HEADER IMMUNE SYSTEM 17-JUL-23 8PUL TITLE CHILOB 7/4 H2 HC-K223C/C224S KAPPA LC-C214S F(AB')2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: CHILOB 7/4 H2 HEAVY CHAIN K223C/C224S; COMPND 3 CHAIN: A, C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: CHILOB 7/4 H2 KAPPA CHAIN C214S; COMPND 7 CHAIN: B, D; 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.ELLIOTT,H.FISHER,I.TEWS REVDAT 1 05-MAR-25 8PUL 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. 1.93 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) : 1.93 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 81.18 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 85.6 REMARK 3 NUMBER OF REFLECTIONS : 71045 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) : 0.203 REMARK 3 FREE R VALUE : 0.239 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.962 REMARK 3 FREE R VALUE TEST SET COUNT : 3525 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) : 1.93 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.98 REMARK 3 REFLECTION IN BIN (WORKING SET) : 4226 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 73.58 REMARK 3 BIN R VALUE (WORKING SET) : 0.3740 REMARK 3 BIN FREE R VALUE SET COUNT : 222 REMARK 3 BIN FREE R VALUE : 0.3750 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6632 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 18 REMARK 3 SOLVENT ATOMS : 322 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 61.60 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -1.04200 REMARK 3 B22 (A**2) : 2.55100 REMARK 3 B33 (A**2) : -1.50900 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): 0.177 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.159 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.170 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.618 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966 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): 6846 ; 0.003 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): 6204 ; 0.001 ; 0.016 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9317 ; 0.794 ; 1.651 REMARK 3 BOND ANGLES OTHERS (DEGREES): 14407 ; 0.298 ; 1.567 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 874 ; 7.333 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 21 ; 4.997 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1121 ;10.896 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1057 ; 0.039 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7882 ; 0.003 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1506 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 955 ; 0.171 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 16 ; 0.216 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3217 ; 0.169 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 292 ; 0.126 ; 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): 3475 ; 2.928 ; 3.869 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3475 ; 2.926 ; 3.869 