HEADER CELL ADHESION/IMMUNE SYSTEM 02-JAN-20 6VEL TITLE CRYSTAL STRUCTURE OF HUMAN E-CADHERIN BOUND BY MOUSE MONOCLONAL TITLE 2 ANTIBODY 66E8FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: 66E8 FAB HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 SYNONYM: MUMUA.20194.A.LG23; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: 66E8 FAB LIGHT CHAIN; COMPND 8 CHAIN: L; COMPND 9 SYNONYM: MUMUA.20195.A.LH23; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: UBIQUITIN-LIKE PROTEIN, SMT3,CADHERIN-1 CHIMERA; COMPND 13 CHAIN: C; COMPND 14 SYNONYM: CAM 120/80,EPITHELIAL CADHERIN,E-CADHERIN,UVOMORULIN; COMPND 15 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET-21A_MODIFIED; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 10 ORGANISM_TAXID: 10090; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 12 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 13 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 14 EXPRESSION_SYSTEM_PLASMID: LH; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 / SOURCE 17 S288C), HOMO SAPIENS; SOURCE 18 ORGANISM_COMMON: BAKER'S YEAST, HUMAN; SOURCE 19 ORGANISM_TAXID: 559292, 9606; SOURCE 20 STRAIN: ATCC 204508 / S288C; SOURCE 21 GENE: SMT3, YDR510W, D9719.15, CDH1, CDHE, UVO; SOURCE 22 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 23 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 24 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 25 EXPRESSION_SYSTEM_PLASMID: PET-21A_MODIFIED KEYWDS SSGCID, CADHERIN, E-CADHERIN, ANTIBODY, STRUCTURAL GENOMICS, SEATTLE KEYWDS 2 STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE, CELL ADHESION, KEYWDS 3 CELL ADHESION-IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE,SEATTLE AUTHOR 2 STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID) REVDAT 1 29-JAN-20 6VEL 0 JRNL AUTH M.J.BOLEJACK,J.ABENDROTH,A.Y.MAKER,B.M.GUMBINER,D.D.LORIMER, JRNL AUTH 2 P.S.HORANYI,T.E.EDWARDS JRNL TITL CRYSTAL STRUCTURE OF HUMAN E-CADHERIN BOUND BY MOUSE JRNL TITL 2 MONOCLONAL ANTIBODY 66E8FAB JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.65 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.17.1-3660 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.54 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 30872 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.186 REMARK 3 R VALUE (WORKING SET) : 0.183 REMARK 3 FREE R VALUE : 0.233 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990 REMARK 3 FREE R VALUE TEST SET COUNT : 1542 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 46.5400 - 5.8900 1.00 2797 138 0.1826 0.2357 REMARK 3 2 5.8900 - 4.6800 1.00 2708 139 0.1523 0.1861 REMARK 3 3 4.6800 - 4.0900 1.00 2688 130 0.1392 0.1867 REMARK 3 4 4.0900 - 3.7100 1.00 2679 142 0.1753 0.2280 REMARK 3 5 3.7100 - 3.4500 1.00 2653 131 0.1998 0.2509 REMARK 3 6 3.4500 - 3.2400 1.00 2601 169 0.2104 0.2641 REMARK 3 7 3.2400 - 3.0800 1.00 2660 150 0.2227 0.2511 REMARK 3 8 3.0800 - 2.9500 1.00 2636 130 0.2236 0.2961 REMARK 3 9 2.9500 - 2.8300 1.00 2649 134 0.2258 0.2736 REMARK 3 10 2.8300 - 2.7400 1.00 2627 122 0.2274 0.3082 REMARK 3 11 2.7400 - 2.6500 1.00 2632 157 0.2454 0.2941 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) : 0.360 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.120 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 60.26 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 72.01 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 : 0.004 4866 REMARK 3 ANGLE : 0.666 6667 REMARK 3 CHIRALITY : 0.045 769 REMARK 3 PLANARITY : 0.004 859 REMARK 3 DIHEDRAL : 17.718 1691 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 10 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 20 