HEADER VIRAL PROTEIN/IMMUNE SYSTEM 04-JUL-24 9IMX TITLE IMMUNE COMPLEX OF HEV E2S AND P1-5B NANOBODY COMPND MOL_ID: 1; COMPND 2 MOLECULE: SECRETED PROTEIN ORF2; COMPND 3 CHAIN: A, B, E, F; COMPND 4 SYNONYM: ORF2S; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: P1-5B NANOBODY; COMPND 8 CHAIN: C, D, G, H; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HEPATITIS E VIRUS (STRAIN PAKISTAN); SOURCE 3 ORGANISM_TAXID: 33774; SOURCE 4 GENE: ORF2; SOURCE 5 EXPRESSION_SYSTEM: BACTERIAL EXPRESSION VECTOR PET-11A; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 1944663; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 9 ORGANISM_TAXID: 30538; SOURCE 10 EXPRESSION_SYSTEM: MAMMALIAN EXPRESSION VECTOR EGFP-MCS-PCDNA3.1; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 2021194 KEYWDS IMMUNE COMPLEX, HEPATITIS E VIRUS, NANOBODY, VIRAL PROTEIN/IMMUNE KEYWDS 2 SYSTEM, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR L.TINGTING,X.WENHUI,G.YING,L.SHAOWEI REVDAT 1 03-SEP-25 9IMX 0 JRNL AUTH L.TINGTING,X.WENHUI,G.YING,L.SHAOWEI JRNL TITL IMMUNE COMPLEX OF HEV E2S AND P1-5B NANOBODY JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0403 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) : 2.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 66.22 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 85.4 REMARK 3 NUMBER OF REFLECTIONS : 68192 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) : 0.275 REMARK 3 R VALUE (WORKING SET) : 0.217 REMARK 3 FREE R VALUE : 0.245 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.800 REMARK 3 FREE R VALUE TEST SET COUNT : 2000 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) : 2.20 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23 REMARK 3 REFLECTION IN BIN (WORKING SET) : 0 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 0.00 REMARK 3 BIN R VALUE (WORKING SET) : 0.0000 REMARK 3 BIN FREE R VALUE SET COUNT : 0 REMARK 3 BIN FREE R VALUE : 0.0000 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 7272 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 118 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.06 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 4.77000 REMARK 3 B22 (A**2) : 4.46000 REMARK 3 B33 (A**2) : -9.22000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -4.36000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.057 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.047 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.092 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.970 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.861 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.837 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7438 ; 0.009 ; 0.011 REMARK 3 BOND LENGTHS OTHERS (A): 6744 ; 0.002 ; 0.016 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10152 ; 1.640 ; 1.640 REMARK 3 BOND ANGLES OTHERS (DEGREES): 15442 ; 0.541 ; 1.560 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 942 ; 8.585 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 40 ;12.769 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1038 ;18.372 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1150 ; 0.072 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8776 ; 0.010 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1824 ; 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): 3828 ; 3.106 ; 2.552 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3828 ; 3.105 ; 2.552 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4750 ; 4.308 ; 4.579 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4751 ; 4.308 ; 4.579 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3610 ; 2.492 ; 2.432 