HEADER IMMUNE SYSTEM 02-FEB-24 8RWB TITLE CRYSTAL STRUCTURE OF ULBP6 IN COMPLEX WITH A BLOCKING ANTIBODY COMPND MOL_ID: 1; COMPND 2 MOLECULE: UL16-BINDING PROTEIN 6; COMPND 3 CHAIN: P; COMPND 4 SYNONYM: RETINOIC ACID EARLY TRANSCRIPT 1L PROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: HEAVY CHAIN; COMPND 8 CHAIN: H; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: LIGHT CHAIN; COMPND 12 CHAIN: L; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: RAET1L, ULBP6; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 10 ORGANISM_TAXID: 32630; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 15 ORGANISM_TAXID: 32630; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS FAB, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR S.BHARILL,I.CHEN,N.IVIC,Z.BAHRAMI DIZICHEH,Y.WU,S.DOAMEKPOR,P.KOENIG, AUTHOR 2 G.FUH REVDAT 1 12-FEB-25 8RWB 0 JRNL AUTH S.BHARILL,I.CHEN,N.IVIC,Z.BAHRAMI DIZICHEH,Y.WU,S.DOAMEKPOR, JRNL AUTH 2 P.KOENIG,G.FUH JRNL TITL CRYSTAL STRUCTURE OF ULBP6 IN COMPLEX WITH A BLOCKING JRNL TITL 2 ANTIBODY JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.31 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0267 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) : 2.31 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 86.03 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 52.4 REMARK 3 NUMBER OF REFLECTIONS : 19970 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) : 0.216 REMARK 3 FREE R VALUE : 0.287 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.038 REMARK 3 FREE R VALUE TEST SET COUNT : 1006 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) : 2.31 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.37 REMARK 3 REFLECTION IN BIN (WORKING SET) : 52 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 1.96 REMARK 3 BIN R VALUE (WORKING SET) : 0.3700 REMARK 3 BIN FREE R VALUE SET COUNT : 3 REMARK 3 BIN FREE R VALUE : 0.5380 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4617 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 60 REMARK 3 SOLVENT ATOMS : 134 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.24 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.67300 REMARK 3 B22 (A**2) : -0.98800 REMARK 3 B33 (A**2) : 0.07900 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.18200 REMARK 3 B23 (A**2) : 0.00000 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): 0.421 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.277 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.238 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.917 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.852 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4812 ; 0.004 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 4346 ; 0.002 ; 0.017 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6561 ; 1.422 ; 1.656 REMARK 3 BOND ANGLES OTHERS (DEGREES): 10051 ; 1.069 ; 1.584 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 618 ; 8.385 ; 5.146 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 215 ;36.953 ;23.209 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 765 ;15.511 ;15.118 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;13.761 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 640 ; 0.046 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5501 ; 0.004 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1091 ; 0.002 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 747 ; 0.151 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 42 ; 0.151 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2174 ; 0.147 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 121 ; 0.112 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL 