HEADER IMMUNE SYSTEM 05-JUN-24 9FM0 TITLE HUMAN ANTIBODY (FAB) AND P. AERUGINOSA (T3SS) PROTEIN PCRV-FRAGMENT TITLE 2 COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: HUMAN FAB HEAVY CHAIN (FABHC) V-REGION; COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HUMAN FAB LIGHT CHAIN (FABLC) V-REGION; COMPND 7 CHAIN: C, D; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: TYPE III SECRETION PROTEIN PCRV; COMPND 11 CHAIN: E, F; COMPND 12 ENGINEERED: YES; COMPND 13 OTHER_DETAILS: N-TER TAG FROM RESIDUE K17 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 CELL: MEMORY B; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: HEK293F; SOURCE 8 EXPRESSION_SYSTEM_ORGAN: KIDNEY; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 CELL: MEMORY B; SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 EXPRESSION_SYSTEM_CELL_LINE: HEK293F; SOURCE 16 EXPRESSION_SYSTEM_TISSUE: KIDNEY; SOURCE 17 MOL_ID: 3; SOURCE 18 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA; SOURCE 19 ORGANISM_TAXID: 287; SOURCE 20 STRAIN: PA01; SOURCE 21 GENE: PCRV, PA1706; SOURCE 22 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 23 EXPRESSION_SYSTEM_TAXID: 469008 KEYWDS HUMAN ANTIBODIES, TYPE III SECRETION SYSTEM, PCRV, VIRULENCE, KEYWDS 2 PSEUDOMONAS, BACTERIAL INFECTION, ANTIMICROBIALS, ANTI-VIRULENCE, KEYWDS 3 MAB, AMR, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR J.M.DESVEAUX,C.CONTRERAS MARTEL,A.DESSEN REVDAT 1 18-JUN-25 9FM0 0 JRNL AUTH J.M.DESVEAUX,E.FAUDRY,C.CONTRERAS-MARTEL,F.CRETIN, JRNL AUTH 2 S.DERGAN-DYLON,A.AMEN,I.BALLY,V.TARDIVY-CASEMAJOR, JRNL AUTH 3 F.CHENAVIER,Y.CASPAR,I.ATTREE,A.DESSEN,P.POIGNARD JRNL TITL HUMAN ANTIBODIES THAT TARGET THE TYPE III SECRETION SYSTEM JRNL TITL 2 OF PSEUDOMONAS AERUGINOSA INHIBIT TRANSLOCON FUNCTION AND JRNL TITL 3 CYTOTOXICITY JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.56 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0425 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.56 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.21 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 3 NUMBER OF REFLECTIONS : 52157 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) : 0.210 REMARK 3 FREE R VALUE : 0.237 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.999 REMARK 3 FREE R VALUE TEST SET COUNT : 2086 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) : 2.56 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.63 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3647 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.25 REMARK 3 BIN R VALUE (WORKING SET) : 0.3940 REMARK 3 BIN FREE R VALUE SET COUNT : 175 REMARK 3 BIN FREE R VALUE : 0.4510 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 8596 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 46 REMARK 3 SOLVENT ATOMS : 392 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 45.86 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.74 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.30600 REMARK 3 B22 (A**2) : -0.23300 REMARK 3 B33 (A**2) : 0.15600 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.47400 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.440 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.262 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.264 