E 68 O MET E 81
SHEET 1 AC6 5 GLU E 10 VAL E 12 0
SHEET 2 AC6 5 THR E 114 VAL E 118 1 O THR E 115 N GLU E 10
SHEET 3 AC6 5 ALA E 92 GLY E 99 -1 N TYR E 94 O THR E 114
SHEET 4 AC6 5 MET E 34 SER E 40 -1 N HIS E 35 O ALA E 97
SHEET 5 AC6 5 SER E 44 ILE E 51 -1 O GLU E 46 N LYS E 38
SHEET 1 AC7 4 GLU E 10 VAL E 12 0
SHEET 2 AC7 4 THR E 114 VAL E 118 1 O THR E 115 N GLU E 10
SHEET 3 AC7 4 ALA E 92 GLY E 99 -1 N TYR E 94 O THR E 114
SHEET 4 AC7 4 PHE E 107 TRP E 110 -1 O TYR E 109 N ARG E 98
SHEET 1 AC8 4 SER E 127 LEU E 131 0
SHEET 2 AC8 4 THR E 142 TYR E 152 -1 O LYS E 150 N SER E 127
SHEET 3 AC8 4 TYR E 183 PRO E 192 -1 O TYR E 183 N TYR E 152
SHEET 4 AC8 4 VAL E 170 THR E 172 -1 N HIS E 171 O VAL E 188
SHEET 1 AC9 4 SER E 127 LEU E 131 0
SHEET 2 AC9 4 THR E 142 TYR E 152 -1 O LYS E 150 N SER E 127
SHEET 3 AC9 4 TYR E 183 PRO E 192 -1 O TYR E 183 N TYR E 152
SHEET 4 AC9 4 VAL E 176 LEU E 177 -1 N VAL E 176 O SER E 184
SHEET 1 AD1 3 THR E 158 TRP E 161 0
SHEET 2 AD1 3 ILE E 202 HIS E 207 -1 O ASN E 206 N THR E 158
SHEET 3 AD1 3 THR E 212 LYS E 217 -1 O LYS E 216 N CYS E 203
SHEET 1 AD2 4 MET F 4 GLN F 6 0
SHEET 2 AD2 4 VAL F 19 ALA F 25 -1 O LYS F 24 N THR F 5
SHEET 3 AD2 4 ASP F 70 ILE F 75 -1 O ILE F 75 N VAL F 19
SHEET 4 AD2 4 PHE F 62 SER F 67 -1 N THR F 63 O THR F 74
SHEET 1 AD3 6 PHE F 10 LEU F 14 0
SHEET 2 AD3 6 THR F 102 LYS F 107 1 O GLU F 105 N MET F 11
SHEET 3 AD3 6 VAL F 85 GLN F 90 -1 N TYR F 86 O THR F 102
SHEET 4 AD3 6 VAL F 33 GLN F 38 -1 N ALA F 34 O GLN F 89
SHEET 5 AD3 6 LYS F 45 TYR F 49 -1 O LYS F 45 N GLN F 37
SHEET 6 AD3 6 TYR F 53 ARG F 54 -1 O TYR F 53 N TYR F 49
SHEET 1 AD4 4 PHE F 10 LEU F 14 0
SHEET 2 AD4 4 THR F 102 LYS F 107 1 O GLU F 105 N MET F 11
SHEET 3 AD4 4 VAL F 85 GLN F 90 -1 N TYR F 86 O THR F 102
SHEET 4 AD4 4 THR F 97 PHE F 98 -1 O THR F 97 N GLN F 90
SHEET 1 AD5 4 SER F 114 PHE F 118 0
SHEET 2 AD5 4 THR F 129 PHE F 139 -1 O VAL F 133 N PHE F 118
SHEET 3 AD5 4 TYR F 173 SER F 182 -1 O LEU F 179 N VAL F 132
SHEET 4 AD5 4 SER F 159 VAL F 163 -1 N GLN F 160 O THR F 178
SHEET 1 AD6 4 ALA F 153 LEU F 154 0
SHEET 2 AD6 4 ALA F 144 VAL F 150 -1 N VAL F 150 O ALA F 153
SHEET 3 AD6 4 VAL F 191 HIS F 198 -1 O ALA F 193 N LYS F 149
SHEET 4 AD6 4 VAL F 205 ASN F 210 -1 O VAL F 205 N VAL F 196
SHEET 1 AD7 4 PHE G 20 ASN G 29 0
SHEET 2 AD7 4 GLN G 32 PHE G 39 -1 O GLN G 32 N ASN G 29
SHEET 3 AD7 4 ILE G 71 THR G 76 -1 O TYR G 72 N CYS G 37
SHEET 4 AD7 4 ARG G 66 LEU G 68 -1 N ARG G 66 O PHE G 73
SHEET 1 AD8 4 CYS G 62 ASN G 64 0
SHEET 2 AD8 4 GLU G 50 CYS G 54 -1 N ILE G 53 O LEU G 63
SHEET 3 AD8 4 SER G 85 LYS G 90 -1 O ASN G 86 N CYS G 54