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): 2430 ; 1.769 ; 4.611 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2429 ; 1.762 ; 4.609 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3042 ; 3.116 ; 6.908 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3043 ; 3.116 ; 6.910 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2382 ; 1.401 ; 4.622 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2383 ; 1.401 ; 4.622 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3517 ; 2.508 ; 6.893 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3518 ; 2.508 ; 6.893 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 : NULL 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 8RWB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-FEB-24. REMARK 100 THE DEPOSITION ID IS D_1292136349. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 02-NOV-22 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 : SLS REMARK 200 BEAMLINE : X10SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9998 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 S 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19970 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.307 REMARK 200 RESOLUTION RANGE LOW (A) : 86.031 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 92.3 REMARK 200 DATA REDUNDANCY : 4.000 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.31 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.66 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 : NULL 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 (%): 63.19 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.34 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: GLYCEROL 10.0 %V/V MES: 0.10 M PH:6.00 REMARK 280 PEG 1K 5.0 %W/V PEG 600 30.0 %W/V, VAPOR DIFFUSION, TEMPERATURE REMARK 280 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 53.27550 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.90150 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 53.27550 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 47.90150 REMARK 290 SMTRY3 4 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: P, 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 480 REMARK 480 ZERO OCCUPANCY ATOM REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 480 M RES C SSEQI ATOMS REMARK 480 LYS P 59 NZ REMARK 480 LYS P 80 NZ REMARK 480 LYS P 88 NZ REMARK 480 LYS P 116 CE NZ REMARK 480 LYS P 130 CG CD CE NZ REMARK 480 GLU P 132 CG CD OE1 OE2 REMARK 480 LYS P 167 NZ REMARK 480 SER H 149 OG REMARK 480 SER H 150 OG REMARK 480 LYS H 151 NZ REMARK 480 SER H 152 OG REMARK 480 SER H 210 OG REMARK 480 ILE H 217 CD1 REMARK 480 LYS H 232 NZ REMARK 480 LYS H 236 CE NZ REMARK 480 LYS L 60 NZ REMARK 480 LYS L 163 CD CE NZ REMARK 480 LYS L 167 CD CE NZ REMARK 480 LYS L 187 CE NZ REMARK 480 LYS L 206 CE NZ REMARK 480 LYS L 208 NZ 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 LEU P 81 -3.77 84.62 REMARK 500 GLU P 117 -147.22 60.48 REMARK 500 SER H 74 19.29 59.17 REMARK 500 SER H 104 49.39 39.47 REMARK 500 PHE H 122 84.96 -67.58 REMARK 500 ALA H 147 105.00 -55.25 REMARK 500 SER H 149 59.80 28.01 REMARK 500 ASP H 166 80.13 53.40 REMARK 500 ILE L 69 -56.71 77.30 REMARK 500 ILE L 101 107.70 -52.17 REMARK 500 ASN L 156 66.19 62.63 REMARK 500 LYS L 208 -57.90 -123.30 REMARK 500 SER L 220 -72.00 -54.89 REMARK 500 REMARK 500 REMARK: NULL DBREF 8RWB P 29 200 UNP Q5VY80 ULBP6_HUMAN 29 200 DBREF 8RWB H 21 237 PDB 8RWB 8RWB 21 237 DBREF 8RWB L 20 231 PDB 8RWB 8RWB 20 231 SEQADV 8RWB THR P 85 UNP Q5VY80 MET 85 VARIANT SEQRES 1 P 172 ASP PRO HIS SER LEU CYS TYR ASP ILE THR VAL ILE PRO SEQRES 2 P 172 LYS PHE ARG PRO GLY PRO ARG