HEADER IMMUNE SYSTEM 09-AUG-24 9GFG TITLE BCR FAB FROM THE SUBSET 1 CHRONIC LYMPHOCYTIC LEUKAEMIA CASE P3129 COMPND MOL_ID: 1; COMPND 2 MOLECULE: BCR P3129 HEAVY CHAIN; COMPND 3 CHAIN: H, A, C, E; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: BCR P3129 LIGHT CHAIN; COMPND 7 CHAIN: L, B, D, F; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_TAXID: 9606; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM_CELL_LINE: HEK293 KEYWDS BCR, FAB, CHRONIC LYMPHOCYTIC LEUKAEMIA, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR C.MINICI,M.DEGANO REVDAT 1 20-AUG-25 9GFG 0 JRNL AUTH P.G.COCOMAZZI,A.IATROU,C.MINICI,M.DEGANO JRNL TITL DEFECTIVE CELL-AUTONOMOUS SIGNALLING AND ANTIGENIC JRNL TITL 2 POLYREACTIVITY OF B-CELL RECEPTORS FROM CHRONIC LYMPHOCYTIC JRNL TITL 3 LEUKAEMIA STEREOTYPED SUBSET 1 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 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) : 2.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 80.60 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 92899 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.221 REMARK 3 R VALUE (WORKING SET) : 0.220 REMARK 3 FREE R VALUE : 0.246 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900 REMARK 3 FREE R VALUE TEST SET COUNT : 4549 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 80.6000 - 7.1400 0.99 3079 136 0.1906 0.2235 REMARK 3 2 7.1400 - 5.6700 0.99 2952 184 0.1989 0.2100 REMARK 3 3 5.6700 - 4.9500 1.00 2952 169 0.1638 0.2139 REMARK 3 4 4.9500 - 4.5000 1.00 2980 138 0.1525 0.1651 REMARK 3 5 4.5000 - 4.1800 1.00 2957 157 0.1608 0.1849 REMARK 3 6 4.1800 - 3.9300 1.00 2976 141 0.1896 0.2044 REMARK 3 7 3.9300 - 3.7300 1.00 2930 168 0.2172 0.2512 REMARK 3 8 3.7300 - 3.5700 1.00 2970 156 0.2134 0.2389 REMARK 3 9 3.5700 - 3.4300 1.00 2955 143 0.2185 0.2217 REMARK 3 10 3.4300 - 3.3200 1.00 2959 142 0.2262 0.2496 REMARK 3 11 3.3200 - 3.2100 1.00 2934 159 0.2545 0.2868 REMARK 3 12 3.2100 - 3.1200 1.00 2931 154 0.2829 0.3311 REMARK 3 13 3.1200 - 3.0400 1.00 2904 173 0.2776 0.2969 REMARK 3 14 3.0400 - 2.9600 1.00 2955 146 0.2683 0.2936 REMARK 3 15 2.9600 - 2.9000 1.00 2966 149 0.2573 0.2946 REMARK 3 16 2.9000 - 2.8300 1.00 2898 145 0.2568 0.2720 REMARK 3 17 2.8300 - 2.7800 1.00 3001 158 0.2589 0.2893 REMARK 3 18 2.7800 - 2.7300 1.00 2929 146 0.2848 0.3444 REMARK 3 19 2.7300 - 2.6800 1.00 2881 187 0.2913 0.3130 REMARK 3 20 2.6800 - 2.6300 1.00 2933 158 0.3083 0.3137 REMARK 3 21 2.6300 - 2.5900 1.00 2932 152 0.3476 0.3775 REMARK 3 22 2.5900 - 2.5500 1.00 2950 133 0.3686 0.3881 REMARK 3 23 2.5500 - 2.5100 1.00 2927 167 0.3553 0.3494 REMARK 3 24 2.5100 - 2.4800 1.00 2955 145 0.3417 0.4151 REMARK 3 25 2.4800 - 2.4400 1.00 2912 141 0.3593 0.4142 REMARK 3 26 2.4400 - 2.4100 1.00 2971 147 0.3589 0.3599 REMARK 3 27 2.4100 - 2.3800 1.00 2890 144 0.3687 0.4194 REMARK 3 28 2.3800 - 2.3500 1.00 2947 150 0.3646 0.3910 REMARK 3 29 2.3500 - 2.3300 1.00 2984 130 0.3806 0.3710 REMARK 3 30 2.3300 - 2.3000 0.97 2840 131 0.3966 0.4609 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) : 0.342 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.501 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 85.74 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 13472 REMARK 3 ANGLE : 0.634 18279 REMARK 3 CHIRALITY : 0.046 2040 REMARK 3 PLANARITY : 0.004 2322 REMARK 3 DIHEDRAL : 12.672 4862 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 8 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (CHAIN 'H' AND RESID 1 THROUGH 225) REMARK 3 ORIGIN FOR THE GROUP (A): 5.9827 22.3355 -47.0014 REMARK 3 T TENSOR REMARK 3 T11: 0.7771 T22: 0.3110 REMARK 3 T33: 0.4311 T12: -0.0045 REMARK 3 T13: -0.0425 T23: 0.0316 REMARK 3 L TENSOR REMARK 3 L11: 4.3427 L22: 0.7995 REMARK 3 L33: 3.0242 L12: -0.0165 REMARK 3 L13: -2.4401 L23: -0.0009 REMARK 3 S TENSOR REMARK 3 S11: 0.1537 S12: 0.2998 S13: 0.0815 REMARK 3 S21: -0.1373 S22: 0.0013 S23: -0.0780 REMARK 3 S31: -0.0075 S32: -0.1605 S33: -0.1465 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN 'L' AND RESID 1 THROUGH 214) REMARK 3 ORIGIN FOR THE GROUP (A): 8.7494 4.5377 -45.9638 REMARK 3 T TENSOR REMARK 3 T11: 0.8423 T22: 0.3778 REMARK 3 T33: 0.4655 T12: 0.0129 REMARK 3 T13: -0.0963 T23: 0.0314 REMARK 3 L TENSOR REMARK 3 L11: 3.0078 L22: 1.0370 REMARK 3 L33: 0.9385 L12: 0.2478 REMARK 3 L13: -0.0740 L23: 0.0899 REMARK 3 S TENSOR REMARK 3 S11: 0.0156 S12: -0.2655 S13: -0.3234 REMARK 3 S21: 0.0346 S22: -0.0048 S23: -0.2594 REMARK 3 S31: 0.4689 S32: -0.0141 S33: -0.0023 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (CHAIN 