THROUGH 141 ) REMARK 3 ORIGIN FOR THE GROUP (A): -60.7177 50.8828 11.0362 REMARK 3 T TENSOR REMARK 3 T11: 0.3697 T22: 0.3818 REMARK 3 T33: 0.2956 T12: 0.0118 REMARK 3 T13: 0.0754 T23: -0.0037 REMARK 3 L TENSOR REMARK 3 L11: 1.9560 L22: 6.7943 REMARK 3 L33: 2.7402 L12: -0.2244 REMARK 3 L13: -0.4440 L23: 0.7376 REMARK 3 S TENSOR REMARK 3 S11: 0.1509 S12: -0.0078 S13: 0.3031 REMARK 3 S21: 0.0516 S22: -0.0187 S23: -0.0255 REMARK 3 S31: -0.2787 S32: -0.0130 S33: -0.1509 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 142 THROUGH 179 ) REMARK 3 ORIGIN FOR THE GROUP (A): -61.6682 76.5402 -13.2586 REMARK 3 T TENSOR REMARK 3 T11: 0.9588 T22: 0.7988 REMARK 3 T33: 0.7563 T12: 0.2578 REMARK 3 T13: 0.2641 T23: 0.2154 REMARK 3 L TENSOR REMARK 3 L11: 5.8189 L22: 8.8734 REMARK 3 L33: 2.3518 L12: 1.3910 REMARK 3 L13: 1.1388 L23: 1.0350 REMARK 3 S TENSOR REMARK 3 S11: 0.3093 S12: 0.7957 S13: 0.4420 REMARK 3 S21: -0.0831 S22: 0.2142 S23: 0.6379 REMARK 3 S31: -1.1926 S32: -1.4063 S33: -0.5642 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 180 THROUGH 235 ) REMARK 3 ORIGIN FOR THE GROUP (A): -63.0937 75.6532 -14.8010 REMARK 3 T TENSOR REMARK 3 T11: 0.9278 T22: 0.9093 REMARK 3 T33: 0.7945 T12: 0.2149 REMARK 3 T13: 0.2222 T23: 0.2435 REMARK 3 L TENSOR REMARK 3 L11: 2.3486 L22: 4.6168 REMARK 3 L33: 5.7485 L12: 0.1034 REMARK 3 L13: -0.3742 L23: -1.3169 REMARK 3 S TENSOR REMARK 3 S11: 0.1021 S12: 0.4684 S13: 0.5043 REMARK 3 S21: -0.2207 S22: 0.5459 S23: 0.6977 REMARK 3 S31: -1.4050 S32: -1.0245 S33: -0.6002 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 20 THROUGH 109 ) REMARK 3 ORIGIN FOR THE GROUP (A): -49.7531 40.3819 -6.5197 REMARK 3 T TENSOR REMARK 3 T11: 0.3028 T22: 0.3587 REMARK 3 T33: 0.2985 T12: 0.0246 REMARK 3 T13: 0.0273 T23: -0.0269 REMARK 3 L TENSOR REMARK 3 L11: 3.0977 L22: 4.6096 REMARK 3 L33: 7.5119 L12: 0.4415 REMARK 3 L13: 0.3493 L23: -2.0740 REMARK 3 S TENSOR REMARK 3 S11: -0.0103 S12: 0.2693 S13: 0.1151 REMARK 3 S21: -0.1843 S22: 0.0107 S23: -0.1746 REMARK 3 S31: 0.0526 S32: 0.2895 S33: 0.0212 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 110 THROUGH 147 ) REMARK 3 ORIGIN FOR THE GROUP (A): -50.5968 62.2750 -9.5649 REMARK 3 T TENSOR REMARK 3 T11: 0.7129 T22: 0.4051 REMARK 3 T33: 0.4976 T12: -0.0517 REMARK 3 T13: 0.1294 T23: -0.0165 REMARK 3 L TENSOR REMARK 3 L11: 1.3648 L22: 0.3089 REMARK 3 L33: 1.4505 L12: 0.3854 REMARK 3 L13: -0.7710 L23: 0.3691 REMARK 3 S TENSOR REMARK 3 S11: 0.2557 S12: -0.0189 S13: 0.5050 REMARK 3 S21: 0.2560 S22: 0.1547 S23: 0.0542 REMARK 3 S31: -0.9727 S32: 0.0580 S33: -0.3925 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 148 THROUGH 193 ) REMARK 3 ORIGIN FOR THE GROUP (A): -46.7853 70.5911 -15.2488 REMARK 3 T TENSOR REMARK 3 T11: 0.8163 T22: 0.6024 REMARK 3 T33: 0.6971 T12: -0.1851 REMARK 3 T13: 0.2387 T23: -0.0375 REMARK 3 L TENSOR REMARK 3 L11: 3.5525 L22: 9.0551 REMARK 3 L33: 6.3299 L12: 0.2904 REMARK 3 L13: -0.8175 L23: 1.8108 REMARK 3 S TENSOR REMARK 3 S11: 0.5212 S12: -0.1854 S13: 0.7031 REMARK 3 S21: 1.0725 S22: 0.5194 S23: 0.2466 REMARK 3 S31: -1.1772 S32: 0.3461 S33: -0.8533 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 194 THROUGH 229 ) REMARK 3 ORIGIN FOR THE GROUP (A): -43.4571 80.5541 -17.2181 REMARK 3 T TENSOR REMARK 3 T11: 1.5605 T22: 0.6978 REMARK 3 T33: 1.2667 T12: -0.4294 REMARK 3 T13: 0.4728 T23: -0.0797 REMARK 3 L TENSOR REMARK 3 L11: 1.3665 L22: 2.4264 REMARK 3 L33: 0.5252 L12: 0.2019 REMARK 3 L13: 0.6351 L23: -0.7484 REMARK 3 S TENSOR REMARK 3 S11: 0.4939 S12: 0.0387 S13: 1.5169 REMARK 3 S21: -0.0474 S22: 0.5904 S23: -0.6954 REMARK 3 S31: -2.0746 S32: 0.8432 S33: -0.5162 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 102 THROUGH 173 ) REMARK 3 ORIGIN FOR THE GROUP (A): -17.6733 22.8984 5.3613 REMARK 3 T TENSOR REMARK 3 T11: 0.6117 T22: 1.2097 REMARK 3 T33: 0.8783 T12: 0.2449 REMARK 3 T13: -0.0444 T23: -0.2851 REMARK 3 L TENSOR REMARK 3 L11: 6.2445 L22: 3.1495 REMARK 3 L33: 2.4528 L12: 0.7720 REMARK 3 L13: -1.5617 L23: -0.4326 REMARK 3 S TENSOR REMARK 3 S11: 0.4807 S12: 2.2797 S13: -0.8338 REMARK 3 S21: -0.0937 S22: -0.0162 S23: -0.7773 REMARK 3 S31: -0.1963 S32: 0.5761 S33: -0.4508 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 174 THROUGH 247 ) REMARK 3 ORIGIN FOR THE GROUP (A): -41.9293 18.6590 12.9579 REMARK 3 T TENSOR REMARK 3 T11: 0.7176 T22: 0.4496 REMARK 3 T33: 0.5973 T12: 0.1354 REMARK 3 T13: -0.1063 T23: -0.0882 REMARK 3 L TENSOR REMARK 3 L11: 6.7048 L22: 0.8920 REMARK 3 L33: 2.4721 L12: 1.4845 REMARK 3 L13: -1.7480 L23: 0.4585 REMARK 3 S TENSOR REMARK 3 S11: -0.2686 S12: 0.4794 S13: -1.1872 REMARK 3 S21: 0.2091 S22: 0.2459 S23: -0.4322 REMARK 3 S31: 0.4920 S32: 0.3374 S33: 0.1268 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 248 THROUGH 314 ) REMARK 3 ORIGIN FOR THE GROUP (A): -65.8171 24.8745 20.0295 REMARK 3 T TENSOR REMARK 3 T11: 0.6378 T22: 0.4109 REMARK 3 T33: 0.3110 T12: -0.0419 REMARK 3 T13: 0.0066 T23: 0.0117 REMARK 3 L TENSOR REMARK 3 L11: 2.6506 L22: 2.2439 REMARK 3 L33: 3.1038 L12: 0.5552 REMARK 3 L13: -2.4633 L23: -0.3933 REMARK 3 S TENSOR REMARK 3 S11: 0.0744 S12: 0.1805 S13: 0.0081 REMARK 3 S21: 0.3865 S22: 0.0764 S23: 0.2039 REMARK 3 S31: 0.5651 S32: -0.3205 S33: -0.1601 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 6VEL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JAN-20. REMARK 100 THE DEPOSITION ID IS D_1000246194. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 18-JUL-19 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 21-ID-F REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872 REMARK 200 MONOCHROMATOR : DIAMOND [111] REMARK 200 OPTICS : BERYLLIUM LENSES REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30906 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.650 REMARK 200 RESOLUTION RANGE LOW (A) : 46.540 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 8.734 REMARK 200 R MERGE (I) : 0.06100 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 24.6800 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.72 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 8.98 REMARK 200 R MERGE FOR SHELL (I) : 0.59500 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.560 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: 2O72 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 59.52 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.04 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: A COMPLEX OF HOSAA.19747.A.KW2, REMARK 280 MUMUA.20194.A.LG23, AND MUMUA.20195.A.LH23 WAS CRYSTALLIZED AT REMARK 280 10.4 MG/ML AT 14C AND MIXED 1:1 WITH 12.5% (W/V) PEG 4000, 20% REMARK 280 (V/V) 1,2,6-HEXANETRIOL, 0.1M GLYGLY/AMPD PH 8.5, 0.03M OF EACH REMARK 280 LITHIUM SULFATE, SODIUM SULFATE, AND POTASSIUM SULFATE. TRAY REMARK 280 307437A10: PUCK CKT8-9., VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 290K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+1/3 REMARK 290 3555 -X+Y,-X,Z+2/3 REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z+2/3 REMARK 290 6555 -X,-X+Y,-Z+1/3 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 30.10667 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 60.21333 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 60.21333 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 30.10667 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6150 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 29420 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -137.