HEADER IMMUNE SYSTEM 06-FEB-25 9I9H TITLE STRUCTURE OF FAB-FRAGMENT GB11 IN COMPLEX WITH SIALYL LEWIS A COMPND MOL_ID: 1; COMPND 2 MOLECULE: IGG ANTIBODY FAB FRAGMENT; COMPND 3 CHAIN: A, H, C, E; COMPND 4 OTHER_DETAILS: HEAVY CHAIN; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: IGG ANTIBODY FAB FRAGMENT; COMPND 7 CHAIN: B, L, D, F; COMPND 8 OTHER_DETAILS: LIGHT CHAIN SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 ORGAN: SPLEEN; SOURCE 5 MOL_ID: 2; SOURCE 6 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 7 ORGANISM_TAXID: 10090; SOURCE 8 TISSUE: SPLEEN KEYWDS FAB FRAGMENT, CARBOHYDRATE, COMPLEX, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR A.FREITAG,S.KHAN-KILJI,R.NEDIELKOV,S.MURALI KUMAR,M.KRUMMHAAR, AUTHOR 2 J.LUEHLE,F.GOERDELER,J.ARNDT,C.KAMPHUES,M.A.MROGINSKI,C.ROTH, AUTHOR 3 P.H.SEEBERGER,H.M.MOELLER,O.MOSCOVITZ REVDAT 1 18-FEB-26 9I9H 0 JRNL AUTH A.FREITAG,S.KHAN-KILJI,R.NEDIELKOV,S.MURALI KUMAR, JRNL AUTH 2 M.KRUMMHAAR,J.LUEHLE,F.GOERDELER,J.ARNDT,C.KAMPHUES, JRNL AUTH 3 M.A.MROGINSKI,C.ROTH,P.H.SEEBERGER,H.M.MOELLER,O.MOSCOVITZ JRNL TITL AN INTEGRATIVE APPROACH TO DEVELOP AND CHARACTERISE JRNL TITL 2 ANTIBODIES AGAINST THE CANCER ASSOCIATED ANTIGEN SIALYL JRNL TITL 3 LEWIS A (CA 19-9) JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.96 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0419 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.96 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.70 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7 REMARK 3 NUMBER OF REFLECTIONS : 37583 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.210 REMARK 3 FREE R VALUE : 0.248 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.306 REMARK 3 FREE R VALUE TEST SET COUNT : 1994 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.96 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.04 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2657 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.35 REMARK 3 BIN R VALUE (WORKING SET) : 0.3540 REMARK 3 BIN FREE R VALUE SET COUNT : 145 REMARK 3 BIN FREE R VALUE : 0.3620 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 13216 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 259 REMARK 3 SOLVENT ATOMS : 18 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 49.14 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 61.59 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 2.25600 REMARK 3 B22 (A**2) : 0.20400 REMARK 3 B33 (A**2) : -2.44700 REMARK 3 B12 (A**2) : -1.53500 REMARK 3 B13 (A**2) : 0.41600 REMARK 3 B23 (A**2) : 0.36600 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.462 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.926 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.884 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 13817 ; 0.005 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): 12434 ; 0.002 ; 0.016 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 18784 ; 1.321 ; 1.812 REMARK 3 BOND ANGLES OTHERS (DEGREES): 28862 ; 0.741 ; 1.743 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1710 ; 7.814 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 64 ; 6.989 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2173 ;15.574 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2105 ; 0.060 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 15989 ; 0.005 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 3087 ; 0.006 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2495 ; 0.252 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 236 ; 0.271 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 6660 ; 0.179 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 341 ; 0.259 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): 2 ; 0.132 ; 0.200 REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 6861 ; 5.303 ; 6.096 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 6861 ; 5.302 ; 6.096 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8564 ; 8.594 ;10.944 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 8565 ; 8.594 ;10.945 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6956 ; 5.015 ; 6.414 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 6957 ; 5.015 ; 6.414 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 10220 ; 8.284 ;11.641 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 10221 ; 8.284 ;11.641 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 12 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 A 1 A 217 NULL REMARK 3 