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 27.515 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.944 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.920 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8835 ; 0.006 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): 8148 ; 0.001 ; 0.016 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11978 ; 1.266 ; 1.802 REMARK 3 BOND ANGLES OTHERS (DEGREES): 18847 ; 0.456 ; 1.741 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1133 ; 7.449 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 45 ; 5.495 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1417 ;11.536 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1337 ; 0.055 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10459 ; 0.013 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 2021 ; 0.012 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1507 ; 0.203 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 64 ; 0.183 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4226 ; 0.177 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 265 ; 0.243 ; 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): 4536 ; 2.154 ; 2.908 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4536 ; 2.152 ; 2.908 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5660 ; 3.543 ; 5.215 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 5661 ; 3.543 ; 5.215 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4299 ; 2.810 ; 3.238 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 4300 ; 2.810 ; 3.239 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 6315 ; 4.588 ; 5.773 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 6316 ; 4.588 ; 5.774 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 : 3 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 1 A 214 NULL REMARK 3 2 A 1 A 214 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 3 REMARK 3 CHAIN NAMES : A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 3 A 122 A 249 NULL REMARK 3 3 A 122 A 249 NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 6 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 225 REMARK 3 ORIGIN FOR THE GROUP (A): 17.6407 -8.1989 49.7537 REMARK 3 T TENSOR REMARK 3 T11: 0.1030 T22: 0.0208 REMARK 3 T33: 0.2340 T12: -0.0168 REMARK 3 T13: -0.0246 T23: -0.0173 REMARK 3 L TENSOR REMARK 3 L11: 0.9720 L22: 0.4017 REMARK 3 L33: 1.9617 L12: -0.0941 REMARK 3 L13: -0.5340 L23: 0.0407 REMARK 3 S TENSOR REMARK 3 S11: -0.0063 S12: 0.0973 S13: -0.0354 REMARK 3 S21: -0.0472 S22: 0.0173 S23: -0.0725 REMARK 3 S31: 0.0211 S32: 0.0513 S33: -0.0110 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 0 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 ORIGIN FOR THE GROUP (A): -0.8849 63.7661 49.6351 REMARK 3 T TENSOR REMARK 3 T11: 0.0992 T22: 0.0273 REMARK 3 T33: 0.2394 T12: -0.0243 REMARK 3 T13: 0.0029 T23: 0.0243 REMARK 3 L TENSOR REMARK 3 L11: 0.9817 L22: 0.4342 REMARK 3 L33: 1.9425 L12: -0.0678 REMARK 3 L13: 0.4699 L23: -0.0741 REMARK 3 S TENSOR REMARK 3 S11: -0.0298 S12: 0.1251 S13: 0.0524 REMARK 3 S21: -0.0755 S22: 0.0131 S23: 0.0664 REMARK 3 S31: -0.0767 S32: -0.0236 S33: 0.0167 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): 23.3057 7.5298 42.7331 