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, C 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 S SO4 C 402 LIES ON A SPECIAL POSITION. REMARK 375 O2 SO4 C 402 LIES ON A SPECIAL POSITION. 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 HIS H -2 REMARK 465 HIS H -1 REMARK 465 HIS H 0 REMARK 465 MET H 1 REMARK 465 GLY H 2 REMARK 465 TRP H 3 REMARK 465 SER H 4 REMARK 465 CYS H 5 REMARK 465 ILE H 6 REMARK 465 ILE H 7 REMARK 465 LEU H 8 REMARK 465 PHE H 9 REMARK 465 LEU H 10 REMARK 465 VAL H 11 REMARK 465 ALA H 12 REMARK 465 THR H 13 REMARK 465 ALA H 14 REMARK 465 THR H 15 REMARK 465 GLY H 16 REMARK 465 VAL H 17 REMARK 465 HIS H 18 REMARK 465 SER H 19 REMARK 465 GLY H 149 REMARK 465 SER H 150 REMARK 465 ALA H 151 REMARK 465 ALA H 152 REMARK 465 GLN H 153 REMARK 465 ASP H 236 REMARK 465 CYS H 237 REMARK 465 HIS H 238 REMARK 465 HIS H 239 REMARK 465 HIS H 240 REMARK 465 HIS H 241 REMARK 465 HIS H 242 REMARK 465 HIS H 243 REMARK 465 MET L 1 REMARK 465 GLY L 2 REMARK 465 TRP L 3 REMARK 465 SER L 4 REMARK 465 CYS L 5 REMARK 465 ILE L 6 REMARK 465 ILE L 7 REMARK 465 LEU L 8 REMARK 465 PHE L 9 REMARK 465 LEU L 10 REMARK 465 VAL L 11 REMARK 465 ALA L 12 REMARK 465 THR L 13 REMARK 465 ALA L 14 REMARK 465 THR L 15 REMARK 465 GLY L 16 REMARK 465 VAL L 17 REMARK 465 HIS L 18 REMARK 465 SER L 19 REMARK 465 ARG L 230 REMARK 465 ASN L 231 REMARK 465 GLU L 232 REMARK 465 CYS L 233 REMARK 465 MET C -12 REMARK 465 ALA C -11 REMARK 465 SER C -10 REMARK 465 MET C -9 REMARK 465 HIS C -8 REMARK 465 HIS C -7 REMARK 465 HIS C -6 REMARK 465 HIS C -5 REMARK 465 HIS C -4 REMARK 465 HIS C -3 REMARK 465 GLY C -2 REMARK 465 SER C -1 REMARK 465 SER C 0 REMARK 465 MET C 1 REMARK 465 ALA C 2 REMARK 465 SER C 3 REMARK 465 MET C 4 REMARK 465 SER C 5 REMARK 465 ASP C 6 REMARK 465 SER C 7 REMARK 465 GLU C 8 REMARK 465 VAL C 9 REMARK 465 ASN C 10 REMARK 465 GLN C 11 REMARK 465 GLU C 12 REMARK 465 ALA C 13 REMARK 465 LYS C 14 REMARK 465 PRO C 15 REMARK 465 GLU C 16 REMARK 465 VAL C 17 REMARK 465 LYS C 18 REMARK 465 PRO C 19 REMARK 465 GLU C 20 REMARK 465 VAL C 21 REMARK 465 LYS C 22 REMARK 465 PRO C 23 REMARK 465 GLU C 24 REMARK 465 THR C 25 REMARK 465 HIS C 26 REMARK 465 ILE C 27 REMARK 465 ASN C 28 REMARK 465 LEU C 29 REMARK 465 LYS C 30 REMARK 465 VAL C 31 REMARK 465 SER C 32 REMARK 465 ASP C 33 REMARK 465 GLY C 34 REMARK 465 SER C 35 REMARK 465 SER C 36 REMARK 465 GLU C 37 REMARK 465 ILE C 38 REMARK 465 PHE C 39 REMARK 465 PHE C 40 REMARK 465 LYS C 41 REMARK 465 ILE C 42 REMARK 465 LYS C 43 REMARK 465 LYS C 44 REMARK 465 THR C 45 REMARK 465 THR C 46 REMARK 465 PRO C 47 REMARK 465 LEU C 48 REMARK 465 ARG C 49 REMARK 465 ARG C 50 REMARK 465 LEU C 51 REMARK 465 MET C 52 REMARK 465 GLU C 53 REMARK 465 ALA C 54 REMARK 465 PHE C 55 REMARK 465 ALA C 56 REMARK 465 LYS C 57 REMARK 465 ARG C 58 REMARK 465 GLN C 59 REMARK 465 GLY C 60 REMARK 465 LYS C 61 REMARK 465 GLU C 62 REMARK 465 MET C 63 REMARK 465 ASP C 64 REMARK 465 SER C 65 REMARK 465 LEU C 66 REMARK 465 ARG C 67 REMARK 465 PHE C 68 REMARK 465 LEU C 69 REMARK 465 TYR C 70 REMARK 465 ASP C 71 REMARK 465 GLY C 72 REMARK 465 ILE C 73 REMARK 465 ARG C 74 REMARK 465 ILE C 75 REMARK 465 GLN C 76 REMARK 465 ALA C 77 REMARK 465 ASP C 78 REMARK 465 GLN C 79 REMARK 465 THR C 80 REMARK 465 PRO C 81 REMARK 465 GLU C 82 REMARK 465 ASP C 83 REMARK 465 LEU C 84 REMARK 465 ASP C 85 REMARK 465 MET C 86 REMARK 465 GLU C 87 REMARK 465 ASP C 88 REMARK 465 ASN C 89 REMARK 465 ASP C 90 REMARK 465 ILE C 91 REMARK 465 ILE C 92 REMARK 465 GLU C 93 REMARK 465 ALA C 94 REMARK 465 HIS C 95 REMARK 465 ARG C 96 REMARK 465 GLU C 97 REMARK 465 GLN C 98 REMARK 465 ILE C 99 REMARK 