1 A 1 A 217 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 2 A 1 A 217 NULL REMARK 3 2 A 1 A 217 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 3 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 3 A 1 A 217 NULL REMARK 3 3 A 1 A 217 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 4 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 4 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 4 A 1 A 212 NULL REMARK 3 4 A 1 A 212 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 5 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 5 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 5 A 1 A 212 NULL REMARK 3 5 A 1 A 212 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 6 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 6 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 6 A 1 A 212 NULL REMARK 3 6 A 1 A 212 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 7 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 7 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 7 A 1 A 212 NULL REMARK 3 7 A 1 A 212 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 8 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 8 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 8 A 1 A 212 NULL REMARK 3 8 A 1 A 212 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 9 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 9 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 9 A 1 A 212 NULL REMARK 3 9 A 1 A 212 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 10 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 10 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 10 A 1 A 217 NULL REMARK 3 10 A 1 A 217 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 11 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 11 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 11 A 1 A 217 NULL REMARK 3 11 A 1 A 217 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 12 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 12 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 12 A 1 A 217 NULL REMARK 3 12 A 1 A 217 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK BULK SOLVENT REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THEIR REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 9I9H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-FEB-25. REMARK 100 THE DEPOSITION ID IS D_1292145166. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 10-DEC-21 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : BESSY REMARK 200 BEAMLINE : 14.2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9184 REMARK 200 MONOCHROMATOR : SI (111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40947 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900 REMARK 200 RESOLUTION RANGE LOW (A) : 26.980 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2 REMARK 200 DATA REDUNDANCY : 3.000 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 2.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.02 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL 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 (%): 51.10 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM MALONATE PEG 3350, VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 292K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,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 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: OCTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, L, D, F, H, C, E, T, V, REMARK 350 AND CHAINS: U, S 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 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 O3 NAG V 1 H1 GAL V 2 0.30 REMARK 500 O3 NAG U 1 H1 GAL U 2 0.43 REMARK 500 O3 NAG T 1 H1 GAL T 2 0.45 REMARK 500 O4 NAG U 1 H1 FUC U 4 0.48 REMARK 500 O4 NAG S 1 H1 FUC S 2 0.55 REMARK 500 O4 NAG T 1 H1 FUC T 3 0.56 REMARK 500 O4 NAG V 1 H1 FUC V 3 0.63 REMARK 500 O3 NAG S 1 H1 GAL H 301 0.64 REMARK 500 HO3 NAG T 1 H1 GAL T 2 0.79 REMARK 500 HO3 NAG U 1 H1 GAL U 2 0.81 REMARK 500 HO3 GAL T 2 C2 SIA B 301 0.88 REMARK 500 HG CYS H 142 SG CYS H 197 0.90 REMARK 500 HO3 GAL U 2 C2 SIA U 3 0.93 REMARK 500 HG CYS A 142 SG CYS A 197 0.94 REMARK 500 HO3 NAG V 1 H1 GAL V 2 0.95 REMARK 500 HG CYS C 142 SG CYS C 197 0.95 REMARK 500 SG CYS F 134 HG CYS F 194 1.00 REMARK 500 SG CYS D 134 HG CYS D 194 1.03 REMARK 500 HG CYS E 142 SG CYS E 197 1.03 REMARK 500 HG CYS H 22 SG CYS H 98 1.04 REMARK 500 HG CYS E 22 SG CYS E 98 1.04 REMARK 500 SG CYS H 142 HG CYS H 197 1.05 REMARK 500 