HEADER IMMUNE SYSTEM 08-JAN-24 8XS2 TITLE CRYSTAL STRUCTURE OF FAB FRAGMENT OF ANTI-OSTEOCALCIN C-TERMINAL TITLE 2 PEPTIDE ANTIBODY KTM219 WITH ADDITION OF FLUOROPHORE TAMRA COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEAVY CHAIN FRAGMENT (FD) OF ANTI-OSTEOCALCIN ANTIBODY COMPND 3 KTM219; COMPND 4 CHAIN: H; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: LIGHT CHAIN OF ANTI-OSTEOCALCIN ANTIBODY KTM219; COMPND 8 CHAIN: L; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 CELL_LINE: HYBRIDOMA KTM-219; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: SHUFFLE T7 EXPRESS LYSY; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-FAB(KTM219); SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 12 ORGANISM_TAXID: 10090; SOURCE 13 CELL_LINE: HYBRIDOMA KTM-219; SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 16 EXPRESSION_SYSTEM_STRAIN: SHUFFLE T7 EXPRESS LYSY; SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PET-FAB(KTM219) KEYWDS ANTIBODY, IMMUNOGLOBULIN FOLD, OSTEOCALCIN, QUENCHBODY (Q-BODY), OPEN KEYWDS 2 SANDWICH IMMUNOASSAY, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR S.YAZAKI,H.UEDA,R.ARAI REVDAT 1 15-JAN-25 8XS2 0 JRNL AUTH S.YAZAKI,M.KOMATSU,H.UEDA,R.ARAI JRNL TITL CRYSTAL STRUCTURE OF FAB FRAGMENT OF ANTI-OSTEOCALCIN JRNL TITL 2 C-TERMINAL PEPTIDE ANTIBODY KTM219 WITH ADDITION OF JRNL TITL 3 FLUOROPHORE TAMRA JRNL REF TO BE PUBLISHED JRNL REFN REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH R.ABE,H.J.JEONG,D.ARAKAWA,J.DONG,H.OHASHI,R.KAIGOME,F.SAIKI, REMARK 1 AUTH 2 K.YAMANE,H.TAKAGI,H.UEDA REMARK 1 TITL ULTRA Q-BODIES: QUENCH-BASED ANTIBODY PROBES THAT UTILIZE REMARK 1 TITL 2 DYE-DYE INTERACTIONS WITH ENHANCED ANTIGEN-DEPENDENT REMARK 1 TITL 3 FLUORESCENCE. REMARK 1 REF SCI REP V. 4 4640 2014 REMARK 1 REFN ESSN 2045-2322 REMARK 1 PMID 24721819 REMARK 1 DOI 10.1038/SREP04640 REMARK 1 REFERENCE 2 REMARK 1 AUTH J.DONG,H.UEDA REMARK 1 TITL RECENT ADVANCES IN QUENCHBODY, A FLUORESCENT IMMUNOSENSOR. REMARK 1 REF SENSORS (BASEL) V. 21 2021 REMARK 1 REFN ESSN 1424-8220 REMARK 1 PMID 33572319 REMARK 1 DOI 10.1016/J.CPLETT.2018.03.011 REMARK 2 REMARK 2 RESOLUTION. 2.14 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0135 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) : 2.14 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0 REMARK 3 NUMBER OF REFLECTIONS : 23209 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) : 0.204 REMARK 3 R VALUE (WORKING SET) : 0.202 REMARK 3 FREE R VALUE : 0.244 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900 REMARK 3 FREE R VALUE TEST SET COUNT : 1193 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) : 2.14 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.20 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1265 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 72.37 REMARK 3 BIN R VALUE (WORKING SET) : 0.2760 REMARK 3 BIN FREE R VALUE SET COUNT : 63 REMARK 3 BIN FREE R VALUE : 0.3290 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3237 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 8 REMARK 3 SOLVENT ATOMS : 257 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 27.60 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.03 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.40000 REMARK 3 B22 (A**2) : -0.24000 REMARK 3 B33 (A**2) : 0.64000 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): 0.275 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.209 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.150 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.033 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.945 