465 GLY C 100 REMARK 465 GLY C 101 REMARK 465 VAL C 182 REMARK 465 SER C 183 REMARK 465 SER C 184 REMARK 465 ASN C 185 REMARK 465 THR C 315 REMARK 465 ASN C 316 REMARK 465 ASP C 317 REMARK 465 ASN C 318 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 LYS H 32 CG CD CE NZ REMARK 470 LYS H 62 CG CD CE NZ REMARK 470 LYS H 137 CG CD CE NZ REMARK 470 ASN H 155 CG OD1 ND2 REMARK 470 MET H 157 CG SD CE REMARK 470 LYS H 227 CG CD CE NZ REMARK 470 LYS H 230 CG CD CE NZ REMARK 470 LYS H 231 CG CD CE NZ REMARK 470 ARG H 235 CG CD NE CZ NH1 NH2 REMARK 470 ARG L 43 CG CD NE CZ NH1 NH2 REMARK 470 LYS L 61 CG CD CE NZ REMARK 470 LYS L 166 CG CD CE NZ REMARK 470 LYS L 168 CG CD CE NZ REMARK 470 ILE L 169 CG1 CG2 CD1 REMARK 470 LYS L 188 CG CD CE NZ REMARK 470 LEU L 198 CG CD1 CD2 REMARK 470 LEU L 200 CG CD1 CD2 REMARK 470 LYS L 202 CG CD CE NZ REMARK 470 ASP L 203 CG OD1 OD2 REMARK 470 GLU L 204 CG CD OE1 OE2 REMARK 470 SER L 227 OG REMARK 470 PHE L 228 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS C 115 CG CD CE NZ REMARK 470 LYS C 129 CG CD CE NZ REMARK 470 LYS C 131 CG CD CE NZ REMARK 470 LYS C 134 CG CD CE NZ REMARK 470 PHE C 136 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG C 156 CG CD NE CZ NH1 NH2 REMARK 470 GLU C 157 CG CD OE1 OE2 REMARK 470 ARG C 171 CG CD NE CZ NH1 NH2 REMARK 470 ASN C 187 CG OD1 ND2 REMARK 470 VAL C 189 CG1 CG2 REMARK 470 GLU C 283 CG CD OE1 OE2 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 TYR H 120 -76.32 -142.32 REMARK 500 PRO H 169 96.05 -61.08 REMARK 500 PRO H 171 -167.95 -106.76 REMARK 500 SER H 182 -30.74 -131.66 REMARK 500 SER L 49 -126.99 56.41 REMARK 500 TYR L 71 11.63 -145.38 REMARK 500 ALA C 144 -57.15 -134.46 REMARK 500 ASP C 145 -88.25 -97.59 REMARK 500 ARG C 171 -66.28 -102.08 REMARK 500 THR C 313 -166.75 -105.52 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA C 405 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU C 112 OE1 REMARK 620 2 GLU C 170 OE1 114.5 REMARK 620 3 GLU C 170 OE2 92.3 49.8 REMARK 620 4 ASP C 201 OD1 94.7 71.5 117.7 REMARK 620 5 GLN C 202 O 80.7 158.6 149.0 93.1 REMARK 620 6 ASP C 204 OD1 94.6 115.8 74.7 164.1 75.8 REMARK 620 7 ASP C 237 OD1 169.5 75.3 91.6 92.1 91.0 77.1 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA C 404 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU C 112 OE2 REMARK 620 2 ASP C 168 OD1 82.6 REMARK 620 3 GLU C 170 OE2 87.7 97.1 REMARK 620 4 ASP C 204 OD2 87.0 157.1 102.8 REMARK 620 5 HOH C 501 O 73.8 83.2 161.4 74.3 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA C 401 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASN C 205 O REMARK 620 2 ASP C 235 OD1 97.7 REMARK 620 3 ASP C 235 OD2 88.4 55.6 REMARK 620 4 ASP C 237 OD2 84.8 80.8 134.5 REMARK 620 5 ASN C 244 O 168.3 85.8 84.3 106.8 REMARK 620 6 ASP C 296 OD2 88.3 132.6 77.9 146.5 81.2 REMARK 620 N 1 2 3 4 5 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 L 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 L 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 401 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 402 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 403 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 404 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 405 DBREF 6VEL H -2 243 PDB 6VEL 6VEL -2 243 DBREF 6VEL L 1 233 PDB 6VEL 6VEL 1 233 DBREF 6VEL C 4 101 UNP Q12306 SMT3_YEAST 1 98 DBREF 6VEL C 102 318 UNP P12830 CADH1_HUMAN 155 371 SEQADV 6VEL MET C -12 UNP Q12306 EXPRESSION TAG SEQADV 6VEL ALA C -11 UNP Q12306 EXPRESSION TAG SEQADV 6VEL SER C -10 UNP Q12306 EXPRESSION TAG SEQADV 6VEL MET C -9 UNP Q12306 EXPRESSION TAG SEQADV 6VEL HIS C -8 UNP Q12306 EXPRESSION TAG SEQADV 6VEL HIS C -7 UNP