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3611 ; 2.492 ; 2.432 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 5403 ; 3.542 ; 4.520 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 8975 ; 5.189 ;24.530 REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 8967 ; 5.188 ;24.530 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 : 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 457 A 602 REMARK 3 ORIGIN FOR THE GROUP (A): -3.4084 32.5170 18.2279 REMARK 3 T TENSOR REMARK 3 T11: 0.1368 T22: 0.0898 REMARK 3 T33: 0.0090 T12: -0.0072 REMARK 3 T13: -0.0160 T23: -0.0231 REMARK 3 L TENSOR REMARK 3 L11: 0.2756 L22: 0.3814 REMARK 3 L33: 0.1155 L12: -0.1456 REMARK 3 L13: 0.1719 L23: -0.1398 REMARK 3 S TENSOR REMARK 3 S11: 0.0032 S12: 0.0098 S13: -0.0080 REMARK 3 S21: 0.0311 S22: 0.0015 S23: 0.0119 REMARK 3 S31: -0.0106 S32: 0.0078 S33: -0.0048 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 : B 459 B 602 REMARK 3 ORIGIN FOR THE GROUP (A): -1.7029 10.5508 28.0543 REMARK 3 T TENSOR REMARK 3 T11: 0.1522 T22: 0.0819 REMARK 3 T33: 0.0029 T12: 0.0041 REMARK 3 T13: -0.0136 T23: -0.0120 REMARK 3 L TENSOR REMARK 3 L11: 0.3840 L22: 0.2278 REMARK 3 L33: 0.0061 L12: 0.2901 REMARK 3 L13: -0.0416 L23: -0.0351 REMARK 3 S TENSOR REMARK 3 S11: 0.0233 S12: -0.0457 S13: 0.0094 REMARK 3 S21: -0.0179 S22: -0.0240 S23: 0.0089 REMARK 3 S31: 0.0123 S32: 0.0021 S33: 0.0007 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 : C 1 C 109 REMARK 3 ORIGIN FOR THE GROUP (A): 15.0476 10.4455 4.9412 REMARK 3 T TENSOR REMARK 3 T11: 0.1100 T22: 0.1154 REMARK 3 T33: 0.0547 T12: 0.0058 REMARK 3 T13: -0.0164 T23: 0.0142 REMARK 3 L TENSOR REMARK 3 L11: 0.0105 L22: 0.4684 REMARK 3 L33: 0.0019 L12: 0.0620 REMARK 3 L13: -0.0032 L23: -0.0169 REMARK 3 S TENSOR REMARK 3 S11: 0.0207 S12: -0.0125 S13: 0.0022 REMARK 3 S21: 0.0166 S22: -0.0299 S23: 0.0526 REMARK 3 S31: -0.0015 S32: 0.0113 S33: 0.0092 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 : D 2 D 109 REMARK 3 ORIGIN FOR THE GROUP (A): 13.1831 36.0903 40.8722 REMARK 3 T TENSOR REMARK 3 T11: 0.1377 T22: 0.1459 REMARK 3 T33: 0.0328 T12: -0.0020 REMARK 3 T13: -0.0021 T23: 0.0040 REMARK 3 L TENSOR REMARK 3 L11: 0.2288 L22: 0.2640 REMARK 3 L33: 0.0090 L12: -0.2346 REMARK 3 L13: 0.0287 L23: -0.0183 REMARK 3 S TENSOR REMARK 3 S11: -0.0104 S12: 0.0380 S13: 0.0232 REMARK 3 S21: 0.0125 S22: 0.0136 S23: -0.0322 REMARK 3 S31: -0.0016 S32: 0.0302 S33: -0.0033 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 : E 457 E 602 REMARK 3 ORIGIN FOR THE GROUP (A): 13.8665 34.9701 70.6366 REMARK 3 T TENSOR REMARK 3 T11: 0.1228 T22: 0.1117 REMARK 3 T33: 0.0552 T12: 0.0110 REMARK 3 T13: -0.0025 T23: 0.0044 REMARK 3 L TENSOR REMARK 3 L11: 0.3417 L22: 0.3459 REMARK 3 L33: 0.1698 L12: -0.0734 REMARK 3 L13: 0.0632 L23: -0.2420 REMARK 3 S TENSOR REMARK 3 S11: 0.0167 S12: 0.0029 S13: 0.0279 REMARK 3 S21: 0.0307 S22: -0.0021 S23: 0.0205 REMARK 3 S31: -0.0231 S32: -0.0007 S33: -0.0147 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 : F 459 F 602 REMARK 3 ORIGIN FOR THE GROUP (A): -8.3700 31.0414 78.9489 REMARK 3 T TENSOR REMARK 3 T11: 0.1496 T22: 0.1072 REMARK 3 T33: 0.0607 T12: -0.0074 REMARK 3 T13: -0.0247 T23: 0.0021 REMARK 3 L TENSOR REMARK 3 L11: 0.5416 L22: 0.0981 REMARK 3 L33: 0.0129 L12: -0.0330 REMARK 3 L13: -0.0772 L23: 0.0042 REMARK 3 S TENSOR REMARK 3 S11: -0.0040 S12: -0.0164 S13: -0.0440 REMARK 3 S21: 0.0657 S22: 0.0045 S23: 0.0512 REMARK 3 S31: 0.0099 S32: -0.0089 S33: -0.0005 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 : G 1 G 109 REMARK 3 ORIGIN FOR THE GROUP (A): -4.4400 12.5680 57.5806 REMARK 3 T TENSOR REMARK 3 T11: 0.1419 T22: 0.1466 REMARK 3 T33: 0.0578 T12: -0.0003 REMARK 3 T13: -0.0136 T23: 0.0062 REMARK 3 L TENSOR REMARK 3 L11: 0.0366 L22: 0.3696 REMARK 3 L33: 0.2010 L12: -0.1132 REMARK 3 L13: -0.0855 L23: 0.2612 REMARK 3 S TENSOR REMARK 3 S11: -0.0160 S12: -0.0088 S13: -0.0015 REMARK 3 S21: 0.0050 S22: 0.0122 S23: 0.0177 REMARK 3 S31: 0.0508 S32: 0.0129 S33: 0.0037 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 : H 2 H 109 REMARK 3 ORIGIN FOR THE GROUP (A): 17.6171 20.9698 94.8178 REMARK 3 T TENSOR REMARK 3 T11: 0.1665 T22: 0.1293 REMARK 3 T33: 0.0917 T12: 0.0049 REMARK 3 T13: 0.0037 T23: 0.0047 REMARK 3 L TENSOR REMARK 3 L11: 0.1154 L22: 0.6584 REMARK 3 L33: 0.4923 L12: 0.0675 REMARK 3 L13: 0.2190 L23: 0.0325 REMARK 3 S TENSOR REMARK 3 S11: -0.0392 S12: 0.0530 S13: -0.0159 REMARK 3 S21: 0.0160 S22: 0.0519 S23: 0.0615 REMARK 3 S31: 0.0106 S32: 0.1189 S33: -0.0127 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 9IMX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 08-JUL-24. REMARK 100 THE DEPOSITION ID IS D_1300049175. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 05-JUN-24 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRF REMARK 200 BEAMLINE : BL02U1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.979 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROCESS REMARK 200 DATA SCALING SOFTWARE : AUTOPROCESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70266 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200 REMARK 200 RESOLUTION RANGE LOW (A) : 66.220 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6 REMARK 200 DATA REDUNDANCY : 6.900 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 4.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.31 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL 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: PHENIX REMARK 200 STARTING MODEL: 3GGQ,7KN5 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.34 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 6% ISOPROPANOL, 0.1M SODIUM ACETATE PH REMARK 280 4.5, 20% PEG MME550, EVAPORATION, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 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 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 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4 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 APPLY THE FOLLOWING TO CHAINS: A, C 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350 REMARK 350 BIOMOLECULE: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, G 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: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, H 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 603 REMARK 465 HIS A 604 REMARK 465 SER A 605 REMARK 465 VAL A 606 REMARK 465 ALA B 457 REMARK 465 PRO B 458 REMARK 465 PRO B 603 REMARK 465 HIS B 604 REMARK 465 SER B 605 REMARK 465 VAL B 606 REMARK 465 VAL C 12 REMARK 465 GLN C 13 REMARK 465 PRO C 14 REMARK 465 GLY C 15 REMARK 465 GLY C 16 REMARK 465 SER C 17 REMARK 465 LEU C 18 REMARK 465 ARG C 19 REMARK 465 ARG C 38 REMARK 465 GLN C 39 REMARK 465 ALA C 40 REMARK 465 PRO C 41 REMARK 465 GLY C 42 REMARK 465 LYS C 43 REMARK 465 GLU C 44 REMARK 465 ARG C 45 REMARK 465 GLU C 46 REMARK 465 GLN C 80A REMARK 465 MET C 80B REMARK 465 SER C 80C REMARK 465 SER C 80D REMARK 465 LEU C 80E REMARK 465 GLN C 80F REMARK 465 PRO C 80G REMARK 465 GLU C 80H REMARK 465 ASP C 80I REMARK 465 THR C 110 REMARK 465 VAL C 111 REMARK 465 SER C 112 REMARK 465 SER C 113 REMARK 465 HIS C 114 REMARK 465 HIS C 115 REMARK 465 HIS C 116 REMARK 465 HIS C 117 REMARK 465 HIS C 118 REMARK 465 HIS C 119 REMARK 465 ASP D 1 REMARK 465 VAL D 12 REMARK 465 GLN D 13 REMARK 465 PRO D 14 REMARK 465 GLY D 15 REMARK 465 GLY D 16 REMARK 465 SER D 17 REMARK 465 