HEADER IMMUNE SYSTEM 06-SEP-24 9GOX TITLE CRYSTAL STRUCTURE OF FAB B6-D9 IN COMPLEX WITH CD38 COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB B6-D9 HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB B6-D9 LIGHT CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ADP-RIBOSYL CYCLASE/CYCLIC ADP-RIBOSE HYDROLASE 1; COMPND 11 CHAIN: A; COMPND 12 SYNONYM: 2'-PHOSPHO-ADP-RIBOSYL CYCLASE,2'-PHOSPHO-ADP-RIBOSYL COMPND 13 CYCLASE/2'-PHOSPHO-CYCLIC-ADP-RIBOSE TRANSFERASE,2'-PHOSPHO-CYCLIC- COMPND 14 ADP-RIBOSE TRANSFERASE,ADP-RIBOSYL CYCLASE 1,ADPRC 1,CYCLIC ADP- COMPND 15 RIBOSE HYDROLASE 1,CADPR HYDROLASE 1,T10; COMPND 16 EC: 3.2.2.-,3.2.2.6,2.4.99.20; COMPND 17 ENGINEERED: YES; COMPND 18 OTHER_DETAILS: EXTRACELLULAR DOMAIN OF UNIPROT ENTRY P28907 FUSED TO COMPND 19 A C-TERMINAL 8-HISTIDINE PEPTIDE TAG 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: HEK CELLS; 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 MOL_ID: 3; SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 14 ORGANISM_COMMON: HUMAN; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 GENE: CD38; SOURCE 17 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS FAB, BIPARATOPIC BISPECIFIC ANTIBODY, ANTIBODY, INNATE CELL KEYWDS 2 MODULATOR, CD38, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR C.DREYFUS,R.FREIER REVDAT 1 12-FEB-25 9GOX 0 JRNL AUTH J.LOYAU,T.MONNEY,M.MONTEFIORI,F.BOKHOVCHUK,J.STREULI, JRNL AUTH 2 M.BLACKBURN,A.GOEPFERT,L.N.CARO,S.CHAKRABORTI,S.DE ANGELIS, JRNL AUTH 3 C.GRANDCLEMENT,S.BLEIN,M.L.MBOW,A.SRIVASTAVA,M.PERRO, JRNL AUTH 4 S.SAMMICHELI,E.A.ZHUKOVSKY,M.DYSON,C.DREYFUS JRNL TITL BIPARATOPIC BINDING OF ISB 1442 TO CD38 IN TRANS ENABLES JRNL TITL 2 INCREASED CELL ANTIBODY DENSITY AND INCREASED AVIDITY. JRNL REF MABS V. 17 57471 2025 JRNL REFN ESSN 1942-0870 JRNL PMID 39882744 JRNL DOI 10.1080/19420862.2025.2457471 REMARK 2 REMARK 2 RESOLUTION. 1.84 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 : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.84 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 71.27 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 77.0 REMARK 3 NUMBER OF REFLECTIONS : 69483 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.176 REMARK 3 R VALUE (WORKING SET) : 0.174 REMARK 3 FREE R VALUE : 0.208 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 3668 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) : 1.84 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.89 REMARK 3 REFLECTION IN BIN (WORKING SET) : 169 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 2.57 REMARK 3 BIN R VALUE (WORKING SET) : 0.3030 REMARK 3 BIN FREE R VALUE SET COUNT : 9 REMARK 3 BIN FREE R VALUE : 0.5370 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 5341 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 113 REMARK 3 SOLVENT ATOMS : 696 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 34.96 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.96 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.01000 REMARK 3 B22 (A**2) : 0.01000 REMARK 3 B33 (A**2) : -0.03000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.134 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.128 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.093 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.306 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.951 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5756 ; 0.006 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 5250 ; 0.002 ; 0.017 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7869 ; 1.426 ; 1.658 REMARK 3 BOND ANGLES OTHERS (DEGREES): 12182 ; 1.216 ; 1.581 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 