HEADER IMMUNE SYSTEM 09-AUG-24 9GFF TITLE BCR FAB FROM THE SUBSET 1 CHRONIC LYMPHOCYTIC LEUKAEMIA CASE P10015 COMPND MOL_ID: 1; COMPND 2 MOLECULE: BCR P10015 HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: BCR P10015 LIGHT CHAIN; COMPND 7 CHAIN: L; 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 B-CELL RECEPTOR, FAB, CHRONICL LYMPHOCYTIC LEUKAEMIA, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR C.MINICI,M.DEGANO REVDAT 1 20-AUG-25 9GFF 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. 2.80 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) : 2.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 86.56 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 17228 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.210 REMARK 3 R VALUE (WORKING SET) : 0.209 REMARK 3 FREE R VALUE : 0.235 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.620 REMARK 3 FREE R VALUE TEST SET COUNT : 796 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 86.5600 - 5.0900 1.00 2798 114 0.1749 0.2418 REMARK 3 2 5.0900 - 4.0400 1.00 2732 153 0.1676 0.1773 REMARK 3 3 4.0400 - 3.5300 1.00 2722 135 0.2338 0.2532 REMARK 3 4 3.5300 - 3.2000 1.00 2726 141 0.2628 0.2690 REMARK 3 5 3.2000 - 2.9700 1.00 2722 134 0.3004 0.2762 REMARK 3 6 2.9700 - 2.8000 1.00 2732 119 0.3517 0.3697 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) : 0.321 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.555 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 90.83 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 3489 REMARK 3 ANGLE : 0.695 4747 REMARK 3 CHIRALITY : 0.047 536 REMARK 3 PLANARITY : 0.004 606 REMARK 3 DIHEDRAL : 13.336 1265 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 4 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 118 ) REMARK 3 ORIGIN FOR THE GROUP (A): -22.2691 -34.4678 -12.3975 REMARK 3 T TENSOR REMARK 3 T11: 0.4174 T22: 0.8246 REMARK 3 T33: 0.4585 T12: -0.0057 REMARK 3 T13: 0.0499 T23: 0.0484 REMARK 3 L TENSOR REMARK 3 L11: 2.4627 L22: 5.5048 REMARK 3 L33: 5.7028 L12: 0.2652 REMARK 3 L13: -0.0737 L23: 2.0501 REMARK 3 S TENSOR REMARK 3 S11: 0.0256 S12: 0.2803 S13: 0.0320 REMARK 3 S21: -0.1897 S22: -0.0825 S23: -0.2750 REMARK 3 S31: -0.1474 S32: 0.9015 S33: -0.0172 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 119 THROUGH 224) REMARK 3 ORIGIN FOR THE GROUP (A): -17.2079 -31.6491 20.5970 REMARK 3 T TENSOR REMARK 3 T11: 0.6603 T22: 1.1489 REMARK 3 T33: 0.7566 T12: -0.1207 REMARK 3 T13: -0.1264 T23: 0.0708 REMARK 3 L TENSOR REMARK 3 L11: 2.1063 L22: 3.1758 REMARK 3 L33: 4.4607 L12: -0.1968 REMARK 3 L13: -0.5401 L23: -1.7758 REMARK 3 S TENSOR REMARK 3 S11: -0.0514 S12: -0.0283 S13: -0.1508 REMARK 3 S21: 0.2847 S22: -0.2638 S23: -0.4556 REMARK 3 S31: -0.4240 S32: 1.0790 S33: 0.3033 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 109 ) REMARK 3 ORIGIN FOR THE GROUP (A): -41.4603 -41.0461 -4.0856 REMARK 3 T TENSOR REMARK 3 T11: 0.4944 T22: 0.4651 REMARK 3 T33: 0.5468 T12: -0.0073 REMARK 3 T13: 0.0773 T23: -0.0022 REMARK 3 L TENSOR REMARK 3 L11: 2.8321 L22: 3.3772 REMARK 3 L33: 6.9224 L12: 0.0909 REMARK 3 L13: 0.0028 L23: 0.6890 REMARK 3 S TENSOR REMARK 3 S11: 0.0129 S12: -0.1264 S13: -0.0893 REMARK 3 S21: 0.2361 S22: -0.2439 S23: 0.2496 REMARK 3 S31: 0.3378 S32: 0.1231 S33: 0.2410 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 110 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): -28.7046 -21.2673 