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.919 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3327 ; 0.010 ; 0.019 REMARK 3 BOND LENGTHS OTHERS (A): 3039 ; 0.006 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4523 ; 1.456 ; 1.947 REMARK 3 BOND ANGLES OTHERS (DEGREES): 7054 ; 0.903 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 427 ; 7.019 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 126 ;36.081 ;25.079 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 531 ;14.215 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 6 ;21.643 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 513 ; 0.076 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3757 ; 0.005 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): 731 ; 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): 1712 ; 1.640 ; 2.934 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1709 ; 1.637 ; 2.930 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2134 ; 2.711 ; 4.383 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2135 ; 2.711 ; 4.385 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1614 ; 1.729 ; 3.034 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1615 ; 1.728 ; 3.035 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2389 ; 2.879 ; 4.471 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3685 ; 5.151 ;23.477 REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3685 ; 5.157 ;23.479 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 8XS2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-JAN-24. REMARK 100 THE DEPOSITION ID IS D_1300044014. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 23-FEB-19 REMARK 200 TEMPERATURE (KELVIN) : 95 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : PHOTON FACTORY REMARK 200 BEAMLINE : BL-5A REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.000 REMARK 200 MONOCHROMATOR : NUMERICAL LINK TYPE SI(111) REMARK 200 DOUBLE CRYSTAL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24972 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.140 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 200 DATA REDUNDANCY : 12.60 REMARK 200 R MERGE (I) : 0.11500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.14 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1 REMARK 200 DATA REDUNDANCY IN SHELL : 11.80 REMARK 200 R MERGE FOR SHELL (I) : 1.01500 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.470 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: 5X5X REMARK 200 REMARK 200 REMARK: PLATE-LIKE CRYSTAL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 43.07 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, 0.3 M AMMONIUM ACETATE, REMARK 280 25% PEG 3350, 0.6 MM TAMRA, PH 7.5, VAPOR DIFFUSION, HANGING REMARK 280 DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 21 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,-Z+1/2 REMARK 290 4555 -X+1/2,-Y,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 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 33.09250 REMARK 290 SMTRY2 3 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 48.32650 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 33.09250 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 48.32650 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3190 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19650 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L 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 MET H -3 REMARK 465 ALA H -2 REMARK 465 THR H -1 REMARK 465 GLY H 0 REMARK 465 SER H 128 REMARK 465 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 LYS H 214 REMARK 465 SER H 215 REMARK 465 ALA H 216 REMARK 465 SER H 217 REMARK 