HEADER IMMUNE SYSTEM 25-JUN-19 6PHG TITLE PREDICTED GERMLINE VARIANT OF HUMAN TRANSMISSION BLOCKING ANTIBODY TITLE 2 2544 COMPND MOL_ID: 1; COMPND 2 MOLECULE: GERMLINE 2544 ANTIBODY FAB, HEAVY CHAIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: GERMLINE 2544 ANTIBODY FAB, LIGHT CHAIN; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS FAB, COMPLEX, ANTIGEN, IMMUNOGLOBULIN, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR B.R.MCLEOD,J.P.JULIEN REVDAT 1 02-OCT-19 6PHG 0 JRNL AUTH B.R.MCLEOD,K.MIURA,S.W.SCALLY,A.BOSCH,N.NGUYEN,H.SHIN,D.KIM, JRNL AUTH 2 W.VOLKMUTH,S.RAMISCH,J.A.CHICHESTER,S.STREATFIELD,C.WOODS, JRNL AUTH 3 W.R.SCHIEF,D.EMERLING,C.R.KING,J.P.JULIEN JRNL TITL POTENT ANTIBODY LINEAGE AGAINST MALARIA TRANSMISSION JRNL TITL 2 ELICITED BY HUMAN VACCINATION WITH PFS25 JRNL REF NAT COMMUN 2019 JRNL REFN ESSN 2041-1723 JRNL DOI 10.1038/S41467-019-11980-6 REMARK 2 REMARK 2 RESOLUTION. 2.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.11.1_2575 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.78 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 29699 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.185 REMARK 3 R VALUE (WORKING SET) : 0.182 REMARK 3 FREE R VALUE : 0.228 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.730 REMARK 3 FREE R VALUE TEST SET COUNT : 1999 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 35.7875 - 4.8166 1.00 2050 143 0.1599 0.1901 REMARK 3 2 4.8166 - 3.8245 1.00 1997 140 0.1352 0.1841 REMARK 3 3 3.8245 - 3.3415 1.00 1987 152 0.1689 0.2416 REMARK 3 4 3.3415 - 3.0361 1.00 1983 139 0.1901 0.2172 REMARK 3 5 3.0361 - 2.8186 1.00 1985 150 0.1980 0.2207 REMARK 3 6 2.8186 - 2.6525 1.00 1956 153 0.2041 0.2476 REMARK 3 7 2.6525 - 2.5197 1.00 1974 142 0.2046 0.2388 REMARK 3 8 2.5197 - 2.4100 1.00 1977 145 0.2050 0.2825 REMARK 3 9 2.4100 - 2.3173 1.00 1966 133 0.2068 0.2799 REMARK 3 10 2.3173 - 2.2373 1.00 1966 142 0.2169 0.2653 REMARK 3 11 2.2373 - 2.1674 1.00 1961 144 0.2180 0.2530 REMARK 3 12 2.1674 - 2.1054 1.00 1953 137 0.2394 0.2781 REMARK 3 13 2.1054 - 2.0500 1.00 1987 150 0.2569 0.3292 REMARK 3 14 2.0500 - 2.0000 1.00 1958 129 0.2905 0.3752 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.240 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.320 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.004 3316 REMARK 3 ANGLE : 0.696 4516 REMARK 3 CHIRALITY : 0.046 503 REMARK 3 PLANARITY : 0.004 578 REMARK 3 DIHEDRAL : 10.126 1967 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 11 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 91 ) REMARK 3 ORIGIN FOR THE GROUP (A): 26.2986 34.1202 72.9122 REMARK 3 T TENSOR REMARK 3 T11: 0.2230 T22: 0.2674 REMARK 3 T33: 0.1825 T12: 0.0554 REMARK 3 T13: -0.0368 T23: -0.0261 REMARK 3 L TENSOR REMARK 3 L11: 