LEU D 18 REMARK 465 ARG D 19 REMARK 465 ARG D 38 REMARK 465 GLN D 39 REMARK 465 ALA D 40 REMARK 465 PRO D 41 REMARK 465 GLY D 42 REMARK 465 LYS D 43 REMARK 465 GLU D 44 REMARK 465 ARG D 45 REMARK 465 GLU D 46 REMARK 465 GLN D 80A REMARK 465 MET D 80B REMARK 465 SER D 80C REMARK 465 SER D 80D REMARK 465 LEU D 80E REMARK 465 GLN D 80F REMARK 465 PRO D 80G REMARK 465 GLU D 80H REMARK 465 ASP D 80I REMARK 465 THR D 110 REMARK 465 VAL D 111 REMARK 465 SER D 112 REMARK 465 SER D 113 REMARK 465 HIS D 114 REMARK 465 HIS D 115 REMARK 465 HIS D 116 REMARK 465 HIS D 117 REMARK 465 HIS D 118 REMARK 465 HIS D 119 REMARK 465 PRO E 603 REMARK 465 HIS E 604 REMARK 465 SER E 605 REMARK 465 VAL E 606 REMARK 465 ALA F 457 REMARK 465 PRO F 458 REMARK 465 PRO F 603 REMARK 465 HIS F 604 REMARK 465 SER F 605 REMARK 465 VAL F 606 REMARK 465 VAL G 12 REMARK 465 GLN G 13 REMARK 465 PRO G 14 REMARK 465 GLY G 15 REMARK 465 GLY G 16 REMARK 465 SER G 17 REMARK 465 LEU G 18 REMARK 465 ARG G 19 REMARK 465 ARG G 38 REMARK 465 GLN G 39 REMARK 465 ALA G 40 REMARK 465 PRO G 41 REMARK 465 GLY G 42 REMARK 465 LYS G 43 REMARK 465 GLU G 44 REMARK 465 ARG G 45 REMARK 465 GLU G 46 REMARK 465 GLN G 80A REMARK 465 MET G 80B REMARK 465 SER G 80C REMARK 465 SER G 80D REMARK 465 LEU G 80E REMARK 465 GLN G 80F REMARK 465 PRO G 80G REMARK 465 GLU G 80H REMARK 465 ASP G 80I REMARK 465 THR G 110 REMARK 465 VAL G 111 REMARK 465 SER G 112 REMARK 465 SER G 113 REMARK 465 HIS G 114 REMARK 465 HIS G 115 REMARK 465 HIS G 116 REMARK 465 HIS G 117 REMARK 465 HIS G 118 REMARK 465 HIS G 119 REMARK 465 ASP H 1 REMARK 465 VAL H 12 REMARK 465 GLN H 13 REMARK 465 PRO H 14 REMARK 465 GLY H 15 REMARK 465 GLY H 16 REMARK 465 SER H 17 REMARK 465 LEU H 18 REMARK 465 ARG H 19 REMARK 465 ARG H 38 REMARK 465 GLN H 39 REMARK 465 ALA H 40 REMARK 465 PRO H 41 REMARK 465 GLY H 42 REMARK 465 LYS H 43 REMARK 465 GLU H 44 REMARK 465 ARG H 45 REMARK 465 GLU H 46 REMARK 465 GLN H 80A REMARK 465 MET H 80B REMARK 465 SER H 80C REMARK 465 SER H 80D REMARK 465 LEU H 80E REMARK 465 GLN H 80F REMARK 465 PRO H 80G REMARK 465 GLU H 80H REMARK 465 ASP H 80I REMARK 465 THR H 110 REMARK 465 VAL H 111 REMARK 465 SER H 112 REMARK 465 SER H 113 REMARK 465 HIS H 114 REMARK 465 HIS H 115 REMARK 465 HIS H 116 REMARK 465 HIS H 117 REMARK 465 HIS H 118 REMARK 465 HIS H 119 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 OG SER F 483 O HOH F 701 1.65 REMARK 500 OH TYR C 79 O HOH C 201 1.67 REMARK 500 SG CYS D 22 SG CYS D 92 1.67 REMARK 500 O HOH A 718 O HOH A 722 1.74 REMARK 500 N ALA C 60 O HOH C 202 1.84 REMARK 500 O GLN A 530 O HOH A 701 1.87 REMARK 500 O VAL A 492 O HOH A 702 1.87 REMARK 500 OG1 THR E 552 O HOH E 701 1.88 REMARK 500 OH TYR E 532 O HOH E 702 1.89 REMARK 500 OD1 ASP G 1 OG1 THR G 26 1.90 REMARK 500 O VAL F 503 O HOH F 702 1.90 REMARK 500 O ILE H 34 O HOH H 201 1.91 REMARK 500 OD1 ASP D 61 O HOH D 201 1.92 REMARK 500 O VAL B 503 O HOH B 701 1.92 REMARK 500 O THR A 505 O HOH A 703 1.95 REMARK 500 ND1 HIS B 577 O HOH B 702 1.97 REMARK 500 N LEU C 80 O HOH C 203 1.99 REMARK 500 C VAL B 503 O HOH B 701 1.99 REMARK 500 OD2 ASP G 30 O HOH G 201 2.00 REMARK 500 O GLU A 549 O HOH A 704 2.03 REMARK 500 O GLU B 572 O HOH B 702 2.03 REMARK 500 NE2 GLN B 531 O HOH B 703 2.04 REMARK 500 OG1 THR H 87 O HOH H 202 2.04 REMARK 500 OG1 THR E 520 O HOH E 703 2.04 REMARK 500 O ALA A 457 N SER A 459 2.04 REMARK 500 N GLU F 549 O HOH F 703 2.05 REMARK 500 O HOH A 713 O HOH A 721 2.06 REMARK 500 OG SER C 70 O HOH C 204 2.06 REMARK 500 O HOH F 708 O HOH F 709 2.06 REMARK 500 NH2 ARG B 524 OE1 GLN G 105 2.07 REMARK 500 O HOH E 708 O HOH E 713 2.07 REMARK 500 OD2 ASP B 481 O HOH B 704 2.08 REMARK 500 O THR A 553 OG SER B 566 2.09 