SHEET 4 AD8 4 THR G 97 ILE G 101 -1 O THR G 97 N VAL G 89
SHEET 1 AD9 3 PHE G 113 ARG G 120 0
SHEET 2 AD9 3 ASP G 125 ASN G 131 -1 O VAL G 127 N VAL G 118
SHEET 3 AD9 3 LYS G 167 LEU G 171 -1 O LEU G 168 N VAL G 128
SHEET 1 AE1 4 THR G 159 LEU G 163 0
SHEET 2 AE1 4 LEU G 143 GLN G 151 -1 N TYR G 149 O THR G 159
SHEET 3 AE1 4 MET G 180 PRO G 189 -1 O GLU G 182 N ARG G 150
SHEET 4 AE1 4 TYR G 204 ARG G 207 -1 O PHE G 206 N TYR G 181
SHEET 1 AE2 4 GLN H 3 GLN H 6 0
SHEET 2 AE2 4 VAL H 18 SER H 25 -1 O LYS H 23 N GLN H 5
SHEET 3 AE2 4 SER H 77 GLU H 82 -1 O TYR H 80 N MET H 20
SHEET 4 AE2 4 LYS H 67 VAL H 72 -1 N LEU H 70 O VAL H 79
SHEET 1 AE3 5 GLU H 10 VAL H 12 0
SHEET 2 AE3 5 THR H 114 VAL H 118 1 O THR H 115 N GLU H 10
SHEET 3 AE3 5 ALA H 92 GLY H 99 -1 N TYR H 94 O THR H 114
SHEET 4 AE3 5 MET H 34 SER H 40 -1 N HIS H 35 O ALA H 97
SHEET 5 AE3 5 LEU H 45 ILE H 51 -1 O GLU H 46 N LYS H 38
SHEET 1 AE4 4 GLU H 10 VAL H 12 0
SHEET 2 AE4 4 THR H 114 VAL H 118 1 O THR H 115 N GLU H 10
SHEET 3 AE4 4 ALA H 92 GLY H 99 -1 N TYR H 94 O THR H 114
SHEET 4 AE4 4 PHE H 107 TRP H 110 -1 O TYR H 109 N ARG H 98
SHEET 1 AE5 4 SER H 127 LEU H 131 0
SHEET 2 AE5 4 THR H 142 TYR H 152 -1 O LYS H 150 N SER H 127
SHEET 3 AE5 4 TYR H 183 PRO H 192 -1 O TYR H 183 N TYR H 152
SHEET 4 AE5 4 VAL H 170 THR H 172 -1 N HIS H 171 O VAL H 188
SHEET 1 AE6 4 THR H 138 SER H 139 0
SHEET 2 AE6 4 THR H 142 TYR H 152 -1 O THR H 142 N SER H 139
SHEET 3 AE6 4 TYR H 183 PRO H 192 -1 O TYR H 183 N TYR H 152
SHEET 4 AE6 4 VAL H 176 LEU H 177 -1 N VAL H 176 O SER H 184
SHEET 1 AE7 3 THR H 158 TRP H 161 0
SHEET 2 AE7 3 ILE H 202 HIS H 207 -1 O ASN H 206 N THR H 158
SHEET 3 AE7 3 THR H 212 LYS H 217 -1 O THR H 212 N HIS H 207
SHEET 1 AE8 4 PHE I 20 ASN I 29 0
SHEET 2 AE8 4 GLN I 32 PHE I 39 -1 O THR I 36 N TYR I 23
SHEET 3 AE8 4 ILE I 71 THR I 76 -1 O TYR I 72 N CYS I 37
SHEET 4 AE8 4 ARG I 66 LEU I 68 -1 N LEU I 68 O ILE I 71
SHEET 1 AE9 3 GLU I 50 CYS I 54 0
SHEET 2 AE9 3 LYS I 84 VAL I 91 -1 O ASN I 86 N CYS I 54
SHEET 3 AE9 3 LYS I 94 ASP I 102 -1 O LEU I 96 N VAL I 89
SHEET 1 AF1 3 PHE I 113 ARG I 120 0
SHEET 2 AF1 3 ASP I 125 ASN I 131 -1 O VAL I 127 N VAL I 118
SHEET 3 AF1 3 LYS I 167 LEU I 171 -1 O LEU I 168 N VAL I 128
SHEET 1 AF2 4 THR I 159 LEU I 163 0
SHEET 2 AF2 4 LEU I 143 GLN I 151 -1 N TYR I 149 O THR I 159
SHEET 3 AF2 4 MET I 180 PRO I 189 -1 O GLU I 182 N ARG I 150
SHEET 4 AF2 4 TYR I 204 ARG I 207 -1 O PHE I 206 N TYR I 181
SHEET 1 AF3 4 PHE J 20 ASN J 29 0
SHEET 2 AF3 4 GLN J 32 PHE J 39 -1 O THR J 36 N TYR J 23
SHEET 3 AF3 4 ILE J 71 THR J 76 -1 O TYR J 72 N CYS J 37