Q12306 EXPRESSION TAG SEQADV 6VEL HIS C -6 UNP Q12306 EXPRESSION TAG SEQADV 6VEL HIS C -5 UNP Q12306 EXPRESSION TAG SEQADV 6VEL HIS C -4 UNP Q12306 EXPRESSION TAG SEQADV 6VEL HIS C -3 UNP Q12306 EXPRESSION TAG SEQADV 6VEL GLY C -2 UNP Q12306 EXPRESSION TAG SEQADV 6VEL SER C -1 UNP Q12306 EXPRESSION TAG SEQADV 6VEL SER C 0 UNP Q12306 EXPRESSION TAG SEQADV 6VEL MET C 1 UNP Q12306 EXPRESSION TAG SEQADV 6VEL ALA C 2 UNP Q12306 EXPRESSION TAG SEQADV 6VEL SER C 3 UNP Q12306 EXPRESSION TAG SEQRES 1 H 246 HIS HIS HIS MET GLY TRP SER CYS ILE ILE LEU PHE LEU SEQRES 2 H 246 VAL ALA THR ALA THR GLY VAL HIS SER GLU VAL GLN LEU SEQRES 3 H 246 GLN GLN SER GLY PRO GLU LEU VAL LYS PRO GLY ALA SER SEQRES 4 H 246 VAL LYS ILE SER CYS LYS ALA SER GLY TYR SER PHE THR SEQRES 5 H 246 GLY TYR PHE MET ASN TRP VAL LYS GLN SER HIS GLY LYS SEQRES 6 H 246 SER LEU GLU TRP ILE GLY ARG ILE ASN PRO TYR ASN GLY SEQRES 7 H 246 ASP THR PHE TYR LYS GLN ARG PHE LYS GLY LYS ALA THR SEQRES 8 H 246 LEU THR VAL ASP LYS SER SER SER THR VAL HIS MET ASP SEQRES 9 H 246 LEU LEU SER LEU THR SER GLU ASP SER ALA VAL TYR TYR SEQRES 10 H 246 CYS GLY ARG GLY ASN TYR TYR PHE ASP TYR TRP GLY GLN SEQRES 11 H 246 GLY THR THR LEU THR VAL SER SER ALA LYS THR THR PRO SEQRES 12 H 246 PRO SER VAL TYR PRO LEU ALA PRO GLY SER ALA ALA GLN SEQRES 13 H 246 THR ASN SER MET VAL THR LEU GLY CYS LEU VAL LYS GLY SEQRES 14 H 246 TYR PHE PRO GLU PRO VAL THR VAL THR TRP ASN SER GLY SEQRES 15 H 246 SER LEU SER SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 16 H 246 GLN SER ASP LEU TYR THR LEU SER SER SER VAL THR VAL SEQRES 17 H 246 PRO SER SER PRO ARG PRO SER GLU THR VAL THR CYS ASN SEQRES 18 H 246 VAL ALA HIS PRO ALA SER SER THR LYS VAL ASP LYS LYS SEQRES 19 H 246 ILE VAL PRO ARG ASP CYS HIS HIS HIS HIS HIS HIS SEQRES 1 L 233 MET GLY TRP SER CYS ILE ILE LEU PHE LEU VAL ALA THR SEQRES 2 L 233 ALA THR GLY VAL HIS SER ASP VAL GLN ILE THR GLN SER SEQRES 3 L 233 PRO SER TYR LEU ALA ALA SER PRO GLY GLU THR ILE THR SEQRES 4 L 233 ILE ASN CYS ARG THR SER LYS ASN ILE SER LYS TYR LEU SEQRES 5 L 233 ALA TRP TYR GLN GLU LYS PRO GLY LYS THR ASN LYS LEU SEQRES 6 L 233 LEU ILE TYR SER GLY TYR THR LEU GLN SER GLY ILE PRO SEQRES 7 L 233 SER ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR SEQRES 8 L 233 LEU THR ILE SER SER LEU GLU PRO GLU ASP PHE ALA MET SEQRES 9 L 233 TYR TYR CYS GLN GLN HIS ASN GLU TYR PRO TYR THR PHE SEQRES 10 L 233 GLY GLY GLY THR LYS LEU GLU ILE LYS ARG ALA ASP ALA SEQRES 11 L 233 ALA PRO THR VAL SER ILE PHE PRO PRO SER SER GLU GLN SEQRES 12 L 233 LEU THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN SEQRES 13 L 233 ASN PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE SEQRES 14 L 233 ASP GLY SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP SEQRES 15 L 233 THR ASP GLN ASP SER LYS ASP SER THR TYR SER MET SER SEQRES 16 L 233 SER THR LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS SEQRES 17 L 233 ASN SER TYR THR CYS GLU ALA THR HIS LYS THR SER THR SEQRES 18 L 233 SER PRO ILE VAL LYS SER PHE ASN ARG ASN GLU CYS SEQRES 1 C 331 MET ALA SER MET HIS HIS HIS HIS HIS HIS GLY SER SER SEQRES 2 C 331 MET ALA SER MET SER ASP SER GLU VAL ASN GLN GLU ALA SEQRES 3 C 331 LYS PRO GLU VAL LYS PRO GLU VAL LYS PRO GLU THR HIS SEQRES 4 C 331 ILE ASN LEU LYS VAL SER ASP GLY SER SER GLU ILE PHE SEQRES 5 C 331 PHE LYS ILE LYS LYS THR THR PRO LEU ARG ARG LEU MET SEQRES 6 C 331 GLU ALA PHE ALA LYS ARG GLN GLY LYS GLU MET ASP SER SEQRES 7 C 331 LEU ARG PHE LEU TYR ASP GLY ILE ARG ILE GLN ALA ASP SEQRES 8 C 331 GLN THR PRO GLU ASP LEU ASP MET GLU ASP ASN ASP ILE SEQRES 9 C 331 ILE GLU ALA HIS ARG GLU GLN ILE GLY GLY ASP TRP VAL SEQRES 10 C 331 ILE PRO PRO ILE SER CYS PRO GLU ASN