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4335 ; 4.489 ; 6.938 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4336 ; 4.491 ; 6.940 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3371 ; 3.569 ; 4.187 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3372 ; 3.569 ; 4.188 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4975 ; 5.440 ; 7.550 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4976 ; 5.439 ; 7.551 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 : 2 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 A 1 A 225 NULL REMARK 3 1 A 1 A 225 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 2 A 232 A 444 NULL REMARK 3 2 A 232 A 444 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 8 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: 0.2649 T22: 0.2354 REMARK 3 T33: 0.8429 T12: 0.1118 REMARK 3 T13: -0.1126 T23: -0.4115 REMARK 3 L TENSOR REMARK 3 L11: 4.7352 L22: 1.4407 REMARK 3 L33: 2.4015 L12: 1.2328 REMARK 3 L13: 1.2711 L23: 0.4705 REMARK 3 S TENSOR REMARK 3 S11: 0.2981 S12: 1.0285 S13: -1.9009 REMARK 3 S21: -0.0662 S22: 0.2798 S23: -0.5517 REMARK 3 S31: 0.7357 S32: 0.4177 S33: -0.5778 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 228 REMARK 3 ORIGIN FOR THE GROUP (A): 0.0000 0.0000 0.0000 REMARK 3 T TENSOR REMARK 3 T11: 0.1873 T22: 0.2388 REMARK 3 T33: 0.1576 T12: 0.0391 REMARK 3 T13: 0.1428 T23: 0.0178 REMARK 3 L TENSOR REMARK 3 L11: 3.0574 L22: 4.4486 REMARK 3 L33: 2.1645 L12: -1.3833 REMARK 3 L13: 0.5885 L23: -1.4872 REMARK 3 S TENSOR REMARK 3 S11: 0.2000 S12: 0.5293 S13: 0.2468 REMARK 3 S21: -0.8314 S22: -0.3539 S23: -0.7178 REMARK 3 S31: 0.4182 S32: 0.4148 S33: 0.1540 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: 0.5013 T22: 0.2381 REMARK 3 T33: 1.1117 T12: -0.3251 REMARK 3 T13: 0.0827 T23: -0.1497 REMARK 3 L TENSOR REMARK 3 L11: 3.8244 L22: 3.7102 REMARK 3 L33: 3.0431 L12: 0.0644 REMARK 3 L13: -0.6816 L23: 0.1038 REMARK 3 S TENSOR REMARK 3 S11: -0.3860 S12: 0.4180 S13: -1.7538 REMARK 3 S21: -0.3456 S22: 0.0625 S23: 0.9536 REMARK 3 S31: 1.1799 S32: -0.7992 S33: 0.3236 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: 0.1315 T22: 0.0121 REMARK 3 T33: 0.1760 T12: 0.0213 REMARK 3 T13: 0.0712 T23: -0.0139 REMARK 3 L TENSOR REMARK 3 L11: 4.4418 L22: 1.6001 REMARK 3 L33: 1.9613 L12: 0.7196 REMARK 3 L13: -1.1798 L23: -0.2231 REMARK 3 S TENSOR REMARK 3 S11: 0.1868 S12: -0.0760 S13: 0.5120 REMARK 3 S21: -0.2712 S22: -0.0119 S23: -0.1206 REMARK 3 S31: -0.0115 S32: 0.0618 S33: -0.1749 REMARK 3 REMARK 3 TLS GROUP : 5 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: 0.4733 T22: 0.5448 REMARK 3 T33: 0.2352 T12: -0.2779 REMARK 3 T13: 0.0606 T23: -0.0998 REMARK 3 L TENSOR REMARK 3 L11: 2.1424 L22: 1.5935 REMARK 3 L33: 1.9417 L12: 1.2671 REMARK 3 L13: -0.7281 L23: -1.3497 REMARK 3 S TENSOR REMARK 3 S11: -0.8672 S12: 0.9749 S13: -0.1792 REMARK 3 S21: -0.7467 S22: 0.3503 S23: -0.3513 REMARK 3 S31: 0.5335 S32: -0.1738 S33: 0.5169 REMARK 3 REMARK 3 TLS GROUP : 6 