TRP CYS ALA VAL GLN GLY SEQRES 3 P 172 GLN VAL ASP GLU LYS THR PHE LEU HIS TYR ASP CYS GLY SEQRES 4 P 172 ASN LYS THR VAL THR PRO VAL SER PRO LEU GLY LYS LYS SEQRES 5 P 172 LEU ASN VAL THR THR ALA TRP LYS ALA GLN ASN PRO VAL SEQRES 6 P 172 LEU ARG GLU VAL VAL ASP ILE LEU THR GLU GLN LEU LEU SEQRES 7 P 172 ASP ILE GLN LEU GLU ASN TYR THR PRO LYS GLU PRO LEU SEQRES 8 P 172 THR LEU GLN ALA ARG MET SER CYS GLU GLN LYS ALA GLU SEQRES 9 P 172 GLY HIS SER SER GLY SER TRP GLN PHE SER ILE ASP GLY SEQRES 10 P 172 GLN THR PHE LEU LEU PHE ASP SER GLU LYS ARG MET TRP SEQRES 11 P 172 THR THR VAL HIS PRO GLY ALA ARG LYS MET LYS GLU LYS SEQRES 12 P 172 TRP GLU ASN ASP LYS ASP VAL ALA MET SER PHE HIS TYR SEQRES 13 P 172 ILE SER MET GLY ASP CYS ILE GLY TRP LEU GLU ASP PHE SEQRES 14 P 172 LEU MET GLY SEQRES 1 H 217 VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN PRO SEQRES 2 H 217 GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY PHE SEQRES 3 H 217 THR PHE SER THR TYR GLY PHE HIS TRP VAL ARG GLN ALA SEQRES 4 H 217 PRO GLY LYS GLY LEU GLU TRP VAL ALA TYR ILE SER SER SEQRES 5 H 217 ASN SER GLY THR ILE ASP TYR ALA ASP THR VAL LYS GLY SEQRES 6 H 217 ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SER LEU SEQRES 7 H 217 TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR ALA SEQRES 8 H 217 VAL TYR TYR CYS ALA ARG GLN GLY TYR GLY PHE ASP ASN SEQRES 9 H 217 TRP GLY GLN GLY THR THR VAL THR VAL SER SER ALA SER SEQRES 10 H 217 THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER SEQRES 11 H 217 LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU SEQRES 12 H 217 VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP SEQRES 13 H 217 ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO SEQRES 14 H 217 ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER SEQRES 15 H 217 VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR SEQRES 16 H 217 TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS SEQRES 17 H 217 VAL ASP LYS LYS VAL GLU PRO LYS SER SEQRES 1 L 212 ASP ILE GLN LEU THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 212 SER VAL GLY ASP ARG VAL THR ILE THR CYS SER ALA SER SEQRES 3 L 212 SER ARG VAL SER TYR MET ASN TRP TYR GLN GLN LYS PRO SEQRES 4 L 212 GLY LYS SER PRO LYS ILE TRP VAL TYR GLY ILE SER ASN SEQRES 5 L 212 LEU ALA SER GLY VAL PRO SER ARG PHE SER GLY SER GLY SEQRES 6 L 212 SER GLY THR ASP PHE THR PHE THR ILE SER SER LEU GLN SEQRES 7 L 212 PRO GLU ASP ILE ALA THR TYR TYR CYS GLN GLN ARG SER SEQRES 8 L 212 SER HIS PRO LEU THR PHE GLY GLY GLY THR LYS VAL GLU SEQRES 9 L 212 ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 10 L 212 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER SEQRES 11 L 212 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 12 L 212 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 13 L 212 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 14 L 212 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 15 L 212 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 16 L 212 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 17 L 212 ASN ARG GLY GLU HET NAG A 1 14 HET NAG A 2 14 HET NAG P 201 14 HET EDO H 301 4 HET GOL L 301 6 HET EDO L 302 4 HET EDO L 303 4 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM EDO 1,2-ETHANEDIOL HETNAM GOL GLYCEROL HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN EDO ETHYLENE GLYCOL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 4 NAG 3(C8 H15 N O6) FORMUL 6 EDO 3(C2 H6 O2) FORMUL 7 GOL C3 H8 O3 FORMUL 10 HOH *134(H2 O) HELIX 1 AA1 PRO P 41 ARG P 44 5 4 HELIX 2 AA2 THR P 85 ILE P 108 1 24 HELIX 3 AA3 HIS P 162 GLY P 164 5 3 HELIX 4 AA4 ALA P 165 ASP P 175 1 11 HELIX 5 AA5 ASP P 175 GLY P 188 1 14 