4.3829 L22: 2.2105 REMARK 3 L33: 3.7950 L12: -0.9449 REMARK 3 L13: -0.8894 L23: 0.7026 REMARK 3 S TENSOR REMARK 3 S11: -0.2045 S12: -0.3606 S13: 0.1501 REMARK 3 S21: 0.1427 S22: 0.1039 S23: 0.0019 REMARK 3 S31: -0.2399 S32: 0.0838 S33: 0.0853 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 92 THROUGH 115 ) REMARK 3 ORIGIN FOR THE GROUP (A): 29.1440 28.1609 60.0354 REMARK 3 T TENSOR REMARK 3 T11: 0.2982 T22: 0.3961 REMARK 3 T33: 0.2389 T12: 0.0073 REMARK 3 T13: -0.0335 T23: -0.0297 REMARK 3 L TENSOR REMARK 3 L11: 3.8317 L22: 1.9022 REMARK 3 L33: 4.4194 L12: -1.9262 REMARK 3 L13: -3.7713 L23: 2.3359 REMARK 3 S TENSOR REMARK 3 S11: -0.1278 S12: 0.1752 S13: -0.0261 REMARK 3 S21: -0.1348 S22: 0.0553 S23: -0.0693 REMARK 3 S31: -0.1981 S32: 0.0291 S33: 0.0555 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 116 THROUGH 146 ) REMARK 3 ORIGIN FOR THE GROUP (A): -0.4435 35.8036 77.0701 REMARK 3 T TENSOR REMARK 3 T11: 0.4257 T22: 0.5211 REMARK 3 T33: 0.3179 T12: 0.2067 REMARK 3 T13: -0.0009 T23: 0.1155 REMARK 3 L TENSOR REMARK 3 L11: 3.9114 L22: 2.5634 REMARK 3 L33: 1.8650 L12: -0.5272 REMARK 3 L13: -1.8321 L23: 0.1936 REMARK 3 S TENSOR REMARK 3 S11: -0.3592 S12: -0.5255 S13: -0.0094 REMARK 3 S21: 0.3655 S22: 0.4749 S23: 0.3939 REMARK 3 S31: -0.0449 S32: -0.2174 S33: -0.1474 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 147 THROUGH 227 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.5646 30.2901 74.7815 REMARK 3 T TENSOR REMARK 3 T11: 0.4647 T22: 0.4108 REMARK 3 T33: 0.5193 T12: 0.1712 REMARK 3 T13: 0.0803 T23: 0.1496 REMARK 3 L TENSOR REMARK 3 L11: 3.4389 L22: 3.0111 REMARK 3 L33: 3.1575 L12: -0.2267 REMARK 3 L13: 0.0073 L23: 0.9449 REMARK 3 S TENSOR REMARK 3 S11: -0.2272 S12: -0.6809 S13: -0.8419 REMARK 3 S21: 0.4949 S22: 0.1555 S23: 0.3505 REMARK 3 S31: 0.7652 S32: 0.0962 S33: 0.0435 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 4 THROUGH 22 ) REMARK 3 ORIGIN FOR THE GROUP (A): 10.5842 39.3723 48.7369 REMARK 3 T TENSOR REMARK 3 T11: 0.4213 T22: 0.5876 REMARK 3 T33: 0.3336 T12: 0.1724 REMARK 3 T13: -0.0559 T23: 0.0688 REMARK 3 L TENSOR REMARK 3 L11: 4.1034 L22: 5.5092 REMARK 3 L33: 7.2591 L12: 0.9727 REMARK 3 L13: 0.1920 L23: 2.0130 REMARK 3 S TENSOR REMARK 3 S11: -0.2008 S12: 0.8574 S13: 0.4311 REMARK 3 S21: -0.2762 S22: -0.1223 S23: 0.3642 REMARK 3 S31: -0.6726 S32: -0.2803 S33: 0.2949 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 23 THROUGH 42 ) REMARK 3 ORIGIN FOR THE GROUP (A): 23.9663 35.1256 51.0050 REMARK 3 T TENSOR REMARK 3 T11: 0.4246 T22: 0.4127 REMARK 3 T33: 0.4662 T12: -0.0272 REMARK 3 T13: -0.0700 T23: 0.0763 REMARK 3 L TENSOR REMARK 3 L11: 8.1891 L22: 8.1493 REMARK 3 L33: 5.2925 L12: -1.2710 REMARK 3 L13: -0.9659 L23: -0.0084 REMARK 3 S TENSOR REMARK 3 S11: -0.0980 S12: 0.9701 