HEADER IMMUNE SYSTEM 12-MAY-22 7XRZ TITLE CRYSTAL STRUCTURE OF BRIL AND SRP2070_FAB COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: IGG LIGHT CHAIN; COMPND 3 CHAIN: L, A; COMPND 4 MOL_ID: 2; COMPND 5 MOLECULE: IGG HEAVY CHAIN; COMPND 6 CHAIN: H, B; COMPND 7 MOL_ID: 3; COMPND 8 MOLECULE: SOLUBLE CYTOCHROME B562; COMPND 9 CHAIN: X, Y; COMPND 10 SYNONYM: CYTOCHROME B-562; COMPND 11 ENGINEERED: YES; COMPND 12 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 MOL_ID: 2; SOURCE 5 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 6 ORGANISM_TAXID: 10090; SOURCE 7 MOL_ID: 3; SOURCE 8 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 9 ORGANISM_TAXID: 562; SOURCE 10 GENE: CYBC; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS BRIL, ANTIBODY, COMPLEX, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR M.SUZUKI,H.MIYAGI,M.YASUNAGA,H.ASADA,S.IWATA,J.SAITO REVDAT 1 10-MAY-23 7XRZ 0 JRNL AUTH H.MIYAGI,M.SUZUKI,M.YASUNAGA,H.ASADA,S.IWATA,J.I.SAITO JRNL TITL STRUCTURAL INSIGHT INTO AN ANTI-BRIL FAB AS A JRNL TITL 2 G-PROTEIN-COUPLED RECEPTOR CRYSTALLIZATION CHAPERONE. JRNL REF ACTA CRYSTALLOGR D STRUCT 2023 JRNL REF 2 BIOL JRNL REFN ISSN 2059-7983 JRNL PMID 37098908 JRNL DOI 10.1107/S205979832300311X REMARK 2 REMARK 2 RESOLUTION. 2.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0232 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) : 2.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.74 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 94.6 REMARK 3 NUMBER OF REFLECTIONS : 54939 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) : 0.216 REMARK 3 R VALUE (WORKING SET) : 0.214 REMARK 3 FREE R VALUE : 0.268 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 2917 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) : 2.10 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15 REMARK 3 REFLECTION IN BIN (WORKING SET) : 4064 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.50 REMARK 3 BIN R VALUE (WORKING SET) : 0.3390 REMARK 3 BIN FREE R VALUE SET COUNT : 194 REMARK 3 BIN FREE R VALUE : 0.3520 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 8291 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 665 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.42 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.80000 REMARK 3 B22 (A**2) : 0.18000 REMARK 3 B33 (A**2) : 0.48000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.33000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.323 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.237 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.916 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8611 ; 0.004 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 7645 ; 0.036 ; 0.017 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11736 ; 1.319 ; 1.646 REMARK 3 BOND ANGLES OTHERS (DEGREES): 17917 ; 2.382 ; 1.575 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1099 ; 7.413 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 402 ;33.962 ;23.731 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1425 ;17.075 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 33 ;14.539 