'A' AND RESID 1 THROUGH 301) REMARK 3 ORIGIN FOR THE GROUP (A): -36.2126 17.7927 42.3462 REMARK 3 T TENSOR REMARK 3 T11: 0.8165 T22: 0.3923 REMARK 3 T33: 0.4924 T12: 0.0712 REMARK 3 T13: 0.0330 T23: -0.0526 REMARK 3 L TENSOR REMARK 3 L11: 3.5333 L22: 1.5576 REMARK 3 L33: 1.6394 L12: 1.2100 REMARK 3 L13: -0.8966 L23: -0.5476 REMARK 3 S TENSOR REMARK 3 S11: 0.2900 S12: -0.1033 S13: 0.2208 REMARK 3 S21: 0.1584 S22: -0.1984 S23: 0.2689 REMARK 3 S31: -0.4496 S32: -0.1867 S33: -0.1191 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: (CHAIN 'B' AND RESID 1 THROUGH 215) REMARK 3 ORIGIN FOR THE GROUP (A): -34.6076 0.3310 40.3013 REMARK 3 T TENSOR REMARK 3 T11: 0.7575 T22: 0.5129 REMARK 3 T33: 0.4729 T12: -0.0191 REMARK 3 T13: -0.0086 T23: -0.0305 REMARK 3 L TENSOR REMARK 3 L11: 3.4503 L22: 0.7520 REMARK 3 L33: 0.6644 L12: 0.4377 REMARK 3 L13: -0.0876 L23: -0.1562 REMARK 3 S TENSOR REMARK 3 S11: 0.1250 S12: 0.2648 S13: -0.1768 REMARK 3 S21: -0.1420 S22: -0.0652 S23: 0.0581 REMARK 3 S31: -0.0148 S32: -0.2078 S33: -0.0705 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: (CHAIN 'C' AND RESID 2 THROUGH 301) REMARK 3 ORIGIN FOR THE GROUP (A): 15.4907 17.5359 8.7211 REMARK 3 T TENSOR REMARK 3 T11: 0.6773 T22: 0.8543 REMARK 3 T33: 0.8060 T12: -0.1175 REMARK 3 T13: -0.2728 T23: 0.2255 REMARK 3 L TENSOR REMARK 3 L11: 3.5518 L22: 2.0006 REMARK 3 L33: 3.5607 L12: -0.7560 REMARK 3 L13: -3.1990 L23: 0.4796 REMARK 3 S TENSOR REMARK 3 S11: -0.0322 S12: -0.9028 S13: -0.1951 REMARK 3 S21: 0.4394 S22: -0.0876 S23: -0.6358 REMARK 3 S31: -0.3468 S32: 0.7875 S33: 0.1273 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: (CHAIN 'D' AND RESID 1 THROUGH 214) REMARK 3 ORIGIN FOR THE GROUP (A): 4.2399 17.0464 -5.7933 REMARK 3 T TENSOR REMARK 3 T11: 0.5698 T22: 0.5018 REMARK 3 T33: 0.3845 T12: -0.1097 REMARK 3 T13: -0.0730 T23: 0.0274 REMARK 3 L TENSOR REMARK 3 L11: 1.2693 L22: 3.7616 REMARK 3 L33: 3.0503 L12: -1.0089 REMARK 3 L13: -0.2889 L23: -0.8931 REMARK 3 S TENSOR REMARK 3 S11: 0.0789 S12: 0.0102 S13: 0.0341 REMARK 3 S21: -0.4664 S22: -0.0096 S23: -0.1622 REMARK 3 S31: 0.1193 S32: -0.1819 S33: -0.0778 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: (CHAIN 'E' AND RESID 1 THROUGH 301) REMARK 3 ORIGIN FOR THE GROUP (A): -43.0667 16.0463 -14.7807 REMARK 3 T TENSOR REMARK 3 T11: 0.7359 T22: 1.1824 REMARK 3 T33: 0.7777 T12: -0.4147 REMARK 3 T13: -0.1577 T23: 0.1195 REMARK 3 L TENSOR REMARK 3 L11: 0.7418 L22: 0.4966 REMARK 3 L33: 3.4113 L12: -0.7207 REMARK 3 L13: -1.2656 L23: 0.6322 REMARK 3 S TENSOR REMARK 3 S11: -0.1492 S12: 0.2368 S13: -0.1966 REMARK 3 S21: 0.0194 S22: -0.0223 S23: 0.4804 REMARK 3 S31: 0.7840 S32: -1.1435 S33: 0.1546 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: (CHAIN 'F' AND RESID 1 THROUGH 212) REMARK 3 ORIGIN FOR THE GROUP (A): -33.1655 15.5931 1.0576 REMARK 3 T TENSOR REMARK 3 T11: 0.7723 T22: 0.6916 REMARK 3 T33: 0.5860 T12: -0.1411 REMARK 3 T13: -0.0040 T23: 0.0546 REMARK 3 L TENSOR REMARK 3 L11: 0.9977 L22: 1.5458 REMARK 3 L33: 3.2793 L12: 0.0174 REMARK 3 L13: -1.1947 L23: -0.5689 REMARK 3 S TENSOR REMARK 3 S11: -0.1851 S12: 0.1281 S13: -0.0997 REMARK 3 S21: 0.3081 S22: 0.2766 S23: 0.3698 REMARK 3 S31: 0.7418 S32: -0.2023 S33: -0.1046 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 2 REMARK 3 NCS GROUP : ens_1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "A" and (resid 2 through 80 or REMARK 3 resid 82 through 133 or resid 143 through REMARK 3 165 or resid 172 through 187 or resid 189 REMARK 3 through 195 or resid 207 through 223)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "C" and (resid 2 through 80 or REMARK 3 resid 82 through 133 or resid 143 through REMARK 3 165 or resid 172 through 187 or resid 189 REMARK 3 through 195 or resid 207 through 223)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "E" and (resid 2 through 80 or REMARK 3 resid 82 through 187 or resid 189 through REMARK 3 195 or resid 207 through 223)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "H" and (resid 2 through 80 or REMARK 3 resid 82 through 133 or resid 143 through REMARK 3 165 or resid 172 through 187 or resid 189 REMARK 3 through 195 or resid 207 through 223)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_2 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "B" and (resid 1 through 82 or REMARK 3 resid 84 through 90 or resid 92 through REMARK 3 104 or resid 106 through 164 or resid 166 REMARK 3 through 212)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "D" and (resid 1 through 82 or REMARK 3 resid 84 through 90 or resid 92 through REMARK 3 104 or resid 106 through 164 or resid 166 REMARK 3 through 212)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "F" and (resid 1 through 82 or REMARK 3 resid 84 through 90 or resid 92 through REMARK 3 104 or resid 106 through 164 or resid 166 REMARK 3 through 212)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "L" and (resid 1 through 82 or REMARK 3 resid 84 through 90 or resid 92 through REMARK 3 104 or resid 106 through 164 or resid 166 REMARK 3 through 212)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9GFG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-AUG-24. REMARK 100 THE DEPOSITION ID IS D_1292140881. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 18-MAY-17 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : MASSIF-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.966 REMARK 200 MONOCHROMATOR : SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 120564 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.110 REMARK 200 RESOLUTION RANGE LOW (A) : 115.200 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 6.400 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.11 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.16 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.600 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 (%): 55.41 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM POTASSIUM TARTRATE PH 7, REMARK 280 0.1 M MAGNESIUM CHLORIDE, 20% PEG 3,350, PH 7.0, VAPOR DIFFUSION, REMARK 280 HANGING DROP, TEMPERATURE 293K 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 43.94550 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, G REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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: DIMERIC 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: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLU H 135 REMARK 465 ASN H 136 REMARK 465 SER H 137 REMARK 465 PRO H 138 REMARK 465 SER H 139 REMARK 465 ASP H 140 REMARK 465 THR H 141 REMARK 465 VAL H 225 REMARK 465 CYS L 215 REMARK 465 GLU A 135 REMARK 465 ASN A 136 REMARK 465 SER A 137 REMARK 465 PRO A 138 REMARK 465 SER A 139 REMARK 465 ASP A 140 REMARK 465 THR A 141 REMARK 465 VAL A 225 REMARK 465 GLN C 1 REMARK 465 GLU C 135 REMARK 465 ASN C 136 REMARK 465 SER C 137 REMARK 465 PRO C 138 REMARK 465 SER C 139 REMARK 465 ASP C 140 REMARK 465 THR C 141 REMARK 465 LYS C 196 REMARK 465 ASP C 197 REMARK 465 VAL C 198 REMARK 465 MET C 199 REMARK 465 GLN C 200 REMARK 465 GLY C 201 REMARK 465 THR C 202 REMARK 465 ASP C 203 REMARK 465 GLU C 204 REMARK 465 HIS C 205 REMARK 465 PRO C 224 REMARK 465 VAL C 225 REMARK 465 CYS D 215 REMARK 465 CYS E 134 REMARK 465 GLU E 135 REMARK 465 ASN E 136 REMARK 465 SER E 137 REMARK 465 PRO E 138 REMARK 465 SER E 139 REMARK 465 ASP E 140 REMARK 465 THR E 141 REMARK 465 SER E 142 REMARK 465 ASN E 166 REMARK 465 ASN E 167 REMARK 465 SER E 168 REMARK 465 ASP E 169 REMARK 465 ILE E 170 REMARK 465 SER E 171 REMARK 465 VAL E 198 REMARK 465 MET E 199 REMARK 465 GLN E 200 REMARK 465 GLY E 201 REMARK 465 THR E 202 REMARK 465 ASP E 203 REMARK 465 GLU E 204 REMARK 465 HIS E 205 REMARK 465 PRO E 224 REMARK 465 VAL E 225 REMARK 465 GLY F 213 REMARK 465 GLU F 214 REMARK 465 CYS F 215 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 O ALA L 13 H LYS L 108 1.48 REMARK 500 HH11 ARG H 87 OE2 GLU H 89 1.53 REMARK 500 HH11 ARG C 87 OE2 GLU C 89 1.55 REMARK 500 OE2 GLU D 106 HH TYR D 174 1.56 REMARK 500 ND2 ASN H 166 O5 NAG G 1 2.03 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 HOH L 420 O HOH B 405 1554 2.18 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 ASP H 103 -109.69 66.59 REMARK 500 ARG H 174 122.86 -35.16 REMARK 500 SER L 30 -123.36 58.40 REMARK 500 ALA L 51 -40.76 77.81 REMARK 500 SER L 52 11.71 -144.59 REMARK 500 ALA L 84 -178.93 175.40 REMARK 500 ASP A 103 -111.27 65.41 REMARK 500 VAL A 198 -77.35 -84.46 REMARK 500 SER B 30 -126.02 59.66 REMARK 500 ALA B 51 -41.42 78.97 REMARK 500 SER B 52 11.03 -144.71 REMARK 500 LYS B 170 -60.34 -101.01 REMARK 500 GLU B 214 -146.33 83.09 REMARK 500 ASP C 103 -109.14 67.69 REMARK 500 SER D 30 -125.38 58.51 REMARK 500 ALA D 51 -41.90 79.15 REMARK 500 SER D 52 11.27 -144.05 REMARK 500 ALA D 84 -174.67 -170.13 REMARK 500 LYS D 170 -61.81 -98.70 REMARK 500 ASP E 103 -110.33 66.19 REMARK 500 SER F 30 -124.90 58.88 REMARK 500 ALA F 51 -41.56 78.59 REMARK 500 SER F 52 11.37 -144.97 REMARK 500 ALA F 84 -175.30 -176.36 REMARK 500 LYS F 170 -63.80 -99.21 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 