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: 0.2719 T22: 0.2645 REMARK 3 T33: 0.0729 T12: 0.1504 REMARK 3 T13: 0.0325 T23: 0.0692 REMARK 3 L TENSOR REMARK 3 L11: 1.2559 L22: 2.1768 REMARK 3 L33: 2.0588 L12: 0.9817 REMARK 3 L13: -1.3300 L23: -1.9919 REMARK 3 S TENSOR REMARK 3 S11: -0.0069 S12: 0.2681 S13: -0.1016 REMARK 3 S21: -0.5292 S22: -0.2038 S23: -0.2150 REMARK 3 S31: 0.3623 S32: -0.0084 S33: 0.2106 REMARK 3 REMARK 3 TLS GROUP : 7 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: 0.5002 T22: 0.1947 REMARK 3 T33: 0.4063 T12: -0.0395 REMARK 3 T13: 0.2501 T23: -0.0664 REMARK 3 L TENSOR REMARK 3 L11: 0.4792 L22: 1.5593 REMARK 3 L33: 1.4932 L12: 0.4880 REMARK 3 L13: -0.3314 L23: -0.6830 REMARK 3 S TENSOR REMARK 3 S11: -0.3178 S12: 0.0599 S13: -0.3419 REMARK 3 S21: -0.7409 S22: -0.0305 S23: -0.6257 REMARK 3 S31: 0.1545 S32: 0.1320 S33: 0.3483 REMARK 3 REMARK 3 TLS GROUP : 8 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: 0.2598 T22: 0.4818 REMARK 3 T33: 0.1019 T12: -0.1007 REMARK 3 T13: 0.1538 T23: 0.0092 REMARK 3 L TENSOR REMARK 3 L11: 1.6063 L22: 3.0562 REMARK 3 L33: 2.2431 L12: 0.7124 REMARK 3 L13: -0.6398 L23: -1.1493 REMARK 3 S TENSOR REMARK 3 S11: -0.0839 S12: 0.5424 S13: 0.0192 REMARK 3 S21: -0.7565 S22: -0.0010 S23: -0.5009 REMARK 3 S31: 0.0026 S32: 0.4214 S33: 0.0849 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 : 1.00 REMARK 3 ION PROBE RADIUS : 0.70 REMARK 3 SHRINKAGE RADIUS : 0.70 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THEIR REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 8PUL 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_1292131027. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 25-MAY-22 REMARK 200 TEMPERATURE (KELVIN) : 45 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I23 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 2.7552 REMARK 200 MONOCHROMATOR : SILICON CRYSTAL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 12M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS REMARK 200 DATA SCALING SOFTWARE : XIA2 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 71110 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.930 REMARK 200 RESOLUTION RANGE LOW (A) : 151.920 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 85.7 REMARK 200 DATA REDUNDANCY : 9.580 REMARK 200 R MERGE (I) : 0.05800 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 16.9300 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.93 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97 REMARK 200 COMPLETENESS FOR SHELL (%) : 73.7 REMARK 200 DATA REDUNDANCY IN SHELL : 7.30 REMARK 200 R MERGE FOR SHELL (I) : 1.87900 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.283 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 (%): 56.27 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS, 15% PEG 4000, 15% GLYCEROL, REMARK 280 PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 294.