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1161 ; 0.052 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9654 ; 0.005 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1725 ; 0.005 ; 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): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL 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 : 10 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 : L 1 L 108 REMARK 3 ORIGIN FOR THE GROUP (A): -47.2760 -25.8260 212.1000 REMARK 3 T TENSOR REMARK 3 T11: 0.0488 T22: 0.0865 REMARK 3 T33: 0.0402 T12: 0.0024 REMARK 3 T13: 0.0376 T23: 0.0131 REMARK 3 L TENSOR REMARK 3 L11: 4.9375 L22: 1.9747 REMARK 3 L33: 2.5289 L12: 2.7818 REMARK 3 L13: 0.8986 L23: 0.6817 REMARK 3 S TENSOR REMARK 3 S11: -0.0102 S12: 0.1542 S13: 0.0928 REMARK 3 S21: -0.1329 S22: 0.1578 S23: -0.0422 REMARK 3 S31: -0.0414 S32: 0.0422 S33: -0.1477 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 : L 109 L 213 REMARK 3 ORIGIN FOR THE GROUP (A): -21.1130 -35.4070 190.1110 REMARK 3 T TENSOR REMARK 3 T11: 0.0880 T22: 0.1932 REMARK 3 T33: 0.0629 T12: 0.0050 REMARK 3 T13: 0.0062 T23: 0.0025 REMARK 3 L TENSOR REMARK 3 L11: 2.2096 L22: 3.9052 REMARK 3 L33: 3.7380 L12: -2.4325 REMARK 3 L13: -1.5419 L23: 2.6052 REMARK 3 S TENSOR REMARK 3 S11: 0.1733 S12: 0.1849 S13: 0.0194 REMARK 3 S21: -0.2716 S22: -0.1691 S23: 0.1779 REMARK 3 S31: 0.0197 S32: -0.1531 S33: -0.0043 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 1 H 119 REMARK 3 ORIGIN FOR THE GROUP (A): -51.3970 -47.9470 213.9760 REMARK 3 T TENSOR REMARK 3 T11: 0.0962 T22: 0.1007 REMARK 3 T33: 0.1382 T12: -0.0507 REMARK 3 T13: 0.0039 T23: 0.0205 REMARK 3 L TENSOR REMARK 3 L11: 2.6788 L22: 1.3165 REMARK 3 L33: 3.3043 L12: -0.5468 REMARK 3 L13: -1.7021 L23: 1.4814 REMARK 3 S TENSOR REMARK 3 S11: -0.1270 S12: -0.0415 S13: -0.3006 REMARK 3 S21: 0.1497 S22: 0.0398 S23: -0.1038 REMARK 3 S31: 0.4472 S32: -0.0374 S33: 0.0873 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 120 H 221 REMARK 3 ORIGIN FOR THE GROUP (A): -15.3540 -43.7650 202.1560 REMARK 3 T TENSOR REMARK 3 T11: 0.0355 T22: 0.1804 REMARK 3 T33: 0.0019 T12: 0.0449 REMARK 3 T13: 0.0004 T23: -0.0030 REMARK 3 L TENSOR REMARK 3 L11: 4.5347 L22: 6.1599 REMARK 3 L33: 1.5739 L12: 1.0372 REMARK 3 L13: -0.4793 L23: -0.2801 REMARK 3 S TENSOR REMARK 3 S11: -0.2017 S12: -0.1429 S13: -0.0022 REMARK 3 S21: -0.1318 S22: 0.1871 S23: -0.0820 REMARK 3 S31: -0.0706 S32: 0.1892 S33: 0.0147 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : X 2 X 105 REMARK 3 ORIGIN FOR THE GROUP (A): -75.2520 -39.3380 213.5360 REMARK 3 T TENSOR REMARK 3 T11: 0.0873 T22: 0.3089 REMARK 3 T33: 0.2346 T12: -0.0956 REMARK 3 T13: -0.0283 T23: 0.0775 REMARK 3 L TENSOR REMARK 3 L11: 2.7375 L22: 2.5197 REMARK 3 L33: 6.8409 L12: -0.0353 REMARK 3 L13: 2.2574 L23: 0.4283 REMARK 3 S TENSOR REMARK 3 S11: 0.0568 S12: -0.1297 S13: 0.1078 REMARK 3 S21: -0.2725 S22: -0.0021 S23: 0.3318 REMARK 3 S31: -0.0785 S32: -0.7712 S33: -0.0547 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 1 A 108 REMARK 3 ORIGIN FOR THE GROUP (A): -18.5880 -15.7320 163.9450 REMARK 3 T TENSOR REMARK 3 T11: 0.0329 T22: 0.0874 REMARK 