S13: 1.4936 REMARK 3 S21: -0.6092 S22: -0.1166 S23: -0.4910 REMARK 3 S31: -0.7614 S32: 0.2771 S33: 0.2515 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 43 THROUGH 95 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.8588 28.8214 50.0118 REMARK 3 T TENSOR REMARK 3 T11: 0.2620 T22: 0.4427 REMARK 3 T33: 0.2913 T12: 0.0716 REMARK 3 T13: -0.0206 T23: -0.0497 REMARK 3 L TENSOR REMARK 3 L11: 6.6188 L22: 2.7908 REMARK 3 L33: 2.9299 L12: -2.5520 REMARK 3 L13: -0.1830 L23: 0.4477 REMARK 3 S TENSOR REMARK 3 S11: -0.0219 S12: 0.6900 S13: -0.3975 REMARK 3 S21: -0.1491 S22: -0.2821 S23: 0.3608 REMARK 3 S31: -0.1079 S32: -0.6323 S33: 0.2633 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 96 THROUGH 109 ) REMARK 3 ORIGIN FOR THE GROUP (A): 18.9528 38.2882 55.0492 REMARK 3 T TENSOR REMARK 3 T11: 0.3550 T22: 0.2551 REMARK 3 T33: 0.2926 T12: 0.0374 REMARK 3 T13: 0.0129 T23: 0.0459 REMARK 3 L TENSOR REMARK 3 L11: 6.3843 L22: 5.1282 REMARK 3 L33: 5.0023 L12: 0.1188 REMARK 3 L13: -0.2999 L23: 1.2181 REMARK 3 S TENSOR REMARK 3 S11: -0.2266 S12: 0.0964 S13: 1.1240 REMARK 3 S21: 0.0191 S22: -0.0543 S23: -0.1896 REMARK 3 S31: -0.4698 S32: -0.1751 S33: 0.1255 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 110 THROUGH 153 ) REMARK 3 ORIGIN FOR THE GROUP (A): -12.2981 39.1830 65.0671 REMARK 3 T TENSOR REMARK 3 T11: 0.2627 T22: 0.2959 REMARK 3 T33: 0.3503 T12: 0.0697 REMARK 3 T13: 0.0298 T23: 0.0417 REMARK 3 L TENSOR REMARK 3 L11: 3.2229 L22: 1.7728 REMARK 3 L33: 2.6918 L12: -0.7219 REMARK 3 L13: -0.0377 L23: 0.4287 REMARK 3 S TENSOR REMARK 3 S11: -0.1508 S12: -0.3749 S13: -0.4026 REMARK 3 S21: 0.2823 S22: 0.1838 S23: 0.1573 REMARK 3 S31: 0.5192 S32: 0.2249 S33: -0.0518 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 154 THROUGH 191 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.6781 43.0732 67.6427 REMARK 3 T TENSOR REMARK 3 T11: 0.2695 T22: 0.2931 REMARK 3 T33: 0.2720 T12: 0.0713 REMARK 3 T13: 0.0228 T23: 0.0643 REMARK 3 L TENSOR REMARK 3 L11: 2.7807 L22: 1.1282 REMARK 3 L33: 2.7195 L12: 0.0025 REMARK 3 L13: 0.1059 L23: 0.1000 REMARK 3 S TENSOR REMARK 3 S11: -0.1941 S12: -0.2868 S13: -0.1549 REMARK 3 S21: 0.1654 S22: 0.2403 S23: 0.0502 REMARK 3 S31: 0.1850 S32: 0.2137 S33: -0.0085 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 192 THROUGH 216 ) REMARK 3 ORIGIN FOR THE GROUP (A): -20.9153 42.4101 63.6522 REMARK 3 T TENSOR REMARK 3 T11: 0.2533 T22: 0.3419 REMARK 3 T33: 0.3714 T12: 0.0329 REMARK 3 T13: 0.0054 T23: 0.0425 REMARK 3 L TENSOR REMARK 3 L11: 4.3386 L22: 2.6548 REMARK 3 L33: 7.0303 L12: -1.7162 REMARK 3 L13: -3.3971 L23: 2.1470 REMARK 3 S TENSOR REMARK 3 S11: -0.0815 S12: 0.3096 S13: -0.4621 REMARK 3 S21: -0.0033 S22: -0.0444 S23: 0.0782 REMARK 3 S31: -0.2312 S32: -0.8622 S33: 0.1005 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 6PHG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUN-19. REMARK 100 THE DEPOSITION ID IS D_1000242555. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 13-DEC-17 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 : CLSI REMARK 200 BEAMLINE : 08ID-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29727 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000 REMARK 200 RESOLUTION RANGE LOW (A) : 40.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 6.700 REMARK 200 R MERGE (I) : 0.08200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 13.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 6.70 REMARK 200 R MERGE FOR SHELL (I) : 0.59900 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.900 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: IN HOUSE MODEL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 46.38 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE PH 4.5, 25 % REMARK 280 (W/V) PEG 3350, VAPOR DIFFUSION, TEMPERATURE 293K 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 65.42150 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.27850 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 65.42150 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.27850 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4060 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19310 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 A 379 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 SER A 142 REMARK 465 THR A 143 REMARK 465 SER A 144 REMARK 465 CYS A 228 REMARK 465 ASP B 1 REMARK 465 ILE B 2 REMARK 465 VAL B 3 REMARK 465 GLN B 26A REMARK 465 SER B 26B REMARK 465 LEU B 26C REMARK 465 LEU B 26D REMARK 465 HIS B 26E REMARK 465 SER B 26F REMARK 465 ASN B 26G REMARK 465 SER B 71 REMARK 465 GLY B 72 REMARK 465 THR B 73 REMARK 465 ASP B 74 REMARK 465 CYS B 217 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS A 141 CG CD CE NZ REMARK 470 LYS A 213 CG CD CE NZ REMARK 470 LYS A 218 CG CD CE NZ REMARK 470 LYS A 226 CG CD CE NZ REMARK 470 SER B 26 OG REMARK 470 GLU B 85 CG CD OE1 OE2 REMARK 470 ASP B 125 CG OD1 OD2 REMARK 470 LYS B 172 CG CD CE NZ REMARK 470 LYS B 193 CG CD CE NZ 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 ASP A 156 72.47 62.91 REMARK 500 SER B 56 15.96 -150.47 REMARK 500 LEU B 96 -159.60 -93.28 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 401 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 6PHB RELATED DB: PDB DBREF 6PHG A 1 228 PDB 6PHG 6PHG 1 228 DBREF 6PHG B 1 217 PDB 6PHG 6PHG 1 217 SEQRES 1 A 228 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 A 228 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 A 228 PHE THR PHE SER SER TYR SER MET ASN TRP VAL ARG GLN SEQRES 4 A 228 