REMARK 3 T TENSOR REMARK 3 T11: 0.1482 T22: 0.1204 REMARK 3 T33: 0.2728 T12: -0.0056 REMARK 3 T13: -0.0241 T23: 0.0448 REMARK 3 L TENSOR REMARK 3 L11: 0.6695 L22: 0.8005 REMARK 3 L33: 1.3757 L12: 0.1124 REMARK 3 L13: -0.3580 L23: 0.2687 REMARK 3 S TENSOR REMARK 3 S11: 0.0215 S12: 0.2377 S13: 0.0693 REMARK 3 S21: -0.2476 S22: 0.0621 S23: -0.0094 REMARK 3 S31: -0.1567 S32: 0.0096 S33: -0.0836 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): -6.4741 48.0463 42.5650 REMARK 3 T TENSOR REMARK 3 T11: 0.1245 T22: 0.1396 REMARK 3 T33: 0.2670 T12: -0.0128 REMARK 3 T13: 0.0012 T23: -0.0449 REMARK 3 L TENSOR REMARK 3 L11: 0.7216 L22: 0.8253 REMARK 3 L33: 1.7333 L12: 0.1522 REMARK 3 L13: 0.4598 L23: -0.3324 REMARK 3 S TENSOR REMARK 3 S11: 0.0287 S12: 0.2438 S13: -0.0781 REMARK 3 S21: -0.2146 S22: 0.0787 S23: 0.0469 REMARK 3 S31: 0.1725 S32: -0.0197 S33: -0.1074 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): 8.6746 7.3384 88.6407 REMARK 3 T TENSOR REMARK 3 T11: 0.1354 T22: 0.1465 REMARK 3 T33: 0.1835 T12: -0.0125 REMARK 3 T13: -0.0393 T23: -0.0113 REMARK 3 L TENSOR REMARK 3 L11: 1.7968 L22: 3.9159 REMARK 3 L33: 1.6476 L12: -1.2840 REMARK 3 L13: -0.0680 L23: 0.2199 REMARK 3 S TENSOR REMARK 3 S11: -0.0151 S12: -0.1904 S13: 0.0502 REMARK 3 S21: 0.2873 S22: 0.0754 S23: 0.0418 REMARK 3 S31: 0.0279 S32: -0.1130 S33: -0.0604 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): 8.6795 47.9998 88.5453 REMARK 3 T TENSOR REMARK 3 T11: 0.1530 T22: 0.1139 REMARK 3 T33: 0.1828 T12: -0.0111 REMARK 3 T13: 0.0192 T23: 0.0000 REMARK 3 L TENSOR REMARK 3 L11: 1.5133 L22: 2.4248 REMARK 3 L33: 1.8944 L12: -0.2443 REMARK 3 L13: 0.1113 L23: -0.2316 REMARK 3 S TENSOR REMARK 3 S11: 0.0079 S12: -0.0882 S13: -0.0069 REMARK 3 S21: 0.3139 S22: 0.0131 S23: 0.0222 REMARK 3 S31: -0.0694 S32: 0.0378 S33: -0.0209 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 : 1.20 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 THEIR REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 9FM0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-JUN-24. REMARK 100 THE DEPOSITION ID IS D_1292138981. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-APR-23 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 4.5-5.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : MASSIF-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.965459 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS 20220820 REMARK 200 DATA SCALING SOFTWARE : XSCALE 20220820 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52157 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.559 REMARK 200 RESOLUTION RANGE LOW (A) : 49.210 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 200 DATA REDUNDANCY : 3.380 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.20000 REMARK 200 FOR THE DATA SET : 5.0200 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.56 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.71 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2 REMARK 200 DATA REDUNDANCY IN SHELL : 3.30 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 1.53000 REMARK 200 FOR SHELL : 0.720 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER 2.8.3 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: PLATES REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 