GLU LYS GLY PRO SEQRES 11 C 331 PHE PRO LYS ASN LEU VAL GLN ILE LYS SER ASN LYS ASP SEQRES 12 C 331 LYS GLU GLY LYS VAL PHE TYR SER ILE THR GLY GLN GLY SEQRES 13 C 331 ALA ASP THR PRO PRO VAL GLY VAL PHE ILE ILE GLU ARG SEQRES 14 C 331 GLU THR GLY TRP LEU LYS VAL THR GLU PRO LEU ASP ARG SEQRES 15 C 331 GLU ARG ILE ALA THR TYR THR LEU PHE SER HIS ALA VAL SEQRES 16 C 331 SER SER ASN GLY ASN ALA VAL GLU ASP PRO MET GLU ILE SEQRES 17 C 331 LEU ILE THR VAL THR ASP GLN ASN ASP ASN LYS PRO GLU SEQRES 18 C 331 PHE THR GLN GLU VAL PHE LYS GLY SER VAL MET GLU GLY SEQRES 19 C 331 ALA LEU PRO GLY THR SER VAL MET GLU VAL THR ALA THR SEQRES 20 C 331 ASP ALA ASP ASP ASP VAL ASN THR TYR ASN ALA ALA ILE SEQRES 21 C 331 ALA TYR THR ILE LEU SER GLN ASP PRO GLU LEU PRO ASP SEQRES 22 C 331 LYS ASN MET PHE THR ILE ASN ARG ASN THR GLY VAL ILE SEQRES 23 C 331 SER VAL VAL THR THR GLY LEU ASP ARG GLU SER PHE PRO SEQRES 24 C 331 THR TYR THR LEU VAL VAL GLN ALA ALA ASP LEU GLN GLY SEQRES 25 C 331 GLU GLY LEU SER THR THR ALA THR ALA VAL ILE THR VAL SEQRES 26 C 331 THR ASP THR ASN ASP ASN HET SO4 H 301 5 HET SO4 H 302 5 HET SO4 L 301 5 HET SO4 L 302 5 HET CA C 401 1 HET SO4 C 402 5 HET SO4 C 403 5 HET CA C 404 1 HET NA C 405 1 HETNAM SO4 SULFATE ION HETNAM CA CALCIUM ION HETNAM NA SODIUM ION FORMUL 4 SO4 6(O4 S 2-) FORMUL 8 CA 2(CA 2+) FORMUL 12 NA NA 1+ FORMUL 13 HOH *128(H2 O) HELIX 1 AA1 SER H 47 TYR H 51 5 5 HELIX 2 AA2 GLN H 81 LYS H 84 5 4 HELIX 3 AA3 LYS H 93 SER H 95 5 3 HELIX 4 AA4 THR H 106 SER H 110 5 5 HELIX 5 AA5 SER H 178 SER H 180 5 3 HELIX 6 AA6 PRO H 222 SER H 225 5 4 HELIX 7 AA7 GLU L 98 PHE L 102 5 5 HELIX 8 AA8 SER L 140 GLY L 147 1 8 HELIX 9 AA9 LYS L 202 GLU L 206 1 5 HELIX 10 AB1 SER C 127 LYS C 131 5 5 HELIX 11 AB2 LEU C 297 GLU C 300 5 4 SHEET 1 AA1 4 GLN H 22 GLN H 25 0 SHEET 2 AA1 4 VAL H 37 SER H 44 -1 O LYS H 42 N GLN H 24 SHEET 3 AA1 4 THR H 97 LEU H 102 -1 O LEU H 102 N VAL H 37 SHEET 4 AA1 4 ALA H 87 ASP H 92 -1 N THR H 88 O ASP H 101 SHEET 1 AA2 6 GLU H 29 VAL H 31 0 SHEET 2 AA2 6 THR H 129 VAL H 133 1 O THR H 130 N GLU H 29 SHEET 3 AA2 6 ALA H 111 ARG H 117 -1 N ALA H 111 O LEU H 131 SHEET 4 AA2 6 MET H 53 GLN H 58 -1 N VAL H 56 O TYR H 114 SHEET 5 AA2 6 LEU H 64 ILE H 70 -1 O GLU H 65 N LYS H 57 SHEET 6 AA2 6 THR H 77 TYR H 79 -1 O PHE H 78 N ARG H 69 SHEET 1 AA3 4 GLU H 29 VAL H 31 0 SHEET 2 AA3 4 THR H 129 VAL H 133 1 O THR H 130 N GLU H 29 SHEET 3 AA3 4 ALA H 111 ARG H 117 -1 N ALA H 111 O LEU H 131 SHEET 4 AA3 4 TYR H 124 TRP H 125 -1 O TYR H 124 N ARG H 117 SHEET 1 AA4 4 SER H 142 LEU H 146 0 SHEET 2 AA4 4 VAL H 158 TYR H 167 -1 O LYS H 165 N SER H 142 SHEET 3 AA4 4 TYR H 197 VAL H 205 -1 O LEU H 199 N VAL H 164 SHEET 4 AA4 4 VAL H 185 THR H 187 -1 N HIS H 186 O SER H 202 SHEET 1 AA5 4 SER H 142 LEU H 146 0 SHEET 2 AA5 4 VAL H 158 TYR H 167 -1 O LYS H 165 N SER H 142 SHEET 3 AA5 4 TYR H 197 VAL H 205 -1 O LEU H 199 N VAL H 164 SHEET 4 AA5 4 VAL H 191 LEU H 192 -1 N VAL H 191 O THR H 198 SHEET 1 AA6 3 THR H 173 TRP H 176 0 SHEET 2 AA6 3 VAL H 215 HIS H 221 -1 O ASN H 218 N THR H 175 SHEET 3 AA6 3 THR H 226 ILE H 232 -1 O ILE H 232 N VAL H 215 SHEET 1 AA7 4 ILE L 23 SER L 26 0 SHEET 2 AA7 4 ILE L 38 THR L 44 -1 O ARG L 43 N THR L 24 SHEET 3 AA7 4 ASP L 89 ILE L 94 -1 O LEU L 92 N ILE L 40 SHEET 4 AA7 4 PHE L 81 GLY L 85 -1 N SER L 82 O THR L 93 SHEET 1 AA8 6 TYR L 29 ALA L 32 0 SHEET 2 AA8 6 THR L 121 ILE L 125 1 O GLU L 124 N LEU L 30 SHEET 3 AA8 6 MET L 104 GLN L 109 -1 N TYR L 105 O THR L 121 SHEET 4 AA8 6 LEU L 52 GLU L 57 -1 N TYR L 55 O TYR L 106 SHEET 5 AA8 6 LYS L 64 TYR L 68 -1 O LEU L 66 N TRP L 54 SHEET 6 AA8 6 THR L 72 LEU L 73 -1 O THR L 72 N TYR L 68 SHEET 1 AA9 4 TYR L 29 ALA L 32 0 SHEET 2 AA9 4 