REMARK 500 OH TYR F 485 OE2 GLU F 572 2.10 REMARK 500 OE1 GLN B 531 O HOH B 703 2.10 REMARK 500 CA ALA A 504 O HOH B 701 2.12 REMARK 500 O LEU F 588 O HOH F 704 2.14 REMARK 500 O HOH C 208 O HOH C 215 2.16 REMARK 500 O SER C 25 N PHE C 27 2.16 REMARK 500 ND2 ASN F 468 NH1 ARG F 542 2.17 REMARK 500 NZ LYS E 544 O ASN E 560 2.17 REMARK 500 OD1 ASP C 1 O HOH C 205 2.18 REMARK 500 OD1 ASP A 522 OH TYR C 32 2.18 REMARK 500 O SER H 25 N PHE H 27 2.19 REMARK 500 O SER D 25 N PHE D 27 2.19 REMARK 500 OG1 THR F 552 O HOH F 703 2.19 REMARK 500 OD1 ASP E 522 OH TYR G 32 2.19 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 NZ LYS C 75 OG1 THR C 77 2655 1.98 REMARK 500 O LYS C 75 NZ LYS C 75 2655 2.11 REMARK 500 REMARK 500 REMARK: NULL 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 ARG F 542 NE - CZ - NH1 ANGL. DEV. = -4.0 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 PRO A 458 88.41 -39.70 REMARK 500 ALA A 477 41.37 70.62 REMARK 500 SER A 483 -35.59 -145.96 REMARK 500 ASP A 515 75.64 -64.21 REMARK 500 PRO A 525 178.90 -52.94 REMARK 500 SER A 527 157.83 -46.59 REMARK 500 THR A 552 -166.18 41.78 REMARK 500 THR A 553 23.27 -152.55 REMARK 500 THR A 585 -158.15 -152.59 REMARK 500 PRO A 592 70.41 -48.06 REMARK 500 SER A 594 119.45 57.53 REMARK 500 ARG B 460 85.08 -163.19 REMARK 500 ALA B 477 39.96 74.54 REMARK 500 SER B 483 -38.72 -150.95 REMARK 500 THR B 484 -60.33 -121.64 REMARK 500 ASP B 515 78.14 -67.86 REMARK 500 PRO B 525 -176.82 -50.41 REMARK 500 THR B 552 -154.84 -98.66 REMARK 500 THR B 553 31.81 -144.67 REMARK 500 THR B 585 -154.95 -160.23 REMARK 500 PRO B 592 76.97 -55.88 REMARK 500 SER B 594 119.05 63.65 REMARK 500 THR C 26 -67.38 41.86 REMARK 500 THR C 57 -91.07 66.52 REMARK 500 ASP C 58 158.92 70.51 REMARK 500 TYR C 59 -45.65 -145.68 REMARK 500 LYS C 64 -19.37 -49.26 REMARK 500 TRP C 97 -115.58 -85.58 REMARK 500 TYR C 100G 18.79 -68.66 REMARK 500 THR D 26 -69.14 42.20 REMARK 500 THR D 57 -96.76 66.44 REMARK 500 ASP D 58 162.54 70.05 REMARK 500 TYR D 59 -64.93 -143.47 REMARK 500 SER D 62 -47.87 95.95 REMARK 500 TRP D 97 -125.71 -71.67 REMARK 500 TYR D 100G 17.26 -69.94 REMARK 500 SER E 483 -34.79 -146.66 REMARK 500 ASP E 515 75.97 -62.10 REMARK 500 PRO E 525 -177.77 -52.65 REMARK 500 SER E 527 160.78 -47.99 REMARK 500 THR E 552 -162.93 53.59 REMARK 500 THR E 553 19.68 -147.10 REMARK 500 ALA E 574 -174.14 -172.75 REMARK 500 ALA E 575 109.26 -49.79 REMARK 500 THR E 585 -158.69 -156.92 REMARK 500 PRO E 592 70.83 -50.00 REMARK 500 SER E 594 120.50 64.15 REMARK 500 ARG F 460 85.53 179.23 REMARK 500 SER F 483 -34.25 -145.40 REMARK 500 SER F 487 -169.90 -127.61 REMARK 500 REMARK 500 THIS ENTRY HAS 70 RAMACHANDRAN OUTLIERS. 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 TRP H 97 ALA H 98 -147.10 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG A 460 0.10 SIDE CHAIN REMARK 500 ARG A 524 0.07 SIDE CHAIN REMARK 500 ARG A 578 0.10 SIDE CHAIN REMARK 500 ARG B 542 0.10 SIDE CHAIN REMARK 500 ARG C 53 0.09 SIDE CHAIN REMARK 500 ARG C 66 0.10 SIDE CHAIN REMARK 500 ARG C 71 0.09 SIDE CHAIN REMARK 500 ARG C 100F 0.11 SIDE CHAIN REMARK 500 ARG E 460 0.10 SIDE CHAIN REMARK 500 ARG E 578 0.10 SIDE CHAIN REMARK 500 ARG F 460 0.08 SIDE CHAIN REMARK 500 ARG H 66 0.07 SIDE CHAIN REMARK 500 ARG H 100F 0.12 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 723 DISTANCE = 11.14 ANGSTROMS REMARK 525 HOH A 724 DISTANCE = 12.17 ANGSTROMS REMARK 525 HOH B 722 DISTANCE = 7.18 ANGSTROMS REMARK 525 HOH F 715 DISTANCE = 5.83 ANGSTROMS DBREF 9IMX A 457 606 UNP P33426 CAPSD_HEVPA 457 606 DBREF 9IMX B 457 606 UNP P33426 CAPSD_HEVPA 457 606 DBREF 9IMX C 1 119 PDB 9IMX 9IMX 1 119 DBREF 9IMX D 1 119 PDB 9IMX 9IMX 1 119 DBREF 9IMX E 457 