62.20 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.25 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: MICRO-SEEDING, 0.1 M SODIUM ACETATE PH REMARK 280 5, 25% PEG 1000, 0.001M ZNCL2, PH 5.0, VAPOR DIFFUSION, HANGING REMARK 280 DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,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 46.15400 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 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: 6700 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 25050 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, E 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: 6680 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 25080 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, F REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET E 119 REMARK 465 GLU E 120 REMARK 465 VAL E 121 REMARK 465 MET F 119 REMARK 465 GLU F 120 REMARK 465 VAL F 121 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ALA A 92 169.52 176.77 REMARK 500 GLU A 106 -71.55 -139.46 REMARK 500 ASP A 152 58.63 76.54 REMARK 500 ASN A 163 54.51 37.45 REMARK 500 ALA B 92 170.52 176.33 REMARK 500 GLU B 106 -70.91 -139.24 REMARK 500 ASP B 152 58.17 77.49 REMARK 500 ASN B 163 54.75 37.31 REMARK 500 SER C 30 -122.67 53.91 REMARK 500 THR C 51 -44.02 72.28 REMARK 500 ASN C 138 69.98 60.36 REMARK 500 LYS C 190 -54.00 -121.81 REMARK 500 SER D 30 -122.91 53.14 REMARK 500 THR D 51 -46.05 74.61 REMARK 500 PHE D 83 109.82 -55.32 REMARK 500 ASN D 138 69.35 60.77 REMARK 500 ASP E 165 -158.44 -97.03 REMARK 500 VAL E 172 41.52 -93.10 REMARK 500 ASP F 165 -159.45 -97.67 REMARK 500 VAL F 172 42.16 -93.39 REMARK 500 SER F 202 15.04 -140.83 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 E 128 0.07 SIDE CHAIN REMARK 500 ARG F 128 0.07 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 E 339 DISTANCE = 5.84 ANGSTROMS DBREF 9FM0 A 1 225 PDB 9FM0 9FM0 1 225 DBREF 9FM0 B 1 225 PDB 9FM0 9FM0 1 225 DBREF 9FM0 C 1 214 PDB 9FM0 9FM0 1 214 DBREF 9FM0 D 1 214 PDB 9FM0 9FM0 1 214 DBREF 9FM0 E 132 249 UNP G3XD49 G3XD49_PSEAE 132 249 DBREF 9FM0 F 132 249 UNP G3XD49 G3XD49_PSEAE 132 249 SEQADV 9FM0 MET E 119 UNP G3XD49 INITIATING METHIONINE SEQADV 9FM0 GLU E 120 UNP G3XD49 EXPRESSION TAG SEQADV 9FM0 VAL E 121 UNP G3XD49 EXPRESSION TAG SEQADV 9FM0 ARG E 122 UNP G3XD49 EXPRESSION TAG SEQADV 9FM0 ASN E 123 UNP G3XD49 EXPRESSION TAG SEQADV 9FM0 LEU E 124 UNP G3XD49 EXPRESSION TAG SEQADV 9FM0 ASN E 125 UNP G3XD49 EXPRESSION TAG SEQADV 9FM0 ALA E 126 UNP G3XD49 EXPRESSION TAG SEQADV 9FM0 ALA E 127 UNP G3XD49 EXPRESSION TAG SEQADV 9FM0 ARG E 128 UNP G3XD49 EXPRESSION TAG SEQADV 9FM0 GLU E 129 UNP G3XD49 EXPRESSION TAG SEQADV 9FM0 LEU E 130 UNP G3XD49 EXPRESSION TAG SEQADV 9FM0 PHE E 131 UNP G3XD49 EXPRESSION TAG SEQADV 9FM0 MET F 119 UNP G3XD49 INITIATING METHIONINE SEQADV 9FM0 GLU F 120 UNP G3XD49 EXPRESSION TAG SEQADV 9FM0 VAL F 121 UNP G3XD49 EXPRESSION TAG SEQADV 9FM0 ARG F 122 UNP G3XD49 EXPRESSION TAG SEQADV 9FM0 ASN F 123 UNP G3XD49 EXPRESSION TAG SEQADV 9FM0 LEU F 124 UNP G3XD49 EXPRESSION TAG SEQADV 9FM0 ASN F 125 UNP G3XD49 EXPRESSION TAG SEQADV 9FM0 ALA F 126 UNP G3XD49 EXPRESSION TAG SEQADV 9FM0 ALA F 127 UNP G3XD49 EXPRESSION TAG SEQADV 9FM0 ARG F 128 UNP G3XD49 