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER TYR ILE SER SEQRES 5 A 228 SER SER SER SER THR ILE TYR TYR ALA ASP SER VAL LYS SEQRES 6 A 228 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SER SEQRES 7 A 228 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 A 228 ALA VAL TYR TYR CYS ALA ARG VAL GLU TYR TYR TYR ASP SEQRES 9 A 228 SER SER GLY TYR TYR TYR ASP PHE ASP TYR TRP GLY GLN SEQRES 10 A 228 GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY SEQRES 11 A 228 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 12 A 228 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 A 228 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 A 228 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 A 228 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 A 228 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 17 A 228 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 A 228 LYS VAL GLU PRO LYS SER CYS SEQRES 1 B 218 ASP ILE VAL MET THR GLN SER PRO LEU SER LEU PRO VAL SEQRES 2 B 218 THR PRO GLY GLU PRO ALA SER ILE SER CYS ARG SER SER SEQRES 3 B 218 GLN SER LEU LEU HIS SER ASN GLY TYR ASN TYR LEU ASP SEQRES 4 B 218 TRP TYR LEU GLN LYS PRO GLY GLN SER PRO GLN LEU LEU SEQRES 5 B 218 ILE TYR LEU GLY SER ASN ARG ALA SER GLY VAL PRO ASP SEQRES 6 B 218 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 B 218 LYS ILE SER ARG VAL GLU ALA GLU ASP VAL GLY VAL TYR SEQRES 8 B 218 TYR CYS MET GLN ALA LEU GLN THR PRO THR PHE GLY GLN SEQRES 9 B 218 GLY THR ARG LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SEQRES 10 B 218 SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SEQRES 11 B 218 SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE SEQRES 12 B 218 TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN SEQRES 13 B 218 ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU SEQRES 14 B 218 GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER THR SEQRES 15 B 218 LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL SEQRES 16 B 218 TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO SEQRES 17 B 218 VAL THR LYS SER PHE ASN ARG GLY GLU CYS HET GOL B 401 6 HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 3 GOL C3 H8 O3 FORMUL 4 HOH *197(H2 O) HELIX 1 AA1 THR A 28 TYR A 32 5 5 HELIX 2 AA2 ASN A 74 LYS A 76 5 3 HELIX 3 AA3 ARG A 87 THR A 91 5 5 HELIX 4 AA4 SER A 168 ALA A 170 5 3 HELIX 5 AA5 SER A 199 LEU A 201 5 3 HELIX 6 AA6 LYS A 213 ASN A 216 5 4 HELIX 7 AA7 GLU B 83 VAL B 87 5 5 HELIX 8 AA8 SER B 124 LYS B 129 1 6 HELIX 9 AA9 LYS B 186 HIS B 192 1 7 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 VAL A 5 SHEET 3 AA1 4 SER 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 THR A 69 O GLN A 82 SHEET 1 AA2 6 LEU A 11 VAL A 12 0 SHEET 2 AA2 6 THR A 119 VAL A 123 1 O THR A 122 N VAL