3 T33: 0.0614 T12: -0.0044 REMARK 3 T13: 0.0327 T23: -0.0133 REMARK 3 L TENSOR REMARK 3 L11: 3.6565 L22: 2.5843 REMARK 3 L33: 1.5817 L12: -1.6174 REMARK 3 L13: 0.1091 L23: -0.0716 REMARK 3 S TENSOR REMARK 3 S11: -0.0622 S12: -0.0731 S13: 0.2118 REMARK 3 S21: 0.2159 S22: 0.0505 S23: 0.1805 REMARK 3 S31: -0.0787 S32: -0.1313 S33: 0.0116 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 109 A 214 REMARK 3 ORIGIN FOR THE GROUP (A): -44.4580 -27.1440 182.9940 REMARK 3 T TENSOR REMARK 3 T11: 0.1243 T22: 0.4006 REMARK 3 T33: 0.0344 T12: 0.0084 REMARK 3 T13: 0.0302 T23: -0.0742 REMARK 3 L TENSOR REMARK 3 L11: 2.0904 L22: 4.8675 REMARK 3 L33: 3.5009 L12: 0.9072 REMARK 3 L13: -1.0770 L23: -3.0797 REMARK 3 S TENSOR REMARK 3 S11: -0.0469 S12: -0.4645 S13: 0.0775 REMARK 3 S21: 0.3002 S22: 0.0251 S23: -0.0380 REMARK 3 S31: 0.0986 S32: 0.0291 S33: 0.0219 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 1 B 119 REMARK 3 ORIGIN FOR THE GROUP (A): -14.2960 -37.2880 158.8520 REMARK 3 T TENSOR REMARK 3 T11: 0.0181 T22: 0.0630 REMARK 3 T33: 0.0120 T12: 0.0035 REMARK 3 T13: 0.0076 T23: 0.0026 REMARK 3 L TENSOR REMARK 3 L11: 3.0501 L22: 1.9763 REMARK 3 L33: 2.8689 L12: 0.4278 REMARK 3 L13: -1.4025 L23: -1.0667 REMARK 3 S TENSOR REMARK 3 S11: -0.0608 S12: -0.0037 S13: -0.1114 REMARK 3 S21: 0.0357 S22: 0.0025 S23: 0.0015 REMARK 3 S31: 0.1533 S32: -0.1223 S33: 0.0584 REMARK 3 REMARK 3 TLS GROUP : 9 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 120 B 221 REMARK 3 ORIGIN FOR THE GROUP (A): -51.7760 -34.3830 170.9890 REMARK 3 T TENSOR REMARK 3 T11: 0.0563 T22: 0.2282 REMARK 3 T33: 0.0359 T12: -0.0742 REMARK 3 T13: 0.0129 T23: -0.0157 REMARK 3 L TENSOR REMARK 3 L11: 3.7408 L22: 4.9835 REMARK 3 L33: 2.4611 L12: -1.8002 REMARK 3 L13: -0.6547 L23: 0.9637 REMARK 3 S TENSOR REMARK 3 S11: -0.1186 S12: -0.4070 S13: 0.1048 REMARK 3 S21: 0.1256 S22: 0.0829 S23: 0.1915 REMARK 3 S31: 0.0898 S32: -0.1697 S33: 0.0356 REMARK 3 REMARK 3 TLS GROUP : 10 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : Y 2 Y 105 REMARK 3 ORIGIN FOR THE GROUP (A): 9.1640 -29.5350 164.4010 REMARK 3 T TENSOR REMARK 3 T11: 0.0961 T22: 0.2065 REMARK 3 T33: 0.2771 T12: 0.0120 REMARK 3 T13: -0.0075 T23: -0.0123 REMARK 3 L TENSOR REMARK 3 L11: 2.4520 L22: 2.8906 REMARK 3 L33: 6.1408 L12: -0.4740 REMARK 3 L13: 0.7524 L23: -0.7365 REMARK 3 S TENSOR REMARK 3 S11: -0.0256 S12: -0.3374 S13: 0.2483 REMARK 3 S21: 0.4384 S22: 0.0147 S23: -0.3932 REMARK 3 S31: -0.3873 S32: 0.2478 S33: 0.0108 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 U VALUES : WITH TLS ADDED REMARK 4 REMARK 4 7XRZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-MAY-22. REMARK 100 THE DEPOSITION ID IS D_1300029478. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 25-APR-18 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.5 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) : 1.00004 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.21 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57858 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100 REMARK 200 RESOLUTION RANGE LOW (A) : 48.640 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.9 REMARK 200 DATA REDUNDANCY : 2.300 REMARK 200 R MERGE (I) : 0.06300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.16 REMARK 200 COMPLETENESS FOR SHELL (%) : 94.7 REMARK 200 DATA REDUNDANCY IN SHELL : 2.30 REMARK 200 R MERGE FOR SHELL (I) : 0.64500 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER 2.6.1 REMARK 200 STARTING MODEL: 1M6T, 1F58 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 44.88 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, TRIS-HCL, PH 8.5, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 277.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 46.91400 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.61950 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 46.91400 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 37.61950 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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: 5890 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 23930 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, X 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 REMARK 350 BIOMOLECULE: 2 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: 5900 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 24160 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, Y 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 365 LIES ON A SPECIAL POSITION. REMARK 375 HOH A 346 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 L 214 REMARK 465 ASP H 136 REMARK 465 THR H 137 REMARK 465 SER H 138 REMARK 465 GLY X 1 REMARK 465 LEU X 106 REMARK 465 GLY Y 1 REMARK 465 LEU Y 106 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 SER L 30 -127.66 54.18 REMARK 500 SER L 40 -120.89 -131.45 REMARK 500 ALA L 51 -51.61 73.21 REMARK 500 CYS H 134 95.29 -54.42 REMARK 500 SER H 178 60.24 38.37 REMARK 500 SER A 30 -129.87 56.35 REMARK 500 SER A 40 -115.71 -130.98 REMARK 500 ALA A 51 -49.71 73.73 REMARK 500 ASN A 212 67.06 63.42 REMARK 500 PRO B 41 116.05 -35.25 REMARK 500 ALA B 92 172.86 178.00 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 ASN A 31 12.18 REMARK 500 ASN A 31 12.16 REMARK 500 REMARK 500 REMARK: NULL DBREF 7XRZ L 1 214 PDB 7XRZ 7XRZ 1 214 DBREF 7XRZ H 1 221 PDB 7XRZ 7XRZ 1 221 DBREF 7XRZ X 2 106 UNP P0ABE7 C562_ECOLX 24 128 DBREF 7XRZ A 1 214 PDB 7XRZ 7XRZ 1 214 DBREF 7XRZ B 1 221 PDB 7XRZ 7XRZ 1 221 DBREF 7XRZ Y 2 106 UNP P0ABE7 C562_ECOLX 24 128 SEQADV 7XRZ GLY X 1 UNP P0ABE7 EXPRESSION TAG SEQADV 7XRZ TRP X 7 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 7XRZ ILE X 102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION SEQADV 7XRZ LEU X 106 UNP P0ABE7 ARG 128 ENGINEERED MUTATION SEQADV 7XRZ GLY Y 1 UNP P0ABE7 EXPRESSION TAG SEQADV 7XRZ TRP Y 7 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 7XRZ ILE Y 102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION SEQADV 7XRZ LEU Y 106 UNP P0ABE7 ARG 128 ENGINEERED MUTATION SEQRES 1 L 214 ASP ILE VAL LEU THR GLN SER PRO ALA THR LEU SER VAL SEQRES 2 L 214 THR PRO GLY ASP ARG VAL SER LEU SER CYS ARG ALA SER SEQRES 3 L 214 GLN SER VAL SER ASN TYR LEU HIS TRP TYR GLN GLN LYS SEQRES 4 L 214 SER HIS GLU SER PRO ARG LEU LEU ILE LYS TYR