HO4 NAG V 1 H1 FUC V 3 1.06 REMARK 500 SG CYS A 142 HG CYS A 197 1.07 REMARK 500 HO4 NAG U 1 H1 FUC U 4 1.08 REMARK 500 SG CYS C 142 HG CYS C 197 1.11 REMARK 500 HO4 NAG S 1 H1 FUC S 2 1.12 REMARK 500 C2 SIA L 301 HO3 GAL H 301 1.14 REMARK 500 SG CYS D 23 HG CYS D 88 1.15 REMARK 500 SG CYS F 23 HG CYS F 88 1.15 REMARK 500 SG CYS H 22 HG CYS H 98 1.20 REMARK 500 SG CYS E 22 HG CYS E 98 1.20 REMARK 500 SG CYS E 142 HG CYS E 197 1.20 REMARK 500 HO4 NAG T 1 H1 FUC T 3 1.22 REMARK 500 HE1 TRP C 33 HO2 GAL U 2 1.23 REMARK 500 HO3 GAL V 2 C2 SIA F 301 1.25 REMARK 500 HO3 GAL U 2 O6 SIA U 3 1.28 REMARK 500 O ASN E 53 H ALA E 55 1.47 REMARK 500 O6 SIA L 301 HO3 GAL H 301 1.53 REMARK 500 C3 NAG S 1 H1 GAL H 301 1.53 REMARK 500 C3 NAG V 1 H1 GAL V 2 1.54 REMARK 500 O3 GAL T 2 C2 SIA B 301 1.55 REMARK 500 C2 SIA L 301 O3 GAL H 301 1.58 REMARK 500 HG CYS D 134 SG CYS D 194 1.59 REMARK 500 HO3 GAL V 2 O6 SIA F 301 1.59 REMARK 500 HO3 GAL T 2 O6 SIA B 301 1.59 REMARK 500 HG CYS F 134 SG CYS F 194 1.59 REMARK 500 O3 NAG S 1 C1 GAL H 301 1.60 REMARK 500 O HIS F 189 HH12 ARG F 211 1.60 REMARK 500 O3 GAL V 2 C2 SIA F 301 1.67 REMARK 500 REMARK 500 THIS ENTRY HAS 51 CLOSE CONTACTS 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 HZ2 LYS H 210 HG1 THR E 206 1556 1.13 REMARK 500 HG1 THR H 206 HZ2 LYS E 210 1556 1.34 REMARK 500 OD2 ASP F 92 HZ2 LYS C 19 1565 1.43 REMARK 500 OD2 ASP F 92 NZ LYS C 19 1565 1.89 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 GLN A 173 CB - CA - C ANGL. DEV. = 12.3 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 MET A 18 130.26 -175.27 REMARK 500 LYS A 43 15.16 -142.44 REMARK 500 SER A 130 157.19 92.35 REMARK 500 ALA A 131 -6.84 81.11 REMARK 500 GLN A 133 -125.13 52.10 REMARK 500 SER A 162 -49.32 -137.33 REMARK 500 GLN A 173 -113.39 -115.29 REMARK 500 ASP A 216 -88.16 -40.79 REMARK 500 CYS B 23 119.28 -160.10 REMARK 500 ALA B 51 -29.22 66.00 REMARK 500 SER B 63 149.81 -173.11 REMARK 500 ASP B 110 150.27 -49.77 REMARK 500 SER B 127 23.45 -142.99 REMARK 500 ALA B 130 89.20 -150.03 REMARK 500 ASN B 138 61.84 71.21 REMARK 500 LYS B 199 -173.67 -64.89 REMARK 500 THR B 200 -41.05 74.10 REMARK 500 ALA L 51 -29.10 65.08 REMARK 500 ASN L 52 -11.29 -140.40 REMARK 500 SER L 127 23.48 -142.74 REMARK 500 ASN L 138 61.30 71.43 REMARK 500 ALA D 51 -28.30 64.23 REMARK 500 SER D 63 149.70 -172.90 REMARK 500 SER D 127 23.41 -142.61 REMARK 500 ALA D 130 89.69 -150.43 REMARK 500 ASN D 138 61.05 71.07 REMARK 500 ALA F 51 -28.21 64.67 REMARK 500 SER F 127 24.27 -142.58 REMARK 500 ALA F 130 89.24 -150.53 REMARK 500 ASN F 138 61.67 70.75 REMARK 500 THR F 202 -38.22 78.95 REMARK 500 MET H 18 131.14 -174.62 REMARK 500 LYS H 43 15.31 -143.64 REMARK 500 SER H 130 -35.38 87.02 REMARK 500 ALA H 131 40.11 -99.74 REMARK 500 SER H 162 -53.09 -140.37 REMARK 500 SER H 174 -124.03 73.26 REMARK 500 ASP H 216 -85.49 -70.66 REMARK 500 MET C 18 131.45 -174.10 REMARK 500 LYS C 43 15.18 -142.33 REMARK 500 SER C 130 -42.20 92.27 REMARK 500 ALA C 131 41.00 -100.86 REMARK 500 SER C 162 -50.18 -137.73 REMARK 500 LYS E 3 117.05 82.00 REMARK 500 GLU E 5 -62.82 -123.72 REMARK 500 GLU E 6 133.45 56.34 REMARK 500 MET E 18 129.76 -172.62 REMARK 500 PHE E 27 26.00 39.19 REMARK 500 PHE E 27 64.11 -4.75 REMARK 500 THR E 28 111.25 48.07 REMARK 500 REMARK 500 THIS ENTRY HAS 64 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG B 50 0.09 SIDE CHAIN REMARK 500 ARG L 50 0.09 SIDE CHAIN REMARK 500 ARG D 50 0.09 SIDE CHAIN REMARK 500 ARG F 96 0.09 SIDE CHAIN 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 SIA B 301 REMARK 610 SIA L 301 REMARK 610 SIA F 301 REMARK 610 GAL H 301 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 916Q RELATED DB: PDB DBREF 9I9H A 1 217 PDB 9I9H 9I9H 1 217 DBREF 9I9H B 1 212 PDB 9I9H 9I9H 1 212 DBREF 9I9H L 1 212 PDB 9I9H 9I9H 1 212 DBREF 9I9H D 1 212 PDB 9I9H 9I9H 1 212 DBREF 9I9H F 1 212 PDB 9I9H 9I9H 1 212 DBREF 9I9H H 1 217 PDB 9I9H 9I9H 1 217 DBREF 9I9H C 1 217 PDB 9I9H 9I9H 1 217 DBREF 9I9H E 1 217 PDB 9I9H 9I9H 1 217 SEQRES 1 A 217 GLU VAL LYS LEU GLU GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 A 217 PRO GLY GLY SER MET LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 A 217 PHE THR PHE SER ASP ALA TRP MET ASP TRP VAL ARG GLN SEQRES 4 A 217 SER PRO GLU LYS GLY LEU GLU TRP VAL ALA GLU ILE GLY SEQRES 5 A 217 ASN TYR ALA ILE ASN HIS ALA THR TYR TYR ALA GLU SER SEQRES 6 A 217 VAL LYS GLY ARG PHE ALA ILE SER ARG ASP ASP SER LYS SEQRES 7 A 217 SER SER VAL TYR LEU GLN MET ASN SER LEU ARG PRO GLU SEQRES 8 A 217 ASP