25.7790 REMARK 3 T TENSOR REMARK 3 T11: 0.8332 T22: 0.8593 REMARK 3 T33: 0.5872 T12: -0.0650 REMARK 3 T13: -0.2278 T23: 0.1045 REMARK 3 L TENSOR REMARK 3 L11: 4.7845 L22: 2.6006 REMARK 3 L33: 2.4297 L12: 1.0516 REMARK 3 L13: -1.2023 L23: 0.8444 REMARK 3 S TENSOR REMARK 3 S11: -0.1422 S12: -0.5860 S13: 0.4636 REMARK 3 S21: 0.1727 S22: 0.0006 S23: -0.3889 REMARK 3 S31: -0.7372 S32: 0.4791 S33: 0.2012 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 9GFF 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_1292140885. 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 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 : 23294 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.510 REMARK 200 RESOLUTION RANGE LOW (A) : 86.570 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 12.40 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 14.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.51 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9 REMARK 200 DATA REDUNDANCY IN SHELL : 11.70 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.200 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 66.71 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.69 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SUCCINATE PH 7 AND 1.5 REMARK 280 M AMMONIUM SULFATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE REMARK 280 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z REMARK 290 3555 -X+Y,-X,Z REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+1/2 REMARK 290 6555 X-Y,X,Z+1/2 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 0.00000 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 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 61.52400 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 61.52400 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 61.52400 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 VAL H 225 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 SG CYS H 134 HG CYS L 215 0.99 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 OH TYR H 33 OG SER H 195 4444 2.14 REMARK 500 O MET L 4 NH2 ARG L 24 2455 2.14 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 SER H 7 -179.02 -63.41 REMARK 500 SER H 77 44.58 37.48 REMARK 500 TRP H 101 160.42 63.35 REMARK 500 VAL H 103 -75.14 -95.17 REMARK 500 SER H 137 65.79 -155.52 REMARK 500 ASN H 167 -33.85 84.35 REMARK 500 SER H 171 36.26 -89.67 REMARK 500 SER L 30 -126.56 50.02 REMARK 500 ALA L 51 -43.92 80.48 REMARK 500 ALA L 84 174.87 178.43 REMARK 500 ASN L 139 74.76 44.90 REMARK 500 SER L 163 115.10 -160.78 REMARK 500 REMARK 500 REMARK: NULL DBREF 9GFF H 1 225 PDB 9GFF 9GFF 1 225 DBREF 9GFF L 1 215 PDB 9GFF 9GFF 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 GLY TYR TYR MET HIS TRP VAL ARG GLN SEQRES 4 H 225 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 H 225 PRO ASN SER GLY GLY THR ASN TYR ALA GLN LYS PHE GLN SEQRES 6 H 225 GLY ARG VAL THR MET THR ARG ASP THR SER ILE SER THR SEQRES 7 H 225 ALA TYR MET GLU LEU SER ARG LEU ARG SER ASP ASP THR SEQRES 8 H 225 ALA VAL TYR TYR CYS ALA ARG ALA GLN TRP LEU VAL VAL SEQRES 9 H 225 THR ASN 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 MET 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 TRP 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 HET NAG A 1 14 HET NAG A 2 14 HET FUC A 3 10 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE 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 FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L- HETSYN 2 FUC FUCOSE; FUCOSE FORMUL 3 NAG 2(C8 H15 N O6) FORMUL 3 FUC C6 H12 O5 FORMUL 4 HOH *20(H2 O) HELIX 1 AA1 THR H 28 TYR H 32 5 5 HELIX 2 AA2 GLN H 62 GLN H 65 5 4 HELIX 3 AA3 ARG H 87 THR H 91 5 5 HELIX 4 AA4 PRO H 194 GLN H 200 1 7 HELIX 5 AA5 GLN L 79 PHE L 83 5 5 HELIX 6 AA6 SER L 122 SER L 128 1 7 HELIX 7 AA7 LYS L 184 GLU L 188 1 5 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 THR H 71 O TYR H 80 SHEET 1 AA2 6 GLU H 10 LYS H 12 0 SHEET 2 AA2 6 LEU H 115 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 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AA2 6 LEU H 45 ILE H 51 -1 O MET H 48 N TRP H 36 SHEET 6 AA2 6 THR H 58 TYR H 60 -1 O ASN H 59 N TRP H 50 SHEET 1 AA3 4 GLU H 10 LYS H 12 0 SHEET 2 AA3 4 LEU H 115 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 ASN H 106 TRP H 110 -1 O TYR H 109 N ARG H 98 SHEET 1 AA4 4 THR H 127 VAL H 132 0 SHEET 2 AA4 4 VAL H 144 PHE H 153 -1 O LEU H 149 N PHE H 129 SHEET 3 AA4 4 LYS H 184 LEU H 193 -1 O LEU H 193 N VAL H 144 SHEET 4 AA4 4 ARG H 174 GLY H 175 -1 N ARG H 174 O GLN H 190 SHEET 1 AA5 4 THR H 127 VAL H 132 0 SHEET 2 AA5 4 VAL H 144 PHE H 153 -1 O LEU H 149 N PHE H 129 SHEET 3 AA5 4 LYS H 184 LEU H 193 -1 O LEU H 193 N VAL H 144 SHEET 4 AA5 4 VAL H 179 ARG H 181 -1 N ARG H 181 O LYS H 184 SHEET 1 AA6 3 THR H 159 LYS H 163 0 SHEET 2 AA6 3 HIS H 205 GLN H 211 -1 O LYS H 209 N SER H 161 SHEET 3 AA6 3 LYS H 217 PRO H 222 -1 O VAL H 221 N VAL H 206 SHEET 1 AA7 4 MET L 4 SER L 7 0 SHEET 2 AA7 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA7 4 ASP L 70 ILE L 75 -1 O PHE L 71 N CYS L 23 SHEET 4 AA7 4 PHE L 62 SER L 67 -1 N SER L 65 O THR L 72 SHEET 1 AA8 6 SER L 10 SER L 14 0 SHEET 2 AA8 6 THR L 103 LYS L 108 1 O GLU L 106 N LEU L 11 SHEET 3 AA8 6 ALA L 84 GLN L 90 -1 N ALA L 84 O LEU L 105 SHEET 4 AA8 6 LEU L 33 GLN L 38 -1 N TYR L 36 O TYR L 87 SHEET 5 AA8 6 LYS L 45 TYR L 49 -1 O ILE L 48 N TRP L 35 SHEET 6 AA8 6 SER L 53 LEU L 54 -1 O SER L 53 N TYR L 49 SHEET 1 AA9 4 SER L 10 SER L 14 0 SHEET 2 AA9 4 THR L 103 LYS L 108 1 O GLU L 106 N LEU L 11 SHEET 3 AA9 4 ALA L 84 GLN L 90 -1 N ALA L 84 O LEU L 105 SHEET 4 AA9 4 THR L 98 PHE L 99 -1 O THR L 98 N GLN L 90 SHEET 1 AB1 4 SER L 115 PHE L 119 0 SHEET 2 AB1 4 THR L 130 PHE L 140 -1 O LEU L 136 N PHE L 117 SHEET 3 AB1 4 TYR L 174 SER L 183 -1 O TYR L 174 N PHE L 140 SHEET 4 AB1 4 SER L 160 GLN L 161 -1 N GLN L 161 O THR L 179 SHEET 1 AB2 3 LYS L 146 VAL L 151 0 SHEET 2 AB2 3 VAL L 192 THR L 198 -1 O ALA L 194 N LYS L 150 SHEET 3 AB2 3 VAL L 206 ASN L 211 -1 O VAL L 206 N VAL L 197 SSBOND 1 CYS H 22 CYS H 96 1555 1555 2.03 SSBOND 2 CYS H 134 CYS L 215 1555 1555 2.04 SSBOND 3 CYS H 148 CYS H 208 1555 1555 2.03 SSBOND 4 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 5 CYS L 135 CYS L 195 1555 1555 2.05 LINK ND2 ASN H 166 C1 NAG A 1 1555 1555 1.44 LINK O4 NAG A 1 C1 NAG A 2 1555 1555 1.44 LINK O6 NAG A 1 C1 FUC A 3 1555 1555 1.43 CISPEP 1 LEU H 154 PRO H 155 0 2.29 CISPEP 2 SER L 7 PRO L 8 0 0.90 CISPEP 3 THR L 94 PRO L 95 0 -8.06 CISPEP 4 PRO L 95 PRO L 96 0 -3.34 CISPEP 5 TYR L 141 PRO L 142 0 2.22 CRYST1 99.952 99.952 123.048 90.00 90.00 120.00 P 63 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 0.010005 0.005776 0.000000 0.00000 SCALE2 0.000000 0.011553 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008127 0.00000