NAG C 301 DBREF 9GFG H 1 225 PDB 9GFG 9GFG 1 225 DBREF 9GFG L 1 215 PDB 9GFG 9GFG 1 215 DBREF 9GFG A 1 225 PDB 9GFG 9GFG 1 225 DBREF 9GFG B 1 215 PDB 9GFG 9GFG 1 215 DBREF 9GFG C 1 225 PDB 9GFG 9GFG 1 225 DBREF 9GFG D 1 215 PDB 9GFG 9GFG 1 215 DBREF 9GFG E 1 225 PDB 9GFG 9GFG 1 225 DBREF 9GFG F 1 215 PDB 9GFG 9GFG 1 215 SEQRES 1 H 225 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 225 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 H 225 TYR THR PHE THR SER TYR ALA MET HIS TRP VAL ARG GLN SEQRES 4 H 225 ALA PRO GLY GLN ARG LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 H 225 ALA GLY ASN GLY ASN THR LYS TYR SER GLN LYS PHE GLN SEQRES 6 H 225 GLY ARG VAL THR ILE THR ARG ASP THR SER ALA SER THR SEQRES 7 H 225 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 H 225 ALA VAL TYR TYR CYS ALA ARG GLU GLN TRP LEU ASP LEU SEQRES 9 H 225 ALA HIS PHE ASP TYR TRP GLY GLN GLY THR LEU VAL THR SEQRES 10 H 225 VAL SER SER GLY SER ALA SER ALA PRO THR LEU PHE PRO SEQRES 11 H 225 LEU VAL SER CYS GLU ASN SER PRO SER ASP THR SER SER SEQRES 12 H 225 VAL ALA VAL GLY CYS LEU ALA GLN ASP PHE LEU PRO ASP SEQRES 13 H 225 SER ILE THR PHE SER TRP LYS TYR LYS ASN ASN SER ASP SEQRES 14 H 225 ILE SER SER THR ARG GLY PHE PRO SER VAL LEU ARG GLY SEQRES 15 H 225 GLY LYS TYR ALA ALA THR SER GLN VAL LEU LEU PRO SER SEQRES 16 H 225 LYS ASP VAL MET GLN GLY THR ASP GLU HIS VAL VAL CYS SEQRES 17 H 225 LYS VAL GLN HIS PRO ASN GLY ASN LYS GLU LYS ASN VAL SEQRES 18 H 225 PRO LEU PRO VAL SEQRES 1 L 215 ASP ILE GLN LEU THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 215 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 215 GLN SER ILE SER SER TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 L 215 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA ALA SER SEQRES 5 L 215 SER LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 215 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 215 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER SEQRES 8 L 215 TYR SER THR PRO PRO TYR THR PHE GLY GLN GLY THR LYS SEQRES 9 L 215 LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 L 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 L 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 L 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 L 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 L 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 L 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 L 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 L 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 A 225 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 A 225 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 A 225 TYR THR PHE THR SER TYR ALA MET HIS TRP VAL ARG GLN SEQRES 4 A 225 ALA PRO GLY GLN ARG LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 A 225 ALA GLY ASN GLY ASN THR LYS TYR SER GLN LYS PHE GLN SEQRES 6 A 225 GLY ARG VAL THR ILE THR ARG ASP THR SER ALA SER THR SEQRES 7 A 225 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 A 225 ALA VAL TYR TYR CYS ALA ARG GLU GLN TRP LEU ASP LEU SEQRES 9 A 225 ALA HIS PHE ASP TYR TRP GLY GLN GLY THR LEU VAL THR SEQRES 10 A 225 VAL SER SER GLY SER ALA SER ALA PRO THR LEU PHE PRO SEQRES 11 A 225 LEU VAL SER CYS GLU ASN SER PRO SER ASP THR SER SER SEQRES 12 A 225 VAL ALA VAL GLY CYS LEU ALA GLN ASP PHE LEU PRO ASP SEQRES 13 A 225 SER ILE THR PHE SER TRP LYS TYR LYS ASN ASN SER ASP SEQRES 14 A 225 ILE SER SER THR ARG GLY PHE PRO SER VAL LEU ARG GLY SEQRES 15 A 225 GLY LYS TYR ALA ALA THR SER GLN VAL LEU LEU PRO SER SEQRES 16 A 225 LYS ASP VAL MET GLN GLY THR ASP GLU HIS VAL VAL CYS SEQRES 17 A 225 LYS VAL GLN HIS PRO ASN GLY ASN LYS GLU LYS ASN VAL SEQRES 18 A 225 PRO LEU PRO VAL SEQRES 1 B 215 ASP ILE GLN LEU THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 B 215 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 B 215 GLN SER ILE SER SER TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 B 215 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA ALA SER SEQRES 5 B 215 SER LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 B 215 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 B 215 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER SEQRES 8 B 215 TYR SER THR PRO PRO TYR THR PHE GLY GLN GLY THR LYS SEQRES 9 B 215 LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 B 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 B 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 B 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 