606 UNP P33426 CAPSD_HEVPA 457 606 DBREF 9IMX F 457 606 UNP P33426 CAPSD_HEVPA 457 606 DBREF 9IMX G 1 119 PDB 9IMX 9IMX 1 119 DBREF 9IMX H 1 119 PDB 9IMX 9IMX 1 119 SEQRES 1 A 150 ALA PRO SER ARG PRO PHE SER VAL LEU ARG ALA ASN ASP SEQRES 2 A 150 VAL LEU TRP LEU SER LEU THR ALA ALA GLU TYR ASP GLN SEQRES 3 A 150 SER THR TYR GLY SER SER THR GLY PRO VAL TYR VAL SER SEQRES 4 A 150 ASP SER VAL THR LEU VAL ASN VAL ALA THR GLY ALA GLN SEQRES 5 A 150 ALA VAL ALA ARG SER LEU ASP TRP THR LYS VAL THR LEU SEQRES 6 A 150 ASP GLY ARG PRO LEU SER THR ILE GLN GLN TYR SER LYS SEQRES 7 A 150 THR PHE PHE VAL LEU PRO LEU ARG GLY LYS LEU SER PHE SEQRES 8 A 150 TRP GLU ALA GLY THR THR LYS ALA GLY TYR PRO TYR ASN SEQRES 9 A 150 TYR ASN THR THR ALA SER ASP GLN LEU LEU VAL GLU ASN SEQRES 10 A 150 ALA ALA GLY HIS ARG VAL ALA ILE SER THR TYR THR THR SEQRES 11 A 150 SER LEU GLY ALA GLY PRO VAL SER ILE SER ALA VAL ALA SEQRES 12 A 150 VAL LEU ALA PRO HIS SER VAL SEQRES 1 B 150 ALA PRO SER ARG PRO PHE SER VAL LEU ARG ALA ASN ASP SEQRES 2 B 150 VAL LEU TRP LEU SER LEU THR ALA ALA GLU TYR ASP GLN SEQRES 3 B 150 SER THR TYR GLY SER SER THR GLY PRO VAL TYR VAL SER SEQRES 4 B 150 ASP SER VAL THR LEU VAL ASN VAL ALA THR GLY ALA GLN SEQRES 5 B 150 ALA VAL ALA ARG SER LEU ASP TRP THR LYS VAL THR LEU SEQRES 6 B 150 ASP GLY ARG PRO LEU SER THR ILE GLN GLN TYR SER LYS SEQRES 7 B 150 THR PHE PHE VAL LEU PRO LEU ARG GLY LYS LEU SER PHE SEQRES 8 B 150 TRP GLU ALA GLY THR THR LYS ALA GLY TYR PRO TYR ASN SEQRES 9 B 150 TYR ASN THR THR ALA SER ASP GLN LEU LEU VAL GLU ASN SEQRES 10 B 150 ALA ALA GLY HIS ARG VAL ALA ILE SER THR TYR THR THR SEQRES 11 B 150 SER LEU GLY ALA GLY PRO VAL SER ILE SER ALA VAL ALA SEQRES 12 B 150 VAL LEU ALA PRO HIS SER VAL SEQRES 1 C 132 ASP VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 C 132 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER THR SEQRES 3 C 132 PHE THR LEU ASP TYR TYR ALA ILE GLY TRP PHE ARG GLN SEQRES 4 C 132 ALA PRO GLY LYS GLU ARG GLU GLY VAL SER CYS ILE SER SEQRES 5 C 132 SER ARG GLY GLY SER THR ASP TYR ALA ASP SER VAL LYS SEQRES 6 C 132 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 C 132 VAL TYR LEU GLN MET SER SER LEU GLN PRO GLU ASP THR SEQRES 8 C 132 ALA VAL TYR TYR CYS ALA ALA ALA GLY TRP ALA GLY TYR SEQRES 9 C 132 GLY CYS PRO PRO ASN ARG TYR GLU TYR ASP TYR TRP GLY SEQRES 10 C 132 GLN GLY THR GLN VAL THR VAL SER SER HIS HIS HIS HIS SEQRES 11 C 132 HIS HIS SEQRES 1 D 132 ASP VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 D 132 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER THR SEQRES 3 D 132 PHE THR LEU ASP TYR TYR ALA ILE GLY TRP PHE ARG GLN SEQRES 4 D 132 ALA PRO GLY LYS GLU ARG GLU GLY VAL SER CYS ILE SER SEQRES 5 D 132 SER ARG GLY GLY SER THR ASP TYR ALA ASP SER VAL LYS SEQRES 6 D 132 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 D 132 VAL TYR LEU GLN MET SER SER LEU GLN PRO GLU ASP THR SEQRES 8 D 132 ALA VAL TYR TYR CYS ALA ALA ALA GLY TRP ALA GLY TYR SEQRES 9 D 132 GLY CYS PRO PRO ASN ARG TYR GLU TYR ASP TYR TRP GLY SEQRES 10 D 132 GLN GLY THR GLN VAL THR VAL SER SER HIS HIS HIS HIS SEQRES 11 D 132 HIS HIS SEQRES 1 E 150 ALA PRO SER ARG PRO PHE SER VAL LEU ARG ALA ASN ASP SEQRES 2 E 150 VAL LEU TRP LEU SER LEU THR ALA ALA GLU TYR ASP GLN SEQRES 3 E 150 SER THR TYR GLY SER SER THR GLY PRO VAL TYR VAL SER SEQRES 4 E 150 ASP SER VAL THR LEU VAL ASN VAL ALA THR GLY ALA GLN SEQRES 5 E 150 ALA VAL ALA ARG SER LEU ASP TRP THR LYS VAL THR LEU SEQRES 6 E 150 ASP GLY ARG PRO LEU SER THR ILE GLN GLN TYR SER LYS SEQRES 7 E 150 THR PHE PHE VAL LEU PRO LEU ARG GLY LYS LEU SER PHE SEQRES 8 E 150 TRP GLU ALA GLY THR THR LYS ALA GLY TYR PRO TYR ASN SEQRES 9 E 150 TYR ASN THR THR ALA SER