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 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 37.49750 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.96200 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.90900 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 75.96200 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.49750 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.90900 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, D 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 PRO A 229 REMARK 465 PRO A 230 REMARK 465 CYS A 231 REMARK 465 GLU C 100 REMARK 465 VAL C 101 REMARK 465 TYR C 102 REMARK 465 GLY C 103 REMARK 465 ARG C 104 REMARK 465 ASN C 105 REMARK 465 TYR C 106 REMARK 465 TYR C 107 REMARK 465 SER C 139 REMARK 465 THR C 140 REMARK 465 SER C 141 REMARK 465 ASN C 197 REMARK 465 VAL C 226 REMARK 465 GLU C 227 REMARK 465 CYS C 228 REMARK 465 PRO C 229 REMARK 465 PRO C 230 REMARK 465 CYS C 231 REMARK 465 SER B 445 REMARK 465 SER D 445 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 HE22 GLN B 355 HG SER B 362 1.15 REMARK 500 HE22 GLN D 355 HG SER D 362 1.15 REMARK 500 HH TYR A 60 H MET A 70 1.19 REMARK 500 HH TYR C 60 H MET C 70 1.20 REMARK 500 HD1 HIS A 35 HE1 TRP A 47 1.23 REMARK 500 HD1 HIS C 35 HE1 TRP C 47 1.27 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 A 102 -90.64 -109.49 REMARK 500 ASN A 105 38.46 -145.12 REMARK 500 SER A 141 58.50 -93.67 REMARK 500 SER A 195 79.92 -67.11 REMARK 500 SER A 196 45.30 -107.32 REMARK 500 ASN A 197 -125.87 63.70 REMARK 500 SER A 224 50.53 -101.54 REMARK 500 GLU A 227 -67.08 -90.42 REMARK 500 SER C 224 64.67 -103.19 REMARK 500 THR B 282 -47.67 75.49 REMARK 500 ASN B 369 72.60 58.17 REMARK 500 LYS B 400 -66.15 -102.28 REMARK 500 LEU D 278 -60.06 -104.11 REMARK 500 THR D 282 -48.46 76.34 REMARK 500 ASN D 369 73.02 57.35 REMARK 500 LYS D 400 -64.86 -102.56 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 6TKB RELATED DB: PDB REMARK 900 SAME ANTIBODY WITH DIFFERENT MUTATIONS REMARK 900 RELATED ID: 6TKC RELATED DB: PDB REMARK 900 SAME ANTIBODY WITH DIFFERENT MUTATIONS REMARK 900 RELATED ID: 6TKD RELATED DB: PDB REMARK 900 SAME ANTIBODY WITH DIFFERENT MUTATIONS REMARK 900 RELATED ID: 6TKE RELATED DB: PDB REMARK 900 SAME ANTIBODY WITH DIFFERENT MUTATIONS REMARK 900 RELATED ID: 6TKF RELATED DB: PDB REMARK 900 SAME ANTIBODY WITH DIFFERENT MUTATIONS REMARK 900 RELATED ID: 6FAX RELATED DB: PDB REMARK 900 WILDTYPE ANTIBODY BOUND TO CD40 RECEPTOR REMARK 900 RELATED ID: SASDSD7 RELATED DB: SASBDB REMARK 900 SEC-SAXS DATA FOR THE SAME PROTEIN IN SOLUTION DBREF 8PUL A 1 231 PDB 8PUL 8PUL 1 231 DBREF 8PUL C 1 231 PDB 8PUL 8PUL 1 231 DBREF 8PUL B 232 445 PDB 8PUL 8PUL 232 445 DBREF 8PUL D 232 445 PDB 8PUL 8PUL 232 445 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 THR VAL GLU SEQRES 18 A 231 ARG CYS SER CYS VAL GLU CYS PRO PRO CYS SEQRES 1 C 231 GLU VAL GLN LEU GLN GLN SER GLY PRO ASP LEU VAL LYS SEQRES 2 C 231 PRO GLY ALA SER VAL LYS ILE SER CYS LYS THR SER GLY SEQRES 3 C 231 TYR THR PHE THR