EXPRESSION TAG SEQADV 9FM0 GLU F 129 UNP G3XD49 EXPRESSION TAG SEQADV 9FM0 LEU F 130 UNP G3XD49 EXPRESSION TAG SEQADV 9FM0 PHE F 131 UNP G3XD49 EXPRESSION TAG SEQRES 1 A 225 GLN VAL GLN LEU LEU GLY SER GLY GLY GLY LEU VAL GLN SEQRES 2 A 225 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 A 225 PHE THR PHE ARG ASN TYR ALA MET ILE TRP VAL ARG GLN SEQRES 4 A 225 ALA PRO GLY LYS GLY LEU ASP TRP VAL SER THR ILE SER SEQRES 5 A 225 GLY THR GLY ASP SER SER ASP TYR ALA ASP SER VAL ARG SEQRES 6 A 225 GLY ARG PHE THR VAL SER ARG ASP ASN SER LYS ASN THR SEQRES 7 A 225 LEU TYR LEU GLU MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 A 225 ALA VAL PHE TYR CYS ALA LYS ASP SER ARG GLY ALA ALA SEQRES 9 A 225 ALA GLU PHE PHE ASP TYR TRP GLY GLN GLY ILE PHE VAL SEQRES 10 A 225 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 A 225 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 A 225 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 A 225 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 A 225 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 A 225 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 A 225 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 A 225 LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO SEQRES 18 A 225 LYS SER CYS ASP SEQRES 1 B 225 GLN VAL GLN LEU LEU GLY SER GLY GLY GLY LEU VAL GLN SEQRES 2 B 225 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 B 225 PHE THR PHE ARG ASN TYR ALA MET ILE TRP VAL ARG GLN SEQRES 4 B 225 ALA PRO GLY LYS GLY LEU ASP TRP VAL SER THR ILE SER SEQRES 5 B 225 GLY THR GLY ASP SER SER ASP TYR ALA ASP SER VAL ARG SEQRES 6 B 225 GLY ARG PHE THR VAL SER ARG ASP ASN SER LYS ASN THR SEQRES 7 B 225 LEU TYR LEU GLU MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 B 225 ALA VAL PHE TYR CYS ALA LYS ASP SER ARG GLY ALA ALA SEQRES 9 B 225 ALA GLU PHE PHE ASP TYR TRP GLY GLN GLY ILE PHE VAL SEQRES 10 B 225 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 B 225 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 B 225 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 B 225 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 B 225 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 B 225 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 B 225 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 B 225 LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO SEQRES 18 B 225 LYS SER CYS ASP SEQRES 1 C 214 ALA ILE ARG MET THR GLN SER PRO SER SER PHE SER ALA SEQRES 2 C 214 SER ILE GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 C 214 GLN GLY ILE SER SER TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4 C 214 PRO GLY LYS ALA PRO ASN LEU LEU ILE TYR ALA THR SER SEQRES 5 C 214 SER LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 C 214 GLY SER GLY THR ASP PHE THR LEU THR ILE THR SER LEU SEQRES 7 C 214 GLN SER GLU ASP PHE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 C 214 TYR SER HIS PRO LEU THR PHE GLY GLY GLY THR LYS VAL SEQRES 9 C 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 C 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 C 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 C 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 C 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 