ALA SER SEQRES 5 L 214 GLN SER ILE SER GLY ILE PRO SER ARG PHE SER GLY SER SEQRES 6 L 214 GLY SER GLY THR ASP PHE THR LEU SER ILE ASN SER VAL SEQRES 7 L 214 GLU THR GLU ASP PHE GLY MET TYR PHE CYS GLN GLN SER SEQRES 8 L 214 ASN SER TRP PRO LEU THR PHE GLY ALA GLY THR LYS LEU SEQRES 9 L 214 GLU LEU ARG ARG ALA ASP ALA ALA PRO THR VAL SER ILE SEQRES 10 L 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SEQRES 11 L 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP SEQRES 12 L 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN SEQRES 13 L 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR SEQRES 15 L 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU SEQRES 16 L 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER SEQRES 17 L 214 PHE ASN ARG ASN GLU CYS SEQRES 1 H 221 GLN ILE GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS SEQRES 2 H 221 PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA SER GLY SEQRES 3 H 221 TYR THR PHE THR ASP PHE TYR ILE ASN TRP MET LYS GLN SEQRES 4 H 221 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY TRP ILE PHE SEQRES 5 H 221 PRO GLY SER GLY ASN THR HIS TYR ASN GLU LYS PHE LYS SEQRES 6 H 221 GLY LYS ALA THR LEU ILE VAL ASP THR SER SER SER THR SEQRES 7 H 221 ALA PHE MET GLN LEU ASN SER LEU THR SER GLU ASP SER SEQRES 8 H 221 ALA VAL TYR PHE CYS THR ARG PRO VAL SER TYR TYR TYR SEQRES 9 H 221 ASP PHE ASP TYR TRP GLY GLN GLY THR THR LEU THR VAL SEQRES 10 H 221 SER SER ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU SEQRES 11 H 221 ALA PRO VAL CYS GLY ASP THR SER GLY SER SER VAL THR SEQRES 12 H 221 LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL SEQRES 13 H 221 THR LEU THR TRP ASN SER GLY SER LEU SER SER GLY VAL SEQRES 14 H 221 HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR SEQRES 15 H 221 LEU SER SER SER VAL THR VAL THR SER SER THR TRP PRO SEQRES 16 H 221 SER GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER SEQRES 17 H 221 SER THR LYS VAL ASP LYS LYS ILE GLU PRO ARG GLY PRO SEQRES 1 X 106 GLY ASP LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN SEQRES 2 X 106 LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL SEQRES 3 X 106 LYS ASP ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP SEQRES 4 X 106 ALA GLN LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER SEQRES 5 X 106 PRO ASP SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE SEQRES 6 X 106 ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU SEQRES 7 X 106 ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA SEQRES 8 X 106 GLU GLN LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS SEQRES 9 X 106 TYR LEU SEQRES 1 A 214 ASP ILE VAL LEU THR GLN SER PRO ALA THR LEU SER VAL SEQRES 2 A 214 THR PRO GLY ASP ARG VAL SER LEU SER CYS ARG ALA SER SEQRES 3 A 214 GLN SER VAL SER ASN TYR LEU HIS TRP TYR GLN GLN LYS SEQRES 4 A 214 SER HIS GLU SER PRO ARG LEU LEU ILE LYS TYR ALA SER SEQRES 5 A 214 GLN SER ILE SER GLY ILE PRO SER ARG PHE SER GLY SER SEQRES 6 A 214 GLY SER GLY THR ASP PHE THR LEU SER ILE ASN SER VAL SEQRES 7 A 214 GLU THR GLU ASP PHE GLY MET TYR PHE CYS GLN GLN SER SEQRES 8 A 214 ASN SER TRP PRO LEU THR PHE GLY ALA GLY