SHEET 4 AF3 4 ARG J 66 LEU J 68 -1 N LEU J 68 O ILE J 71
SHEET 1 AF4 4 CYS J 62 ASN J 64 0
SHEET 2 AF4 4 GLU J 50 CYS J 54 -1 N ILE J 53 O LEU J 63
SHEET 3 AF4 4 SER J 85 LYS J 90 -1 O ASN J 86 N CYS J 54
SHEET 4 AF4 4 SER J 95 ILE J 101 -1 O LEU J 96 N VAL J 89
SHEET 1 AF5 3 PHE J 113 ARG J 120 0
SHEET 2 AF5 3 ASP J 125 ASN J 131 -1 O VAL J 127 N VAL J 118
SHEET 3 AF5 3 LYS J 167 LEU J 171 -1 O LEU J 170 N PHE J 126
SHEET 1 AF6 4 THR J 159 LEU J 163 0
SHEET 2 AF6 4 LEU J 143 GLN J 151 -1 N VAL J 147 O VAL J 161
SHEET 3 AF6 4 MET J 180 PRO J 189 -1 O ILE J 188 N MET J 144
SHEET 4 AF6 4 TYR J 204 ARG J 207 -1 O PHE J 206 N TYR J 181
SHEET 1 AF7 3 PHE K 20 ASN K 29 0
SHEET 2 AF7 3 GLN K 32 PHE K 39 -1 O ALA K 38 N SER K 21
SHEET 3 AF7 3 GLU K 75 THR K 76 -1 O THR K 76 N HIS K 33
SHEET 1 AF8 2 GLU K 52 ILE K 53 0
SHEET 2 AF8 2 LEU K 63 ASN K 64 -1 O LEU K 63 N ILE K 53
SHEET 1 AF9 2 LYS K 84 CYS K 88 0
SHEET 2 AF9 2 CYS K 98 ASP K 102 -1 O LYS K 99 N ILE K 87
SHEET 1 AG1 3 PHE K 113 ARG K 120 0
SHEET 2 AG1 3 ASP K 125 ASN K 131 -1 O VAL K 127 N VAL K 118
SHEET 3 AG1 3 LYS K 167 LEU K 171 -1 O LEU K 170 N PHE K 126
SHEET 1 AG2 4 THR K 159 LEU K 163 0
SHEET 2 AG2 4 LEU K 143 GLN K 151 -1 N TYR K 149 O THR K 159
SHEET 3 AG2 4 MET K 180 PRO K 189 -1 O GLU K 182 N ARG K 150
SHEET 4 AG2 4 TYR K 204 ARG K 207 -1 O PHE K 206 N TYR K 181
SHEET 1 AG3 4 MET L 4 GLN L 6 0
SHEET 2 AG3 4 VAL L 19 ALA L 25 -1 O LYS L 24 N THR L 5
SHEET 3 AG3 4 ASP L 70 ILE L 75 -1 O PHE L 73 N ILE L 21
SHEET 4 AG3 4 PHE L 62 SER L 67 -1 N THR L 63 O THR L 74
SHEET 1 AG4 6 PHE L 10 LEU L 14 0
SHEET 2 AG4 6 THR L 102 LYS L 107 1 O GLU L 105 N MET L 11
SHEET 3 AG4 6 VAL L 85 GLN L 90 -1 N TYR L 86 O THR L 102
SHEET 4 AG4 6 VAL L 33 GLN L 38 -1 N ALA L 34 O GLN L 89
SHEET 5 AG4 6 LYS L 45 TYR L 49 -1 O LYS L 45 N GLN L 37
SHEET 6 AG4 6 TYR L 53 ARG L 54 -1 O TYR L 53 N TYR L 49
SHEET 1 AG5 4 PHE L 10 LEU L 14 0
SHEET 2 AG5 4 THR L 102 LYS L 107 1 O GLU L 105 N MET L 11
SHEET 3 AG5 4 VAL L 85 GLN L 90 -1 N TYR L 86 O THR L 102
SHEET 4 AG5 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90
SHEET 1 AG6 4 SER L 114 PHE L 118 0
SHEET 2 AG6 4 THR L 129 PHE L 139 -1 O VAL L 133 N PHE L 118
SHEET 3 AG6 4 TYR L 173 SER L 182 -1 O TYR L 173 N PHE L 139
SHEET 4 AG6 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178
SHEET 1 AG7 4 ALA L 153 LEU L 154 0
SHEET 2 AG7 4 ALA L 144 VAL L 150 -1 N VAL L 150 O ALA L 153
SHEET 3 AG7 4 VAL L 191 HIS L 198 -1 O ALA L 193 N LYS L 149
SHEET 4 AG7 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196
SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.03