746 ; 7.599 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 260 ;36.112 ;22.962 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 924 ;13.889 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;19.447 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 773 ; 0.062 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7264 ; 0.005 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1307 ; 0.002 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL 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): 2849 ; 1.856 ; 3.566 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2847 ; 1.851 ; 3.564 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3586 ; 2.874 ; 5.338 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3587 ; 2.874 ; 5.340 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2907 ; 2.437 ; 3.785 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2905 ; 2.437 ; 3.784 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4265 ; 3.782 ; 5.554 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 6378 ; 6.258 ;42.210 REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 6219 ; 6.090 ;41.470 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 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 THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 9GOX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-SEP-24. REMARK 100 THE DEPOSITION ID IS D_1292141419. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 04-MAY-22 REMARK 200 TEMPERATURE (KELVIN) : 80 REMARK 200 PH : 7.2 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) : 0.9999 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROC, XDS (VERSION JAN 31, REMARK 200 AUTOPROC REMARK 200 DATA SCALING SOFTWARE : AUTOPROC (VERSION 1.1.7), REMARK 200 AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 73151 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.840 REMARK 200 RESOLUTION RANGE LOW (A) : 71.270 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 77.0 REMARK 200 DATA REDUNDANCY : 11.40 REMARK 200 R MERGE (I) : 0.13600 REMARK 200 R SYM (I) : 0.13600 REMARK 200 FOR THE DATA SET : 12.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.84 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02 REMARK 200 COMPLETENESS FOR SHELL (%) : 68.8 REMARK 200 DATA REDUNDANCY IN SHELL : 12.80 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 1.64000 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: MOLREP REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 65.11 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.52 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 7 % V/V T-MATE PH 7.0, 0.1 M HEPES PH REMARK 280 7.2, 20 % V/V PEG SMEAR MEDIUM (BCS SCREEN, MOLECULAR DIMENSIONS) REMARK 280 , VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -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 -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 39.38450 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 83.02250 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 83.02250 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 59.07675 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 83.02250 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 83.02250 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 19.69225 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 83.02250 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 83.02250 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 59.07675 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 83.02250 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 83.02250 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 