THR LYS LEU SEQRES 9 A 214 GLU LEU ARG ARG ALA ASP ALA ALA PRO THR VAL SER ILE SEQRES 10 A 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SEQRES 11 A 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP SEQRES 12 A 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN SEQRES 13 A 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS SEQRES 14 A 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR SEQRES 15 A 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU SEQRES 16 A 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER SEQRES 17 A 214 PHE ASN ARG ASN GLU CYS SEQRES 1 B 221 GLN ILE GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS SEQRES 2 B 221 PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA SER GLY SEQRES 3 B 221 TYR THR PHE THR ASP PHE TYR ILE ASN TRP MET LYS GLN SEQRES 4 B 221 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY TRP ILE PHE SEQRES 5 B 221 PRO GLY SER GLY ASN THR HIS TYR ASN GLU LYS PHE LYS SEQRES 6 B 221 GLY LYS ALA THR LEU ILE VAL ASP THR SER SER SER THR SEQRES 7 B 221 ALA PHE MET GLN LEU ASN SER LEU THR SER GLU ASP SER SEQRES 8 B 221 ALA VAL TYR PHE CYS THR ARG PRO VAL SER TYR TYR TYR SEQRES 9 B 221 ASP PHE ASP TYR TRP GLY GLN GLY THR THR LEU THR VAL SEQRES 10 B 221 SER SER ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU SEQRES 11 B 221 ALA PRO VAL CYS GLY ASP THR SER GLY SER SER VAL THR SEQRES 12 B 221 LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL SEQRES 13 B 221 THR LEU THR TRP ASN SER GLY SER LEU SER SER GLY VAL SEQRES 14 B 221 HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR SEQRES 15 B 221 LEU SER SER SER VAL THR VAL THR SER SER THR TRP PRO SEQRES 16 B 221 SER GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER SEQRES 17 B 221 SER THR LYS VAL ASP LYS LYS ILE GLU PRO ARG GLY PRO SEQRES 1 Y 106 GLY ASP LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN SEQRES 2 Y 106 LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL SEQRES 3 Y 106 LYS ASP ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP SEQRES 4 Y 106 ALA GLN LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER SEQRES 5 Y 106 PRO ASP SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE SEQRES 6 Y 106 ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU SEQRES 7 Y 106 ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA SEQRES 8 Y 106 GLU GLN LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS SEQRES 9 Y 106 TYR LEU FORMUL 7 HOH *665(H2 O) HELIX 1 AA1 GLU L 79 PHE L 83 5 5 HELIX 2 AA2 SER L 121 SER L 127 1 7 HELIX 3 AA3 LYS L 183 GLU L 187 1 5 HELIX 4 AA4 THR H 28 PHE H 32 5 5 HELIX 5 AA5 GLU H 62 LYS H 65 5 4 HELIX 6 AA6 THR H 87 SER H 91 5 5 HELIX 7 AA7 SER H 162 SER H 164 5 3 HELIX 8 AA8 PRO H 206 SER H 209 5 4 HELIX 9 AA9 LEU X 3 ALA X 20 1 18 HELIX 10 AB1 ASN X 22 LYS X 42 1 21 HELIX 11 AB2 PRO X 45 GLU X 49 5 5 HELIX 12 AB3 SER X 55 GLU X 81 1 27 HELIX 13 AB4 LYS X 83 ILE X 102 1 20 HELIX 14 AB5 GLU A 79 PHE A 83 5 5 HELIX 15 AB6 SER A 121 GLY A 128 1 8 HELIX 16 AB7 LYS A 183 GLU A 187 1 5 HELIX 17 AB8 THR B 28 PHE B 32 5 5 HELIX 18 AB9 THR B 74 SER B 76 5 3 HELIX 19 AC1 THR B 87 SER B 91 5 5 HELIX 20 AC2 SER B 162 SER