C 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 C 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 C 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 C 214 PHE ASN ARG GLY GLU CYS SEQRES 1 D 214 ALA ILE ARG MET THR GLN SER PRO SER SER PHE SER ALA SEQRES 2 D 214 SER ILE GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 D 214 GLN GLY ILE SER SER TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4 D 214 PRO GLY LYS ALA PRO ASN LEU LEU ILE TYR ALA THR SER SEQRES 5 D 214 SER LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 D 214 GLY SER GLY THR ASP PHE THR LEU THR ILE THR SER LEU SEQRES 7 D 214 GLN SER GLU ASP PHE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 D 214 TYR SER HIS PRO LEU THR PHE GLY GLY GLY THR LYS VAL 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 CYS SEQRES 1 E 131 MET GLU VAL ARG ASN LEU ASN ALA ALA ARG GLU LEU PHE SEQRES 2 E 131 LEU ASP GLU LEU LYS ALA LEU THR ALA GLU LEU LYS VAL SEQRES 3 E 131 TYR SER VAL ILE GLN SER GLN ILE ASN ALA ALA LEU SER SEQRES 4 E 131 ALA LYS GLN GLY ILE ARG ILE ASP ALA GLY GLY ILE ASP SEQRES 5 E 131 LEU VAL ASP PRO THR LEU TYR GLY TYR ALA VAL GLY ASP SEQRES 6 E 131 PRO ARG TRP LYS ASP SER PRO GLU TYR ALA LEU LEU SER SEQRES 7 E 131 ASN LEU ASP THR PHE SER GLY LYS LEU SER ILE LYS ASP SEQRES 8 E 131 PHE LEU SER GLY SER PRO LYS GLN SER GLY GLU LEU LYS SEQRES 9 E 131 GLY LEU SER ASP GLU TYR PRO PHE GLU LYS ASP ASN ASN SEQRES 10 E 131 PRO VAL GLY ASN PHE ALA THR THR VAL SER ASP ARG SER SEQRES 11 E 131 ARG SEQRES 1 F 131 MET GLU VAL ARG ASN LEU ASN ALA ALA ARG GLU LEU PHE SEQRES 2 F 131 LEU ASP GLU LEU LYS ALA LEU THR ALA GLU LEU LYS VAL SEQRES 3 F 131 TYR SER VAL ILE GLN SER GLN ILE ASN ALA ALA LEU SER SEQRES 4 F 131 ALA LYS GLN GLY ILE ARG ILE ASP ALA GLY GLY ILE ASP SEQRES 5 F 131 LEU VAL ASP PRO THR LEU TYR GLY TYR ALA VAL GLY ASP SEQRES 6 F 131 PRO ARG TRP LYS ASP SER PRO GLU TYR ALA LEU LEU SER SEQRES 7 F 131 ASN LEU ASP THR PHE SER GLY LYS LEU SER ILE LYS ASP SEQRES 8 F 131 PHE LEU SER GLY SER PRO LYS GLN SER GLY GLU LEU LYS SEQRES 9 F 131 GLY LEU SER ASP GLU TYR PRO PHE GLU LYS ASP ASN ASN SEQRES 10 F 131 PRO VAL GLY ASN PHE ALA THR THR VAL SER ASP ARG SER SEQRES 11 F 131 ARG HET CL A 301 1 HET PEG A 302 7 HET CL B 301 1 HET PEG B 302 7 HET CL C 301 1 HET PEG C 302 7 HET PEG C 303 7 HET CL D 301 1 HET PEG D 302 7 HET PEG D 303 7 HETNAM CL CHLORIDE ION HETNAM PEG DI(HYDROXYETHYL)ETHER FORMUL 7 CL 4(CL 1-) FORMUL 8 PEG 6(C4 H10 O3) FORMUL 17 HOH *392(H2 O) HELIX 1 AA1 THR A 28 TYR A 32 5 5 HELIX 2 AA2 ARG A 87 THR A 91 5 5 HELIX 3 AA3 SER A 135 LYS A 137 5 3 HELIX 4 AA4 SER A 164 ALA A 166 5 3 HELIX 5 AA5 PRO A 210 ASN A 212 5 3 HELIX 6 AA6 THR B 28 TYR B 32 5 5 HELIX 7 AA7 ARG B 87 THR B 91 5 5 HELIX 8 AA8 SER B 135 LYS B 137 5 3 HELIX 9 AA9 SER B 164 ALA B 166 5 3 HELIX 10 AB1 PRO B 210 ASN B 212 5 3 HELIX 11 AB2 GLN C 79 PHE C 83 5 5 HELIX 12 AB3 SER C 121 SER C 127 1 7 HELIX 13 AB4 LYS C 183 HIS C 189 1 7 HELIX 14 AB5 GLY C 212 CYS C 214 5 3 HELIX 15 AB6 GLN D 79 PHE D 83 5 5 HELIX 16 AB7 SER D 121 SER D 127 1 7 HELIX 17 AB8 LYS D 183 HIS D 189 1 7 HELIX 18 AB9 GLY D 212 CYS D 214 5 3 HELIX 19 AC1 ASN E 123 ALA E 158 1 36 HELIX 20 AC2 ASP E 173 GLY E 178 5 6 HELIX 21 AC3 ASP E 183 ASP E 188 5 6 HELIX 22 AC4 SER E 189 