19.69225 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 39.38450 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: 9300 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 30580 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL 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 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 HOH L 591 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 CYS H 216 REMARK 465 ARG A 45 REMARK 465 TRP A 46 REMARK 465 ARG A 47 REMARK 465 THR A 297 REMARK 465 SER A 298 REMARK 465 GLU A 299 REMARK 465 ILE A 300 REMARK 465 HIS A 301 REMARK 465 HIS A 302 REMARK 465 HIS A 303 REMARK 465 HIS A 304 REMARK 465 HIS A 305 REMARK 465 HIS A 306 REMARK 465 HIS A 307 REMARK 465 HIS A 308 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 GLN H 1 NE2 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 GLN H 61 CD OE1 NE2 REMARK 480 LYS H 129 CD CE NZ REMARK 480 LYS H 201 CD CE NZ REMARK 480 LYS H 210 NZ REMARK 480 LYS H 214 CE NZ REMARK 480 LYS L 145 NZ REMARK 480 LYS L 190 CE NZ REMARK 480 LYS A 69 CE NZ REMARK 480 ILE A 73 CD1 REMARK 480 ARG A 78 CZ NH1 NH2 REMARK 480 GLU A 104 CD OE1 OE2 REMARK 480 LYS A 214 NZ REMARK 480 LYS A 218 NZ REMARK 480 ARG A 247 CD NE CZ NH1 NH2 REMARK 480 LYS A 260 NZ REMARK 480 LYS A 276 CE NZ REMARK 480 LYS A 283 CE NZ REMARK 480 GLU A 292 CG CD OE1 OE2 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 OE1 GLN H 3 O HOH H 401 2.09 REMARK 500 NE2 GLN A 48 O HOH A 501 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 TYR H 99 127.14 -38.33 REMARK 500 SER L 30 -127.97 50.54 REMARK 500 SER L 30 -126.73 48.20 REMARK 500 ALA L 51 -31.97 68.41 REMARK 500 ALA L 84 174.49 178.26 REMARK 500 ASN L 152 -1.90 77.09 REMARK 500 ILE A 128 42.93 -153.32 REMARK 500 ASP A 179 -60.13 -104.40 REMARK 500 ASP A 202 -122.36 64.51 REMARK 500 VAL A 225 -62.86 -120.35 REMARK 500 SER A 294 -158.44 58.78 REMARK 500 SER A 294 -158.24 58.78 REMARK 500 REMARK 500 REMARK: NULL DBREF 9GOX H 1 216 PDB 9GOX 9GOX 1 216 DBREF 9GOX L 1 214 PDB 9GOX 9GOX 1 214 DBREF 9GOX A 45 300 UNP P28907 CD38_HUMAN 45 300 SEQADV 9GOX HIS A 301 UNP P28907 EXPRESSION TAG SEQADV 9GOX HIS A 302 UNP P28907 EXPRESSION TAG SEQADV 9GOX HIS A 303 UNP P28907 EXPRESSION TAG SEQADV 9GOX HIS A 304 UNP P28907 EXPRESSION TAG SEQADV 9GOX HIS A 305 UNP P28907 EXPRESSION TAG SEQADV 9GOX HIS A 306 UNP P28907 EXPRESSION TAG SEQADV 9GOX HIS A 307 UNP P28907 EXPRESSION TAG SEQADV 9GOX HIS A 308 UNP P28907 EXPRESSION TAG SEQRES 1 H 224 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 224 PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 H 224 GLY PHE PHE SER HIS TYR ILE ILE ASN TRP VAL ARG GLN SEQRES 4 H 224 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY ARG VAL ILE SEQRES 5 H 224 PRO VAL ILE ASP ASP ALA TYR TYR ALA GLN LYS PHE GLN SEQRES 6 H 224 GLY ARG VAL THR ILE THR ALA ASP GLU SER THR SER THR SEQRES 7 H 224 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 H 224 ALA VAL TYR TYR CYS ALA ARG SER ARG GLY TYR TYR GLY SEQRES 9 H 224 SER PHE TYR PHE ASP ILE TRP GLY GLN GLY THR LEU VAL SEQRES 10 H 224 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 H 224 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 H 224 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 H 224 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 H 224 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 H 224 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 H 224 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 H 224 LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO SEQRES 18 H 224 LYS SER CYS SEQRES 1 L 214 GLU ILE VAL MET THR GLN SER PRO ALA THR LEU SER VAL SEQRES 2 L 214 