THR GLY ILE TYR PHE CYS THR VAL ARG PHE ALA TYR SEQRES 9 A 217 TRP GLY GLN GLY THR LEU VAL THR VAL SER ALA ALA LYS SEQRES 10 A 217 THR THR PRO PRO SER VAL TYR PRO LEU ALA PRO GLY SER SEQRES 11 A 217 ALA ALA GLN THR ASN SER MET VAL THR LEU GLY CYS LEU SEQRES 12 A 217 VAL LYS GLY TYR PHE PRO GLU PRO VAL THR VAL THR TRP SEQRES 13 A 217 ASN SER GLY SER LEU SER SER GLY VAL HIS THR PHE PRO SEQRES 14 A 217 ALA VAL LEU GLN SER ASP LEU TYR THR LEU SER SER SER SEQRES 15 A 217 VAL THR VAL PRO SER SER THR TRP PRO SER GLU THR VAL SEQRES 16 A 217 THR CYS ASN VAL ALA HIS PRO ALA SER SER THR LYS VAL SEQRES 17 A 217 ASP LYS LYS ILE VAL PRO ARG ASP CYS SEQRES 1 B 212 ASP ILE LYS MET THR GLN SER PRO SER SER MET TYR ALA SEQRES 2 B 212 SER LEU GLY GLU ARG VAL THR PHE THR CYS ARG ALA SER SEQRES 3 B 212 GLN ASP ILE ASN SER TYR LEU SER TRP PHE GLN GLN LYS SEQRES 4 B 212 PRO GLY LYS SER PRO LYS THR LEU ILE TYR ARG ALA ASN SEQRES 5 B 212 ARG LEU VAL ASP GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 B 212 GLY SER GLY GLN ASP TYR SER LEU THR ILE SER SER LEU SEQRES 7 B 212 GLU TYR GLU ASP MET GLY ILE TYR PHE CYS LEU GLN TYR SEQRES 8 B 212 ASP GLU PHE PRO ARG THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 B 212 GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE SEQRES 10 B 212 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SEQRES 11 B 212 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP SEQRES 12 B 212 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN SEQRES 13 B 212 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS SEQRES 14 B 212 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR SEQRES 15 B 212 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU SEQRES 16 B 212 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER SEQRES 17 B 212 PHE ASN ARG ASN SEQRES 1 L 212 ASP ILE LYS MET THR GLN SER PRO SER SER MET TYR ALA SEQRES 2 L 212 SER LEU GLY GLU ARG VAL THR PHE THR CYS ARG ALA SER SEQRES 3 L 212 GLN ASP ILE ASN SER TYR LEU SER TRP PHE GLN GLN LYS SEQRES 4 L 212 PRO GLY LYS SER PRO LYS THR LEU ILE TYR ARG ALA ASN SEQRES 5 L 212 ARG LEU VAL ASP GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 212 GLY SER GLY GLN ASP TYR SER LEU THR ILE SER SER LEU SEQRES 7 L 212 GLU TYR GLU ASP MET GLY ILE TYR PHE CYS LEU GLN TYR SEQRES 8 L 212 ASP GLU PHE PRO ARG THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 L 212 GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE SEQRES 10 L 212 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SEQRES 11 L 212 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP SEQRES 12 L 212 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN SEQRES 13 L 212 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS SEQRES 14 L 212 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR SEQRES 15 L 212 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU SEQRES 16 L 212 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER SEQRES 17 L 212 PHE ASN ARG ASN SEQRES 1 D 212 ASP ILE LYS MET THR GLN SER PRO SER SER MET TYR ALA SEQRES 2 D 212 SER LEU GLY GLU ARG VAL THR PHE THR CYS ARG ALA SER SEQRES 3 D 212 GLN ASP ILE ASN SER TYR LEU SER TRP PHE GLN GLN LYS SEQRES 4 D 212 PRO GLY LYS SER PRO LYS THR LEU ILE TYR ARG ALA ASN SEQRES 5 D 212 ARG LEU VAL ASP GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 D 212 GLY SER GLY GLN ASP TYR SER LEU THR ILE SER SER LEU SEQRES 7 D 212 GLU TYR GLU ASP MET GLY ILE TYR PHE CYS LEU GLN TYR SEQRES 8 D 212 ASP GLU PHE PRO ARG THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 D 212 GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE SEQRES 10 D 212 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SEQRES 11 D 212 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP SEQRES 12 D 212 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN SEQRES 13 D 212 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS SEQRES 14 D 212 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR SEQRES 15 D 212 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU SEQRES 16 D 212 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER SEQRES 17 D 212 PHE ASN ARG ASN SEQRES 1 F 212 ASP ILE LYS MET THR GLN SER PRO SER SER MET TYR ALA SEQRES 2 F 212 SER LEU GLY GLU ARG VAL THR PHE THR CYS ARG ALA SER SEQRES 3 F 212 GLN ASP ILE ASN SER TYR LEU SER TRP PHE GLN GLN LYS SEQRES 4 F 212 PRO GLY LYS SER PRO LYS THR LEU ILE TYR ARG ALA ASN SEQRES 5 F 212 ARG LEU VAL ASP GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 F 212 GLY SER GLY GLN ASP TYR SER LEU THR