B 164 5 3 HELIX 21 AC3 PRO B 206 SER B 209 5 4 HELIX 22 AC4 LEU Y 3 LYS Y 19 1 17 HELIX 23 AC5 ASN Y 22 GLN Y 41 1 20 HELIX 24 AC6 PRO Y 45 GLU Y 49 5 5 HELIX 25 AC7 SER Y 55 GLY Y 82 1 28 HELIX 26 AC8 LYS Y 83 ILE Y 102 1 20 SHEET 1 AA1 4 LEU L 4 SER L 7 0 SHEET 2 AA1 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA1 4 ASP L 70 ILE L 75 -1 O LEU L 73 N LEU L 21 SHEET 4 AA1 4 PHE L 62 SER L 65 -1 N SER L 63 O SER L 74 SHEET 1 AA2 6 THR L 10 VAL L 13 0 SHEET 2 AA2 6 THR L 102 LEU L 106 1 O LYS L 103 N LEU L 11 SHEET 3 AA2 6 GLY L 84 GLN L 90 -1 N GLY L 84 O LEU L 104 SHEET 4 AA2 6 LEU L 33 GLN L 38 -1 N HIS L 34 O GLN L 89 SHEET 5 AA2 6 ARG L 45 LYS L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AA2 6 GLN L 53 SER L 54 -1 O GLN L 53 N LYS L 49 SHEET 1 AA3 4 THR L 10 VAL L 13 0 SHEET 2 AA3 4 THR L 102 LEU L 106 1 O LYS L 103 N LEU L 11 SHEET 3 AA3 4 GLY L 84 GLN L 90 -1 N GLY L 84 O LEU L 104 SHEET 4 AA3 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AA4 4 THR L 114 PHE L 118 0 SHEET 2 AA4 4 GLY L 129 PHE L 139 -1 O ASN L 137 N THR L 114 SHEET 3 AA4 4 TYR L 173 THR L 182 -1 O LEU L 181 N ALA L 130 SHEET 4 AA4 4 VAL L 159 TRP L 163 -1 N SER L 162 O SER L 176 SHEET 1 AA5 4 SER L 153 ARG L 155 0 SHEET 2 AA5 4 ASN L 145 ILE L 150 -1 N ILE L 150 O SER L 153 SHEET 3 AA5 4 SER L 191 HIS L 198 -1 O GLU L 195 N LYS L 147 SHEET 4 AA5 4 SER L 201 ASN L 210 -1 O ILE L 205 N ALA L 196 SHEET 1 AA6 4 GLN H 3 GLN H 6 0 SHEET 2 AA6 4 VAL H 18 SER H 25 -1 O LYS H 23 N GLN H 5 SHEET 3 AA6 4 THR H 78 LEU H 83 -1 O ALA H 79 N CYS H 22 SHEET 4 AA6 4 ALA H 68 ASP H 73 -1 N ILE H 71 O PHE H 80 SHEET 1 AA7 6 GLU H 10 VAL H 12 0 SHEET 2 AA7 6 THR H 113 VAL H 117 1 O THR H 116 N GLU H 10 SHEET 3 AA7 6 ALA H 92 ARG H 98 -1 N ALA H 92 O LEU H 115 SHEET 4 AA7 6 ILE H 34 GLN H 39 -1 N ASN H 35 O THR H 97 SHEET 5 AA7 6 GLU H 46 ILE H 51 -1 O ILE H 48 N TRP H 36 SHEET 6 AA7 6 THR H 58 TYR H 60 -1 O HIS H 59 N TRP H 50 SHEET 1 AA8 4 GLU H 10 VAL H 12 0 SHEET 2 AA8 4 THR H 113 VAL H 117 1 O THR H 116 N GLU H 10 SHEET 3 AA8 4 ALA H 92 ARG H 98 -1 N ALA H 92 O LEU H 115 SHEET 4 AA8 4 TYR H 108 TRP H 109 -1 O TYR H 108 N ARG H 98 SHEET 1 AA9 4 SER H 126 LEU H 130 0 SHEET 2 AA9 4 SER H 141 TYR H 151 -1 O LYS H 149 N SER H 126 SHEET 3 AA9 4 LEU H 180 THR H 190 -1 O LEU H 183 N VAL H 148 SHEET 4 AA9 4 VAL H 169 THR H 171 -1 N HIS H 170 O SER H 186 SHEET 1 AB1 4 SER H 126 LEU H 130 0 SHEET 2 AB1 4 SER H 141 TYR H 151 -1 O LYS H 149 N SER H 126 SHEET 3 AB1 4 LEU H 180 THR H 190 -1 O LEU H 183 N VAL H 148 SHEET 4 AB1 4 VAL H 175 GLN H 177 -1 N GLN H 177 O LEU H 180 SHEET 1 AB2 3 THR H 157 TRP H 160 0 SHEET 2 AB2 3 THR H 200 HIS H 205 -1 O ASN H 202 N THR H 159 SHEET 3 AB2 3 THR H 210 LYS H 215 -1 O VAL H 212 N VAL H 203 SHEET 1 AB3 4 LEU A 4 SER A 7 0 SHEET 2 AB3 4 VAL A 19 ALA A 25 -1 O ARG A 24 N THR A 5 SHEET 3 AB3 4 ASP A 70 ILE A 75 -1 O LEU A 73 N LEU A 21 SHEET 4 AB3 4 PHE A 62 SER A 67 -1 N SER A 63 O SER A 74 SHEET 1 AB4 6 THR A 10 VAL A 13 0 SHEET 2 AB4 6 THR A 102 LEU A 106 1 O LYS A 103 N LEU A 11 SHEET 3 AB4 6 GLY A 84 GLN A 90 -1 N GLY A 84 O LEU A 104 SHEET 4 AB4 6 LEU A 33 GLN A 38 -1 N GLN A 38 O MET A 85 