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 L 214 GLN SER VAL SER SER ASN LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 214 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SER SEQRES 5 L 214 THR ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6 L 214 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 214 GLN SER GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN TYR SEQRES 8 L 214 ASN ASN TRP PRO TRP THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 L 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 214 PHE ASN ARG GLY GLU CYS SEQRES 1 A 264 ARG TRP ARG GLN GLN TRP SER GLY PRO GLY THR THR LYS SEQRES 2 A 264 ARG PHE PRO GLU THR VAL LEU ALA ARG CYS VAL LYS TYR SEQRES 3 A 264 THR GLU ILE HIS PRO GLU MET ARG HIS VAL ASP CYS GLN SEQRES 4 A 264 SER VAL TRP ASP ALA PHE LYS GLY ALA PHE ILE SER LYS SEQRES 5 A 264 HIS PRO CYS ASN ILE THR GLU GLU ASP TYR GLN PRO LEU SEQRES 6 A 264 MET LYS LEU GLY THR GLN THR VAL PRO CYS ASN LYS ILE SEQRES 7 A 264 LEU LEU TRP SER ARG ILE LYS ASP LEU ALA HIS GLN PHE SEQRES 8 A 264 THR GLN VAL GLN ARG ASP MET PHE THR LEU GLU ASP THR SEQRES 9 A 264 LEU LEU GLY TYR LEU ALA ASP ASP LEU THR TRP CYS GLY SEQRES 10 A 264 GLU PHE ASN THR SER LYS ILE ASN TYR GLN SER CYS PRO SEQRES 11 A 264 ASP TRP ARG LYS ASP CYS SER ASN ASN PRO VAL SER VAL SEQRES 12 A 264 PHE TRP LYS THR VAL SER ARG ARG PHE ALA GLU ALA ALA SEQRES 13 A 264 CYS ASP VAL VAL HIS VAL MET LEU ASN GLY SER ARG SER SEQRES 14 A 264 LYS ILE PHE ASP LYS ASN SER THR PHE GLY SER VAL GLU SEQRES 15 A 264 VAL HIS ASN LEU GLN PRO GLU LYS VAL GLN THR LEU GLU SEQRES 16 A 264 ALA TRP VAL ILE HIS GLY GLY ARG GLU ASP SER ARG ASP SEQRES 17 A 264 LEU CYS GLN ASP PRO THR ILE LYS GLU LEU GLU SER ILE SEQRES 18 A 264 ILE SER LYS ARG ASN ILE GLN PHE SER CYS LYS ASN ILE SEQRES 19 A 264 TYR ARG PRO ASP LYS PHE LEU GLN CYS VAL LYS ASN PRO SEQRES 20 A 264 GLU ASP SER SER CYS THR SER GLU ILE HIS HIS HIS HIS SEQRES 21 A 264 HIS HIS HIS HIS HET SO4 H 301 5 HET EDO H 302 4 HET EDO L 301 4 HET EDO L 302 4 HET NAG A 401 14 HET NAG A 402 14 HET NAG A 403 14 HET SO4 A 404 5 HET EDO A 405 4 HET EDO A 406 4 HET GOL A 407 6 HET EDO A 408 4 HET EDO A 409 4 HET ACT A 410 4 HET EDO A 411 4 HET EDO A 412 4 HET EPE A 413 15 HETNAM SO4 SULFATE ION HETNAM EDO 1,2-ETHANEDIOL HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM GOL GLYCEROL HETNAM ACT ACETATE ION HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID HETSYN EDO ETHYLENE GLYCOL HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL HETSYN EPE HEPES FORMUL 4 SO4 2(O4 S 2-) FORMUL 5 EDO 9(C2 H6 O2) FORMUL 8 NAG 3(C8 H15 N O6) FORMUL 14 GOL C3 H8 O3 FORMUL 17 ACT C2 H3 O2 1- FORMUL 20 EPE C8 H18 N2 O4 S FORMUL 21 HOH *696(H2 O) HELIX 1 AA1 PRO H 52A ASP H 55 5 4 HELIX 2 AA2 GLN H 61 GLN H 64 5 4 HELIX 3 AA3 GLU H 73 THR H 75 5 3 HELIX 4 AA4 ARG H 83 THR H 87 5 5 HELIX 5 AA5 SER H 156 ALA H 158 5 3 HELIX 6 AA6 SER H 187 LEU H 189 5 3 HELIX 7 AA7 LYS H 201 ASN H 204 5 4 HELIX 8 AA8 GLN L 79 PHE L 83 5 5 HELIX 9 AA9 SER L 121 LYS L 126 1 6 HELIX 10 AB1 LYS L 183 LYS L 188 1 6 HELIX 11 AB2 ARG A 58 HIS A 74 1 17 HELIX 12 AB3 PRO A 75 ARG A 78 5 4 HELIX 13 AB4 ASP A 81 ILE A 94 1 14 HELIX 14 AB5 THR A 102 ASP A 105 5 4 HELIX 15 AB6 TYR A 106 GLY A 113 1 8 HELIX 16 AB7 ILE A 128 GLN A 139 1 12 HELIX 17 AB8 THR A 144 ASP A 147 5 4 HELIX 18 AB9 THR A 148 ASP A 155 1 8 HELIX 19 AC1 ASN A 183 ALA A 200 1 18 HELIX 20 AC2 SER A 220 VAL A 225 1 6 HELIX 21 AC3 GLU A 226 LEU A 230 5 5 HELIX 22 AC4 ASP A 252 GLN A 255 5 4 HELIX 23 AC5 ASP A 256 LYS A 268 1 13 HELIX 24 AC6 ARG A 280 ASN A 290 1 11 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 77 LEU H 82 -1 O MET H 80 N VAL H 20 SHEET 4 