ILE SER SER LEU SEQRES 7 F 212 GLU TYR GLU ASP MET GLY ILE TYR PHE CYS LEU GLN TYR SEQRES 8 F 212 ASP GLU PHE PRO ARG THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 F 212 GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE SEQRES 10 F 212 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SEQRES 11 F 212 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP SEQRES 12 F 212 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN SEQRES 13 F 212 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS SEQRES 14 F 212 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR SEQRES 15 F 212 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU SEQRES 16 F 212 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER SEQRES 17 F 212 PHE ASN ARG ASN SEQRES 1 H 217 GLU VAL LYS LEU GLU GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 217 PRO GLY GLY SER MET LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 H 217 PHE THR PHE SER ASP ALA TRP MET ASP TRP VAL ARG GLN SEQRES 4 H 217 SER PRO GLU LYS GLY LEU GLU TRP VAL ALA GLU ILE GLY SEQRES 5 H 217 ASN TYR ALA ILE ASN HIS ALA THR TYR TYR ALA GLU SER SEQRES 6 H 217 VAL LYS GLY ARG PHE ALA ILE SER ARG ASP ASP SER LYS SEQRES 7 H 217 SER SER VAL TYR LEU GLN MET ASN SER LEU ARG PRO GLU SEQRES 8 H 217 ASP THR GLY ILE TYR PHE CYS THR VAL ARG PHE ALA TYR SEQRES 9 H 217 TRP GLY GLN GLY THR LEU VAL THR VAL SER ALA ALA LYS SEQRES 10 H 217 THR THR PRO PRO SER VAL TYR PRO LEU ALA PRO GLY SER SEQRES 11 H 217 ALA ALA GLN THR ASN SER MET VAL THR LEU GLY CYS LEU SEQRES 12 H 217 VAL LYS GLY TYR PHE PRO GLU PRO VAL THR VAL THR TRP SEQRES 13 H 217 ASN SER GLY SER LEU SER SER GLY VAL HIS THR PHE PRO SEQRES 14 H 217 ALA VAL LEU GLN SER ASP LEU TYR THR LEU SER SER SER SEQRES 15 H 217 VAL THR VAL PRO SER SER THR TRP PRO SER GLU THR VAL SEQRES 16 H 217 THR CYS ASN VAL ALA HIS PRO ALA SER SER THR LYS VAL SEQRES 17 H 217 ASP LYS LYS ILE VAL PRO ARG ASP CYS SEQRES 1 C 217 GLU VAL LYS LEU GLU GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 C 217 PRO GLY GLY SER MET LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 C 217 PHE THR PHE SER ASP ALA TRP MET ASP TRP VAL ARG GLN SEQRES 4 C 217 SER PRO GLU LYS GLY LEU GLU TRP VAL ALA GLU ILE GLY SEQRES 5 C 217 ASN TYR ALA ILE ASN HIS ALA THR TYR TYR ALA GLU SER SEQRES 6 C 217 VAL LYS GLY ARG PHE ALA ILE SER ARG ASP ASP SER LYS SEQRES 7 C 217 SER SER VAL TYR LEU GLN MET ASN SER LEU ARG PRO GLU SEQRES 8 C 217 ASP THR GLY ILE TYR PHE CYS THR VAL ARG PHE ALA TYR SEQRES 9 C 217 TRP GLY GLN GLY THR LEU VAL THR VAL SER ALA ALA LYS SEQRES 10 C 217 THR THR PRO PRO SER VAL TYR PRO LEU ALA PRO GLY SER SEQRES 11 C 217 ALA ALA GLN THR ASN SER MET VAL THR LEU GLY CYS LEU SEQRES 12 C 217 VAL LYS GLY TYR PHE PRO GLU PRO VAL THR VAL THR TRP SEQRES 13 C 217 ASN SER GLY SER LEU SER SER GLY VAL HIS THR PHE PRO SEQRES 14 C 217 ALA VAL LEU GLN SER ASP LEU TYR THR LEU SER SER SER SEQRES 15 C 217 VAL THR VAL PRO SER SER THR TRP PRO SER GLU THR VAL SEQRES 16 C 217 THR CYS ASN VAL ALA HIS PRO ALA SER SER THR LYS VAL SEQRES 17 C 217 ASP LYS LYS ILE VAL PRO ARG ASP CYS SEQRES 1 E 217 GLU VAL LYS LEU GLU GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 E 217 PRO GLY GLY SER MET LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 E 217 PHE THR PHE SER ASP ALA TRP MET ASP TRP VAL ARG GLN SEQRES 4 E 217 SER PRO GLU LYS GLY LEU GLU TRP VAL ALA GLU ILE GLY SEQRES 5 E 217 ASN TYR ALA ILE ASN HIS ALA THR TYR TYR ALA GLU SER SEQRES 6 E 217 VAL LYS GLY ARG PHE ALA ILE SER ARG ASP ASP SER LYS SEQRES 7 E 217 SER SER VAL TYR LEU GLN MET ASN SER LEU ARG PRO GLU SEQRES 8 E 217 ASP THR GLY ILE TYR PHE CYS THR VAL ARG PHE ALA TYR SEQRES 9 E 217 TRP GLY GLN GLY THR LEU VAL THR VAL SER ALA ALA LYS SEQRES 10 E 217 THR THR PRO PRO SER VAL TYR PRO LEU ALA PRO GLY SER SEQRES 11 E 217 ALA ALA GLN THR ASN SER MET VAL THR LEU GLY CYS LEU SEQRES 12 E 217 VAL LYS GLY TYR PHE PRO GLU PRO VAL THR VAL THR TRP SEQRES 13 E 217 ASN SER GLY SER LEU SER SER GLY VAL HIS THR PHE PRO SEQRES 14 E 217 ALA VAL LEU GLN SER ASP LEU TYR THR LEU SER SER SER SEQRES 15 E 217 VAL THR VAL PRO SER SER THR TRP PRO SER GLU THR VAL SEQRES 16 E 217 THR CYS ASN VAL ALA HIS PRO ALA SER SER THR LYS VAL SEQRES 17 E 217 ASP LYS LYS ILE VAL PRO ARG ASP CYS HET NAG T 1 30 HET GAL T 2 22 HET FUC T 3 21 HET NAG V 1 30 HET GAL V 2 22 HET FUC V 3 21 HET NAG U 1 30 HET GAL U 2 22 HET SIA U 3 37 HET FUC U 4 21 HET NAG S 1 30 HET FUC S 2 21 HET SIA B 301 37 HET SIA L 301 37 HET PEG L 302 17 HET SIA F 301 37 HET GAL H 301 22 HET PEG H 