GLU TYR ILE MET HIS TRP VAL LYS GLN SEQRES 4 C 231 SER HIS GLY LYS SER LEU GLU TRP ILE GLY GLY ILE ILE SEQRES 5 C 231 PRO ASN ASN GLY GLY THR SER TYR ASN GLN LYS PHE LYS SEQRES 6 C 231 ASP LYS ALA THR MET THR VAL ASP LYS SER SER SER THR SEQRES 7 C 231 GLY TYR MET GLU LEU ARG SER LEU THR SER GLU ASP SER SEQRES 8 C 231 ALA VAL TYR TYR CYS THR ARG ARG GLU VAL TYR GLY ARG SEQRES 9 C 231 ASN TYR TYR ALA LEU ASP TYR TRP GLY GLN GLY THR LEU SEQRES 10 C 231 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 C 231 PHE PRO LEU ALA PRO CYS SER ARG SER THR SER GLU SER SEQRES 12 C 231 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 C 231 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 C 231 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 C 231 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 C 231 SER ASN PHE GLY THR GLN THR TYR THR CYS ASN VAL ASP SEQRES 17 C 231 HIS LYS PRO SER ASN THR LYS VAL ASP LYS THR VAL GLU SEQRES 18 C 231 ARG CYS 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 GLU 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 SEQRES 1 D 214 ASP ILE GLN MET THR GLN THR THR SER SER LEU SER ALA SEQRES 2 D 214 SER LEU GLY ASP ARG VAL THR ILE THR CYS SER ALA SER SEQRES 3 D 214 GLN GLY ILE ASN ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 D 214 PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SER SEQRES 5 D 214 SER LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 D 214 GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN LEU SEQRES 7 D 214 GLU PRO GLU ASP ILE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 D 214 SER ASN LEU PRO TYR THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 D 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 D 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 D 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 D 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 D 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 D 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 D 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 D 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 D 214 PHE ASN ARG GLY GLU SER HET GOL A 301 14 HET GOL A 302 14 HET GOL A 303 14 HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 5 GOL 3(C3 H8 O3) FORMUL 8 HOH *322(H2 O) HELIX 1 AA1 THR A 28 TYR A 32 5 5 HELIX 2 AA2 GLN A 62 LYS A 65 5 4 HELIX 3 AA3 LYS A 74 SER A 76 5 3 HELIX 4 AA4 THR A 87 SER A 91 5 5 HELIX 5 AA5 SER A 165 ALA A 167 5 3 HELIX 6 AA6 LYS A 210 ASN A 213 5 4 HELIX 7 AA7 THR C 28 TYR C 32 5 5 HELIX 8 AA8 GLN C 62 LYS C 65 5 4 HELIX 9 AA9 LYS C 74 SER C 76 5 3 HELIX 10 AB1 THR C 87 SER C 91 5 5 HELIX 11 AB2 SER C 165 ALA C 167 5 3 HELIX 12 AB3 LYS C 210 ASN C 213 5 4 HELIX 13 AB4 GLU B 310 ILE B 314 5 5 HELIX 14 AB5 SER B 352 LYS B 357 1 6 HELIX 15 AB6 LYS B 414 GLU B 418 1 5 HELIX 16 AB7 GLU D 310 ILE D 314 5 5 HELIX 17 AB8 SER D 352 LYS D 357 1 6 HELIX 18 AB9 LYS D 414 GLU D 418 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 