AA1 4 VAL H 67 ASP H 72 -1 N ASP H 72 O THR H 77 SHEET 1 AA2 6 GLU H 10 LYS H 12 0 SHEET 2 AA2 6 THR H 107 VAL H 111 1 O THR H 110 N LYS H 12 SHEET 3 AA2 6 ALA H 88 ARG H 96 -1 N TYR H 90 O THR H 107 SHEET 4 AA2 6 TYR H 32 GLN H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 AA2 6 GLU H 46 ILE H 52 -1 O MET H 48 N TRP H 36 SHEET 6 AA2 6 ASP H 56 TYR H 59 -1 O ASP H 56 N ILE H 52 SHEET 1 AA3 4 GLU H 10 LYS H 12 0 SHEET 2 AA3 4 THR H 107 VAL H 111 1 O THR H 110 N LYS H 12 SHEET 3 AA3 4 ALA H 88 ARG H 96 -1 N TYR H 90 O THR H 107 SHEET 4 AA3 4 PHE H 100D TRP H 103 -1 O ILE H 102 N ARG H 94 SHEET 1 AA4 4 SER H 120 LEU H 124 0 SHEET 2 AA4 4 THR H 135 TYR H 145 -1 O GLY H 139 N LEU H 124 SHEET 3 AA4 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AA4 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AA5 4 THR H 131 SER H 132 0 SHEET 2 AA5 4 THR H 135 TYR H 145 -1 O THR H 135 N SER H 132 SHEET 3 AA5 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AA5 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AA6 3 THR H 151 TRP H 154 0 SHEET 2 AA6 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AA6 3 THR H 205 LYS H 210 -1 O VAL H 207 N VAL H 198 SHEET 1 AA7 4 MET L 4 SER L 7 0 SHEET 2 AA7 4 ALA L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA7 4 GLU L 70 ILE L 75 -1 O LEU L 73 N LEU L 21 SHEET 4 AA7 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AA8 6 THR L 10 VAL L 13 0 SHEET 2 AA8 6 THR L 102 ILE L 106 1 O LYS L 103 N LEU L 11 SHEET 3 AA8 6 ALA L 84 GLN L 90 -1 N ALA L 84 O VAL L 104 SHEET 4 AA8 6 LEU L 33 GLN L 38 -1 N GLN L 38 O VAL L 85 SHEET 5 AA8 6 ARG L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AA8 6 THR L 53 ARG L 54 -1 O THR L 53 N TYR L 49 SHEET 1 AA9 4 THR L 10 VAL L 13 0 SHEET 2 AA9 4 THR L 102 ILE L 106 1 O LYS L 103 N LEU L 11 SHEET 3 AA9 4 ALA L 84 GLN L 90 -1 N ALA L 84 O VAL L 104 SHEET 4 AA9 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AB1 4 SER L 114 PHE L 118 0 SHEET 2 AB1 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 AB1 4 TYR L 173 SER L 182 -1 O SER L 177 N CYS L 134 SHEET 4 AB1 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AB2 4 ALA L 153 LEU L 154 0 SHEET 2 AB2 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB2 4 VAL L 191 THR L 197 -1 O GLU L 195 N GLN L 147 SHEET 4 AB2 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SHEET 1 AB3 2 GLY A 52 PRO A 53 0 SHEET 2 AB3 2 SER A 172 CYS A 173 -1 O CYS A 173 N GLY A 52 SHEET 1 AB4 4 LEU A 123 SER A 126 0 SHEET 2 AB4 4 ASP A 202 ASN A 209 1 O HIS A 205 N LEU A 124 SHEET 3 AB4 4 VAL A 235 ILE A 243 1 O TRP A 241 N LEU A 208 SHEET 4 AB4 4 GLN A 272 ILE A 278 1 O ILE A 278 N VAL A 242 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.00 SSBOND 2 CYS H 140 CYS H 196 1555 1555 2.05 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.14 SSBOND 4 CYS L 134 CYS L 194 1555 1555 2.02 SSBOND 5 CYS A 67 CYS A 82 1555 1555 2.20 SSBOND 6 CYS A 99 CYS A 180 1555 1555 2.00 SSBOND 7 CYS A 119 CYS A 201 1555 1555 2.07 SSBOND 8 CYS A 160 CYS A 173 1555 1555 2.08 SSBOND 9 CYS A 254 CYS A 275 1555 1555 2.11 SSBOND 10 CYS A 287 CYS A 296 1555 1555 2.05 LINK ND2 ASN A 100 C1 NAG A 403 1555 1555 1.44 LINK ND2 ASN A 209 C1 NAG A 401 1555 1555 1.43 LINK ND2 ASN A 219 C1 NAG A 402 1555 1555 1.45 CISPEP 1 PHE H 146 PRO H 147 0 -7.61 CISPEP 2 GLU H 148 PRO H 149 0 -4.88 CISPEP 3 SER L 7 PRO L 8 0 -9.93 CISPEP 4 TRP L 94 PRO L 95 0 0.45 CISPEP 5 TYR L 140 PRO L 141 0 -0.66 CRYST1 166.045 166.045 78.769 90.00 90.00 90.00 P 43 21 2 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.006022 0.000000 0.000000 0.00000 SCALE2 0.000000 0.006022 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012695 0.00000