A 12 SHEET 3 AA2 6 ALA A 92 ASP A 104 -1 N ALA A 92 O VAL A 121 SHEET 4 AA2 6 MET A 34 GLN A 39 -1 N VAL A 37 O TYR A 95 SHEET 5 AA2 6 LEU A 45 ILE A 51 -1 O GLU A 46 N ARG A 38 SHEET 6 AA2 6 ILE A 58 TYR A 60 -1 O TYR A 59 N TYR A 50 SHEET 1 AA3 4 LEU A 11 VAL A 12 0 SHEET 2 AA3 4 THR A 119 VAL A 123 1 O THR A 122 N VAL A 12 SHEET 3 AA3 4 ALA A 92 ASP A 104 -1 N ALA A 92 O VAL A 121 SHEET 4 AA3 4 GLY A 107 TRP A 115 -1 O TYR A 109 N TYR A 102 SHEET 1 AA4 4 SER A 132 LEU A 136 0 SHEET 2 AA4 4 THR A 147 TYR A 157 -1 O LEU A 153 N PHE A 134 SHEET 3 AA4 4 TYR A 188 PRO A 197 -1 O TYR A 188 N TYR A 157 SHEET 4 AA4 4 VAL A 175 THR A 177 -1 N HIS A 176 O VAL A 193 SHEET 1 AA5 4 SER A 132 LEU A 136 0 SHEET 2 AA5 4 THR A 147 TYR A 157 -1 O LEU A 153 N PHE A 134 SHEET 3 AA5 4 TYR A 188 PRO A 197 -1 O TYR A 188 N TYR A 157 SHEET 4 AA5 4 VAL A 181 LEU A 182 -1 N VAL A 181 O SER A 189 SHEET 1 AA6 3 THR A 163 TRP A 166 0 SHEET 2 AA6 3 TYR A 206 HIS A 212 -1 O ASN A 209 N SER A 165 SHEET 3 AA6 3 THR A 217 VAL A 223 -1 O VAL A 219 N VAL A 210 SHEET 1 AA7 6 LEU B 9 VAL B 13 0 SHEET 2 AA7 6 THR B 105 ILE B 109 1 O ARG B 106 N LEU B 9 SHEET 3 AA7 6 GLY B 88 ALA B 95 -1 N TYR B 90 O THR B 105 SHEET 4 AA7 6 LEU B 37 GLN B 42 -1 N TYR B 40 O TYR B 91 SHEET 5 AA7 6 GLN B 49 TYR B 53 -1 O LEU B 51 N TRP B 39 SHEET 6 AA7 6 ASN B 57 ARG B 58 -1 O ASN B 57 N TYR B 53 SHEET 1 AA8 4 LEU B 9 VAL B 13 0 SHEET 2 AA8 4 THR B 105 ILE B 109 1 O ARG B 106 N LEU B 9 SHEET 3 AA8 4 GLY B 88 ALA B 95 -1 N TYR B 90 O THR B 105 SHEET 4 AA8 4 PRO B 99 PHE B 101 -1 O THR B 100 N GLN B 94 SHEET 1 AA9 3 ALA B 19 SER B 22 0 SHEET 2 AA9 3 THR B 76 ILE B 79 -1 O LEU B 77 N ILE B 21 SHEET 3 AA9 3 PHE B 66 SER B 69 -1 N SER B 67 O LYS B 78 SHEET 1 AB1 4 SER B 117 PHE B 121 0 SHEET 2 AB1 4 THR B 132 PHE B 142 -1 O LEU B 138 N PHE B 119 SHEET 3 AB1 4 TYR B 176 SER B 185 -1 O LEU B 182 N VAL B 135 SHEET 4 AB1 4 SER B 162 VAL B 166 -1 N GLN B 163 O THR B 181 SHEET 1 AB2 3 ALA B 147 VAL B 153 0 SHEET 2 AB2 3 VAL B 194 HIS B 201 -1 O GLU B 198 N GLN B 150 SHEET 3 AB2 3 VAL B 208 ASN B 213 -1 O VAL B 208 N VAL B 199 SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.07 SSBOND 2 CYS A 152 CYS A 208 1555 1555 2.03 SSBOND 3 CYS B 23 CYS B 92 1555 1555 2.04 SSBOND 4 CYS B 137 CYS B 197 1555 1555 2.04 CISPEP 1 PHE A 158 PRO A 159 0 -7.49 CISPEP 2 GLU A 160 PRO A 161 0 -4.23 CISPEP 3 TYR B 143 PRO B 144 0 3.99 SITE 1 AC1 11 PHE A 178 PRO A 179 VAL A 181 SER A 189 SITE 2 AC1 11 LEU A 190 SER A 191 SER B 165 SER B 179 SITE 3 AC1 11 SER B 180 THR B 181 HOH B 505 CRYST1 130.843 60.557 61.079 90.00 113.62 90.00 C 1 2 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 0.007643 0.000000 0.003342 0.00000 SCALE2 0.000000 0.016513 0.000000 0.00000 SCALE3 0.000000 0.000000 0.017869 0.00000