MET A 81 N ILE A 20 SHEET 4 AA1 4 ALA A 68 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 THR A 116 VAL A 120 1 O THR A 119 N ASP A 10 SHEET 3 AA2 6 ALA A 92 VAL A 101 -1 N ALA A 92 O VAL A 118 SHEET 4 AA2 6 MET A 34 GLN A 39 -1 N VAL A 37 O TYR A 95 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 THR A 116 VAL A 120 1 O THR A 119 N ASP A 10 SHEET 3 AA3 4 ALA A 92 VAL A 101 -1 N ALA A 92 O VAL A 118 SHEET 4 AA3 4 TYR A 107 TRP A 112 -1 O ALA A 108 N GLU A 100 SHEET 1 AA4 4 SER A 129 LEU A 133 0 SHEET 2 AA4 4 THR A 144 TYR A 154 -1 O LEU A 150 N PHE A 131 SHEET 3 AA4 4 TYR A 185 PRO A 194 -1 O LEU A 187 N VAL A 151 SHEET 4 AA4 4 VAL A 172 THR A 174 -1 N HIS A 173 O VAL A 190 SHEET 1 AA5 4 SER A 129 LEU A 133 0 SHEET 2 AA5 4 THR A 144 TYR A 154 -1 O LEU A 150 N PHE A 131 SHEET 3 AA5 4 TYR A 185 PRO A 194 -1 O LEU A 187 N VAL A 151 SHEET 4 AA5 4 VAL A 178 LEU A 179 -1 N VAL A 178 O SER A 186 SHEET 1 AA6 3 THR A 160 TRP A 163 0 SHEET 2 AA6 3 THR A 204 HIS A 209 -1 O ASN A 206 N SER A 162 SHEET 3 AA6 3 THR A 214 THR A 219 -1 O VAL A 216 N VAL A 207 SHEET 1 AA7 5 CYS A 225 VAL A 226 0 SHEET 2 AA7 5 VAL D 436 ARG D 442 -1 O ASN D 441 N VAL A 226 SHEET 3 AA7 5 VAL D 422 THR D 428 -1 N VAL D 427 O VAL D 436 SHEET 4 AA7 5 LYS D 376 VAL D 381 -1 N GLN D 378 O GLU D 426 SHEET 5 AA7 5 ALA D 384 LEU D 385 -1 O ALA D 384 N VAL D 381 SHEET 1 AA8 4 GLN C 3 GLN C 6 0 SHEET 2 AA8 4 VAL C 18 SER C 25 -1 O LYS C 23 N GLN C 5 SHEET 3 AA8 4 THR C 78 LEU C 83 -1 O MET C 81 N ILE C 20 SHEET 4 AA8 4 ALA C 68 ASP C 73 -1 N THR C 71 O TYR C 80 SHEET 1 AA9 6 ASP C 10 VAL C 12 0 SHEET 2 AA9 6 THR C 116 VAL C 120 1 O THR C 119 N ASP C 10 SHEET 3 AA9 6 ALA C 92 ARG C 99 -1 N ALA C 92 O VAL C 118 SHEET 4 AA9 6 ILE C 33 GLN C 39 -1 N VAL C 37 O TYR C 95 SHEET 5 AA9 6 LEU C 45 ILE C 51 -1 O GLU C 46 N LYS C 38 SHEET 6 AA9 6 THR C 58 TYR C 60 -1 O SER C 59 N GLY C 50 SHEET 1 AB1 4 ASP C 10 VAL C 12 0 SHEET 2 AB1 4 THR C 116 VAL C 120 1 O THR C 119 N ASP C 10 SHEET 3 AB1 4 ALA C 92 ARG C 99 -1 N ALA C 92 O VAL C 118 SHEET 4 AB1 4 TYR C 111 TRP C 112 -1 O TYR C 111 N ARG C 98 SHEET 1 AB2 4 SER C 129 LEU C 133 0 SHEET 2 AB2 4 THR C 144 TYR C 154 -1 O LEU C 150 N PHE C 131 SHEET 3 AB2 4 TYR C 185 PRO C 194 -1 O TYR C 185 N TYR C 154 SHEET 4 AB2 4 VAL C 172 THR C 174 -1 N HIS C 173 O VAL C 190 SHEET 1 AB3 4 SER C 129 LEU C 133 0 SHEET 2 AB3 4 THR C 144 TYR C 154 -1 O LEU C 150 N PHE C 131 SHEET 3 AB3 4 TYR C 185 PRO C 194 -1 O TYR C 185 N TYR C 154 SHEET 4 AB3 4 VAL C 178 LEU C 179 -1 N VAL C 178 O SER C 186 SHEET 1 AB4 3 THR C 160 TRP C 163 0 SHEET 2 AB4 3 THR C 204 HIS C 209 -1 O ASN C 206 N SER C 162 SHEET 3 AB4 3 THR C 214 THR C 219 -1 O VAL C 216 N VAL C 207 SHEET 1 AB5 4 MET B 235 THR B 236 0 SHEET 2 AB5 4 VAL B 250 ALA B 256 -1 O SER B 255 N THR B 236 SHEET 3 AB5 4 ASP B 301 ILE B 306 -1 O LEU B 304 N ILE B 252 SHEET 4 AB5 4 PHE B 293 SER B 298 -1 N SER B 294 O THR B 305 SHEET 1 AB6 6 SER B 241 SER B 245 0 SHEET 2 AB6 6 THR B 