302 17 HET PEG C 301 17 HET PEG C 302 17 HET PEG E 301 17 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM GAL BETA-D-GALACTOPYRANOSE HETNAM FUC ALPHA-L-FUCOPYRANOSE HETNAM SIA N-ACETYL-ALPHA-NEURAMINIC ACID HETNAM PEG DI(HYDROXYETHYL)ETHER 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 GAL BETA-D-GALACTOSE; D-GALACTOSE; GALACTOSE HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L- HETSYN 2 FUC FUCOSE; FUCOSE HETSYN SIA N-ACETYLNEURAMINIC ACID; SIALIC ACID; ALPHA-SIALIC HETSYN 2 SIA ACID; O-SIALIC ACID FORMUL 9 NAG 4(C8 H15 N O6) FORMUL 9 GAL 4(C6 H12 O6) FORMUL 9 FUC 4(C6 H12 O5) FORMUL 11 SIA 4(C11 H19 N O9) FORMUL 15 PEG 5(C4 H10 O3) FORMUL 22 HOH *18(H2 O) HELIX 1 AA1 GLU A 64 LYS A 67 5 4 HELIX 2 AA2 ARG A 89 THR A 93 5 5 HELIX 3 AA3 SER A 158 SER A 160 5 3 HELIX 4 AA4 PRO A 202 SER A 205 5 4 HELIX 5 AA5 GLU B 79 MET B 83 5 5 HELIX 6 AA6 SER B 121 THR B 126 1 6 HELIX 7 AA7 LYS B 183 GLU B 187 1 5 HELIX 8 AA8 GLU L 79 MET L 83 5 5 HELIX 9 AA9 SER L 121 THR L 126 1 6 HELIX 10 AB1 LYS L 183 GLU L 187 1 5 HELIX 11 AB2 GLU D 79 MET D 83 5 5 HELIX 12 AB3 SER D 121 THR D 126 1 6 HELIX 13 AB4 LYS D 183 GLU D 187 1 5 HELIX 14 AB5 GLU F 79 MET F 83 5 5 HELIX 15 AB6 SER F 121 THR F 126 1 6 HELIX 16 AB7 LYS F 183 GLU F 187 1 5 HELIX 17 AB8 GLU H 64 LYS H 67 5 4 HELIX 18 AB9 ARG H 89 THR H 93 5 5 HELIX 19 AC1 SER H 158 SER H 160 5 3 HELIX 20 AC2 PRO H 202 SER H 205 5 4 HELIX 21 AC3 GLU C 64 LYS C 67 5 4 HELIX 22 AC4 ARG C 89 THR C 93 5 5 HELIX 23 AC5 SER C 158 SER C 160 5 3 HELIX 24 AC6 PRO C 202 SER C 205 5 4 HELIX 25 AC7 ARG E 89 THR E 93 5 5 HELIX 26 AC8 SER E 158 SER E 160 5 3 HELIX 27 AC9 PRO E 202 SER E 205 5 4 SHEET 1 AA1 4 LYS A 3 SER A 7 0 SHEET 2 AA1 4 MET A 18 SER A 25 -1 O ALA A 23 N GLU A 5 SHEET 3 AA1 4 SER A 80 MET A 85 -1 O MET A 85 N MET A 18 SHEET 4 AA1 4 PHE A 70 ASP A 75 -1 N ALA A 71 O GLN A 84 SHEET 1 AA2 6 GLY A 10 VAL A 12 0 SHEET 2 AA2 6 THR A 109 VAL A 113 1 O LEU A 110 N GLY A 10 SHEET 3 AA2 6 GLY A 94 VAL A 100 -1 N GLY A 94 O VAL A 111 SHEET 4 AA2 6 MET A 34 SER A 40 -1 N VAL A 37 O PHE A 97 SHEET 5 AA2 6 GLY A 44 ILE A 51 -1 O GLU A 46 N ARG A 38 SHEET 6 AA2 6 THR A 60 TYR A 62 -1 O TYR A 61 N GLU A 50 SHEET 1 AA3 4 GLY A 10 VAL A 12 0 SHEET 2 AA3 4 THR A 109 VAL A 113 1 O LEU A 110 N GLY A 10 SHEET 3 AA3 4 GLY A 94 VAL A 100 -1 N GLY A 94 O VAL A 111 SHEET 4 AA3 4 TYR A 104 TRP A 105 -1 O TYR A 104 N VAL A 100 SHEET 1 AA4 4 SER A 122 LEU A 126 0 SHEET 2 AA4 4 MET A 137 TYR A 147 -1 O LEU A 143 N TYR A 124 SHEET 3 AA4 4 TYR A 177 PRO A 186 -1 O TYR A 177 N TYR A 147 SHEET 4 AA4 4 VAL A 165 THR A 167 -1 N HIS A 166 O SER A 182 SHEET 1 AA5 4 SER A 122 LEU A 126 0 SHEET 2 AA5 4 MET A 137 TYR A 147 -1 O LEU A 143 N TYR A 124 SHEET 3 AA5 4 TYR A 177 PRO A 186 -1 O TYR A 177 N TYR A 147 SHEET 4 AA5 4 VAL A 171 LEU A 172 -1 N VAL A 171 O THR A 178 SHEET 1 AA6 3 THR A 153 TRP A 156 0 SHEET 2 AA6 3 VAL A 195 HIS A 201 -1 O ASN A 198 N THR A 155 SHEET 3 AA6 3 THR A 206 ILE A 212 -1 O VAL A 208 N VAL A 199 SHEET 1 AA7 4 MET B 4 SER B 7 0 SHEET 2 AA7 4 VAL B 19 ALA B 25 -1 O ARG B 24 N THR B 5 SHEET 3 AA7 4 ASP B 70 ILE B 75 -1 O LEU B 73 N PHE B 21 SHEET 4 AA7 4 PHE B 62 SER B 67 -1 N SER B 63 O THR B 74 SHEET 1 AA8 6 SER B 10 SER B 14 0 SHEET 2 AA8 6 THR B 102 LYS B 107 1 O LYS B 107 N ALA B 13 SHEET 3 AA8 6 GLY B 84 GLN B 90 -1 N GLY B 84 O LEU B 104 SHEET 4 AA8 6 LEU B 33 GLN B 38 -1 N GLN B 38 O ILE B 85 SHEET 5 AA8 6 PRO B 44 TYR B 49 -1 O LEU B 47 N TRP B 35 SHEET 6 AA8 6 ARG B 53 LEU B 54 -1 O ARG B 53 N TYR B 49 SHEET 1 AA9 4 SER B 10 SER B 14 0 SHEET 2 AA9 4 THR B 102 LYS B 107 1 O LYS B 107 N ALA B 13 SHEET 3 AA9 4 GLY B 84 GLN B 90 -1 N GLY B 84 O LEU B 104 SHEET 4 AA9 4 THR B 97 PHE B 98 -1 O THR B 97 N GLN B 90 SHEET 1 AB1 4 THR B 114 PHE B 118 0 SHEET 2 AB1 4 GLY B 129 PHE B 139 -1 O ASN B 137 N THR B 114 SHEET 3 AB1 4 TYR B 173 THR B 182 -1 O LEU B 179 N VAL B 132 SHEET 4 AB1 4 ASN B 161 TRP B 163 -1 N SER B 162 O SER B 176 SHEET 1 AB2 4 SER B 153 ARG B 155 0 SHEET 2 AB2 4 TRP B 148 ILE B 150 -1 N TRP B 148 O ARG B 155 SHEET 3 AB2 4 SER B 191 ALA B 196 -1 O THR B 193 N LYS B 149 SHEET 4 AB2 4 ILE B 205 ASN B 210 -1 O ILE B 205 N ALA B 196 SHEET 1 AB3 4 MET L 4 SER L 7 0 SHEET 2 AB3 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AB3 4 ASP L 70 ILE L 75 -1 O LEU L 73 N PHE L 21 SHEET 4 AB3 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AB4 6 SER L 10 SER L 14 0 SHEET 2 AB4 6 THR L 102 LYS L 107 1 O LYS L 107 N ALA L 13 SHEET 3 AB4 6 GLY L 84 GLN L 90 -1 N GLY L 84 O LEU L 104 SHEET 