HEADER IMMUNE SYSTEM 17-JUL-23 8PUK TITLE CHILOB 7/4 H2 HC-T219C/C224S KAPPA LC-E123C/C214S F(AB')2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: CHILOB 7/4 H2 HEAVY CHAIN T219C/C224S; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: CHILOB 7/4 H2 KAPPA CHAIN E123C/C214S; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 10029 KEYWDS ANTIBODY, IGG2, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR I.G.ELLIOTT,H.FISHER,I.TEWS REVDAT 1 05-MAR-25 8PUK 0 JRNL AUTH I.ELLIOTT,H.FISHER,I.TEWS,J.W.ESSEX,M.S.C.CRAGG JRNL TITL BIOLOGICAL ACTIVITY OF HINGE-RESTRICTED ANTIBODIES. JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.67 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0405 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) : 2.67 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 74.19 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5 REMARK 3 NUMBER OF REFLECTIONS : 16177 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) : 0.242 REMARK 3 FREE R VALUE : 0.283 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.933 REMARK 3 FREE R VALUE TEST SET COUNT : 798 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) : 2.67 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.74 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1083 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.83 REMARK 3 BIN R VALUE (WORKING SET) : 0.4740 REMARK 3 BIN FREE R VALUE SET COUNT : 36 REMARK 3 BIN FREE R VALUE : 0.4650 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3284 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 5 REMARK 3 SOLVENT ATOMS : 46 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 74.39 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 2.78700 REMARK 3 B22 (A**2) : 2.78700 REMARK 3 B33 (A**2) : -9.04000 REMARK 3 B12 (A**2) : 1.39300 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): 0.845 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.359 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.391 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 42.518 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.930 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.890 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3365 ; 0.005 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): 3052 ; 0.001 ; 0.016 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4573 ; 1.167 ; 1.651 REMARK 3 BOND ANGLES OTHERS (DEGREES): 7083 ; 0.391 ; 1.567 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 424 ; 8.475 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 9 ; 7.159 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 549 ;14.849 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 520 ; 0.051 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3840 ; 0.005 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 732 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 652 ; 0.202 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 89 ; 0.183 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1595 ; 0.180 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 89 ; 0.155 ; 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): 1711 ; 1.260 ; 3.559 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1710 ; 1.259 ; 3.559 