ASP GLN LEU LEU VAL GLU ASN SEQRES 10 E 150 ALA ALA GLY HIS ARG VAL ALA ILE SER THR TYR THR THR SEQRES 11 E 150 SER LEU GLY ALA GLY PRO VAL SER ILE SER ALA VAL ALA SEQRES 12 E 150 VAL LEU ALA PRO HIS SER VAL SEQRES 1 F 150 ALA PRO SER ARG PRO PHE SER VAL LEU ARG ALA ASN ASP SEQRES 2 F 150 VAL LEU TRP LEU SER LEU THR ALA ALA GLU TYR ASP GLN SEQRES 3 F 150 SER THR TYR GLY SER SER THR GLY PRO VAL TYR VAL SER SEQRES 4 F 150 ASP SER VAL THR LEU VAL ASN VAL ALA THR GLY ALA GLN SEQRES 5 F 150 ALA VAL ALA ARG SER LEU ASP TRP THR LYS VAL THR LEU SEQRES 6 F 150 ASP GLY ARG PRO LEU SER THR ILE GLN GLN TYR SER LYS SEQRES 7 F 150 THR PHE PHE VAL LEU PRO LEU ARG GLY LYS LEU SER PHE SEQRES 8 F 150 TRP GLU ALA GLY THR THR LYS ALA GLY TYR PRO TYR ASN SEQRES 9 F 150 TYR ASN THR THR ALA SER ASP GLN LEU LEU VAL GLU ASN SEQRES 10 F 150 ALA ALA GLY HIS ARG VAL ALA ILE SER THR TYR THR THR SEQRES 11 F 150 SER LEU GLY ALA GLY PRO VAL SER ILE SER ALA VAL ALA SEQRES 12 F 150 VAL LEU ALA PRO HIS SER VAL SEQRES 1 G 132 ASP VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 G 132 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER THR SEQRES 3 G 132 PHE THR LEU ASP TYR TYR ALA ILE GLY TRP PHE ARG GLN SEQRES 4 G 132 ALA PRO GLY LYS GLU ARG GLU GLY VAL SER CYS ILE SER SEQRES 5 G 132 SER ARG GLY GLY SER THR ASP TYR ALA ASP SER VAL LYS SEQRES 6 G 132 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 G 132 VAL TYR LEU GLN MET SER SER LEU GLN PRO GLU ASP THR SEQRES 8 G 132 ALA VAL TYR TYR CYS ALA ALA ALA GLY TRP ALA GLY TYR SEQRES 9 G 132 GLY CYS PRO PRO ASN ARG TYR GLU TYR ASP TYR TRP GLY SEQRES 10 G 132 GLN GLY THR GLN VAL THR VAL SER SER HIS HIS HIS HIS SEQRES 11 G 132 HIS HIS SEQRES 1 H 132 ASP VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 132 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER THR SEQRES 3 H 132 PHE THR LEU ASP TYR TYR ALA ILE GLY TRP PHE ARG GLN SEQRES 4 H 132 ALA PRO GLY LYS GLU ARG GLU GLY VAL SER CYS ILE SER SEQRES 5 H 132 SER ARG GLY GLY SER THR ASP TYR ALA ASP SER VAL LYS SEQRES 6 H 132 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 H 132 VAL TYR LEU GLN MET SER SER LEU GLN PRO GLU ASP THR SEQRES 8 H 132 ALA VAL TYR TYR CYS ALA ALA ALA GLY TRP ALA GLY TYR SEQRES 9 H 132 GLY CYS PRO PRO ASN ARG TYR GLU TYR ASP TYR TRP GLY SEQRES 10 H 132 GLN GLY THR GLN VAL THR VAL SER SER HIS HIS HIS HIS SEQRES 11 H 132 HIS HIS FORMUL 9 HOH *118(H2 O) HELIX 1 AA1 ASP A 515 LYS A 518 5 4 HELIX 2 AA2 ASP B 515 VAL B 519 5 5 HELIX 3 AA3 SER C 62 ARG C 66 5 5 HELIX 4 AA4 THR D 28 TYR D 32 5 5 HELIX 5 AA5 SER D 62 PHE D 67 1 6 HELIX 6 AA6 ASP E 515 VAL E 519 5 5 HELIX 7 AA7 SER G 62 ARG G 66 5 5 HELIX 8 AA8 SER H 62 PHE H 67 1 6 SHEET 1 AA1 3 VAL A 464 LEU A 465 0 SHEET 2 AA1 3 THR A 520 LEU A 521 1 O THR A 520 N LEU A 465 SHEET 3 AA1 3 ARG A 524 PRO A 525 -1 O ARG A 524 N LEU A 521 SHEET 1 AA2 5 GLN A 508 VAL A 510 0 SHEET 2 AA2 5 SER A 497 ASN A 502 -1 N LEU A 500 O ALA A 509 SHEET 3 AA2 5 VAL A 470 THR A 476 -1 N TRP A 472 O VAL A 501 SHEET 4 AA2 5 ILE A 595 VAL A 600 -1 O ALA A 599 N LEU A 471 SHEET 5 AA2 5 SER A 546 GLU A 549 -1 N TRP A 548 O SER A 596 SHEET 1 AA3 6 GLU A 479 ASP A 481 0 SHEET 2 AA3 6 VAL A 492 SER A 495 -1 O VAL A 492 N ASP A 481 SHEET 3 AA3 6 VAL A 579 SER A 582 -1 O ILE A 581 N TYR A 493 SHEET 4 AA3 6 GLN A 568 GLU A 572 -1 N LEU A 570 O ALA A 580 SHEET 5 AA3 6 LYS A 534 PRO A 540 -1 N PHE A 537 O VAL A 571 SHEET 6 AA3 6 THR A 528 GLN A 531 -1 N GLN A 531 O LYS A 534 SHEET 1 AA4 2 VAL B 464 LEU B 465 0 SHEET 2 AA4 2 THR B 520 LEU B 521 1 O THR B 520 N LEU B 465 SHEET 1 AA5 5 GLN B 508 VAL B 510 0 SHEET 2 AA5 5 SER B 497 ASN B 502 -1 N LEU B 500 O ALA B 509 SHEET 3 AA5 5 VAL B 470 THR B 476 -1 N SER