B 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 B 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 B 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 B 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 B 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 C 225 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 C 225 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 C 225 TYR THR PHE THR SER TYR ALA MET HIS TRP VAL ARG GLN SEQRES 4 C 225 ALA PRO GLY GLN ARG LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 C 225 ALA GLY ASN GLY ASN THR LYS TYR SER GLN LYS PHE GLN SEQRES 6 C 225 GLY ARG VAL THR ILE THR ARG ASP THR SER ALA SER THR SEQRES 7 C 225 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 C 225 ALA VAL TYR TYR CYS ALA ARG GLU GLN TRP LEU ASP LEU SEQRES 9 C 225 ALA HIS PHE ASP TYR TRP GLY GLN GLY THR LEU VAL THR SEQRES 10 C 225 VAL SER SER GLY SER ALA SER ALA PRO THR LEU PHE PRO SEQRES 11 C 225 LEU VAL SER CYS GLU ASN SER PRO SER ASP THR SER SER SEQRES 12 C 225 VAL ALA VAL GLY CYS LEU ALA GLN ASP PHE LEU PRO ASP SEQRES 13 C 225 SER ILE THR PHE SER TRP LYS TYR LYS ASN ASN SER ASP SEQRES 14 C 225 ILE SER SER THR ARG GLY PHE PRO SER VAL LEU ARG GLY SEQRES 15 C 225 GLY LYS TYR ALA ALA THR SER GLN VAL LEU LEU PRO SER SEQRES 16 C 225 LYS ASP VAL MET GLN GLY THR ASP GLU HIS VAL VAL CYS SEQRES 17 C 225 LYS VAL GLN HIS PRO ASN GLY ASN LYS GLU LYS ASN VAL SEQRES 18 C 225 PRO LEU PRO VAL SEQRES 1 D 215 ASP ILE GLN LEU THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 D 215 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 D 215 GLN SER ILE SER SER TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 D 215 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA ALA SER SEQRES 5 D 215 SER LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 D 215 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 D 215 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER SEQRES 8 D 215 TYR SER THR PRO PRO TYR THR PHE GLY GLN GLY THR LYS SEQRES 9 D 215 LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 D 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 D 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 D 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 D 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 D 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 D 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 D 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 D 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 E 225 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 E 225 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 E 225 TYR THR PHE THR SER TYR ALA MET HIS TRP VAL ARG GLN SEQRES 4 E 225 ALA PRO GLY GLN ARG LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 E 225 ALA GLY ASN GLY ASN THR LYS TYR SER GLN LYS PHE GLN SEQRES 6 E 225 GLY ARG VAL THR ILE THR ARG ASP THR SER ALA SER THR SEQRES 7 E 225 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 E 225 ALA VAL TYR TYR CYS ALA ARG GLU GLN TRP LEU ASP LEU SEQRES 9 E 225 ALA HIS PHE ASP TYR TRP GLY GLN GLY THR LEU VAL THR SEQRES 10 E 225 VAL SER SER GLY SER ALA SER ALA PRO THR LEU PHE PRO SEQRES 11 E 225 LEU VAL SER CYS GLU ASN SER PRO SER ASP THR SER SER SEQRES 12 E 225 VAL ALA VAL GLY CYS LEU ALA GLN ASP PHE LEU PRO ASP SEQRES 13 E 225 SER ILE THR PHE SER TRP LYS TYR LYS ASN ASN SER ASP SEQRES 14 E 225 ILE SER SER THR ARG GLY PHE PRO SER VAL LEU ARG GLY SEQRES 15 E 225 GLY LYS TYR ALA ALA THR SER GLN VAL LEU LEU PRO SER SEQRES 16 E 225 LYS ASP VAL MET GLN GLY THR ASP GLU HIS VAL VAL CYS SEQRES 17 E 225 LYS VAL GLN HIS PRO ASN GLY ASN LYS GLU LYS ASN VAL SEQRES 18 E 225 PRO LEU PRO VAL SEQRES 1 F 215 ASP ILE GLN LEU THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 F 215 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 F 215 GLN SER ILE SER SER TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 F 215 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA ALA SER SEQRES 5 F 215 SER LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 F 215 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 F 215 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER SEQRES 8 F 215 TYR SER THR PRO PRO TYR THR PHE GLY GLN GLY THR LYS SEQRES 9 F 215 LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 F 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 F 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 F 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 F 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 F 