4 AB4 6 LEU L 33 GLN L 38 -1 N GLN L 38 O ILE L 85 SHEET 5 AB4 6 PRO L 44 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AB4 6 ARG L 53 LEU L 54 -1 O ARG L 53 N TYR L 49 SHEET 1 AB5 4 SER L 10 SER L 14 0 SHEET 2 AB5 4 THR L 102 LYS L 107 1 O LYS L 107 N ALA L 13 SHEET 3 AB5 4 GLY L 84 GLN L 90 -1 N GLY L 84 O LEU L 104 SHEET 4 AB5 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AB6 4 THR L 114 PHE L 118 0 SHEET 2 AB6 4 GLY L 129 PHE L 139 -1 O VAL L 133 N PHE L 118 SHEET 3 AB6 4 TYR L 173 THR L 182 -1 O LEU L 179 N VAL L 132 SHEET 4 AB6 4 VAL L 159 TRP L 163 -1 N SER L 162 O SER L 176 SHEET 1 AB7 4 SER L 153 ARG L 155 0 SHEET 2 AB7 4 TRP L 148 ILE L 150 -1 N TRP L 148 O ARG L 155 SHEET 3 AB7 4 SER L 191 ALA L 196 -1 O THR L 193 N LYS L 149 SHEET 4 AB7 4 ILE L 205 ASN L 210 -1 O ILE L 205 N ALA L 196 SHEET 1 AB8 4 MET D 4 SER D 7 0 SHEET 2 AB8 4 VAL D 19 ALA D 25 -1 O ARG D 24 N THR D 5 SHEET 3 AB8 4 ASP D 70 ILE D 75 -1 O LEU D 73 N PHE D 21 SHEET 4 AB8 4 PHE D 62 SER D 67 -1 N SER D 63 O THR D 74 SHEET 1 AB9 6 SER D 10 SER D 14 0 SHEET 2 AB9 6 THR D 102 LYS D 107 1 O LYS D 107 N ALA D 13 SHEET 3 AB9 6 GLY D 84 GLN D 90 -1 N GLY D 84 O LEU D 104 SHEET 4 AB9 6 LEU D 33 GLN D 38 -1 N GLN D 38 O ILE D 85 SHEET 5 AB9 6 PRO D 44 TYR D 49 -1 O LEU D 47 N TRP D 35 SHEET 6 AB9 6 ARG D 53 LEU D 54 -1 O ARG D 53 N TYR D 49 SHEET 1 AC1 4 SER D 10 SER D 14 0 SHEET 2 AC1 4 THR D 102 LYS D 107 1 O LYS D 107 N ALA D 13 SHEET 3 AC1 4 GLY D 84 GLN D 90 -1 N GLY D 84 O LEU D 104 SHEET 4 AC1 4 THR D 97 PHE D 98 -1 O THR D 97 N GLN D 90 SHEET 1 AC2 4 THR D 114 PHE D 118 0 SHEET 2 AC2 4 GLY D 129 PHE D 139 -1 O VAL D 133 N PHE D 118 SHEET 3 AC2 4 TYR D 173 THR D 182 -1 O LEU D 179 N VAL D 132 SHEET 4 AC2 4 VAL D 159 TRP D 163 -1 N SER D 162 O SER D 176 SHEET 1 AC3 4 SER D 153 ARG D 155 0 SHEET 2 AC3 4 TRP D 148 ILE D 150 -1 N TRP D 148 O ARG D 155 SHEET 3 AC3 4 SER D 191 ALA D 196 -1 O THR D 193 N LYS D 149 SHEET 4 AC3 4 ILE D 205 ASN D 210 -1 O ILE D 205 N ALA D 196 SHEET 1 AC4 4 MET F 4 SER F 7 0 SHEET 2 AC4 4 VAL F 19 ALA F 25 -1 O ARG F 24 N THR F 5 SHEET 3 AC4 4 ASP F 70 ILE F 75 -1 O LEU F 73 N PHE F 21 SHEET 4 AC4 4 PHE F 62 SER F 67 -1 N SER F 63 O THR F 74 SHEET 1 AC5 6 SER F 10 SER F 14 0 SHEET 2 AC5 6 THR F 102 LYS F 107 1 O LYS F 107 N ALA F 13 SHEET 3 AC5 6 GLY F 84 GLN F 90 -1 N GLY F 84 O LEU F 104 SHEET 4 AC5 6 LEU F 33 GLN F 38 -1 N GLN F 38 O ILE F 85 SHEET 5 AC5 6 PRO F 44 TYR F 49 -1 O LEU F 47 N TRP F 35 SHEET 6 AC5 6 ARG F 53 LEU F 54 -1 O ARG F 53 N TYR F 49 SHEET 1 AC6 4 SER F 10 SER F 14 0 SHEET 2 AC6 4 THR F 102 LYS F 107 1 O LYS F 107 N ALA F 13 SHEET 3 AC6 4 GLY F 84 GLN F 90 -1 N GLY F 84 O LEU F 104 SHEET 4 AC6 4 THR F 97 PHE F 98 -1 O THR F 97 N GLN F 90 SHEET 1 AC7 4 THR F 114 PHE F 118 0 SHEET 2 AC7 4 GLY F 129 PHE F 139 -1 O VAL F 133 N PHE F 118 SHEET 3 AC7 4 TYR F 173 THR F 182 -1 O LEU F 179 N VAL F 132 SHEET 4 AC7 4 ASN F 161 TRP F 163 -1 N SER F 162 O SER F 176 SHEET 1 AC8 4 SER F 153 ARG F 155 0 SHEET 2 AC8 4 TRP F 148 ILE F 150 -1 N TRP F 148 O ARG F 155 SHEET 3 AC8 4 SER F 191 ALA F 196 -1 O THR F 193 N LYS F 149 SHEET 4 AC8 4 ILE F 205 ASN F 210 -1 O ILE F 205 N ALA F 196 SHEET 1 AC9 4 LYS H 3 SER H 7 0 SHEET 2 AC9 4 MET H 18 SER H 25 -1 O SER H 25 N LYS H 3 SHEET 3 AC9 4 SER H 80 MET H 85 -1 O MET H 85 N MET H 18 SHEET 4 AC9 4 PHE H 70 ASP H 75 -1 N ALA H 71 O GLN H 84 SHEET 1 AD1 6 GLY H 10 VAL H 12 0 SHEET 2 AD1 6 THR H 109 VAL H 113 1 O LEU H 110 N GLY H 10 SHEET 3 AD1 6 GLY H 94 VAL H 100 -1 N GLY H 94 O VAL H 111 SHEET 4 AD1 6 MET H 34 SER H 40 -1 N VAL H 37 O PHE H 97 SHEET 5 AD1 6 GLY H 44 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AD1 6 THR H 60 TYR H 62 -1 O TYR H 61 N GLU H 50 SHEET 1 AD2 4 GLY H 10 VAL H 12 0 SHEET 2 AD2 4 THR H 109 VAL H 113 1 O LEU H 110 N GLY H 10 SHEET 3 AD2 4 GLY H 94 VAL H 100 -1 N GLY H 94 O VAL H 111 SHEET 4 AD2 4 TYR H 104 TRP H 105 -1 O TYR H 104 N VAL H 100 SHEET 1 AD3 4 SER H 122 LEU H 126 0 SHEET 2 AD3 4 MET H 137 TYR H 147 -1 O LEU H 143 N TYR H 124 SHEET 3 AD3 4 LEU H 176 PRO H 186 -1 O TYR H 177 N TYR H 147 SHEET 4 AD3 4 VAL H 165 THR H 167 -1 N HIS H 166 O SER H 182 SHEET 1 AD4 4 SER H 122 LEU H 126 0 SHEET 2 AD4 4 MET H 137 TYR H 147 -1 O LEU H 143 N TYR H 124 SHEET 3 AD4 4 LEU H 176 PRO H 186 -1 O TYR H 177 N TYR H 147 SHEET 4 AD4 4 VAL H 171 GLN H 173 -1 N GLN H 173 O LEU H 176 SHEET 1 AD5 3 THR H 153 TRP H 156 0 SHEET 2 AD5 3 VAL H 195 HIS H 201 -1 O ASN H 198 N THR H 155 SHEET 3 AD5 3 THR H 206 ILE H 212 -1 O VAL H 208 N VAL H 199 SHEET 1 