HELIX 6 AA6 GLY P 188 GLY P 200 1 13 HELIX 7 AA7 THR H 47 TYR H 51 5 5 HELIX 8 AA8 ASP H 81 LYS H 84 5 4 HELIX 9 AA9 ARG H 106 THR H 110 5 5 HELIX 10 AB1 SER H 209 GLY H 212 5 4 HELIX 11 AB2 LYS H 223 ASN H 226 5 4 HELIX 12 AB3 GLN L 97 ILE L 101 5 5 HELIX 13 AB4 SER L 139 SER L 145 1 7 HELIX 14 AB5 SER L 200 HIS L 207 1 8 SHEET 1 AA1 8 VAL P 71 PRO P 73 0 SHEET 2 AA1 8 THR P 60 ASP P 65 -1 N HIS P 63 O THR P 72 SHEET 3 AA1 8 CYS P 50 VAL P 56 -1 N GLY P 54 O PHE P 61 SHEET 4 AA1 8 HIS P 31 VAL P 39 -1 N CYS P 34 O GLN P 55 SHEET 5 AA1 8 LEU P 121 GLN P 129 -1 O ALA P 123 N ILE P 37 SHEET 6 AA1 8 SER P 135 ILE P 143 -1 O SER P 142 N GLN P 122 SHEET 7 AA1 8 GLN P 146 ASP P 152 -1 O LEU P 149 N PHE P 141 SHEET 8 AA1 8 MET P 157 THR P 160 -1 O THR P 159 N LEU P 150 SHEET 1 AA2 4 GLN H 22 SER H 26 0 SHEET 2 AA2 4 LEU H 37 SER H 44 -1 O ALA H 42 N VAL H 24 SHEET 3 AA2 4 SER H 97 MET H 102 -1 O LEU H 98 N CYS H 41 SHEET 4 AA2 4 PHE H 87 ASP H 92 -1 N THR H 88 O GLN H 101 SHEET 1 AA3 6 LEU H 30 VAL H 31 0 SHEET 2 AA3 6 THR H 129 VAL H 133 1 O THR H 132 N VAL H 31 SHEET 3 AA3 6 ALA H 111 GLN H 118 -1 N TYR H 113 O THR H 129 SHEET 4 AA3 6 GLY H 52 GLN H 58 -1 N VAL H 56 O TYR H 114 SHEET 5 AA3 6 LEU H 64 ILE H 70 -1 O VAL H 67 N TRP H 55 SHEET 6 AA3 6 ILE H 77 TYR H 79 -1 O ASP H 78 N TYR H 69 SHEET 1 AA4 4 LEU H 30 VAL H 31 0 SHEET 2 AA4 4 THR H 129 VAL H 133 1 O THR H 132 N VAL H 31 SHEET 3 AA4 4 ALA H 111 GLN H 118 -1 N TYR H 113 O THR H 129 SHEET 4 AA4 4 PHE H 122 TRP H 125 -1 O ASN H 124 N ARG H 117 SHEET 1 AA5 4 SER H 142 LEU H 146 0 SHEET 2 AA5 4 THR H 157 TYR H 167 -1 O LEU H 163 N PHE H 144 SHEET 3 AA5 4 TYR H 198 PRO H 207 -1 O VAL H 206 N ALA H 158 SHEET 4 AA5 4 VAL H 191 LEU H 192 -1 N VAL H 191 O SER H 199 SHEET 1 AA6 3 THR H 173 TRP H 176 0 SHEET 2 AA6 3 ILE H 217 HIS H 222 -1 O ASN H 221 N THR H 173 SHEET 3 AA6 3 THR H 227 LYS H 232 -1 O VAL H 229 N VAL H 220 SHEET 1 AA7 4 LEU L 23 SER L 26 0 SHEET 2 AA7 4 VAL L 38 ALA L 44 -1 O THR L 41 N SER L 26 SHEET 3 AA7 4 ASP L 88 ILE L 93 -1 O PHE L 89 N CYS L 42 SHEET 4 AA7 4 PHE L 80 SER L 85 -1 N SER L 83 O THR L 90 SHEET 1 AA8 6 SER L 29 SER L 33 0 SHEET 2 AA8 6 THR L 120 LYS L 125 1 O GLU L 123 N LEU L 30 SHEET 3 AA8 6 ALA L 102 GLN L 108 -1 N ALA L 102 O VAL L 122 SHEET 4 AA8 6 MET L 51 GLN L 56 -1 N ASN L 52 O GLN L 107 SHEET 5 AA8 6 LYS L 63 TYR L 67 -1 O TRP L 65 N TRP L 53 SHEET 6 AA8 6 ASN L 71 LEU L 72 -1 O ASN L 71 N TYR L 67 SHEET 1 AA9 4 SER L 132 PHE L 136 0 SHEET 2 AA9 4 ALA L 148 PHE L 157 -1 O LEU L 153 N PHE L 134 SHEET 3 AA9 4 TYR L 191 LEU L 199 -1 O LEU L 199 N ALA L 148 SHEET 4 AA9 4 SER L 177 VAL L 181 -1 N SER L 180 O SER L 194 SHEET 1 AB1 3 ALA L 162 VAL L 168 0 SHEET 2 AB1 3 VAL L 209 HIS L 216 -1 O ALA L 211 N LYS L 167 SHEET 3 AB1 3 VAL L 223 ASN L 228 -1 O VAL L 223 N VAL L 214 SSBOND 1 CYS P 50 CYS P 66 1555 1555 2.05 SSBOND 2 CYS P 127 CYS P 190 1555 1555 2.04 SSBOND 3 CYS H 41 CYS H 115 1555 1555 2.06 SSBOND 4 CYS H 162 CYS H 218 1555 1555 2.05 SSBOND 5 CYS L 42 CYS L 106 1555 1555 2.11 SSBOND 6 CYS L 152 CYS L 212 1555 1555 2.03 LINK ND2 ASN P 68 C1 NAG A 1 1555 1555 1.43 LINK ND2 ASN P 82 C1 NAG P 201 1555 1555 1.45 LINK O4 NAG A 1 C1 NAG A 2 1555 1555 1.45 CISPEP 1 ARG P 44 PRO P 45 0 -12.50 CISPEP 2 SER P 75 PRO P 76 0 -6.90 CISPEP 3 PHE H 168 PRO H 169 0 -10.36 CISPEP 4 GLU H 170 PRO H 171 0 -12.64 CISPEP 5 SER L 26 PRO L 27 0 -2.08 CISPEP 6 HIS L 112 PRO L 113 0 1.61 CISPEP 7 TYR L 158 PRO L 159 0 3.69 CRYST1 106.551 95.803 97.203 90.00 117.74 90.00 C 1 2 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 0.009385 0.000000 0.004936 0.00000 SCALE2 0.000000 0.010438 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011624 0.00000