B 474 O THR B 499 SHEET 4 AA5 5 ILE B 595 VAL B 600 -1 O ALA B 599 N LEU B 471 SHEET 5 AA5 5 SER B 546 GLU B 549 -1 N SER B 546 O VAL B 598 SHEET 1 AA6 7 GLU B 479 ASP B 481 0 SHEET 2 AA6 7 VAL B 492 SER B 495 -1 O VAL B 492 N ASP B 481 SHEET 3 AA6 7 VAL B 579 SER B 582 -1 O VAL B 579 N SER B 495 SHEET 4 AA6 7 GLN B 568 GLU B 572 -1 N LEU B 570 O ALA B 580 SHEET 5 AA6 7 LYS B 534 PRO B 540 -1 N PHE B 537 O VAL B 571 SHEET 6 AA6 7 THR B 528 GLN B 531 -1 N GLN B 531 O LYS B 534 SHEET 7 AA6 7 GLY G 9 LEU G 11 1 O GLY G 9 N THR B 528 SHEET 1 AA7 2 LEU C 4 GLU C 6 0 SHEET 2 AA7 2 CYS C 22 ALA C 24 -1 O ALA C 23 N GLN C 5 SHEET 1 AA8 3 CYS C 50 ILE C 51 0 SHEET 2 AA8 3 ALA C 33 TRP C 36 -1 N ILE C 34 O ILE C 51 SHEET 3 AA8 3 CYS C 92 ALA C 95 -1 O ALA C 95 N ALA C 33 SHEET 1 AA9 2 GLN D 5 SER D 7 0 SHEET 2 AA9 2 SER D 21 ALA D 23 -1 O ALA D 23 N GLN D 5 SHEET 1 AB1 3 CYS D 50 ILE D 51 0 SHEET 2 AB1 3 ALA D 33 TRP D 36 -1 N ILE D 34 O ILE D 51 SHEET 3 AB1 3 CYS D 92 ALA D 95 -1 O ALA D 95 N ALA D 33 SHEET 1 AB2 2 VAL D 89 TYR D 90 0 SHEET 2 AB2 2 THR D 107 GLN D 108 -1 O THR D 107 N TYR D 90 SHEET 1 AB3 2 VAL E 464 LEU E 465 0 SHEET 2 AB3 2 THR E 520 LEU E 521 1 O THR E 520 N LEU E 465 SHEET 1 AB4 6 GLN E 508 VAL E 510 0 SHEET 2 AB4 6 SER E 497 ASN E 502 -1 N LEU E 500 O ALA E 509 SHEET 3 AB4 6 VAL E 470 THR E 476 -1 N TRP E 472 O VAL E 501 SHEET 4 AB4 6 ILE E 595 VAL E 600 -1 O ALA E 597 N LEU E 473 SHEET 5 AB4 6 SER E 546 GLU E 549 -1 N TRP E 548 O SER E 596 SHEET 6 AB4 6 ALA E 555 GLY E 556 -1 O GLY E 556 N PHE E 547 SHEET 1 AB5 6 GLU E 479 ASP E 481 0 SHEET 2 AB5 6 VAL E 492 SER E 495 -1 O VAL E 492 N ASP E 481 SHEET 3 AB5 6 VAL E 579 SER E 582 -1 O ILE E 581 N TYR E 493 SHEET 4 AB5 6 GLN E 568 ASN E 573 -1 N LEU E 570 O ALA E 580 SHEET 5 AB5 6 LYS E 534 PRO E 540 -1 N THR E 535 O ASN E 573 SHEET 6 AB5 6 THR E 528 GLN E 531 -1 N GLN E 531 O LYS E 534 SHEET 1 AB6 2 VAL F 464 LEU F 465 0 SHEET 2 AB6 2 THR F 520 LEU F 521 1 O THR F 520 N LEU F 465 SHEET 1 AB7 5 GLN F 508 VAL F 510 0 SHEET 2 AB7 5 SER F 497 ASN F 502 -1 N LEU F 500 O ALA F 509 SHEET 3 AB7 5 VAL F 470 THR F 476 -1 N SER F 474 O THR F 499 SHEET 4 AB7 5 ILE F 595 VAL F 600 -1 O ALA F 599 N LEU F 471 SHEET 5 AB7 5 SER F 546 GLU F 549 -1 N SER F 546 O VAL F 598 SHEET 1 AB8 6 GLU F 479 ASP F 481 0 SHEET 2 AB8 6 VAL F 492 SER F 495 -1 O VAL F 492 N ASP F 481 SHEET 3 AB8 6 VAL F 579 SER F 582 -1 O ILE F 581 N TYR F 493 SHEET 4 AB8 6 GLN F 568 GLU F 572 -1 N LEU F 570 O ALA F 580 SHEET 5 AB8 6 LYS F 534 PRO F 540 -1 N PHE F 537 O VAL F 571 SHEET 6 AB8 6 THR F 528 GLN F 531 -1 N GLN F 531 O LYS F 534 SHEET 1 AB9 2 LEU G 4 SER G 7 0 SHEET 2 AB9 2 SER G 21 ALA G 24 -1 O ALA G 23 N GLN G 5 SHEET 1 AC1 3 CYS G 50 ILE G 51 0 SHEET 2 AC1 3 ALA G 33 TRP G 36 -1 N ILE G 34 O ILE G 51 SHEET 3 AC1 3 CYS G 92 ALA G 95 -1 O ALA G 95 N ALA G 33 SHEET 1 AC2 2 LEU H 4 SER H 7 0 SHEET 2 AC2 2 SER H 21 ALA H 24 -1 O ALA H 23 N GLN H 5 SHEET 1 AC3 3 CYS H 50 ILE H 51 0 SHEET 2 AC3 3 ALA H 33 TRP H 36 -1 N ILE H 34 O ILE H 51 SHEET 3 AC3 3 CYS H 92 ALA H 95 -1 O ALA H 95 N ALA H 33 SHEET 1 AC4 2 VAL H 89 TYR H 90 0 SHEET 2 AC4 2 THR H 107 GLN H 108 -1 O THR H 107 N TYR H 90 SSBOND 1 CYS C 22 CYS C 92 1555 1555 1.98 SSBOND 2 CYS C 50 CYS C 100B 1555 1555 2.09 SSBOND 3 CYS D 50 CYS D 100B 1555 1555 2.01 SSBOND 4 CYS G 22 CYS G 92 1555 1555 2.00 SSBOND 5 CYS G 50 CYS G 100B 1555 1555 2.16 SSBOND 6 CYS H 22 CYS H 92 1555 1555 1.86 SSBOND 7 CYS H 50 CYS H 100B 1555 1555 2.07 CRYST1 51.393 51.402 265.172 90.00 92.74 90.00 P 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 0.019458 0.000000 0.000930 0.00000 SCALE2 0.000000 0.019454 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003775 0.00000