AD6 4 LYS C 3 SER C 7 0 SHEET 2 AD6 4 MET C 18 SER C 25 -1 O ALA C 23 N GLU C 5 SHEET 3 AD6 4 SER C 80 MET C 85 -1 O MET C 85 N MET C 18 SHEET 4 AD6 4 PHE C 70 ASP C 75 -1 N ALA C 71 O GLN C 84 SHEET 1 AD7 6 GLY C 10 VAL C 12 0 SHEET 2 AD7 6 THR C 109 VAL C 113 1 O LEU C 110 N GLY C 10 SHEET 3 AD7 6 GLY C 94 VAL C 100 -1 N GLY C 94 O VAL C 111 SHEET 4 AD7 6 MET C 34 SER C 40 -1 N VAL C 37 O PHE C 97 SHEET 5 AD7 6 GLY C 44 ILE C 51 -1 O GLU C 46 N ARG C 38 SHEET 6 AD7 6 THR C 60 TYR C 62 -1 O TYR C 61 N GLU C 50 SHEET 1 AD8 4 GLY C 10 VAL C 12 0 SHEET 2 AD8 4 THR C 109 VAL C 113 1 O LEU C 110 N GLY C 10 SHEET 3 AD8 4 GLY C 94 VAL C 100 -1 N GLY C 94 O VAL C 111 SHEET 4 AD8 4 TYR C 104 TRP C 105 -1 O TYR C 104 N VAL C 100 SHEET 1 AD9 4 SER C 122 LEU C 126 0 SHEET 2 AD9 4 MET C 137 TYR C 147 -1 O LEU C 143 N TYR C 124 SHEET 3 AD9 4 LEU C 176 PRO C 186 -1 O TYR C 177 N TYR C 147 SHEET 4 AD9 4 VAL C 165 THR C 167 -1 N HIS C 166 O SER C 182 SHEET 1 AE1 4 SER C 122 LEU C 126 0 SHEET 2 AE1 4 MET C 137 TYR C 147 -1 O LEU C 143 N TYR C 124 SHEET 3 AE1 4 LEU C 176 PRO C 186 -1 O TYR C 177 N TYR C 147 SHEET 4 AE1 4 VAL C 171 GLN C 173 -1 N GLN C 173 O LEU C 176 SHEET 1 AE2 3 THR C 153 TRP C 156 0 SHEET 2 AE2 3 VAL C 195 HIS C 201 -1 O ASN C 198 N THR C 155 SHEET 3 AE2 3 THR C 206 ILE C 212 -1 O VAL C 208 N VAL C 199 SHEET 1 AE3 6 GLY E 10 VAL E 12 0 SHEET 2 AE3 6 THR E 109 VAL E 113 1 O LEU E 110 N GLY E 10 SHEET 3 AE3 6 GLY E 94 THR E 99 -1 N GLY E 94 O VAL E 111 SHEET 4 AE3 6 MET E 34 SER E 40 -1 N VAL E 37 O PHE E 97 SHEET 5 AE3 6 GLY E 44 ILE E 51 -1 O GLU E 46 N ARG E 38 SHEET 6 AE3 6 THR E 60 TYR E 62 -1 O TYR E 61 N GLU E 50 SHEET 1 AE4 3 MET E 18 ALA E 23 0 SHEET 2 AE4 3 SER E 80 MET E 85 -1 O MET E 85 N MET E 18 SHEET 3 AE4 3 ALA E 71 ASP E 75 -1 N ALA E 71 O GLN E 84 SHEET 1 AE5 4 SER E 122 LEU E 126 0 SHEET 2 AE5 4 MET E 137 TYR E 147 -1 O LEU E 143 N TYR E 124 SHEET 3 AE5 4 TYR E 177 PRO E 186 -1 O TYR E 177 N TYR E 147 SHEET 4 AE5 4 VAL E 165 THR E 167 -1 N HIS E 166 O SER E 182 SHEET 1 AE6 4 SER E 122 LEU E 126 0 SHEET 2 AE6 4 MET E 137 TYR E 147 -1 O LEU E 143 N TYR E 124 SHEET 3 AE6 4 TYR E 177 PRO E 186 -1 O TYR E 177 N TYR E 147 SHEET 4 AE6 4 VAL E 171 LEU E 172 -1 N VAL E 171 O THR E 178 SHEET 1 AE7 3 THR E 153 TRP E 156 0 SHEET 2 AE7 3 VAL E 195 HIS E 201 -1 O ASN E 198 N THR E 155 SHEET 3 AE7 3 THR E 206 ILE E 212 -1 O VAL E 208 N VAL E 199 SSBOND 1 CYS A 22 CYS A 98 1555 1555 2.05 SSBOND 2 CYS A 142 CYS A 197 1555 1555 2.12 SSBOND 3 CYS B 23 CYS B 88 1555 1555 2.07 SSBOND 4 CYS B 134 CYS B 194 1555 1555 2.07 SSBOND 5 CYS L 23 CYS L 88 1555 1555 2.05 SSBOND 6 CYS L 134 CYS L 194 1555 1555 2.05 SSBOND 7 CYS D 23 CYS D 88 1555 1555 2.20 SSBOND 8 CYS D 134 CYS D 194 1555 1555 2.10 SSBOND 9 CYS F 23 CYS F 88 1555 1555 2.16 SSBOND 10 CYS F 134 CYS F 194 1555 1555 2.09 SSBOND 11 CYS H 22 CYS H 98 1555 1555 2.25 SSBOND 12 CYS H 142 CYS H 197 1555 1555 2.08 SSBOND 13 CYS C 22 CYS C 98 1555 1555 2.07 SSBOND 14 CYS C 142 CYS C 197 1555 1555 2.13 SSBOND 15 CYS E 22 CYS E 98 1555 1555 2.24 SSBOND 16 CYS E 142 CYS E 197 1555 1555 2.22 LINK O3 NAG T 1 C1 GAL T 2 1555 1555 1.40 LINK O4 NAG T 1 C1 FUC T 3 1555 1555 1.42 LINK O3 NAG V 1 C1 GAL V 2 1555 1555 1.40 LINK O4 NAG V 1 C1 FUC V 3 1555 1555 1.40 LINK O3 NAG U 1 C1 GAL U 2 1555 1555 1.40 LINK O4 NAG U 1 C1 FUC U 4 1555 1555 1.43 LINK O3 GAL U 2 C2 SIA U 3 1555 1555 1.41 LINK O4 NAG S 1 C1 FUC S 2 1555 1555 1.52 CISPEP 1 PHE A 148 PRO A 149 0 -0.16 CISPEP 2 GLU A 150 PRO A 151 0 -3.84 CISPEP 3 TRP A 190 PRO A 191 0 0.35 CISPEP 4 SER B 7 PRO B 8 0 -4.41 CISPEP 5 PHE B 94 PRO B 95 0 1.56 CISPEP 6 TYR B 140 PRO B 141 0 -7.26 CISPEP 7 SER L 7 PRO L 8 0 -4.42 CISPEP 8 PHE L 94 PRO L 95 0 2.05 CISPEP 9 TYR L 140 PRO L 141 0 -7.40 CISPEP 10 SER D 7 PRO D 8 0 -4.50 CISPEP 11 PHE D 94 PRO D 95 0 2.89 CISPEP 12 TYR D 140 PRO D 141 0 -6.75 CISPEP 13 SER F 7 PRO F 8 0 -4.41 CISPEP 14 PHE F 94 PRO F 95 0 1.50 CISPEP 15 TYR F 140 PRO F 141 0 -7.22 CISPEP 16 PHE H 148 PRO H 149 0 0.24 CISPEP 17 GLU H 150 PRO H 151 0 -4.42 CISPEP 18 TRP H 190 PRO H 191 0 1.93 CISPEP 19 PHE C 148 PRO C 149 0 -0.25 CISPEP 20 GLU C 150 PRO C 151 0 -4.20 CISPEP 21 TRP C 190 PRO C 191 0 1.34 CISPEP 22 PHE E 148 PRO E 149 0 0.30 CISPEP 23 GLU E 150 PRO E 151 0 -3.99 CISPEP 24 TRP E 190 PRO E 191 0 0.58 CRYST1 39.838 108.697 108.920 89.60 87.34 89.25 P 1 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.025102 -0.000328 -0.001165 0.00000 SCALE2 0.000000 0.009201 -0.000058 0.00000 SCALE3 0.000000 0.000000 0.009191 0.00000