THR L 121 ILE L 125 1 O GLU L 124 N LEU L 30 SHEET 3 AA9 4 MET L 104 GLN L 109 -1 N TYR L 105 O THR L 121 SHEET 4 AA9 4 THR L 116 PHE L 117 -1 O THR L 116 N GLN L 109 SHEET 1 AB1 4 THR L 133 PHE L 137 0 SHEET 2 AB1 4 GLY L 148 PHE L 158 -1 O ASN L 156 N THR L 133 SHEET 3 AB1 4 TYR L 192 THR L 201 -1 O LEU L 200 N ALA L 149 SHEET 4 AB1 4 VAL L 178 TRP L 182 -1 N SER L 181 O SER L 195 SHEET 1 AB2 4 SER L 172 GLU L 173 0 SHEET 2 AB2 4 ASN L 164 ILE L 169 -1 N ILE L 169 O SER L 172 SHEET 3 AB2 4 TYR L 211 THR L 216 -1 O THR L 212 N LYS L 168 SHEET 4 AB2 4 ILE L 224 PHE L 228 -1 O ILE L 224 N ALA L 215 SHEET 1 AB3 4 ILE C 108 PRO C 111 0 SHEET 2 AB3 4 MET C 193 THR C 200 1 O THR C 198 N ILE C 108 SHEET 3 AB3 4 THR C 174 HIS C 180 -1 N LEU C 177 O ILE C 195 SHEET 4 AB3 4 SER C 138 GLY C 141 -1 N SER C 138 O HIS C 180 SHEET 1 AB4 3 LYS C 120 GLN C 124 0 SHEET 2 AB4 3 TRP C 160 VAL C 163 -1 O LEU C 161 N VAL C 123 SHEET 3 AB4 3 PHE C 152 ILE C 154 -1 N ILE C 153 O LYS C 162 SHEET 1 AB5 2 GLU C 208 PHE C 209 0 SHEET 2 AB5 2 ALA C 233 THR C 234 -1 O THR C 234 N GLU C 208 SHEET 1 AB6 4 VAL C 213 MET C 219 0 SHEET 2 AB6 4 SER C 303 THR C 313 1 O THR C 307 N PHE C 214 SHEET 3 AB6 4 THR C 287 ALA C 295 -1 N LEU C 290 O ALA C 308 SHEET 4 AB6 4 ALA C 248 ASP C 255 -1 N LEU C 252 O VAL C 291 SHEET 1 AB7 3 SER C 227 GLU C 230 0 SHEET 2 AB7 3 VAL C 272 VAL C 275 -1 O ILE C 273 N VAL C 228 SHEET 3 AB7 3 PHE C 264 ILE C 266 -1 N THR C 265 O SER C 274 SSBOND 1 CYS H 41 CYS H 115 1555 1555 2.05 SSBOND 2 CYS H 162 CYS H 217 1555 1555 2.04 SSBOND 3 CYS L 42 CYS L 107 1555 1555 2.04 SSBOND 4 CYS L 153 CYS L 213 1555 1555 2.04 LINK OE1 GLU C 112 NA NA C 405 1555 1555 2.37 LINK OE2 GLU C 112 CA CA C 404 1555 1555 2.60 LINK OD1 ASP C 168 CA CA C 404 1555 1555 2.39 LINK OE1 GLU C 170 NA NA C 405 1555 1555 2.61 LINK OE2 GLU C 170 NA NA C 405 1555 1555 2.58 LINK OE2 GLU C 170 CA CA C 404 1555 1555 2.25 LINK OD1 ASP C 201 NA NA C 405 1555 1555 2.44 LINK O GLN C 202 NA NA C 405 1555 1555 2.39 LINK OD1 ASP C 204 NA NA C 405 1555 1555 2.44 LINK OD2 ASP C 204 CA CA C 404 1555 1555 2.40 LINK O ASN C 205 CA CA C 401 1555 1555 2.34 LINK OD1 ASP C 235 CA CA C 401 1555 1555 2.44 LINK OD2 ASP C 235 CA CA C 401 1555 1555 2.27 LINK OD1 ASP C 237 NA NA C 405 1555 1555 2.22 LINK OD2 ASP C 237 CA CA C 401 1555 1555 2.56 LINK O ASN C 244 CA CA C 401 1555 1555 2.36 LINK OD2 ASP C 296 CA CA C 401 1555 1555 2.46 LINK CA CA C 404 O HOH C 501 1555 1555 2.37 CISPEP 1 GLU H 170 PRO H 171 0 0.08 CISPEP 2 SER L 26 PRO L 27 0 -3.16 CISPEP 3 TYR L 113 PRO L 114 0 -10.74 CISPEP 4 TYR L 159 PRO L 160 0 2.71 CISPEP 5 GLY C 116 PRO C 117 0 -2.95 CISPEP 6 PHE C 118 PRO C 119 0 6.03 CISPEP 7 PRO C 147 PRO C 148 0 -1.32 CISPEP 8 ASP C 255 PRO C 256 0 0.24 CISPEP 9 LEU C 258 PRO C 259 0 2.52 SITE 1 AC1 5 SO4 C 403 GLY H 118 ASN H 119 TYR H 120 SITE 2 AC1 5 TYR H 121 SITE 1 AC2 7 LYS C 206 SER C 303 THR C 304 TYR H 120 SITE 2 AC2 7 TYR H 121 TYR L 51 HIS L 110 SITE 1 AC3 6 GLY C 301 GLU L 112 TYR L 113 HOH L 402 SITE 2 AC3 6 HOH L 405 HOH L 434 SITE 1 AC4 5 GLN L 56 LYS L 64 PHE L 81 GLU L 100 SITE 2 AC4 5 ASP L 101 SITE 1 AC5 6 ASN C 203 ASN C 205 ASP C 235 ASP C 237 SITE 2 AC5 6 ASN C 244 ASP C 296 SITE 1 AC6 4 VAL C 104 ILE C 105 MET C 193 HOH C 511 SITE 1 AC7 3 THR C 305 GLY H 50 SO4 H 301 SITE 1 AC8 5 GLU C 112 ASP C 168 GLU C 170 ASP C 204 SITE 2 AC8 5 HOH C 501 SITE 1 AC9 6 GLU C 112 GLU C 170 ASP C 201 GLN C 202 SITE 2 AC9 6 ASP C 204 ASP C 237 CRYST1 142.170 142.170 90.320 90.00 90.00 120.00 P 31 2 1 6 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 0.007034 0.004061 0.000000 0.00000 SCALE2 0.000000 0.008122 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011072 0.00000