ASN E 197 1 9 HELIX 23 AC5 SER E 206 GLY E 213 1 8 HELIX 24 AC6 ASN E 235 ARG E 249 1 15 HELIX 25 AC7 ASN F 123 ALA F 158 1 36 HELIX 26 AC8 ASP F 173 GLY F 178 5 6 HELIX 27 AC9 ASP F 183 ASP F 188 5 6 HELIX 28 AD1 SER F 189 ASN F 197 1 9 HELIX 29 AD2 SER F 206 GLY F 213 1 8 HELIX 30 AD3 ASN F 235 ARG F 249 1 15 SHEET 1 AA1 4 GLN A 3 SER A 7 0 SHEET 2 AA1 4 LEU A 18 SER A 25 -1 O ALA A 23 N LEU A 5 SHEET 3 AA1 4 THR A 78 MET A 83 -1 O MET A 83 N LEU A 18 SHEET 4 AA1 4 PHE A 68 ASP A 73 -1 N SER A 71 O TYR A 80 SHEET 1 AA2 6 GLY A 10 VAL A 12 0 SHEET 2 AA2 6 ILE A 115 VAL A 119 1 O THR A 118 N GLY A 10 SHEET 3 AA2 6 ALA A 92 ASP A 99 -1 N ALA A 92 O VAL A 117 SHEET 4 AA2 6 MET A 34 GLN A 39 -1 N VAL A 37 O TYR A 95 SHEET 5 AA2 6 ASP A 46 ILE A 51 -1 O VAL A 48 N TRP A 36 SHEET 6 AA2 6 SER A 58 TYR A 60 -1 O ASP A 59 N THR A 50 SHEET 1 AA3 4 GLY A 10 VAL A 12 0 SHEET 2 AA3 4 ILE A 115 VAL A 119 1 O THR A 118 N GLY A 10 SHEET 3 AA3 4 ALA A 92 ASP A 99 -1 N ALA A 92 O VAL A 117 SHEET 4 AA3 4 PHE A 108 TRP A 111 -1 O TYR A 110 N LYS A 98 SHEET 1 AA4 4 SER A 128 LEU A 132 0 SHEET 2 AA4 4 THR A 143 TYR A 153 -1 O LYS A 151 N SER A 128 SHEET 3 AA4 4 TYR A 184 PRO A 193 -1 O VAL A 192 N ALA A 144 SHEET 4 AA4 4 VAL A 171 THR A 173 -1 N HIS A 172 O VAL A 189 SHEET 1 AA5 4 THR A 139 SER A 140 0 SHEET 2 AA5 4 THR A 143 TYR A 153 -1 O THR A 143 N SER A 140 SHEET 3 AA5 4 TYR A 184 PRO A 193 -1 O VAL A 192 N ALA A 144 SHEET 4 AA5 4 VAL A 177 LEU A 178 -1 N VAL A 177 O SER A 185 SHEET 1 AA6 3 VAL A 158 TRP A 162 0 SHEET 2 AA6 3 TYR A 202 HIS A 208 -1 O ASN A 205 N SER A 161 SHEET 3 AA6 3 THR A 213 VAL A 219 -1 O VAL A 219 N TYR A 202 SHEET 1 AA7 4 GLN B 3 SER B 7 0 SHEET 2 AA7 4 LEU B 18 SER B 25 -1 O ALA B 23 N LEU B 5 SHEET 3 AA7 4 THR B 78 MET B 83 -1 O MET B 83 N LEU B 18 SHEET 4 AA7 4 PHE B 68 ASP B 73 -1 N SER B 71 O TYR B 80 SHEET 1 AA8 6 GLY B 10 VAL B 12 0 SHEET 2 AA8 6 ILE B 115 VAL B 119 1 O THR B 118 N GLY B 10 SHEET 3 AA8 6 ALA B 92 ASP B 99 -1 N ALA B 92 O VAL B 117 SHEET 4 AA8 6 MET B 34 GLN B 39 -1 N VAL B 37 O TYR B 95 SHEET 5 AA8 6 ASP B 46 ILE B 51 -1 O VAL B 48 N TRP B 36 SHEET 6 AA8 6 SER B 58 TYR B 60 -1 O ASP B 59 N THR B 50 SHEET 1 AA9 4 GLY B 10 VAL B 12 0 SHEET 2 AA9 4 ILE B 115 VAL B 119 1 O THR B 118 N GLY B 10 SHEET 3 AA9 4 ALA B 92 ASP B 99 -1 N ALA B 92 O VAL B 117 SHEET 4 AA9 4 PHE B 108 TRP B 111 -1 O TYR B 110 N LYS B 98 SHEET 1 AB1 4 SER B 128 LEU B 132 0 SHEET 2 AB1 4 THR B 143 TYR B 153 -1 O LYS B 151 N SER B 128 SHEET 3 AB1 4 TYR B 184 PRO B 193 -1 O VAL B 192 N ALA B 144 SHEET 4 AB1 4 VAL B 171 THR B 173 -1 N HIS B 172 O VAL B 189 SHEET 1 AB2 4 THR B 139 SER B 140 0 SHEET 2 AB2 4 THR B 143 TYR B 153 -1 O THR B 143 N SER B 140 SHEET 3 AB2 4 TYR B 184 PRO B 193 -1 O VAL B 192 N ALA B 144 SHEET 4 AB2 4 VAL B 177 LEU B 178 -1 N VAL B 177 O SER B 185 SHEET 1 AB3 3 VAL B 158 TRP B 162 0 SHEET 2 AB3 3 TYR B 202 HIS B 208 -1 O ASN B 205 N SER B 161 SHEET 3 AB3 3 THR B 213 VAL B 219 -1 O VAL B 219 N TYR B 202 SHEET 1 AB4 4 MET C 4 SER C 7 0 SHEET 2 AB4 4 VAL C 19 ALA C 25 -1 O THR C 22 N SER C 7 SHEET 3 AB4 4 ASP C 70 ILE C 75 -1 O LEU C 73 N ILE C 21 SHEET 4 AB4 4 PHE C 62 SER C 67 -1 N SER C 63 O THR C 74 SHEET 1 AB5 6 SER C 10 SER C 14 0 SHEET 2 AB5 6 THR C 102 LYS C 107 1 O GLU C 105 N PHE C 