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 F 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 F 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 F 215 SER PHE ASN ARG GLY GLU CYS HET NAG G 1 26 HET NAG G 2 27 HET GOL H 301 14 HET GOL H 302 14 HET GOL H 303 14 HET GOL L 301 14 HET NAG A 301 27 HET GOL A 302 14 HET GOL A 303 14 HET GOL B 301 13 HET GOL B 302 14 HET NAG C 301 27 HET GOL D 301 12 HET GOL D 302 14 HET GOL D 303 14 HET GOL E 301 14 HET GOL F 301 13 HET GOL F 302 13 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM GOL GLYCEROL 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 GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 9 NAG 4(C8 H15 N O6) FORMUL 10 GOL 14(C3 H8 O3) FORMUL 26 HOH *161(H2 O) HELIX 1 AA1 THR H 28 SER H 31 5 4 HELIX 2 AA2 ARG H 87 THR H 91 5 5 HELIX 3 AA3 SER H 195 GLN H 200 1 6 HELIX 4 AA4 GLN L 79 PHE L 83 5 5 HELIX 5 AA5 SER L 122 LYS L 127 1 6 HELIX 6 AA6 LYS L 184 LYS L 189 1 6 HELIX 7 AA7 THR A 28 SER A 31 5 4 HELIX 8 AA8 ARG A 87 THR A 91 5 5 HELIX 9 AA9 SER A 195 GLN A 200 1 6 HELIX 10 AB1 GLN B 79 PHE B 83 5 5 HELIX 11 AB2 SER B 122 LYS B 127 1 6 HELIX 12 AB3 LYS B 184 LYS B 189 1 6 HELIX 13 AB4 THR C 28 SER C 31 5 4 HELIX 14 AB5 ARG C 87 THR C 91 5 5 HELIX 15 AB6 GLN D 79 PHE D 83 5 5 HELIX 16 AB7 SER D 122 LYS D 127 1 6 HELIX 17 AB8 LYS D 184 LYS D 189 1 6 HELIX 18 AB9 THR E 28 SER E 31 5 4 HELIX 19 AC1 ARG E 87 THR E 91 5 5 HELIX 20 AC2 GLN F 79 PHE F 83 5 5 HELIX 21 AC3 SER F 122 LYS F 127 1 6 HELIX 22 AC4 LYS F 184 LYS F 189 1 6 SHEET 1 AA1 4 GLN H 3 GLN H 6 0 SHEET 2 AA1 4 VAL H 18 SER H 25 -1 O LYS H 23 N VAL H 5 SHEET 3 AA1 4 THR H 78 LEU H 83 -1 O MET H 81 N VAL H 20 SHEET 4 AA1 4 VAL H 68 ASP H 73 -1 N ASP H 73 O THR H 78 SHEET 1 AA2 6 GLU H 10 LYS H 12 0 SHEET 2 AA2 6 THR H 114 VAL H 118 1 O THR H 117 N GLU H 10 SHEET 3 AA2 6 ALA H 92 GLN H 100 -1 N ALA H 92 O VAL H 116 SHEET 4 AA2 6 ALA H 33 GLN H 39 -1 N HIS H 35 O ALA H 97 SHEET 5 AA2 6 LEU H 45 ASN H 52 -1 O GLU H 46 N ARG H 38 SHEET 6 AA2 6 THR H 58 TYR H 60 -1 O LYS H 59 N TRP H 50 SHEET 1 AA3 4 GLU H 10 LYS H 12 0 SHEET 2 AA3 4 THR H 114 VAL H 118 1 O THR H 117 N GLU H 10 SHEET 3 AA3 4 ALA H 92 GLN H 100 -1 N ALA H 92 O VAL H 116 SHEET 4 AA3 4 HIS H 106 TRP H 110 -1 O HIS H 106 N GLN H 100 SHEET 1 AA4 4 THR H 127 VAL H 132 0 SHEET 2 AA4 4 SER H 143 PHE H 153 -1 O LEU H 149 N PHE H 129 SHEET 3 AA4 4 LYS H 184 PRO H 194 -1 O ALA H 187 N ALA H 150 SHEET 4 AA4 4 VAL H 179 ARG H 181 -1 N ARG H 181 O LYS H 184 SHEET 1 AA5 3 THR H 159 LYS H 163 0 SHEET 2 AA5 3 HIS H 205 GLN H 211 -1 O LYS H 209 N SER H 161 SHEET 3 AA5 3 LYS H 217 PRO H 222 -1 O VAL H 221 N VAL H 206 SHEET 1 AA6 4 LEU L 4 SER L 7 0 SHEET 2 AA6 4 VAL L 19 ALA L 25 -1 O THR L 22 N SER L 7 SHEET 3 AA6 4 ASP L 70 ILE L 75 -1 O ILE L 75 N VAL L 19 SHEET 4 AA6 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AA7 6 SER L 10 SER L 14 0 SHEET 2 AA7 6 THR L 103 LYS L 108 1 O LYS L 108 N ALA L 13 SHEET 3 AA7 6 ALA L 84 GLN L 90 -1 N ALA L 84 O LEU L 105 SHEET 4 AA7 6 LEU L 33 GLN L 38 -1 N TYR L 36 O TYR L 87 SHEET 5 AA7 6 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AA7 6 SER L 53 LEU L 54 -1 O SER L 53 N TYR L 49 SHEET 1 AA8 4 SER L 10 SER L 14 0 SHEET 2 AA8 4 THR L 103 LYS L 108 1 O LYS L 108 N ALA L 13 SHEET 3 AA8 4 ALA L 84 GLN L 90 -1 N ALA L 84 O LEU L 105 SHEET 4 AA8 4 THR L 98 PHE L 99 -1 O THR L 98 N GLN L 90 SHEET 1 AA9 4 SER L 115 PHE L 119 0 SHEET 2 AA9 4 THR L 130 PHE L 140 -1 O VAL L 134 N PHE L 119 SHEET 3 AA9 4 TYR L 174 SER L 183 -1 O TYR L 174 N PHE L 140 SHEET 4 AA9 4 SER L 160 VAL L 164 -1 N GLN L 161 O THR L 179 SHEET 1 AB1 4 ALA L 154 LEU L 155 0 SHEET 2 AB1 4 LYS L 146 VAL L 151 -1 N VAL L 151 O ALA L 154 SHEET 3 AB1 4 VAL L 192 THR L 198 -1 O ALA L 194 N LYS L 150 SHEET 4 AB1 4 VAL L 206 ASN L 211 -1 O VAL L 206 N VAL L 197 SHEET 1 AB2 4 GLN A 3 GLN A 6 0 SHEET 2 AB2 4 VAL A 18 SER A 25 -1 O LYS A 23 N VAL A 5 SHEET 3 AB2 4 THR A 78 LEU A 83 -1 O MET A 81 N VAL A 20 SHEET 4 AB2 4 VAL A 68 ASP A 73 -1 N ASP A 73 O THR A 78 SHEET 1 AB3 6 GLU A 10 LYS A 12 0 SHEET 2 AB3 6 THR A 114 VAL A 118 1 O LEU A 115 N GLU A 10 SHEET 3 AB3 6 ALA A 92 GLN A 100 -1 N ALA A 92 O VAL A 116 SHEET 4 AB3 6 ALA A 33 GLN A 39 -1 N VAL A 37 O TYR A 95 SHEET 5 AB3 6 GLU A 46 ASN A 52 -1 O GLU A 46 N ARG A 38 SHEET 6 AB3 6 THR A 58 TYR A 60 -1 O LYS A 59 N TRP A 50 SHEET 1 AB4 4 GLU A 10 LYS A 12 0 SHEET 2 AB4 4 THR A 114 VAL A 118 1 O LEU A 115 N GLU A 10 SHEET 3 AB4 4 ALA A 92 GLN A 100 -1 N ALA A 92 O VAL A 116 SHEET 4 AB4 4 HIS A 106 TRP A 110 -1 O HIS A 