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2130 ; 2.185 ; 6.391 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2131 ; 2.185 ; 6.391 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1654 ; 1.388 ; 3.743 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1651 ; 1.356 ; 3.720 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2443 ; 2.161 ; 6.756 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2438 ; 2.115 ; 6.715 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 : 4 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 1 A 122 REMARK 3 ORIGIN FOR THE GROUP (A): 0.0000 0.0000 0.0000 REMARK 3 T TENSOR REMARK 3 T11: 0.7039 T22: 0.2011 REMARK 3 T33: 1.0990 T12: -0.2006 REMARK 3 T13: 0.1319 T23: 0.1628 REMARK 3 L TENSOR REMARK 3 L11: 0.5504 L22: 4.3724 REMARK 3 L33: 1.0398 L12: -1.3557 REMARK 3 L13: -0.6903 L23: 2.0631 REMARK 3 S TENSOR REMARK 3 S11: -0.3347 S12: -0.0595 S13: -0.0688 REMARK 3 S21: 1.2400 S22: 0.0419 S23: 1.0604 REMARK 3 S31: 0.6162 S32: -0.0434 S33: 0.2929 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 123 A 227 REMARK 3 ORIGIN FOR THE GROUP (A): 0.0000 0.0000 0.0000 REMARK 3 T TENSOR REMARK 3 T11: 0.5055 T22: 0.1801 REMARK 3 T33: 1.8480 T12: -0.0867 REMARK 3 T13: -0.4804 T23: 0.0716 REMARK 3 L TENSOR REMARK 3 L11: 0.2718 L22: 5.7555 REMARK 3 L33: 0.9555 L12: -1.0260 REMARK 3 L13: 0.2229 L23: -0.8255 REMARK 3 S TENSOR REMARK 3 S11: 0.2555 S12: -0.0624 S13: -0.3538 REMARK 3 S21: -1.0041 S22: 0.2000 S23: 2.9258 REMARK 3 S31: 0.6406 S32: -0.2091 S33: -0.4554 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 0 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 ORIGIN FOR THE GROUP (A): 0.0000 0.0000 0.0000 REMARK 3 T TENSOR REMARK 3 T11: 0.1110 T22: 0.1469 REMARK 3 T33: 0.2443 T12: -0.0102 REMARK 3 T13: -0.0054 T23: 0.0021 REMARK 3 L TENSOR REMARK 3 L11: 0.4567 L22: 4.5445 REMARK 3 L33: 0.2248 L12: -1.3332 REMARK 3 L13: -0.2909 L23: 0.9882 REMARK 3 S TENSOR REMARK 3 S11: 0.0450 S12: 0.0775 S13: -0.0865 REMARK 3 S21: -0.0562 S22: -0.1609 S23: 0.6151 REMARK 3 S31: 0.0118 S32: -0.0299 S33: 0.1159 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 0 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 ORIGIN FOR THE GROUP (A): 0.0000 0.0000 0.0000 REMARK 3 T TENSOR REMARK 3 T11: 0.2638 T22: 0.0564 REMARK 3 T33: 0.3316 T12: -0.1192 REMARK 3 T13: 0.0568 T23: -0.0010 REMARK 3 L TENSOR REMARK 3 L11: 0.2818 L22: 3.2117 REMARK 3 L33: 0.2571 L12: 0.7666 REMARK 3 L13: 0.2274 L23: 0.8803 REMARK 3 S TENSOR REMARK 3 S11: 0.1575 S12: -0.0502 S13: 0.1984 REMARK 3 S21: 0.5336 S22: -0.2067 S23: 0.0757 REMARK 3 S31: 0.1977 S32: -0.0804 S33: 0.0493 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 : 1.30 REMARK 3 ION PROBE RADIUS : 1.00 REMARK 3 SHRINKAGE RADIUS : 1.00 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THEIR REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 8PUK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-JUL-23. REMARK 100 THE DEPOSITION ID IS D_1292131024. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 13-APR-22; 25-APR-22 REMARK 200 TEMPERATURE (KELVIN) : 100; 45 REMARK 200 PH : 8; 8 REMARK 200 NUMBER OF CRYSTALS USED : 2 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y; Y REMARK 200 RADIATION SOURCE : ESRF; DIAMOND REMARK 200 BEAMLINE : MASSIF-3; I23 REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9677; 2.75 REMARK 200 MONOCHROMATOR : SI(111); SI CRYSTAL REMARK 200 OPTICS : NULL; NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL; PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 4M; DECTRIS REMARK 200 PILATUS 12M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS, XIA2 REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16178 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.670 REMARK 200 RESOLUTION RANGE LOW (A) : 74.193 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8 REMARK 200 DATA REDUNDANCY : 7.100 REMARK 200 R MERGE (I) : 0.12900 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.67 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.1 REMARK 200 DATA REDUNDANCY IN SHELL : 13.10 REMARK 200 R MERGE FOR SHELL (I) : 1.72500 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.900 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; 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: NEEDLE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 58.42 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.96 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS, 15% PEG 4000, 0.2M REMARK 280 (NH4)2SO4, PH 8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE REMARK 280 294.15K. 0.1M TRIS, 25% PEG 4000, 15% GLYCEROL, PH 8, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 294.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z REMARK 290 3555 -X+Y,-X,Z REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z REMARK 290 6555 -X,-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 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 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: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 10100 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 37200 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -93.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 350 BIOMT1 2 -0.500000 0.866025 0.000000 0.00000 REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000 REMARK 350 BIOMT3 2 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 GLY A 103 REMARK 465 ARG A 104 REMARK 465 ASN A 105 REMARK 465 ARG A 138 REMARK 465 SER A 139 REMARK 465 THR A 140 REMARK 465 SER A 141 REMARK 465 SER A 196 REMARK 465 ASN A 197 REMARK 465 PHE A 198 REMARK 465 CYS A 228 REMARK 465 PRO A 229 REMARK 465 PRO A 230 REMARK 465 CYS A 231 REMARK 465 GLU B 213 REMARK 465 SER B 214 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 O ASP B 82 HH TYR B 86 1.47 REMARK 500 O LEU A 147 H VAL A 191 1.54 REMARK 500 HD1 HIS A 209 OG SER A 212 1.56 REMARK 500 O SER A 40 H LYS A 43 1.58 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 HG SER B 9 H SER B 202 3565 1.08 REMARK 500 HG1 THR B 8 H ALA B 112 3565 1.11 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 PRO A 9 174.54 -51.17 REMARK 500 PRO A 14 90.42 -65.95 REMARK 500 ALA A 16 -155.68 -77.74 REMARK 500 PHE A 29 -65.87 71.06 REMARK 500 LYS A 43 23.76 82.71 REMARK 500 MET A 81 118.36 -163.58 REMARK 500 SER A 85 76.27 9.82 REMARK 500 ALA A 108 169.36 174.61 REMARK 500 ALA A 123 128.83 -29.33 REMARK 500 CYS A 136 -71.29 -108.30 REMARK 500 ASP A 153 70.82 45.67 REMARK 500 PRO A 156 -156.19 -81.66 REMARK 500 PRO A 211 -4.74 -57.10 REMARK 500 ASN A 213 58.13 39.88 REMARK 500 ASN B 31 15.36 53.94 REMARK 500 THR B 51 -52.28 79.91 REMARK 500 SER B 67 170.03 177.40 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 PRO A 156 GLU A 157 -149.50 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 6TKB RELATED DB: PDB REMARK 900 SAME ANTIBODY F(AB')2 WITH DIFFERENT MUTATIONS REMARK 900 RELATED ID: 6TKC RELATED DB: PDB REMARK 900 SAME ANTIBODY F(AB')2 WITH DIFFERENT MUTATIONS REMARK 900 RELATED ID: 6TKD RELATED DB: PDB REMARK 900 SAME ANTIBODY F(AB')2 WITH DIFFERENT MUTATIONS REMARK 900 RELATED ID: 6TKE RELATED DB: PDB REMARK 900 SAME ANTIBODY F(AB')2 WITH DIFFERENT MUTATIONS REMARK 900 RELATED ID: 6TKF RELATED DB: PDB REMARK 900 SAME ANTIBODY F(AB')2 WITH DIFFERENT MUTATIONS REMARK 900 RELATED ID: 6FAX RELATED DB: PDB REMARK 900 WILDTYPE ANTIBODY F(AB') BOUND TO CD40 RECEPTOR REMARK 900 RELATED ID: SASDSC7 RELATED DB: SASBDB REMARK 900 SEC-SAXS DATA FOR SAME ANTIBODY F(AB')2 IN SOLUTION DBREF 8PUK A 1 231 PDB 8PUK 8PUK 1 231 DBREF 8PUK B 1 214 PDB 8PUK 8PUK 1 214 SEQRES 1 A 231 GLU VAL GLN LEU GLN GLN SER GLY PRO ASP LEU VAL LYS SEQRES 2 A 231 PRO GLY ALA SER VAL LYS ILE SER CYS LYS THR SER GLY SEQRES 3 A 231 TYR THR PHE THR GLU TYR ILE MET HIS TRP VAL LYS GLN SEQRES 4 A 231 SER HIS GLY LYS SER LEU GLU TRP ILE GLY GLY ILE ILE SEQRES 5 A 231 PRO ASN ASN GLY GLY THR SER TYR ASN GLN LYS PHE LYS SEQRES 6 A 231 ASP LYS ALA THR MET THR VAL ASP LYS SER SER SER THR SEQRES 7 A 231 GLY TYR MET GLU LEU ARG SER LEU THR SER GLU ASP SER SEQRES 8 A 231 ALA VAL TYR TYR CYS THR ARG ARG GLU VAL TYR GLY ARG SEQRES 9 A 231 ASN TYR TYR ALA LEU ASP TYR TRP GLY GLN GLY THR LEU SEQRES 10 A 231 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 A 231 PHE PRO LEU ALA PRO CYS SER ARG SER THR SER GLU SER SEQRES 12 A 231 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 A 231 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 A 231 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 A 231 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 A 231 SER ASN PHE GLY THR GLN THR TYR THR CYS ASN VAL ASP SEQRES 17 A 231 HIS LYS PRO SER ASN THR LYS VAL ASP LYS CYS VAL GLU SEQRES 18 A 231 ARG LYS SER CYS VAL GLU CYS PRO PRO CYS SEQRES 1 B 214 ASP ILE GLN MET THR GLN THR THR SER SER LEU SER ALA SEQRES 2 B 214 SER LEU GLY ASP ARG VAL THR ILE THR CYS SER ALA SER SEQRES 3 B 214 GLN GLY ILE ASN ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 B 214 PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SER SEQRES 5 B 214 SER LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 B 214 GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN LEU SEQRES 7 B 214 GLU PRO GLU ASP ILE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 B 214 SER ASN LEU PRO TYR THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 B 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 B 214 PHE PRO PRO SER ASP CYS GLN LEU LYS SER GLY THR ALA SEQRES 11 B 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 B 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 B 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 B 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 B 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 B 