333 LYS B 338 1 O GLU B 336 N LEU B 242 SHEET 3 AB6 6 ALA B 315 GLN B 321 -1 N ALA B 315 O LEU B 335 SHEET 4 AB6 6 LEU B 264 GLN B 269 -1 N GLN B 269 O THR B 316 SHEET 5 AB6 6 VAL B 275 TYR B 280 -1 O LYS B 276 N GLN B 268 SHEET 6 AB6 6 SER B 284 LEU B 285 -1 O SER B 284 N TYR B 280 SHEET 1 AB7 4 SER B 241 SER B 245 0 SHEET 2 AB7 4 THR B 333 LYS B 338 1 O GLU B 336 N LEU B 242 SHEET 3 AB7 4 ALA B 315 GLN B 321 -1 N ALA B 315 O LEU B 335 SHEET 4 AB7 4 THR B 328 PHE B 329 -1 O THR B 328 N GLN B 321 SHEET 1 AB8 4 SER B 345 PHE B 349 0 SHEET 2 AB8 4 THR B 360 PHE B 370 -1 O LEU B 366 N PHE B 347 SHEET 3 AB8 4 TYR B 404 SER B 413 -1 O LEU B 406 N LEU B 367 SHEET 4 AB8 4 SER B 390 VAL B 394 -1 N GLN B 391 O THR B 409 SHEET 1 AB9 4 ALA B 384 LEU B 385 0 SHEET 2 AB9 4 LYS B 376 VAL B 381 -1 N VAL B 381 O ALA B 384 SHEET 3 AB9 4 VAL B 422 THR B 428 -1 O GLU B 426 N GLN B 378 SHEET 4 AB9 4 VAL B 436 ASN B 441 -1 O VAL B 436 N VAL B 427 SHEET 1 AC1 4 MET D 235 THR D 236 0 SHEET 2 AC1 4 VAL D 250 ALA D 256 -1 O SER D 255 N THR D 236 SHEET 3 AC1 4 ASP D 301 ILE D 306 -1 O LEU D 304 N ILE D 252 SHEET 4 AC1 4 PHE D 293 SER D 298 -1 N SER D 294 O THR D 305 SHEET 1 AC2 6 SER D 241 SER D 245 0 SHEET 2 AC2 6 THR D 333 LYS D 338 1 O GLU D 336 N LEU D 242 SHEET 3 AC2 6 ALA D 315 GLN D 321 -1 N ALA D 315 O LEU D 335 SHEET 4 AC2 6 LEU D 264 GLN D 269 -1 N GLN D 269 O THR D 316 SHEET 5 AC2 6 VAL D 275 TYR D 280 -1 O LYS D 276 N GLN D 268 SHEET 6 AC2 6 SER D 284 LEU D 285 -1 O SER D 284 N TYR D 280 SHEET 1 AC3 4 SER D 241 SER D 245 0 SHEET 2 AC3 4 THR D 333 LYS D 338 1 O GLU D 336 N LEU D 242 SHEET 3 AC3 4 ALA D 315 GLN D 321 -1 N ALA D 315 O LEU D 335 SHEET 4 AC3 4 THR D 328 PHE D 329 -1 O THR D 328 N GLN D 321 SHEET 1 AC4 4 SER D 345 PHE D 349 0 SHEET 2 AC4 4 THR D 360 PHE D 370 -1 O LEU D 366 N PHE D 347 SHEET 3 AC4 4 TYR D 404 SER D 413 -1 O LEU D 406 N LEU D 367 SHEET 4 AC4 4 SER D 390 VAL D 394 -1 N GLN D 391 O THR D 409 SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.05 SSBOND 2 CYS A 136 CYS C 225 1555 1555 2.04 SSBOND 3 CYS A 149 CYS A 205 1555 1555 2.04 SSBOND 4 CYS A 223 CYS C 223 1555 1555 2.04 SSBOND 5 CYS A 225 CYS C 136 1555 1555 2.05 SSBOND 6 CYS C 22 CYS C 96 1555 1555 2.05 SSBOND 7 CYS C 149 CYS C 205 1555 1555 2.03 SSBOND 8 CYS B 254 CYS B 319 1555 1555 2.09 SSBOND 9 CYS B 365 CYS B 425 1555 1555 2.05 SSBOND 10 CYS D 254 CYS D 319 1555 1555 2.06 SSBOND 11 CYS D 365 CYS D 425 1555 1555 2.05 CISPEP 1 PHE A 155 PRO A 156 0 -8.97 CISPEP 2 GLU A 157 PRO A 158 0 -4.79 CISPEP 3 PHE C 155 PRO C 156 0 -8.62 CISPEP 4 GLU C 157 PRO C 158 0 -4.24 CISPEP 5 LEU B 325 PRO B 326 0 -3.87 CISPEP 6 TYR B 371 PRO B 372 0 1.24 CISPEP 7 LEU D 325 PRO D 326 0 -5.54 CISPEP 8 TYR D 371 PRO D 372 0 1.25 CRYST1 74.995 95.818 151.924 90.00 90.00 90.00 P 21 21 21 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 0.013334 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010436 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006582 0.00000