106 N GLN A 100 SHEET 1 AB5 4 THR A 127 LEU A 131 0 SHEET 2 AB5 4 VAL A 144 PHE A 153 -1 O LEU A 149 N PHE A 129 SHEET 3 AB5 4 LYS A 184 LEU A 193 -1 O ALA A 187 N ALA A 150 SHEET 4 AB5 4 THR A 173 GLY A 175 -1 N ARG A 174 O GLN A 190 SHEET 1 AB6 4 THR A 127 LEU A 131 0 SHEET 2 AB6 4 VAL A 144 PHE A 153 -1 O LEU A 149 N PHE A 129 SHEET 3 AB6 4 LYS A 184 LEU A 193 -1 O ALA A 187 N ALA A 150 SHEET 4 AB6 4 VAL A 179 ARG A 181 -1 N ARG A 181 O LYS A 184 SHEET 1 AB7 3 THR A 159 LYS A 163 0 SHEET 2 AB7 3 HIS A 205 GLN A 211 -1 O LYS A 209 N SER A 161 SHEET 3 AB7 3 LYS A 217 PRO A 222 -1 O VAL A 221 N VAL A 206 SHEET 1 AB8 4 LEU B 4 SER B 7 0 SHEET 2 AB8 4 VAL B 19 ALA B 25 -1 O THR B 22 N SER B 7 SHEET 3 AB8 4 ASP B 70 ILE B 75 -1 O LEU B 73 N ILE B 21 SHEET 4 AB8 4 PHE B 62 SER B 67 -1 N SER B 63 O THR B 74 SHEET 1 AB9 6 SER B 10 ALA B 13 0 SHEET 2 AB9 6 THR B 103 ILE B 107 1 O GLU B 106 N LEU B 11 SHEET 3 AB9 6 THR B 85 GLN B 90 -1 N TYR B 86 O THR B 103 SHEET 4 AB9 6 LEU B 33 GLN B 38 -1 N TYR B 36 O TYR B 87 SHEET 5 AB9 6 LYS B 45 TYR B 49 -1 O LYS B 45 N GLN B 37 SHEET 6 AB9 6 SER B 53 LEU B 54 -1 O SER B 53 N TYR B 49 SHEET 1 AC1 4 SER B 10 ALA B 13 0 SHEET 2 AC1 4 THR B 103 ILE B 107 1 O GLU B 106 N LEU B 11 SHEET 3 AC1 4 THR B 85 GLN B 90 -1 N TYR B 86 O THR B 103 SHEET 4 AC1 4 THR B 98 PHE B 99 -1 O THR B 98 N GLN B 90 SHEET 1 AC2 4 SER B 115 PHE B 119 0 SHEET 2 AC2 4 THR B 130 PHE B 140 -1 O VAL B 134 N PHE B 119 SHEET 3 AC2 4 TYR B 174 SER B 183 -1 O TYR B 174 N PHE B 140 SHEET 4 AC2 4 SER B 160 VAL B 164 -1 N GLN B 161 O THR B 179 SHEET 1 AC3 4 ALA B 154 LEU B 155 0 SHEET 2 AC3 4 LYS B 146 VAL B 151 -1 N VAL B 151 O ALA B 154 SHEET 3 AC3 4 VAL B 192 THR B 198 -1 O ALA B 194 N LYS B 150 SHEET 4 AC3 4 VAL B 206 ASN B 211 -1 O VAL B 206 N VAL B 197 SHEET 1 AC4 4 GLN C 3 GLN C 6 0 SHEET 2 AC4 4 VAL C 18 SER C 25 -1 O LYS C 23 N VAL C 5 SHEET 3 AC4 4 THR C 78 LEU C 83 -1 O MET C 81 N VAL C 20 SHEET 4 AC4 4 VAL C 68 ASP C 73 -1 N ASP C 73 O THR C 78 SHEET 1 AC5 6 GLU C 10 LYS C 12 0 SHEET 2 AC5 6 THR C 114 VAL C 118 1 O LEU C 115 N GLU C 10 SHEET 3 AC5 6 ALA C 92 GLN C 100 -1 N ALA C 92 O VAL C 116 SHEET 4 AC5 6 ALA C 33 GLN C 39 -1 N VAL C 37 O TYR C 95 SHEET 5 AC5 6 LEU C 45 ASN C 52 -1 O GLU C 46 N ARG C 38 SHEET 6 AC5 6 THR C 58 TYR C 60 -1 O LYS C 59 N TRP C 50 SHEET 1 AC6 4 GLU C 10 LYS C 12 0 SHEET 2 AC6 4 THR C 114 VAL C 118 1 O LEU C 115 N GLU C 10 SHEET 3 AC6 4 ALA C 92 GLN C 100 -1 N ALA C 92 O VAL C 116 SHEET 4 AC6 4 HIS C 106 TRP C 110 -1 O HIS C 106 N GLN C 100 SHEET 1 AC7 4 THR C 127 LEU C 131 0 SHEET 2 AC7 4 SER C 143 PHE C 153 -1 O LEU C 149 N PHE C 129 SHEET 3 AC7 4 LYS C 184 PRO C 194 -1 O ALA C 187 N ALA C 150 SHEET 4 AC7 4 THR C 173 GLY C 175 -1 N ARG C 174 O GLN C 190 SHEET 1 AC8 4 THR C 127 LEU C 131 0 SHEET 2 AC8 4 SER C 143 PHE C 153 -1 O LEU C 149 N PHE C 129 SHEET 3 AC8 4 LYS C 184 PRO C 194 -1 O ALA C 187 N ALA C 150 SHEET 4 AC8 4 VAL C 179 ARG C 181 -1 N ARG C 181 O LYS C 184 SHEET 1 AC9 3 THR C 159 LYS C 163 0 SHEET 2 AC9 3 VAL C 207 GLN C 211 -1 O LYS C 209 N SER C 161 SHEET 3 AC9 3 LYS C 217 ASN C 220 -1 O LYS C 219 N CYS C 208 SHEET 1 AD1 4 LEU D 4 SER D 7 0 SHEET 2 AD1 4 VAL D 19 ALA D 25 -1 O THR D 22 N SER D 7 SHEET 3 AD1 4 ASP D 70 ILE D 75 -1 O ILE D 75 N VAL D 19 SHEET 4 AD1 4 PHE D 62 SER D 67 -1 N SER D 63 O THR D 74 SHEET 1 AD2 6 SER D 10 ALA D 13 0 SHEET 2 AD2 6 THR D 103 ILE D 107 1 O GLU D 106 N LEU D 11 SHEET 3 AD2 6 THR D 85 GLN D 90 -1 N TYR D 86 O THR D 103 SHEET 4 AD2 6 LEU D 33 GLN D 38 -1 N ASN D 34 O GLN D 89 SHEET 5 AD2 6 LYS D 45 TYR D 49 -1 O LEU D 47 N TRP D 35 SHEET 6 AD2 6 SER D 53 LEU D 54 -1 O SER D 53 N TYR D 49 SHEET 1 AD3 4 SER D 115 PHE D 119 0 SHEET 2 AD3 4 THR D 130 PHE D 140 -1 O VAL D 134 N PHE D 119 SHEET 3 AD3 4 TYR D 174 SER D 183 -1 O TYR D 174 N PHE D 140 SHEET 4 AD3 4 SER D 160 VAL D 164 -1 N GLN D 161 O THR D 179 SHEET 1 AD4 4 ALA D 154 LEU D 155 0 SHEET 2 AD4 4 LYS D 146 VAL D 151 -1 N VAL D 151 O ALA D 154 SHEET 3 AD4 4 VAL D 192 THR D 198 -1 O ALA D 194 N LYS D 150 SHEET 4 AD4 4 VAL D 206 ASN D 211 -1 O VAL D 206 N VAL D 197 SHEET 1 AD5 4 GLN E 3 GLN E 6 0 SHEET 2 AD5 4 VAL E 18 SER E 25 -1 O LYS E 23 N VAL E 5 SHEET 3 AD5 4 THR E 78 LEU E 83 -1 O MET E 81 N VAL E 20 SHEET 4 AD5 4 VAL E 68 ASP E 73 -1 N THR E 69 O GLU E 82 SHEET 1 AD6 6 GLU E 10 LYS E 12 0 SHEET 2 AD6 6 THR E 114 VAL E 118 1 O THR E 117 N GLU E 10 SHEET 3 AD6 6 ALA E 92 GLN E 100 -1 N ALA E 92 O VAL E 116 SHEET 4 AD6 6 ALA E 33 GLN E 39 -1 N VAL E 37 O TYR E 95 SHEET 5 AD6 6 LEU E 45 ASN E 52 -1 O GLU E 46 N ARG E 