SSBOND 2 CYS A 147 CYS A 203 1555 1555 2.03
SSBOND 3 CYS B 23 CYS B 88 1555 1555 2.03
SSBOND 4 CYS B 134 CYS B 194 1555 1555 2.04
SSBOND 5 CYS C 22 CYS C 96 1555 1555 2.03
SSBOND 6 CYS C 147 CYS C 203 1555 1555 2.03
SSBOND 7 CYS D 23 CYS D 88 1555 1555 2.04
SSBOND 8 CYS D 134 CYS D 194 1555 1555 2.04
SSBOND 9 CYS E 22 CYS E 96 1555 1555 2.03
SSBOND 10 CYS E 147 CYS E 203 1555 1555 2.03
SSBOND 11 CYS F 23 CYS F 88 1555 1555 2.04
SSBOND 12 CYS F 134 CYS F 194 1555 1555 2.04
SSBOND 13 CYS G 22 CYS G 37 1555 1555 2.03
SSBOND 14 CYS G 54 CYS G 62 1555 1555 2.04
SSBOND 15 CYS G 88 CYS G 98 1555 1555 2.04
SSBOND 16 CYS H 22 CYS H 96 1555 1555 2.03
SSBOND 17 CYS H 147 CYS H 203 1555 1555 2.03
SSBOND 18 CYS I 22 CYS I 37 1555 1555 2.03
SSBOND 19 CYS I 54 CYS I 62 1555 1555 2.03
SSBOND 20 CYS I 88 CYS I 98 1555 1555 2.03
SSBOND 21 CYS J 22 CYS J 37 1555 1555 2.03
SSBOND 22 CYS J 54 CYS J 62 1555 1555 2.03
SSBOND 23 CYS J 88 CYS J 98 1555 1555 2.03
SSBOND 24 CYS K 22 CYS K 37 1555 1555 2.03
SSBOND 25 CYS K 54 CYS K 62 1555 1555 2.03
SSBOND 26 CYS K 88 CYS K 98 1555 1555 2.04
SSBOND 27 CYS L 23 CYS L 88 1555 1555 2.04
SSBOND 28 CYS L 134 CYS L 194 1555 1555 2.04
LINK ND2 ASN G 29 C1 NAG G 305 1555 1555 1.44
LINK ND2 ASN G 131 C1 NAG M 1 1555 1555 1.44
LINK ND2 ASN I 45 C1 NAG I 301 1555 1555 1.43
LINK ND2 ASN I 131 C1 NAG N 1 1555 1555 1.44
LINK ND2 ASN J 29 C1 NAG J 303 1555 1555 1.44
LINK ND2 ASN J 131 C1 NAG O 1 1555 1555 1.44
LINK ND2 ASN K 131 C1 NAG K 301 1555 1555 1.45
LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.37
LINK O4 NAG M 2 C1 BMA M 3 1555 1555 1.37
LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.38
LINK O4 NAG N 2 C1 BMA N 3 1555 1555 1.37
LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.38
CISPEP 1 PHE A 153 PRO A 154 0 -4.12
CISPEP 2 GLU A 155 PRO A 156 0 -1.33
CISPEP 3 ILE B 94 PRO B 95 0 0.82
CISPEP 4 TYR B 140 PRO B 141 0 2.41
CISPEP 5 PHE C 153 PRO C 154 0 -3.86
CISPEP 6 GLU C 155 PRO C 156 0 -1.09
CISPEP 7 ILE D 94 PRO D 95 0 0.66
CISPEP 8 TYR D 140 PRO D 141 0 2.36
CISPEP 9 PHE E 153 PRO E 154 0 -4.34
CISPEP 10 GLU E 155 PRO E 156 0 -0.67
CISPEP 11 ILE F 94 PRO F 95 0 1.29
CISPEP 12 TYR F 140 PRO F 141 0 2.80
CISPEP 13 PHE H 153 PRO H 154 0 -4.17
CISPEP 14 GLU H 155 PRO H 156 0 -0.84
CISPEP 15 ILE L 94 PRO L 95 0 0.92
CISPEP 16 TYR L 140 PRO L 141 0 3.17
CRYST1 84.900 219.680 90.350 90.00 104.33 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.011779 0.000000 0.003008 0.00000
SCALE2 0.000000 0.004552 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011423 0.00000
(ATOM LINES ARE NOT SHOWN.)
END