11 SHEET 3 AB5 6 ALA C 84 GLN C 90 -1 N ALA C 84 O VAL C 104 SHEET 4 AB5 6 LEU C 33 GLN C 38 -1 N TYR C 36 O TYR C 87 SHEET 5 AB5 6 ASN C 45 TYR C 49 -1 O LEU C 47 N TRP C 35 SHEET 6 AB5 6 SER C 53 LEU C 54 -1 O SER C 53 N TYR C 49 SHEET 1 AB6 4 SER C 10 SER C 14 0 SHEET 2 AB6 4 THR C 102 LYS C 107 1 O GLU C 105 N PHE C 11 SHEET 3 AB6 4 ALA C 84 GLN C 90 -1 N ALA C 84 O VAL C 104 SHEET 4 AB6 4 THR C 97 PHE C 98 -1 O THR C 97 N GLN C 90 SHEET 1 AB7 4 SER C 114 PHE C 118 0 SHEET 2 AB7 4 THR C 129 PHE C 139 -1 O ASN C 137 N SER C 114 SHEET 3 AB7 4 TYR C 173 SER C 182 -1 O LEU C 175 N LEU C 136 SHEET 4 AB7 4 SER C 159 VAL C 163 -1 N GLN C 160 O THR C 178 SHEET 1 AB8 4 ALA C 153 LEU C 154 0 SHEET 2 AB8 4 LYS C 145 VAL C 150 -1 N VAL C 150 O ALA C 153 SHEET 3 AB8 4 VAL C 191 THR C 197 -1 O THR C 197 N LYS C 145 SHEET 4 AB8 4 VAL C 205 ASN C 210 -1 O VAL C 205 N VAL C 196 SHEET 1 AB9 4 MET D 4 SER D 7 0 SHEET 2 AB9 4 VAL D 19 ALA D 25 -1 O THR D 22 N SER D 7 SHEET 3 AB9 4 ASP D 70 ILE D 75 -1 O LEU D 73 N ILE D 21 SHEET 4 AB9 4 PHE D 62 SER D 67 -1 N SER D 63 O THR D 74 SHEET 1 AC1 6 SER D 10 SER D 14 0 SHEET 2 AC1 6 THR D 102 LYS D 107 1 O GLU D 105 N PHE D 11 SHEET 3 AC1 6 ALA D 84 GLN D 90 -1 N ALA D 84 O VAL D 104 SHEET 4 AC1 6 LEU D 33 GLN D 38 -1 N TYR D 36 O TYR D 87 SHEET 5 AC1 6 ASN D 45 TYR D 49 -1 O LEU D 47 N TRP D 35 SHEET 6 AC1 6 SER D 53 LEU D 54 -1 O SER D 53 N TYR D 49 SHEET 1 AC2 4 SER D 10 SER D 14 0 SHEET 2 AC2 4 THR D 102 LYS D 107 1 O GLU D 105 N PHE D 11 SHEET 3 AC2 4 ALA D 84 GLN D 90 -1 N ALA D 84 O VAL D 104 SHEET 4 AC2 4 THR D 97 PHE D 98 -1 O THR D 97 N GLN D 90 SHEET 1 AC3 4 SER D 114 PHE D 118 0 SHEET 2 AC3 4 THR D 129 PHE D 139 -1 O ASN D 137 N SER D 114 SHEET 3 AC3 4 TYR D 173 SER D 182 -1 O LEU D 175 N LEU D 136 SHEET 4 AC3 4 SER D 159 VAL D 163 -1 N GLN D 160 O THR D 178 SHEET 1 AC4 4 ALA D 153 LEU D 154 0 SHEET 2 AC4 4 LYS D 145 VAL D 150 -1 N VAL D 150 O ALA D 153 SHEET 3 AC4 4 VAL D 191 THR D 197 -1 O GLU D 195 N GLN D 147 SHEET 4 AC4 4 VAL D 205 ASN D 210 -1 O VAL D 205 N VAL D 196 SHEET 1 AC5 2 ILE E 162 ARG E 163 0 SHEET 2 AC5 2 GLU E 227 TYR E 228 -1 O TYR E 228 N ILE E 162 SHEET 1 AC6 2 ILE F 162 ARG F 163 0 SHEET 2 AC6 2 GLU F 227 TYR F 228 -1 O TYR F 228 N ILE F 162 SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.23 SSBOND 2 CYS A 148 CYS A 204 1555 1555 2.14 SSBOND 3 CYS B 22 CYS B 96 1555 1555 2.25 SSBOND 4 CYS B 148 CYS B 204 1555 1555 2.15 SSBOND 5 CYS C 23 CYS C 88 1555 1555 2.25 SSBOND 6 CYS C 134 CYS C 194 1555 1555 2.19 SSBOND 7 CYS D 23 CYS D 88 1555 1555 2.27 SSBOND 8 CYS D 134 CYS D 194 1555 1555 2.23 CISPEP 1 PHE A 154 PRO A 155 0 -4.29 CISPEP 2 GLU A 156 PRO A 157 0 -11.07 CISPEP 3 PHE B 154 PRO B 155 0 -4.35 CISPEP 4 GLU B 156 PRO B 157 0 -11.16 CISPEP 5 SER C 7 PRO C 8 0 -6.23 CISPEP 6 HIS C 94 PRO C 95 0 1.01 CISPEP 7 TYR C 140 PRO C 141 0 4.23 CISPEP 8 SER D 7 PRO D 8 0 -6.07 CISPEP 9 HIS D 94 PRO D 95 0 2.72 CISPEP 10 TYR D 140 PRO D 141 0 4.10 CISPEP 11 SER E 214 PRO E 215 0 3.62 CISPEP 12 SER F 214 PRO F 215 0 4.94 CRYST1 87.582 92.308 105.220 90.00 104.83 90.00 P 1 21 1 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.011418 0.000000 0.003023 0.00000 SCALE2 0.000000 0.010833 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009831 0.00000