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 B 214 PHE ASN ARG GLY GLU SER HET SO4 A 301 5 HETNAM SO4 SULFATE ION FORMUL 3 SO4 O4 S 2- FORMUL 4 HOH *46(H2 O) HELIX 1 AA1 THR A 87 SER A 91 5 5 HELIX 2 AA2 SER A 165 ALA A 167 5 3 HELIX 3 AA3 LYS A 210 ASN A 213 5 4 HELIX 4 AA4 GLU B 79 ILE B 83 5 5 HELIX 5 AA5 SER B 121 LYS B 126 1 6 HELIX 6 AA6 LYS B 183 GLU B 187 1 5 SHEET 1 AA1 4 GLN A 3 GLN A 6 0 SHEET 2 AA1 4 VAL A 18 SER A 25 -1 O LYS A 23 N GLN A 5 SHEET 3 AA1 4 THR A 78 LEU A 83 -1 O LEU A 83 N VAL A 18 SHEET 4 AA1 4 MET A 70 ASP A 73 -1 N THR A 71 O TYR A 80 SHEET 1 AA2 6 ASP A 10 VAL A 12 0 SHEET 2 AA2 6 LEU A 117 VAL A 120 1 O THR A 119 N ASP A 10 SHEET 3 AA2 6 ALA A 92 GLU A 100 -1 N ALA A 92 O VAL A 118 SHEET 4 AA2 6 ILE A 33 GLN A 39 -1 N HIS A 35 O THR A 97 SHEET 5 AA2 6 LEU A 45 ILE A 51 -1 O GLU A 46 N LYS A 38 SHEET 6 AA2 6 THR A 58 TYR A 60 -1 O SER A 59 N GLY A 50 SHEET 1 AA3 4 ASP A 10 VAL A 12 0 SHEET 2 AA3 4 LEU A 117 VAL A 120 1 O THR A 119 N ASP A 10 SHEET 3 AA3 4 ALA A 92 GLU A 100 -1 N ALA A 92 O VAL A 118 SHEET 4 AA3 4 ALA A 108 TRP A 112 -1 O TYR A 111 N ARG A 98 SHEET 1 AA4 4 SER A 129 LEU A 133 0 SHEET 2 AA4 4 ALA A 145 TYR A 154 -1 O LEU A 150 N PHE A 131 SHEET 3 AA4 4 TYR A 185 VAL A 193 -1 O VAL A 191 N LEU A 147 SHEET 4 AA4 4 VAL A 172 THR A 174 -1 N HIS A 173 O VAL A 190 SHEET 1 AA5 3 THR A 160 TRP A 163 0 SHEET 2 AA5 3 THR A 204 HIS A 209 -1 O ASP A 208 N THR A 160 SHEET 3 AA5 3 THR A 214 CYS A 219 -1 O THR A 214 N HIS A 209 SHEET 1 AA6 4 MET B 4 THR B 5 0 SHEET 2 AA6 4 VAL B 19 ALA B 25 -1 O SER B 24 N THR B 5 SHEET 3 AA6 4 ASP B 70 ILE B 75 -1 O LEU B 73 N ILE B 21 SHEET 4 AA6 4 PHE B 62 SER B 67 -1 N SER B 65 O SER B 72 SHEET 1 AA7 6 SER B 10 SER B 14 0 SHEET 2 AA7 6 THR B 102 LYS B 107 1 O LYS B 107 N ALA B 13 SHEET 3 AA7 6 ALA B 84 GLN B 90 -1 N ALA B 84 O LEU B 104 SHEET 4 AA7 6 LEU B 33 GLN B 38 -1 N TYR B 36 O TYR B 87 SHEET 5 AA7 6 VAL B 44 TYR B 49 -1 O ILE B 48 N TRP B 35 SHEET 6 AA7 6 SER B 53 LEU B 54 -1 O SER B 53 N TYR B 49 SHEET 1 AA8 4 SER B 10 SER B 14 0 SHEET 2 AA8 4 THR B 102 LYS B 107 1 O LYS B 107 N ALA B 13 SHEET 3 AA8 4 ALA B 84 GLN B 90 -1 N ALA B 84 O LEU B 104 SHEET 4 AA8 4 THR B 97 PHE B 98 -1 O THR B 97 N GLN B 90 SHEET 1 AA9 4 SER B 114 PHE B 118 0 SHEET 2 AA9 4 THR B 129 PHE B 139 -1 O VAL B 133 N PHE B 118 SHEET 3 AA9 4 TYR B 173 SER B 182 -1 O LEU B 181 N ALA B 130 SHEET 4 AA9 4 SER B 159 VAL B 163 -1 N SER B 162 O SER B 176 SHEET 1 AB1 4 ALA B 153 LEU B 154 0 SHEET 2 AB1 4 LYS B 145 VAL B 150 -1 N VAL B 150 O ALA B 153 SHEET 3 AB1 4 VAL B 191 THR B 197 -1 O THR B 197 N LYS B 145 SHEET 4 AB1 4 VAL B 205 ASN B 210 -1 O VAL B 205 N VAL B 196 SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.07 SSBOND 2 CYS A 136 CYS A 225 1555 4555 2.08 SSBOND 3 CYS A 149 CYS A 205 1555 1555 2.03 SSBOND 4 CYS A 219 CYS B 123 1555 4555 2.11 SSBOND 5 CYS B 23 CYS B 88 1555 1555 2.07 SSBOND 6 CYS B 134 CYS B 194 1555 1555 2.01 CISPEP 1 PHE A 155 PRO A 156 0 -5.45 CISPEP 2 LEU B 94 PRO B 95 0 -6.02 CISPEP 3 TYR B 140 PRO B 141 0 1.13 CRYST1 148.167 148.167 45.295 90.00 90.00 120.00 P 3 2 1 6 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.006749 0.003897 0.000000 0.00000 SCALE2 0.000000 0.007793 0.000000 0.00000 SCALE3 0.000000 0.000000 0.022077 0.00000