465 ALA H 218 REMARK 465 ALA H 219 REMARK 465 HIS H 220 REMARK 465 HIS H 221 REMARK 465 HIS H 222 REMARK 465 HIS H 223 REMARK 465 HIS H 224 REMARK 465 HIS H 225 REMARK 465 GLY H 226 REMARK 465 ALA H 227 REMARK 465 ALA H 228 REMARK 465 GLU H 229 REMARK 465 GLN H 230 REMARK 465 LYS H 231 REMARK 465 LEU H 232 REMARK 465 ILE H 233 REMARK 465 SER H 234 REMARK 465 GLU H 235 REMARK 465 GLU H 236 REMARK 465 ASP H 237 REMARK 465 LEU H 238 REMARK 465 ASN H 239 REMARK 465 GLY H 240 REMARK 465 ALA H 241 REMARK 465 ALA H 242 REMARK 465 MET L -1 REMARK 465 GLY L 212 REMARK 465 GLU L 213 REMARK 465 GLY L 214 REMARK 465 GLY L 215 REMARK 465 GLY L 216 REMARK 465 SER L 217 REMARK 465 ASP L 218 REMARK 465 TYR L 219 REMARK 465 LYS L 220 REMARK 465 ASP L 221 REMARK 465 ASP L 222 REMARK 465 ASP L 223 REMARK 465 ASP L 224 REMARK 465 LYS L 225 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 CYS H 22 CA - CB - SG ANGL. DEV. = 9.0 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 ALA H 114 144.13 -37.65 REMARK 500 THR H 160 -32.17 -132.46 REMARK 500 THR L 50 63.70 33.74 REMARK 500 LEU L 51 -64.04 84.29 REMARK 500 ASN L 138 71.50 47.87 REMARK 500 ASN L 152 -1.10 69.45 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5X5X RELATED DB: PDB REMARK 900 THE SAME ANTIBODY FAB FRAGMENT WITHOUT ADDITION OF FLUOROPHORE REMARK 900 RELATED ID: 8XS1 RELATED DB: PDB REMARK 900 THE SAME ANTIBODY FAB COMPLEXED WITH OSTEOCALCIN C-TERMINAL PEPTIDE REMARK 900 ANTIGEN DBREF 8XS2 H -3 242 PDB 8XS2 8XS2 -3 242 DBREF 8XS2 L -1 225 PDB 8XS2 8XS2 -1 225 SEQRES 1 H 249 MET ALA THR GLY GLN VAL LYS LEU GLN GLN SER GLY ALA SEQRES 2 H 249 GLU PHE VAL LYS ALA GLY ALA SER VAL LYS LEU SER CYS SEQRES 3 H 249 LYS THR SER GLY TYR THR PHE ASN ASN TYR TRP ILE HIS SEQRES 4 H 249 TRP VAL LYS GLN SER PRO GLY GLN GLY LEU GLU TRP ILE SEQRES 5 H 249 GLY GLU ILE ASP PRO SER ASP GLY TYR SER ASN TYR ASN SEQRES 6 H 249 GLN LYS PHE LYS GLY LYS ALA THR LEU THR VAL ASP LYS SEQRES 7 H 249 SER SER SER THR ALA TYR MET HIS LEU ASN SER LEU THR SEQRES 8 H 249 SER GLU ASP SER ALA VAL TYR TYR CYS THR SER SER THR SEQRES 9 H 249 SER VAL GLY GLY SER TRP GLY GLN GLY THR THR VAL THR SEQRES 10 H 249 VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO SEQRES 11 H 249 LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA SEQRES 12 H 249 ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO SEQRES 13 H 249 VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY SEQRES 14 H 249 VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU SEQRES 15 H 249 TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER SEQRES 16 H 249 LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS SEQRES 17 H 249 PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SEQRES 18 H 249 SER ALA SER ALA ALA HIS HIS HIS HIS HIS HIS GLY ALA SEQRES 19 H 249 ALA GLU GLN LYS LEU ILE SER GLU GLU ASP LEU ASN GLY SEQRES 20 H 249 ALA ALA SEQRES 1 L 232 MET SER ASP ILE GLU LEU THR GLN SER PRO LEU SER LEU SEQRES 2 L 232 PRO VAL SER LEU GLY ASP GLN ALA SER ILE SER CYS THR SEQRES 3 L 232 SER SER GLN SER LEU LEU HIS SER ASN GLY ASP THR TYR SEQRES 4 L 232 LEU HIS TRP TYR LEU GLN LYS PRO GLY GLN SER PRO LYS SEQRES 5 L 232 LEU LEU ILE TYR THR LEU SER ASN ARG PHE SER GLY VAL SEQRES 6 L 232 PRO ASP ARG PHE SER GLY SER GLY SER GLY THR ASP PHE SEQRES 7 L 232 THR LEU LYS ILE SER ARG VAL GLU ALA ALA ASP LEU GLY SEQRES 8 L 232 ILE TYR PHE CYS SER GLN THR THR HIS VAL PRO TYR THR SEQRES 9 L 232 PHE GLY GLY GLY THR LYS LEU GLU ILE LYS ARG ALA ASP SEQRES 10 L 232 ALA ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU SEQRES 11 L 232 GLN LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU SEQRES 12 L 232 ASN ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS SEQRES 13 L 232 VAL ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER SEQRES 14 L 232 VAL THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SEQRES 15 L 232 SER SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS SEQRES 16 L 232 HIS LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SEQRES 17 L 232 SER SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU GLY SEQRES 18 L 232 GLY GLY SER ASP TYR LYS ASP ASP ASP ASP LYS HET ACT H 301 4 HET ACT L 301 4 HETNAM ACT ACETATE ION FORMUL 3 ACT 2(C2 H3 O2 1-) FORMUL 5 HOH *257(H2 O) HELIX 1 AA1 THR H 28 TYR H 32 5 5 HELIX 2 AA2 THR H 83 SER H 87 5 5 HELIX 3 AA3 SER H 95 GLY H 99 5 5 HELIX 4 AA4 SER H 187 LEU H 189 5 3 HELIX 5 AA5 GLU L 79 LEU L 83 5 5 HELIX 6 AA6 SER L 121 SER L 127 1 7 HELIX 7 AA7 LYS L 183 GLU L 187 1 5 SHEET 1 AA1 4 LYS H 3 GLN H 6 0 SHEET 2 AA1 4 VAL H 18 SER H 25 -1 O LYS H 23 N GLN H 5 SHEET 3 AA1 4 THR H 77 LEU H 82 -1 O MET H 80 N LEU H 20 SHEET 4 AA1 4 ALA H 67 ASP H 72 -1 N THR H 70 O TYR H 79 SHEET 1 AA2 6 GLU H 10 VAL H 12 0 SHEET 2 AA2 6 THR H 107 VAL H 111 1 O THR H 110 N GLU H 10 SHEET 3 AA2 6 ALA H 88 THR H 93 -1 N ALA H 88 O VAL H 109 SHEET 4 AA2 6 ILE H 34 SER H 40 -1 N VAL H 37 O TYR H 91 SHEET 5 AA2 6 GLY H 44 ILE H 51 -1 O GLU H 46 N LYS H 38 SHEET 6 AA2 6 SER H 57 TYR H 59 -1 O ASN H 58 N GLU H 50 SHEET 1 AA3 4 SER H 120 LEU H 124 0 SHEET 2 AA3 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AA3 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AA3 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AA4 4 SER H 120 LEU H 124 0 SHEET 2 AA4 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 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 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AA5 3 THR H 151 TRP H 154 0 SHEET 2 AA5 3 TYR H 194 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AA5 3 THR H 205 VAL H 211 -1 O VAL H 207 N VAL H 198 SHEET 1 AA6 4 LEU L 4 SER L 7 0 SHEET 2 AA6 4 ALA L 19 SER L 25 -1 O THR L 24 N THR L 5 SHEET 3 AA6 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AA6 4 PHE L 62 SER L 67 -1 N SER L 63 O LYS L 74 SHEET 1 AA7 6 SER L 10 VAL L 13 0 SHEET 2 AA7 6 THR L 102 ILE L 106 1 O LYS L 103 N LEU L 11 SHEET 3 AA7 6 GLY L 84 GLN L 90 -1 N GLY L 84 O LEU L 104 SHEET 4 AA7 6 LEU L 33 GLN L 38 -1 N TYR L 36 O PHE L 87 SHEET 5 AA7 6 LYS L 45 TYR L 49 -1 O ILE L 48 N TRP L 35 SHEET 6 AA7 6 ASN L 53 ARG L 54 -1 O ASN L 53 N TYR L 49 SHEET 1 AA8 4 SER L 10 VAL L 13 0 SHEET 2 AA8 4 THR L 102 ILE L 106 1 O LYS L 103 N LEU L 11 SHEET 3 AA8 4 GLY L 84 GLN L 90 -1 N GLY L 84 O LEU L 104 SHEET 4 AA8 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AA9 4 SER L 114 PHE L 118 0 SHEET 2 AA9 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 AA9 4 TYR L 173 SER L 182 -1 O LEU L 179 N VAL L 132 SHEET 4 AA9 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AB1 4 ALA L 153 LEU L 154 0 SHEET 2 AB1 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB1 4 VAL L 191 THR L 197 -1 O GLU L 195 N GLN L 147 SHEET 4 AB1 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.14 SSBOND 2 CYS H 140 CYS H 196 1555 1555 2.03 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.07 SSBOND 4 CYS L 134 CYS L 194 1555 1555 2.05 CISPEP 1 PHE H 146 PRO H 147 0 -8.15 CISPEP 2 GLU H 148 PRO H 149 0 -5.79 CISPEP 3 SER L 7 PRO L 8 0 -6.25 CISPEP 4 VAL L 94 PRO L 95 0 2.19 CISPEP 5 TYR L 140 PRO L 141 0 3.06 CRYST1 66.185 69.520 96.653 90.00 90.00 90.00 P 21 2 21 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 0.015109 0.000000 0.000000 0.00000 SCALE2 0.000000 0.014384 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010346 0.00000