38 SHEET 6 AD6 6 THR E 58 TYR E 60 -1 O LYS E 59 N TRP E 50 SHEET 1 AD7 4 GLU E 10 LYS E 12 0 SHEET 2 AD7 4 THR E 114 VAL E 118 1 O THR E 117 N GLU E 10 SHEET 3 AD7 4 ALA E 92 GLN E 100 -1 N ALA E 92 O VAL E 116 SHEET 4 AD7 4 HIS E 106 TRP E 110 -1 O HIS E 106 N GLN E 100 SHEET 1 AD8 4 THR E 127 LEU E 131 0 SHEET 2 AD8 4 VAL E 144 PHE E 153 -1 O LEU E 149 N PHE E 129 SHEET 3 AD8 4 LYS E 184 LEU E 193 -1 O LEU E 193 N VAL E 144 SHEET 4 AD8 4 THR E 173 GLY E 175 -1 N ARG E 174 O GLN E 190 SHEET 1 AD9 4 THR E 127 LEU E 131 0 SHEET 2 AD9 4 VAL E 144 PHE E 153 -1 O LEU E 149 N PHE E 129 SHEET 3 AD9 4 LYS E 184 LEU E 193 -1 O LEU E 193 N VAL E 144 SHEET 4 AD9 4 VAL E 179 ARG E 181 -1 N ARG E 181 O LYS E 184 SHEET 1 AE1 3 THR E 159 LYS E 163 0 SHEET 2 AE1 3 VAL E 207 GLN E 211 -1 O LYS E 209 N SER E 161 SHEET 3 AE1 3 LYS E 217 ASN E 220 -1 O LYS E 219 N CYS E 208 SHEET 1 AE2 4 LEU F 4 SER F 7 0 SHEET 2 AE2 4 VAL F 19 ALA F 25 -1 O THR F 22 N SER F 7 SHEET 3 AE2 4 ASP F 70 ILE F 75 -1 O ILE F 75 N VAL F 19 SHEET 4 AE2 4 PHE F 62 SER F 67 -1 N SER F 63 O THR F 74 SHEET 1 AE3 6 SER F 10 ALA F 13 0 SHEET 2 AE3 6 THR F 103 ILE F 107 1 O GLU F 106 N LEU F 11 SHEET 3 AE3 6 THR F 85 GLN F 90 -1 N TYR F 86 O THR F 103 SHEET 4 AE3 6 LEU F 33 GLN F 38 -1 N TYR F 36 O TYR F 87 SHEET 5 AE3 6 LYS F 45 TYR F 49 -1 O LEU F 47 N TRP F 35 SHEET 6 AE3 6 SER F 53 LEU F 54 -1 O SER F 53 N TYR F 49 SHEET 1 AE4 4 SER F 115 PHE F 119 0 SHEET 2 AE4 4 THR F 130 PHE F 140 -1 O VAL F 134 N PHE F 119 SHEET 3 AE4 4 TYR F 174 SER F 183 -1 O TYR F 174 N PHE F 140 SHEET 4 AE4 4 SER F 160 VAL F 164 -1 N GLN F 161 O THR F 179 SHEET 1 AE5 4 ALA F 154 LEU F 155 0 SHEET 2 AE5 4 LYS F 146 VAL F 151 -1 N VAL F 151 O ALA F 154 SHEET 3 AE5 4 VAL F 192 THR F 198 -1 O ALA F 194 N LYS F 150 SHEET 4 AE5 4 VAL F 206 ASN F 211 -1 O VAL F 206 N VAL F 197 SSBOND 1 CYS H 22 CYS H 96 1555 1555 2.04 SSBOND 2 CYS H 148 CYS H 208 1555 1555 2.04 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.05 SSBOND 4 CYS L 135 CYS L 195 1555 1555 2.05 SSBOND 5 CYS A 22 CYS A 96 1555 1555 2.04 SSBOND 6 CYS A 134 CYS B 215 1555 1555 2.04 SSBOND 7 CYS A 148 CYS A 208 1555 1555 2.04 SSBOND 8 CYS B 23 CYS B 88 1555 1555 2.05 SSBOND 9 CYS B 135 CYS B 195 1555 1555 2.05 SSBOND 10 CYS C 22 CYS C 96 1555 1555 2.03 SSBOND 11 CYS C 148 CYS C 208 1555 1555 2.04 SSBOND 12 CYS D 23 CYS D 88 1555 1555 2.05 SSBOND 13 CYS D 135 CYS D 195 1555 1555 2.04 SSBOND 14 CYS E 22 CYS E 96 1555 1555 2.03 SSBOND 15 CYS E 148 CYS E 208 1555 1555 2.04 SSBOND 16 CYS F 23 CYS F 88 1555 1555 2.05 SSBOND 17 CYS F 135 CYS F 195 1555 1555 2.04 LINK ND2 ASN H 166 C1 NAG G 1 1555 1555 1.39 LINK ND2 ASN A 166 C1 NAG A 301 1555 1555 1.46 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.42 CISPEP 1 LEU H 154 PRO H 155 0 4.69 CISPEP 2 SER L 7 PRO L 8 0 -6.76 CISPEP 3 THR L 94 PRO L 95 0 -5.14 CISPEP 4 PRO L 95 PRO L 96 0 -1.76 CISPEP 5 TYR L 141 PRO L 142 0 2.34 CISPEP 6 LEU A 154 PRO A 155 0 3.67 CISPEP 7 SER B 7 PRO B 8 0 -5.17 CISPEP 8 THR B 94 PRO B 95 0 -5.31 CISPEP 9 PRO B 95 PRO B 96 0 -2.38 CISPEP 10 TYR B 141 PRO B 142 0 2.51 CISPEP 11 LEU C 154 PRO C 155 0 4.17 CISPEP 12 SER D 7 PRO D 8 0 -6.41 CISPEP 13 THR D 94 PRO D 95 0 -5.05 CISPEP 14 PRO D 95 PRO D 96 0 -2.69 CISPEP 15 TYR D 141 PRO D 142 0 2.13 CISPEP 16 LEU E 154 PRO E 155 0 4.12 CISPEP 17 SER F 7 PRO F 8 0 -6.32 CISPEP 18 THR F 94 PRO F 95 0 -5.31 CISPEP 19 PRO F 95 PRO F 96 0 -2.46 CISPEP 20 TYR F 141 PRO F 142 0 2.38 CRYST1 104.696 87.891 115.528 90.00 94.59 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 0.009551 0.000000 0.000767 0.00000 SCALE2 0.000000 0.011378 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008684 0.00000 MTRIX1 1 -0.692887 0.563031 0.450448 -37.74660 1 MTRIX2 1 0.566414 0.038436 0.823224 2.90112 1 MTRIX3 1 0.446188 0.825541 -0.345540 23.18050 1 MTRIX1 2 0.675180 -0.529242 -0.513843 10.82147 1 MTRIX2 2 0.620991 0.031845 0.783170 5.15024 1 MTRIX3 2 -0.398123 -0.847873 0.350156 -26.44235 1 MTRIX1 3 -0.981800 -0.169275 -0.086111 -22.52463 1 MTRIX2 3 -0.172544 0.984482 0.032004 -2.90021 1 MTRIX3 3 0.079357 0.046279 -0.995771 -2.77335 1 MTRIX1 4 -0.671807 0.558652 0.486399 -38.72622 1 MTRIX2 4 0.571370 -0.027058 0.820246 3.75920 1 MTRIX3 4 0.471393 0.828961 -0.301019 22.33535 1 MTRIX1 5 0.654051 -0.525706 -0.543921 11.30272 1 MTRIX2 5 0.638105 -0.002731 0.769945 6.46622 1 MTRIX3 5 -0.406250 -0.850662 0.333669 -25.97448 1 MTRIX1 6 -0.971307 -0.188730 -0.144718 -18.88045 1 MTRIX2 6 -0.188351 0.981964 -0.016445 -1.65002 1 MTRIX3 6 0.145212 0.011285 -0.989336 -1.11379 1