SHEET 5 AB4 6 ARG A 45 LYS A 49 -1 O ARG A 45 N GLN A 37 SHEET 6 AB4 6 GLN A 53 SER A 54 -1 O GLN A 53 N LYS A 49 SHEET 1 AB5 4 THR A 10 VAL A 13 0 SHEET 2 AB5 4 THR A 102 LEU A 106 1 O LYS A 103 N LEU A 11 SHEET 3 AB5 4 GLY A 84 GLN A 90 -1 N GLY A 84 O LEU A 104 SHEET 4 AB5 4 THR A 97 PHE A 98 -1 O THR A 97 N GLN A 90 SHEET 1 AB6 4 THR A 114 PHE A 118 0 SHEET 2 AB6 4 GLY A 129 PHE A 139 -1 O ASN A 137 N THR A 114 SHEET 3 AB6 4 TYR A 173 THR A 182 -1 O LEU A 179 N VAL A 132 SHEET 4 AB6 4 VAL A 159 TRP A 163 -1 N SER A 162 O SER A 176 SHEET 1 AB7 4 SER A 153 ARG A 155 0 SHEET 2 AB7 4 ASN A 145 ILE A 150 -1 N TRP A 148 O ARG A 155 SHEET 3 AB7 4 SER A 191 HIS A 198 -1 O THR A 193 N LYS A 149 SHEET 4 AB7 4 SER A 201 ASN A 210 -1 O ILE A 205 N ALA A 196 SHEET 1 AB8 4 GLN B 3 GLN B 6 0 SHEET 2 AB8 4 VAL B 18 SER B 25 -1 O LYS B 23 N GLN B 5 SHEET 3 AB8 4 THR B 78 LEU B 83 -1 O ALA B 79 N CYS B 22 SHEET 4 AB8 4 ALA B 68 ASP B 73 -1 N THR B 69 O GLN B 82 SHEET 1 AB9 6 GLU B 10 VAL B 12 0 SHEET 2 AB9 6 THR B 113 VAL B 117 1 O THR B 116 N GLU B 10 SHEET 3 AB9 6 ALA B 92 ARG B 98 -1 N ALA B 92 O LEU B 115 SHEET 4 AB9 6 ILE B 34 GLN B 39 -1 N ASN B 35 O THR B 97 SHEET 5 AB9 6 GLU B 46 ILE B 51 -1 O ILE B 48 N TRP B 36 SHEET 6 AB9 6 THR B 58 TYR B 60 -1 O HIS B 59 N TRP B 50 SHEET 1 AC1 4 GLU B 10 VAL B 12 0 SHEET 2 AC1 4 THR B 113 VAL B 117 1 O THR B 116 N GLU B 10 SHEET 3 AC1 4 ALA B 92 ARG B 98 -1 N ALA B 92 O LEU B 115 SHEET 4 AC1 4 TYR B 108 TRP B 109 -1 O TYR B 108 N ARG B 98 SHEET 1 AC2 4 SER B 126 LEU B 130 0 SHEET 2 AC2 4 SER B 141 TYR B 151 -1 O LEU B 147 N TYR B 128 SHEET 3 AC2 4 LEU B 180 THR B 190 -1 O TYR B 181 N TYR B 151 SHEET 4 AC2 4 VAL B 169 THR B 171 -1 N HIS B 170 O SER B 186 SHEET 1 AC3 4 SER B 126 LEU B 130 0 SHEET 2 AC3 4 SER B 141 TYR B 151 -1 O LEU B 147 N TYR B 128 SHEET 3 AC3 4 LEU B 180 THR B 190 -1 O TYR B 181 N TYR B 151 SHEET 4 AC3 4 VAL B 175 GLN B 177 -1 N GLN B 177 O LEU B 180 SHEET 1 AC4 3 THR B 157 TRP B 160 0 SHEET 2 AC4 3 THR B 200 HIS B 205 -1 O ALA B 204 N THR B 157 SHEET 3 AC4 3 THR B 210 LYS B 215 -1 O VAL B 212 N VAL B 203 SSBOND 1 CYS L 23 CYS L 88 1555 1555 2.06 SSBOND 2 CYS L 134 CYS L 194 1555 1555 2.02 SSBOND 3 CYS H 22 CYS H 96 1555 1555 2.05 SSBOND 4 CYS H 146 CYS H 201 1555 1555 2.06 SSBOND 5 CYS A 23 CYS A 88 1555 1555 2.06 SSBOND 6 CYS A 134 CYS A 194 1555 1555 2.03 SSBOND 7 CYS A 214 CYS B 134 1555 1555 2.05 SSBOND 8 CYS B 22 CYS B 96 1555 1555 2.05 SSBOND 9 CYS B 146 CYS B 201 1555 1555 2.02 CISPEP 1 SER L 7 PRO L 8 0 -26.36 CISPEP 2 TRP L 94 PRO L 95 0 -7.10 CISPEP 3 TYR L 140 PRO L 141 0 0.34 CISPEP 4 PHE H 152 PRO H 153 0 -5.84 CISPEP 5 GLU H 154 PRO H 155 0 -6.37 CISPEP 6 TRP H 194 PRO H 195 0 11.00 CISPEP 7 SER A 7 PRO A 8 0 -14.96 CISPEP 8 TRP A 94 PRO A 95 0 -6.62 CISPEP 9 TYR A 140 PRO A 141 0 -2.34 CISPEP 10 PHE B 152 PRO B 153 0 -6.26 CISPEP 11 GLU B 154 PRO B 155 0 -5.05 CISPEP 12 TRP B 194 PRO B 195 0 4.69 CRYST1 93.828 75.239 152.231 90.00 99.67 90.00 C 1 2 1 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 0.010658 0.000000 0.001815 0.00000 SCALE2 0.000000 0.013291 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006664 0.00000